data_8QNW
# 
_entry.id   8QNW 
# 
_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   8QNW         pdb_00008qnw 10.2210/pdb8qnw/pdb 
WWPDB D_1292133634 ?            ?                   
# 
_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                        8QNW 
_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 
# 
_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 '(4S)-2-METHYL-2,4-PENTANEDIOL'   118.174   1   ? ? ? ? 
4 non-polymer syn 'SULFATE ION'                     96.063    1   ? ? ? ? 
5 water       nat water                             18.015    430 ? ? ? ? 
# 
_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 '(4S)-2-METHYL-2,4-PENTANEDIOL' MPD 
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 
MPD non-polymer         . '(4S)-2-METHYL-2,4-PENTANEDIOL' ?                          'C6 H14 O2'       118.174 
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 
# 
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   9   ASN ASN 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 385 376 376 GLN GLN 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 
# 
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   401 386 FMN FMN A . 
C 3 MPD 1   402 387 MPD MPD A . 
D 4 SO4 1   403 388 SO4 SO4 A . 
E 5 HOH 1   501 343 HOH HOH A . 
E 5 HOH 2   502 413 HOH HOH A . 
E 5 HOH 3   503 133 HOH HOH A . 
E 5 HOH 4   504 373 HOH HOH A . 
E 5 HOH 5   505 304 HOH HOH A . 
E 5 HOH 6   506 272 HOH HOH A . 
E 5 HOH 7   507 128 HOH HOH A . 
E 5 HOH 8   508 102 HOH HOH A . 
E 5 HOH 9   509 175 HOH HOH A . 
E 5 HOH 10  510 319 HOH HOH A . 
E 5 HOH 11  511 330 HOH HOH A . 
E 5 HOH 12  512 211 HOH HOH A . 
E 5 HOH 13  513 303 HOH HOH A . 
E 5 HOH 14  514 111 HOH HOH A . 
E 5 HOH 15  515 229 HOH HOH A . 
E 5 HOH 16  516 223 HOH HOH A . 
E 5 HOH 17  517 188 HOH HOH A . 
E 5 HOH 18  518 166 HOH HOH A . 
E 5 HOH 19  519 153 HOH HOH A . 
E 5 HOH 20  520 201 HOH HOH A . 
E 5 HOH 21  521 112 HOH HOH A . 
E 5 HOH 22  522 40  HOH HOH A . 
E 5 HOH 23  523 127 HOH HOH A . 
E 5 HOH 24  524 22  HOH HOH A . 
E 5 HOH 25  525 34  HOH HOH A . 
E 5 HOH 26  526 393 HOH HOH A . 
E 5 HOH 27  527 131 HOH HOH A . 
E 5 HOH 28  528 13  HOH HOH A . 
E 5 HOH 29  529 242 HOH HOH A . 
E 5 HOH 30  530 39  HOH HOH A . 
E 5 HOH 31  531 142 HOH HOH A . 
E 5 HOH 32  532 116 HOH HOH A . 
E 5 HOH 33  533 252 HOH HOH A . 
E 5 HOH 34  534 140 HOH HOH A . 
E 5 HOH 35  535 276 HOH HOH A . 
E 5 HOH 36  536 185 HOH HOH A . 
E 5 HOH 37  537 352 HOH HOH A . 
E 5 HOH 38  538 29  HOH HOH A . 
E 5 HOH 39  539 193 HOH HOH A . 
E 5 HOH 40  540 37  HOH HOH A . 
E 5 HOH 41  541 165 HOH HOH A . 
E 5 HOH 42  542 281 HOH HOH A . 
E 5 HOH 43  543 58  HOH HOH A . 
E 5 HOH 44  544 152 HOH HOH A . 
E 5 HOH 45  545 182 HOH HOH A . 
E 5 HOH 46  546 425 HOH HOH A . 
E 5 HOH 47  547 20  HOH HOH A . 
E 5 HOH 48  548 249 HOH HOH A . 
E 5 HOH 49  549 12  HOH HOH A . 
E 5 HOH 50  550 47  HOH HOH A . 
E 5 HOH 51  551 424 HOH HOH A . 
E 5 HOH 52  552 84  HOH HOH A . 
E 5 HOH 53  553 4   HOH HOH A . 
E 5 HOH 54  554 160 HOH HOH A . 
E 5 HOH 55  555 76  HOH HOH A . 
E 5 HOH 56  556 228 HOH HOH A . 
E 5 HOH 57  557 335 HOH HOH A . 
E 5 HOH 58  558 70  HOH HOH A . 
E 5 HOH 59  559 100 HOH HOH A . 
E 5 HOH 60  560 306 HOH HOH A . 
E 5 HOH 61  561 151 HOH HOH A . 
E 5 HOH 62  562 52  HOH HOH A . 
E 5 HOH 63  563 200 HOH HOH A . 
E 5 HOH 64  564 103 HOH HOH A . 
E 5 HOH 65  565 64  HOH HOH A . 
E 5 HOH 66  566 287 HOH HOH A . 
E 5 HOH 67  567 312 HOH HOH A . 
E 5 HOH 68  568 162 HOH HOH A . 
E 5 HOH 69  569 420 HOH HOH A . 
E 5 HOH 70  570 110 HOH HOH A . 
E 5 HOH 71  571 323 HOH HOH A . 
E 5 HOH 72  572 298 HOH HOH A . 
E 5 HOH 73  573 144 HOH HOH A . 
E 5 HOH 74  574 96  HOH HOH A . 
E 5 HOH 75  575 197 HOH HOH A . 
E 5 HOH 76  576 60  HOH HOH A . 
E 5 HOH 77  577 156 HOH HOH A . 
E 5 HOH 78  578 422 HOH HOH A . 
E 5 HOH 79  579 187 HOH HOH A . 
E 5 HOH 80  580 85  HOH HOH A . 
E 5 HOH 81  581 80  HOH HOH A . 
E 5 HOH 82  582 212 HOH HOH A . 
E 5 HOH 83  583 79  HOH HOH A . 
E 5 HOH 84  584 97  HOH HOH A . 
E 5 HOH 85  585 41  HOH HOH A . 
E 5 HOH 86  586 190 HOH HOH A . 
E 5 HOH 87  587 380 HOH HOH A . 
E 5 HOH 88  588 325 HOH HOH A . 
E 5 HOH 89  589 90  HOH HOH A . 
E 5 HOH 90  590 68  HOH HOH A . 
E 5 HOH 91  591 248 HOH HOH A . 
E 5 HOH 92  592 117 HOH HOH A . 
E 5 HOH 93  593 125 HOH HOH A . 
E 5 HOH 94  594 14  HOH HOH A . 
E 5 HOH 95  595 278 HOH HOH A . 
E 5 HOH 96  596 355 HOH HOH A . 
E 5 HOH 97  597 28  HOH HOH A . 
E 5 HOH 98  598 406 HOH HOH A . 
E 5 HOH 99  599 120 HOH HOH A . 
E 5 HOH 100 600 83  HOH HOH A . 
E 5 HOH 101 601 282 HOH HOH A . 
E 5 HOH 102 602 45  HOH HOH A . 
E 5 HOH 103 603 285 HOH HOH A . 
E 5 HOH 104 604 36  HOH HOH A . 
E 5 HOH 105 605 88  HOH HOH A . 
E 5 HOH 106 606 129 HOH HOH A . 
E 5 HOH 107 607 65  HOH HOH A . 
E 5 HOH 108 608 24  HOH HOH A . 
E 5 HOH 109 609 132 HOH HOH A . 
E 5 HOH 110 610 26  HOH HOH A . 
E 5 HOH 111 611 324 HOH HOH A . 
E 5 HOH 112 612 18  HOH HOH A . 
E 5 HOH 113 613 387 HOH HOH A . 
E 5 HOH 114 614 155 HOH HOH A . 
E 5 HOH 115 615 171 HOH HOH A . 
E 5 HOH 116 616 130 HOH HOH A . 
E 5 HOH 117 617 149 HOH HOH A . 
E 5 HOH 118 618 49  HOH HOH A . 
E 5 HOH 119 619 67  HOH HOH A . 
E 5 HOH 120 620 71  HOH HOH A . 
E 5 HOH 121 621 10  HOH HOH A . 
E 5 HOH 122 622 374 HOH HOH A . 
E 5 HOH 123 623 183 HOH HOH A . 
E 5 HOH 124 624 75  HOH HOH A . 
E 5 HOH 125 625 264 HOH HOH A . 
E 5 HOH 126 626 51  HOH HOH A . 
E 5 HOH 127 627 82  HOH HOH A . 
E 5 HOH 128 628 386 HOH HOH A . 
E 5 HOH 129 629 136 HOH HOH A . 
E 5 HOH 130 630 3   HOH HOH A . 
E 5 HOH 131 631 77  HOH HOH A . 
E 5 HOH 132 632 9   HOH HOH A . 
E 5 HOH 133 633 50  HOH HOH A . 
E 5 HOH 134 634 78  HOH HOH A . 
E 5 HOH 135 635 314 HOH HOH A . 
E 5 HOH 136 636 217 HOH HOH A . 
E 5 HOH 137 637 19  HOH HOH A . 
E 5 HOH 138 638 366 HOH HOH A . 
E 5 HOH 139 639 23  HOH HOH A . 
E 5 HOH 140 640 284 HOH HOH A . 
E 5 HOH 141 641 35  HOH HOH A . 
E 5 HOH 142 642 56  HOH HOH A . 
E 5 HOH 143 643 251 HOH HOH A . 
E 5 HOH 144 644 169 HOH HOH A . 
E 5 HOH 145 645 32  HOH HOH A . 
E 5 HOH 146 646 238 HOH HOH A . 
E 5 HOH 147 647 245 HOH HOH A . 
E 5 HOH 148 648 263 HOH HOH A . 
E 5 HOH 149 649 6   HOH HOH A . 
E 5 HOH 150 650 336 HOH HOH A . 
E 5 HOH 151 651 365 HOH HOH A . 
E 5 HOH 152 652 161 HOH HOH A . 
E 5 HOH 153 653 2   HOH HOH A . 
E 5 HOH 154 654 177 HOH HOH A . 
E 5 HOH 155 655 11  HOH HOH A . 
E 5 HOH 156 656 181 HOH HOH A . 
E 5 HOH 157 657 27  HOH HOH A . 
E 5 HOH 158 658 53  HOH HOH A . 
E 5 HOH 159 659 123 HOH HOH A . 
E 5 HOH 160 660 222 HOH HOH A . 
E 5 HOH 161 661 105 HOH HOH A . 
E 5 HOH 162 662 16  HOH HOH A . 
E 5 HOH 163 663 302 HOH HOH A . 
E 5 HOH 164 664 135 HOH HOH A . 
E 5 HOH 165 665 42  HOH HOH A . 
E 5 HOH 166 666 196 HOH HOH A . 
E 5 HOH 167 667 230 HOH HOH A . 
E 5 HOH 168 668 353 HOH HOH A . 
E 5 HOH 169 669 107 HOH HOH A . 
E 5 HOH 170 670 21  HOH HOH A . 
E 5 HOH 171 671 92  HOH HOH A . 
E 5 HOH 172 672 398 HOH HOH A . 
E 5 HOH 173 673 224 HOH HOH A . 
E 5 HOH 174 674 63  HOH HOH A . 
E 5 HOH 175 675 446 HOH HOH A . 
E 5 HOH 176 676 247 HOH HOH A . 
E 5 HOH 177 677 254 HOH HOH A . 
E 5 HOH 178 678 163 HOH HOH A . 
E 5 HOH 179 679 145 HOH HOH A . 
E 5 HOH 180 680 69  HOH HOH A . 
E 5 HOH 181 681 5   HOH HOH A . 
E 5 HOH 182 682 15  HOH HOH A . 
E 5 HOH 183 683 31  HOH HOH A . 
E 5 HOH 184 684 322 HOH HOH A . 
E 5 HOH 185 685 279 HOH HOH A . 
E 5 HOH 186 686 220 HOH HOH A . 
E 5 HOH 187 687 43  HOH HOH A . 
E 5 HOH 188 688 48  HOH HOH A . 
E 5 HOH 189 689 174 HOH HOH A . 
E 5 HOH 190 690 57  HOH HOH A . 
E 5 HOH 191 691 318 HOH HOH A . 
E 5 HOH 192 692 59  HOH HOH A . 
E 5 HOH 193 693 114 HOH HOH A . 
E 5 HOH 194 694 150 HOH HOH A . 
E 5 HOH 195 695 25  HOH HOH A . 
E 5 HOH 196 696 141 HOH HOH A . 
E 5 HOH 197 697 104 HOH HOH A . 
E 5 HOH 198 698 46  HOH HOH A . 
E 5 HOH 199 699 184 HOH HOH A . 
E 5 HOH 200 700 95  HOH HOH A . 
E 5 HOH 201 701 81  HOH HOH A . 
E 5 HOH 202 702 126 HOH HOH A . 
E 5 HOH 203 703 297 HOH HOH A . 
E 5 HOH 204 704 198 HOH HOH A . 
E 5 HOH 205 705 269 HOH HOH A . 
E 5 HOH 206 706 54  HOH HOH A . 
E 5 HOH 207 707 239 HOH HOH A . 
E 5 HOH 208 708 309 HOH HOH A . 
E 5 HOH 209 709 91  HOH HOH A . 
E 5 HOH 210 710 436 HOH HOH A . 
E 5 HOH 211 711 372 HOH HOH A . 
E 5 HOH 212 712 443 HOH HOH A . 
E 5 HOH 213 713 206 HOH HOH A . 
E 5 HOH 214 714 326 HOH HOH A . 
E 5 HOH 215 715 119 HOH HOH A . 
E 5 HOH 216 716 33  HOH HOH A . 
E 5 HOH 217 717 441 HOH HOH A . 
E 5 HOH 218 718 259 HOH HOH A . 
E 5 HOH 219 719 189 HOH HOH A . 
E 5 HOH 220 720 61  HOH HOH A . 
E 5 HOH 221 721 7   HOH HOH A . 
E 5 HOH 222 722 213 HOH HOH A . 
E 5 HOH 223 723 194 HOH HOH A . 
E 5 HOH 224 724 113 HOH HOH A . 
E 5 HOH 225 725 118 HOH HOH A . 
E 5 HOH 226 726 17  HOH HOH A . 
E 5 HOH 227 727 139 HOH HOH A . 
E 5 HOH 228 728 62  HOH HOH A . 
E 5 HOH 229 729 209 HOH HOH A . 
E 5 HOH 230 730 232 HOH HOH A . 
E 5 HOH 231 731 241 HOH HOH A . 
E 5 HOH 232 732 1   HOH HOH A . 
E 5 HOH 233 733 292 HOH HOH A . 
E 5 HOH 234 734 38  HOH HOH A . 
E 5 HOH 235 735 409 HOH HOH A . 
E 5 HOH 236 736 87  HOH HOH A . 
E 5 HOH 237 737 208 HOH HOH A . 
E 5 HOH 238 738 342 HOH HOH A . 
E 5 HOH 239 739 158 HOH HOH A . 
E 5 HOH 240 740 99  HOH HOH A . 
E 5 HOH 241 741 233 HOH HOH A . 
E 5 HOH 242 742 273 HOH HOH A . 
E 5 HOH 243 743 179 HOH HOH A . 
E 5 HOH 244 744 244 HOH HOH A . 
E 5 HOH 245 745 348 HOH HOH A . 
E 5 HOH 246 746 170 HOH HOH A . 
E 5 HOH 247 747 392 HOH HOH A . 
E 5 HOH 248 748 93  HOH HOH A . 
E 5 HOH 249 749 94  HOH HOH A . 
E 5 HOH 250 750 405 HOH HOH A . 
E 5 HOH 251 751 191 HOH HOH A . 
E 5 HOH 252 752 442 HOH HOH A . 
E 5 HOH 253 753 262 HOH HOH A . 
E 5 HOH 254 754 173 HOH HOH A . 
E 5 HOH 255 755 218 HOH HOH A . 
E 5 HOH 256 756 337 HOH HOH A . 
E 5 HOH 257 757 379 HOH HOH A . 
E 5 HOH 258 758 157 HOH HOH A . 
E 5 HOH 259 759 394 HOH HOH A . 
E 5 HOH 260 760 414 HOH HOH A . 
E 5 HOH 261 761 72  HOH HOH A . 
E 5 HOH 262 762 30  HOH HOH A . 
E 5 HOH 263 763 55  HOH HOH A . 
E 5 HOH 264 764 146 HOH HOH A . 
E 5 HOH 265 765 134 HOH HOH A . 
E 5 HOH 266 766 431 HOH HOH A . 
E 5 HOH 267 767 172 HOH HOH A . 
E 5 HOH 268 768 347 HOH HOH A . 
E 5 HOH 269 769 256 HOH HOH A . 
E 5 HOH 270 770 439 HOH HOH A . 
E 5 HOH 271 771 400 HOH HOH A . 
E 5 HOH 272 772 108 HOH HOH A . 
E 5 HOH 273 773 86  HOH HOH A . 
E 5 HOH 274 774 66  HOH HOH A . 
E 5 HOH 275 775 8   HOH HOH A . 
E 5 HOH 276 776 147 HOH HOH A . 
E 5 HOH 277 777 215 HOH HOH A . 
E 5 HOH 278 778 115 HOH HOH A . 
E 5 HOH 279 779 320 HOH HOH A . 
E 5 HOH 280 780 180 HOH HOH A . 
E 5 HOH 281 781 362 HOH HOH A . 
E 5 HOH 282 782 270 HOH HOH A . 
E 5 HOH 283 783 73  HOH HOH A . 
E 5 HOH 284 784 296 HOH HOH A . 
E 5 HOH 285 785 121 HOH HOH A . 
E 5 HOH 286 786 388 HOH HOH A . 
E 5 HOH 287 787 178 HOH HOH A . 
E 5 HOH 288 788 385 HOH HOH A . 
E 5 HOH 289 789 159 HOH HOH A . 
E 5 HOH 290 790 109 HOH HOH A . 
E 5 HOH 291 791 382 HOH HOH A . 
E 5 HOH 292 792 351 HOH HOH A . 
E 5 HOH 293 793 344 HOH HOH A . 
E 5 HOH 294 794 255 HOH HOH A . 
E 5 HOH 295 795 227 HOH HOH A . 
E 5 HOH 296 796 106 HOH HOH A . 
E 5 HOH 297 797 440 HOH HOH A . 
E 5 HOH 298 798 246 HOH HOH A . 
E 5 HOH 299 799 310 HOH HOH A . 
E 5 HOH 300 800 444 HOH HOH A . 
E 5 HOH 301 801 74  HOH HOH A . 
E 5 HOH 302 802 316 HOH HOH A . 
E 5 HOH 303 803 253 HOH HOH A . 
E 5 HOH 304 804 89  HOH HOH A . 
E 5 HOH 305 805 300 HOH HOH A . 
E 5 HOH 306 806 237 HOH HOH A . 
E 5 HOH 307 807 234 HOH HOH A . 
E 5 HOH 308 808 235 HOH HOH A . 
E 5 HOH 309 809 268 HOH HOH A . 
E 5 HOH 310 810 286 HOH HOH A . 
E 5 HOH 311 811 216 HOH HOH A . 
E 5 HOH 312 812 265 HOH HOH A . 
E 5 HOH 313 813 299 HOH HOH A . 
E 5 HOH 314 814 288 HOH HOH A . 
E 5 HOH 315 815 377 HOH HOH A . 
E 5 HOH 316 816 399 HOH HOH A . 
E 5 HOH 317 817 432 HOH HOH A . 
E 5 HOH 318 818 294 HOH HOH A . 
E 5 HOH 319 819 168 HOH HOH A . 
E 5 HOH 320 820 356 HOH HOH A . 
E 5 HOH 321 821 289 HOH HOH A . 
E 5 HOH 322 822 416 HOH HOH A . 
E 5 HOH 323 823 341 HOH HOH A . 
E 5 HOH 324 824 397 HOH HOH A . 
E 5 HOH 325 825 143 HOH HOH A . 
E 5 HOH 326 826 331 HOH HOH A . 
E 5 HOH 327 827 447 HOH HOH A . 
E 5 HOH 328 828 358 HOH HOH A . 
E 5 HOH 329 829 257 HOH HOH A . 
E 5 HOH 330 830 354 HOH HOH A . 
E 5 HOH 331 831 214 HOH HOH A . 
E 5 HOH 332 832 315 HOH HOH A . 
E 5 HOH 333 833 199 HOH HOH A . 
E 5 HOH 334 834 205 HOH HOH A . 
E 5 HOH 335 835 44  HOH HOH A . 
E 5 HOH 336 836 277 HOH HOH A . 
E 5 HOH 337 837 421 HOH HOH A . 
E 5 HOH 338 838 435 HOH HOH A . 
E 5 HOH 339 839 210 HOH HOH A . 
E 5 HOH 340 840 271 HOH HOH A . 
E 5 HOH 341 841 426 HOH HOH A . 
E 5 HOH 342 842 340 HOH HOH A . 
E 5 HOH 343 843 307 HOH HOH A . 
E 5 HOH 344 844 305 HOH HOH A . 
E 5 HOH 345 845 293 HOH HOH A . 
E 5 HOH 346 846 122 HOH HOH A . 
E 5 HOH 347 847 360 HOH HOH A . 
E 5 HOH 348 848 202 HOH HOH A . 
E 5 HOH 349 849 370 HOH HOH A . 
E 5 HOH 350 850 240 HOH HOH A . 
E 5 HOH 351 851 427 HOH HOH A . 
E 5 HOH 352 852 275 HOH HOH A . 
E 5 HOH 353 853 369 HOH HOH A . 
E 5 HOH 354 854 250 HOH HOH A . 
E 5 HOH 355 855 101 HOH HOH A . 
E 5 HOH 356 856 290 HOH HOH A . 
E 5 HOH 357 857 411 HOH HOH A . 
E 5 HOH 358 858 338 HOH HOH A . 
E 5 HOH 359 859 167 HOH HOH A . 
E 5 HOH 360 860 334 HOH HOH A . 
E 5 HOH 361 861 266 HOH HOH A . 
E 5 HOH 362 862 428 HOH HOH A . 
E 5 HOH 363 863 438 HOH HOH A . 
E 5 HOH 364 864 148 HOH HOH A . 
E 5 HOH 365 865 317 HOH HOH A . 
E 5 HOH 366 866 346 HOH HOH A . 
E 5 HOH 367 867 418 HOH HOH A . 
E 5 HOH 368 868 261 HOH HOH A . 
E 5 HOH 369 869 357 HOH HOH A . 
E 5 HOH 370 870 137 HOH HOH A . 
E 5 HOH 371 871 267 HOH HOH A . 
E 5 HOH 372 872 221 HOH HOH A . 
E 5 HOH 373 873 403 HOH HOH A . 
E 5 HOH 374 874 345 HOH HOH A . 
E 5 HOH 375 875 203 HOH HOH A . 
E 5 HOH 376 876 434 HOH HOH A . 
E 5 HOH 377 877 98  HOH HOH A . 
E 5 HOH 378 878 274 HOH HOH A . 
E 5 HOH 379 879 226 HOH HOH A . 
E 5 HOH 380 880 364 HOH HOH A . 
E 5 HOH 381 881 225 HOH HOH A . 
E 5 HOH 382 882 402 HOH HOH A . 
E 5 HOH 383 883 407 HOH HOH A . 
E 5 HOH 384 884 258 HOH HOH A . 
E 5 HOH 385 885 329 HOH HOH A . 
E 5 HOH 386 886 124 HOH HOH A . 
E 5 HOH 387 887 207 HOH HOH A . 
E 5 HOH 388 888 243 HOH HOH A . 
E 5 HOH 389 889 417 HOH HOH A . 
E 5 HOH 390 890 433 HOH HOH A . 
E 5 HOH 391 891 359 HOH HOH A . 
E 5 HOH 392 892 327 HOH HOH A . 
E 5 HOH 393 893 291 HOH HOH A . 
E 5 HOH 394 894 412 HOH HOH A . 
E 5 HOH 395 895 363 HOH HOH A . 
E 5 HOH 396 896 176 HOH HOH A . 
E 5 HOH 397 897 368 HOH HOH A . 
E 5 HOH 398 898 192 HOH HOH A . 
E 5 HOH 399 899 138 HOH HOH A . 
E 5 HOH 400 900 231 HOH HOH A . 
E 5 HOH 401 901 389 HOH HOH A . 
E 5 HOH 402 902 390 HOH HOH A . 
E 5 HOH 403 903 401 HOH HOH A . 
E 5 HOH 404 904 384 HOH HOH A . 
E 5 HOH 405 905 219 HOH HOH A . 
E 5 HOH 406 906 186 HOH HOH A . 
E 5 HOH 407 907 204 HOH HOH A . 
E 5 HOH 408 908 349 HOH HOH A . 
E 5 HOH 409 909 339 HOH HOH A . 
E 5 HOH 410 910 195 HOH HOH A . 
E 5 HOH 411 911 361 HOH HOH A . 
E 5 HOH 412 912 301 HOH HOH A . 
E 5 HOH 413 913 396 HOH HOH A . 
E 5 HOH 414 914 154 HOH HOH A . 
E 5 HOH 415 915 367 HOH HOH A . 
E 5 HOH 416 916 260 HOH HOH A . 
E 5 HOH 417 917 445 HOH HOH A . 
E 5 HOH 418 918 419 HOH HOH A . 
E 5 HOH 419 919 280 HOH HOH A . 
E 5 HOH 420 920 381 HOH HOH A . 
E 5 HOH 421 921 371 HOH HOH A . 
E 5 HOH 422 922 437 HOH HOH A . 
E 5 HOH 423 923 283 HOH HOH A . 
E 5 HOH 424 924 375 HOH HOH A . 
E 5 HOH 425 925 295 HOH HOH A . 
E 5 HOH 426 926 308 HOH HOH A . 
E 5 HOH 427 927 376 HOH HOH A . 
E 5 HOH 428 928 321 HOH HOH A . 
E 5 HOH 429 929 164 HOH HOH A . 
E 5 HOH 430 930 332 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 ASN 9   ? CG  ? A ASN 18  CG  
2  1 Y 1 A ASN 9   ? OD1 ? A ASN 18  OD1 
3  1 Y 1 A ASN 9   ? ND2 ? A ASN 18  ND2 
4  1 Y 1 A LYS 20  ? CG  ? A LYS 29  CG  
5  1 Y 1 A LYS 20  ? CD  ? A LYS 29  CD  
6  1 Y 1 A LYS 20  ? CE  ? A LYS 29  CE  
7  1 Y 1 A LYS 20  ? NZ  ? A LYS 29  NZ  
8  1 Y 1 A GLU 116 ? CG  ? A GLU 125 CG  
9  1 Y 1 A GLU 116 ? CD  ? A GLU 125 CD  
10 1 Y 1 A GLU 116 ? OE1 ? A GLU 125 OE1 
11 1 Y 1 A GLU 116 ? OE2 ? A GLU 125 OE2 
12 1 Y 1 A GLU 130 ? CG  ? A GLU 139 CG  
13 1 Y 1 A GLU 130 ? CD  ? A GLU 139 CD  
14 1 Y 1 A GLU 130 ? OE1 ? A GLU 139 OE1 
15 1 Y 1 A GLU 130 ? OE2 ? A GLU 139 OE2 
16 1 Y 1 A ASP 243 ? CG  ? A ASP 252 CG  
17 1 Y 1 A ASP 243 ? OD1 ? A ASP 252 OD1 
18 1 Y 1 A ASP 243 ? OD2 ? A ASP 252 OD2 
19 1 Y 1 A LYS 265 ? CG  ? A LYS 274 CG  
20 1 Y 1 A LYS 265 ? CD  ? A LYS 274 CD  
21 1 Y 1 A LYS 265 ? CE  ? A LYS 274 CE  
22 1 Y 1 A LYS 265 ? NZ  ? A LYS 274 NZ  
23 1 Y 1 A HIS 269 ? CG  ? A HIS 278 CG  
24 1 Y 1 A HIS 269 ? ND1 ? A HIS 278 ND1 
25 1 Y 1 A HIS 269 ? CD2 ? A HIS 278 CD2 
26 1 Y 1 A HIS 269 ? CE1 ? A HIS 278 CE1 
27 1 Y 1 A HIS 269 ? NE2 ? A HIS 278 NE2 
28 1 Y 1 A ASP 284 ? CG  ? A ASP 293 CG  
29 1 Y 1 A ASP 284 ? OD1 ? A ASP 293 OD1 
30 1 Y 1 A ASP 284 ? OD2 ? A ASP 293 OD2 
31 1 Y 1 A GLU 289 ? CG  ? A GLU 298 CG  
32 1 Y 1 A GLU 289 ? CD  ? A GLU 298 CD  
33 1 Y 1 A GLU 289 ? OE1 ? A GLU 298 OE1 
34 1 Y 1 A GLU 289 ? OE2 ? A GLU 298 OE2 
35 1 Y 1 A GLU 290 ? CG  ? A GLU 299 CG  
36 1 Y 1 A GLU 290 ? CD  ? A GLU 299 CD  
37 1 Y 1 A GLU 290 ? OE1 ? A GLU 299 OE1 
38 1 Y 1 A GLU 290 ? OE2 ? A GLU 299 OE2 
39 1 Y 1 A GLU 291 ? CG  ? A GLU 300 CG  
40 1 Y 1 A GLU 291 ? CD  ? A GLU 300 CD  
41 1 Y 1 A GLU 291 ? OE1 ? A GLU 300 OE1 
42 1 Y 1 A GLU 291 ? OE2 ? A GLU 300 OE2 
43 1 Y 1 A GLU 320 ? CG  ? A GLU 329 CG  
44 1 Y 1 A GLU 320 ? CD  ? A GLU 329 CD  
45 1 Y 1 A GLU 320 ? OE1 ? A GLU 329 OE1 
46 1 Y 1 A GLU 320 ? OE2 ? A GLU 329 OE2 
47 1 Y 1 A GLN 376 ? CG  ? A GLN 385 CG  
48 1 Y 1 A GLN 376 ? CD  ? A GLN 385 CD  
49 1 Y 1 A GLN 376 ? OE1 ? A GLN 385 OE1 
50 1 Y 1 A GLN 376 ? NE2 ? A GLN 385 NE2 
# 
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                     8QNW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     88.030 
_cell.length_a_esd                 ? 
_cell.length_b                     89.760 
_cell.length_b_esd                 ? 
_cell.length_c                     49.570 
_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                         8QNW 
_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                   8QNW 
_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             2.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.22 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM MES/Tris, 50 mM ammonium sulfate, 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   1.0332 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, DESY BEAMLINE P11' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0332 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   P11 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QNW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.55 
_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                                     523244 
_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                           95.61 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.85 
_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                                    1.55 
_reflns_shell.d_res_low                                     1.58 
_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                             10512 
_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                                  0.444 
_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                                 8QNW 
_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                            1.55 
_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                     55233 
_refine.ls_number_reflns_R_free                  2762 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.62 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1608 
_refine.ls_R_factor_R_free                       0.1921 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1592 
_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                          1.35 
_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                 19.49 
_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                            0.19 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2800 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         44 
_refine_hist.number_atoms_solvent             433 
_refine_hist.number_atoms_total               3277 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        44.01 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  ? 2908 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.047  ? 3957 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.219 ? 1044 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.068  ? 436  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.013  ? 509  ? 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' 1.55 1.58  . . 100 1899 70.00  . . . . 0.3241 . . . . . . . . . . . 0.4067 
'X-RAY DIFFRACTION' 1.58 1.61  . . 107 2028 75.00  . . . . 0.3180 . . . . . . . . . . . 0.3763 
'X-RAY DIFFRACTION' 1.61 1.64  . . 116 2211 82.00  . . . . 0.2706 . . . . . . . . . . . 0.3041 
'X-RAY DIFFRACTION' 1.64 1.67  . . 126 2394 89.00  . . . . 0.2415 . . . . . . . . . . . 0.2806 
'X-RAY DIFFRACTION' 1.67 1.71  . . 140 2663 98.00  . . . . 0.2080 . . . . . . . . . . . 0.2483 
'X-RAY DIFFRACTION' 1.71 1.75  . . 141 2688 99.00  . . . . 0.1793 . . . . . . . . . . . 0.2214 
'X-RAY DIFFRACTION' 1.75 1.79  . . 142 2698 100.00 . . . . 0.1715 . . . . . . . . . . . 0.2119 
'X-RAY DIFFRACTION' 1.79 1.84  . . 145 2749 100.00 . . . . 0.1721 . . . . . . . . . . . 0.1969 
'X-RAY DIFFRACTION' 1.84 1.89  . . 141 2690 100.00 . . . . 0.1765 . . . . . . . . . . . 0.2355 
'X-RAY DIFFRACTION' 1.89 1.95  . . 144 2717 100.00 . . . . 0.1639 . . . . . . . . . . . 0.2083 
'X-RAY DIFFRACTION' 1.95 2.02  . . 143 2723 100.00 . . . . 0.1551 . . . . . . . . . . . 0.2009 
'X-RAY DIFFRACTION' 2.02 2.10  . . 144 2736 100.00 . . . . 0.1495 . . . . . . . . . . . 0.1837 
'X-RAY DIFFRACTION' 2.10 2.20  . . 143 2722 100.00 . . . . 0.1457 . . . . . . . . . . . 0.1860 
'X-RAY DIFFRACTION' 2.20 2.32  . . 144 2731 100.00 . . . . 0.1468 . . . . . . . . . . . 0.1798 
'X-RAY DIFFRACTION' 2.32 2.46  . . 145 2761 100.00 . . . . 0.1515 . . . . . . . . . . . 0.1687 
'X-RAY DIFFRACTION' 2.46 2.65  . . 145 2745 100.00 . . . . 0.1586 . . . . . . . . . . . 0.1887 
'X-RAY DIFFRACTION' 2.65 2.92  . . 146 2774 100.00 . . . . 0.1571 . . . . . . . . . . . 0.2050 
'X-RAY DIFFRACTION' 2.92 3.34  . . 146 2779 100.00 . . . . 0.1547 . . . . . . . . . . . 0.1795 
'X-RAY DIFFRACTION' 3.34 4.21  . . 148 2816 100.00 . . . . 0.1355 . . . . . . . . . . . 0.1732 
'X-RAY DIFFRACTION' 4.21 44.01 . . 156 2947 100.00 . . . . 0.1513 . . . . . . . . . . . 0.1678 
# 
_struct.entry_id                     8QNW 
_struct.title                        'OPR3 variant with redesigned loop 6 (8aa)' 
_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        8QNW 
_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              8QNW 
_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 8QNW MET A 1   ? UNP Q9FEW9 ?   ?   'initiating methionine' -8  1  
1 8QNW ALA A 2   ? UNP Q9FEW9 ?   ?   'expression tag'        -7  2  
1 8QNW SER A 3   ? UNP Q9FEW9 ?   ?   'expression tag'        -6  3  
1 8QNW HIS A 4   ? UNP Q9FEW9 ?   ?   'expression tag'        -5  4  
1 8QNW HIS A 5   ? UNP Q9FEW9 ?   ?   'expression tag'        -4  5  
1 8QNW HIS A 6   ? UNP Q9FEW9 ?   ?   'expression tag'        -3  6  
1 8QNW HIS A 7   ? UNP Q9FEW9 ?   ?   'expression tag'        -2  7  
1 8QNW HIS A 8   ? UNP Q9FEW9 ?   ?   'expression tag'        -1  8  
1 8QNW HIS A 9   ? UNP Q9FEW9 ?   ?   'expression tag'        0   9  
1 8QNW GLY A 292 ? UNP Q9FEW9 ARG 283 'engineered mutation'   283 10 
1 8QNW ASP A 293 ? UNP Q9FEW9 TYR 284 'engineered mutation'   284 11 
1 8QNW GLY A 294 ? UNP Q9FEW9 VAL 285 'engineered mutation'   285 12 
1 8QNW ARG A 295 ? UNP Q9FEW9 ALA 286 'engineered mutation'   286 13 
1 8QNW ?   A ?   ? UNP Q9FEW9 TYR 287 deletion                ?   14 
1 8QNW ?   A ?   ? UNP Q9FEW9 GLY 288 deletion                ?   15 
1 8QNW ?   A ?   ? UNP Q9FEW9 GLN 289 deletion                ?   16 
1 8QNW ?   A ?   ? UNP Q9FEW9 THR 290 deletion                ?   17 
1 8QNW ?   A ?   ? UNP Q9FEW9 GLU 291 deletion                ?   18 
1 8QNW ?   A ?   ? UNP Q9FEW9 ALA 292 deletion                ?   19 
1 8QNW ?   A ?   ? UNP Q9FEW9 GLY 293 deletion                ?   20 
1 8QNW ?   A ?   ? UNP Q9FEW9 ARG 294 deletion                ?   21 
1 8QNW ?   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 ASN A 260 ? GLY A 280 ? ASN A 251 GLY A 271 1 ? 21 
HELX_P HELX_P11 AB2 GLU A 298 ? TYR A 312 ? GLU A 289 TYR A 303 1 ? 15 
HELX_P HELX_P12 AB3 THR A 323 ? GLN A 333 ? THR A 314 GLN A 324 1 ? 11 
HELX_P HELX_P13 AB4 GLY A 342 ? ASN A 348 ? GLY A 333 ASN A 339 1 ? 7  
HELX_P HELX_P14 AB5 ASP A 350 ? ASN A 358 ? ASP A 341 ASN A 349 1 ? 9  
HELX_P HELX_P15 AB6 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 ? 10 ? 
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      
AA2 9 10 ? 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  THR A 74  ? MET A 75  ? THR A 65  MET A 66  
AA2 2  VAL A 111 ? TRP A 117 ? VAL A 102 TRP A 108 
AA2 3  GLY A 190 ? GLY A 195 ? GLY A 181 GLY A 186 
AA2 4  VAL A 243 ? VAL A 247 ? VAL A 234 VAL A 238 
AA2 5  TYR A 285 ? THR A 289 ? TYR A 276 THR A 280 
AA2 6  PHE A 316 ? SER A 319 ? PHE A 307 SER A 310 
AA2 7  LEU A 338 ? TYR A 341 ? LEU A 329 TYR A 332 
AA2 8  VAL A 36  ? LEU A 38  ? VAL A 27  LEU A 29  
AA2 9  PHE A 68  ? ILE A 70  ? PHE A 59  ILE A 61  
AA2 10 VAL A 111 ? TRP A 117 ? VAL A 102 TRP A 108 
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 THR A 74  ? N THR A 65  O TRP A 117 ? O TRP A 108 
AA2 2 3  N LEU A 116 ? N LEU A 107 O GLU A 192 ? O GLU A 183 
AA2 3 4  N ILE A 193 ? N ILE A 184 O ARG A 246 ? O ARG A 237 
AA2 4 5  N VAL A 245 ? N VAL A 236 O HIS A 287 ? O HIS A 278 
AA2 5 6  N LEU A 286 ? N LEU A 277 O ILE A 317 ? O ILE A 308 
AA2 6 7  N CYS A 318 ? N CYS A 309 O SER A 340 ? O SER A 331 
AA2 7 8  O VAL A 339 ? O VAL A 330 N VAL A 37  ? N VAL A 28  
AA2 8 9  N LEU A 38  ? N LEU A 29  O PHE A 68  ? O PHE A 59  
AA2 9 10 N LEU A 69  ? N LEU A 60  O VAL A 111 ? O VAL A 102 
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                   8QNW 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    803 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    913 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.12 
# 
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  ? ? -48.23  153.02  
2 1 ASP A 205 ? ? -100.50 -161.70 
3 1 ASP A 341 ? ? -94.62  43.21   
4 1 TYR A 369 ? ? -130.07 -62.12  
# 
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 ARG 286 ? A ARG 295 
19 1 Y 1 A GLY 287 ? A GLY 296 
20 1 Y 1 A GLY 377 ? A GLY 386 
21 1 Y 1 A ASN 378 ? A ASN 387 
22 1 Y 1 A GLY 379 ? A GLY 388 
23 1 Y 1 A SER 380 ? A SER 389 
24 1 Y 1 A ASN 381 ? A ASN 390 
25 1 Y 1 A GLY 382 ? A GLY 391 
26 1 Y 1 A PRO 383 ? A PRO 392 
27 1 Y 1 A LEU 384 ? A LEU 393 
28 1 Y 1 A SER 385 ? A SER 394 
29 1 Y 1 A ARG 386 ? A ARG 395 
30 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 
MPD C1     C N N 302 
MPD C2     C N N 303 
MPD O2     O N N 304 
MPD CM     C N N 305 
MPD C3     C N N 306 
MPD C4     C N S 307 
MPD O4     O N N 308 
MPD C5     C N N 309 
MPD H11    H N N 310 
MPD H12    H N N 311 
MPD H13    H N N 312 
MPD HO2    H N N 313 
MPD HM1    H N N 314 
MPD HM2    H N N 315 
MPD HM3    H N N 316 
MPD H31    H N N 317 
MPD H32    H N N 318 
MPD H4     H N N 319 
MPD HO4    H N N 320 
MPD H51    H N N 321 
MPD H52    H N N 322 
MPD H53    H N N 323 
PHE N      N N N 324 
PHE CA     C N S 325 
PHE C      C N N 326 
PHE O      O N N 327 
PHE CB     C N N 328 
PHE CG     C Y N 329 
PHE CD1    C Y N 330 
PHE CD2    C Y N 331 
PHE CE1    C Y N 332 
PHE CE2    C Y N 333 
PHE CZ     C Y N 334 
PHE OXT    O N N 335 
PHE H      H N N 336 
PHE H2     H N N 337 
PHE HA     H N N 338 
PHE HB2    H N N 339 
PHE HB3    H N N 340 
PHE HD1    H N N 341 
PHE HD2    H N N 342 
PHE HE1    H N N 343 
PHE HE2    H N N 344 
PHE HZ     H N N 345 
PHE HXT    H N N 346 
PRO N      N N N 347 
PRO CA     C N S 348 
PRO C      C N N 349 
PRO O      O N N 350 
PRO CB     C N N 351 
PRO CG     C N N 352 
PRO CD     C N N 353 
PRO OXT    O N N 354 
PRO H      H N N 355 
PRO HA     H N N 356 
PRO HB2    H N N 357 
PRO HB3    H N N 358 
PRO HG2    H N N 359 
PRO HG3    H N N 360 
PRO HD2    H N N 361 
PRO HD3    H N N 362 
PRO HXT    H N N 363 
SER N      N N N 364 
SER CA     C N S 365 
SER C      C N N 366 
SER O      O N N 367 
SER CB     C N N 368 
SER OG     O N N 369 
SER OXT    O N N 370 
SER H      H N N 371 
SER H2     H N N 372 
SER HA     H N N 373 
SER HB2    H N N 374 
SER HB3    H N N 375 
SER HG     H N N 376 
SER HXT    H N N 377 
SO4 S      S N N 378 
SO4 O1     O N N 379 
SO4 O2     O N N 380 
SO4 O3     O N N 381 
SO4 O4     O N N 382 
THR N      N N N 383 
THR CA     C N S 384 
THR C      C N N 385 
THR O      O N N 386 
THR CB     C N R 387 
THR OG1    O N N 388 
THR CG2    C N N 389 
THR OXT    O N N 390 
THR H      H N N 391 
THR H2     H N N 392 
THR HA     H N N 393 
THR HB     H N N 394 
THR HG1    H N N 395 
THR HG21   H N N 396 
THR HG22   H N N 397 
THR HG23   H N N 398 
THR HXT    H N N 399 
TRP N      N N N 400 
TRP CA     C N S 401 
TRP C      C N N 402 
TRP O      O N N 403 
TRP CB     C N N 404 
TRP CG     C Y N 405 
TRP CD1    C Y N 406 
TRP CD2    C Y N 407 
TRP NE1    N Y N 408 
TRP CE2    C Y N 409 
TRP CE3    C Y N 410 
TRP CZ2    C Y N 411 
TRP CZ3    C Y N 412 
TRP CH2    C Y N 413 
TRP OXT    O N N 414 
TRP H      H N N 415 
TRP H2     H N N 416 
TRP HA     H N N 417 
TRP HB2    H N N 418 
TRP HB3    H N N 419 
TRP HD1    H N N 420 
TRP HE1    H N N 421 
TRP HE3    H N N 422 
TRP HZ2    H N N 423 
TRP HZ3    H N N 424 
TRP HH2    H N N 425 
TRP HXT    H N N 426 
TYR N      N N N 427 
TYR CA     C N S 428 
TYR C      C N N 429 
TYR O      O N N 430 
TYR CB     C N N 431 
TYR CG     C Y N 432 
TYR CD1    C Y N 433 
TYR CD2    C Y N 434 
TYR CE1    C Y N 435 
TYR CE2    C Y N 436 
TYR CZ     C Y N 437 
TYR OH     O N N 438 
TYR OXT    O N N 439 
TYR H      H N N 440 
TYR H2     H N N 441 
TYR HA     H N N 442 
TYR HB2    H N N 443 
TYR HB3    H N N 444 
TYR HD1    H N N 445 
TYR HD2    H N N 446 
TYR HE1    H N N 447 
TYR HE2    H N N 448 
TYR HH     H N N 449 
TYR HXT    H N N 450 
VAL N      N N N 451 
VAL CA     C N S 452 
VAL C      C N N 453 
VAL O      O N N 454 
VAL CB     C N N 455 
VAL CG1    C N N 456 
VAL CG2    C N N 457 
VAL OXT    O N N 458 
VAL H      H N N 459 
VAL H2     H N N 460 
VAL HA     H N N 461 
VAL HB     H N N 462 
VAL HG11   H N N 463 
VAL HG12   H N N 464 
VAL HG13   H N N 465 
VAL HG21   H N N 466 
VAL HG22   H N N 467 
VAL HG23   H N N 468 
VAL HXT    H N N 469 
# 
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 
MPD C1    C2     sing N N 291 
MPD C1    H11    sing N N 292 
MPD C1    H12    sing N N 293 
MPD C1    H13    sing N N 294 
MPD C2    O2     sing N N 295 
MPD C2    CM     sing N N 296 
MPD C2    C3     sing N N 297 
MPD O2    HO2    sing N N 298 
MPD CM    HM1    sing N N 299 
MPD CM    HM2    sing N N 300 
MPD CM    HM3    sing N N 301 
MPD C3    C4     sing N N 302 
MPD C3    H31    sing N N 303 
MPD C3    H32    sing N N 304 
MPD C4    O4     sing N N 305 
MPD C4    C5     sing N N 306 
MPD C4    H4     sing N N 307 
MPD O4    HO4    sing N N 308 
MPD C5    H51    sing N N 309 
MPD C5    H52    sing N N 310 
MPD C5    H53    sing N N 311 
PHE N     CA     sing N N 312 
PHE N     H      sing N N 313 
PHE N     H2     sing N N 314 
PHE CA    C      sing N N 315 
PHE CA    CB     sing N N 316 
PHE CA    HA     sing N N 317 
PHE C     O      doub N N 318 
PHE C     OXT    sing N N 319 
PHE CB    CG     sing N N 320 
PHE CB    HB2    sing N N 321 
PHE CB    HB3    sing N N 322 
PHE CG    CD1    doub Y N 323 
PHE CG    CD2    sing Y N 324 
PHE CD1   CE1    sing Y N 325 
PHE CD1   HD1    sing N N 326 
PHE CD2   CE2    doub Y N 327 
PHE CD2   HD2    sing N N 328 
PHE CE1   CZ     doub Y N 329 
PHE CE1   HE1    sing N N 330 
PHE CE2   CZ     sing Y N 331 
PHE CE2   HE2    sing N N 332 
PHE CZ    HZ     sing N N 333 
PHE OXT   HXT    sing N N 334 
PRO N     CA     sing N N 335 
PRO N     CD     sing N N 336 
PRO N     H      sing N N 337 
PRO CA    C      sing N N 338 
PRO CA    CB     sing N N 339 
PRO CA    HA     sing N N 340 
PRO C     O      doub N N 341 
PRO C     OXT    sing N N 342 
PRO CB    CG     sing N N 343 
PRO CB    HB2    sing N N 344 
PRO CB    HB3    sing N N 345 
PRO CG    CD     sing N N 346 
PRO CG    HG2    sing N N 347 
PRO CG    HG3    sing N N 348 
PRO CD    HD2    sing N N 349 
PRO CD    HD3    sing N N 350 
PRO OXT   HXT    sing N N 351 
SER N     CA     sing N N 352 
SER N     H      sing N N 353 
SER N     H2     sing N N 354 
SER CA    C      sing N N 355 
SER CA    CB     sing N N 356 
SER CA    HA     sing N N 357 
SER C     O      doub N N 358 
SER C     OXT    sing N N 359 
SER CB    OG     sing N N 360 
SER CB    HB2    sing N N 361 
SER CB    HB3    sing N N 362 
SER OG    HG     sing N N 363 
SER OXT   HXT    sing N N 364 
SO4 S     O1     doub N N 365 
SO4 S     O2     doub N N 366 
SO4 S     O3     sing N N 367 
SO4 S     O4     sing N N 368 
THR N     CA     sing N N 369 
THR N     H      sing N N 370 
THR N     H2     sing N N 371 
THR CA    C      sing N N 372 
THR CA    CB     sing N N 373 
THR CA    HA     sing N N 374 
THR C     O      doub N N 375 
THR C     OXT    sing N N 376 
THR CB    OG1    sing N N 377 
THR CB    CG2    sing N N 378 
THR CB    HB     sing N N 379 
THR OG1   HG1    sing N N 380 
THR CG2   HG21   sing N N 381 
THR CG2   HG22   sing N N 382 
THR CG2   HG23   sing N N 383 
THR OXT   HXT    sing N N 384 
TRP N     CA     sing N N 385 
TRP N     H      sing N N 386 
TRP N     H2     sing N N 387 
TRP CA    C      sing N N 388 
TRP CA    CB     sing N N 389 
TRP CA    HA     sing N N 390 
TRP C     O      doub N N 391 
TRP C     OXT    sing N N 392 
TRP CB    CG     sing N N 393 
TRP CB    HB2    sing N N 394 
TRP CB    HB3    sing N N 395 
TRP CG    CD1    doub Y N 396 
TRP CG    CD2    sing Y N 397 
TRP CD1   NE1    sing Y N 398 
TRP CD1   HD1    sing N N 399 
TRP CD2   CE2    doub Y N 400 
TRP CD2   CE3    sing Y N 401 
TRP NE1   CE2    sing Y N 402 
TRP NE1   HE1    sing N N 403 
TRP CE2   CZ2    sing Y N 404 
TRP CE3   CZ3    doub Y N 405 
TRP CE3   HE3    sing N N 406 
TRP CZ2   CH2    doub Y N 407 
TRP CZ2   HZ2    sing N N 408 
TRP CZ3   CH2    sing Y N 409 
TRP CZ3   HZ3    sing N N 410 
TRP CH2   HH2    sing N N 411 
TRP OXT   HXT    sing N N 412 
TYR N     CA     sing N N 413 
TYR N     H      sing N N 414 
TYR N     H2     sing N N 415 
TYR CA    C      sing N N 416 
TYR CA    CB     sing N N 417 
TYR CA    HA     sing N N 418 
TYR C     O      doub N N 419 
TYR C     OXT    sing N N 420 
TYR CB    CG     sing N N 421 
TYR CB    HB2    sing N N 422 
TYR CB    HB3    sing N N 423 
TYR CG    CD1    doub Y N 424 
TYR CG    CD2    sing Y N 425 
TYR CD1   CE1    sing Y N 426 
TYR CD1   HD1    sing N N 427 
TYR CD2   CE2    doub Y N 428 
TYR CD2   HD2    sing N N 429 
TYR CE1   CZ     doub Y N 430 
TYR CE1   HE1    sing N N 431 
TYR CE2   CZ     sing Y N 432 
TYR CE2   HE2    sing N N 433 
TYR CZ    OH     sing N N 434 
TYR OH    HH     sing N N 435 
TYR OXT   HXT    sing N N 436 
VAL N     CA     sing N N 437 
VAL N     H      sing N N 438 
VAL N     H2     sing N N 439 
VAL CA    C      sing N N 440 
VAL CA    CB     sing N N 441 
VAL CA    HA     sing N N 442 
VAL C     O      doub N N 443 
VAL C     OXT    sing N N 444 
VAL CB    CG1    sing N N 445 
VAL CB    CG2    sing N N 446 
VAL CB    HB     sing N N 447 
VAL CG1   HG11   sing N N 448 
VAL CG1   HG12   sing N N 449 
VAL CG1   HG13   sing N N 450 
VAL CG2   HG21   sing N N 451 
VAL CG2   HG22   sing N N 452 
VAL CG2   HG23   sing N N 453 
VAL OXT   HXT    sing N N 454 
# 
_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                    8QNW 
_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]   0.011360 
_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]   0.011141 
_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]   0.020173 
_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 18  ? 36.527 8.901  -2.393 1.00 53.22 ? 9   ASN A N     1 
ATOM   2    C CA    . ASN A 1 18  ? 37.076 7.872  -1.513 1.00 51.01 ? 9   ASN A CA    1 
ATOM   3    C C     . ASN A 1 18  ? 36.505 7.985  -0.100 1.00 54.92 ? 9   ASN A C     1 
ATOM   4    O O     . ASN A 1 18  ? 36.463 7.012  0.647  1.00 54.03 ? 9   ASN A O     1 
ATOM   5    C CB    . ASN A 1 18  ? 38.604 7.976  -1.465 1.00 49.56 ? 9   ASN A CB    1 
ATOM   6    N N     . ASN A 1 19  ? 36.042 9.187  0.238  1.00 39.86 ? 10  ASN A N     1 
ATOM   7    C CA    . ASN A 1 19  ? 35.732 9.559  1.612  1.00 32.18 ? 10  ASN A CA    1 
ATOM   8    C C     . ASN A 1 19  ? 34.273 9.238  1.935  1.00 28.20 ? 10  ASN A C     1 
ATOM   9    O O     . ASN A 1 19  ? 33.369 9.850  1.344  1.00 27.46 ? 10  ASN A O     1 
ATOM   10   C CB    . ASN A 1 19  ? 36.021 11.044 1.789  1.00 36.79 ? 10  ASN A CB    1 
ATOM   11   C CG    . ASN A 1 19  ? 35.858 11.516 3.198  1.00 31.68 ? 10  ASN A CG    1 
ATOM   12   O OD1   . ASN A 1 19  ? 35.186 10.884 4.014  1.00 29.91 ? 10  ASN A OD1   1 
ATOM   13   N ND2   . ASN A 1 19  ? 36.486 12.643 3.506  1.00 33.46 ? 10  ASN A ND2   1 
ATOM   14   N N     . PRO A 1 20  ? 33.989 8.298  2.842  1.00 29.64 ? 11  PRO A N     1 
ATOM   15   C CA    . PRO A 1 20  ? 32.581 7.950  3.116  1.00 25.47 ? 11  PRO A CA    1 
ATOM   16   C C     . PRO A 1 20  ? 31.779 9.081  3.743  1.00 21.65 ? 11  PRO A C     1 
ATOM   17   O O     . PRO A 1 20  ? 30.540 9.030  3.706  1.00 22.48 ? 11  PRO A O     1 
ATOM   18   C CB    . PRO A 1 20  ? 32.694 6.757  4.072  1.00 30.18 ? 11  PRO A CB    1 
ATOM   19   C CG    . PRO A 1 20  ? 34.001 6.985  4.764  1.00 38.76 ? 11  PRO A CG    1 
ATOM   20   C CD    . PRO A 1 20  ? 34.917 7.562  3.720  1.00 30.66 ? 11  PRO A CD    1 
ATOM   21   N N     . LEU A 1 21  ? 32.434 10.085 4.331  1.00 23.95 ? 12  LEU A N     1 
ATOM   22   C CA    . LEU A 1 21  ? 31.712 11.282 4.756  1.00 21.48 ? 12  LEU A CA    1 
ATOM   23   C C     . LEU A 1 21  ? 31.034 11.965 3.577  1.00 23.35 ? 12  LEU A C     1 
ATOM   24   O O     . LEU A 1 21  ? 30.113 12.760 3.770  1.00 21.73 ? 12  LEU A O     1 
ATOM   25   C CB    . LEU A 1 21  ? 32.664 12.269 5.424  1.00 24.71 ? 12  LEU A CB    1 
ATOM   26   C CG    . LEU A 1 21  ? 33.029 12.002 6.877  1.00 23.87 ? 12  LEU A CG    1 
ATOM   27   C CD1   . LEU A 1 21  ? 33.985 13.097 7.322  1.00 24.01 ? 12  LEU A CD1   1 
ATOM   28   C CD2   . LEU A 1 21  ? 31.769 11.966 7.747  1.00 22.23 ? 12  LEU A CD2   1 
ATOM   29   N N     . PHE A 1 22  ? 31.460 11.671 2.349  1.00 21.79 ? 13  PHE A N     1 
ATOM   30   C CA    . PHE A 1 22  ? 30.847 12.278 1.180  1.00 21.37 ? 13  PHE A CA    1 
ATOM   31   C C     . PHE A 1 22  ? 30.047 11.274 0.375  1.00 24.89 ? 13  PHE A C     1 
ATOM   32   O O     . PHE A 1 22  ? 29.817 11.470 -0.825 1.00 28.48 ? 13  PHE A O     1 
ATOM   33   C CB    . PHE A 1 22  ? 31.920 12.995 0.353  1.00 21.72 ? 13  PHE A CB    1 
ATOM   34   C CG    . PHE A 1 22  ? 32.411 14.196 1.065  1.00 26.41 ? 13  PHE A CG    1 
ATOM   35   C CD1   . PHE A 1 22  ? 33.429 14.088 1.996  1.00 28.70 ? 13  PHE A CD1   1 
ATOM   36   C CD2   . PHE A 1 22  ? 31.730 15.402 0.952  1.00 27.52 ? 13  PHE A CD2   1 
ATOM   37   C CE1   . PHE A 1 22  ? 33.828 15.193 2.759  1.00 34.45 ? 13  PHE A CE1   1 
ATOM   38   C CE2   . PHE A 1 22  ? 32.129 16.513 1.698  1.00 28.89 ? 13  PHE A CE2   1 
ATOM   39   C CZ    . PHE A 1 22  ? 33.176 16.400 2.611  1.00 26.70 ? 13  PHE A CZ    1 
ATOM   40   N N     . SER A 1 23  ? 29.620 10.219 1.013  1.00 22.99 ? 14  SER A N     1 
ATOM   41   C CA    . SER A 1 23  ? 28.593 9.440  0.354  1.00 22.89 ? 14  SER A CA    1 
ATOM   42   C C     . SER A 1 23  ? 27.220 9.970  0.742  1.00 28.13 ? 14  SER A C     1 
ATOM   43   O O     . SER A 1 23  ? 27.027 10.449 1.864  1.00 24.85 ? 14  SER A O     1 
ATOM   44   C CB    . SER A 1 23  ? 28.710 7.974  0.732  1.00 30.39 ? 14  SER A CB    1 
ATOM   45   O OG    . SER A 1 23  ? 28.626 7.833  2.127  1.00 31.04 ? 14  SER A OG    1 
ATOM   46   N N     . PRO A 1 24  ? 26.263 9.902  -0.177 1.00 20.56 ? 15  PRO A N     1 
ATOM   47   C CA    . PRO A 1 24  ? 24.915 10.393 0.109  1.00 19.95 ? 15  PRO A CA    1 
ATOM   48   C C     . PRO A 1 24  ? 24.210 9.547  1.155  1.00 22.79 ? 15  PRO A C     1 
ATOM   49   O O     . PRO A 1 24  ? 24.536 8.380  1.392  1.00 24.52 ? 15  PRO A O     1 
ATOM   50   C CB    . PRO A 1 24  ? 24.209 10.305 -1.247 1.00 26.97 ? 15  PRO A CB    1 
ATOM   51   C CG    . PRO A 1 24  ? 24.987 9.272  -2.003 1.00 32.04 ? 15  PRO A CG    1 
ATOM   52   C CD    . PRO A 1 24  ? 26.405 9.450  -1.573 1.00 28.00 ? 15  PRO A CD    1 
ATOM   53   N N     . TYR A 1 25  ? 23.232 10.175 1.800  1.00 22.02 ? 16  TYR A N     1 
ATOM   54   C CA    . TYR A 1 25  ? 22.457 9.514  2.842  1.00 20.17 ? 16  TYR A CA    1 
ATOM   55   C C     . TYR A 1 25  ? 21.023 10.010 2.782  1.00 24.21 ? 16  TYR A C     1 
ATOM   56   O O     . TYR A 1 25  ? 20.784 11.217 2.670  1.00 21.92 ? 16  TYR A O     1 
ATOM   57   C CB    . TYR A 1 25  ? 23.056 9.776  4.234  1.00 22.56 ? 16  TYR A CB    1 
ATOM   58   C CG    . TYR A 1 25  ? 22.361 8.960  5.284  1.00 20.19 ? 16  TYR A CG    1 
ATOM   59   C CD1   . TYR A 1 25  ? 22.630 7.605  5.422  1.00 21.45 ? 16  TYR A CD1   1 
ATOM   60   C CD2   . TYR A 1 25  ? 21.403 9.530  6.114  1.00 21.24 ? 16  TYR A CD2   1 
ATOM   61   C CE1   . TYR A 1 25  ? 21.965 6.830  6.362  1.00 21.05 ? 16  TYR A CE1   1 
ATOM   62   C CE2   . TYR A 1 25  ? 20.724 8.755  7.067  1.00 18.69 ? 16  TYR A CE2   1 
ATOM   63   C CZ    . TYR A 1 25  ? 21.017 7.413  7.174  1.00 20.23 ? 16  TYR A CZ    1 
ATOM   64   O OH    . TYR A 1 25  ? 20.352 6.649  8.094  1.00 21.62 ? 16  TYR A OH    1 
ATOM   65   N N     . LYS A 1 26  ? 20.073 9.085  2.861  1.00 19.10 ? 17  LYS A N     1 
ATOM   66   C CA    . LYS A 1 26  ? 18.664 9.440  2.910  1.00 22.70 ? 17  LYS A CA    1 
ATOM   67   C C     . LYS A 1 26  ? 18.233 9.521  4.368  1.00 24.23 ? 17  LYS A C     1 
ATOM   68   O O     . LYS A 1 26  ? 18.120 8.501  5.046  1.00 26.54 ? 17  LYS A O     1 
ATOM   69   C CB    . LYS A 1 26  ? 17.818 8.439  2.122  1.00 25.29 ? 17  LYS A CB    1 
ATOM   70   C CG    . LYS A 1 26  ? 16.474 9.037  1.704  1.00 35.09 ? 17  LYS A CG    1 
ATOM   71   C CD    . LYS A 1 26  ? 15.468 7.978  1.256  1.00 44.66 ? 17  LYS A CD    1 
ATOM   72   C CE    . LYS A 1 26  ? 14.143 8.633  0.873  1.00 44.48 ? 17  LYS A CE    1 
ATOM   73   N NZ    . LYS A 1 26  ? 14.339 9.594  -0.247 1.00 52.72 ? 17  LYS A NZ    1 
ATOM   74   N N     . MET A 1 27  ? 18.032 10.747 4.851  1.00 22.43 ? 18  MET A N     1 
ATOM   75   C CA    . MET A 1 27  ? 17.470 11.023 6.182  1.00 21.04 ? 18  MET A CA    1 
ATOM   76   C C     . MET A 1 27  ? 15.967 11.199 6.047  1.00 25.79 ? 18  MET A C     1 
ATOM   77   O O     . MET A 1 27  ? 15.458 12.314 5.930  1.00 25.66 ? 18  MET A O     1 
ATOM   78   C CB    . MET A 1 27  ? 18.095 12.268 6.789  1.00 20.74 ? 18  MET A CB    1 
ATOM   79   C CG    . MET A 1 27  ? 17.917 12.387 8.311  1.00 23.18 ? 18  MET A CG    1 
ATOM   80   S SD    . MET A 1 27  ? 18.660 13.894 8.983  1.00 25.26 ? 18  MET A SD    1 
ATOM   81   C CE    . MET A 1 27  ? 17.951 15.262 8.049  1.00 23.69 ? 18  MET A CE    1 
ATOM   82   N N     . GLY A 1 28  ? 15.260 10.071 6.025  1.00 37.37 ? 19  GLY A N     1 
ATOM   83   C CA    . GLY A 1 28  ? 13.819 10.110 5.834  1.00 37.55 ? 19  GLY A CA    1 
ATOM   84   C C     . GLY A 1 28  ? 13.521 10.667 4.467  1.00 22.38 ? 19  GLY A C     1 
ATOM   85   O O     . GLY A 1 28  ? 14.006 10.157 3.451  1.00 33.57 ? 19  GLY A O     1 
ATOM   86   N N     . LYS A 1 29  ? 12.744 11.759 4.405  1.00 28.45 ? 20  LYS A N     1 
ATOM   87   C CA    . LYS A 1 29  ? 12.451 12.345 3.099  1.00 25.54 ? 20  LYS A CA    1 
ATOM   88   C C     . LYS A 1 29  ? 13.607 13.145 2.519  1.00 23.51 ? 20  LYS A C     1 
ATOM   89   O O     . LYS A 1 29  ? 13.564 13.485 1.321  1.00 27.88 ? 20  LYS A O     1 
ATOM   90   C CB    . LYS A 1 29  ? 11.212 13.250 3.180  1.00 31.94 ? 20  LYS A CB    1 
ATOM   91   N N     . PHE A 1 30  ? 14.647 13.432 3.291  1.00 18.03 ? 21  PHE A N     1 
ATOM   92   C CA    . PHE A 1 30  ? 15.680 14.361 2.871  1.00 19.60 ? 21  PHE A CA    1 
ATOM   93   C C     . PHE A 1 30  ? 16.871 13.613 2.286  1.00 20.28 ? 21  PHE A C     1 
ATOM   94   O O     . PHE A 1 30  ? 17.444 12.722 2.934  1.00 22.45 ? 21  PHE A O     1 
ATOM   95   C CB    . PHE A 1 30  ? 16.118 15.239 4.045  1.00 22.70 ? 21  PHE A CB    1 
ATOM   96   C CG    . PHE A 1 30  ? 14.957 15.875 4.780  1.00 22.51 ? 21  PHE A CG    1 
ATOM   97   C CD1   . PHE A 1 30  ? 14.256 16.923 4.218  1.00 30.07 ? 21  PHE A CD1   1 
ATOM   98   C CD2   . PHE A 1 30  ? 14.562 15.399 6.022  1.00 24.61 ? 21  PHE A CD2   1 
ATOM   99   C CE1   . PHE A 1 30  ? 13.187 17.497 4.898  1.00 25.37 ? 21  PHE A CE1   1 
ATOM   100  C CE2   . PHE A 1 30  ? 13.501 15.963 6.687  1.00 29.35 ? 21  PHE A CE2   1 
ATOM   101  C CZ    . PHE A 1 30  ? 12.817 17.002 6.132  1.00 26.41 ? 21  PHE A CZ    1 
ATOM   102  N N     . ASN A 1 31  ? 17.240 13.974 1.050  1.00 18.50 ? 22  ASN A N     1 
ATOM   103  C CA    . ASN A 1 31  ? 18.370 13.364 0.367  1.00 20.45 ? 22  ASN A CA    1 
ATOM   104  C C     . ASN A 1 31  ? 19.611 14.188 0.674  1.00 20.44 ? 22  ASN A C     1 
ATOM   105  O O     . ASN A 1 31  ? 19.840 15.234 0.063  1.00 25.51 ? 22  ASN A O     1 
ATOM   106  C CB    . ASN A 1 31  ? 18.104 13.305 -1.138 1.00 18.79 ? 22  ASN A CB    1 
ATOM   107  C CG    . ASN A 1 31  ? 16.865 12.495 -1.468 1.00 21.68 ? 22  ASN A CG    1 
ATOM   108  O OD1   . ASN A 1 31  ? 16.775 11.323 -1.100 1.00 25.40 ? 22  ASN A OD1   1 
ATOM   109  N ND2   . ASN A 1 31  ? 15.880 13.122 -2.094 1.00 23.43 ? 22  ASN A ND2   1 
ATOM   110  N N     . LEU A 1 32  ? 20.427 13.728 1.613  1.00 17.90 ? 23  LEU A N     1 
ATOM   111  C CA    . LEU A 1 32  ? 21.644 14.467 1.915  1.00 17.30 ? 23  LEU A CA    1 
ATOM   112  C C     . LEU A 1 32  ? 22.787 14.026 1.017  1.00 17.57 ? 23  LEU A C     1 
ATOM   113  O O     . LEU A 1 32  ? 22.890 12.856 0.626  1.00 20.05 ? 23  LEU A O     1 
ATOM   114  C CB    . LEU A 1 32  ? 22.035 14.284 3.393  1.00 16.01 ? 23  LEU A CB    1 
ATOM   115  C CG    . LEU A 1 32  ? 20.927 14.616 4.380  1.00 15.63 ? 23  LEU A CG    1 
ATOM   116  C CD1   . LEU A 1 32  ? 21.482 14.369 5.812  1.00 17.59 ? 23  LEU A CD1   1 
ATOM   117  C CD2   . LEU A 1 32  ? 20.490 16.066 4.244  1.00 18.95 ? 23  LEU A CD2   1 
ATOM   118  N N     . SER A 1 33  ? 23.668 14.973 0.700  1.00 17.21 ? 24  SER A N     1 
ATOM   119  C CA    . SER A 1 33  ? 24.757 14.684 -0.223 1.00 17.67 ? 24  SER A CA    1 
ATOM   120  C C     . SER A 1 33  ? 26.044 14.340 0.486  1.00 21.06 ? 24  SER A C     1 
ATOM   121  O O     . SER A 1 33  ? 26.981 13.840 -0.160 1.00 21.21 ? 24  SER A O     1 
ATOM   122  C CB    . SER A 1 33  ? 24.980 15.880 -1.161 1.00 23.04 ? 24  SER A CB    1 
ATOM   123  O OG    . SER A 1 33  ? 25.631 16.920 -0.450 1.00 31.52 ? 24  SER A OG    1 
ATOM   124  N N     . HIS A 1 34  ? 26.116 14.609 1.791  1.00 19.21 ? 25  HIS A N     1 
ATOM   125  C CA    . HIS A 1 34  ? 27.285 14.275 2.578  1.00 17.14 ? 25  HIS A CA    1 
ATOM   126  C C     . HIS A 1 34  ? 26.834 14.198 4.032  1.00 14.74 ? 25  HIS A C     1 
ATOM   127  O O     . HIS A 1 34  ? 25.701 14.571 4.366  1.00 16.77 ? 25  HIS A O     1 
ATOM   128  C CB    . HIS A 1 34  ? 28.395 15.312 2.372  1.00 16.66 ? 25  HIS A CB    1 
ATOM   129  C CG    . HIS A 1 34  ? 28.019 16.686 2.840  1.00 17.37 ? 25  HIS A CG    1 
ATOM   130  N ND1   . HIS A 1 34  ? 27.993 17.037 4.178  1.00 17.52 ? 25  HIS A ND1   1 
ATOM   131  C CD2   . HIS A 1 34  ? 27.669 17.795 2.149  1.00 20.66 ? 25  HIS A CD2   1 
ATOM   132  C CE1   . HIS A 1 34  ? 27.631 18.304 4.285  1.00 19.20 ? 25  HIS A CE1   1 
ATOM   133  N NE2   . HIS A 1 34  ? 27.430 18.787 3.065  1.00 17.20 ? 25  HIS A NE2   1 
ATOM   134  N N     . ARG A 1 35  ? 27.745 13.758 4.887  1.00 16.58 ? 26  ARG A N     1 
ATOM   135  C CA    . ARG A 1 35  ? 27.388 13.359 6.246  1.00 15.88 ? 26  ARG A CA    1 
ATOM   136  C C     . ARG A 1 35  ? 27.869 14.337 7.296  1.00 18.05 ? 26  ARG A C     1 
ATOM   137  O O     . ARG A 1 35  ? 27.763 14.022 8.488  1.00 16.78 ? 26  ARG A O     1 
ATOM   138  C CB    . ARG A 1 35  ? 27.947 11.972 6.569  1.00 19.48 ? 26  ARG A CB    1 
ATOM   139  C CG    . ARG A 1 35  ? 27.919 11.050 5.408  1.00 25.13 ? 26  ARG A CG    1 
ATOM   140  C CD    . ARG A 1 35  ? 26.760 10.186 5.449  1.00 20.65 ? 26  ARG A CD    1 
ATOM   141  N NE    . ARG A 1 35  ? 26.831 9.048  4.517  1.00 22.27 ? 26  ARG A NE    1 
ATOM   142  C CZ    . ARG A 1 35  ? 26.386 7.835  4.813  1.00 24.18 ? 26  ARG A CZ    1 
ATOM   143  N NH1   . ARG A 1 35  ? 26.050 7.508  6.060  1.00 20.78 ? 26  ARG A NH1   1 
ATOM   144  N NH2   . ARG A 1 35  ? 26.281 6.929  3.844  1.00 20.55 ? 26  ARG A NH2   1 
ATOM   145  N N     . VAL A 1 36  ? 28.395 15.498 6.905  1.00 16.68 ? 27  VAL A N     1 
ATOM   146  C CA    . VAL A 1 36  ? 28.936 16.465 7.864  1.00 16.31 ? 27  VAL A CA    1 
ATOM   147  C C     . VAL A 1 36  ? 27.806 17.397 8.261  1.00 15.77 ? 27  VAL A C     1 
ATOM   148  O O     . VAL A 1 36  ? 27.252 18.095 7.408  1.00 18.10 ? 27  VAL A O     1 
ATOM   149  C CB    . VAL A 1 36  ? 30.107 17.257 7.263  1.00 19.59 ? 27  VAL A CB    1 
ATOM   150  C CG1   . VAL A 1 36  ? 30.635 18.327 8.262  1.00 17.90 ? 27  VAL A CG1   1 
ATOM   151  C CG2   . VAL A 1 36  ? 31.208 16.320 6.779  1.00 22.08 ? 27  VAL A CG2   1 
ATOM   152  N N     . VAL A 1 37  ? 27.494 17.442 9.555  1.00 16.26 ? 28  VAL A N     1 
ATOM   153  C CA    . VAL A 1 37  ? 26.320 18.137 10.076 1.00 15.98 ? 28  VAL A CA    1 
ATOM   154  C C     . VAL A 1 37  ? 26.781 19.314 10.925 1.00 14.43 ? 28  VAL A C     1 
ATOM   155  O O     . VAL A 1 37  ? 27.725 19.181 11.706 1.00 15.32 ? 28  VAL A O     1 
ATOM   156  C CB    . VAL A 1 37  ? 25.448 17.188 10.930 1.00 15.64 ? 28  VAL A CB    1 
ATOM   157  C CG1   . VAL A 1 37  ? 24.279 17.944 11.560 1.00 14.59 ? 28  VAL A CG1   1 
ATOM   158  C CG2   . VAL A 1 37  ? 24.943 16.029 10.034 1.00 15.12 ? 28  VAL A CG2   1 
ATOM   159  N N     . LEU A 1 38  ? 26.106 20.448 10.793 1.00 14.33 ? 29  LEU A N     1 
ATOM   160  C CA    . LEU A 1 38  ? 26.359 21.556 11.718 1.00 15.84 ? 29  LEU A CA    1 
ATOM   161  C C     . LEU A 1 38  ? 25.639 21.274 13.022 1.00 14.67 ? 29  LEU A C     1 
ATOM   162  O O     . LEU A 1 38  ? 24.411 21.226 13.046 1.00 15.14 ? 29  LEU A O     1 
ATOM   163  C CB    . LEU A 1 38  ? 25.887 22.896 11.145 1.00 15.52 ? 29  LEU A CB    1 
ATOM   164  C CG    . LEU A 1 38  ? 25.839 24.089 12.119 1.00 18.28 ? 29  LEU A CG    1 
ATOM   165  C CD1   . LEU A 1 38  ? 27.244 24.463 12.534 1.00 16.98 ? 29  LEU A CD1   1 
ATOM   166  C CD2   . LEU A 1 38  ? 25.159 25.299 11.468 1.00 19.02 ? 29  LEU A CD2   1 
ATOM   167  N N     . ALA A 1 39  ? 26.400 21.089 14.099 1.00 16.35 ? 30  ALA A N     1 
ATOM   168  C CA    . ALA A 1 39  ? 25.794 20.878 15.412 1.00 14.15 ? 30  ALA A CA    1 
ATOM   169  C C     . ALA A 1 39  ? 25.127 22.163 15.914 1.00 16.47 ? 30  ALA A C     1 
ATOM   170  O O     . ALA A 1 39  ? 25.543 23.279 15.565 1.00 15.75 ? 30  ALA A O     1 
ATOM   171  C CB    . ALA A 1 39  ? 26.855 20.413 16.416 1.00 16.00 ? 30  ALA A CB    1 
ATOM   172  N N     . PRO A 1 40  ? 24.089 22.030 16.738 1.00 15.06 ? 31  PRO A N     1 
ATOM   173  C CA    . PRO A 1 40  ? 23.405 23.219 17.271 1.00 16.13 ? 31  PRO A CA    1 
ATOM   174  C C     . PRO A 1 40  ? 24.332 23.989 18.194 1.00 16.06 ? 31  PRO A C     1 
ATOM   175  O O     . PRO A 1 40  ? 24.893 23.418 19.135 1.00 16.05 ? 31  PRO A O     1 
ATOM   176  C CB    . PRO A 1 40  ? 22.216 22.627 18.044 1.00 15.93 ? 31  PRO A CB    1 
ATOM   177  C CG    . PRO A 1 40  ? 22.676 21.221 18.438 1.00 14.21 ? 31  PRO A CG    1 
ATOM   178  C CD    . PRO A 1 40  ? 23.508 20.771 17.246 1.00 13.00 ? 31  PRO A CD    1 
ATOM   179  N N     . MET A 1 41  ? 24.468 25.299 17.954 1.00 15.37 ? 32  MET A N     1 
ATOM   180  C CA    . MET A 1 41  ? 25.220 26.120 18.899 1.00 13.47 ? 32  MET A CA    1 
ATOM   181  C C     . MET A 1 41  ? 24.634 27.500 19.135 1.00 14.79 ? 32  MET A C     1 
ATOM   182  O O     . MET A 1 41  ? 24.511 28.317 18.219 1.00 17.21 ? 32  MET A O     1 
ATOM   183  C CB    . MET A 1 41  ? 26.734 26.241 18.608 1.00 17.03 ? 32  MET A CB    1 
ATOM   184  C CG    . MET A 1 41  ? 27.498 24.965 18.263 1.00 16.97 ? 32  MET A CG    1 
ATOM   185  S SD    . MET A 1 41  ? 29.113 25.347 17.561 1.00 18.82 ? 32  MET A SD    1 
ATOM   186  C CE    . MET A 1 41  ? 28.622 25.407 15.823 1.00 17.98 ? 32  MET A CE    1 
ATOM   187  N N     . THR A 1 42  ? 24.363 27.745 20.420 1.00 15.44 ? 33  THR A N     1 
ATOM   188  C CA    . THR A 1 42  ? 23.980 29.043 20.947 1.00 15.47 ? 33  THR A CA    1 
ATOM   189  C C     . THR A 1 42  ? 25.102 30.046 20.741 1.00 17.41 ? 33  THR A C     1 
ATOM   190  O O     . THR A 1 42  ? 26.236 29.816 21.175 1.00 16.42 ? 33  THR A O     1 
ATOM   191  C CB    . THR A 1 42  ? 23.700 28.868 22.435 1.00 16.01 ? 33  THR A CB    1 
ATOM   192  O OG1   . THR A 1 42  ? 22.541 28.042 22.609 1.00 18.74 ? 33  THR A OG1   1 
ATOM   193  C CG2   . THR A 1 42  ? 23.492 30.245 23.115 1.00 15.21 ? 33  THR A CG2   1 
ATOM   194  N N     . ARG A 1 43  ? 24.784 31.160 20.078 1.00 15.93 ? 34  ARG A N     1 
ATOM   195  C CA    . ARG A 1 43  ? 25.756 32.221 19.841 1.00 15.96 ? 34  ARG A CA    1 
ATOM   196  C C     . ARG A 1 43  ? 25.296 33.596 20.335 1.00 14.10 ? 34  ARG A C     1 
ATOM   197  O O     . ARG A 1 43  ? 26.108 34.534 20.349 1.00 14.86 ? 34  ARG A O     1 
ATOM   198  C CB    . ARG A 1 43  ? 26.097 32.298 18.343 1.00 15.73 ? 34  ARG A CB    1 
ATOM   199  C CG    . ARG A 1 43  ? 26.558 30.939 17.753 1.00 15.38 ? 34  ARG A CG    1 
ATOM   200  C CD    . ARG A 1 43  ? 27.845 30.395 18.329 1.00 15.04 ? 34  ARG A CD    1 
ATOM   201  N NE    . ARG A 1 43  ? 28.879 31.421 18.400 1.00 14.87 ? 34  ARG A NE    1 
ATOM   202  C CZ    . ARG A 1 43  ? 29.637 31.765 17.370 1.00 16.55 ? 34  ARG A CZ    1 
ATOM   203  N NH1   . ARG A 1 43  ? 29.494 31.177 16.199 1.00 16.53 ? 34  ARG A NH1   1 
ATOM   204  N NH2   . ARG A 1 43  ? 30.548 32.725 17.524 1.00 18.16 ? 34  ARG A NH2   1 
ATOM   205  N N     . CYS A 1 44  ? 24.039 33.754 20.737 1.00 14.28 ? 35  CYS A N     1 
ATOM   206  C CA    . CYS A 1 44  ? 23.583 34.965 21.443 1.00 15.12 ? 35  CYS A CA    1 
ATOM   207  C C     . CYS A 1 44  ? 23.621 36.210 20.566 1.00 17.54 ? 35  CYS A C     1 
ATOM   208  O O     . CYS A 1 44  ? 23.822 37.314 21.078 1.00 16.97 ? 35  CYS A O     1 
ATOM   209  C CB    . CYS A 1 44  ? 24.382 35.220 22.737 1.00 13.73 ? 35  CYS A CB    1 
ATOM   210  S SG    . CYS A 1 44  ? 24.430 33.767 23.820 1.00 18.74 ? 35  CYS A SG    1 
ATOM   211  N N     . ARG A 1 45  ? 23.395 36.066 19.260 1.00 15.58 ? 36  ARG A N     1 
ATOM   212  C CA    . ARG A 1 45  ? 23.260 37.235 18.378 1.00 15.86 ? 36  ARG A CA    1 
ATOM   213  C C     . ARG A 1 45  ? 21.804 37.599 18.095 1.00 17.40 ? 36  ARG A C     1 
ATOM   214  O O     . ARG A 1 45  ? 21.551 38.568 17.368 1.00 16.25 ? 36  ARG A O     1 
ATOM   215  C CB    . ARG A 1 45  ? 24.013 37.001 17.044 1.00 16.73 ? 36  ARG A CB    1 
ATOM   216  C CG    . ARG A 1 45  ? 25.454 37.530 17.064 1.00 18.04 ? 36  ARG A CG    1 
ATOM   217  C CD    . ARG A 1 45  ? 26.358 36.665 17.946 1.00 19.15 ? 36  ARG A CD    1 
ATOM   218  N NE    . ARG A 1 45  ? 27.760 37.049 17.829 1.00 15.30 ? 36  ARG A NE    1 
ATOM   219  C CZ    . ARG A 1 45  ? 28.761 36.376 18.385 1.00 17.35 ? 36  ARG A CZ    1 
ATOM   220  N NH1   . ARG A 1 45  ? 28.543 35.277 19.116 1.00 14.78 ? 36  ARG A NH1   1 
ATOM   221  N NH2   . ARG A 1 45  ? 30.009 36.792 18.174 1.00 15.12 ? 36  ARG A NH2   1 
ATOM   222  N N     . ALA A 1 46  ? 20.837 36.845 18.636 1.00 16.68 ? 37  ALA A N     1 
ATOM   223  C CA    . ALA A 1 46  ? 19.422 37.048 18.296 1.00 17.38 ? 37  ALA A CA    1 
ATOM   224  C C     . ALA A 1 46  ? 18.820 38.038 19.283 1.00 16.06 ? 37  ALA A C     1 
ATOM   225  O O     . ALA A 1 46  ? 18.119 37.682 20.246 1.00 17.02 ? 37  ALA A O     1 
ATOM   226  C CB    . ALA A 1 46  ? 18.662 35.731 18.297 1.00 17.22 ? 37  ALA A CB    1 
ATOM   227  N N     . LEU A 1 47  ? 19.120 39.311 19.037 1.00 16.74 ? 38  LEU A N     1 
ATOM   228  C CA    . LEU A 1 47  ? 18.815 40.354 20.013 1.00 20.08 ? 38  LEU A CA    1 
ATOM   229  C C     . LEU A 1 47  ? 17.326 40.363 20.351 1.00 23.59 ? 38  LEU A C     1 
ATOM   230  O O     . LEU A 1 47  ? 16.477 40.275 19.454 1.00 19.71 ? 38  LEU A O     1 
ATOM   231  C CB    . LEU A 1 47  ? 19.251 41.711 19.460 1.00 19.39 ? 38  LEU A CB    1 
ATOM   232  C CG    . LEU A 1 47  ? 20.723 41.804 19.055 1.00 18.52 ? 38  LEU A CG    1 
ATOM   233  C CD1   . LEU A 1 47  ? 21.060 43.226 18.608 1.00 23.51 ? 38  LEU A CD1   1 
ATOM   234  C CD2   . LEU A 1 47  ? 21.660 41.396 20.194 1.00 20.08 ? 38  LEU A CD2   1 
ATOM   235  N N     . ASN A 1 48  ? 17.025 40.412 21.658 1.00 25.13 ? 39  ASN A N     1 
ATOM   236  C CA    . ASN A 1 48  ? 15.656 40.415 22.187 1.00 24.84 ? 39  ASN A CA    1 
ATOM   237  C C     . ASN A 1 48  ? 14.853 39.191 21.736 1.00 18.21 ? 39  ASN A C     1 
ATOM   238  O O     . ASN A 1 48  ? 13.627 39.252 21.580 1.00 23.03 ? 39  ASN A O     1 
ATOM   239  C CB    . ASN A 1 48  ? 14.930 41.699 21.807 1.00 29.77 ? 39  ASN A CB    1 
ATOM   240  C CG    . ASN A 1 48  ? 15.371 42.884 22.637 1.00 31.36 ? 39  ASN A CG    1 
ATOM   241  O OD1   . ASN A 1 48  ? 15.960 42.753 23.738 1.00 29.35 ? 39  ASN A OD1   1 
ATOM   242  N ND2   . ASN A 1 48  ? 15.135 44.053 22.097 1.00 25.37 ? 39  ASN A ND2   1 
ATOM   243  N N     . ASN A 1 49  ? 15.555 38.082 21.534 1.00 16.79 ? 40  ASN A N     1 
ATOM   244  C CA    . ASN A 1 49  ? 14.996 36.790 21.138 1.00 18.22 ? 40  ASN A CA    1 
ATOM   245  C C     . ASN A 1 49  ? 14.416 36.799 19.737 1.00 18.27 ? 40  ASN A C     1 
ATOM   246  O O     . ASN A 1 49  ? 13.689 35.879 19.351 1.00 17.75 ? 40  ASN A O     1 
ATOM   247  C CB    . ASN A 1 49  ? 13.950 36.282 22.139 1.00 17.39 ? 40  ASN A CB    1 
ATOM   248  C CG    . ASN A 1 49  ? 14.410 36.420 23.581 1.00 19.49 ? 40  ASN A CG    1 
ATOM   249  O OD1   . ASN A 1 49  ? 13.702 37.001 24.414 1.00 21.07 ? 40  ASN A OD1   1 
ATOM   250  N ND2   . ASN A 1 49  ? 15.572 35.849 23.899 1.00 16.07 ? 40  ASN A ND2   1 
ATOM   251  N N     . ILE A 1 50  ? 14.752 37.798 18.941 1.00 17.18 ? 41  ILE A N     1 
ATOM   252  C CA    . ILE A 1 50  ? 14.268 37.892 17.573 1.00 17.82 ? 41  ILE A CA    1 
ATOM   253  C C     . ILE A 1 50  ? 15.417 37.488 16.656 1.00 16.78 ? 41  ILE A C     1 
ATOM   254  O O     . ILE A 1 50  ? 16.498 38.082 16.745 1.00 18.34 ? 41  ILE A O     1 
ATOM   255  C CB    . ILE A 1 50  ? 13.779 39.307 17.256 1.00 19.56 ? 41  ILE A CB    1 
ATOM   256  C CG1   . ILE A 1 50  ? 12.640 39.671 18.220 1.00 23.26 ? 41  ILE A CG1   1 
ATOM   257  C CG2   . ILE A 1 50  ? 13.322 39.379 15.797 1.00 22.71 ? 41  ILE A CG2   1 
ATOM   258  C CD1   . ILE A 1 50  ? 12.316 41.139 18.212 1.00 37.91 ? 41  ILE A CD1   1 
ATOM   259  N N     . PRO A 1 51  ? 15.231 36.504 15.781 1.00 18.32 ? 42  PRO A N     1 
ATOM   260  C CA    . PRO A 1 51  ? 16.272 36.198 14.798 1.00 19.56 ? 42  PRO A CA    1 
ATOM   261  C C     . PRO A 1 51  ? 16.653 37.453 14.013 1.00 21.94 ? 42  PRO A C     1 
ATOM   262  O O     . PRO A 1 51  ? 15.794 38.233 13.589 1.00 24.94 ? 42  PRO A O     1 
ATOM   263  C CB    . PRO A 1 51  ? 15.606 35.155 13.893 1.00 20.84 ? 42  PRO A CB    1 
ATOM   264  C CG    . PRO A 1 51  ? 14.538 34.540 14.716 1.00 19.29 ? 42  PRO A CG    1 
ATOM   265  C CD    . PRO A 1 51  ? 14.054 35.636 15.643 1.00 18.57 ? 42  PRO A CD    1 
ATOM   266  N N     . GLN A 1 52  ? 17.951 37.631 13.800 1.00 20.49 ? 43  GLN A N     1 
ATOM   267  C CA    . GLN A 1 52  ? 18.488 38.831 13.175 1.00 21.89 ? 43  GLN A CA    1 
ATOM   268  C C     . GLN A 1 52  ? 19.098 38.498 11.830 1.00 22.16 ? 43  GLN A C     1 
ATOM   269  O O     . GLN A 1 52  ? 19.488 37.362 11.566 1.00 20.79 ? 43  GLN A O     1 
ATOM   270  C CB    . GLN A 1 52  ? 19.550 39.488 14.065 1.00 21.35 ? 43  GLN A CB    1 
ATOM   271  C CG    . GLN A 1 52  ? 19.014 39.779 15.449 1.00 20.48 ? 43  GLN A CG    1 
ATOM   272  C CD    . GLN A 1 52  ? 18.185 41.039 15.491 1.00 26.80 ? 43  GLN A CD    1 
ATOM   273  O OE1   . GLN A 1 52  ? 18.451 42.006 14.765 1.00 30.90 ? 43  GLN A OE1   1 
ATOM   274  N NE2   . GLN A 1 52  ? 17.132 41.028 16.317 1.00 22.09 ? 43  GLN A NE2   1 
ATOM   275  N N     . ALA A 1 53  ? 19.224 39.537 10.996 1.00 20.45 ? 44  ALA A N     1 
ATOM   276  C CA    . ALA A 1 53  ? 19.885 39.371 9.706  1.00 20.95 ? 44  ALA A CA    1 
ATOM   277  C C     . ALA A 1 53  ? 21.249 38.698 9.844  1.00 21.17 ? 44  ALA A C     1 
ATOM   278  O O     . ALA A 1 53  ? 21.673 37.945 8.955  1.00 23.04 ? 44  ALA A O     1 
ATOM   279  C CB    . ALA A 1 53  ? 20.034 40.734 9.036  1.00 22.09 ? 44  ALA A CB    1 
ATOM   280  N N     . ALA A 1 54  ? 21.968 38.988 10.934 1.00 19.63 ? 45  ALA A N     1 
ATOM   281  C CA    . ALA A 1 54  ? 23.261 38.349 11.159 1.00 20.31 ? 45  ALA A CA    1 
ATOM   282  C C     . ALA A 1 54  ? 23.152 36.831 11.152 1.00 18.83 ? 45  ALA A C     1 
ATOM   283  O O     . ALA A 1 54  ? 24.045 36.149 10.633 1.00 19.29 ? 45  ALA A O     1 
ATOM   284  C CB    . ALA A 1 54  ? 23.856 38.824 12.481 1.00 22.01 ? 45  ALA A CB    1 
ATOM   285  N N     . LEU A 1 55  ? 22.082 36.273 11.743 1.00 16.62 ? 46  LEU A N     1 
ATOM   286  C CA    . LEU A 1 55  ? 21.917 34.817 11.741 1.00 15.23 ? 46  LEU A CA    1 
ATOM   287  C C     . LEU A 1 55  ? 21.794 34.284 10.319 1.00 15.17 ? 46  LEU A C     1 
ATOM   288  O O     . LEU A 1 55  ? 22.275 33.187 10.007 1.00 17.71 ? 46  LEU A O     1 
ATOM   289  C CB    . LEU A 1 55  ? 20.684 34.422 12.550 1.00 18.61 ? 46  LEU A CB    1 
ATOM   290  C CG    . LEU A 1 55  ? 20.851 34.251 14.059 1.00 17.81 ? 46  LEU A CG    1 
ATOM   291  C CD1   . LEU A 1 55  ? 21.155 35.607 14.775 1.00 17.39 ? 46  LEU A CD1   1 
ATOM   292  C CD2   . LEU A 1 55  ? 19.573 33.607 14.663 1.00 19.89 ? 46  LEU A CD2   1 
ATOM   293  N N     . GLY A 1 56  ? 21.125 35.035 9.452  1.00 19.38 ? 47  GLY A N     1 
ATOM   294  C CA    . GLY A 1 56  ? 20.997 34.600 8.071  1.00 19.20 ? 47  GLY A CA    1 
ATOM   295  C C     . GLY A 1 56  ? 22.343 34.527 7.384  1.00 18.20 ? 47  GLY A C     1 
ATOM   296  O O     . GLY A 1 56  ? 22.643 33.562 6.690  1.00 19.65 ? 47  GLY A O     1 
ATOM   297  N N     . GLU A 1 57  ? 23.204 35.521 7.620  1.00 18.72 ? 48  GLU A N     1 
ATOM   298  C CA    . GLU A 1 57  ? 24.537 35.449 7.024  1.00 21.98 ? 48  GLU A CA    1 
ATOM   299  C C     . GLU A 1 57  ? 25.335 34.274 7.584  1.00 19.23 ? 48  GLU A C     1 
ATOM   300  O O     . GLU A 1 57  ? 26.017 33.563 6.842  1.00 19.54 ? 48  GLU A O     1 
ATOM   301  C CB    . GLU A 1 57  ? 25.287 36.767 7.252  1.00 23.77 ? 48  GLU A CB    1 
ATOM   302  C CG    . GLU A 1 57  ? 26.683 36.749 6.617  1.00 24.94 ? 48  GLU A CG    1 
ATOM   303  C CD    . GLU A 1 57  ? 27.407 38.093 6.724  1.00 49.98 ? 48  GLU A CD    1 
ATOM   304  O OE1   . GLU A 1 57  ? 27.068 38.889 7.625  1.00 57.76 ? 48  GLU A OE1   1 
ATOM   305  O OE2   . GLU A 1 57  ? 28.286 38.369 5.876  1.00 55.36 ? 48  GLU A OE2   1 
ATOM   306  N N     . TYR A 1 58  ? 25.215 34.032 8.891  1.00 15.86 ? 49  TYR A N     1 
ATOM   307  C CA    . TYR A 1 58  ? 25.974 32.976 9.551  1.00 16.47 ? 49  TYR A CA    1 
ATOM   308  C C     . TYR A 1 58  ? 25.595 31.587 9.051  1.00 16.84 ? 49  TYR A C     1 
ATOM   309  O O     . TYR A 1 58  ? 26.472 30.768 8.743  1.00 16.66 ? 49  TYR A O     1 
ATOM   310  C CB    . TYR A 1 58  ? 25.730 33.094 11.042 1.00 17.81 ? 49  TYR A CB    1 
ATOM   311  C CG    . TYR A 1 58  ? 26.232 31.983 11.908 1.00 17.98 ? 49  TYR A CG    1 
ATOM   312  C CD1   . TYR A 1 58  ? 27.561 31.933 12.302 1.00 17.88 ? 49  TYR A CD1   1 
ATOM   313  C CD2   . TYR A 1 58  ? 25.360 31.016 12.396 1.00 16.08 ? 49  TYR A CD2   1 
ATOM   314  C CE1   . TYR A 1 58  ? 28.019 30.913 13.147 1.00 15.98 ? 49  TYR A CE1   1 
ATOM   315  C CE2   . TYR A 1 58  ? 25.805 30.028 13.264 1.00 19.72 ? 49  TYR A CE2   1 
ATOM   316  C CZ    . TYR A 1 58  ? 27.127 29.995 13.636 1.00 18.74 ? 49  TYR A CZ    1 
ATOM   317  O OH    . TYR A 1 58  ? 27.577 29.034 14.529 1.00 22.83 ? 49  TYR A OH    1 
ATOM   318  N N     . TYR A 1 59  ? 24.295 31.297 8.975  1.00 15.63 ? 50  TYR A N     1 
ATOM   319  C CA    . TYR A 1 59  ? 23.872 29.984 8.497  1.00 14.80 ? 50  TYR A CA    1 
ATOM   320  C C     . TYR A 1 59  ? 24.106 29.840 6.996  1.00 14.26 ? 50  TYR A C     1 
ATOM   321  O O     . TYR A 1 59  ? 24.434 28.748 6.516  1.00 16.79 ? 50  TYR A O     1 
ATOM   322  C CB    . TYR A 1 59  ? 22.408 29.741 8.867  1.00 15.51 ? 50  TYR A CB    1 
ATOM   323  C CG    . TYR A 1 59  ? 22.211 29.491 10.355 1.00 16.40 ? 50  TYR A CG    1 
ATOM   324  C CD1   . TYR A 1 59  ? 22.747 28.358 10.965 1.00 16.08 ? 50  TYR A CD1   1 
ATOM   325  C CD2   . TYR A 1 59  ? 21.495 30.382 11.148 1.00 15.29 ? 50  TYR A CD2   1 
ATOM   326  C CE1   . TYR A 1 59  ? 22.586 28.115 12.343 1.00 15.38 ? 50  TYR A CE1   1 
ATOM   327  C CE2   . TYR A 1 59  ? 21.329 30.148 12.523 1.00 18.04 ? 50  TYR A CE2   1 
ATOM   328  C CZ    . TYR A 1 59  ? 21.879 29.027 13.102 1.00 18.16 ? 50  TYR A CZ    1 
ATOM   329  O OH    . TYR A 1 59  ? 21.693 28.846 14.443 1.00 20.13 ? 50  TYR A OH    1 
ATOM   330  N N     . GLU A 1 60  ? 23.923 30.919 6.235  1.00 17.63 ? 51  GLU A N     1 
ATOM   331  C CA    . GLU A 1 60  ? 24.183 30.846 4.803  1.00 18.69 ? 51  GLU A CA    1 
ATOM   332  C C     . GLU A 1 60  ? 25.643 30.516 4.525  1.00 17.94 ? 51  GLU A C     1 
ATOM   333  O O     . GLU A 1 60  ? 25.948 29.728 3.613  1.00 20.95 ? 51  GLU A O     1 
ATOM   334  C CB    . GLU A 1 60  ? 23.786 32.166 4.145  1.00 18.26 ? 51  GLU A CB    1 
ATOM   335  C CG    . GLU A 1 60  ? 24.052 32.220 2.632  1.00 22.92 ? 51  GLU A CG    1 
ATOM   336  C CD    . GLU A 1 60  ? 23.708 33.577 2.033  1.00 35.16 ? 51  GLU A CD    1 
ATOM   337  O OE1   . GLU A 1 60  ? 24.053 34.603 2.658  1.00 47.45 ? 51  GLU A OE1   1 
ATOM   338  O OE2   . GLU A 1 60  ? 23.120 33.618 0.926  1.00 48.08 ? 51  GLU A OE2   1 
ATOM   339  N N     . GLN A 1 61  ? 26.565 31.088 5.307  1.00 16.31 ? 52  GLN A N     1 
ATOM   340  C CA    . GLN A 1 61  ? 27.987 30.807 5.102  1.00 15.97 ? 52  GLN A CA    1 
ATOM   341  C C     . GLN A 1 61  ? 28.285 29.336 5.261  1.00 16.71 ? 52  GLN A C     1 
ATOM   342  O O     . GLN A 1 61  ? 29.176 28.806 4.588  1.00 20.81 ? 52  GLN A O     1 
ATOM   343  C CB    . GLN A 1 61  ? 28.849 31.565 6.112  1.00 16.85 ? 52  GLN A CB    1 
ATOM   344  C CG    . GLN A 1 61  ? 28.996 33.050 5.841  1.00 18.53 ? 52  GLN A CG    1 
ATOM   345  C CD    . GLN A 1 61  ? 29.893 33.752 6.857  1.00 20.39 ? 52  GLN A CD    1 
ATOM   346  O OE1   . GLN A 1 61  ? 30.100 33.277 7.977  1.00 21.12 ? 52  GLN A OE1   1 
ATOM   347  N NE2   . GLN A 1 61  ? 30.449 34.882 6.456  1.00 22.91 ? 52  GLN A NE2   1 
ATOM   348  N N     . ARG A 1 62  ? 27.560 28.669 6.162  1.00 17.98 ? 53  ARG A N     1 
ATOM   349  C CA    . ARG A 1 62  ? 27.854 27.289 6.521  1.00 17.28 ? 53  ARG A CA    1 
ATOM   350  C C     . ARG A 1 62  ? 27.024 26.278 5.731  1.00 19.84 ? 53  ARG A C     1 
ATOM   351  O O     . ARG A 1 62  ? 27.393 25.096 5.675  1.00 20.23 ? 53  ARG A O     1 
ATOM   352  C CB    . ARG A 1 62  ? 27.665 27.117 8.046  1.00 17.27 ? 53  ARG A CB    1 
ATOM   353  C CG    . ARG A 1 62  ? 28.815 27.829 8.801  1.00 18.94 ? 53  ARG A CG    1 
ATOM   354  C CD    . ARG A 1 62  ? 28.478 28.329 10.219 1.00 17.39 ? 53  ARG A CD    1 
ATOM   355  N NE    . ARG A 1 62  ? 29.655 29.026 10.726 1.00 16.50 ? 53  ARG A NE    1 
ATOM   356  C CZ    . ARG A 1 62  ? 30.061 30.214 10.296 1.00 16.61 ? 53  ARG A CZ    1 
ATOM   357  N NH1   . ARG A 1 62  ? 29.288 30.978 9.521  1.00 16.11 ? 53  ARG A NH1   1 
ATOM   358  N NH2   . ARG A 1 62  ? 31.270 30.658 10.648 1.00 19.61 ? 53  ARG A NH2   1 
ATOM   359  N N     . ALA A 1 63  ? 25.960 26.735 5.071  1.00 16.19 ? 54  ALA A N     1 
ATOM   360  C CA    . ALA A 1 63  ? 25.109 25.868 4.268  1.00 18.50 ? 54  ALA A CA    1 
ATOM   361  C C     . ALA A 1 63  ? 25.850 25.340 3.038  1.00 19.36 ? 54  ALA A C     1 
ATOM   362  O O     . ALA A 1 63  ? 26.643 26.048 2.412  1.00 21.99 ? 54  ALA A O     1 
ATOM   363  C CB    . ALA A 1 63  ? 23.865 26.635 3.800  1.00 18.48 ? 54  ALA A CB    1 
ATOM   364  N N     . THR A 1 64  ? 25.555 24.094 2.681  1.00 17.46 ? 55  THR A N     1 
ATOM   365  C CA    . THR A 1 64  ? 26.105 23.470 1.478  1.00 17.78 ? 55  THR A CA    1 
ATOM   366  C C     . THR A 1 64  ? 24.966 22.743 0.785  1.00 15.57 ? 55  THR A C     1 
ATOM   367  O O     . THR A 1 64  ? 23.960 22.377 1.407  1.00 18.09 ? 55  THR A O     1 
ATOM   368  C CB    . THR A 1 64  ? 27.253 22.480 1.791  1.00 22.21 ? 55  THR A CB    1 
ATOM   369  O OG1   . THR A 1 64  ? 26.826 21.559 2.804  1.00 18.03 ? 55  THR A OG1   1 
ATOM   370  C CG2   . THR A 1 64  ? 28.488 23.219 2.311  1.00 21.47 ? 55  THR A CG2   1 
ATOM   371  N N     . ALA A 1 65  ? 25.126 22.513 -0.518 1.00 17.95 ? 56  ALA A N     1 
ATOM   372  C CA    . ALA A 1 65  ? 24.114 21.771 -1.255 1.00 20.79 ? 56  ALA A CA    1 
ATOM   373  C C     . ALA A 1 65  ? 23.999 20.345 -0.724 1.00 20.06 ? 56  ALA A C     1 
ATOM   374  O O     . ALA A 1 65  ? 24.978 19.588 -0.713 1.00 22.80 ? 56  ALA A O     1 
ATOM   375  C CB    . ALA A 1 65  ? 24.453 21.759 -2.748 1.00 23.00 ? 56  ALA A CB    1 
ATOM   376  N N     . GLY A 1 66  ? 22.805 19.981 -0.281 1.00 19.73 ? 57  GLY A N     1 
ATOM   377  C CA    . GLY A 1 66  ? 22.598 18.660 0.282  1.00 19.06 ? 57  GLY A CA    1 
ATOM   378  C C     . GLY A 1 66  ? 23.175 18.468 1.667  1.00 20.41 ? 57  GLY A C     1 
ATOM   379  O O     . GLY A 1 66  ? 23.235 17.338 2.140  1.00 19.86 ? 57  GLY A O     1 
ATOM   380  N N     . GLY A 1 67  ? 23.630 19.521 2.335  1.00 17.17 ? 58  GLY A N     1 
ATOM   381  C CA    . GLY A 1 67  ? 24.132 19.393 3.694  1.00 16.40 ? 58  GLY A CA    1 
ATOM   382  C C     . GLY A 1 67  ? 23.065 19.733 4.722  1.00 18.57 ? 58  GLY A C     1 
ATOM   383  O O     . GLY A 1 67  ? 22.161 20.526 4.462  1.00 18.87 ? 58  GLY A O     1 
ATOM   384  N N     . PHE A 1 68  ? 23.214 19.151 5.924  1.00 15.21 ? 59  PHE A N     1 
ATOM   385  C CA    . PHE A 1 68  ? 22.244 19.274 7.017  1.00 15.29 ? 59  PHE A CA    1 
ATOM   386  C C     . PHE A 1 68  ? 22.767 20.223 8.090  1.00 16.20 ? 59  PHE A C     1 
ATOM   387  O O     . PHE A 1 68  ? 23.898 20.059 8.569  1.00 15.30 ? 59  PHE A O     1 
ATOM   388  C CB    . PHE A 1 68  ? 21.975 17.899 7.620  1.00 16.08 ? 59  PHE A CB    1 
ATOM   389  C CG    . PHE A 1 68  ? 20.980 17.905 8.750  1.00 15.15 ? 59  PHE A CG    1 
ATOM   390  C CD1   . PHE A 1 68  ? 19.864 18.737 8.724  1.00 16.97 ? 59  PHE A CD1   1 
ATOM   391  C CD2   . PHE A 1 68  ? 21.141 17.048 9.825  1.00 17.01 ? 59  PHE A CD2   1 
ATOM   392  C CE1   . PHE A 1 68  ? 18.948 18.736 9.794  1.00 15.91 ? 59  PHE A CE1   1 
ATOM   393  C CE2   . PHE A 1 68  ? 20.226 17.052 10.913 1.00 17.79 ? 59  PHE A CE2   1 
ATOM   394  C CZ    . PHE A 1 68  ? 19.132 17.879 10.879 1.00 17.60 ? 59  PHE A CZ    1 
ATOM   395  N N     . LEU A 1 69  ? 21.946 21.210 8.452  1.00 13.79 ? 60  LEU A N     1 
ATOM   396  C CA    . LEU A 1 69  ? 22.247 22.182 9.501  1.00 14.16 ? 60  LEU A CA    1 
ATOM   397  C C     . LEU A 1 69  ? 21.240 22.065 10.629 1.00 14.13 ? 60  LEU A C     1 
ATOM   398  O O     . LEU A 1 69  ? 20.040 21.947 10.385 1.00 16.23 ? 60  LEU A O     1 
ATOM   399  C CB    . LEU A 1 69  ? 22.174 23.617 8.948  1.00 17.58 ? 60  LEU A CB    1 
ATOM   400  C CG    . LEU A 1 69  ? 23.050 23.972 7.767  1.00 22.43 ? 60  LEU A CG    1 
ATOM   401  C CD1   . LEU A 1 69  ? 22.875 25.471 7.512  1.00 23.84 ? 60  LEU A CD1   1 
ATOM   402  C CD2   . LEU A 1 69  ? 24.488 23.656 8.091  1.00 23.19 ? 60  LEU A CD2   1 
ATOM   403  N N     . ILE A 1 70  ? 21.713 22.192 11.879 1.00 13.84 ? 61  ILE A N     1 
ATOM   404  C CA    . ILE A 1 70  ? 20.838 22.314 13.039 1.00 13.99 ? 61  ILE A CA    1 
ATOM   405  C C     . ILE A 1 70  ? 21.066 23.680 13.676 1.00 13.19 ? 61  ILE A C     1 
ATOM   406  O O     . ILE A 1 70  ? 22.217 24.063 13.943 1.00 14.83 ? 61  ILE A O     1 
ATOM   407  C CB    . ILE A 1 70  ? 21.106 21.205 14.067 1.00 13.91 ? 61  ILE A CB    1 
ATOM   408  C CG1   . ILE A 1 70  ? 21.000 19.846 13.381 1.00 16.00 ? 61  ILE A CG1   1 
ATOM   409  C CG2   . ILE A 1 70  ? 20.104 21.287 15.222 1.00 16.28 ? 61  ILE A CG2   1 
ATOM   410  C CD1   . ILE A 1 70  ? 21.636 18.737 14.225 1.00 15.51 ? 61  ILE A CD1   1 
ATOM   411  N N     . THR A 1 71  ? 19.976 24.421 13.901 1.00 14.81 ? 62  THR A N     1 
ATOM   412  C CA    . THR A 1 71  ? 20.135 25.739 14.514 1.00 17.16 ? 62  THR A CA    1 
ATOM   413  C C     . THR A 1 71  ? 20.552 25.653 15.982 1.00 16.27 ? 62  THR A C     1 
ATOM   414  O O     . THR A 1 71  ? 20.379 24.650 16.683 1.00 16.94 ? 62  THR A O     1 
ATOM   415  C CB    . THR A 1 71  ? 18.853 26.590 14.494 1.00 15.96 ? 62  THR A CB    1 
ATOM   416  O OG1   . THR A 1 71  ? 17.896 26.058 15.428 1.00 14.86 ? 62  THR A OG1   1 
ATOM   417  C CG2   . THR A 1 71  ? 18.233 26.645 13.101 1.00 17.02 ? 62  THR A CG2   1 
ATOM   418  N N     . GLU A 1 72  ? 21.038 26.789 16.445 1.00 14.73 ? 63  GLU A N     1 
ATOM   419  C CA    . GLU A 1 72  ? 21.156 27.083 17.862 1.00 13.80 ? 63  GLU A CA    1 
ATOM   420  C C     . GLU A 1 72  ? 19.856 26.762 18.592 1.00 16.86 ? 63  GLU A C     1 
ATOM   421  O O     . GLU A 1 72  ? 18.765 26.841 18.032 1.00 15.61 ? 63  GLU A O     1 
ATOM   422  C CB    . GLU A 1 72  ? 21.472 28.570 18.029 1.00 17.12 ? 63  GLU A CB    1 
ATOM   423  C CG    . GLU A 1 72  ? 20.374 29.504 17.545 1.00 17.10 ? 63  GLU A CG    1 
ATOM   424  C CD    . GLU A 1 72  ? 20.927 30.795 16.956 1.00 21.46 ? 63  GLU A CD    1 
ATOM   425  O OE1   . GLU A 1 72  ? 21.343 30.829 15.772 1.00 22.20 ? 63  GLU A OE1   1 
ATOM   426  O OE2   . GLU A 1 72  ? 20.950 31.798 17.693 1.00 21.19 ? 63  GLU A OE2   1 
ATOM   427  N N     . GLY A 1 73  ? 19.956 26.449 19.877 1.00 14.92 ? 64  GLY A N     1 
ATOM   428  C CA    . GLY A 1 73  ? 18.742 26.196 20.627 1.00 14.70 ? 64  GLY A CA    1 
ATOM   429  C C     . GLY A 1 73  ? 17.815 27.404 20.590 1.00 14.40 ? 64  GLY A C     1 
ATOM   430  O O     . GLY A 1 73  ? 18.244 28.554 20.711 1.00 16.45 ? 64  GLY A O     1 
ATOM   431  N N     . THR A 1 74  ? 16.524 27.132 20.494 1.00 14.90 ? 65  THR A N     1 
ATOM   432  C CA    . THR A 1 74  ? 15.526 28.156 20.244 1.00 15.78 ? 65  THR A CA    1 
ATOM   433  C C     . THR A 1 74  ? 14.398 28.024 21.272 1.00 14.86 ? 65  THR A C     1 
ATOM   434  O O     . THR A 1 74  ? 13.893 26.915 21.527 1.00 15.83 ? 65  THR A O     1 
ATOM   435  C CB    . THR A 1 74  ? 15.035 28.025 18.782 1.00 15.69 ? 65  THR A CB    1 
ATOM   436  O OG1   . THR A 1 74  ? 16.139 28.210 17.867 1.00 17.12 ? 65  THR A OG1   1 
ATOM   437  C CG2   . THR A 1 74  ? 13.959 29.049 18.427 1.00 16.20 ? 65  THR A CG2   1 
ATOM   438  N N     . MET A 1 75  ? 14.020 29.156 21.871 1.00 15.62 ? 66  MET A N     1 
ATOM   439  C CA    . MET A 1 75  ? 13.016 29.163 22.937 1.00 19.46 ? 66  MET A CA    1 
ATOM   440  C C     . MET A 1 75  ? 11.661 28.669 22.454 1.00 17.66 ? 66  MET A C     1 
ATOM   441  O O     . MET A 1 75  ? 11.219 28.996 21.350 1.00 16.30 ? 66  MET A O     1 
ATOM   442  C CB    . MET A 1 75  ? 12.824 30.569 23.520 1.00 17.24 ? 66  MET A CB    1 
ATOM   443  C CG    . MET A 1 75  ? 14.108 31.238 23.994 1.00 17.92 ? 66  MET A CG    1 
ATOM   444  S SD    . MET A 1 75  ? 13.802 32.991 24.416 1.00 19.04 ? 66  MET A SD    1 
ATOM   445  C CE    . MET A 1 75  ? 12.523 32.940 25.692 1.00 19.70 ? 66  MET A CE    1 
ATOM   446  N N     . ILE A 1 76  ? 10.994 27.890 23.312 1.00 14.94 ? 67  ILE A N     1 
ATOM   447  C CA    . ILE A 1 76  ? 9.635  27.424 23.052 1.00 15.55 ? 67  ILE A CA    1 
ATOM   448  C C     . ILE A 1 76  ? 8.564  28.216 23.791 1.00 17.88 ? 67  ILE A C     1 
ATOM   449  O O     . ILE A 1 76  ? 7.368  27.927 23.605 1.00 19.56 ? 67  ILE A O     1 
ATOM   450  C CB    . ILE A 1 76  ? 9.473  25.931 23.403 1.00 13.44 ? 67  ILE A CB    1 
ATOM   451  C CG1   . ILE A 1 76  ? 9.660  25.686 24.912 1.00 14.32 ? 67  ILE A CG1   1 
ATOM   452  C CG2   . ILE A 1 76  ? 10.483 25.065 22.575 1.00 16.63 ? 67  ILE A CG2   1 
ATOM   453  C CD1   . ILE A 1 76  ? 9.298  24.275 25.332 1.00 16.15 ? 67  ILE A CD1   1 
ATOM   454  N N     . SER A 1 77  ? 8.946  29.152 24.655 1.00 15.61 ? 68  SER A N     1 
ATOM   455  C CA    . SER A 1 77  ? 8.020  29.879 25.516 1.00 19.07 ? 68  SER A CA    1 
ATOM   456  C C     . SER A 1 77  ? 8.785  31.012 26.177 1.00 18.05 ? 68  SER A C     1 
ATOM   457  O O     . SER A 1 77  ? 10.015 30.980 26.216 1.00 19.55 ? 68  SER A O     1 
ATOM   458  C CB    . SER A 1 77  ? 7.427  28.963 26.593 1.00 19.30 ? 68  SER A CB    1 
ATOM   459  O OG    . SER A 1 77  ? 8.416  28.703 27.589 1.00 19.24 ? 68  SER A OG    1 
ATOM   460  N N     . PRO A 1 78  ? 8.075  31.997 26.743 1.00 19.17 ? 69  PRO A N     1 
ATOM   461  C CA    . PRO A 1 78  ? 8.766  33.093 27.457 1.00 22.79 ? 69  PRO A CA    1 
ATOM   462  C C     . PRO A 1 78  ? 9.605  32.647 28.656 1.00 20.16 ? 69  PRO A C     1 
ATOM   463  O O     . PRO A 1 78  ? 10.508 33.389 29.075 1.00 21.56 ? 69  PRO A O     1 
ATOM   464  C CB    . PRO A 1 78  ? 7.607  33.996 27.910 1.00 24.18 ? 69  PRO A CB    1 
ATOM   465  C CG    . PRO A 1 78  ? 6.533  33.745 26.908 1.00 23.69 ? 69  PRO A CG    1 
ATOM   466  C CD    . PRO A 1 78  ? 6.639  32.269 26.561 1.00 22.62 ? 69  PRO A CD    1 
ATOM   467  N N     . THR A 1 79  ? 9.368  31.459 29.201 1.00 18.95 ? 70  THR A N     1 
ATOM   468  C CA    . THR A 1 79  ? 10.082 30.998 30.383 1.00 17.59 ? 70  THR A CA    1 
ATOM   469  C C     . THR A 1 79  ? 11.202 30.020 30.070 1.00 20.68 ? 70  THR A C     1 
ATOM   470  O O     . THR A 1 79  ? 11.815 29.493 31.000 1.00 20.80 ? 70  THR A O     1 
ATOM   471  C CB    . THR A 1 79  ? 9.106  30.365 31.383 1.00 22.41 ? 70  THR A CB    1 
ATOM   472  O OG1   . THR A 1 79  ? 8.271  29.422 30.689 1.00 25.99 ? 70  THR A OG1   1 
ATOM   473  C CG2   . THR A 1 79  ? 8.222  31.442 32.021 1.00 26.07 ? 70  THR A CG2   1 
ATOM   474  N N     . SER A 1 80  ? 11.527 29.786 28.790 1.00 15.21 ? 71  SER A N     1 
ATOM   475  C CA    . SER A 1 80  ? 12.419 28.682 28.448 1.00 15.08 ? 71  SER A CA    1 
ATOM   476  C C     . SER A 1 80  ? 13.887 29.079 28.299 1.00 15.75 ? 71  SER A C     1 
ATOM   477  O O     . SER A 1 80  ? 14.724 28.210 28.017 1.00 15.66 ? 71  SER A O     1 
ATOM   478  C CB    . SER A 1 80  ? 11.912 28.018 27.158 1.00 19.47 ? 71  SER A CB    1 
ATOM   479  O OG    . SER A 1 80  ? 11.944 28.951 26.134 1.00 21.91 ? 71  SER A OG    1 
ATOM   480  N N     . ALA A 1 81  ? 14.237 30.353 28.469 1.00 18.05 ? 72  ALA A N     1 
ATOM   481  C CA    . ALA A 1 81  ? 15.590 30.833 28.211 1.00 17.97 ? 72  ALA A CA    1 
ATOM   482  C C     . ALA A 1 81  ? 16.456 30.899 29.468 1.00 17.94 ? 72  ALA A C     1 
ATOM   483  O O     . ALA A 1 81  ? 15.985 31.228 30.563 1.00 19.22 ? 72  ALA A O     1 
ATOM   484  C CB    . ALA A 1 81  ? 15.562 32.238 27.571 1.00 15.63 ? 72  ALA A CB    1 
ATOM   485  N N     . GLY A 1 82  ? 17.750 30.635 29.272 1.00 15.97 ? 73  GLY A N     1 
ATOM   486  C CA    . GLY A 1 82  ? 18.770 30.806 30.305 1.00 17.23 ? 73  GLY A CA    1 
ATOM   487  C C     . GLY A 1 82  ? 20.079 31.377 29.775 1.00 18.80 ? 73  GLY A C     1 
ATOM   488  O O     . GLY A 1 82  ? 21.131 31.261 30.425 1.00 16.50 ? 73  GLY A O     1 
ATOM   489  N N     . PHE A 1 83  ? 20.021 32.003 28.597 1.00 16.12 ? 74  PHE A N     1 
ATOM   490  C CA    . PHE A 1 83  ? 21.112 32.681 27.907 1.00 17.74 ? 74  PHE A CA    1 
ATOM   491  C C     . PHE A 1 83  ? 20.564 33.975 27.332 1.00 16.44 ? 74  PHE A C     1 
ATOM   492  O O     . PHE A 1 83  ? 19.364 34.066 27.040 1.00 16.91 ? 74  PHE A O     1 
ATOM   493  C CB    . PHE A 1 83  ? 21.706 31.840 26.756 1.00 15.66 ? 74  PHE A CB    1 
ATOM   494  C CG    . PHE A 1 83  ? 22.815 30.900 27.187 1.00 16.18 ? 74  PHE A CG    1 
ATOM   495  C CD1   . PHE A 1 83  ? 22.497 29.721 27.830 1.00 16.30 ? 74  PHE A CD1   1 
ATOM   496  C CD2   . PHE A 1 83  ? 24.153 31.188 26.929 1.00 17.46 ? 74  PHE A CD2   1 
ATOM   497  C CE1   . PHE A 1 83  ? 23.503 28.830 28.246 1.00 18.93 ? 74  PHE A CE1   1 
ATOM   498  C CE2   . PHE A 1 83  ? 25.163 30.325 27.325 1.00 19.51 ? 74  PHE A CE2   1 
ATOM   499  C CZ    . PHE A 1 83  ? 24.839 29.133 27.982 1.00 21.28 ? 74  PHE A CZ    1 
ATOM   500  N N     . PRO A 1 84  ? 21.399 34.998 27.192 1.00 15.84 ? 75  PRO A N     1 
ATOM   501  C CA    . PRO A 1 84  ? 20.933 36.264 26.604 1.00 17.35 ? 75  PRO A CA    1 
ATOM   502  C C     . PRO A 1 84  ? 20.851 36.179 25.085 1.00 18.78 ? 75  PRO A C     1 
ATOM   503  O O     . PRO A 1 84  ? 21.694 35.545 24.448 1.00 18.05 ? 75  PRO A O     1 
ATOM   504  C CB    . PRO A 1 84  ? 22.019 37.257 27.019 1.00 21.06 ? 75  PRO A CB    1 
ATOM   505  C CG    . PRO A 1 84  ? 23.282 36.400 26.972 1.00 17.03 ? 75  PRO A CG    1 
ATOM   506  C CD    . PRO A 1 84  ? 22.851 34.996 27.436 1.00 18.62 ? 75  PRO A CD    1 
ATOM   507  N N     . HIS A 1 85  ? 19.815 36.818 24.522 1.00 14.77 ? 76  HIS A N     1 
ATOM   508  C CA    . HIS A 1 85  ? 19.700 37.062 23.068 1.00 16.31 ? 76  HIS A CA    1 
ATOM   509  C C     . HIS A 1 85  ? 19.758 35.756 22.294 1.00 15.88 ? 76  HIS A C     1 
ATOM   510  O O     . HIS A 1 85  ? 20.428 35.646 21.261 1.00 17.28 ? 76  HIS A O     1 
ATOM   511  C CB    . HIS A 1 85  ? 20.781 38.037 22.629 1.00 21.57 ? 76  HIS A CB    1 
ATOM   512  C CG    . HIS A 1 85  ? 20.765 39.278 23.450 1.00 16.20 ? 76  HIS A CG    1 
ATOM   513  N ND1   . HIS A 1 85  ? 19.661 40.099 23.499 1.00 22.42 ? 76  HIS A ND1   1 
ATOM   514  C CD2   . HIS A 1 85  ? 21.669 39.802 24.307 1.00 22.45 ? 76  HIS A CD2   1 
ATOM   515  C CE1   . HIS A 1 85  ? 19.896 41.094 24.336 1.00 24.38 ? 76  HIS A CE1   1 
ATOM   516  N NE2   . HIS A 1 85  ? 21.105 40.934 24.840 1.00 20.84 ? 76  HIS A NE2   1 
ATOM   517  N N     . VAL A 1 86  ? 19.048 34.762 22.818 1.00 17.18 ? 77  VAL A N     1 
ATOM   518  C CA    . VAL A 1 86  ? 18.818 33.533 22.061 1.00 17.71 ? 77  VAL A CA    1 
ATOM   519  C C     . VAL A 1 86  ? 17.483 33.642 21.331 1.00 15.56 ? 77  VAL A C     1 
ATOM   520  O O     . VAL A 1 86  ? 16.542 34.262 21.837 1.00 17.05 ? 77  VAL A O     1 
ATOM   521  C CB    . VAL A 1 86  ? 18.866 32.308 22.978 1.00 17.05 ? 77  VAL A CB    1 
ATOM   522  C CG1   . VAL A 1 86  ? 20.245 32.217 23.642 1.00 20.39 ? 77  VAL A CG1   1 
ATOM   523  C CG2   . VAL A 1 86  ? 17.783 32.380 24.043 1.00 19.92 ? 77  VAL A CG2   1 
ATOM   524  N N     . PRO A 1 87  ? 17.339 33.047 20.153 1.00 13.81 ? 78  PRO A N     1 
ATOM   525  C CA    . PRO A 1 87  ? 16.097 33.232 19.400 1.00 14.71 ? 78  PRO A CA    1 
ATOM   526  C C     . PRO A 1 87  ? 14.985 32.413 20.006 1.00 16.46 ? 78  PRO A C     1 
ATOM   527  O O     . PRO A 1 87  ? 15.226 31.400 20.667 1.00 16.57 ? 78  PRO A O     1 
ATOM   528  C CB    . PRO A 1 87  ? 16.445 32.714 18.002 1.00 14.81 ? 78  PRO A CB    1 
ATOM   529  C CG    . PRO A 1 87  ? 17.568 31.693 18.239 1.00 15.32 ? 78  PRO A CG    1 
ATOM   530  C CD    . PRO A 1 87  ? 18.330 32.226 19.441 1.00 14.54 ? 78  PRO A CD    1 
ATOM   531  N N     . GLY A 1 88  ? 13.749 32.868 19.790 1.00 17.19 ? 79  GLY A N     1 
ATOM   532  C CA    . GLY A 1 88  ? 12.572 32.077 20.080 1.00 15.37 ? 79  GLY A CA    1 
ATOM   533  C C     . GLY A 1 88  ? 11.861 31.684 18.789 1.00 16.38 ? 79  GLY A C     1 
ATOM   534  O O     . GLY A 1 88  ? 12.163 32.187 17.713 1.00 17.20 ? 79  GLY A O     1 
ATOM   535  N N     . ILE A 1 89  ? 10.911 30.765 18.916 1.00 16.09 ? 80  ILE A N     1 
ATOM   536  C CA    . ILE A 1 89  ? 10.014 30.462 17.802 1.00 15.89 ? 80  ILE A CA    1 
ATOM   537  C C     . ILE A 1 89  ? 8.609  30.282 18.349 1.00 20.34 ? 80  ILE A C     1 
ATOM   538  O O     . ILE A 1 89  ? 7.796  29.533 17.797 1.00 21.21 ? 80  ILE A O     1 
ATOM   539  C CB    . ILE A 1 89  ? 10.521 29.248 16.999 1.00 18.82 ? 80  ILE A CB    1 
ATOM   540  C CG1   . ILE A 1 89  ? 9.879  29.202 15.592 1.00 21.06 ? 80  ILE A CG1   1 
ATOM   541  C CG2   . ILE A 1 89  ? 10.380 27.920 17.786 1.00 21.62 ? 80  ILE A CG2   1 
ATOM   542  C CD1   . ILE A 1 89  ? 10.764 28.509 14.594 1.00 27.93 ? 80  ILE A CD1   1 
ATOM   543  N N     . PHE A 1 90  ? 8.294  31.016 19.414 1.00 15.97 ? 81  PHE A N     1 
ATOM   544  C CA    . PHE A 1 90  ? 6.957  30.939 20.004 1.00 16.11 ? 81  PHE A CA    1 
ATOM   545  C C     . PHE A 1 90  ? 6.056  32.114 19.627 1.00 20.41 ? 81  PHE A C     1 
ATOM   546  O O     . PHE A 1 90  ? 4.878  32.101 19.989 1.00 24.72 ? 81  PHE A O     1 
ATOM   547  C CB    . PHE A 1 90  ? 7.040  30.804 21.551 1.00 19.04 ? 81  PHE A CB    1 
ATOM   548  C CG    . PHE A 1 90  ? 7.835  31.899 22.241 1.00 21.20 ? 81  PHE A CG    1 
ATOM   549  C CD1   . PHE A 1 90  ? 9.214  31.796 22.402 1.00 16.53 ? 81  PHE A CD1   1 
ATOM   550  C CD2   . PHE A 1 90  ? 7.196  33.034 22.738 1.00 22.60 ? 81  PHE A CD2   1 
ATOM   551  C CE1   . PHE A 1 90  ? 9.937  32.822 23.055 1.00 16.73 ? 81  PHE A CE1   1 
ATOM   552  C CE2   . PHE A 1 90  ? 7.909  34.048 23.367 1.00 22.41 ? 81  PHE A CE2   1 
ATOM   553  C CZ    . PHE A 1 90  ? 9.271  33.950 23.522 1.00 21.77 ? 81  PHE A CZ    1 
ATOM   554  N N     . THR A 1 91  ? 6.566  33.136 18.940 1.00 21.28 ? 82  THR A N     1 
ATOM   555  C CA    . THR A 1 91  ? 5.737  34.249 18.492 1.00 24.28 ? 82  THR A CA    1 
ATOM   556  C C     . THR A 1 91  ? 5.725  34.309 16.973 1.00 22.22 ? 82  THR A C     1 
ATOM   557  O O     . THR A 1 91  ? 6.639  33.825 16.306 1.00 20.81 ? 82  THR A O     1 
ATOM   558  C CB    . THR A 1 91  ? 6.215  35.611 19.022 1.00 21.33 ? 82  THR A CB    1 
ATOM   559  O OG1   . THR A 1 91  ? 7.387  36.019 18.306 1.00 22.04 ? 82  THR A OG1   1 
ATOM   560  C CG2   . THR A 1 91  ? 6.522  35.555 20.518 1.00 24.15 ? 82  THR A CG2   1 
ATOM   561  N N     . LYS A 1 92  ? 4.685  34.943 16.431 1.00 24.95 ? 83  LYS A N     1 
ATOM   562  C CA    . LYS A 1 92  ? 4.608  35.067 14.985 1.00 26.85 ? 83  LYS A CA    1 
ATOM   563  C C     . LYS A 1 92  ? 5.657  36.023 14.444 1.00 19.93 ? 83  LYS A C     1 
ATOM   564  O O     . LYS A 1 92  ? 6.112  35.849 13.296 1.00 21.29 ? 83  LYS A O     1 
ATOM   565  C CB    . LYS A 1 92  ? 3.205  35.494 14.574 1.00 31.13 ? 83  LYS A CB    1 
ATOM   566  C CG    . LYS A 1 92  ? 2.156  34.454 14.934 1.00 26.72 ? 83  LYS A CG    1 
ATOM   567  C CD    . LYS A 1 92  ? 2.553  33.032 14.477 1.00 33.79 ? 83  LYS A CD    1 
ATOM   568  C CE    . LYS A 1 92  ? 1.469  32.010 14.805 1.00 37.19 ? 83  LYS A CE    1 
ATOM   569  N NZ    . LYS A 1 92  ? 1.612  30.735 14.036 1.00 37.70 ? 83  LYS A NZ    1 
ATOM   570  N N     . GLU A 1 93  ? 6.045  37.032 15.229 1.00 20.01 ? 84  GLU A N     1 
ATOM   571  C CA    . GLU A 1 93  ? 7.163  37.879 14.829 1.00 21.65 ? 84  GLU A CA    1 
ATOM   572  C C     . GLU A 1 93  ? 8.432  37.051 14.643 1.00 23.37 ? 84  GLU A C     1 
ATOM   573  O O     . GLU A 1 93  ? 9.173  37.243 13.670 1.00 22.49 ? 84  GLU A O     1 
ATOM   574  C CB    . GLU A 1 93  ? 7.382  38.979 15.862 1.00 26.98 ? 84  GLU A CB    1 
ATOM   575  C CG    . GLU A 1 93  ? 8.557  39.885 15.526 1.00 27.99 ? 84  GLU A CG    1 
ATOM   576  C CD    . GLU A 1 93  ? 8.870  40.909 16.620 1.00 37.18 ? 84  GLU A CD    1 
ATOM   577  O OE1   . GLU A 1 93  ? 8.714  40.604 17.822 1.00 37.97 ? 84  GLU A OE1   1 
ATOM   578  O OE2   . GLU A 1 93  ? 9.247  42.045 16.265 1.00 39.20 ? 84  GLU A OE2   1 
ATOM   579  N N     . GLN A 1 94  ? 8.700  36.119 15.573 1.00 18.84 ? 85  GLN A N     1 
ATOM   580  C CA    . GLN A 1 94  ? 9.877  35.267 15.427 1.00 18.40 ? 85  GLN A CA    1 
ATOM   581  C C     . GLN A 1 94  ? 9.771  34.370 14.196 1.00 17.55 ? 85  GLN A C     1 
ATOM   582  O O     . GLN A 1 94  ? 10.771 34.120 13.519 1.00 19.00 ? 85  GLN A O     1 
ATOM   583  C CB    . GLN A 1 94  ? 10.086 34.423 16.700 1.00 17.52 ? 85  GLN A CB    1 
ATOM   584  C CG    . GLN A 1 94  ? 10.533 35.245 17.888 1.00 17.61 ? 85  GLN A CG    1 
ATOM   585  C CD    . GLN A 1 94  ? 10.191 34.583 19.216 1.00 18.14 ? 85  GLN A CD    1 
ATOM   586  O OE1   . GLN A 1 94  ? 9.505  33.553 19.254 1.00 19.23 ? 85  GLN A OE1   1 
ATOM   587  N NE2   . GLN A 1 94  ? 10.624 35.191 20.301 1.00 20.87 ? 85  GLN A NE2   1 
ATOM   588  N N     . VAL A 1 95  ? 8.574  33.840 13.918 1.00 19.07 ? 86  VAL A N     1 
ATOM   589  C CA    . VAL A 1 95  ? 8.373  33.005 12.740 1.00 18.67 ? 86  VAL A CA    1 
ATOM   590  C C     . VAL A 1 95  ? 8.708  33.797 11.472 1.00 18.83 ? 86  VAL A C     1 
ATOM   591  O O     . VAL A 1 95  ? 9.453  33.319 10.603 1.00 18.53 ? 86  VAL A O     1 
ATOM   592  C CB    . VAL A 1 95  ? 6.932  32.449 12.708 1.00 20.21 ? 86  VAL A CB    1 
ATOM   593  C CG1   . VAL A 1 95  ? 6.639  31.795 11.362 1.00 20.40 ? 86  VAL A CG1   1 
ATOM   594  C CG2   . VAL A 1 95  ? 6.695  31.460 13.839 1.00 20.51 ? 86  VAL A CG2   1 
ATOM   595  N N     . ARG A 1 96  ? 8.218  35.042 11.379 1.00 20.98 ? 87  ARG A N     1 
ATOM   596  C CA    . ARG A 1 96  ? 8.483  35.846 10.184 1.00 22.93 ? 87  ARG A CA    1 
ATOM   597  C C     . ARG A 1 96  ? 9.974  36.063 9.974  1.00 23.51 ? 87  ARG A C     1 
ATOM   598  O O     . ARG A 1 96  ? 10.454 36.050 8.831  1.00 20.83 ? 87  ARG A O     1 
ATOM   599  C CB    . ARG A 1 96  ? 7.763  37.199 10.275 1.00 23.41 ? 87  ARG A CB    1 
ATOM   600  C CG    . ARG A 1 96  ? 6.259  37.079 10.089 1.00 30.76 ? 87  ARG A CG    1 
ATOM   601  C CD    . ARG A 1 96  ? 5.607  38.452 9.906  1.00 31.34 ? 87  ARG A CD    1 
ATOM   602  N NE    . ARG A 1 96  ? 5.709  39.264 11.115 1.00 31.79 ? 87  ARG A NE    1 
ATOM   603  C CZ    . ARG A 1 96  ? 4.876  39.207 12.147 1.00 32.89 ? 87  ARG A CZ    1 
ATOM   604  N NH1   . ARG A 1 96  ? 3.890  38.325 12.198 1.00 33.92 ? 87  ARG A NH1   1 
ATOM   605  N NH2   . ARG A 1 96  ? 5.032  40.066 13.149 1.00 33.00 ? 87  ARG A NH2   1 
ATOM   606  N N     . GLU A 1 97  ? 10.731 36.271 11.060 1.00 18.36 ? 88  GLU A N     1 
ATOM   607  C CA    . GLU A 1 97  ? 12.150 36.548 10.874 1.00 17.57 ? 88  GLU A CA    1 
ATOM   608  C C     . GLU A 1 97  ? 12.946 35.270 10.610 1.00 19.69 ? 88  GLU A C     1 
ATOM   609  O O     . GLU A 1 97  ? 13.892 35.280 9.811  1.00 18.68 ? 88  GLU A O     1 
ATOM   610  C CB    . GLU A 1 97  ? 12.692 37.306 12.079 1.00 19.42 ? 88  GLU A CB    1 
ATOM   611  C CG    . GLU A 1 97  ? 12.023 38.686 12.289 1.00 23.25 ? 88  GLU A CG    1 
ATOM   612  C CD    . GLU A 1 97  ? 11.987 39.534 11.028 1.00 28.55 ? 88  GLU A CD    1 
ATOM   613  O OE1   . GLU A 1 97  ? 13.046 39.707 10.396 1.00 32.34 ? 88  GLU A OE1   1 
ATOM   614  O OE2   . GLU A 1 97  ? 10.897 40.025 10.657 1.00 39.77 ? 88  GLU A OE2   1 
ATOM   615  N N     . TRP A 1 98  ? 12.566 34.156 11.248 1.00 16.52 ? 89  TRP A N     1 
ATOM   616  C CA    . TRP A 1 98  ? 13.166 32.875 10.886 1.00 14.30 ? 89  TRP A CA    1 
ATOM   617  C C     . TRP A 1 98  ? 12.951 32.535 9.410  1.00 17.20 ? 89  TRP A C     1 
ATOM   618  O O     . TRP A 1 98  ? 13.848 31.987 8.767  1.00 18.62 ? 89  TRP A O     1 
ATOM   619  C CB    . TRP A 1 98  ? 12.586 31.759 11.749 1.00 16.08 ? 89  TRP A CB    1 
ATOM   620  C CG    . TRP A 1 98  ? 13.281 31.518 13.077 1.00 16.24 ? 89  TRP A CG    1 
ATOM   621  C CD1   . TRP A 1 98  ? 12.726 31.597 14.321 1.00 20.02 ? 89  TRP A CD1   1 
ATOM   622  C CD2   . TRP A 1 98  ? 14.650 31.125 13.268 1.00 15.92 ? 89  TRP A CD2   1 
ATOM   623  N NE1   . TRP A 1 98  ? 13.665 31.255 15.278 1.00 17.27 ? 89  TRP A NE1   1 
ATOM   624  C CE2   . TRP A 1 98  ? 14.854 30.978 14.652 1.00 18.06 ? 89  TRP A CE2   1 
ATOM   625  C CE3   . TRP A 1 98  ? 15.720 30.907 12.405 1.00 17.38 ? 89  TRP A CE3   1 
ATOM   626  C CZ2   . TRP A 1 98  ? 16.081 30.601 15.183 1.00 18.55 ? 89  TRP A CZ2   1 
ATOM   627  C CZ3   . TRP A 1 98  ? 16.941 30.519 12.933 1.00 17.68 ? 89  TRP A CZ3   1 
ATOM   628  C CH2   . TRP A 1 98  ? 17.113 30.379 14.314 1.00 18.67 ? 89  TRP A CH2   1 
ATOM   629  N N     . LYS A 1 99  ? 11.759 32.809 8.873  1.00 16.21 ? 90  LYS A N     1 
ATOM   630  C CA    . LYS A 1 99  ? 11.485 32.525 7.450  1.00 19.68 ? 90  LYS A CA    1 
ATOM   631  C C     . LYS A 1 99  ? 12.562 33.100 6.543  1.00 20.57 ? 90  LYS A C     1 
ATOM   632  O O     . LYS A 1 99  ? 12.978 32.461 5.567  1.00 20.84 ? 90  LYS A O     1 
ATOM   633  C CB    . LYS A 1 99  ? 10.090 33.075 7.085  1.00 20.76 ? 90  LYS A CB    1 
ATOM   634  C CG    . LYS A 1 99  ? 9.593  33.079 5.582  1.00 32.58 ? 90  LYS A CG    1 
ATOM   635  C CD    . LYS A 1 99  ? 10.035 32.017 4.578  1.00 48.84 ? 90  LYS A CD    1 
ATOM   636  C CE    . LYS A 1 99  ? 9.896  30.610 5.073  1.00 47.53 ? 90  LYS A CE    1 
ATOM   637  N NZ    . LYS A 1 99  ? 10.768 29.572 4.440  1.00 30.12 ? 90  LYS A NZ    1 
ATOM   638  N N     . LYS A 1 100 ? 13.028 34.304 6.846  1.00 18.82 ? 91  LYS A N     1 
ATOM   639  C CA    . LYS A 1 100 ? 14.029 34.933 6.001  1.00 19.85 ? 91  LYS A CA    1 
ATOM   640  C C     . LYS A 1 100 ? 15.358 34.186 6.053  1.00 24.75 ? 91  LYS A C     1 
ATOM   641  O O     . LYS A 1 100 ? 16.061 34.090 5.042  1.00 22.49 ? 91  LYS A O     1 
ATOM   642  C CB    . LYS A 1 100 ? 14.189 36.379 6.448  1.00 22.09 ? 91  LYS A CB    1 
ATOM   643  C CG    . LYS A 1 100 ? 13.024 37.234 5.987  1.00 27.42 ? 91  LYS A CG    1 
ATOM   644  C CD    . LYS A 1 100 ? 12.486 38.164 7.044  1.00 38.08 ? 91  LYS A CD    1 
ATOM   645  C CE    . LYS A 1 100 ? 13.401 39.334 7.272  1.00 35.25 ? 91  LYS A CE    1 
ATOM   646  N NZ    . LYS A 1 100 ? 12.633 40.513 7.825  1.00 37.25 ? 91  LYS A NZ    1 
ATOM   647  N N     . ILE A 1 101 ? 15.701 33.629 7.216  1.00 16.52 ? 92  ILE A N     1 
ATOM   648  C CA    . ILE A 1 101 ? 16.920 32.850 7.360  1.00 16.26 ? 92  ILE A CA    1 
ATOM   649  C C     . ILE A 1 101 ? 16.774 31.492 6.687  1.00 18.06 ? 92  ILE A C     1 
ATOM   650  O O     . ILE A 1 101 ? 17.696 31.016 6.014  1.00 18.71 ? 92  ILE A O     1 
ATOM   651  C CB    . ILE A 1 101 ? 17.238 32.706 8.866  1.00 18.86 ? 92  ILE A CB    1 
ATOM   652  C CG1   . ILE A 1 101 ? 17.615 34.072 9.426  1.00 18.85 ? 92  ILE A CG1   1 
ATOM   653  C CG2   . ILE A 1 101 ? 18.307 31.639 9.078  1.00 18.60 ? 92  ILE A CG2   1 
ATOM   654  C CD1   . ILE A 1 101 ? 17.332 34.188 10.931 1.00 21.82 ? 92  ILE A CD1   1 
ATOM   655  N N     . VAL A 1 102 ? 15.634 30.828 6.894  1.00 18.41 ? 93  VAL A N     1 
ATOM   656  C CA    . VAL A 1 102 ? 15.411 29.520 6.284  1.00 17.10 ? 93  VAL A CA    1 
ATOM   657  C C     . VAL A 1 102 ? 15.473 29.636 4.765  1.00 17.63 ? 93  VAL A C     1 
ATOM   658  O O     . VAL A 1 102 ? 16.034 28.776 4.071  1.00 19.06 ? 93  VAL A O     1 
ATOM   659  C CB    . VAL A 1 102 ? 14.066 28.941 6.760  1.00 17.52 ? 93  VAL A CB    1 
ATOM   660  C CG1   . VAL A 1 102 ? 13.708 27.666 5.964  1.00 19.87 ? 93  VAL A CG1   1 
ATOM   661  C CG2   . VAL A 1 102 ? 14.147 28.636 8.259  1.00 19.75 ? 93  VAL A CG2   1 
ATOM   662  N N     . ASP A 1 103 ? 14.940 30.730 4.232  1.00 19.42 ? 94  ASP A N     1 
ATOM   663  C CA    . ASP A 1 103 ? 14.958 30.926 2.782  1.00 19.90 ? 94  ASP A CA    1 
ATOM   664  C C     . ASP A 1 103 ? 16.369 31.023 2.217  1.00 21.67 ? 94  ASP A C     1 
ATOM   665  O O     . ASP A 1 103 ? 16.639 30.464 1.145  1.00 22.97 ? 94  ASP A O     1 
ATOM   666  C CB    . ASP A 1 103 ? 14.163 32.181 2.425  1.00 24.38 ? 94  ASP A CB    1 
ATOM   667  C CG    . ASP A 1 103 ? 12.669 31.938 2.385  1.00 36.48 ? 94  ASP A CG    1 
ATOM   668  O OD1   . ASP A 1 103 ? 12.223 30.794 2.650  1.00 29.78 ? 94  ASP A OD1   1 
ATOM   669  O OD2   . ASP A 1 103 ? 11.936 32.925 2.163  1.00 38.38 ? 94  ASP A OD2   1 
ATOM   670  N N     . VAL A 1 104 ? 17.273 31.761 2.873  1.00 19.67 ? 95  VAL A N     1 
ATOM   671  C CA    . VAL A 1 104 ? 18.625 31.853 2.321  1.00 20.72 ? 95  VAL A CA    1 
ATOM   672  C C     . VAL A 1 104 ? 19.368 30.528 2.453  1.00 25.03 ? 95  VAL A C     1 
ATOM   673  O O     . VAL A 1 104 ? 20.196 30.191 1.599  1.00 21.31 ? 95  VAL A O     1 
ATOM   674  C CB    . VAL A 1 104 ? 19.433 33.027 2.923  1.00 25.97 ? 95  VAL A CB    1 
ATOM   675  C CG1   . VAL A 1 104 ? 18.723 34.331 2.672  1.00 28.91 ? 95  VAL A CG1   1 
ATOM   676  C CG2   . VAL A 1 104 ? 19.689 32.849 4.426  1.00 24.70 ? 95  VAL A CG2   1 
ATOM   677  N N     . VAL A 1 105 ? 19.064 29.732 3.480  1.00 17.44 ? 96  VAL A N     1 
ATOM   678  C CA    . VAL A 1 105 ? 19.706 28.430 3.592  1.00 17.35 ? 96  VAL A CA    1 
ATOM   679  C C     . VAL A 1 105 ? 19.196 27.477 2.515  1.00 18.49 ? 96  VAL A C     1 
ATOM   680  O O     . VAL A 1 105 ? 19.976 26.748 1.886  1.00 18.18 ? 96  VAL A O     1 
ATOM   681  C CB    . VAL A 1 105 ? 19.479 27.884 5.019  1.00 17.98 ? 96  VAL A CB    1 
ATOM   682  C CG1   . VAL A 1 105 ? 19.865 26.429 5.109  1.00 21.64 ? 96  VAL A CG1   1 
ATOM   683  C CG2   . VAL A 1 105 ? 20.273 28.741 5.996  1.00 20.23 ? 96  VAL A CG2   1 
ATOM   684  N N     . HIS A 1 106 ? 17.890 27.477 2.281  1.00 19.06 ? 97  HIS A N     1 
ATOM   685  C CA    . HIS A 1 106 ? 17.313 26.647 1.228  1.00 20.70 ? 97  HIS A CA    1 
ATOM   686  C C     . HIS A 1 106 ? 17.780 27.078 -0.156 1.00 21.27 ? 97  HIS A C     1 
ATOM   687  O O     . HIS A 1 106 ? 17.853 26.250 -1.075 1.00 21.47 ? 97  HIS A O     1 
ATOM   688  C CB    . HIS A 1 106 ? 15.795 26.703 1.312  1.00 19.57 ? 97  HIS A CB    1 
ATOM   689  C CG    . HIS A 1 106 ? 15.241 25.835 2.390  1.00 20.15 ? 97  HIS A CG    1 
ATOM   690  N ND1   . HIS A 1 106 ? 13.937 25.917 2.818  1.00 22.47 ? 97  HIS A ND1   1 
ATOM   691  C CD2   . HIS A 1 106 ? 15.823 24.858 3.125  1.00 20.99 ? 97  HIS A CD2   1 
ATOM   692  C CE1   . HIS A 1 106 ? 13.735 25.024 3.777  1.00 20.68 ? 97  HIS A CE1   1 
ATOM   693  N NE2   . HIS A 1 106 ? 14.866 24.372 3.983  1.00 22.50 ? 97  HIS A NE2   1 
ATOM   694  N N     . ALA A 1 107 ? 18.094 28.360 -0.328 1.00 18.00 ? 98  ALA A N     1 
ATOM   695  C CA    . ALA A 1 107 ? 18.612 28.807 -1.617 1.00 19.83 ? 98  ALA A CA    1 
ATOM   696  C C     . ALA A 1 107 ? 19.991 28.226 -1.913 1.00 27.72 ? 98  ALA A C     1 
ATOM   697  O O     . ALA A 1 107 ? 20.403 28.205 -3.087 1.00 24.15 ? 98  ALA A O     1 
ATOM   698  C CB    . ALA A 1 107 ? 18.628 30.332 -1.652 1.00 18.12 ? 98  ALA A CB    1 
ATOM   699  N N     . LYS A 1 108 ? 20.691 27.720 -0.894 1.00 21.98 ? 99  LYS A N     1 
ATOM   700  C CA    . LYS A 1 108 ? 21.938 26.987 -1.075 1.00 19.95 ? 99  LYS A CA    1 
ATOM   701  C C     . LYS A 1 108 ? 21.721 25.487 -1.230 1.00 23.03 ? 99  LYS A C     1 
ATOM   702  O O     . LYS A 1 108 ? 22.702 24.759 -1.422 1.00 27.96 ? 99  LYS A O     1 
ATOM   703  C CB    . LYS A 1 108 ? 22.904 27.242 0.100  1.00 24.95 ? 99  LYS A CB    1 
ATOM   704  C CG    . LYS A 1 108 ? 23.456 28.667 0.169  1.00 34.47 ? 99  LYS A CG    1 
ATOM   705  C CD    . LYS A 1 108 ? 24.866 28.706 -0.385 1.00 42.75 ? 99  LYS A CD    1 
ATOM   706  C CE    . LYS A 1 108 ? 25.776 29.639 0.372  1.00 44.14 ? 99  LYS A CE    1 
ATOM   707  N NZ    . LYS A 1 108 ? 26.794 28.860 1.123  1.00 29.96 ? 99  LYS A NZ    1 
ATOM   708  N N     . GLY A 1 109 ? 20.478 25.011 -1.125 1.00 20.51 ? 100 GLY A N     1 
ATOM   709  C CA    . GLY A 1 109 ? 20.178 23.595 -1.232 1.00 19.45 ? 100 GLY A CA    1 
ATOM   710  C C     . GLY A 1 109 ? 20.385 22.792 0.030  1.00 19.22 ? 100 GLY A C     1 
ATOM   711  O O     . GLY A 1 109 ? 20.446 21.559 -0.029 1.00 18.38 ? 100 GLY A O     1 
ATOM   712  N N     . ALA A 1 110 ? 20.508 23.462 1.159  1.00 18.06 ? 101 ALA A N     1 
ATOM   713  C CA    . ALA A 1 110 ? 20.733 22.792 2.435  1.00 16.98 ? 101 ALA A CA    1 
ATOM   714  C C     . ALA A 1 110 ? 19.407 22.448 3.101  1.00 19.89 ? 101 ALA A C     1 
ATOM   715  O O     . ALA A 1 110 ? 18.351 22.971 2.755  1.00 17.91 ? 101 ALA A O     1 
ATOM   716  C CB    . ALA A 1 110 ? 21.581 23.677 3.346  1.00 17.76 ? 101 ALA A CB    1 
ATOM   717  N N     . VAL A 1 111 ? 19.476 21.541 4.073  1.00 17.71 ? 102 VAL A N     1 
ATOM   718  C CA    . VAL A 1 111 ? 18.330 21.113 4.866  1.00 14.35 ? 102 VAL A CA    1 
ATOM   719  C C     . VAL A 1 111 ? 18.557 21.669 6.263  1.00 14.62 ? 102 VAL A C     1 
ATOM   720  O O     . VAL A 1 111 ? 19.691 21.632 6.747  1.00 15.84 ? 102 VAL A O     1 
ATOM   721  C CB    . VAL A 1 111 ? 18.229 19.575 4.897  1.00 15.78 ? 102 VAL A CB    1 
ATOM   722  C CG1   . VAL A 1 111 ? 17.151 19.092 5.900  1.00 18.04 ? 102 VAL A CG1   1 
ATOM   723  C CG2   . VAL A 1 111 ? 17.948 19.045 3.477  1.00 20.09 ? 102 VAL A CG2   1 
ATOM   724  N N     . ILE A 1 112 ? 17.536 22.252 6.880  1.00 14.39 ? 103 ILE A N     1 
ATOM   725  C CA    . ILE A 1 112 ? 17.802 22.863 8.191  1.00 13.80 ? 103 ILE A CA    1 
ATOM   726  C C     . ILE A 1 112 ? 16.695 22.523 9.179  1.00 14.86 ? 103 ILE A C     1 
ATOM   727  O O     . ILE A 1 112 ? 15.504 22.655 8.868  1.00 16.03 ? 103 ILE A O     1 
ATOM   728  C CB    . ILE A 1 112 ? 18.008 24.390 8.073  1.00 15.25 ? 103 ILE A CB    1 
ATOM   729  C CG1   . ILE A 1 112 ? 18.289 25.011 9.438  1.00 16.30 ? 103 ILE A CG1   1 
ATOM   730  C CG2   . ILE A 1 112 ? 16.834 25.077 7.361  1.00 18.34 ? 103 ILE A CG2   1 
ATOM   731  C CD1   . ILE A 1 112 ? 18.929 26.414 9.286  1.00 19.27 ? 103 ILE A CD1   1 
ATOM   732  N N     . PHE A 1 113 ? 17.097 22.071 10.369 1.00 14.48 ? 104 PHE A N     1 
ATOM   733  C CA    . PHE A 1 113 ? 16.184 21.812 11.487 1.00 14.04 ? 104 PHE A CA    1 
ATOM   734  C C     . PHE A 1 113 ? 16.351 22.870 12.578 1.00 17.28 ? 104 PHE A C     1 
ATOM   735  O O     . PHE A 1 113 ? 17.474 23.313 12.854 1.00 15.67 ? 104 PHE A O     1 
ATOM   736  C CB    . PHE A 1 113 ? 16.458 20.436 12.123 1.00 13.61 ? 104 PHE A CB    1 
ATOM   737  C CG    . PHE A 1 113 ? 15.767 19.274 11.455 1.00 15.35 ? 104 PHE A CG    1 
ATOM   738  C CD1   . PHE A 1 113 ? 15.486 19.279 10.078 1.00 17.46 ? 104 PHE A CD1   1 
ATOM   739  C CD2   . PHE A 1 113 ? 15.457 18.126 12.205 1.00 18.91 ? 104 PHE A CD2   1 
ATOM   740  C CE1   . PHE A 1 113 ? 14.882 18.162 9.450  1.00 16.93 ? 104 PHE A CE1   1 
ATOM   741  C CE2   . PHE A 1 113 ? 14.852 17.019 11.601 1.00 16.73 ? 104 PHE A CE2   1 
ATOM   742  C CZ    . PHE A 1 113 ? 14.569 17.036 10.196 1.00 18.98 ? 104 PHE A CZ    1 
ATOM   743  N N     . CYS A 1 114 ? 15.252 23.244 13.233 1.00 14.27 ? 105 CYS A N     1 
ATOM   744  C CA    . CYS A 1 114 ? 15.311 24.147 14.373 1.00 15.50 ? 105 CYS A CA    1 
ATOM   745  C C     . CYS A 1 114 ? 15.372 23.326 15.668 1.00 13.04 ? 105 CYS A C     1 
ATOM   746  O O     . CYS A 1 114 ? 14.476 22.514 15.934 1.00 15.13 ? 105 CYS A O     1 
ATOM   747  C CB    . CYS A 1 114 ? 14.073 25.061 14.377 1.00 13.34 ? 105 CYS A CB    1 
ATOM   748  S SG    . CYS A 1 114 ? 13.997 26.228 15.736 1.00 18.09 ? 105 CYS A SG    1 
ATOM   749  N N     . GLN A 1 115 ? 16.365 23.605 16.507 1.00 13.99 ? 106 GLN A N     1 
ATOM   750  C CA    . GLN A 1 115 ? 16.454 22.949 17.820 1.00 13.68 ? 106 GLN A CA    1 
ATOM   751  C C     . GLN A 1 115 ? 15.569 23.666 18.846 1.00 17.03 ? 106 GLN A C     1 
ATOM   752  O O     . GLN A 1 115 ? 15.743 24.863 19.099 1.00 16.11 ? 106 GLN A O     1 
ATOM   753  C CB    . GLN A 1 115 ? 17.892 22.915 18.324 1.00 15.23 ? 106 GLN A CB    1 
ATOM   754  C CG    . GLN A 1 115 ? 17.942 22.033 19.569 1.00 15.14 ? 106 GLN A CG    1 
ATOM   755  C CD    . GLN A 1 115 ? 19.257 22.072 20.290 1.00 17.67 ? 106 GLN A CD    1 
ATOM   756  O OE1   . GLN A 1 115 ? 19.665 23.109 20.779 1.00 15.21 ? 106 GLN A OE1   1 
ATOM   757  N NE2   . GLN A 1 115 ? 19.926 20.926 20.359 1.00 14.58 ? 106 GLN A NE2   1 
ATOM   758  N N     . LEU A 1 116 ? 14.660 22.918 19.476 1.00 14.16 ? 107 LEU A N     1 
ATOM   759  C CA    . LEU A 1 116 ? 13.703 23.465 20.433 1.00 13.21 ? 107 LEU A CA    1 
ATOM   760  C C     . LEU A 1 116 ? 14.280 23.256 21.833 1.00 13.89 ? 107 LEU A C     1 
ATOM   761  O O     . LEU A 1 116 ? 14.513 22.111 22.246 1.00 17.10 ? 107 LEU A O     1 
ATOM   762  C CB    . LEU A 1 116 ? 12.338 22.783 20.310 1.00 14.64 ? 107 LEU A CB    1 
ATOM   763  C CG    . LEU A 1 116 ? 11.657 22.872 18.930 1.00 16.17 ? 107 LEU A CG    1 
ATOM   764  C CD1   . LEU A 1 116 ? 10.267 22.283 19.044 1.00 19.27 ? 107 LEU A CD1   1 
ATOM   765  C CD2   . LEU A 1 116 ? 11.643 24.331 18.430 1.00 16.60 ? 107 LEU A CD2   1 
ATOM   766  N N     . TRP A 1 117 ? 14.463 24.342 22.570 1.00 13.70 ? 108 TRP A N     1 
ATOM   767  C CA    . TRP A 1 117 ? 15.273 24.327 23.794 1.00 15.01 ? 108 TRP A CA    1 
ATOM   768  C C     . TRP A 1 117 ? 14.532 24.940 24.977 1.00 16.48 ? 108 TRP A C     1 
ATOM   769  O O     . TRP A 1 117 ? 14.127 26.112 24.925 1.00 17.63 ? 108 TRP A O     1 
ATOM   770  C CB    . TRP A 1 117 ? 16.567 25.096 23.530 1.00 17.17 ? 108 TRP A CB    1 
ATOM   771  C CG    . TRP A 1 117 ? 17.601 25.123 24.624 1.00 14.02 ? 108 TRP A CG    1 
ATOM   772  C CD1   . TRP A 1 117 ? 17.806 24.209 25.644 1.00 15.44 ? 108 TRP A CD1   1 
ATOM   773  C CD2   . TRP A 1 117 ? 18.621 26.112 24.749 1.00 16.32 ? 108 TRP A CD2   1 
ATOM   774  N NE1   . TRP A 1 117 ? 18.909 24.600 26.389 1.00 15.53 ? 108 TRP A NE1   1 
ATOM   775  C CE2   . TRP A 1 117 ? 19.413 25.768 25.859 1.00 17.01 ? 108 TRP A CE2   1 
ATOM   776  C CE3   . TRP A 1 117 ? 18.933 27.282 24.022 1.00 16.06 ? 108 TRP A CE3   1 
ATOM   777  C CZ2   . TRP A 1 117 ? 20.505 26.546 26.256 1.00 20.30 ? 108 TRP A CZ2   1 
ATOM   778  C CZ3   . TRP A 1 117 ? 20.020 28.059 24.421 1.00 16.59 ? 108 TRP A CZ3   1 
ATOM   779  C CH2   . TRP A 1 117 ? 20.800 27.675 25.513 1.00 18.02 ? 108 TRP A CH2   1 
ATOM   780  N N     . HIS A 1 118 ? 14.393 24.168 26.061 1.00 13.74 ? 109 HIS A N     1 
ATOM   781  C CA    . HIS A 1 118 ? 13.952 24.707 27.342 1.00 15.25 ? 109 HIS A CA    1 
ATOM   782  C C     . HIS A 1 118 ? 15.030 24.409 28.377 1.00 15.16 ? 109 HIS A C     1 
ATOM   783  O O     . HIS A 1 118 ? 15.409 23.245 28.559 1.00 15.03 ? 109 HIS A O     1 
ATOM   784  C CB    . HIS A 1 118 ? 12.615 24.097 27.755 1.00 14.61 ? 109 HIS A CB    1 
ATOM   785  C CG    . HIS A 1 118 ? 11.909 24.860 28.823 1.00 15.47 ? 109 HIS A CG    1 
ATOM   786  N ND1   . HIS A 1 118 ? 12.481 25.136 30.049 1.00 15.34 ? 109 HIS A ND1   1 
ATOM   787  C CD2   . HIS A 1 118 ? 10.654 25.367 28.866 1.00 17.57 ? 109 HIS A CD2   1 
ATOM   788  C CE1   . HIS A 1 118 ? 11.621 25.812 30.787 1.00 17.19 ? 109 HIS A CE1   1 
ATOM   789  N NE2   . HIS A 1 118 ? 10.496 25.950 30.103 1.00 17.32 ? 109 HIS A NE2   1 
ATOM   790  N N     . VAL A 1 119 ? 15.497 25.454 29.072 1.00 14.77 ? 110 VAL A N     1 
ATOM   791  C CA    . VAL A 1 119 ? 16.609 25.278 30.006 1.00 15.11 ? 110 VAL A CA    1 
ATOM   792  C C     . VAL A 1 119 ? 16.184 24.790 31.382 1.00 16.52 ? 110 VAL A C     1 
ATOM   793  O O     . VAL A 1 119 ? 17.049 24.399 32.177 1.00 14.62 ? 110 VAL A O     1 
ATOM   794  C CB    . VAL A 1 119 ? 17.394 26.585 30.219 1.00 13.91 ? 110 VAL A CB    1 
ATOM   795  C CG1   . VAL A 1 119 ? 17.951 27.074 28.895 1.00 14.92 ? 110 VAL A CG1   1 
ATOM   796  C CG2   . VAL A 1 119 ? 16.491 27.670 30.833 1.00 14.78 ? 110 VAL A CG2   1 
ATOM   797  N N     . GLY A 1 120 ? 14.898 24.787 31.681 1.00 12.56 ? 111 GLY A N     1 
ATOM   798  C CA    . GLY A 1 120 ? 14.500 24.376 33.026 1.00 16.01 ? 111 GLY A CA    1 
ATOM   799  C C     . GLY A 1 120 ? 15.184 25.220 34.085 1.00 17.50 ? 111 GLY A C     1 
ATOM   800  O O     . GLY A 1 120 ? 15.212 26.451 34.015 1.00 16.76 ? 111 GLY A O     1 
ATOM   801  N N     . ARG A 1 121 ? 15.758 24.547 35.093 1.00 14.24 ? 112 ARG A N     1 
ATOM   802  C CA    . ARG A 1 121 ? 16.300 25.280 36.234 1.00 16.79 ? 112 ARG A CA    1 
ATOM   803  C C     . ARG A 1 121 ? 17.577 26.033 35.899 1.00 17.36 ? 112 ARG A C     1 
ATOM   804  O O     . ARG A 1 121 ? 18.064 26.795 36.749 1.00 17.07 ? 112 ARG A O     1 
ATOM   805  C CB    . ARG A 1 121 ? 16.549 24.324 37.410 1.00 16.08 ? 112 ARG A CB    1 
ATOM   806  C CG    . ARG A 1 121 ? 17.684 23.340 37.190 1.00 13.77 ? 112 ARG A CG    1 
ATOM   807  C CD    . ARG A 1 121 ? 17.837 22.387 38.398 1.00 15.52 ? 112 ARG A CD    1 
ATOM   808  N NE    . ARG A 1 121 ? 18.954 21.488 38.157 1.00 16.60 ? 112 ARG A NE    1 
ATOM   809  C CZ    . ARG A 1 121 ? 19.549 20.775 39.101 1.00 17.95 ? 112 ARG A CZ    1 
ATOM   810  N NH1   . ARG A 1 121 ? 19.120 20.792 40.360 1.00 20.51 ? 112 ARG A NH1   1 
ATOM   811  N NH2   . ARG A 1 121 ? 20.592 20.024 38.775 1.00 18.64 ? 112 ARG A NH2   1 
ATOM   812  N N     . ALA A 1 122 ? 18.129 25.856 34.694 1.00 15.80 ? 113 ALA A N     1 
ATOM   813  C CA    . ALA A 1 122 ? 19.357 26.542 34.299 1.00 15.28 ? 113 ALA A CA    1 
ATOM   814  C C     . ALA A 1 122 ? 19.044 27.938 33.760 1.00 16.53 ? 113 ALA A C     1 
ATOM   815  O O     . ALA A 1 122 ? 19.246 28.250 32.582 1.00 17.41 ? 113 ALA A O     1 
ATOM   816  C CB    . ALA A 1 122 ? 20.099 25.709 33.265 1.00 16.64 ? 113 ALA A CB    1 
ATOM   817  N N     . SER A 1 123 ? 18.532 28.775 34.652 1.00 17.19 ? 114 SER A N     1 
ATOM   818  C CA    . SER A 1 123 ? 18.096 30.115 34.276 1.00 17.11 ? 114 SER A CA    1 
ATOM   819  C C     . SER A 1 123 ? 18.338 31.022 35.477 1.00 15.97 ? 114 SER A C     1 
ATOM   820  O O     . SER A 1 123 ? 19.048 30.644 36.417 1.00 16.38 ? 114 SER A O     1 
ATOM   821  C CB    . SER A 1 123 ? 16.634 30.102 33.806 1.00 15.50 ? 114 SER A CB    1 
ATOM   822  O OG    . SER A 1 123 ? 16.298 31.372 33.239 1.00 17.52 ? 114 SER A OG    1 
ATOM   823  N N     . HIS A 1 124 ? 17.709 32.191 35.462 1.00 17.30 ? 115 HIS A N     1 
ATOM   824  C CA    . HIS A 1 124 ? 17.941 33.249 36.447 1.00 15.19 ? 115 HIS A CA    1 
ATOM   825  C C     . HIS A 1 124 ? 16.779 34.216 36.318 1.00 18.69 ? 115 HIS A C     1 
ATOM   826  O O     . HIS A 1 124 ? 16.168 34.330 35.247 1.00 18.09 ? 115 HIS A O     1 
ATOM   827  C CB    . HIS A 1 124 ? 19.281 33.946 36.159 1.00 16.58 ? 115 HIS A CB    1 
ATOM   828  C CG    . HIS A 1 124 ? 19.722 34.897 37.226 1.00 20.78 ? 115 HIS A CG    1 
ATOM   829  N ND1   . HIS A 1 124 ? 19.239 36.183 37.312 1.00 21.27 ? 115 HIS A ND1   1 
ATOM   830  C CD2   . HIS A 1 124 ? 20.642 34.767 38.212 1.00 21.32 ? 115 HIS A CD2   1 
ATOM   831  C CE1   . HIS A 1 124 ? 19.814 36.798 38.332 1.00 24.79 ? 115 HIS A CE1   1 
ATOM   832  N NE2   . HIS A 1 124 ? 20.678 35.966 38.889 1.00 20.20 ? 115 HIS A NE2   1 
ATOM   833  N N     . GLU A 1 125 ? 16.496 34.946 37.414 1.00 18.50 ? 116 GLU A N     1 
ATOM   834  C CA    . GLU A 1 125 ? 15.443 35.965 37.377 1.00 20.65 ? 116 GLU A CA    1 
ATOM   835  C C     . GLU A 1 125 ? 15.592 36.925 36.192 1.00 18.02 ? 116 GLU A C     1 
ATOM   836  O O     . GLU A 1 125 ? 14.589 37.349 35.607 1.00 20.30 ? 116 GLU A O     1 
ATOM   837  C CB    . GLU A 1 125 ? 15.438 36.763 38.693 1.00 22.05 ? 116 GLU A CB    1 
ATOM   838  N N     . VAL A 1 126 ? 16.830 37.263 35.814 1.00 19.57 ? 117 VAL A N     1 
ATOM   839  C CA    . VAL A 1 126 ? 17.046 38.264 34.769 1.00 17.60 ? 117 VAL A CA    1 
ATOM   840  C C     . VAL A 1 126 ? 16.523 37.751 33.426 1.00 19.06 ? 117 VAL A C     1 
ATOM   841  O O     . VAL A 1 126 ? 16.205 38.548 32.532 1.00 20.55 ? 117 VAL A O     1 
ATOM   842  C CB    . VAL A 1 126 ? 18.537 38.663 34.686 1.00 16.56 ? 117 VAL A CB    1 
ATOM   843  C CG1   . VAL A 1 126 ? 19.407 37.537 34.083 1.00 16.94 ? 117 VAL A CG1   1 
ATOM   844  C CG2   . VAL A 1 126 ? 18.688 39.966 33.915 1.00 17.93 ? 117 VAL A CG2   1 
ATOM   845  N N     . TYR A 1 127 ? 16.409 36.427 33.279 1.00 16.78 ? 118 TYR A N     1 
ATOM   846  C CA    . TYR A 1 127 ? 15.969 35.795 32.034 1.00 15.93 ? 118 TYR A CA    1 
ATOM   847  C C     . TYR A 1 127 ? 14.496 35.409 32.052 1.00 20.38 ? 118 TYR A C     1 
ATOM   848  O O     . TYR A 1 127 ? 13.989 34.890 31.045 1.00 20.73 ? 118 TYR A O     1 
ATOM   849  C CB    . TYR A 1 127 ? 16.797 34.540 31.741 1.00 15.61 ? 118 TYR A CB    1 
ATOM   850  C CG    . TYR A 1 127 ? 18.226 34.844 31.424 1.00 14.47 ? 118 TYR A CG    1 
ATOM   851  C CD1   . TYR A 1 127 ? 18.541 35.720 30.379 1.00 16.72 ? 118 TYR A CD1   1 
ATOM   852  C CD2   . TYR A 1 127 ? 19.264 34.256 32.147 1.00 13.94 ? 118 TYR A CD2   1 
ATOM   853  C CE1   . TYR A 1 127 ? 19.859 36.008 30.067 1.00 15.84 ? 118 TYR A CE1   1 
ATOM   854  C CE2   . TYR A 1 127 ? 20.587 34.566 31.864 1.00 17.31 ? 118 TYR A CE2   1 
ATOM   855  C CZ    . TYR A 1 127 ? 20.868 35.452 30.822 1.00 16.20 ? 118 TYR A CZ    1 
ATOM   856  O OH    . TYR A 1 127 ? 22.180 35.736 30.544 1.00 19.25 ? 118 TYR A OH    1 
ATOM   857  N N     . GLN A 1 128 ? 13.805 35.606 33.186 1.00 20.31 ? 119 GLN A N     1 
ATOM   858  C CA    . GLN A 1 128 ? 12.442 35.140 33.351 1.00 19.88 ? 119 GLN A CA    1 
ATOM   859  C C     . GLN A 1 128 ? 11.462 36.310 33.354 1.00 23.88 ? 119 GLN A C     1 
ATOM   860  O O     . GLN A 1 128 ? 11.766 37.382 33.895 1.00 25.88 ? 119 GLN A O     1 
ATOM   861  C CB    . GLN A 1 128 ? 12.273 34.376 34.674 1.00 22.39 ? 119 GLN A CB    1 
ATOM   862  C CG    . GLN A 1 128 ? 13.006 33.044 34.707 1.00 18.63 ? 119 GLN A CG    1 
ATOM   863  C CD    . GLN A 1 128 ? 12.428 32.059 33.707 1.00 22.52 ? 119 GLN A CD    1 
ATOM   864  O OE1   . GLN A 1 128 ? 11.208 31.998 33.530 1.00 24.36 ? 119 GLN A OE1   1 
ATOM   865  N NE2   . GLN A 1 128 ? 13.299 31.303 33.033 1.00 20.45 ? 119 GLN A NE2   1 
ATOM   866  N N     . PRO A 1 129 ? 10.263 36.114 32.815 1.00 24.56 ? 120 PRO A N     1 
ATOM   867  C CA    . PRO A 1 129 ? 9.225  37.153 32.916 1.00 27.34 ? 120 PRO A CA    1 
ATOM   868  C C     . PRO A 1 129 ? 8.948  37.495 34.370 1.00 28.92 ? 120 PRO A C     1 
ATOM   869  O O     . PRO A 1 129 ? 8.815  36.608 35.217 1.00 31.08 ? 120 PRO A O     1 
ATOM   870  C CB    . PRO A 1 129 ? 8.003  36.501 32.256 1.00 28.75 ? 120 PRO A CB    1 
ATOM   871  C CG    . PRO A 1 129 ? 8.554  35.456 31.374 1.00 33.92 ? 120 PRO A CG    1 
ATOM   872  C CD    . PRO A 1 129 ? 9.795  34.939 32.056 1.00 28.45 ? 120 PRO A CD    1 
ATOM   873  N N     . ALA A 1 130 ? 8.874  38.798 34.659 1.00 33.08 ? 121 ALA A N     1 
ATOM   874  C CA    . ALA A 1 130 ? 8.593  39.308 36.006 1.00 30.94 ? 121 ALA A CA    1 
ATOM   875  C C     . ALA A 1 130 ? 9.573  38.789 37.050 1.00 33.93 ? 121 ALA A C     1 
ATOM   876  O O     . ALA A 1 130 ? 9.267  38.783 38.254 1.00 32.20 ? 121 ALA A O     1 
ATOM   877  C CB    . ALA A 1 130 ? 7.161  38.979 36.439 1.00 39.58 ? 121 ALA A CB    1 
ATOM   878  N N     . GLY A 1 131 ? 10.748 38.341 36.618 1.00 33.52 ? 122 GLY A N     1 
ATOM   879  C CA    . GLY A 1 131 ? 11.733 37.818 37.544 1.00 28.71 ? 122 GLY A CA    1 
ATOM   880  C C     . GLY A 1 131 ? 11.259 36.596 38.296 1.00 30.93 ? 122 GLY A C     1 
ATOM   881  O O     . GLY A 1 131 ? 11.740 36.328 39.399 1.00 29.05 ? 122 GLY A O     1 
ATOM   882  N N     . ALA A 1 132 ? 10.330 35.836 37.721 1.00 28.66 ? 123 ALA A N     1 
ATOM   883  C CA    . ALA A 1 132 ? 9.828  34.639 38.377 1.00 30.86 ? 123 ALA A CA    1 
ATOM   884  C C     . ALA A 1 132 ? 10.895 33.546 38.413 1.00 29.24 ? 123 ALA A C     1 
ATOM   885  O O     . ALA A 1 132 ? 11.870 33.570 37.664 1.00 26.10 ? 123 ALA A O     1 
ATOM   886  C CB    . ALA A 1 132 ? 8.583  34.125 37.664 1.00 29.58 ? 123 ALA A CB    1 
ATOM   887  N N     . ALA A 1 133 ? 10.688 32.573 39.301 1.00 24.01 ? 124 ALA A N     1 
ATOM   888  C CA    . ALA A 1 133 ? 11.598 31.435 39.414 1.00 25.28 ? 124 ALA A CA    1 
ATOM   889  C C     . ALA A 1 133 ? 11.537 30.545 38.169 1.00 20.68 ? 124 ALA A C     1 
ATOM   890  O O     . ALA A 1 133 ? 10.456 30.307 37.630 1.00 23.74 ? 124 ALA A O     1 
ATOM   891  C CB    . ALA A 1 133 ? 11.251 30.594 40.638 1.00 23.88 ? 124 ALA A CB    1 
ATOM   892  N N     . PRO A 1 134 ? 12.673 30.010 37.725 1.00 21.96 ? 125 PRO A N     1 
ATOM   893  C CA    . PRO A 1 134 ? 12.662 29.006 36.647 1.00 19.46 ? 125 PRO A CA    1 
ATOM   894  C C     . PRO A 1 134 ? 11.974 27.732 37.108 1.00 20.25 ? 125 PRO A C     1 
ATOM   895  O O     . PRO A 1 134 ? 11.835 27.476 38.305 1.00 21.68 ? 125 PRO A O     1 
ATOM   896  C CB    . PRO A 1 134 ? 14.152 28.739 36.378 1.00 22.47 ? 125 PRO A CB    1 
ATOM   897  C CG    . PRO A 1 134 ? 14.902 29.861 37.092 1.00 31.92 ? 125 PRO A CG    1 
ATOM   898  C CD    . PRO A 1 134 ? 14.023 30.289 38.225 1.00 20.46 ? 125 PRO A CD    1 
ATOM   899  N N     . ILE A 1 135 ? 11.565 26.916 36.141 1.00 18.05 ? 126 ILE A N     1 
ATOM   900  C CA    . ILE A 1 135 ? 10.814 25.684 36.421 1.00 20.11 ? 126 ILE A CA    1 
ATOM   901  C C     . ILE A 1 135 ? 11.713 24.469 36.224 1.00 19.17 ? 126 ILE A C     1 
ATOM   902  O O     . ILE A 1 135 ? 12.698 24.519 35.473 1.00 18.41 ? 126 ILE A O     1 
ATOM   903  C CB    . ILE A 1 135 ? 9.547  25.565 35.544 1.00 19.78 ? 126 ILE A CB    1 
ATOM   904  C CG1   . ILE A 1 135 ? 9.903  25.529 34.045 1.00 21.56 ? 126 ILE A CG1   1 
ATOM   905  C CG2   . ILE A 1 135 ? 8.588  26.722 35.859 1.00 26.57 ? 126 ILE A CG2   1 
ATOM   906  C CD1   . ILE A 1 135 ? 8.925  24.711 33.217 1.00 22.79 ? 126 ILE A CD1   1 
ATOM   907  N N     . SER A 1 136 ? 11.376 23.368 36.911 1.00 18.11 ? 127 SER A N     1 
ATOM   908  C CA    . SER A 1 136 ? 12.166 22.142 36.808 1.00 17.65 ? 127 SER A CA    1 
ATOM   909  C C     . SER A 1 136 ? 11.334 20.936 37.262 1.00 16.37 ? 127 SER A C     1 
ATOM   910  O O     . SER A 1 136 ? 10.189 21.058 37.718 1.00 18.30 ? 127 SER A O     1 
ATOM   911  C CB    . SER A 1 136 ? 13.467 22.257 37.619 1.00 16.04 ? 127 SER A CB    1 
ATOM   912  O OG    . SER A 1 136 ? 14.349 21.165 37.359 1.00 18.87 ? 127 SER A OG    1 
ATOM   913  N N     . SER A 1 137 ? 11.946 19.754 37.142 1.00 16.93 ? 128 SER A N     1 
ATOM   914  C CA    . SER A 1 137 ? 11.433 18.552 37.800 1.00 16.64 ? 128 SER A CA    1 
ATOM   915  C C     . SER A 1 137 ? 11.528 18.674 39.303 1.00 17.30 ? 128 SER A C     1 
ATOM   916  O O     . SER A 1 137 ? 10.720 18.085 40.030 1.00 17.61 ? 128 SER A O     1 
ATOM   917  C CB    . SER A 1 137 ? 12.250 17.339 37.375 1.00 17.42 ? 128 SER A CB    1 
ATOM   918  O OG    . SER A 1 137 ? 13.616 17.588 37.704 1.00 17.52 ? 128 SER A OG    1 
ATOM   919  N N     . THR A 1 138 ? 12.493 19.461 39.768 1.00 18.34 ? 129 THR A N     1 
ATOM   920  C CA    . THR A 1 138 ? 12.956 19.486 41.138 1.00 14.74 ? 129 THR A CA    1 
ATOM   921  C C     . THR A 1 138 ? 12.862 20.904 41.694 1.00 16.39 ? 129 THR A C     1 
ATOM   922  O O     . THR A 1 138 ? 12.767 21.879 40.938 1.00 18.83 ? 129 THR A O     1 
ATOM   923  C CB    . THR A 1 138 ? 14.407 18.956 41.204 1.00 18.48 ? 129 THR A CB    1 
ATOM   924  O OG1   . THR A 1 138 ? 14.824 18.924 42.569 1.00 20.14 ? 129 THR A OG1   1 
ATOM   925  C CG2   . THR A 1 138 ? 15.410 19.821 40.368 1.00 16.58 ? 129 THR A CG2   1 
ATOM   926  N N     . GLU A 1 139 ? 12.839 21.018 43.029 1.00 20.46 ? 130 GLU A N     1 
ATOM   927  C CA    . GLU A 1 139 ? 12.950 22.331 43.659 1.00 20.83 ? 130 GLU A CA    1 
ATOM   928  C C     . GLU A 1 139 ? 14.391 22.661 44.060 1.00 20.56 ? 130 GLU A C     1 
ATOM   929  O O     . GLU A 1 139 ? 14.634 23.737 44.637 1.00 21.55 ? 130 GLU A O     1 
ATOM   930  C CB    . GLU A 1 139 ? 12.008 22.432 44.878 1.00 23.04 ? 130 GLU A CB    1 
ATOM   931  N N     . LYS A 1 140 ? 15.377 21.759 43.764 1.00 18.16 ? 131 LYS A N     1 
ATOM   932  C CA    . LYS A 1 140 ? 16.783 21.990 44.125 1.00 18.26 ? 131 LYS A CA    1 
ATOM   933  C C     . LYS A 1 140 ? 17.495 22.850 43.079 1.00 20.29 ? 131 LYS A C     1 
ATOM   934  O O     . LYS A 1 140 ? 17.366 22.611 41.867 1.00 19.77 ? 131 LYS A O     1 
ATOM   935  C CB    . LYS A 1 140 ? 17.542 20.664 44.264 1.00 21.75 ? 131 LYS A CB    1 
ATOM   936  C CG    . LYS A 1 140 ? 17.012 19.735 45.362 1.00 21.00 ? 131 LYS A CG    1 
ATOM   937  C CD    . LYS A 1 140 ? 16.986 20.434 46.750 1.00 33.37 ? 131 LYS A CD    1 
ATOM   938  C CE    . LYS A 1 140 ? 18.188 20.060 47.600 1.00 39.78 ? 131 LYS A CE    1 
ATOM   939  N NZ    . LYS A 1 140 ? 17.814 19.819 49.030 1.00 41.36 ? 131 LYS A NZ    1 
ATOM   940  N N     . PRO A 1 141 ? 18.292 23.820 43.518 1.00 19.88 ? 132 PRO A N     1 
ATOM   941  C CA    . PRO A 1 141 ? 19.089 24.612 42.571 1.00 17.34 ? 132 PRO A CA    1 
ATOM   942  C C     . PRO A 1 141 ? 20.264 23.818 42.054 1.00 20.47 ? 132 PRO A C     1 
ATOM   943  O O     . PRO A 1 141 ? 20.765 22.905 42.717 1.00 19.52 ? 132 PRO A O     1 
ATOM   944  C CB    . PRO A 1 141 ? 19.566 25.799 43.414 1.00 19.85 ? 132 PRO A CB    1 
ATOM   945  C CG    . PRO A 1 141 ? 19.627 25.241 44.828 1.00 22.08 ? 132 PRO A CG    1 
ATOM   946  C CD    . PRO A 1 141 ? 18.528 24.210 44.922 1.00 20.81 ? 132 PRO A CD    1 
ATOM   947  N N     . ILE A 1 142 ? 20.703 24.163 40.831 1.00 16.82 ? 133 ILE A N     1 
ATOM   948  C CA    . ILE A 1 142 ? 22.044 23.775 40.415 1.00 16.86 ? 133 ILE A CA    1 
ATOM   949  C C     . ILE A 1 142 ? 23.045 24.213 41.493 1.00 17.92 ? 133 ILE A C     1 
ATOM   950  O O     . ILE A 1 142 ? 22.934 25.309 42.044 1.00 20.17 ? 133 ILE A O     1 
ATOM   951  C CB    . ILE A 1 142 ? 22.364 24.410 39.051 1.00 20.04 ? 133 ILE A CB    1 
ATOM   952  C CG1   . ILE A 1 142 ? 21.396 23.855 38.009 1.00 17.26 ? 133 ILE A CG1   1 
ATOM   953  C CG2   . ILE A 1 142 ? 23.811 24.171 38.650 1.00 18.27 ? 133 ILE A CG2   1 
ATOM   954  C CD1   . ILE A 1 142 ? 21.307 24.754 36.742 1.00 18.96 ? 133 ILE A CD1   1 
ATOM   955  N N     . SER A 1 143 ? 24.037 23.369 41.784 1.00 20.43 ? 134 SER A N     1 
ATOM   956  C CA    . SER A 1 143 ? 24.957 23.716 42.871 1.00 21.26 ? 134 SER A CA    1 
ATOM   957  C C     . SER A 1 143 ? 25.902 24.848 42.455 1.00 27.71 ? 134 SER A C     1 
ATOM   958  O O     . SER A 1 143 ? 26.057 25.162 41.277 1.00 23.28 ? 134 SER A O     1 
ATOM   959  C CB    . SER A 1 143 ? 25.787 22.511 43.295 1.00 24.80 ? 134 SER A CB    1 
ATOM   960  O OG    . SER A 1 143 ? 26.656 22.106 42.258 1.00 26.04 ? 134 SER A OG    1 
ATOM   961  N N     . ASN A 1 144 ? 26.586 25.449 43.442 1.00 27.67 ? 135 ASN A N     1 
ATOM   962  C CA    . ASN A 1 144 ? 27.475 26.564 43.104 1.00 26.72 ? 135 ASN A CA    1 
ATOM   963  C C     . ASN A 1 144 ? 28.807 26.122 42.485 1.00 28.85 ? 135 ASN A C     1 
ATOM   964  O O     . ASN A 1 144 ? 29.691 26.964 42.288 1.00 32.96 ? 135 ASN A O     1 
ATOM   965  C CB    . ASN A 1 144 ? 27.727 27.465 44.319 1.00 38.16 ? 135 ASN A CB    1 
ATOM   966  C CG    . ASN A 1 144 ? 28.206 26.703 45.518 1.00 44.59 ? 135 ASN A CG    1 
ATOM   967  O OD1   . ASN A 1 144 ? 28.898 25.690 45.394 1.00 43.54 ? 135 ASN A OD1   1 
ATOM   968  N ND2   . ASN A 1 144 ? 27.882 27.215 46.700 1.00 46.24 ? 135 ASN A ND2   1 
ATOM   969  N N     . ARG A 1 145 ? 28.954 24.847 42.127 1.00 24.17 ? 136 ARG A N     1 
ATOM   970  C CA    . ARG A 1 145 ? 29.998 24.426 41.206 1.00 28.15 ? 136 ARG A CA    1 
ATOM   971  C C     . ARG A 1 145 ? 29.831 25.093 39.837 1.00 28.63 ? 136 ARG A C     1 
ATOM   972  O O     . ARG A 1 145 ? 30.799 25.208 39.075 1.00 29.90 ? 136 ARG A O     1 
ATOM   973  C CB    . ARG A 1 145 ? 29.955 22.893 41.078 1.00 30.77 ? 136 ARG A CB    1 
ATOM   974  C CG    . ARG A 1 145 ? 30.797 22.298 39.971 1.00 42.33 ? 136 ARG A CG    1 
ATOM   975  C CD    . ARG A 1 145 ? 30.758 20.769 39.978 1.00 40.89 ? 136 ARG A CD    1 
ATOM   976  N NE    . ARG A 1 145 ? 31.528 20.231 38.861 1.00 58.36 ? 136 ARG A NE    1 
ATOM   977  C CZ    . ARG A 1 145 ? 31.261 19.094 38.231 1.00 54.82 ? 136 ARG A CZ    1 
ATOM   978  N NH1   . ARG A 1 145 ? 30.254 18.316 38.600 1.00 52.75 ? 136 ARG A NH1   1 
ATOM   979  N NH2   . ARG A 1 145 ? 32.023 18.728 37.205 1.00 51.28 ? 136 ARG A NH2   1 
ATOM   980  N N     . TRP A 1 146 ? 28.626 25.544 39.525 1.00 23.57 ? 137 TRP A N     1 
ATOM   981  C CA    . TRP A 1 146 ? 28.291 26.087 38.215 1.00 21.94 ? 137 TRP A CA    1 
ATOM   982  C C     . TRP A 1 146 ? 27.787 27.504 38.391 1.00 22.77 ? 137 TRP A C     1 
ATOM   983  O O     . TRP A 1 146 ? 27.118 27.811 39.375 1.00 23.57 ? 137 TRP A O     1 
ATOM   984  C CB    . TRP A 1 146 ? 27.215 25.255 37.525 1.00 23.34 ? 137 TRP A CB    1 
ATOM   985  C CG    . TRP A 1 146 ? 27.548 23.806 37.473 1.00 21.55 ? 137 TRP A CG    1 
ATOM   986  C CD1   . TRP A 1 146 ? 27.221 22.844 38.403 1.00 27.72 ? 137 TRP A CD1   1 
ATOM   987  C CD2   . TRP A 1 146 ? 28.300 23.147 36.460 1.00 23.23 ? 137 TRP A CD2   1 
ATOM   988  N NE1   . TRP A 1 146 ? 27.719 21.623 38.008 1.00 27.22 ? 137 TRP A NE1   1 
ATOM   989  C CE2   . TRP A 1 146 ? 28.387 21.783 36.820 1.00 24.37 ? 137 TRP A CE2   1 
ATOM   990  C CE3   . TRP A 1 146 ? 28.905 23.574 35.268 1.00 24.99 ? 137 TRP A CE3   1 
ATOM   991  C CZ2   . TRP A 1 146 ? 29.057 20.837 36.016 1.00 26.54 ? 137 TRP A CZ2   1 
ATOM   992  C CZ3   . TRP A 1 146 ? 29.570 22.630 34.475 1.00 33.60 ? 137 TRP A CZ3   1 
ATOM   993  C CH2   . TRP A 1 146 ? 29.644 21.289 34.861 1.00 26.17 ? 137 TRP A CH2   1 
ATOM   994  N N     . ARG A 1 147 ? 28.073 28.350 37.388 1.00 22.49 ? 138 ARG A N     1 
ATOM   995  C CA    . ARG A 1 147 ? 27.652 29.744 37.388 1.00 22.96 ? 138 ARG A CA    1 
ATOM   996  C C     . ARG A 1 147 ? 26.993 30.036 36.044 1.00 17.10 ? 138 ARG A C     1 
ATOM   997  O O     . ARG A 1 147 ? 27.356 29.444 35.029 1.00 22.85 ? 138 ARG A O     1 
ATOM   998  C CB    . ARG A 1 147 ? 28.852 30.669 37.588 1.00 25.31 ? 138 ARG A CB    1 
ATOM   999  C CG    . ARG A 1 147 ? 29.481 30.607 38.951 1.00 31.87 ? 138 ARG A CG    1 
ATOM   1000 C CD    . ARG A 1 147 ? 28.505 30.861 40.054 1.00 35.05 ? 138 ARG A CD    1 
ATOM   1001 N NE    . ARG A 1 147 ? 28.940 30.239 41.302 1.00 48.93 ? 138 ARG A NE    1 
ATOM   1002 C CZ    . ARG A 1 147 ? 29.533 30.892 42.292 1.00 54.67 ? 138 ARG A CZ    1 
ATOM   1003 N NH1   . ARG A 1 147 ? 29.834 32.178 42.185 1.00 55.38 ? 138 ARG A NH1   1 
ATOM   1004 N NH2   . ARG A 1 147 ? 29.830 30.241 43.416 1.00 55.76 ? 138 ARG A NH2   1 
ATOM   1005 N N     . ILE A 1 148 ? 26.012 30.937 36.033 1.00 19.24 ? 139 ILE A N     1 
ATOM   1006 C CA    . ILE A 1 148 ? 25.264 31.255 34.817 1.00 18.15 ? 139 ILE A CA    1 
ATOM   1007 C C     . ILE A 1 148 ? 25.830 32.536 34.211 1.00 17.83 ? 139 ILE A C     1 
ATOM   1008 O O     . ILE A 1 148 ? 26.126 33.498 34.929 1.00 19.12 ? 139 ILE A O     1 
ATOM   1009 C CB    . ILE A 1 148 ? 23.750 31.390 35.108 1.00 17.28 ? 139 ILE A CB    1 
ATOM   1010 C CG1   . ILE A 1 148 ? 22.962 31.489 33.809 1.00 17.44 ? 139 ILE A CG1   1 
ATOM   1011 C CG2   . ILE A 1 148 ? 23.430 32.588 36.031 1.00 22.17 ? 139 ILE A CG2   1 
ATOM   1012 C CD1   . ILE A 1 148 ? 21.460 31.387 33.954 1.00 17.36 ? 139 ILE A CD1   1 
ATOM   1013 N N     . LEU A 1 149 ? 26.007 32.541 32.895 1.00 19.09 ? 140 LEU A N     1 
ATOM   1014 C CA    . LEU A 1 149 ? 26.436 33.750 32.188 1.00 19.07 ? 140 LEU A CA    1 
ATOM   1015 C C     . LEU A 1 149 ? 25.311 34.775 32.262 1.00 20.19 ? 140 LEU A C     1 
ATOM   1016 O O     . LEU A 1 149 ? 24.169 34.473 31.907 1.00 16.89 ? 140 LEU A O     1 
ATOM   1017 C CB    . LEU A 1 149 ? 26.790 33.403 30.738 1.00 16.31 ? 140 LEU A CB    1 
ATOM   1018 C CG    . LEU A 1 149 ? 27.122 34.615 29.856 1.00 20.19 ? 140 LEU A CG    1 
ATOM   1019 C CD1   . LEU A 1 149 ? 28.389 35.324 30.372 1.00 23.35 ? 140 LEU A CD1   1 
ATOM   1020 C CD2   . LEU A 1 149 ? 27.286 34.135 28.414 1.00 19.97 ? 140 LEU A CD2   1 
ATOM   1021 N N     . MET A 1 150 ? 25.616 35.988 32.785 1.00 15.63 ? 141 MET A N     1 
ATOM   1022 C CA    . MET A 1 150 ? 24.621 37.051 32.857 1.00 18.48 ? 141 MET A CA    1 
ATOM   1023 C C     . MET A 1 150 ? 24.659 37.928 31.613 1.00 18.80 ? 141 MET A C     1 
ATOM   1024 O O     . MET A 1 150 ? 25.646 37.924 30.863 1.00 19.15 ? 141 MET A O     1 
ATOM   1025 C CB    . MET A 1 150 ? 24.860 37.915 34.099 1.00 16.05 ? 141 MET A CB    1 
ATOM   1026 C CG    . MET A 1 150 ? 24.808 37.079 35.384 1.00 19.58 ? 141 MET A CG    1 
ATOM   1027 S SD    . MET A 1 150 ? 23.121 36.544 35.767 1.00 21.92 ? 141 MET A SD    1 
ATOM   1028 C CE    . MET A 1 150 ? 22.363 38.077 36.293 1.00 23.19 ? 141 MET A CE    1 
ATOM   1029 N N     . PRO A 1 151 ? 23.603 38.710 31.374 1.00 16.42 ? 142 PRO A N     1 
ATOM   1030 C CA    . PRO A 1 151 ? 23.601 39.586 30.185 1.00 16.09 ? 142 PRO A CA    1 
ATOM   1031 C C     . PRO A 1 151 ? 24.718 40.623 30.182 1.00 19.26 ? 142 PRO A C     1 
ATOM   1032 O O     . PRO A 1 151 ? 25.082 41.103 29.096 1.00 21.06 ? 142 PRO A O     1 
ATOM   1033 C CB    . PRO A 1 151 ? 22.226 40.258 30.242 1.00 18.20 ? 142 PRO A CB    1 
ATOM   1034 C CG    . PRO A 1 151 ? 21.382 39.317 31.015 1.00 22.45 ? 142 PRO A CG    1 
ATOM   1035 C CD    . PRO A 1 151 ? 22.291 38.714 32.047 1.00 23.08 ? 142 PRO A CD    1 
ATOM   1036 N N     . ASP A 1 152 ? 25.275 40.990 31.341 1.00 17.22 ? 143 ASP A N     1 
ATOM   1037 C CA    . ASP A 1 152 ? 26.361 41.966 31.356 1.00 22.68 ? 143 ASP A CA    1 
ATOM   1038 C C     . ASP A 1 152 ? 27.741 41.315 31.261 1.00 27.85 ? 143 ASP A C     1 
ATOM   1039 O O     . ASP A 1 152 ? 28.756 42.014 31.383 1.00 25.82 ? 143 ASP A O     1 
ATOM   1040 C CB    . ASP A 1 152 ? 26.275 42.871 32.603 1.00 21.81 ? 143 ASP A CB    1 
ATOM   1041 C CG    . ASP A 1 152 ? 26.359 42.116 33.925 1.00 25.82 ? 143 ASP A CG    1 
ATOM   1042 O OD1   . ASP A 1 152 ? 26.651 40.902 33.930 1.00 24.72 ? 143 ASP A OD1   1 
ATOM   1043 O OD2   . ASP A 1 152 ? 26.136 42.758 34.994 1.00 28.60 ? 143 ASP A OD2   1 
ATOM   1044 N N     . GLY A 1 153 ? 27.800 39.994 31.064 1.00 24.97 ? 144 GLY A N     1 
ATOM   1045 C CA    . GLY A 1 153 ? 29.056 39.281 30.959 1.00 24.03 ? 144 GLY A CA    1 
ATOM   1046 C C     . GLY A 1 153 ? 29.658 38.786 32.254 1.00 28.85 ? 144 GLY A C     1 
ATOM   1047 O O     . GLY A 1 153 ? 30.698 38.108 32.210 1.00 32.88 ? 144 GLY A O     1 
ATOM   1048 N N     . THR A 1 154 ? 29.063 39.110 33.399 1.00 22.97 ? 145 THR A N     1 
ATOM   1049 C CA    . THR A 1 154 ? 29.467 38.511 34.656 1.00 23.36 ? 145 THR A CA    1 
ATOM   1050 C C     . THR A 1 154 ? 28.845 37.123 34.767 1.00 22.80 ? 145 THR A C     1 
ATOM   1051 O O     . THR A 1 154 ? 28.097 36.679 33.893 1.00 21.65 ? 145 THR A O     1 
ATOM   1052 C CB    . THR A 1 154 ? 29.060 39.394 35.835 1.00 26.13 ? 145 THR A CB    1 
ATOM   1053 O OG1   . THR A 1 154 ? 27.630 39.422 35.959 1.00 25.18 ? 145 THR A OG1   1 
ATOM   1054 C CG2   . THR A 1 154 ? 29.588 40.839 35.637 1.00 32.29 ? 145 THR A CG2   1 
ATOM   1055 N N     . HIS A 1 155 ? 29.147 36.440 35.866 1.00 25.02 ? 146 HIS A N     1 
ATOM   1056 C CA    . HIS A 1 155 ? 28.635 35.101 36.120 1.00 22.68 ? 146 HIS A CA    1 
ATOM   1057 C C     . HIS A 1 155 ? 27.851 35.130 37.424 1.00 28.52 ? 146 HIS A C     1 
ATOM   1058 O O     . HIS A 1 155 ? 28.333 35.653 38.429 1.00 34.87 ? 146 HIS A O     1 
ATOM   1059 C CB    . HIS A 1 155 ? 29.791 34.108 36.146 1.00 25.79 ? 146 HIS A CB    1 
ATOM   1060 C CG    . HIS A 1 155 ? 30.227 33.699 34.781 1.00 31.12 ? 146 HIS A CG    1 
ATOM   1061 N ND1   . HIS A 1 155 ? 31.163 34.406 34.058 1.00 39.43 ? 146 HIS A ND1   1 
ATOM   1062 C CD2   . HIS A 1 155 ? 29.813 32.691 33.975 1.00 40.55 ? 146 HIS A CD2   1 
ATOM   1063 C CE1   . HIS A 1 155 ? 31.327 33.838 32.877 1.00 43.87 ? 146 HIS A CE1   1 
ATOM   1064 N NE2   . HIS A 1 155 ? 30.521 32.795 32.802 1.00 47.59 ? 146 HIS A NE2   1 
ATOM   1065 N N     . GLY A 1 156 ? 26.613 34.636 37.389 1.00 21.77 ? 147 GLY A N     1 
ATOM   1066 C CA    . GLY A 1 156 ? 25.682 34.782 38.482 1.00 20.69 ? 147 GLY A CA    1 
ATOM   1067 C C     . GLY A 1 156 ? 25.346 33.426 39.081 1.00 22.87 ? 147 GLY A C     1 
ATOM   1068 O O     . GLY A 1 156 ? 25.838 32.390 38.638 1.00 20.56 ? 147 GLY A O     1 
ATOM   1069 N N     . ILE A 1 157 ? 24.481 33.461 40.089 1.00 20.79 ? 148 ILE A N     1 
ATOM   1070 C CA    . ILE A 1 157 ? 24.161 32.287 40.899 1.00 20.31 ? 148 ILE A CA    1 
ATOM   1071 C C     . ILE A 1 157 ? 22.868 31.690 40.376 1.00 19.52 ? 148 ILE A C     1 
ATOM   1072 O O     . ILE A 1 157 ? 21.850 32.391 40.270 1.00 21.46 ? 148 ILE A O     1 
ATOM   1073 C CB    . ILE A 1 157 ? 24.009 32.676 42.382 1.00 21.23 ? 148 ILE A CB    1 
ATOM   1074 C CG1   . ILE A 1 157 ? 25.355 33.095 42.959 1.00 27.90 ? 148 ILE A CG1   1 
ATOM   1075 C CG2   . ILE A 1 157 ? 23.528 31.456 43.191 1.00 25.10 ? 148 ILE A CG2   1 
ATOM   1076 C CD1   . ILE A 1 157 ? 26.494 32.201 42.601 1.00 37.56 ? 148 ILE A CD1   1 
ATOM   1077 N N     . TYR A 1 158 ? 22.872 30.384 40.096 1.00 23.04 ? 149 TYR A N     1 
ATOM   1078 C CA    . TYR A 1 158 ? 21.620 29.746 39.695 1.00 19.10 ? 149 TYR A CA    1 
ATOM   1079 C C     . TYR A 1 158 ? 20.645 29.733 40.870 1.00 18.21 ? 149 TYR A C     1 
ATOM   1080 O O     . TYR A 1 158 ? 21.002 29.248 41.961 1.00 21.90 ? 149 TYR A O     1 
ATOM   1081 C CB    . TYR A 1 158 ? 21.849 28.320 39.224 1.00 18.64 ? 149 TYR A CB    1 
ATOM   1082 C CG    . TYR A 1 158 ? 22.500 28.172 37.865 1.00 17.59 ? 149 TYR A CG    1 
ATOM   1083 C CD1   . TYR A 1 158 ? 21.775 28.375 36.703 1.00 15.79 ? 149 TYR A CD1   1 
ATOM   1084 C CD2   . TYR A 1 158 ? 23.831 27.798 37.756 1.00 18.39 ? 149 TYR A CD2   1 
ATOM   1085 C CE1   . TYR A 1 158 ? 22.383 28.196 35.436 1.00 16.24 ? 149 TYR A CE1   1 
ATOM   1086 C CE2   . TYR A 1 158 ? 24.451 27.647 36.531 1.00 18.68 ? 149 TYR A CE2   1 
ATOM   1087 C CZ    . TYR A 1 158 ? 23.719 27.845 35.369 1.00 19.97 ? 149 TYR A CZ    1 
ATOM   1088 O OH    . TYR A 1 158 ? 24.356 27.679 34.143 1.00 22.52 ? 149 TYR A OH    1 
ATOM   1089 N N     . PRO A 1 159 ? 19.412 30.184 40.682 1.00 21.21 ? 150 PRO A N     1 
ATOM   1090 C CA    . PRO A 1 159 ? 18.452 30.256 41.785 1.00 19.31 ? 150 PRO A CA    1 
ATOM   1091 C C     . PRO A 1 159 ? 17.722 28.936 42.003 1.00 20.72 ? 150 PRO A C     1 
ATOM   1092 O O     . PRO A 1 159 ? 17.793 28.001 41.197 1.00 20.67 ? 150 PRO A O     1 
ATOM   1093 C CB    . PRO A 1 159 ? 17.474 31.332 41.308 1.00 28.71 ? 150 PRO A CB    1 
ATOM   1094 C CG    . PRO A 1 159 ? 17.441 31.095 39.758 1.00 22.35 ? 150 PRO A CG    1 
ATOM   1095 C CD    . PRO A 1 159 ? 18.852 30.699 39.416 1.00 22.29 ? 150 PRO A CD    1 
ATOM   1096 N N     . LYS A 1 160 ? 16.987 28.890 43.106 1.00 22.84 ? 151 LYS A N     1 
ATOM   1097 C CA    . LYS A 1 160 ? 16.092 27.772 43.374 1.00 20.98 ? 151 LYS A CA    1 
ATOM   1098 C C     . LYS A 1 160 ? 14.967 27.716 42.345 1.00 20.27 ? 151 LYS A C     1 
ATOM   1099 O O     . LYS A 1 160 ? 14.236 28.705 42.187 1.00 23.13 ? 151 LYS A O     1 
ATOM   1100 C CB    . LYS A 1 160 ? 15.517 27.927 44.785 1.00 23.17 ? 151 LYS A CB    1 
ATOM   1101 C CG    . LYS A 1 160 ? 14.675 26.756 45.265 1.00 28.27 ? 151 LYS A CG    1 
ATOM   1102 C CD    . LYS A 1 160 ? 14.341 26.896 46.753 1.00 28.78 ? 151 LYS A CD    1 
ATOM   1103 C CE    . LYS A 1 160 ? 13.240 27.931 47.015 1.00 38.99 ? 151 LYS A CE    1 
ATOM   1104 N NZ    . LYS A 1 160 ? 12.962 28.045 48.501 1.00 43.50 ? 151 LYS A NZ    1 
ATOM   1105 N N     . PRO A 1 161 ? 14.779 26.598 41.644 1.00 19.15 ? 152 PRO A N     1 
ATOM   1106 C CA    . PRO A 1 161 ? 13.642 26.463 40.732 1.00 19.41 ? 152 PRO A CA    1 
ATOM   1107 C C     . PRO A 1 161 ? 12.364 26.078 41.468 1.00 20.84 ? 152 PRO A C     1 
ATOM   1108 O O     . PRO A 1 161 ? 12.370 25.690 42.633 1.00 22.05 ? 152 PRO A O     1 
ATOM   1109 C CB    . PRO A 1 161 ? 14.078 25.331 39.789 1.00 21.31 ? 152 PRO A CB    1 
ATOM   1110 C CG    . PRO A 1 161 ? 14.922 24.456 40.667 1.00 17.84 ? 152 PRO A CG    1 
ATOM   1111 C CD    . PRO A 1 161 ? 15.640 25.401 41.650 1.00 17.06 ? 152 PRO A CD    1 
ATOM   1112 N N     . ARG A 1 162 ? 11.259 26.199 40.743 1.00 21.23 ? 153 ARG A N     1 
ATOM   1113 C CA    . ARG A 1 162 ? 9.948  25.713 41.152 1.00 20.95 ? 153 ARG A CA    1 
ATOM   1114 C C     . ARG A 1 162 ? 9.703  24.340 40.522 1.00 20.36 ? 153 ARG A C     1 
ATOM   1115 O O     . ARG A 1 162 ? 9.788  24.193 39.294 1.00 20.35 ? 153 ARG A O     1 
ATOM   1116 C CB    . ARG A 1 162 ? 8.899  26.735 40.707 1.00 26.89 ? 153 ARG A CB    1 
ATOM   1117 C CG    . ARG A 1 162 ? 7.467  26.432 41.025 1.00 33.50 ? 153 ARG A CG    1 
ATOM   1118 C CD    . ARG A 1 162 ? 6.624  27.666 40.714 1.00 29.50 ? 153 ARG A CD    1 
ATOM   1119 N NE    . ARG A 1 162 ? 6.615  28.037 39.298 1.00 29.58 ? 153 ARG A NE    1 
ATOM   1120 C CZ    . ARG A 1 162 ? 5.853  27.443 38.388 1.00 23.72 ? 153 ARG A CZ    1 
ATOM   1121 N NH1   . ARG A 1 162 ? 5.117  26.396 38.695 1.00 25.82 ? 153 ARG A NH1   1 
ATOM   1122 N NH2   . ARG A 1 162 ? 5.819  27.924 37.148 1.00 27.41 ? 153 ARG A NH2   1 
ATOM   1123 N N     . ALA A 1 163 ? 9.408  23.327 41.347 1.00 19.50 ? 154 ALA A N     1 
ATOM   1124 C CA    . ALA A 1 163 ? 9.108  21.995 40.821 1.00 19.67 ? 154 ALA A CA    1 
ATOM   1125 C C     . ALA A 1 163 ? 7.684  22.010 40.288 1.00 22.78 ? 154 ALA A C     1 
ATOM   1126 O O     . ALA A 1 163 ? 6.765  22.416 40.998 1.00 27.02 ? 154 ALA A O     1 
ATOM   1127 C CB    . ALA A 1 163 ? 9.263  20.932 41.910 1.00 22.10 ? 154 ALA A CB    1 
ATOM   1128 N N     . ILE A 1 164 ? 7.493  21.623 39.025 1.00 19.05 ? 155 ILE A N     1 
ATOM   1129 C CA    . ILE A 1 164 ? 6.163  21.794 38.443 1.00 18.93 ? 155 ILE A CA    1 
ATOM   1130 C C     . ILE A 1 164 ? 5.312  20.554 38.650 1.00 17.36 ? 155 ILE A C     1 
ATOM   1131 O O     . ILE A 1 164 ? 5.810  19.431 38.759 1.00 19.87 ? 155 ILE A O     1 
ATOM   1132 C CB    . ILE A 1 164 ? 6.270  22.155 36.956 1.00 17.83 ? 155 ILE A CB    1 
ATOM   1133 C CG1   . ILE A 1 164 ? 7.027  21.061 36.200 1.00 19.69 ? 155 ILE A CG1   1 
ATOM   1134 C CG2   . ILE A 1 164 ? 6.945  23.517 36.872 1.00 19.46 ? 155 ILE A CG2   1 
ATOM   1135 C CD1   . ILE A 1 164 ? 6.987  21.254 34.677 1.00 18.45 ? 155 ILE A CD1   1 
ATOM   1136 N N     . GLY A 1 165 ? 3.997  20.777 38.721 1.00 16.92 ? 156 GLY A N     1 
ATOM   1137 C CA    . GLY A 1 165 ? 3.038  19.694 38.790 1.00 17.03 ? 156 GLY A CA    1 
ATOM   1138 C C     . GLY A 1 165 ? 2.805  19.092 37.424 1.00 18.84 ? 156 GLY A C     1 
ATOM   1139 O O     . GLY A 1 165 ? 3.305  19.567 36.403 1.00 16.90 ? 156 GLY A O     1 
ATOM   1140 N N     . THR A 1 166 ? 2.007  18.025 37.394 1.00 17.33 ? 157 THR A N     1 
ATOM   1141 C CA    . THR A 1 166 ? 1.878  17.319 36.125 1.00 16.32 ? 157 THR A CA    1 
ATOM   1142 C C     . THR A 1 166 ? 0.992  18.054 35.126 1.00 16.67 ? 157 THR A C     1 
ATOM   1143 O O     . THR A 1 166 ? 1.196  17.903 33.920 1.00 16.67 ? 157 THR A O     1 
ATOM   1144 C CB    . THR A 1 166 ? 1.378  15.885 36.329 1.00 19.48 ? 157 THR A CB    1 
ATOM   1145 O OG1   . THR A 1 166 ? 0.048  15.872 36.869 1.00 17.26 ? 157 THR A OG1   1 
ATOM   1146 C CG2   . THR A 1 166 ? 2.338  15.103 37.220 1.00 19.56 ? 157 THR A CG2   1 
ATOM   1147 N N     . TYR A 1 167 ? 0.030  18.869 35.569 1.00 16.53 ? 158 TYR A N     1 
ATOM   1148 C CA    . TYR A 1 167 ? -0.679 19.697 34.591 1.00 17.42 ? 158 TYR A CA    1 
ATOM   1149 C C     . TYR A 1 167 ? 0.292  20.647 33.892 1.00 17.25 ? 158 TYR A C     1 
ATOM   1150 O O     . TYR A 1 167 ? 0.296  20.759 32.651 1.00 17.09 ? 158 TYR A O     1 
ATOM   1151 C CB    . TYR A 1 167 ? -1.807 20.477 35.266 1.00 17.02 ? 158 TYR A CB    1 
ATOM   1152 C CG    . TYR A 1 167 ? -2.445 21.454 34.314 1.00 17.51 ? 158 TYR A CG    1 
ATOM   1153 C CD1   . TYR A 1 167 ? -3.173 20.999 33.215 1.00 19.51 ? 158 TYR A CD1   1 
ATOM   1154 C CD2   . TYR A 1 167 ? -2.297 22.825 34.490 1.00 20.40 ? 158 TYR A CD2   1 
ATOM   1155 C CE1   . TYR A 1 167 ? -3.744 21.881 32.336 1.00 21.48 ? 158 TYR A CE1   1 
ATOM   1156 C CE2   . TYR A 1 167 ? -2.866 23.720 33.617 1.00 21.12 ? 158 TYR A CE2   1 
ATOM   1157 C CZ    . TYR A 1 167 ? -3.588 23.233 32.536 1.00 22.32 ? 158 TYR A CZ    1 
ATOM   1158 O OH    . TYR A 1 167 ? -4.175 24.088 31.643 1.00 23.69 ? 158 TYR A OH    1 
ATOM   1159 N N     . GLU A 1 168 ? 1.148  21.307 34.671 1.00 16.92 ? 159 GLU A N     1 
ATOM   1160 C CA    . GLU A 1 168 ? 2.142  22.205 34.090 1.00 15.42 ? 159 GLU A CA    1 
ATOM   1161 C C     . GLU A 1 168 ? 3.090  21.457 33.152 1.00 19.28 ? 159 GLU A C     1 
ATOM   1162 O O     . GLU A 1 168 ? 3.455  21.987 32.092 1.00 15.83 ? 159 GLU A O     1 
ATOM   1163 C CB    . GLU A 1 168 ? 2.903  22.946 35.206 1.00 19.53 ? 159 GLU A CB    1 
ATOM   1164 C CG    . GLU A 1 168 ? 3.774  24.044 34.629 1.00 27.33 ? 159 GLU A CG    1 
ATOM   1165 C CD    . GLU A 1 168 ? 4.141  25.158 35.608 1.00 28.26 ? 159 GLU A CD    1 
ATOM   1166 O OE1   . GLU A 1 168 ? 3.708  25.121 36.786 1.00 29.27 ? 159 GLU A OE1   1 
ATOM   1167 O OE2   . GLU A 1 168 ? 4.849  26.097 35.151 1.00 29.77 ? 159 GLU A OE2   1 
ATOM   1168 N N     . ILE A 1 169 ? 3.457  20.212 33.486 1.00 16.86 ? 160 ILE A N     1 
ATOM   1169 C CA    . ILE A 1 169 ? 4.210  19.385 32.539 1.00 17.70 ? 160 ILE A CA    1 
ATOM   1170 C C     . ILE A 1 169 ? 3.465  19.281 31.214 1.00 16.81 ? 160 ILE A C     1 
ATOM   1171 O O     . ILE A 1 169 ? 4.049  19.463 30.141 1.00 15.39 ? 160 ILE A O     1 
ATOM   1172 C CB    . ILE A 1 169 ? 4.482  17.988 33.131 1.00 18.34 ? 160 ILE A CB    1 
ATOM   1173 C CG1   . ILE A 1 169 ? 5.489  18.094 34.274 1.00 17.82 ? 160 ILE A CG1   1 
ATOM   1174 C CG2   . ILE A 1 169 ? 4.982  17.042 32.014 1.00 17.28 ? 160 ILE A CG2   1 
ATOM   1175 C CD1   . ILE A 1 169 ? 5.720  16.735 35.033 1.00 19.08 ? 160 ILE A CD1   1 
ATOM   1176 N N     . SER A 1 170 ? 2.157  18.991 31.263 1.00 17.44 ? 161 SER A N     1 
ATOM   1177 C CA    . SER A 1 170 ? 1.422  18.861 30.008 1.00 17.11 ? 161 SER A CA    1 
ATOM   1178 C C     . SER A 1 170 ? 1.352  20.193 29.266 1.00 18.76 ? 161 SER A C     1 
ATOM   1179 O O     . SER A 1 170 ? 1.292  20.211 28.033 1.00 18.83 ? 161 SER A O     1 
ATOM   1180 C CB    . SER A 1 170 ? 0.015  18.291 30.259 1.00 18.57 ? 161 SER A CB    1 
ATOM   1181 O OG    . SER A 1 170 ? -0.853 19.252 30.858 1.00 20.92 ? 161 SER A OG    1 
ATOM   1182 N N     . GLN A 1 171 ? 1.395  21.312 29.993 1.00 17.41 ? 162 GLN A N     1 
ATOM   1183 C CA    . GLN A 1 171 ? 1.432  22.611 29.321 1.00 16.68 ? 162 GLN A CA    1 
ATOM   1184 C C     . GLN A 1 171 ? 2.768  22.836 28.623 1.00 16.99 ? 162 GLN A C     1 
ATOM   1185 O O     . GLN A 1 171 ? 2.821  23.450 27.542 1.00 17.14 ? 162 GLN A O     1 
ATOM   1186 C CB    . GLN A 1 171 ? 1.202  23.727 30.327 1.00 18.40 ? 162 GLN A CB    1 
ATOM   1187 C CG    . GLN A 1 171 ? -0.210 23.865 30.889 1.00 20.76 ? 162 GLN A CG    1 
ATOM   1188 C CD    . GLN A 1 171 ? -0.283 25.048 31.853 1.00 28.99 ? 162 GLN A CD    1 
ATOM   1189 O OE1   . GLN A 1 171 ? 0.432  25.086 32.862 1.00 30.86 ? 162 GLN A OE1   1 
ATOM   1190 N NE2   . GLN A 1 171 ? -1.131 26.027 31.535 1.00 30.43 ? 162 GLN A NE2   1 
ATOM   1191 N N     . VAL A 1 172 ? 3.869  22.407 29.252 1.00 16.09 ? 163 VAL A N     1 
ATOM   1192 C CA    . VAL A 1 172 ? 5.168  22.552 28.613 1.00 16.93 ? 163 VAL A CA    1 
ATOM   1193 C C     . VAL A 1 172 ? 5.225  21.695 27.355 1.00 16.51 ? 163 VAL A C     1 
ATOM   1194 O O     . VAL A 1 172 ? 5.795  22.095 26.330 1.00 17.05 ? 163 VAL A O     1 
ATOM   1195 C CB    . VAL A 1 172 ? 6.301  22.192 29.588 1.00 16.49 ? 163 VAL A CB    1 
ATOM   1196 C CG1   . VAL A 1 172 ? 7.631  22.218 28.851 1.00 20.29 ? 163 VAL A CG1   1 
ATOM   1197 C CG2   . VAL A 1 172 ? 6.316  23.183 30.745 1.00 17.99 ? 163 VAL A CG2   1 
ATOM   1198 N N     . VAL A 1 173 ? 4.655  20.496 27.423 1.00 14.34 ? 164 VAL A N     1 
ATOM   1199 C CA    . VAL A 1 173 ? 4.579  19.652 26.236 1.00 15.59 ? 164 VAL A CA    1 
ATOM   1200 C C     . VAL A 1 173 ? 3.855  20.387 25.117 1.00 18.02 ? 164 VAL A C     1 
ATOM   1201 O O     . VAL A 1 173 ? 4.287  20.361 23.958 1.00 16.76 ? 164 VAL A O     1 
ATOM   1202 C CB    . VAL A 1 173 ? 3.887  18.324 26.587 1.00 17.26 ? 164 VAL A CB    1 
ATOM   1203 C CG1   . VAL A 1 173 ? 3.567  17.545 25.330 1.00 16.41 ? 164 VAL A CG1   1 
ATOM   1204 C CG2   . VAL A 1 173 ? 4.765  17.465 27.503 1.00 17.27 ? 164 VAL A CG2   1 
ATOM   1205 N N     . GLU A 1 174 ? 2.760  21.078 25.449 1.00 15.57 ? 165 GLU A N     1 
ATOM   1206 C CA    . GLU A 1 174 ? 2.055  21.845 24.413 1.00 19.18 ? 165 GLU A CA    1 
ATOM   1207 C C     . GLU A 1 174 ? 2.901  23.003 23.871 1.00 18.94 ? 165 GLU A C     1 
ATOM   1208 O O     . GLU A 1 174 ? 2.789  23.341 22.686 1.00 19.31 ? 165 GLU A O     1 
ATOM   1209 C CB    . GLU A 1 174 ? 0.702  22.318 24.972 1.00 21.33 ? 165 GLU A CB    1 
ATOM   1210 C CG    . GLU A 1 174 ? -0.109 23.228 24.018 1.00 21.16 ? 165 GLU A CG    1 
ATOM   1211 C CD    . GLU A 1 174 ? -0.648 22.488 22.802 1.00 28.32 ? 165 GLU A CD    1 
ATOM   1212 O OE1   . GLU A 1 174 ? -0.617 21.240 22.794 1.00 28.47 ? 165 GLU A OE1   1 
ATOM   1213 O OE2   . GLU A 1 174 ? -1.117 23.150 21.839 1.00 30.63 ? 165 GLU A OE2   1 
ATOM   1214 N N     . ASP A 1 175 ? 3.762  23.604 24.694 1.00 17.21 ? 166 ASP A N     1 
ATOM   1215 C CA    . ASP A 1 175 ? 4.685  24.622 24.186 1.00 17.66 ? 166 ASP A CA    1 
ATOM   1216 C C     . ASP A 1 175 ? 5.626  24.044 23.136 1.00 18.33 ? 166 ASP A C     1 
ATOM   1217 O O     . ASP A 1 175 ? 5.926  24.698 22.127 1.00 16.10 ? 166 ASP A O     1 
ATOM   1218 C CB    . ASP A 1 175 ? 5.495  25.210 25.334 1.00 16.12 ? 166 ASP A CB    1 
ATOM   1219 C CG    . ASP A 1 175 ? 4.682  26.161 26.208 1.00 26.75 ? 166 ASP A CG    1 
ATOM   1220 O OD1   . ASP A 1 175 ? 3.660  26.720 25.746 1.00 25.58 ? 166 ASP A OD1   1 
ATOM   1221 O OD2   . ASP A 1 175 ? 5.055  26.325 27.395 1.00 25.20 ? 166 ASP A OD2   1 
ATOM   1222 N N     . TYR A 1 176 ? 6.138  22.835 23.373 1.00 17.32 ? 167 TYR A N     1 
ATOM   1223 C CA    . TYR A 1 176 ? 6.951  22.162 22.363 1.00 15.27 ? 167 TYR A CA    1 
ATOM   1224 C C     . TYR A 1 176 ? 6.148  21.932 21.101 1.00 16.59 ? 167 TYR A C     1 
ATOM   1225 O O     . TYR A 1 176 ? 6.633  22.188 19.993 1.00 15.60 ? 167 TYR A O     1 
ATOM   1226 C CB    . TYR A 1 176 ? 7.471  20.824 22.886 1.00 16.29 ? 167 TYR A CB    1 
ATOM   1227 C CG    . TYR A 1 176 ? 8.709  20.896 23.759 1.00 13.78 ? 167 TYR A CG    1 
ATOM   1228 C CD1   . TYR A 1 176 ? 9.984  21.016 23.195 1.00 13.35 ? 167 TYR A CD1   1 
ATOM   1229 C CD2   . TYR A 1 176 ? 8.609  20.761 25.138 1.00 15.44 ? 167 TYR A CD2   1 
ATOM   1230 C CE1   . TYR A 1 176 ? 11.133 21.021 23.991 1.00 12.82 ? 167 TYR A CE1   1 
ATOM   1231 C CE2   . TYR A 1 176 ? 9.743  20.788 25.941 1.00 16.69 ? 167 TYR A CE2   1 
ATOM   1232 C CZ    . TYR A 1 176 ? 10.989 20.923 25.362 1.00 17.23 ? 167 TYR A CZ    1 
ATOM   1233 O OH    . TYR A 1 176 ? 12.103 20.926 26.174 1.00 16.55 ? 167 TYR A OH    1 
ATOM   1234 N N     . ARG A 1 177 ? 4.909  21.474 21.253 1.00 16.68 ? 168 ARG A N     1 
ATOM   1235 C CA    . ARG A 1 177 ? 4.077  21.176 20.097 1.00 16.55 ? 168 ARG A CA    1 
ATOM   1236 C C     . ARG A 1 177 ? 3.806  22.417 19.267 1.00 17.20 ? 168 ARG A C     1 
ATOM   1237 O O     . ARG A 1 177 ? 3.925  22.379 18.032 1.00 16.65 ? 168 ARG A O     1 
ATOM   1238 C CB    . ARG A 1 177 ? 2.767  20.529 20.548 1.00 16.54 ? 168 ARG A CB    1 
ATOM   1239 C CG    . ARG A 1 177 ? 2.111  19.750 19.409 1.00 20.25 ? 168 ARG A CG    1 
ATOM   1240 C CD    . ARG A 1 177 ? 0.717  19.286 19.778 1.00 25.11 ? 168 ARG A CD    1 
ATOM   1241 N NE    . ARG A 1 177 ? -0.130 20.449 19.975 1.00 27.15 ? 168 ARG A NE    1 
ATOM   1242 C CZ    . ARG A 1 177 ? -0.888 20.972 19.017 1.00 27.68 ? 168 ARG A CZ    1 
ATOM   1243 N NH1   . ARG A 1 177 ? -1.007 20.385 17.834 1.00 30.85 ? 168 ARG A NH1   1 
ATOM   1244 N NH2   . ARG A 1 177 ? -1.536 22.106 19.251 1.00 25.94 ? 168 ARG A NH2   1 
ATOM   1245 N N     . ARG A 1 178 ? 3.441  23.531 19.923 1.00 17.59 ? 169 ARG A N     1 
ATOM   1246 C CA    . ARG A 1 178 ? 3.146  24.767 19.197 1.00 18.08 ? 169 ARG A CA    1 
ATOM   1247 C C     . ARG A 1 178 ? 4.400  25.349 18.571 1.00 16.65 ? 169 ARG A C     1 
ATOM   1248 O O     . ARG A 1 178 ? 4.348  25.918 17.478 1.00 18.51 ? 169 ARG A O     1 
ATOM   1249 C CB    . ARG A 1 178 ? 2.513  25.798 20.127 1.00 19.48 ? 169 ARG A CB    1 
ATOM   1250 C CG    . ARG A 1 178 ? 1.088  25.418 20.514 1.00 23.21 ? 169 ARG A CG    1 
ATOM   1251 C CD    . ARG A 1 178 ? 0.431  26.432 21.410 1.00 29.73 ? 169 ARG A CD    1 
ATOM   1252 N NE    . ARG A 1 178 ? -0.913 25.984 21.773 1.00 33.04 ? 169 ARG A NE    1 
ATOM   1253 C CZ    . ARG A 1 178 ? -1.864 26.772 22.258 1.00 46.32 ? 169 ARG A CZ    1 
ATOM   1254 N NH1   . ARG A 1 178 ? -1.653 28.062 22.470 1.00 42.46 ? 169 ARG A NH1   1 
ATOM   1255 N NH2   . ARG A 1 178 ? -3.055 26.250 22.544 1.00 47.38 ? 169 ARG A NH2   1 
ATOM   1256 N N     . SER A 1 179 ? 5.536  25.237 19.260 1.00 16.16 ? 170 SER A N     1 
ATOM   1257 C CA    . SER A 1 179 ? 6.787  25.689 18.664 1.00 16.21 ? 170 SER A CA    1 
ATOM   1258 C C     . SER A 1 179 ? 7.152  24.857 17.443 1.00 17.89 ? 170 SER A C     1 
ATOM   1259 O O     . SER A 1 179 ? 7.694  25.392 16.477 1.00 17.34 ? 170 SER A O     1 
ATOM   1260 C CB    . SER A 1 179 ? 7.915  25.653 19.708 1.00 17.90 ? 170 SER A CB    1 
ATOM   1261 O OG    . SER A 1 179 ? 7.690  26.664 20.673 1.00 22.39 ? 170 SER A OG    1 
ATOM   1262 N N     . ALA A 1 180 ? 6.873  23.547 17.465 1.00 16.10 ? 171 ALA A N     1 
ATOM   1263 C CA    . ALA A 1 180 ? 7.193  22.728 16.296 1.00 17.43 ? 171 ALA A CA    1 
ATOM   1264 C C     . ALA A 1 180 ? 6.346  23.147 15.104 1.00 16.79 ? 171 ALA A C     1 
ATOM   1265 O O     . ALA A 1 180 ? 6.849  23.222 13.972 1.00 16.63 ? 171 ALA A O     1 
ATOM   1266 C CB    . ALA A 1 180 ? 6.965  21.248 16.592 1.00 15.16 ? 171 ALA A CB    1 
ATOM   1267 N N     . LEU A 1 181 ? 5.067  23.438 15.345 1.00 16.73 ? 172 LEU A N     1 
ATOM   1268 C CA    . LEU A 1 181 ? 4.214  23.906 14.250 1.00 18.93 ? 172 LEU A CA    1 
ATOM   1269 C C     . LEU A 1 181 ? 4.673  25.267 13.744 1.00 19.75 ? 172 LEU A C     1 
ATOM   1270 O O     . LEU A 1 181 ? 4.635  25.532 12.541 1.00 18.74 ? 172 LEU A O     1 
ATOM   1271 C CB    . LEU A 1 181 ? 2.760  23.954 14.708 1.00 17.95 ? 172 LEU A CB    1 
ATOM   1272 C CG    . LEU A 1 181 ? 2.057  22.603 14.931 1.00 20.16 ? 172 LEU A CG    1 
ATOM   1273 C CD1   . LEU A 1 181 ? 0.790  22.787 15.721 1.00 21.62 ? 172 LEU A CD1   1 
ATOM   1274 C CD2   . LEU A 1 181 ? 1.758  21.945 13.563 1.00 19.83 ? 172 LEU A CD2   1 
ATOM   1275 N N     . ASN A 1 182 ? 5.147  26.130 14.641 1.00 16.48 ? 173 ASN A N     1 
ATOM   1276 C CA    . ASN A 1 182 ? 5.690  27.422 14.213 1.00 16.25 ? 173 ASN A CA    1 
ATOM   1277 C C     . ASN A 1 182 ? 6.947  27.238 13.381 1.00 18.00 ? 173 ASN A C     1 
ATOM   1278 O O     . ASN A 1 182 ? 7.166  27.967 12.401 1.00 17.99 ? 173 ASN A O     1 
ATOM   1279 C CB    . ASN A 1 182 ? 5.996  28.291 15.438 1.00 16.82 ? 173 ASN A CB    1 
ATOM   1280 C CG    . ASN A 1 182 ? 4.781  28.981 15.975 1.00 23.32 ? 173 ASN A CG    1 
ATOM   1281 O OD1   . ASN A 1 182 ? 3.698  28.876 15.417 1.00 22.91 ? 173 ASN A OD1   1 
ATOM   1282 N ND2   . ASN A 1 182 ? 4.959  29.731 17.066 1.00 23.58 ? 173 ASN A ND2   1 
ATOM   1283 N N     . ALA A 1 183 ? 7.795  26.265 13.750 1.00 15.72 ? 174 ALA A N     1 
ATOM   1284 C CA    . ALA A 1 183 ? 8.986  26.019 12.945 1.00 15.31 ? 174 ALA A CA    1 
ATOM   1285 C C     . ALA A 1 183 ? 8.617  25.590 11.523 1.00 16.87 ? 174 ALA A C     1 
ATOM   1286 O O     . ALA A 1 183 ? 9.222  26.060 10.555 1.00 17.01 ? 174 ALA A O     1 
ATOM   1287 C CB    . ALA A 1 183 ? 9.863  24.962 13.619 1.00 15.99 ? 174 ALA A CB    1 
ATOM   1288 N N     . ILE A 1 184 ? 7.607  24.721 11.386 1.00 17.68 ? 175 ILE A N     1 
ATOM   1289 C CA    . ILE A 1 184 ? 7.156  24.323 10.056 1.00 17.45 ? 175 ILE A CA    1 
ATOM   1290 C C     . ILE A 1 184 ? 6.620  25.528 9.292  1.00 21.25 ? 175 ILE A C     1 
ATOM   1291 O O     . ILE A 1 184 ? 6.873  25.678 8.081  1.00 18.51 ? 175 ILE A O     1 
ATOM   1292 C CB    . ILE A 1 184 ? 6.106  23.205 10.171 1.00 19.85 ? 175 ILE A CB    1 
ATOM   1293 C CG1   . ILE A 1 184 ? 6.743  21.953 10.767 1.00 19.95 ? 175 ILE A CG1   1 
ATOM   1294 C CG2   . ILE A 1 184 ? 5.461  22.916 8.794  1.00 22.22 ? 175 ILE A CG2   1 
ATOM   1295 C CD1   . ILE A 1 184 ? 7.882  21.398 9.932  1.00 24.27 ? 175 ILE A CD1   1 
ATOM   1296 N N     . GLU A 1 185 ? 5.891  26.412 9.985  1.00 19.74 ? 176 GLU A N     1 
ATOM   1297 C CA    . GLU A 1 185 ? 5.342  27.617 9.351  1.00 19.06 ? 176 GLU A CA    1 
ATOM   1298 C C     . GLU A 1 185 ? 6.452  28.525 8.831  1.00 21.38 ? 176 GLU A C     1 
ATOM   1299 O O     . GLU A 1 185 ? 6.301  29.177 7.784  1.00 21.93 ? 176 GLU A O     1 
ATOM   1300 C CB    . GLU A 1 185 ? 4.448  28.370 10.357 1.00 20.24 ? 176 GLU A CB    1 
ATOM   1301 C CG    . GLU A 1 185 ? 3.666  29.535 9.741  1.00 26.58 ? 176 GLU A CG    1 
ATOM   1302 C CD    . GLU A 1 185 ? 2.895  30.328 10.786 1.00 36.35 ? 176 GLU A CD    1 
ATOM   1303 O OE1   . GLU A 1 185 ? 2.584  29.749 11.847 1.00 35.67 ? 176 GLU A OE1   1 
ATOM   1304 O OE2   . GLU A 1 185 ? 2.595  31.524 10.548 1.00 36.22 ? 176 GLU A OE2   1 
ATOM   1305 N N     . ALA A 1 186 ? 7.583  28.588 9.551  1.00 18.64 ? 177 ALA A N     1 
ATOM   1306 C CA    . ALA A 1 186 ? 8.736  29.349 9.096  1.00 19.00 ? 177 ALA A CA    1 
ATOM   1307 C C     . ALA A 1 186 ? 9.464  28.671 7.949  1.00 19.52 ? 177 ALA A C     1 
ATOM   1308 O O     . ALA A 1 186 ? 10.395 29.269 7.392  1.00 25.50 ? 177 ALA A O     1 
ATOM   1309 C CB    . ALA A 1 186 ? 9.725  29.581 10.244 1.00 17.61 ? 177 ALA A CB    1 
ATOM   1310 N N     . GLY A 1 187 ? 9.099  27.439 7.601  1.00 17.47 ? 178 GLY A N     1 
ATOM   1311 C CA    . GLY A 1 187 ? 9.748  26.748 6.510  1.00 19.96 ? 178 GLY A CA    1 
ATOM   1312 C C     . GLY A 1 187 ? 10.843 25.788 6.900  1.00 18.29 ? 178 GLY A C     1 
ATOM   1313 O O     . GLY A 1 187 ? 11.420 25.150 6.005  1.00 18.15 ? 178 GLY A O     1 
ATOM   1314 N N     . PHE A 1 188 ? 11.135 25.639 8.203  1.00 16.49 ? 179 PHE A N     1 
ATOM   1315 C CA    . PHE A 1 188 ? 12.119 24.648 8.605  1.00 16.98 ? 179 PHE A CA    1 
ATOM   1316 C C     . PHE A 1 188 ? 11.732 23.279 8.087  1.00 15.55 ? 179 PHE A C     1 
ATOM   1317 O O     . PHE A 1 188 ? 10.549 22.935 7.992  1.00 17.61 ? 179 PHE A O     1 
ATOM   1318 C CB    . PHE A 1 188 ? 12.241 24.571 10.125 1.00 13.96 ? 179 PHE A CB    1 
ATOM   1319 C CG    . PHE A 1 188 ? 13.073 25.681 10.732 1.00 14.53 ? 179 PHE A CG    1 
ATOM   1320 C CD1   . PHE A 1 188 ? 14.465 25.623 10.702 1.00 16.79 ? 179 PHE A CD1   1 
ATOM   1321 C CD2   . PHE A 1 188 ? 12.451 26.757 11.352 1.00 15.39 ? 179 PHE A CD2   1 
ATOM   1322 C CE1   . PHE A 1 188 ? 15.241 26.638 11.272 1.00 15.98 ? 179 PHE A CE1   1 
ATOM   1323 C CE2   . PHE A 1 188 ? 13.213 27.775 11.944 1.00 16.13 ? 179 PHE A CE2   1 
ATOM   1324 C CZ    . PHE A 1 188 ? 14.620 27.721 11.896 1.00 17.97 ? 179 PHE A CZ    1 
ATOM   1325 N N     . ASP A 1 189 ? 12.749 22.479 7.786  1.00 15.06 ? 180 ASP A N     1 
ATOM   1326 C CA    . ASP A 1 189 ? 12.502 21.112 7.340  1.00 16.06 ? 180 ASP A CA    1 
ATOM   1327 C C     . ASP A 1 189 ? 12.056 20.226 8.500  1.00 20.39 ? 180 ASP A C     1 
ATOM   1328 O O     . ASP A 1 189 ? 11.381 19.210 8.284  1.00 18.27 ? 180 ASP A O     1 
ATOM   1329 C CB    . ASP A 1 189 ? 13.773 20.581 6.691  1.00 16.55 ? 180 ASP A CB    1 
ATOM   1330 C CG    . ASP A 1 189 ? 14.151 21.381 5.437  1.00 20.82 ? 180 ASP A CG    1 
ATOM   1331 O OD1   . ASP A 1 189 ? 13.423 21.268 4.434  1.00 23.81 ? 180 ASP A OD1   1 
ATOM   1332 O OD2   . ASP A 1 189 ? 15.124 22.169 5.473  1.00 17.85 ? 180 ASP A OD2   1 
ATOM   1333 N N     . GLY A 1 190 ? 12.415 20.595 9.723  1.00 15.88 ? 181 GLY A N     1 
ATOM   1334 C CA    . GLY A 1 190 ? 12.090 19.782 10.876 1.00 15.66 ? 181 GLY A CA    1 
ATOM   1335 C C     . GLY A 1 190 ? 12.565 20.482 12.131 1.00 16.35 ? 181 GLY A C     1 
ATOM   1336 O O     . GLY A 1 190 ? 13.019 21.628 12.096 1.00 15.54 ? 181 GLY A O     1 
ATOM   1337 N N     . ILE A 1 191 ? 12.469 19.763 13.238 1.00 14.08 ? 182 ILE A N     1 
ATOM   1338 C CA    . ILE A 1 191 ? 12.913 20.281 14.530 1.00 15.04 ? 182 ILE A CA    1 
ATOM   1339 C C     . ILE A 1 191 ? 13.732 19.203 15.211 1.00 14.26 ? 182 ILE A C     1 
ATOM   1340 O O     . ILE A 1 191 ? 13.599 18.013 14.925 1.00 16.20 ? 182 ILE A O     1 
ATOM   1341 C CB    . ILE A 1 191 ? 11.736 20.714 15.436 1.00 14.42 ? 182 ILE A CB    1 
ATOM   1342 C CG1   . ILE A 1 191 ? 10.819 19.533 15.755 1.00 15.79 ? 182 ILE A CG1   1 
ATOM   1343 C CG2   . ILE A 1 191 ? 10.979 21.867 14.760 1.00 16.27 ? 182 ILE A CG2   1 
ATOM   1344 C CD1   . ILE A 1 191 ? 11.159 18.864 17.137 1.00 16.81 ? 182 ILE A CD1   1 
ATOM   1345 N N     . GLU A 1 192 ? 14.593 19.639 16.120 1.00 16.46 ? 183 GLU A N     1 
ATOM   1346 C CA    . GLU A 1 192 ? 15.318 18.747 17.009 1.00 14.67 ? 183 GLU A CA    1 
ATOM   1347 C C     . GLU A 1 192 ? 14.905 19.054 18.448 1.00 14.26 ? 183 GLU A C     1 
ATOM   1348 O O     . GLU A 1 192 ? 14.897 20.220 18.861 1.00 15.95 ? 183 GLU A O     1 
ATOM   1349 C CB    . GLU A 1 192 ? 16.815 18.928 16.837 1.00 14.18 ? 183 GLU A CB    1 
ATOM   1350 C CG    . GLU A 1 192 ? 17.616 18.026 17.788 1.00 18.07 ? 183 GLU A CG    1 
ATOM   1351 C CD    . GLU A 1 192 ? 19.106 18.143 17.606 1.00 17.01 ? 183 GLU A CD    1 
ATOM   1352 O OE1   . GLU A 1 192 ? 19.653 17.421 16.760 1.00 17.29 ? 183 GLU A OE1   1 
ATOM   1353 O OE2   . GLU A 1 192 ? 19.759 18.946 18.313 1.00 17.54 ? 183 GLU A OE2   1 
ATOM   1354 N N     . ILE A 1 193 ? 14.567 18.013 19.205 1.00 13.19 ? 184 ILE A N     1 
ATOM   1355 C CA    . ILE A 1 193 ? 14.305 18.160 20.635 1.00 14.18 ? 184 ILE A CA    1 
ATOM   1356 C C     . ILE A 1 193 ? 15.632 18.181 21.406 1.00 15.20 ? 184 ILE A C     1 
ATOM   1357 O O     . ILE A 1 193 ? 16.411 17.220 21.352 1.00 16.09 ? 184 ILE A O     1 
ATOM   1358 C CB    . ILE A 1 193 ? 13.382 17.035 21.136 1.00 16.49 ? 184 ILE A CB    1 
ATOM   1359 C CG1   . ILE A 1 193 ? 11.975 17.111 20.488 1.00 14.99 ? 184 ILE A CG1   1 
ATOM   1360 C CG2   . ILE A 1 193 ? 13.268 17.094 22.647 1.00 17.10 ? 184 ILE A CG2   1 
ATOM   1361 C CD1   . ILE A 1 193 ? 11.249 18.424 20.739 1.00 17.33 ? 184 ILE A CD1   1 
ATOM   1362 N N     . HIS A 1 194 ? 15.897 19.281 22.123 1.00 15.24 ? 185 HIS A N     1 
ATOM   1363 C CA    . HIS A 1 194 ? 17.096 19.398 22.970 1.00 14.21 ? 185 HIS A CA    1 
ATOM   1364 C C     . HIS A 1 194 ? 16.805 18.681 24.275 1.00 16.16 ? 185 HIS A C     1 
ATOM   1365 O O     . HIS A 1 194 ? 16.185 19.247 25.179 1.00 16.72 ? 185 HIS A O     1 
ATOM   1366 C CB    . HIS A 1 194 ? 17.467 20.864 23.205 1.00 14.48 ? 185 HIS A CB    1 
ATOM   1367 C CG    . HIS A 1 194 ? 18.822 21.064 23.824 1.00 15.79 ? 185 HIS A CG    1 
ATOM   1368 N ND1   . HIS A 1 194 ? 19.491 20.074 24.519 1.00 16.74 ? 185 HIS A ND1   1 
ATOM   1369 C CD2   . HIS A 1 194 ? 19.628 22.156 23.859 1.00 17.04 ? 185 HIS A CD2   1 
ATOM   1370 C CE1   . HIS A 1 194 ? 20.647 20.550 24.959 1.00 15.63 ? 185 HIS A CE1   1 
ATOM   1371 N NE2   . HIS A 1 194 ? 20.750 21.815 24.584 1.00 17.36 ? 185 HIS A NE2   1 
ATOM   1372 N N     . GLY A 1 195 ? 17.295 17.457 24.386 1.00 15.39 ? 186 GLY A N     1 
ATOM   1373 C CA    . GLY A 1 195 ? 17.129 16.661 25.592 1.00 14.27 ? 186 GLY A CA    1 
ATOM   1374 C C     . GLY A 1 195 ? 18.449 16.390 26.294 1.00 16.10 ? 186 GLY A C     1 
ATOM   1375 O O     . GLY A 1 195 ? 18.593 15.368 26.980 1.00 17.58 ? 186 GLY A O     1 
ATOM   1376 N N     . ALA A 1 196 ? 19.421 17.283 26.121 1.00 16.02 ? 187 ALA A N     1 
ATOM   1377 C CA    . ALA A 1 196 ? 20.803 17.061 26.554 1.00 15.47 ? 187 ALA A CA    1 
ATOM   1378 C C     . ALA A 1 196 ? 21.231 18.097 27.599 1.00 15.33 ? 187 ALA A C     1 
ATOM   1379 O O     . ALA A 1 196 ? 20.499 19.044 27.938 1.00 16.84 ? 187 ALA A O     1 
ATOM   1380 C CB    . ALA A 1 196 ? 21.769 17.118 25.354 1.00 14.10 ? 187 ALA A CB    1 
ATOM   1381 N N     . HIS A 1 197 ? 22.452 17.881 28.119 1.00 16.21 ? 188 HIS A N     1 
ATOM   1382 C CA    . HIS A 1 197 ? 23.256 18.901 28.832 1.00 13.99 ? 188 HIS A CA    1 
ATOM   1383 C C     . HIS A 1 197 ? 22.625 19.444 30.116 1.00 15.53 ? 188 HIS A C     1 
ATOM   1384 O O     . HIS A 1 197 ? 22.907 20.586 30.509 1.00 17.35 ? 188 HIS A O     1 
ATOM   1385 C CB    . HIS A 1 197 ? 23.579 20.068 27.907 1.00 17.14 ? 188 HIS A CB    1 
ATOM   1386 C CG    . HIS A 1 197 ? 24.311 19.656 26.668 1.00 17.08 ? 188 HIS A CG    1 
ATOM   1387 N ND1   . HIS A 1 197 ? 24.063 20.237 25.445 1.00 19.78 ? 188 HIS A ND1   1 
ATOM   1388 C CD2   . HIS A 1 197 ? 25.302 18.758 26.464 1.00 20.79 ? 188 HIS A CD2   1 
ATOM   1389 C CE1   . HIS A 1 197 ? 24.852 19.699 24.532 1.00 18.15 ? 188 HIS A CE1   1 
ATOM   1390 N NE2   . HIS A 1 197 ? 25.623 18.806 25.124 1.00 22.18 ? 188 HIS A NE2   1 
ATOM   1391 N N     . GLY A 1 198 ? 21.796 18.665 30.805 1.00 15.70 ? 189 GLY A N     1 
ATOM   1392 C CA    . GLY A 1 198 ? 21.278 19.141 32.081 1.00 15.41 ? 189 GLY A CA    1 
ATOM   1393 C C     . GLY A 1 198 ? 20.168 20.178 32.010 1.00 15.20 ? 189 GLY A C     1 
ATOM   1394 O O     . GLY A 1 198 ? 19.843 20.792 33.047 1.00 16.79 ? 189 GLY A O     1 
ATOM   1395 N N     . TYR A 1 199 ? 19.595 20.414 30.814 1.00 14.96 ? 190 TYR A N     1 
ATOM   1396 C CA    . TYR A 1 199 ? 18.459 21.322 30.662 1.00 11.88 ? 190 TYR A CA    1 
ATOM   1397 C C     . TYR A 1 199 ? 17.160 20.576 31.005 1.00 14.34 ? 190 TYR A C     1 
ATOM   1398 O O     . TYR A 1 199 ? 17.193 19.532 31.657 1.00 17.44 ? 190 TYR A O     1 
ATOM   1399 C CB    . TYR A 1 199 ? 18.514 21.977 29.270 1.00 12.27 ? 190 TYR A CB    1 
ATOM   1400 C CG    . TYR A 1 199 ? 19.755 22.836 29.117 1.00 14.48 ? 190 TYR A CG    1 
ATOM   1401 C CD1   . TYR A 1 199 ? 19.972 23.918 29.978 1.00 14.56 ? 190 TYR A CD1   1 
ATOM   1402 C CD2   . TYR A 1 199 ? 20.736 22.546 28.171 1.00 16.61 ? 190 TYR A CD2   1 
ATOM   1403 C CE1   . TYR A 1 199 ? 21.112 24.698 29.855 1.00 17.39 ? 190 TYR A CE1   1 
ATOM   1404 C CE2   . TYR A 1 199 ? 21.877 23.322 28.053 1.00 21.37 ? 190 TYR A CE2   1 
ATOM   1405 C CZ    . TYR A 1 199 ? 22.047 24.394 28.887 1.00 18.98 ? 190 TYR A CZ    1 
ATOM   1406 O OH    . TYR A 1 199 ? 23.180 25.169 28.781 1.00 24.43 ? 190 TYR A OH    1 
ATOM   1407 N N     . LEU A 1 200 ? 16.000 21.149 30.675 1.00 14.50 ? 191 LEU A N     1 
ATOM   1408 C CA    . LEU A 1 200 ? 14.752 20.711 31.299 1.00 18.49 ? 191 LEU A CA    1 
ATOM   1409 C C     . LEU A 1 200 ? 14.502 19.217 31.121 1.00 15.76 ? 191 LEU A C     1 
ATOM   1410 O O     . LEU A 1 200 ? 14.173 18.518 32.086 1.00 15.07 ? 191 LEU A O     1 
ATOM   1411 C CB    . LEU A 1 200 ? 13.557 21.507 30.764 1.00 17.83 ? 191 LEU A CB    1 
ATOM   1412 C CG    . LEU A 1 200 ? 12.220 21.095 31.411 1.00 14.88 ? 191 LEU A CG    1 
ATOM   1413 C CD1   . LEU A 1 200 ? 12.159 21.407 32.916 1.00 16.48 ? 191 LEU A CD1   1 
ATOM   1414 C CD2   . LEU A 1 200 ? 11.038 21.798 30.667 1.00 14.96 ? 191 LEU A CD2   1 
ATOM   1415 N N     . ILE A 1 201 ? 14.581 18.715 29.888 1.00 15.28 ? 192 ILE A N     1 
ATOM   1416 C CA    . ILE A 1 201 ? 14.310 17.290 29.671 1.00 14.88 ? 192 ILE A CA    1 
ATOM   1417 C C     . ILE A 1 201 ? 15.305 16.435 30.438 1.00 15.10 ? 192 ILE A C     1 
ATOM   1418 O O     . ILE A 1 201 ? 14.933 15.430 31.053 1.00 15.44 ? 192 ILE A O     1 
ATOM   1419 C CB    . ILE A 1 201 ? 14.324 16.971 28.173 1.00 15.19 ? 192 ILE A CB    1 
ATOM   1420 C CG1   . ILE A 1 201 ? 13.087 17.606 27.519 1.00 15.76 ? 192 ILE A CG1   1 
ATOM   1421 C CG2   . ILE A 1 201 ? 14.350 15.453 27.975 1.00 17.88 ? 192 ILE A CG2   1 
ATOM   1422 C CD1   . ILE A 1 201 ? 13.131 17.628 26.017 1.00 16.18 ? 192 ILE A CD1   1 
ATOM   1423 N N     . ASP A 1 202 ? 16.575 16.828 30.434 1.00 15.41 ? 193 ASP A N     1 
ATOM   1424 C CA    . ASP A 1 202 ? 17.590 16.061 31.175 1.00 17.64 ? 193 ASP A CA    1 
ATOM   1425 C C     . ASP A 1 202 ? 17.362 16.136 32.686 1.00 13.69 ? 193 ASP A C     1 
ATOM   1426 O O     . ASP A 1 202 ? 17.772 15.229 33.423 1.00 16.80 ? 193 ASP A O     1 
ATOM   1427 C CB    . ASP A 1 202 ? 18.996 16.587 30.812 1.00 19.92 ? 193 ASP A CB    1 
ATOM   1428 C CG    . ASP A 1 202 ? 20.089 15.496 30.794 1.00 23.70 ? 193 ASP A CG    1 
ATOM   1429 O OD1   . ASP A 1 202 ? 19.788 14.300 30.590 1.00 21.06 ? 193 ASP A OD1   1 
ATOM   1430 O OD2   . ASP A 1 202 ? 21.278 15.854 30.981 1.00 22.81 ? 193 ASP A OD2   1 
ATOM   1431 N N     . GLN A 1 203 ? 16.746 17.221 33.177 1.00 14.05 ? 194 GLN A N     1 
ATOM   1432 C CA    . GLN A 1 203 ? 16.414 17.314 34.597 1.00 15.22 ? 194 GLN A CA    1 
ATOM   1433 C C     . GLN A 1 203 ? 15.357 16.288 35.004 1.00 16.81 ? 194 GLN A C     1 
ATOM   1434 O O     . GLN A 1 203 ? 15.270 15.941 36.196 1.00 16.71 ? 194 GLN A O     1 
ATOM   1435 C CB    . GLN A 1 203 ? 15.945 18.745 34.902 1.00 14.49 ? 194 GLN A CB    1 
ATOM   1436 C CG    . GLN A 1 203 ? 17.063 19.775 34.843 1.00 16.37 ? 194 GLN A CG    1 
ATOM   1437 C CD    . GLN A 1 203 ? 16.563 21.179 34.537 1.00 13.54 ? 194 GLN A CD    1 
ATOM   1438 O OE1   . GLN A 1 203 ? 15.472 21.579 34.962 1.00 15.99 ? 194 GLN A OE1   1 
ATOM   1439 N NE2   . GLN A 1 203 ? 17.354 21.925 33.776 1.00 14.24 ? 194 GLN A NE2   1 
ATOM   1440 N N     . PHE A 1 204 ? 14.574 15.778 34.039 1.00 14.40 ? 195 PHE A N     1 
ATOM   1441 C CA    . PHE A 1 204 ? 13.668 14.657 34.279 1.00 14.96 ? 195 PHE A CA    1 
ATOM   1442 C C     . PHE A 1 204 ? 14.360 13.310 34.080 1.00 14.68 ? 195 PHE A C     1 
ATOM   1443 O O     . PHE A 1 204 ? 14.097 12.368 34.846 1.00 14.88 ? 195 PHE A O     1 
ATOM   1444 C CB    . PHE A 1 204 ? 12.419 14.768 33.379 1.00 13.16 ? 195 PHE A CB    1 
ATOM   1445 C CG    . PHE A 1 204 ? 11.374 15.727 33.900 1.00 15.35 ? 195 PHE A CG    1 
ATOM   1446 C CD1   . PHE A 1 204 ? 11.409 17.079 33.560 1.00 15.66 ? 195 PHE A CD1   1 
ATOM   1447 C CD2   . PHE A 1 204 ? 10.364 15.275 34.768 1.00 17.86 ? 195 PHE A CD2   1 
ATOM   1448 C CE1   . PHE A 1 204 ? 10.452 17.961 34.061 1.00 18.83 ? 195 PHE A CE1   1 
ATOM   1449 C CE2   . PHE A 1 204 ? 9.412  16.148 35.294 1.00 20.36 ? 195 PHE A CE2   1 
ATOM   1450 C CZ    . PHE A 1 204 ? 9.454  17.506 34.929 1.00 18.26 ? 195 PHE A CZ    1 
ATOM   1451 N N     . LEU A 1 205 ? 15.262 13.213 33.103 1.00 15.75 ? 196 LEU A N     1 
ATOM   1452 C CA    . LEU A 1 205 ? 15.885 11.928 32.777 1.00 14.30 ? 196 LEU A CA    1 
ATOM   1453 C C     . LEU A 1 205 ? 16.834 11.457 33.868 1.00 18.27 ? 196 LEU A C     1 
ATOM   1454 O O     . LEU A 1 205 ? 16.891 10.259 34.166 1.00 19.69 ? 196 LEU A O     1 
ATOM   1455 C CB    . LEU A 1 205 ? 16.683 12.040 31.488 1.00 13.71 ? 196 LEU A CB    1 
ATOM   1456 C CG    . LEU A 1 205 ? 15.865 12.140 30.207 1.00 16.01 ? 196 LEU A CG    1 
ATOM   1457 C CD1   . LEU A 1 205 ? 16.785 12.442 29.038 1.00 17.98 ? 196 LEU A CD1   1 
ATOM   1458 C CD2   . LEU A 1 205 ? 15.079 10.845 29.943 1.00 20.85 ? 196 LEU A CD2   1 
ATOM   1459 N N     . LYS A 1 206 ? 17.634 12.364 34.406 1.00 15.65 ? 197 LYS A N     1 
ATOM   1460 C CA    . LYS A 1 206 ? 18.818 12.003 35.188 1.00 15.35 ? 197 LYS A CA    1 
ATOM   1461 C C     . LYS A 1 206 ? 18.432 11.780 36.653 1.00 18.95 ? 197 LYS A C     1 
ATOM   1462 O O     . LYS A 1 206 ? 17.845 12.667 37.291 1.00 17.71 ? 197 LYS A O     1 
ATOM   1463 C CB    . LYS A 1 206 ? 19.884 13.098 35.059 1.00 16.65 ? 197 LYS A CB    1 
ATOM   1464 C CG    . LYS A 1 206 ? 20.481 13.272 33.633 1.00 16.86 ? 197 LYS A CG    1 
ATOM   1465 C CD    . LYS A 1 206 ? 21.363 12.108 33.262 1.00 17.23 ? 197 LYS A CD    1 
ATOM   1466 C CE    . LYS A 1 206 ? 21.724 12.082 31.760 1.00 17.65 ? 197 LYS A CE    1 
ATOM   1467 N NZ    . LYS A 1 206 ? 22.638 13.175 31.401 1.00 18.91 ? 197 LYS A NZ    1 
ATOM   1468 N N     . ASP A 1 207 ? 18.762 10.605 37.194 1.00 17.87 ? 198 ASP A N     1 
ATOM   1469 C CA    . ASP A 1 207 ? 18.403 10.380 38.593 1.00 19.78 ? 198 ASP A CA    1 
ATOM   1470 C C     . ASP A 1 207 ? 19.264 11.190 39.552 1.00 21.90 ? 198 ASP A C     1 
ATOM   1471 O O     . ASP A 1 207 ? 18.923 11.283 40.735 1.00 22.75 ? 198 ASP A O     1 
ATOM   1472 C CB    . ASP A 1 207 ? 18.395 8.872  38.911 1.00 17.92 ? 198 ASP A CB    1 
ATOM   1473 C CG    . ASP A 1 207 ? 19.772 8.201  38.883 1.00 22.39 ? 198 ASP A CG    1 
ATOM   1474 O OD1   . ASP A 1 207 ? 20.828 8.847  38.692 1.00 26.33 ? 198 ASP A OD1   1 
ATOM   1475 O OD2   . ASP A 1 207 ? 19.774 6.954  39.101 1.00 24.00 ? 198 ASP A OD2   1 
ATOM   1476 N N     . GLY A 1 208 ? 20.314 11.848 39.062 1.00 17.56 ? 199 GLY A N     1 
ATOM   1477 C CA    . GLY A 1 208 ? 21.048 12.808 39.881 1.00 20.40 ? 199 GLY A CA    1 
ATOM   1478 C C     . GLY A 1 208 ? 20.370 14.150 40.066 1.00 23.48 ? 199 GLY A C     1 
ATOM   1479 O O     . GLY A 1 208 ? 20.816 14.960 40.899 1.00 23.73 ? 199 GLY A O     1 
ATOM   1480 N N     . ILE A 1 209 ? 19.297 14.403 39.312 1.00 18.77 ? 200 ILE A N     1 
ATOM   1481 C CA    . ILE A 1 209 ? 18.509 15.623 39.427 1.00 15.20 ? 200 ILE A CA    1 
ATOM   1482 C C     . ILE A 1 209 ? 17.074 15.332 39.830 1.00 16.46 ? 200 ILE A C     1 
ATOM   1483 O O     . ILE A 1 209 ? 16.504 16.024 40.682 1.00 17.46 ? 200 ILE A O     1 
ATOM   1484 C CB    . ILE A 1 209 ? 18.517 16.414 38.093 1.00 16.71 ? 200 ILE A CB    1 
ATOM   1485 C CG1   . ILE A 1 209 ? 19.940 16.795 37.670 1.00 18.66 ? 200 ILE A CG1   1 
ATOM   1486 C CG2   . ILE A 1 209 ? 17.573 17.643 38.220 1.00 16.14 ? 200 ILE A CG2   1 
ATOM   1487 C CD1   . ILE A 1 209 ? 20.026 17.328 36.241 1.00 19.87 ? 200 ILE A CD1   1 
ATOM   1488 N N     . ASN A 1 210 ? 16.458 14.324 39.216 1.00 16.31 ? 201 ASN A N     1 
ATOM   1489 C CA    . ASN A 1 210 ? 15.031 14.080 39.395 1.00 15.32 ? 201 ASN A CA    1 
ATOM   1490 C C     . ASN A 1 210 ? 14.826 13.406 40.744 1.00 18.38 ? 201 ASN A C     1 
ATOM   1491 O O     . ASN A 1 210 ? 15.114 12.210 40.888 1.00 21.52 ? 201 ASN A O     1 
ATOM   1492 C CB    . ASN A 1 210 ? 14.526 13.207 38.250 1.00 17.01 ? 201 ASN A CB    1 
ATOM   1493 C CG    . ASN A 1 210 ? 13.039 13.001 38.275 1.00 19.97 ? 201 ASN A CG    1 
ATOM   1494 O OD1   . ASN A 1 210 ? 12.386 13.176 39.291 1.00 19.31 ? 201 ASN A OD1   1 
ATOM   1495 N ND2   . ASN A 1 210 ? 12.490 12.577 37.140 1.00 15.61 ? 201 ASN A ND2   1 
ATOM   1496 N N     . ASP A 1 211 ? 14.328 14.170 41.721 1.00 14.58 ? 202 ASP A N     1 
ATOM   1497 C CA    . ASP A 1 211 ? 13.972 13.637 43.041 1.00 17.00 ? 202 ASP A CA    1 
ATOM   1498 C C     . ASP A 1 211 ? 12.457 13.554 43.239 1.00 20.71 ? 202 ASP A C     1 
ATOM   1499 O O     . ASP A 1 211 ? 11.988 13.570 44.391 1.00 19.70 ? 202 ASP A O     1 
ATOM   1500 C CB    . ASP A 1 211 ? 14.510 14.497 44.191 1.00 21.87 ? 202 ASP A CB    1 
ATOM   1501 C CG    . ASP A 1 211 ? 14.230 15.989 44.023 1.00 24.58 ? 202 ASP A CG    1 
ATOM   1502 O OD1   . ASP A 1 211 ? 13.527 16.414 43.076 1.00 21.91 ? 202 ASP A OD1   1 
ATOM   1503 O OD2   . ASP A 1 211 ? 14.543 16.740 44.994 1.00 24.60 ? 202 ASP A OD2   1 
ATOM   1504 N N     . ARG A 1 212 ? 11.680 13.524 42.158 1.00 18.14 ? 203 ARG A N     1 
ATOM   1505 C CA    . ARG A 1 212 ? 10.228 13.464 42.254 1.00 18.77 ? 203 ARG A CA    1 
ATOM   1506 C C     . ARG A 1 212 ? 9.770  12.134 42.818 1.00 19.02 ? 203 ARG A C     1 
ATOM   1507 O O     . ARG A 1 212 ? 10.378 11.085 42.570 1.00 20.85 ? 203 ARG A O     1 
ATOM   1508 C CB    . ARG A 1 212 ? 9.577  13.638 40.880 1.00 15.70 ? 203 ARG A CB    1 
ATOM   1509 C CG    . ARG A 1 212 ? 9.889  14.956 40.243 1.00 15.94 ? 203 ARG A CG    1 
ATOM   1510 C CD    . ARG A 1 212 ? 9.229  15.034 38.851 1.00 15.56 ? 203 ARG A CD    1 
ATOM   1511 N NE    . ARG A 1 212 ? 7.793  15.275 38.967 1.00 17.85 ? 203 ARG A NE    1 
ATOM   1512 C CZ    . ARG A 1 212 ? 7.239  16.481 38.936 1.00 16.76 ? 203 ARG A CZ    1 
ATOM   1513 N NH1   . ARG A 1 212 ? 7.980  17.591 38.869 1.00 17.55 ? 203 ARG A NH1   1 
ATOM   1514 N NH2   . ARG A 1 212 ? 5.916  16.582 38.925 1.00 16.72 ? 203 ARG A NH2   1 
ATOM   1515 N N     . THR A 1 213 ? 8.665  12.184 43.564 1.00 21.61 ? 204 THR A N     1 
ATOM   1516 C CA    . THR A 1 213 ? 8.049  10.961 44.060 1.00 21.32 ? 204 THR A CA    1 
ATOM   1517 C C     . THR A 1 213 ? 6.685  10.701 43.427 1.00 24.22 ? 204 THR A C     1 
ATOM   1518 O O     . THR A 1 213 ? 5.937  9.859  43.932 1.00 27.33 ? 204 THR A O     1 
ATOM   1519 C CB    . THR A 1 213 ? 7.950  10.996 45.588 1.00 23.54 ? 204 THR A CB    1 
ATOM   1520 O OG1   . THR A 1 213 ? 7.212  12.148 45.997 1.00 26.31 ? 204 THR A OG1   1 
ATOM   1521 C CG2   . THR A 1 213 ? 9.354  11.073 46.193 1.00 30.02 ? 204 THR A CG2   1 
ATOM   1522 N N     . ASP A 1 214 ? 6.349  11.383 42.321 1.00 20.06 ? 205 ASP A N     1 
ATOM   1523 C CA    . ASP A 1 214 ? 5.134  11.077 41.579 1.00 21.09 ? 205 ASP A CA    1 
ATOM   1524 C C     . ASP A 1 214 ? 5.481  10.227 40.351 1.00 18.24 ? 205 ASP A C     1 
ATOM   1525 O O     . ASP A 1 214 ? 6.559  9.620  40.282 1.00 19.06 ? 205 ASP A O     1 
ATOM   1526 C CB    . ASP A 1 214 ? 4.371  12.366 41.208 1.00 19.27 ? 205 ASP A CB    1 
ATOM   1527 C CG    . ASP A 1 214 ? 5.107  13.250 40.182 1.00 22.90 ? 205 ASP A CG    1 
ATOM   1528 O OD1   . ASP A 1 214 ? 6.224  12.914 39.728 1.00 18.40 ? 205 ASP A OD1   1 
ATOM   1529 O OD2   . ASP A 1 214 ? 4.555  14.331 39.852 1.00 20.31 ? 205 ASP A OD2   1 
ATOM   1530 N N     . GLU A 1 215 ? 4.572  10.173 39.375 1.00 18.92 ? 206 GLU A N     1 
ATOM   1531 C CA    . GLU A 1 215 ? 4.754  9.231  38.284 1.00 18.70 ? 206 GLU A CA    1 
ATOM   1532 C C     . GLU A 1 215 ? 5.763  9.712  37.248 1.00 19.17 ? 206 GLU A C     1 
ATOM   1533 O O     . GLU A 1 215 ? 5.996  9.013  36.254 1.00 19.79 ? 206 GLU A O     1 
ATOM   1534 C CB    . GLU A 1 215 ? 3.404  8.917  37.628 1.00 19.97 ? 206 GLU A CB    1 
ATOM   1535 C CG    . GLU A 1 215 ? 2.889  10.012 36.729 1.00 22.77 ? 206 GLU A CG    1 
ATOM   1536 C CD    . GLU A 1 215 ? 1.981  11.002 37.451 1.00 24.06 ? 206 GLU A CD    1 
ATOM   1537 O OE1   . GLU A 1 215 ? 2.073  11.157 38.687 1.00 26.99 ? 206 GLU A OE1   1 
ATOM   1538 O OE2   . GLU A 1 215 ? 1.189  11.668 36.734 1.00 26.62 ? 206 GLU A OE2   1 
ATOM   1539 N N     . TYR A 1 216 ? 6.403  10.860 37.481 1.00 17.06 ? 207 TYR A N     1 
ATOM   1540 C CA    . TYR A 1 216 ? 7.480  11.347 36.622 1.00 17.91 ? 207 TYR A CA    1 
ATOM   1541 C C     . TYR A 1 216 ? 8.856  11.187 37.259 1.00 19.22 ? 207 TYR A C     1 
ATOM   1542 O O     . TYR A 1 216 ? 9.837  11.691 36.714 1.00 18.52 ? 207 TYR A O     1 
ATOM   1543 C CB    . TYR A 1 216 ? 7.253  12.820 36.243 1.00 18.28 ? 207 TYR A CB    1 
ATOM   1544 C CG    . TYR A 1 216 ? 6.189  13.017 35.193 1.00 15.19 ? 207 TYR A CG    1 
ATOM   1545 C CD1   . TYR A 1 216 ? 4.847  13.061 35.552 1.00 17.25 ? 207 TYR A CD1   1 
ATOM   1546 C CD2   . TYR A 1 216 ? 6.527  13.148 33.845 1.00 14.64 ? 207 TYR A CD2   1 
ATOM   1547 C CE1   . TYR A 1 216 ? 3.852  13.233 34.607 1.00 19.18 ? 207 TYR A CE1   1 
ATOM   1548 C CE2   . TYR A 1 216 ? 5.521  13.326 32.876 1.00 18.17 ? 207 TYR A CE2   1 
ATOM   1549 C CZ    . TYR A 1 216 ? 4.194  13.378 33.276 1.00 19.75 ? 207 TYR A CZ    1 
ATOM   1550 O OH    . TYR A 1 216 ? 3.179  13.561 32.354 1.00 19.85 ? 207 TYR A OH    1 
ATOM   1551 N N     . GLY A 1 217 ? 8.951  10.473 38.390 1.00 18.30 ? 208 GLY A N     1 
ATOM   1552 C CA    . GLY A 1 217 ? 10.228 10.248 39.038 1.00 21.29 ? 208 GLY A CA    1 
ATOM   1553 C C     . GLY A 1 217 ? 10.358 8.812  39.503 1.00 19.24 ? 208 GLY A C     1 
ATOM   1554 O O     . GLY A 1 217 ? 9.387  8.047  39.509 1.00 20.12 ? 208 GLY A O     1 
ATOM   1555 N N     . GLY A 1 218 ? 11.588 8.450  39.872 1.00 20.31 ? 209 GLY A N     1 
ATOM   1556 C CA    . GLY A 1 218 ? 11.817 7.117  40.423 1.00 20.91 ? 209 GLY A CA    1 
ATOM   1557 C C     . GLY A 1 218 ? 12.341 6.178  39.362 1.00 19.24 ? 209 GLY A C     1 
ATOM   1558 O O     . GLY A 1 218 ? 13.506 6.277  38.970 1.00 21.60 ? 209 GLY A O     1 
ATOM   1559 N N     . SER A 1 219 ? 11.472 5.306  38.856 1.00 17.56 ? 210 SER A N     1 
ATOM   1560 C CA    . SER A 1 219 ? 11.863 4.279  37.904 1.00 21.03 ? 210 SER A CA    1 
ATOM   1561 C C     . SER A 1 219 ? 12.340 4.879  36.581 1.00 18.66 ? 210 SER A C     1 
ATOM   1562 O O     . SER A 1 219 ? 12.034 6.028  36.237 1.00 19.94 ? 210 SER A O     1 
ATOM   1563 C CB    . SER A 1 219 ? 10.681 3.351  37.647 1.00 22.50 ? 210 SER A CB    1 
ATOM   1564 O OG    . SER A 1 219 ? 9.654  4.031  36.917 1.00 20.66 ? 210 SER A OG    1 
ATOM   1565 N N     . LEU A 1 220 ? 13.093 4.077  35.822 1.00 18.17 ? 211 LEU A N     1 
ATOM   1566 C CA    . LEU A 1 220 ? 13.460 4.461  34.459 1.00 19.19 ? 211 LEU A CA    1 
ATOM   1567 C C     . LEU A 1 220 ? 12.237 4.856  33.653 1.00 20.72 ? 211 LEU A C     1 
ATOM   1568 O O     . LEU A 1 220 ? 12.240 5.887  32.966 1.00 20.20 ? 211 LEU A O     1 
ATOM   1569 C CB    . LEU A 1 220 ? 14.186 3.312  33.758 1.00 22.36 ? 211 LEU A CB    1 
ATOM   1570 C CG    . LEU A 1 220 ? 15.658 3.120  34.081 1.00 22.15 ? 211 LEU A CG    1 
ATOM   1571 C CD1   . LEU A 1 220 ? 16.107 1.753  33.535 1.00 25.51 ? 211 LEU A CD1   1 
ATOM   1572 C CD2   . LEU A 1 220 ? 16.483 4.209  33.458 1.00 20.67 ? 211 LEU A CD2   1 
ATOM   1573 N N     . ALA A 1 221 ? 11.188 4.024  33.688 1.00 17.84 ? 212 ALA A N     1 
ATOM   1574 C CA    . ALA A 1 221 ? 9.989  4.343  32.924 1.00 17.88 ? 212 ALA A CA    1 
ATOM   1575 C C     . ALA A 1 221 ? 9.436  5.705  33.307 1.00 18.41 ? 212 ALA A C     1 
ATOM   1576 O O     . ALA A 1 221 ? 9.052  6.495  32.429 1.00 20.40 ? 212 ALA A O     1 
ATOM   1577 C CB    . ALA A 1 221 ? 8.929  3.265  33.116 1.00 21.36 ? 212 ALA A CB    1 
ATOM   1578 N N     . ASN A 1 222 ? 9.397  6.006  34.606 1.00 18.00 ? 213 ASN A N     1 
ATOM   1579 C CA    . ASN A 1 222 ? 8.844  7.281  35.041 1.00 16.67 ? 213 ASN A CA    1 
ATOM   1580 C C     . ASN A 1 222 ? 9.728  8.433  34.589 1.00 16.36 ? 213 ASN A C     1 
ATOM   1581 O O     . ASN A 1 222 ? 9.226  9.475  34.142 1.00 17.77 ? 213 ASN A O     1 
ATOM   1582 C CB    . ASN A 1 222 ? 8.681  7.283  36.569 1.00 17.91 ? 213 ASN A CB    1 
ATOM   1583 C CG    . ASN A 1 222 ? 7.483  6.469  37.022 1.00 20.33 ? 213 ASN A CG    1 
ATOM   1584 O OD1   . ASN A 1 222 ? 6.787  5.865  36.203 1.00 21.36 ? 213 ASN A OD1   1 
ATOM   1585 N ND2   . ASN A 1 222 ? 7.218  6.477  38.332 1.00 20.03 ? 213 ASN A ND2   1 
ATOM   1586 N N     . ARG A 1 223 ? 11.042 8.283  34.745 1.00 16.52 ? 214 ARG A N     1 
ATOM   1587 C CA    . ARG A 1 223 ? 11.956 9.335  34.330 1.00 16.48 ? 214 ARG A CA    1 
ATOM   1588 C C     . ARG A 1 223 ? 11.944 9.562  32.830 1.00 17.55 ? 214 ARG A C     1 
ATOM   1589 O O     . ARG A 1 223 ? 12.255 10.676 32.387 1.00 17.15 ? 214 ARG A O     1 
ATOM   1590 C CB    . ARG A 1 223 ? 13.372 9.031  34.800 1.00 17.97 ? 214 ARG A CB    1 
ATOM   1591 C CG    . ARG A 1 223 ? 13.390 9.101  36.316 1.00 16.98 ? 214 ARG A CG    1 
ATOM   1592 C CD    . ARG A 1 223 ? 14.744 9.013  36.965 1.00 20.21 ? 214 ARG A CD    1 
ATOM   1593 N NE    . ARG A 1 223 ? 15.842 8.680  36.089 1.00 29.75 ? 214 ARG A NE    1 
ATOM   1594 C CZ    . ARG A 1 223 ? 16.492 7.529  36.134 1.00 26.17 ? 214 ARG A CZ    1 
ATOM   1595 N NH1   . ARG A 1 223 ? 16.034 6.505  36.834 1.00 26.86 ? 214 ARG A NH1   1 
ATOM   1596 N NH2   . ARG A 1 223 ? 17.611 7.392  35.436 1.00 35.48 ? 214 ARG A NH2   1 
ATOM   1597 N N     . CYS A 1 224 ? 11.566 8.561  32.043 1.00 16.71 ? 215 CYS A N     1 
ATOM   1598 C CA    . CYS A 1 224 ? 11.497 8.723  30.590 1.00 15.90 ? 215 CYS A CA    1 
ATOM   1599 C C     . CYS A 1 224 ? 10.149 9.243  30.106 1.00 15.28 ? 215 CYS A C     1 
ATOM   1600 O O     . CYS A 1 224 ? 9.999  9.498  28.907 1.00 17.85 ? 215 CYS A O     1 
ATOM   1601 C CB    . CYS A 1 224 ? 11.802 7.400  29.891 1.00 18.29 ? 215 CYS A CB    1 
ATOM   1602 S SG    . CYS A 1 224 ? 13.521 6.939  30.025 1.00 22.18 ? 215 CYS A SG    1 
ATOM   1603 N N     . LYS A 1 225 ? 9.177  9.429  31.007 1.00 15.91 ? 216 LYS A N     1 
ATOM   1604 C CA    . LYS A 1 225 ? 7.844  9.850  30.593 1.00 15.82 ? 216 LYS A CA    1 
ATOM   1605 C C     . LYS A 1 225 ? 7.882  11.223 29.923 1.00 17.10 ? 216 LYS A C     1 
ATOM   1606 O O     . LYS A 1 225 ? 7.262  11.437 28.874 1.00 17.02 ? 216 LYS A O     1 
ATOM   1607 C CB    . LYS A 1 225 ? 6.932  9.860  31.816 1.00 18.51 ? 216 LYS A CB    1 
ATOM   1608 C CG    . LYS A 1 225 ? 5.488  9.511  31.624 1.00 35.19 ? 216 LYS A CG    1 
ATOM   1609 C CD    . LYS A 1 225 ? 4.821  9.220  33.002 1.00 26.16 ? 216 LYS A CD    1 
ATOM   1610 C CE    . LYS A 1 225 ? 4.550  7.720  33.178 1.00 33.50 ? 216 LYS A CE    1 
ATOM   1611 N NZ    . LYS A 1 225 ? 4.562  7.262  34.596 1.00 29.45 ? 216 LYS A NZ    1 
ATOM   1612 N N     . PHE A 1 226 ? 8.573  12.190 30.535 1.00 16.23 ? 217 PHE A N     1 
ATOM   1613 C CA    . PHE A 1 226 ? 8.546  13.540 29.966 1.00 16.17 ? 217 PHE A CA    1 
ATOM   1614 C C     . PHE A 1 226 ? 9.105  13.572 28.535 1.00 19.21 ? 217 PHE A C     1 
ATOM   1615 O O     . PHE A 1 226 ? 8.465  14.122 27.629 1.00 18.30 ? 217 PHE A O     1 
ATOM   1616 C CB    . PHE A 1 226 ? 9.293  14.521 30.858 1.00 15.22 ? 217 PHE A CB    1 
ATOM   1617 C CG    . PHE A 1 226 ? 9.210  15.952 30.377 1.00 16.91 ? 217 PHE A CG    1 
ATOM   1618 C CD1   . PHE A 1 226 ? 7.974  16.557 30.141 1.00 21.45 ? 217 PHE A CD1   1 
ATOM   1619 C CD2   . PHE A 1 226 ? 10.354 16.678 30.135 1.00 22.39 ? 217 PHE A CD2   1 
ATOM   1620 C CE1   . PHE A 1 226 ? 7.897  17.874 29.718 1.00 23.54 ? 217 PHE A CE1   1 
ATOM   1621 C CE2   . PHE A 1 226 ? 10.280 17.980 29.700 1.00 19.61 ? 217 PHE A CE2   1 
ATOM   1622 C CZ    . PHE A 1 226 ? 9.053  18.584 29.509 1.00 18.19 ? 217 PHE A CZ    1 
ATOM   1623 N N     . ILE A 1 227 ? 10.290 12.998 28.302 1.00 16.07 ? 218 ILE A N     1 
ATOM   1624 C CA    . ILE A 1 227 ? 10.815 13.049 26.932 1.00 14.55 ? 218 ILE A CA    1 
ATOM   1625 C C     . ILE A 1 227 ? 9.912  12.277 25.974 1.00 16.74 ? 218 ILE A C     1 
ATOM   1626 O O     . ILE A 1 227 ? 9.721  12.694 24.828 1.00 17.29 ? 218 ILE A O     1 
ATOM   1627 C CB    . ILE A 1 227 ? 12.275 12.559 26.847 1.00 16.47 ? 218 ILE A CB    1 
ATOM   1628 C CG1   . ILE A 1 227 ? 12.856 12.926 25.474 1.00 15.18 ? 218 ILE A CG1   1 
ATOM   1629 C CG2   . ILE A 1 227 ? 12.376 11.044 27.078 1.00 17.19 ? 218 ILE A CG2   1 
ATOM   1630 C CD1   . ILE A 1 227 ? 14.338 12.575 25.346 1.00 16.81 ? 218 ILE A CD1   1 
ATOM   1631 N N     . THR A 1 228 ? 9.290  11.189 26.439 1.00 18.20 ? 219 THR A N     1 
ATOM   1632 C CA    . THR A 1 228 ? 8.381  10.448 25.569 1.00 16.10 ? 219 THR A CA    1 
ATOM   1633 C C     . THR A 1 228 ? 7.192  11.311 25.172 1.00 17.58 ? 219 THR A C     1 
ATOM   1634 O O     . THR A 1 228 ? 6.801  11.349 23.992 1.00 18.49 ? 219 THR A O     1 
ATOM   1635 C CB    . THR A 1 228 ? 7.886  9.180  26.263 1.00 17.47 ? 219 THR A CB    1 
ATOM   1636 O OG1   . THR A 1 228 ? 9.006  8.360  26.629 1.00 18.45 ? 219 THR A OG1   1 
ATOM   1637 C CG2   . THR A 1 228 ? 7.008  8.370  25.289 1.00 20.56 ? 219 THR A CG2   1 
ATOM   1638 N N     . GLN A 1 229 ? 6.639  12.054 26.140 1.00 15.68 ? 220 GLN A N     1 
ATOM   1639 C CA    . GLN A 1 229 ? 5.462  12.862 25.854 1.00 15.49 ? 220 GLN A CA    1 
ATOM   1640 C C     . GLN A 1 229 ? 5.807  14.048 24.960 1.00 18.33 ? 220 GLN A C     1 
ATOM   1641 O O     . GLN A 1 229 ? 4.993  14.454 24.120 1.00 17.36 ? 220 GLN A O     1 
ATOM   1642 C CB    . GLN A 1 229 ? 4.828  13.350 27.159 1.00 18.32 ? 220 GLN A CB    1 
ATOM   1643 C CG    . GLN A 1 229 ? 4.044  12.226 27.819 1.00 17.48 ? 220 GLN A CG    1 
ATOM   1644 C CD    . GLN A 1 229 ? 3.801  12.467 29.288 1.00 20.28 ? 220 GLN A CD    1 
ATOM   1645 O OE1   . GLN A 1 229 ? 3.388  11.568 30.017 1.00 33.97 ? 220 GLN A OE1   1 
ATOM   1646 N NE2   . GLN A 1 229 ? 3.994  13.708 29.715 1.00 18.65 ? 220 GLN A NE2   1 
ATOM   1647 N N     . VAL A 1 230 ? 7.000  14.635 25.140 1.00 15.40 ? 221 VAL A N     1 
ATOM   1648 C CA    . VAL A 1 230 ? 7.426  15.731 24.274 1.00 15.32 ? 221 VAL A CA    1 
ATOM   1649 C C     . VAL A 1 230 ? 7.588  15.229 22.849 1.00 15.04 ? 221 VAL A C     1 
ATOM   1650 O O     . VAL A 1 230 ? 7.085  15.838 21.890 1.00 15.69 ? 221 VAL A O     1 
ATOM   1651 C CB    . VAL A 1 230 ? 8.739  16.346 24.782 1.00 15.05 ? 221 VAL A CB    1 
ATOM   1652 C CG1   . VAL A 1 230 ? 9.341  17.303 23.741 1.00 15.33 ? 221 VAL A CG1   1 
ATOM   1653 C CG2   . VAL A 1 230 ? 8.529  17.061 26.110 1.00 15.09 ? 221 VAL A CG2   1 
ATOM   1654 N N     . VAL A 1 231 ? 8.314  14.119 22.687 1.00 15.31 ? 222 VAL A N     1 
ATOM   1655 C CA    . VAL A 1 231 ? 8.534  13.602 21.335 1.00 15.06 ? 222 VAL A CA    1 
ATOM   1656 C C     . VAL A 1 231 ? 7.206  13.201 20.707 1.00 18.46 ? 222 VAL A C     1 
ATOM   1657 O O     . VAL A 1 231 ? 6.927  13.541 19.550 1.00 17.67 ? 222 VAL A O     1 
ATOM   1658 C CB    . VAL A 1 231 ? 9.520  12.422 21.369 1.00 14.39 ? 222 VAL A CB    1 
ATOM   1659 C CG1   . VAL A 1 231 ? 9.621  11.761 19.959 1.00 18.08 ? 222 VAL A CG1   1 
ATOM   1660 C CG2   . VAL A 1 231 ? 10.862 12.911 21.834 1.00 17.32 ? 222 VAL A CG2   1 
ATOM   1661 N N     . GLN A 1 232 ? 6.344  12.515 21.466 1.00 18.20 ? 223 GLN A N     1 
ATOM   1662 C CA    . GLN A 1 232 ? 5.069  12.090 20.885 1.00 20.74 ? 223 GLN A CA    1 
ATOM   1663 C C     . GLN A 1 232 ? 4.241  13.288 20.422 1.00 22.58 ? 223 GLN A C     1 
ATOM   1664 O O     . GLN A 1 232 ? 3.639  13.249 19.337 1.00 19.73 ? 223 GLN A O     1 
ATOM   1665 C CB    . GLN A 1 232 ? 4.271  11.257 21.885 1.00 22.44 ? 223 GLN A CB    1 
ATOM   1666 C CG    . GLN A 1 232 ? 2.945  10.767 21.309 1.00 23.88 ? 223 GLN A CG    1 
ATOM   1667 C CD    . GLN A 1 232 ? 3.131  9.924  20.062 1.00 34.38 ? 223 GLN A CD    1 
ATOM   1668 O OE1   . GLN A 1 232 ? 3.634  8.803  20.139 1.00 29.99 ? 223 GLN A OE1   1 
ATOM   1669 N NE2   . GLN A 1 232 ? 2.715  10.454 18.903 1.00 31.04 ? 223 GLN A NE2   1 
ATOM   1670 N N     . ALA A 1 233 ? 4.214  14.367 21.227 1.00 18.67 ? 224 ALA A N     1 
ATOM   1671 C CA    . ALA A 1 233 ? 3.434  15.543 20.856 1.00 17.18 ? 224 ALA A CA    1 
ATOM   1672 C C     . ALA A 1 233 ? 3.933  16.170 19.552 1.00 20.58 ? 224 ALA A C     1 
ATOM   1673 O O     . ALA A 1 233 ? 3.124  16.547 18.691 1.00 19.89 ? 224 ALA A O     1 
ATOM   1674 C CB    . ALA A 1 233 ? 3.444  16.574 21.989 1.00 18.45 ? 224 ALA A CB    1 
ATOM   1675 N N     . VAL A 1 234 ? 5.254  16.289 19.382 1.00 18.30 ? 225 VAL A N     1 
ATOM   1676 C CA    . VAL A 1 234 ? 5.737  16.950 18.178 1.00 16.39 ? 225 VAL A CA    1 
ATOM   1677 C C     . VAL A 1 234 ? 5.589  16.022 16.976 1.00 19.50 ? 225 VAL A C     1 
ATOM   1678 O O     . VAL A 1 234 ? 5.324  16.494 15.869 1.00 18.26 ? 225 VAL A O     1 
ATOM   1679 C CB    . VAL A 1 234 ? 7.175  17.476 18.323 1.00 18.79 ? 225 VAL A CB    1 
ATOM   1680 C CG1   . VAL A 1 234 ? 7.246  18.579 19.415 1.00 17.34 ? 225 VAL A CG1   1 
ATOM   1681 C CG2   . VAL A 1 234 ? 8.204  16.362 18.591 1.00 19.68 ? 225 VAL A CG2   1 
ATOM   1682 N N     . VAL A 1 235 ? 5.754  14.713 17.180 1.00 17.31 ? 226 VAL A N     1 
ATOM   1683 C CA    . VAL A 1 235 ? 5.490  13.720 16.138 1.00 18.00 ? 226 VAL A CA    1 
ATOM   1684 C C     . VAL A 1 235 ? 4.062  13.833 15.627 1.00 19.83 ? 226 VAL A C     1 
ATOM   1685 O O     . VAL A 1 235 ? 3.817  13.839 14.413 1.00 21.32 ? 226 VAL A O     1 
ATOM   1686 C CB    . VAL A 1 235 ? 5.758  12.297 16.667 1.00 16.59 ? 226 VAL A CB    1 
ATOM   1687 C CG1   . VAL A 1 235 ? 5.135  11.253 15.703 1.00 20.81 ? 226 VAL A CG1   1 
ATOM   1688 C CG2   . VAL A 1 235 ? 7.238  12.037 16.834 1.00 17.17 ? 226 VAL A CG2   1 
ATOM   1689 N N     . SER A 1 236 ? 3.092  13.869 16.547 1.00 17.95 ? 227 SER A N     1 
ATOM   1690 C CA    . SER A 1 236 ? 1.698  13.999 16.145 1.00 20.52 ? 227 SER A CA    1 
ATOM   1691 C C     . SER A 1 236 ? 1.442  15.288 15.381 1.00 21.89 ? 227 SER A C     1 
ATOM   1692 O O     . SER A 1 236 ? 0.609  15.307 14.469 1.00 27.27 ? 227 SER A O     1 
ATOM   1693 C CB    . SER A 1 236 ? 0.792  13.929 17.368 1.00 25.55 ? 227 SER A CB    1 
ATOM   1694 O OG    . SER A 1 236 ? 0.847  12.618 17.911 1.00 30.73 ? 227 SER A OG    1 
ATOM   1695 N N     . ALA A 1 237 ? 2.154  16.362 15.717 1.00 18.82 ? 228 ALA A N     1 
ATOM   1696 C CA    . ALA A 1 237 ? 1.900  17.646 15.074 1.00 20.09 ? 228 ALA A CA    1 
ATOM   1697 C C     . ALA A 1 237 ? 2.538  17.786 13.695 1.00 20.09 ? 228 ALA A C     1 
ATOM   1698 O O     . ALA A 1 237 ? 1.917  18.378 12.803 1.00 23.17 ? 228 ALA A O     1 
ATOM   1699 C CB    . ALA A 1 237 ? 2.384  18.785 15.970 1.00 18.82 ? 228 ALA A CB    1 
ATOM   1700 N N     . ILE A 1 238 ? 3.785  17.342 13.491 1.00 18.32 ? 229 ILE A N     1 
ATOM   1701 C CA    . ILE A 1 238 ? 4.489  17.614 12.237 1.00 15.76 ? 229 ILE A CA    1 
ATOM   1702 C C     . ILE A 1 238 ? 4.973  16.360 11.530 1.00 18.14 ? 229 ILE A C     1 
ATOM   1703 O O     . ILE A 1 238 ? 5.472  16.465 10.394 1.00 20.17 ? 229 ILE A O     1 
ATOM   1704 C CB    . ILE A 1 238 ? 5.672  18.598 12.425 1.00 18.38 ? 229 ILE A CB    1 
ATOM   1705 C CG1   . ILE A 1 238 ? 6.842  17.953 13.198 1.00 19.43 ? 229 ILE A CG1   1 
ATOM   1706 C CG2   . ILE A 1 238 ? 5.220  19.838 13.178 1.00 19.49 ? 229 ILE A CG2   1 
ATOM   1707 C CD1   . ILE A 1 238 ? 8.095  18.869 13.262 1.00 19.19 ? 229 ILE A CD1   1 
ATOM   1708 N N     . GLY A 1 239 ? 4.842  15.184 12.147 1.00 18.72 ? 230 GLY A N     1 
ATOM   1709 C CA    . GLY A 1 239 ? 5.254  13.945 11.519 1.00 19.01 ? 230 GLY A CA    1 
ATOM   1710 C C     . GLY A 1 239 ? 6.611  13.487 11.988 1.00 22.21 ? 230 GLY A C     1 
ATOM   1711 O O     . GLY A 1 239 ? 7.515  14.316 12.122 1.00 18.95 ? 230 GLY A O     1 
ATOM   1712 N N     . ALA A 1 240 ? 6.761  12.181 12.241 1.00 20.14 ? 231 ALA A N     1 
ATOM   1713 C CA    . ALA A 1 240 ? 7.994  11.682 12.841 1.00 20.82 ? 231 ALA A CA    1 
ATOM   1714 C C     . ALA A 1 240 ? 9.207  12.019 11.989 1.00 16.11 ? 231 ALA A C     1 
ATOM   1715 O O     . ALA A 1 240 ? 10.279 12.314 12.537 1.00 18.71 ? 231 ALA A O     1 
ATOM   1716 C CB    . ALA A 1 240 ? 7.908  10.169 13.085 1.00 20.68 ? 231 ALA A CB    1 
ATOM   1717 N N     . ASP A 1 241 ? 9.071  11.978 10.647 1.00 17.06 ? 232 ASP A N     1 
ATOM   1718 C CA    . ASP A 1 241 ? 10.282 12.135 9.838  1.00 17.65 ? 232 ASP A CA    1 
ATOM   1719 C C     . ASP A 1 241 ? 10.817 13.556 9.842  1.00 18.66 ? 232 ASP A C     1 
ATOM   1720 O O     . ASP A 1 241 ? 11.855 13.807 9.212  1.00 21.11 ? 232 ASP A O     1 
ATOM   1721 C CB    . ASP A 1 241 ? 10.061 11.736 8.374  1.00 22.51 ? 232 ASP A CB    1 
ATOM   1722 C CG    . ASP A 1 241 ? 8.831  12.364 7.756  1.00 30.73 ? 232 ASP A CG    1 
ATOM   1723 O OD1   . ASP A 1 241 ? 8.135  13.170 8.395  1.00 35.67 ? 232 ASP A OD1   1 
ATOM   1724 O OD2   . ASP A 1 241 ? 8.539  12.020 6.594  1.00 51.18 ? 232 ASP A OD2   1 
ATOM   1725 N N     . ARG A 1 242 ? 10.127 14.492 10.485 1.00 15.89 ? 233 ARG A N     1 
ATOM   1726 C CA    . ARG A 1 242 ? 10.629 15.840 10.665 1.00 16.22 ? 233 ARG A CA    1 
ATOM   1727 C C     . ARG A 1 242 ? 11.057 16.095 12.109 1.00 16.16 ? 233 ARG A C     1 
ATOM   1728 O O     . ARG A 1 242 ? 11.209 17.247 12.505 1.00 18.00 ? 233 ARG A O     1 
ATOM   1729 C CB    . ARG A 1 242 ? 9.572  16.856 10.241 1.00 15.88 ? 233 ARG A CB    1 
ATOM   1730 C CG    . ARG A 1 242 ? 9.155  16.738 8.767  1.00 18.26 ? 233 ARG A CG    1 
ATOM   1731 C CD    . ARG A 1 242 ? 8.252  17.877 8.400  1.00 20.43 ? 233 ARG A CD    1 
ATOM   1732 N NE    . ARG A 1 242 ? 7.835  17.744 7.006  1.00 28.08 ? 233 ARG A NE    1 
ATOM   1733 C CZ    . ARG A 1 242 ? 8.433  18.322 5.971  1.00 32.37 ? 233 ARG A CZ    1 
ATOM   1734 N NH1   . ARG A 1 242 ? 9.526  19.057 6.120  1.00 23.25 ? 233 ARG A NH1   1 
ATOM   1735 N NH2   . ARG A 1 242 ? 7.915  18.166 4.751  1.00 29.74 ? 233 ARG A NH2   1 
ATOM   1736 N N     . VAL A 1 243 ? 11.276 15.043 12.901 1.00 16.16 ? 234 VAL A N     1 
ATOM   1737 C CA    . VAL A 1 243 ? 11.627 15.212 14.327 1.00 14.89 ? 234 VAL A CA    1 
ATOM   1738 C C     . VAL A 1 243 ? 12.930 14.484 14.606 1.00 17.09 ? 234 VAL A C     1 
ATOM   1739 O O     . VAL A 1 243 ? 13.026 13.263 14.398 1.00 17.51 ? 234 VAL A O     1 
ATOM   1740 C CB    . VAL A 1 243 ? 10.519 14.675 15.238 1.00 14.12 ? 234 VAL A CB    1 
ATOM   1741 C CG1   . VAL A 1 243 ? 10.967 14.662 16.741 1.00 13.40 ? 234 VAL A CG1   1 
ATOM   1742 C CG2   . VAL A 1 243 ? 9.239  15.463 15.048 1.00 18.46 ? 234 VAL A CG2   1 
ATOM   1743 N N     . GLY A 1 244 ? 13.924 15.223 15.096 1.00 14.67 ? 235 GLY A N     1 
ATOM   1744 C CA    . GLY A 1 244 ? 15.137 14.619 15.629 1.00 13.73 ? 235 GLY A CA    1 
ATOM   1745 C C     . GLY A 1 244 ? 15.162 14.775 17.149 1.00 14.31 ? 235 GLY A C     1 
ATOM   1746 O O     . GLY A 1 244 ? 14.455 15.620 17.700 1.00 15.35 ? 235 GLY A O     1 
ATOM   1747 N N     . VAL A 1 245 ? 15.933 13.941 17.840 1.00 14.37 ? 236 VAL A N     1 
ATOM   1748 C CA    . VAL A 1 245 ? 16.002 13.972 19.302 1.00 15.72 ? 236 VAL A CA    1 
ATOM   1749 C C     . VAL A 1 245 ? 17.471 13.961 19.704 1.00 14.84 ? 236 VAL A C     1 
ATOM   1750 O O     . VAL A 1 245 ? 18.224 13.087 19.251 1.00 15.16 ? 236 VAL A O     1 
ATOM   1751 C CB    . VAL A 1 245 ? 15.251 12.773 19.934 1.00 15.54 ? 236 VAL A CB    1 
ATOM   1752 C CG1   . VAL A 1 245 ? 15.277 12.863 21.480 1.00 15.26 ? 236 VAL A CG1   1 
ATOM   1753 C CG2   . VAL A 1 245 ? 13.785 12.763 19.480 1.00 18.17 ? 236 VAL A CG2   1 
ATOM   1754 N N     . ARG A 1 246 ? 17.882 14.909 20.566 1.00 13.34 ? 237 ARG A N     1 
ATOM   1755 C CA    . ARG A 1 246 ? 19.265 14.967 21.026 1.00 16.82 ? 237 ARG A CA    1 
ATOM   1756 C C     . ARG A 1 246 ? 19.333 14.649 22.517 1.00 14.14 ? 237 ARG A C     1 
ATOM   1757 O O     . ARG A 1 246 ? 18.608 15.248 23.322 1.00 15.57 ? 237 ARG A O     1 
ATOM   1758 C CB    . ARG A 1 246 ? 19.893 16.339 20.757 1.00 15.07 ? 237 ARG A CB    1 
ATOM   1759 C CG    . ARG A 1 246 ? 21.397 16.311 20.954 1.00 15.97 ? 237 ARG A CG    1 
ATOM   1760 C CD    . ARG A 1 246 ? 22.077 17.633 20.564 1.00 17.74 ? 237 ARG A CD    1 
ATOM   1761 N NE    . ARG A 1 246 ? 23.385 17.416 19.949 1.00 17.00 ? 237 ARG A NE    1 
ATOM   1762 C CZ    . ARG A 1 246 ? 24.420 18.230 20.085 1.00 16.25 ? 237 ARG A CZ    1 
ATOM   1763 N NH1   . ARG A 1 246 ? 24.366 19.283 20.868 1.00 16.42 ? 237 ARG A NH1   1 
ATOM   1764 N NH2   . ARG A 1 246 ? 25.521 18.012 19.373 1.00 17.46 ? 237 ARG A NH2   1 
ATOM   1765 N N     . VAL A 1 247 ? 20.217 13.719 22.897 1.00 13.85 ? 238 VAL A N     1 
ATOM   1766 C CA    . VAL A 1 247 ? 20.432 13.421 24.316 1.00 13.63 ? 238 VAL A CA    1 
ATOM   1767 C C     . VAL A 1 247 ? 21.930 13.299 24.594 1.00 15.14 ? 238 VAL A C     1 
ATOM   1768 O O     . VAL A 1 247 ? 22.757 13.212 23.686 1.00 15.22 ? 238 VAL A O     1 
ATOM   1769 C CB    . VAL A 1 247 ? 19.709 12.131 24.774 1.00 16.76 ? 238 VAL A CB    1 
ATOM   1770 C CG1   . VAL A 1 247 ? 18.181 12.324 24.745 1.00 20.04 ? 238 VAL A CG1   1 
ATOM   1771 C CG2   . VAL A 1 247 ? 20.115 10.959 23.880 1.00 16.48 ? 238 VAL A CG2   1 
ATOM   1772 N N     . SER A 1 248 ? 22.263 13.261 25.884 1.00 16.74 ? 239 SER A N     1 
ATOM   1773 C CA    . SER A 1 248 ? 23.657 13.137 26.339 1.00 19.40 ? 239 SER A CA    1 
ATOM   1774 C C     . SER A 1 248 ? 23.683 12.371 27.654 1.00 16.64 ? 239 SER A C     1 
ATOM   1775 O O     . SER A 1 248 ? 23.785 12.957 28.734 1.00 17.99 ? 239 SER A O     1 
ATOM   1776 C CB    . SER A 1 248 ? 24.322 14.505 26.534 1.00 15.26 ? 239 SER A CB    1 
ATOM   1777 O OG    . SER A 1 248 ? 23.637 15.339 27.467 1.00 18.42 ? 239 SER A OG    1 
ATOM   1778 N N     . PRO A 1 249 ? 23.602 11.044 27.597 1.00 16.72 ? 240 PRO A N     1 
ATOM   1779 C CA    . PRO A 1 249 ? 23.453 10.286 28.853 1.00 17.82 ? 240 PRO A CA    1 
ATOM   1780 C C     . PRO A 1 249 ? 24.661 10.363 29.757 1.00 17.51 ? 240 PRO A C     1 
ATOM   1781 O O     . PRO A 1 249 ? 24.511 10.156 30.968 1.00 21.33 ? 240 PRO A O     1 
ATOM   1782 C CB    . PRO A 1 249 ? 23.182 8.848  28.380 1.00 23.61 ? 240 PRO A CB    1 
ATOM   1783 C CG    . PRO A 1 249 ? 23.359 8.848  26.938 1.00 24.39 ? 240 PRO A CG    1 
ATOM   1784 C CD    . PRO A 1 249 ? 23.308 10.228 26.419 1.00 20.37 ? 240 PRO A CD    1 
ATOM   1785 N N     . ALA A 1 250 ? 25.843 10.686 29.246 1.00 19.05 ? 241 ALA A N     1 
ATOM   1786 C CA    . ALA A 1 250 ? 26.995 10.734 30.143 1.00 22.66 ? 241 ALA A CA    1 
ATOM   1787 C C     . ALA A 1 250 ? 27.782 12.022 29.961 1.00 26.00 ? 241 ALA A C     1 
ATOM   1788 O O     . ALA A 1 250 ? 29.014 12.009 29.898 1.00 30.71 ? 241 ALA A O     1 
ATOM   1789 C CB    . ALA A 1 250 ? 27.896 9.520  29.935 1.00 28.06 ? 241 ALA A CB    1 
ATOM   1790 N N     . ILE A 1 251 ? 27.092 13.157 29.848 1.00 23.14 ? 242 ILE A N     1 
ATOM   1791 C CA    . ILE A 1 251 ? 27.728 14.459 30.005 1.00 21.25 ? 242 ILE A CA    1 
ATOM   1792 C C     . ILE A 1 251 ? 27.367 15.010 31.381 1.00 25.57 ? 242 ILE A C     1 
ATOM   1793 O O     . ILE A 1 251 ? 26.186 15.091 31.735 1.00 27.79 ? 242 ILE A O     1 
ATOM   1794 C CB    . ILE A 1 251 ? 27.315 15.425 28.881 1.00 17.44 ? 242 ILE A CB    1 
ATOM   1795 C CG1   . ILE A 1 251 ? 27.980 14.983 27.581 1.00 19.60 ? 242 ILE A CG1   1 
ATOM   1796 C CG2   . ILE A 1 251 ? 27.756 16.842 29.223 1.00 20.02 ? 242 ILE A CG2   1 
ATOM   1797 C CD1   . ILE A 1 251 ? 27.815 15.994 26.420 1.00 19.69 ? 242 ILE A CD1   1 
ATOM   1798 N N     . ASP A 1 252 ? 28.387 15.373 32.161 1.00 23.52 ? 243 ASP A N     1 
ATOM   1799 C CA    . ASP A 1 252 ? 28.194 15.969 33.482 1.00 30.77 ? 243 ASP A CA    1 
ATOM   1800 C C     . ASP A 1 252 ? 28.219 17.481 33.299 1.00 32.09 ? 243 ASP A C     1 
ATOM   1801 O O     . ASP A 1 252 ? 29.274 18.122 33.262 1.00 36.23 ? 243 ASP A O     1 
ATOM   1802 C CB    . ASP A 1 252 ? 29.261 15.481 34.456 1.00 37.38 ? 243 ASP A CB    1 
ATOM   1803 N N     . HIS A 1 253 ? 27.037 18.048 33.111 1.00 24.05 ? 244 HIS A N     1 
ATOM   1804 C CA    . HIS A 1 253 ? 26.853 19.485 32.961 1.00 20.88 ? 244 HIS A CA    1 
ATOM   1805 C C     . HIS A 1 253 ? 25.730 19.880 33.898 1.00 19.83 ? 244 HIS A C     1 
ATOM   1806 O O     . HIS A 1 253 ? 24.682 19.228 33.900 1.00 22.87 ? 244 HIS A O     1 
ATOM   1807 C CB    . HIS A 1 253 ? 26.492 19.855 31.509 1.00 18.61 ? 244 HIS A CB    1 
ATOM   1808 C CG    . HIS A 1 253 ? 26.535 21.323 31.226 1.00 22.56 ? 244 HIS A CG    1 
ATOM   1809 N ND1   . HIS A 1 253 ? 25.450 22.016 30.730 1.00 21.85 ? 244 HIS A ND1   1 
ATOM   1810 C CD2   . HIS A 1 253 ? 27.529 22.229 31.374 1.00 25.56 ? 244 HIS A CD2   1 
ATOM   1811 C CE1   . HIS A 1 253 ? 25.775 23.289 30.588 1.00 24.90 ? 244 HIS A CE1   1 
ATOM   1812 N NE2   . HIS A 1 253 ? 27.033 23.443 30.960 1.00 26.44 ? 244 HIS A NE2   1 
ATOM   1813 N N     . LEU A 1 254 ? 25.952 20.923 34.714 1.00 18.75 ? 245 LEU A N     1 
ATOM   1814 C CA    . LEU A 1 254 ? 24.906 21.471 35.579 1.00 20.38 ? 245 LEU A CA    1 
ATOM   1815 C C     . LEU A 1 254 ? 24.332 20.411 36.512 1.00 18.03 ? 245 LEU A C     1 
ATOM   1816 O O     . LEU A 1 254 ? 23.123 20.350 36.733 1.00 17.74 ? 245 LEU A O     1 
ATOM   1817 C CB    . LEU A 1 254 ? 23.790 22.121 34.748 1.00 20.28 ? 245 LEU A CB    1 
ATOM   1818 C CG    . LEU A 1 254 ? 24.277 23.147 33.721 1.00 20.51 ? 245 LEU A CG    1 
ATOM   1819 C CD1   . LEU A 1 254 ? 23.106 23.719 32.917 1.00 19.82 ? 245 LEU A CD1   1 
ATOM   1820 C CD2   . LEU A 1 254 ? 25.043 24.291 34.417 1.00 22.35 ? 245 LEU A CD2   1 
ATOM   1821 N N     . ASP A 1 255 ? 25.208 19.536 37.011 1.00 19.50 ? 246 ASP A N     1 
ATOM   1822 C CA    . ASP A 1 255 ? 24.885 18.487 37.979 1.00 20.42 ? 246 ASP A CA    1 
ATOM   1823 C C     . ASP A 1 255 ? 24.044 17.368 37.378 1.00 25.15 ? 246 ASP A C     1 
ATOM   1824 O O     . ASP A 1 255 ? 23.435 16.587 38.115 1.00 26.91 ? 246 ASP A O     1 
ATOM   1825 C CB    . ASP A 1 255 ? 24.204 19.050 39.243 1.00 23.45 ? 246 ASP A CB    1 
ATOM   1826 C CG    . ASP A 1 255 ? 25.108 19.988 40.024 1.00 23.68 ? 246 ASP A CG    1 
ATOM   1827 O OD1   . ASP A 1 255 ? 26.347 19.874 39.903 1.00 32.13 ? 246 ASP A OD1   1 
ATOM   1828 O OD2   . ASP A 1 255 ? 24.585 20.824 40.774 1.00 32.82 ? 246 ASP A OD2   1 
ATOM   1829 N N     . ALA A 1 256 ? 24.032 17.242 36.053 1.00 22.57 ? 247 ALA A N     1 
ATOM   1830 C CA    . ALA A 1 256 ? 23.347 16.142 35.388 1.00 18.75 ? 247 ALA A CA    1 
ATOM   1831 C C     . ALA A 1 256 ? 24.238 14.916 35.487 1.00 29.56 ? 247 ALA A C     1 
ATOM   1832 O O     . ALA A 1 256 ? 25.324 14.874 34.897 1.00 40.77 ? 247 ALA A O     1 
ATOM   1833 C CB    . ALA A 1 256 ? 23.034 16.489 33.931 1.00 20.46 ? 247 ALA A CB    1 
ATOM   1834 N N     . MET A 1 257 ? 23.801 13.934 36.260 1.00 21.71 ? 248 MET A N     1 
ATOM   1835 C CA    . MET A 1 257 ? 24.500 12.662 36.317 1.00 21.78 ? 248 MET A CA    1 
ATOM   1836 C C     . MET A 1 257 ? 23.432 11.601 36.521 1.00 21.02 ? 248 MET A C     1 
ATOM   1837 O O     . MET A 1 257 ? 22.417 11.860 37.175 1.00 20.92 ? 248 MET A O     1 
ATOM   1838 C CB    . MET A 1 257 ? 25.548 12.652 37.457 1.00 24.63 ? 248 MET A CB    1 
ATOM   1839 C CG    . MET A 1 257 ? 25.091 12.327 38.870 1.00 41.35 ? 248 MET A CG    1 
ATOM   1840 S SD    . MET A 1 257 ? 24.935 10.528 39.139 1.00 69.06 ? 248 MET A SD    1 
ATOM   1841 C CE    . MET A 1 257 ? 23.463 10.361 40.161 1.00 37.05 ? 248 MET A CE    1 
ATOM   1842 N N     . ASP A 1 258 ? 23.634 10.433 35.905 1.00 23.03 ? 249 ASP A N     1 
ATOM   1843 C CA    . ASP A 1 258 ? 22.818 9.267  36.196 1.00 24.02 ? 249 ASP A CA    1 
ATOM   1844 C C     . ASP A 1 258 ? 23.674 8.172  36.804 1.00 22.31 ? 249 ASP A C     1 
ATOM   1845 O O     . ASP A 1 258 ? 24.817 7.973  36.379 1.00 25.46 ? 249 ASP A O     1 
ATOM   1846 C CB    . ASP A 1 258 ? 22.138 8.688  34.961 1.00 22.35 ? 249 ASP A CB    1 
ATOM   1847 C CG    . ASP A 1 258 ? 20.930 7.847  35.337 1.00 32.88 ? 249 ASP A CG    1 
ATOM   1848 O OD1   . ASP A 1 258 ? 19.843 8.413  35.625 1.00 21.39 ? 249 ASP A OD1   1 
ATOM   1849 O OD2   . ASP A 1 258 ? 21.103 6.603  35.433 1.00 25.99 ? 249 ASP A OD2   1 
ATOM   1850 N N     . SER A 1 259 ? 23.075 7.432  37.744 1.00 21.42 ? 250 SER A N     1 
ATOM   1851 C CA    . SER A 1 259 ? 23.758 6.294  38.355 1.00 20.59 ? 250 SER A CA    1 
ATOM   1852 C C     . SER A 1 259 ? 24.089 5.205  37.327 1.00 28.04 ? 250 SER A C     1 
ATOM   1853 O O     . SER A 1 259 ? 25.034 4.431  37.519 1.00 23.17 ? 250 SER A O     1 
ATOM   1854 C CB    . SER A 1 259 ? 22.903 5.727  39.485 1.00 25.66 ? 250 SER A CB    1 
ATOM   1855 O OG    . SER A 1 259 ? 21.704 5.177  38.968 1.00 29.11 ? 250 SER A OG    1 
ATOM   1856 N N     . ASN A 1 260 ? 23.342 5.106  36.232 1.00 19.80 ? 251 ASN A N     1 
ATOM   1857 C CA    . ASN A 1 260 ? 23.628 4.094  35.219 1.00 17.92 ? 251 ASN A CA    1 
ATOM   1858 C C     . ASN A 1 260 ? 23.373 4.699  33.856 1.00 20.67 ? 251 ASN A C     1 
ATOM   1859 O O     . ASN A 1 260 ? 22.313 4.483  33.260 1.00 22.34 ? 251 ASN A O     1 
ATOM   1860 C CB    . ASN A 1 260 ? 22.778 2.840  35.407 1.00 17.85 ? 251 ASN A CB    1 
ATOM   1861 C CG    . ASN A 1 260 ? 23.269 1.665  34.531 1.00 25.26 ? 251 ASN A CG    1 
ATOM   1862 O OD1   . ASN A 1 260 ? 23.863 1.857  33.442 1.00 27.84 ? 251 ASN A OD1   1 
ATOM   1863 N ND2   . ASN A 1 260 ? 22.987 0.439  34.985 1.00 36.30 ? 251 ASN A ND2   1 
ATOM   1864 N N     . PRO A 1 261 ? 24.355 5.426  33.311 1.00 18.63 ? 252 PRO A N     1 
ATOM   1865 C CA    . PRO A 1 261 ? 24.131 6.168  32.055 1.00 19.88 ? 252 PRO A CA    1 
ATOM   1866 C C     . PRO A 1 261 ? 23.748 5.307  30.870 1.00 18.99 ? 252 PRO A C     1 
ATOM   1867 O O     . PRO A 1 261 ? 22.864 5.694  30.097 1.00 18.10 ? 252 PRO A O     1 
ATOM   1868 C CB    . PRO A 1 261 ? 25.481 6.854  31.819 1.00 21.46 ? 252 PRO A CB    1 
ATOM   1869 C CG    . PRO A 1 261 ? 26.061 7.003  33.208 1.00 23.17 ? 252 PRO A CG    1 
ATOM   1870 C CD    . PRO A 1 261 ? 25.670 5.732  33.906 1.00 25.79 ? 252 PRO A CD    1 
ATOM   1871 N N     . LEU A 1 262 ? 24.415 4.163  30.680 1.00 17.73 ? 253 LEU A N     1 
ATOM   1872 C CA    . LEU A 1 262 ? 24.060 3.301  29.555 1.00 18.51 ? 253 LEU A CA    1 
ATOM   1873 C C     . LEU A 1 262 ? 22.628 2.804  29.679 1.00 17.08 ? 253 LEU A C     1 
ATOM   1874 O O     . LEU A 1 262 ? 21.879 2.798  28.697 1.00 19.77 ? 253 LEU A O     1 
ATOM   1875 C CB    . LEU A 1 262 ? 25.033 2.122  29.475 1.00 24.05 ? 253 LEU A CB    1 
ATOM   1876 C CG    . LEU A 1 262 ? 24.679 1.134  28.355 1.00 21.06 ? 253 LEU A CG    1 
ATOM   1877 C CD1   . LEU A 1 262 ? 24.661 1.818  27.003 1.00 25.00 ? 253 LEU A CD1   1 
ATOM   1878 C CD2   . LEU A 1 262 ? 25.687 0.012  28.358 1.00 25.42 ? 253 LEU A CD2   1 
ATOM   1879 N N     . SER A 1 263 ? 22.227 2.378  30.890 1.00 17.19 ? 254 SER A N     1 
ATOM   1880 C CA    . SER A 1 263 ? 20.863 1.915  31.099 1.00 15.69 ? 254 SER A CA    1 
ATOM   1881 C C     . SER A 1 263 ? 19.856 3.022  30.807 1.00 19.70 ? 254 SER A C     1 
ATOM   1882 O O     . SER A 1 263 ? 18.814 2.780  30.186 1.00 17.89 ? 254 SER A O     1 
ATOM   1883 C CB    . SER A 1 263 ? 20.715 1.406  32.530 1.00 20.56 ? 254 SER A CB    1 
ATOM   1884 O OG    . SER A 1 263 ? 19.441 0.866  32.749 1.00 22.48 ? 254 SER A OG    1 
ATOM   1885 N N     . LEU A 1 264 ? 20.140 4.245  31.261 1.00 18.20 ? 255 LEU A N     1 
ATOM   1886 C CA    . LEU A 1 264 ? 19.240 5.354  30.971 1.00 16.83 ? 255 LEU A CA    1 
ATOM   1887 C C     . LEU A 1 264 ? 19.168 5.607  29.470 1.00 19.36 ? 255 LEU A C     1 
ATOM   1888 O O     . LEU A 1 264 ? 18.072 5.762  28.904 1.00 17.80 ? 255 LEU A O     1 
ATOM   1889 C CB    . LEU A 1 264 ? 19.704 6.607  31.720 1.00 18.05 ? 255 LEU A CB    1 
ATOM   1890 C CG    . LEU A 1 264 ? 18.941 7.878  31.346 1.00 21.07 ? 255 LEU A CG    1 
ATOM   1891 C CD1   . LEU A 1 264 ? 17.468 7.762  31.753 1.00 18.60 ? 255 LEU A CD1   1 
ATOM   1892 C CD2   . LEU A 1 264 ? 19.629 9.041  32.050 1.00 19.93 ? 255 LEU A CD2   1 
ATOM   1893 N N     . GLY A 1 265 ? 20.330 5.652  28.798 1.00 16.04 ? 256 GLY A N     1 
ATOM   1894 C CA    . GLY A 1 265 ? 20.319 5.862  27.357 1.00 15.89 ? 256 GLY A CA    1 
ATOM   1895 C C     . GLY A 1 265 ? 19.550 4.783  26.617 1.00 17.93 ? 256 GLY A C     1 
ATOM   1896 O O     . GLY A 1 265 ? 18.790 5.070  25.685 1.00 18.32 ? 256 GLY A O     1 
ATOM   1897 N N     . LEU A 1 266 ? 19.724 3.529  27.030 1.00 16.40 ? 257 LEU A N     1 
ATOM   1898 C CA    . LEU A 1 266 ? 18.984 2.462  26.375 1.00 16.94 ? 257 LEU A CA    1 
ATOM   1899 C C     . LEU A 1 266 ? 17.493 2.576  26.661 1.00 15.61 ? 257 LEU A C     1 
ATOM   1900 O O     . LEU A 1 266 ? 16.671 2.183  25.828 1.00 17.73 ? 257 LEU A O     1 
ATOM   1901 C CB    . LEU A 1 266 ? 19.519 1.111  26.840 1.00 16.78 ? 257 LEU A CB    1 
ATOM   1902 C CG    . LEU A 1 266 ? 20.893 0.725  26.294 1.00 19.30 ? 257 LEU A CG    1 
ATOM   1903 C CD1   . LEU A 1 266 ? 21.345 -0.525 26.995 1.00 20.03 ? 257 LEU A CD1   1 
ATOM   1904 C CD2   . LEU A 1 266 ? 20.897 0.530  24.773 1.00 20.21 ? 257 LEU A CD2   1 
ATOM   1905 N N     . ALA A 1 267 ? 17.124 3.076  27.849 1.00 16.96 ? 258 ALA A N     1 
ATOM   1906 C CA    . ALA A 1 267 ? 15.709 3.245  28.153 1.00 16.03 ? 258 ALA A CA    1 
ATOM   1907 C C     . ALA A 1 267 ? 15.091 4.305  27.253 1.00 17.72 ? 258 ALA A C     1 
ATOM   1908 O O     . ALA A 1 267 ? 13.975 4.126  26.747 1.00 18.23 ? 258 ALA A O     1 
ATOM   1909 C CB    . ALA A 1 267 ? 15.524 3.601  29.633 1.00 18.54 ? 258 ALA A CB    1 
ATOM   1910 N N     . VAL A 1 268 ? 15.826 5.391  27.004 1.00 16.70 ? 259 VAL A N     1 
ATOM   1911 C CA    . VAL A 1 268 ? 15.347 6.434  26.089 1.00 15.01 ? 259 VAL A CA    1 
ATOM   1912 C C     . VAL A 1 268 ? 15.207 5.876  24.680 1.00 15.24 ? 259 VAL A C     1 
ATOM   1913 O O     . VAL A 1 268 ? 14.204 6.114  24.003 1.00 17.20 ? 259 VAL A O     1 
ATOM   1914 C CB    . VAL A 1 268 ? 16.293 7.645  26.103 1.00 19.11 ? 259 VAL A CB    1 
ATOM   1915 C CG1   . VAL A 1 268 ? 15.891 8.652  25.004 1.00 17.80 ? 259 VAL A CG1   1 
ATOM   1916 C CG2   . VAL A 1 268 ? 16.258 8.299  27.472 1.00 19.90 ? 259 VAL A CG2   1 
ATOM   1917 N N     . VAL A 1 269 ? 16.221 5.146  24.218 1.00 15.70 ? 260 VAL A N     1 
ATOM   1918 C CA    . VAL A 1 269 ? 16.150 4.552  22.883 1.00 16.94 ? 260 VAL A CA    1 
ATOM   1919 C C     . VAL A 1 269 ? 14.930 3.647  22.761 1.00 16.49 ? 260 VAL A C     1 
ATOM   1920 O O     . VAL A 1 269 ? 14.208 3.701  21.761 1.00 18.47 ? 260 VAL A O     1 
ATOM   1921 C CB    . VAL A 1 269 ? 17.454 3.798  22.572 1.00 15.26 ? 260 VAL A CB    1 
ATOM   1922 C CG1   . VAL A 1 269 ? 17.291 2.951  21.280 1.00 17.08 ? 260 VAL A CG1   1 
ATOM   1923 C CG2   . VAL A 1 269 ? 18.601 4.802  22.430 1.00 16.52 ? 260 VAL A CG2   1 
ATOM   1924 N N     . GLU A 1 270 ? 14.637 2.840  23.786 1.00 16.26 ? 261 GLU A N     1 
ATOM   1925 C CA    . GLU A 1 270 ? 13.457 1.976  23.694 1.00 17.95 ? 261 GLU A CA    1 
ATOM   1926 C C     . GLU A 1 270 ? 12.173 2.794  23.522 1.00 20.92 ? 261 GLU A C     1 
ATOM   1927 O O     . GLU A 1 270 ? 11.272 2.386  22.788 1.00 21.20 ? 261 GLU A O     1 
ATOM   1928 C CB    . GLU A 1 270 ? 13.331 1.090  24.930 1.00 25.46 ? 261 GLU A CB    1 
ATOM   1929 C CG    . GLU A 1 270 ? 12.292 -0.041 24.793 1.00 28.85 ? 261 GLU A CG    1 
ATOM   1930 C CD    . GLU A 1 270 ? 10.875 0.344  25.252 1.00 43.30 ? 261 GLU A CD    1 
ATOM   1931 O OE1   . GLU A 1 270 ? 10.733 1.206  26.147 1.00 43.60 ? 261 GLU A OE1   1 
ATOM   1932 O OE2   . GLU A 1 270 ? 9.898  -0.271 24.758 1.00 44.95 ? 261 GLU A OE2   1 
ATOM   1933 N N     . ARG A 1 271 ? 12.060 3.939  24.218 1.00 18.56 ? 262 ARG A N     1 
ATOM   1934 C CA    . ARG A 1 271 ? 10.886 4.794  24.037 1.00 17.36 ? 262 ARG A CA    1 
ATOM   1935 C C     . ARG A 1 271 ? 10.795 5.279  22.605 1.00 19.02 ? 262 ARG A C     1 
ATOM   1936 O O     . ARG A 1 271 ? 9.700  5.339  22.037 1.00 20.07 ? 262 ARG A O     1 
ATOM   1937 C CB    . ARG A 1 271 ? 10.928 6.025  24.955 1.00 21.12 ? 262 ARG A CB    1 
ATOM   1938 C CG    . ARG A 1 271 ? 11.093 5.713  26.416 1.00 28.63 ? 262 ARG A CG    1 
ATOM   1939 C CD    . ARG A 1 271 ? 10.159 4.640  26.825 1.00 25.67 ? 262 ARG A CD    1 
ATOM   1940 N NE    . ARG A 1 271 ? 8.762  5.019  26.656 1.00 32.53 ? 262 ARG A NE    1 
ATOM   1941 C CZ    . ARG A 1 271 ? 7.778  4.164  26.399 1.00 41.72 ? 262 ARG A CZ    1 
ATOM   1942 N NH1   . ARG A 1 271 ? 8.022  2.888  26.125 1.00 32.87 ? 262 ARG A NH1   1 
ATOM   1943 N NH2   . ARG A 1 271 ? 6.517  4.598  26.422 1.00 34.76 ? 262 ARG A NH2   1 
ATOM   1944 N N     . LEU A 1 272 ? 11.925 5.702  22.031 1.00 18.75 ? 263 LEU A N     1 
ATOM   1945 C CA    . LEU A 1 272 ? 11.891 6.224  20.672 1.00 18.96 ? 263 LEU A CA    1 
ATOM   1946 C C     . LEU A 1 272 ? 11.480 5.139  19.693 1.00 18.17 ? 263 LEU A C     1 
ATOM   1947 O O     . LEU A 1 272 ? 10.656 5.380  18.805 1.00 17.55 ? 263 LEU A O     1 
ATOM   1948 C CB    . LEU A 1 272 ? 13.251 6.801  20.273 1.00 16.39 ? 263 LEU A CB    1 
ATOM   1949 C CG    . LEU A 1 272 ? 13.692 7.958  21.165 1.00 16.81 ? 263 LEU A CG    1 
ATOM   1950 C CD1   . LEU A 1 272 ? 15.060 8.430  20.741 1.00 18.94 ? 263 LEU A CD1   1 
ATOM   1951 C CD2   . LEU A 1 272 ? 12.661 9.101  21.193 1.00 17.45 ? 263 LEU A CD2   1 
ATOM   1952 N N     . ASN A 1 273 ? 12.044 3.936  19.853 1.00 15.48 ? 264 ASN A N     1 
ATOM   1953 C CA    . ASN A 1 273 ? 11.637 2.815  19.005 1.00 19.43 ? 264 ASN A CA    1 
ATOM   1954 C C     . ASN A 1 273 ? 10.140 2.559  19.120 1.00 17.66 ? 264 ASN A C     1 
ATOM   1955 O O     . ASN A 1 273 ? 9.480  2.256  18.116 1.00 19.61 ? 264 ASN A O     1 
ATOM   1956 C CB    . ASN A 1 273 ? 12.404 1.544  19.377 1.00 17.59 ? 264 ASN A CB    1 
ATOM   1957 C CG    . ASN A 1 273 ? 13.858 1.554  18.918 1.00 19.47 ? 264 ASN A CG    1 
ATOM   1958 O OD1   . ASN A 1 273 ? 14.271 2.363  18.083 1.00 18.70 ? 264 ASN A OD1   1 
ATOM   1959 N ND2   . ASN A 1 273 ? 14.644 0.644  19.478 1.00 20.30 ? 264 ASN A ND2   1 
ATOM   1960 N N     . LYS A 1 274 ? 9.588  2.645  20.343 1.00 17.68 ? 265 LYS A N     1 
ATOM   1961 C CA    . LYS A 1 274 ? 8.158  2.394  20.525 1.00 19.59 ? 265 LYS A CA    1 
ATOM   1962 C C     . LYS A 1 274 ? 7.307  3.503  19.903 1.00 22.96 ? 265 LYS A C     1 
ATOM   1963 O O     . LYS A 1 274 ? 6.275  3.219  19.287 1.00 21.82 ? 265 LYS A O     1 
ATOM   1964 C CB    . LYS A 1 274 ? 7.831  2.223  22.013 1.00 24.30 ? 265 LYS A CB    1 
ATOM   1965 N N     . ILE A 1 275 ? 7.741  4.767  20.011 1.00 18.89 ? 266 ILE A N     1 
ATOM   1966 C CA    . ILE A 1 275 ? 7.012  5.860  19.374 1.00 17.02 ? 266 ILE A CA    1 
ATOM   1967 C C     . ILE A 1 275 ? 6.941  5.629  17.871 1.00 19.49 ? 266 ILE A C     1 
ATOM   1968 O O     . ILE A 1 275 ? 5.907  5.868  17.231 1.00 23.00 ? 266 ILE A O     1 
ATOM   1969 C CB    . ILE A 1 275 ? 7.680  7.212  19.709 1.00 18.68 ? 266 ILE A CB    1 
ATOM   1970 C CG1   . ILE A 1 275 ? 7.452  7.605  21.172 1.00 19.94 ? 266 ILE A CG1   1 
ATOM   1971 C CG2   . ILE A 1 275 ? 7.126  8.323  18.797 1.00 22.66 ? 266 ILE A CG2   1 
ATOM   1972 C CD1   . ILE A 1 275 ? 8.144  8.922  21.575 1.00 19.50 ? 266 ILE A CD1   1 
ATOM   1973 N N     . GLN A 1 276 ? 8.051  5.178  17.285 1.00 19.28 ? 267 GLN A N     1 
ATOM   1974 C CA    . GLN A 1 276 ? 8.102  4.900  15.851 1.00 21.90 ? 267 GLN A CA    1 
ATOM   1975 C C     . GLN A 1 276 ? 7.149  3.776  15.492 1.00 27.50 ? 267 GLN A C     1 
ATOM   1976 O O     . GLN A 1 276 ? 6.409  3.859  14.502 1.00 24.98 ? 267 GLN A O     1 
ATOM   1977 C CB    . GLN A 1 276 ? 9.531  4.536  15.448 1.00 18.94 ? 267 GLN A CB    1 
ATOM   1978 C CG    . GLN A 1 276 ? 10.454 5.746  15.490 1.00 19.35 ? 267 GLN A CG    1 
ATOM   1979 C CD    . GLN A 1 276 ? 11.898 5.458  15.132 1.00 19.83 ? 267 GLN A CD    1 
ATOM   1980 O OE1   . GLN A 1 276 ? 12.660 6.392  14.864 1.00 18.88 ? 267 GLN A OE1   1 
ATOM   1981 N NE2   . GLN A 1 276 ? 12.298 4.190  15.142 1.00 19.74 ? 267 GLN A NE2   1 
ATOM   1982 N N     . LEU A 1 277 ? 7.163  2.711  16.293 1.00 21.74 ? 268 LEU A N     1 
ATOM   1983 C CA    . LEU A 1 277 ? 6.282  1.578  16.046 1.00 27.08 ? 268 LEU A CA    1 
ATOM   1984 C C     . LEU A 1 277 ? 4.823  2.009  16.113 1.00 31.62 ? 268 LEU A C     1 
ATOM   1985 O O     . LEU A 1 277 ? 4.020  1.638  15.252 1.00 31.29 ? 268 LEU A O     1 
ATOM   1986 C CB    . LEU A 1 277 ? 6.572  0.483  17.070 1.00 32.05 ? 268 LEU A CB    1 
ATOM   1987 C CG    . LEU A 1 277 ? 6.224  -0.951 16.716 1.00 53.39 ? 268 LEU A CG    1 
ATOM   1988 C CD1   . LEU A 1 277 ? 7.220  -1.453 15.679 1.00 58.42 ? 268 LEU A CD1   1 
ATOM   1989 C CD2   . LEU A 1 277 ? 6.222  -1.815 17.977 1.00 47.87 ? 268 LEU A CD2   1 
ATOM   1990 N N     . HIS A 1 278 ? 4.470  2.829  17.108 1.00 28.24 ? 269 HIS A N     1 
ATOM   1991 C CA    . HIS A 1 278 ? 3.071  3.215  17.295 1.00 29.84 ? 269 HIS A CA    1 
ATOM   1992 C C     . HIS A 1 278 ? 2.601  4.176  16.211 1.00 38.11 ? 269 HIS A C     1 
ATOM   1993 O O     . HIS A 1 278 ? 1.416  4.181  15.859 1.00 41.84 ? 269 HIS A O     1 
ATOM   1994 C CB    . HIS A 1 278 ? 2.863  3.842  18.676 1.00 30.05 ? 269 HIS A CB    1 
ATOM   1995 N N     . SER A 1 279 ? 3.496  4.995  15.674 1.00 29.45 ? 270 SER A N     1 
ATOM   1996 C CA    . SER A 1 279 ? 3.118  5.946  14.638 1.00 32.03 ? 270 SER A CA    1 
ATOM   1997 C C     . SER A 1 279 ? 3.359  5.418  13.228 1.00 34.91 ? 270 SER A C     1 
ATOM   1998 O O     . SER A 1 279 ? 3.027  6.110  12.261 1.00 40.45 ? 270 SER A O     1 
ATOM   1999 C CB    . SER A 1 279 ? 3.871  7.266  14.832 1.00 35.83 ? 270 SER A CB    1 
ATOM   2000 O OG    . SER A 1 279 ? 5.190  7.152  14.340 1.00 39.02 ? 270 SER A OG    1 
ATOM   2001 N N     . GLY A 1 280 ? 3.917  4.218  13.090 1.00 30.33 ? 271 GLY A N     1 
ATOM   2002 C CA    . GLY A 1 280 ? 4.204  3.671  11.774 1.00 38.02 ? 271 GLY A CA    1 
ATOM   2003 C C     . GLY A 1 280 ? 5.195  4.467  10.954 1.00 37.77 ? 271 GLY A C     1 
ATOM   2004 O O     . GLY A 1 280 ? 5.162  4.399  9.725  1.00 33.00 ? 271 GLY A O     1 
ATOM   2005 N N     . SER A 1 281 ? 6.084  5.222  11.597 1.00 27.36 ? 272 SER A N     1 
ATOM   2006 C CA    . SER A 1 281 ? 7.050  6.040  10.873 1.00 29.57 ? 272 SER A CA    1 
ATOM   2007 C C     . SER A 1 281 ? 8.305  6.191  11.720 1.00 29.31 ? 272 SER A C     1 
ATOM   2008 O O     . SER A 1 281 ? 8.239  6.140  12.944 1.00 29.00 ? 272 SER A O     1 
ATOM   2009 C CB    . SER A 1 281 ? 6.491  7.429  10.542 1.00 35.40 ? 272 SER A CB    1 
ATOM   2010 O OG    . SER A 1 281 ? 7.375  8.122  9.673  1.00 49.20 ? 272 SER A OG    1 
ATOM   2011 N N     . LYS A 1 282 ? 9.440  6.402  11.066 1.00 25.42 ? 273 LYS A N     1 
ATOM   2012 C CA    . LYS A 1 282 ? 10.686 6.615  11.786 1.00 21.40 ? 273 LYS A CA    1 
ATOM   2013 C C     . LYS A 1 282 ? 10.921 8.109  12.015 1.00 15.74 ? 273 LYS A C     1 
ATOM   2014 O O     . LYS A 1 282 ? 10.544 8.962  11.203 1.00 18.73 ? 273 LYS A O     1 
ATOM   2015 C CB    . LYS A 1 282 ? 11.864 6.014  11.013 1.00 25.99 ? 273 LYS A CB    1 
ATOM   2016 C CG    . LYS A 1 282 ? 12.106 4.497  11.285 1.00 30.76 ? 273 LYS A CG    1 
ATOM   2017 C CD    . LYS A 1 282 ? 13.314 3.955  10.515 1.00 40.98 ? 273 LYS A CD    1 
ATOM   2018 C CE    . LYS A 1 282 ? 13.322 2.419  10.498 1.00 37.89 ? 273 LYS A CE    1 
ATOM   2019 N NZ    . LYS A 1 282 ? 12.418 1.871  11.554 1.00 44.68 ? 273 LYS A NZ    1 
ATOM   2020 N N     . LEU A 1 283 ? 11.533 8.422  13.153 1.00 16.94 ? 274 LEU A N     1 
ATOM   2021 C CA    . LEU A 1 283 ? 12.024 9.764  13.388 1.00 19.39 ? 274 LEU A CA    1 
ATOM   2022 C C     . LEU A 1 283 ? 13.076 10.128 12.354 1.00 17.31 ? 274 LEU A C     1 
ATOM   2023 O O     . LEU A 1 283 ? 13.637 9.269  11.655 1.00 16.58 ? 274 LEU A O     1 
ATOM   2024 C CB    . LEU A 1 283 ? 12.636 9.868  14.784 1.00 17.95 ? 274 LEU A CB    1 
ATOM   2025 C CG    . LEU A 1 283 ? 11.658 9.562  15.909 1.00 16.26 ? 274 LEU A CG    1 
ATOM   2026 C CD1   . LEU A 1 283 ? 12.409 9.201  17.209 1.00 20.46 ? 274 LEU A CD1   1 
ATOM   2027 C CD2   . LEU A 1 283 ? 10.752 10.776 16.161 1.00 18.63 ? 274 LEU A CD2   1 
ATOM   2028 N N     . ALA A 1 284 ? 13.363 11.435 12.265 1.00 17.52 ? 275 ALA A N     1 
ATOM   2029 C CA    . ALA A 1 284 ? 14.456 11.882 11.413 1.00 14.19 ? 275 ALA A CA    1 
ATOM   2030 C C     . ALA A 1 284 ? 15.788 11.294 11.873 1.00 16.34 ? 275 ALA A C     1 
ATOM   2031 O O     . ALA A 1 284 ? 16.578 10.819 11.054 1.00 17.25 ? 275 ALA A O     1 
ATOM   2032 C CB    . ALA A 1 284 ? 14.522 13.413 11.403 1.00 18.14 ? 275 ALA A CB    1 
ATOM   2033 N N     . TYR A 1 285 ? 16.034 11.276 13.190 1.00 16.60 ? 276 TYR A N     1 
ATOM   2034 C CA    . TYR A 1 285 ? 17.285 10.737 13.711 1.00 15.13 ? 276 TYR A CA    1 
ATOM   2035 C C     . TYR A 1 285 ? 17.272 10.760 15.233 1.00 16.37 ? 276 TYR A C     1 
ATOM   2036 O O     . TYR A 1 285 ? 16.474 11.456 15.862 1.00 16.38 ? 276 TYR A O     1 
ATOM   2037 C CB    . TYR A 1 285 ? 18.511 11.520 13.244 1.00 15.96 ? 276 TYR A CB    1 
ATOM   2038 C CG    . TYR A 1 285 ? 18.453 12.999 13.593 1.00 17.05 ? 276 TYR A CG    1 
ATOM   2039 C CD1   . TYR A 1 285 ? 18.850 13.482 14.836 1.00 17.48 ? 276 TYR A CD1   1 
ATOM   2040 C CD2   . TYR A 1 285 ? 17.990 13.908 12.668 1.00 15.04 ? 276 TYR A CD2   1 
ATOM   2041 C CE1   . TYR A 1 285 ? 18.772 14.839 15.138 1.00 15.92 ? 276 TYR A CE1   1 
ATOM   2042 C CE2   . TYR A 1 285 ? 17.930 15.244 12.932 1.00 14.97 ? 276 TYR A CE2   1 
ATOM   2043 C CZ    . TYR A 1 285 ? 18.321 15.718 14.165 1.00 13.50 ? 276 TYR A CZ    1 
ATOM   2044 O OH    . TYR A 1 285 ? 18.266 17.071 14.455 1.00 20.17 ? 276 TYR A OH    1 
ATOM   2045 N N     . LEU A 1 286 ? 18.224 10.033 15.797 1.00 14.01 ? 277 LEU A N     1 
ATOM   2046 C CA    . LEU A 1 286 ? 18.682 10.200 17.175 1.00 14.90 ? 277 LEU A CA    1 
ATOM   2047 C C     . LEU A 1 286 ? 20.083 10.790 17.132 1.00 14.35 ? 277 LEU A C     1 
ATOM   2048 O O     . LEU A 1 286 ? 20.935 10.329 16.369 1.00 15.82 ? 277 LEU A O     1 
ATOM   2049 C CB    . LEU A 1 286 ? 18.687 8.858  17.905 1.00 15.27 ? 277 LEU A CB    1 
ATOM   2050 C CG    . LEU A 1 286 ? 19.442 8.800  19.228 1.00 15.42 ? 277 LEU A CG    1 
ATOM   2051 C CD1   . LEU A 1 286 ? 18.761 9.682  20.266 1.00 14.91 ? 277 LEU A CD1   1 
ATOM   2052 C CD2   . LEU A 1 286 ? 19.528 7.357  19.710 1.00 15.72 ? 277 LEU A CD2   1 
ATOM   2053 N N     . HIS A 1 287 ? 20.317 11.804 17.956 1.00 13.68 ? 278 HIS A N     1 
ATOM   2054 C CA    . HIS A 1 287 ? 21.562 12.566 17.973 1.00 13.75 ? 278 HIS A CA    1 
ATOM   2055 C C     . HIS A 1 287 ? 22.123 12.420 19.381 1.00 15.01 ? 278 HIS A C     1 
ATOM   2056 O O     . HIS A 1 287 ? 21.497 12.867 20.346 1.00 16.89 ? 278 HIS A O     1 
ATOM   2057 C CB    . HIS A 1 287 ? 21.218 14.022 17.629 1.00 14.42 ? 278 HIS A CB    1 
ATOM   2058 C CG    . HIS A 1 287 ? 22.379 14.943 17.401 1.00 15.39 ? 278 HIS A CG    1 
ATOM   2059 N ND1   . HIS A 1 287 ? 22.173 16.246 16.996 1.00 15.64 ? 278 HIS A ND1   1 
ATOM   2060 C CD2   . HIS A 1 287 ? 23.721 14.776 17.480 1.00 16.49 ? 278 HIS A CD2   1 
ATOM   2061 C CE1   . HIS A 1 287 ? 23.342 16.840 16.818 1.00 16.07 ? 278 HIS A CE1   1 
ATOM   2062 N NE2   . HIS A 1 287 ? 24.297 15.972 17.110 1.00 16.93 ? 278 HIS A NE2   1 
ATOM   2063 N N     . VAL A 1 288 ? 23.255 11.726 19.531 1.00 14.88 ? 279 VAL A N     1 
ATOM   2064 C CA    . VAL A 1 288 ? 23.834 11.510 20.861 1.00 17.87 ? 279 VAL A CA    1 
ATOM   2065 C C     . VAL A 1 288 ? 25.148 12.271 20.927 1.00 16.11 ? 279 VAL A C     1 
ATOM   2066 O O     . VAL A 1 288 ? 25.986 12.162 20.022 1.00 17.21 ? 279 VAL A O     1 
ATOM   2067 C CB    . VAL A 1 288 ? 24.049 10.015 21.152 1.00 15.35 ? 279 VAL A CB    1 
ATOM   2068 C CG1   . VAL A 1 288 ? 24.804 9.825  22.482 1.00 14.59 ? 279 VAL A CG1   1 
ATOM   2069 C CG2   . VAL A 1 288 ? 22.710 9.274  21.175 1.00 17.57 ? 279 VAL A CG2   1 
ATOM   2070 N N     . THR A 1 289 ? 25.336 13.040 21.994 1.00 15.63 ? 280 THR A N     1 
ATOM   2071 C CA    . THR A 1 289 ? 26.560 13.806 22.124 1.00 18.78 ? 280 THR A CA    1 
ATOM   2072 C C     . THR A 1 289 ? 27.271 13.411 23.416 1.00 19.83 ? 280 THR A C     1 
ATOM   2073 O O     . THR A 1 289 ? 26.650 12.950 24.377 1.00 18.63 ? 280 THR A O     1 
ATOM   2074 C CB    . THR A 1 289 ? 26.256 15.310 22.028 1.00 22.44 ? 280 THR A CB    1 
ATOM   2075 O OG1   . THR A 1 289 ? 27.485 16.043 22.021 1.00 20.38 ? 280 THR A OG1   1 
ATOM   2076 C CG2   . THR A 1 289 ? 25.340 15.795 23.165 1.00 19.94 ? 280 THR A CG2   1 
ATOM   2077 N N     . GLN A 1 290 ? 28.587 13.543 23.402 1.00 19.77 ? 281 GLN A N     1 
ATOM   2078 C CA    . GLN A 1 290 ? 29.477 13.011 24.431 1.00 22.47 ? 281 GLN A CA    1 
ATOM   2079 C C     . GLN A 1 290 ? 30.502 14.075 24.806 1.00 19.54 ? 281 GLN A C     1 
ATOM   2080 O O     . GLN A 1 290 ? 30.704 15.031 24.035 1.00 21.27 ? 281 GLN A O     1 
ATOM   2081 C CB    . GLN A 1 290 ? 30.183 11.765 23.903 1.00 21.20 ? 281 GLN A CB    1 
ATOM   2082 C CG    . GLN A 1 290 ? 31.180 12.107 22.815 1.00 19.06 ? 281 GLN A CG    1 
ATOM   2083 C CD    . GLN A 1 290 ? 31.788 10.899 22.161 1.00 25.51 ? 281 GLN A CD    1 
ATOM   2084 O OE1   . GLN A 1 290 ? 31.521 9.760  22.551 1.00 22.04 ? 281 GLN A OE1   1 
ATOM   2085 N NE2   . GLN A 1 290 ? 32.617 11.136 21.146 1.00 24.02 ? 281 GLN A NE2   1 
ATOM   2086 N N     . PRO A 1 291 ? 31.211 13.915 25.937 1.00 19.80 ? 282 PRO A N     1 
ATOM   2087 C CA    . PRO A 1 291 ? 32.226 14.915 26.313 1.00 25.08 ? 282 PRO A CA    1 
ATOM   2088 C C     . PRO A 1 291 ? 33.300 15.111 25.260 1.00 30.69 ? 282 PRO A C     1 
ATOM   2089 O O     . PRO A 1 291 ? 33.629 16.255 24.935 1.00 35.40 ? 282 PRO A O     1 
ATOM   2090 C CB    . PRO A 1 291 ? 32.800 14.340 27.615 1.00 24.76 ? 282 PRO A CB    1 
ATOM   2091 C CG    . PRO A 1 291 ? 31.680 13.525 28.190 1.00 22.65 ? 282 PRO A CG    1 
ATOM   2092 C CD    . PRO A 1 291 ? 30.988 12.920 26.995 1.00 23.26 ? 282 PRO A CD    1 
ATOM   2093 N N     . GLY A 1 292 ? 33.858 14.026 24.715 1.00 29.28 ? 283 GLY A N     1 
ATOM   2094 C CA    . GLY A 1 292 ? 34.843 14.133 23.645 1.00 37.99 ? 283 GLY A CA    1 
ATOM   2095 C C     . GLY A 1 292 ? 35.983 15.097 23.926 1.00 47.18 ? 283 GLY A C     1 
ATOM   2096 O O     . GLY A 1 292 ? 36.211 16.058 23.181 1.00 49.88 ? 283 GLY A O     1 
ATOM   2097 N N     . ASP A 1 293 ? 36.684 14.864 25.030 1.00 42.95 ? 284 ASP A N     1 
ATOM   2098 C CA    . ASP A 1 293 ? 37.859 15.654 25.400 1.00 52.96 ? 284 ASP A CA    1 
ATOM   2099 C C     . ASP A 1 293 ? 38.839 14.661 26.014 1.00 63.36 ? 284 ASP A C     1 
ATOM   2100 O O     . ASP A 1 293 ? 38.737 14.336 27.201 1.00 66.82 ? 284 ASP A O     1 
ATOM   2101 C CB    . ASP A 1 293 ? 37.502 16.782 26.364 1.00 55.55 ? 284 ASP A CB    1 
ATOM   2102 N N     . GLY A 1 294 ? 39.756 14.158 25.191 1.00 54.14 ? 285 GLY A N     1 
ATOM   2103 C CA    . GLY A 1 294 ? 40.660 13.083 25.571 1.00 57.31 ? 285 GLY A CA    1 
ATOM   2104 C C     . GLY A 1 294 ? 41.314 13.181 26.937 1.00 63.16 ? 285 GLY A C     1 
ATOM   2105 O O     . GLY A 1 294 ? 41.096 12.326 27.800 1.00 71.33 ? 285 GLY A O     1 
ATOM   2106 N N     . SER A 1 297 ? 39.410 8.530  27.956 1.00 48.86 ? 288 SER A N     1 
ATOM   2107 C CA    . SER A 1 297 ? 38.051 8.009  28.045 1.00 42.81 ? 288 SER A CA    1 
ATOM   2108 C C     . SER A 1 297 ? 37.541 7.533  26.688 1.00 45.27 ? 288 SER A C     1 
ATOM   2109 O O     . SER A 1 297 ? 36.366 7.187  26.554 1.00 41.42 ? 288 SER A O     1 
ATOM   2110 C CB    . SER A 1 297 ? 37.107 9.078  28.597 1.00 47.37 ? 288 SER A CB    1 
ATOM   2111 O OG    . SER A 1 297 ? 37.450 9.419  29.924 1.00 62.89 ? 288 SER A OG    1 
ATOM   2112 N N     . GLU A 1 298 ? 38.440 7.504  25.699 1.00 39.99 ? 289 GLU A N     1 
ATOM   2113 C CA    . GLU A 1 298 ? 38.035 7.340  24.304 1.00 42.03 ? 289 GLU A CA    1 
ATOM   2114 C C     . GLU A 1 298 ? 37.343 6.002  24.065 1.00 41.96 ? 289 GLU A C     1 
ATOM   2115 O O     . GLU A 1 298 ? 36.309 5.940  23.389 1.00 32.52 ? 289 GLU A O     1 
ATOM   2116 C CB    . GLU A 1 298 ? 39.249 7.478  23.384 1.00 44.13 ? 289 GLU A CB    1 
ATOM   2117 N N     . GLU A 1 299 ? 37.906 4.912  24.589 1.00 35.01 ? 290 GLU A N     1 
ATOM   2118 C CA    . GLU A 1 299 ? 37.321 3.606  24.293 1.00 40.96 ? 290 GLU A CA    1 
ATOM   2119 C C     . GLU A 1 299 ? 35.968 3.450  24.970 1.00 30.47 ? 290 GLU A C     1 
ATOM   2120 O O     . GLU A 1 299 ? 35.020 2.947  24.353 1.00 34.61 ? 290 GLU A O     1 
ATOM   2121 C CB    . GLU A 1 299 ? 38.266 2.476  24.709 1.00 42.99 ? 290 GLU A CB    1 
ATOM   2122 N N     . GLU A 1 300 ? 35.854 3.884  26.228 1.00 33.94 ? 291 GLU A N     1 
ATOM   2123 C CA    . GLU A 1 300 ? 34.587 3.759  26.940 1.00 33.34 ? 291 GLU A CA    1 
ATOM   2124 C C     . GLU A 1 300 ? 33.511 4.624  26.298 1.00 32.76 ? 291 GLU A C     1 
ATOM   2125 O O     . GLU A 1 300 ? 32.357 4.193  26.168 1.00 28.32 ? 291 GLU A O     1 
ATOM   2126 C CB    . GLU A 1 300 ? 34.757 4.131  28.413 1.00 36.13 ? 291 GLU A CB    1 
ATOM   2127 N N     . GLU A 1 301 ? 33.859 5.854  25.912 1.00 26.80 ? 292 GLU A N     1 
ATOM   2128 C CA    . GLU A 1 301 ? 32.878 6.699  25.232 1.00 28.27 ? 292 GLU A CA    1 
ATOM   2129 C C     . GLU A 1 301 ? 32.465 6.101  23.892 1.00 24.94 ? 292 GLU A C     1 
ATOM   2130 O O     . GLU A 1 301 ? 31.276 6.106  23.551 1.00 24.12 ? 292 GLU A O     1 
ATOM   2131 C CB    . GLU A 1 301 ? 33.418 8.126  25.051 1.00 26.85 ? 292 GLU A CB    1 
ATOM   2132 C CG    . GLU A 1 301 ? 33.337 8.955  26.344 1.00 29.16 ? 292 GLU A CG    1 
ATOM   2133 C CD    . GLU A 1 301 ? 33.878 10.382 26.217 1.00 40.14 ? 292 GLU A CD    1 
ATOM   2134 O OE1   . GLU A 1 301 ? 33.660 11.030 25.172 1.00 33.68 ? 292 GLU A OE1   1 
ATOM   2135 O OE2   . GLU A 1 301 ? 34.506 10.875 27.176 1.00 36.14 ? 292 GLU A OE2   1 
ATOM   2136 N N     . ALA A 1 302 ? 33.426 5.576  23.117 1.00 24.77 ? 293 ALA A N     1 
ATOM   2137 C CA    . ALA A 1 302 ? 33.094 4.975  21.828 1.00 27.44 ? 293 ALA A CA    1 
ATOM   2138 C C     . ALA A 1 302 ? 32.183 3.767  21.990 1.00 30.83 ? 293 ALA A C     1 
ATOM   2139 O O     . ALA A 1 302 ? 31.328 3.516  21.136 1.00 25.27 ? 293 ALA A O     1 
ATOM   2140 C CB    . ALA A 1 302 ? 34.368 4.567  21.080 1.00 30.40 ? 293 ALA A CB    1 
ATOM   2141 N N     . ARG A 1 303 ? 32.347 3.006  23.074 1.00 26.64 ? 294 ARG A N     1 
ATOM   2142 C CA    . ARG A 1 303 ? 31.508 1.827  23.251 1.00 25.39 ? 294 ARG A CA    1 
ATOM   2143 C C     . ARG A 1 303 ? 30.087 2.231  23.623 1.00 22.28 ? 294 ARG A C     1 
ATOM   2144 O O     . ARG A 1 303 ? 29.122 1.658  23.098 1.00 23.08 ? 294 ARG A O     1 
ATOM   2145 C CB    . ARG A 1 303 ? 32.118 0.898  24.296 1.00 28.92 ? 294 ARG A CB    1 
ATOM   2146 C CG    . ARG A 1 303 ? 31.164 -0.172 24.786 1.00 30.74 ? 294 ARG A CG    1 
ATOM   2147 C CD    . ARG A 1 303 ? 31.909 -1.194 25.610 1.00 39.11 ? 294 ARG A CD    1 
ATOM   2148 N NE    . ARG A 1 303 ? 32.245 -0.653 26.919 1.00 41.11 ? 294 ARG A NE    1 
ATOM   2149 C CZ    . ARG A 1 303 ? 32.734 -1.366 27.925 1.00 57.37 ? 294 ARG A CZ    1 
ATOM   2150 N NH1   . ARG A 1 303 ? 33.033 -2.650 27.782 1.00 38.00 ? 294 ARG A NH1   1 
ATOM   2151 N NH2   . ARG A 1 303 ? 32.919 -0.778 29.106 1.00 46.17 ? 294 ARG A NH2   1 
ATOM   2152 N N     . LEU A 1 304 ? 29.939 3.270  24.450 1.00 20.76 ? 295 LEU A N     1 
ATOM   2153 C CA    . LEU A 1 304 ? 28.609 3.790  24.772 1.00 19.36 ? 295 LEU A CA    1 
ATOM   2154 C C     . LEU A 1 304 ? 27.903 4.285  23.515 1.00 20.44 ? 295 LEU A C     1 
ATOM   2155 O O     . LEU A 1 304 ? 26.717 3.999  23.297 1.00 20.01 ? 295 LEU A O     1 
ATOM   2156 C CB    . LEU A 1 304 ? 28.714 4.917  25.810 1.00 20.83 ? 295 LEU A CB    1 
ATOM   2157 C CG    . LEU A 1 304 ? 27.424 5.600  26.288 1.00 21.25 ? 295 LEU A CG    1 
ATOM   2158 C CD1   . LEU A 1 304 ? 27.756 6.417  27.530 1.00 36.13 ? 295 LEU A CD1   1 
ATOM   2159 C CD2   . LEU A 1 304 ? 26.854 6.576  25.273 1.00 32.03 ? 295 LEU A CD2   1 
ATOM   2160 N N     . MET A 1 305 ? 28.615 5.055  22.696 1.00 20.09 ? 296 MET A N     1 
ATOM   2161 C CA    . MET A 1 305 ? 28.023 5.619  21.482 1.00 18.25 ? 296 MET A CA    1 
ATOM   2162 C C     . MET A 1 305 ? 27.533 4.512  20.565 1.00 18.88 ? 296 MET A C     1 
ATOM   2163 O O     . MET A 1 305 ? 26.405 4.557  20.049 1.00 17.81 ? 296 MET A O     1 
ATOM   2164 C CB    . MET A 1 305 ? 29.062 6.495  20.781 1.00 22.39 ? 296 MET A CB    1 
ATOM   2165 C CG    . MET A 1 305 ? 28.597 7.390  19.598 1.00 22.89 ? 296 MET A CG    1 
ATOM   2166 S SD    . MET A 1 305 ? 27.474 8.723  20.105 1.00 23.28 ? 296 MET A SD    1 
ATOM   2167 C CE    . MET A 1 305 ? 28.657 9.980  20.682 1.00 20.55 ? 296 MET A CE    1 
ATOM   2168 N N     . ARG A 1 306 ? 28.381 3.498  20.356 1.00 20.31 ? 297 ARG A N     1 
ATOM   2169 C CA    . ARG A 1 306 ? 28.029 2.388  19.472 1.00 22.83 ? 297 ARG A CA    1 
ATOM   2170 C C     . ARG A 1 306 ? 26.881 1.553  20.046 1.00 17.28 ? 297 ARG A C     1 
ATOM   2171 O O     . ARG A 1 306 ? 26.037 1.044  19.285 1.00 21.19 ? 297 ARG A O     1 
ATOM   2172 C CB    . ARG A 1 306 ? 29.276 1.540  19.231 1.00 24.35 ? 297 ARG A CB    1 
ATOM   2173 C CG    . ARG A 1 306 ? 29.042 0.328  18.343 1.00 35.74 ? 297 ARG A CG    1 
ATOM   2174 C CD    . ARG A 1 306 ? 29.013 0.707  16.886 1.00 42.60 ? 297 ARG A CD    1 
ATOM   2175 N NE    . ARG A 1 306 ? 28.054 -0.120 16.164 1.00 41.96 ? 297 ARG A NE    1 
ATOM   2176 C CZ    . ARG A 1 306 ? 28.225 -0.584 14.934 1.00 46.86 ? 297 ARG A CZ    1 
ATOM   2177 N NH1   . ARG A 1 306 ? 29.314 -0.303 14.230 1.00 38.85 ? 297 ARG A NH1   1 
ATOM   2178 N NH2   . ARG A 1 306 ? 27.277 -1.354 14.396 1.00 41.14 ? 297 ARG A NH2   1 
ATOM   2179 N N     . THR A 1 307 ? 26.825 1.395  21.378 1.00 17.67 ? 298 THR A N     1 
ATOM   2180 C CA    . THR A 1 307 ? 25.749 0.618  21.987 1.00 16.04 ? 298 THR A CA    1 
ATOM   2181 C C     . THR A 1 307 ? 24.390 1.286  21.814 1.00 17.71 ? 298 THR A C     1 
ATOM   2182 O O     . THR A 1 307 ? 23.393 0.617  21.512 1.00 17.90 ? 298 THR A O     1 
ATOM   2183 C CB    . THR A 1 307 ? 26.045 0.418  23.475 1.00 22.73 ? 298 THR A CB    1 
ATOM   2184 O OG1   . THR A 1 307 ? 27.319 -0.226 23.630 1.00 23.84 ? 298 THR A OG1   1 
ATOM   2185 C CG2   . THR A 1 307 ? 24.983 -0.466 24.082 1.00 19.84 ? 298 THR A CG2   1 
ATOM   2186 N N     . LEU A 1 308 ? 24.323 2.616  21.999 1.00 18.21 ? 299 LEU A N     1 
ATOM   2187 C CA    . LEU A 1 308 ? 23.074 3.331  21.731 1.00 18.76 ? 299 LEU A CA    1 
ATOM   2188 C C     . LEU A 1 308 ? 22.703 3.284  20.247 1.00 16.89 ? 299 LEU A C     1 
ATOM   2189 O O     . LEU A 1 308 ? 21.534 3.070  19.904 1.00 15.97 ? 299 LEU A O     1 
ATOM   2190 C CB    . LEU A 1 308 ? 23.191 4.786  22.218 1.00 14.79 ? 299 LEU A CB    1 
ATOM   2191 C CG    . LEU A 1 308 ? 23.526 4.870  23.704 1.00 16.85 ? 299 LEU A CG    1 
ATOM   2192 C CD1   . LEU A 1 308 ? 23.681 6.323  24.066 1.00 22.08 ? 299 LEU A CD1   1 
ATOM   2193 C CD2   . LEU A 1 308 ? 22.414 4.224  24.526 1.00 17.72 ? 299 LEU A CD2   1 
ATOM   2194 N N     . ARG A 1 309 ? 23.682 3.448  19.352 1.00 16.20 ? 300 ARG A N     1 
ATOM   2195 C CA    . ARG A 1 309 ? 23.396 3.355  17.922 1.00 16.85 ? 300 ARG A CA    1 
ATOM   2196 C C     . ARG A 1 309 ? 22.795 1.997  17.594 1.00 17.82 ? 300 ARG A C     1 
ATOM   2197 O O     . ARG A 1 309 ? 21.762 1.905  16.917 1.00 18.58 ? 300 ARG A O     1 
ATOM   2198 C CB    . ARG A 1 309 ? 24.674 3.596  17.119 1.00 14.95 ? 300 ARG A CB    1 
ATOM   2199 C CG    . ARG A 1 309 ? 24.452 3.753  15.609 1.00 14.94 ? 300 ARG A CG    1 
ATOM   2200 C CD    . ARG A 1 309 ? 24.451 2.398  14.872 1.00 18.89 ? 300 ARG A CD    1 
ATOM   2201 N NE    . ARG A 1 309 ? 24.928 2.576  13.496 1.00 17.56 ? 300 ARG A NE    1 
ATOM   2202 C CZ    . ARG A 1 309 ? 24.289 3.275  12.560 1.00 21.93 ? 300 ARG A CZ    1 
ATOM   2203 N NH1   . ARG A 1 309 ? 23.043 3.716  12.739 1.00 18.65 ? 300 ARG A NH1   1 
ATOM   2204 N NH2   . ARG A 1 309 ? 24.916 3.552  11.421 1.00 21.17 ? 300 ARG A NH2   1 
ATOM   2205 N N     . ASN A 1 310 ? 23.417 0.929  18.103 1.00 17.86 ? 301 ASN A N     1 
ATOM   2206 C CA    . ASN A 1 310 ? 22.952 -0.424 17.789 1.00 18.31 ? 301 ASN A CA    1 
ATOM   2207 C C     . ASN A 1 310 ? 21.544 -0.678 18.319 1.00 17.54 ? 301 ASN A C     1 
ATOM   2208 O O     . ASN A 1 310 ? 20.802 -1.491 17.755 1.00 19.50 ? 301 ASN A O     1 
ATOM   2209 C CB    . ASN A 1 310 ? 23.910 -1.466 18.379 1.00 19.48 ? 301 ASN A CB    1 
ATOM   2210 C CG    . ASN A 1 310 ? 25.203 -1.613 17.582 1.00 18.25 ? 301 ASN A CG    1 
ATOM   2211 O OD1   . ASN A 1 310 ? 25.302 -1.181 16.441 1.00 21.54 ? 301 ASN A OD1   1 
ATOM   2212 N ND2   . ASN A 1 310 ? 26.196 -2.245 18.193 1.00 21.20 ? 301 ASN A ND2   1 
ATOM   2213 N N     . ALA A 1 311 ? 21.159 -0.010 19.400 1.00 17.09 ? 302 ALA A N     1 
ATOM   2214 C CA    . ALA A 1 311 ? 19.840 -0.243 19.973 1.00 16.45 ? 302 ALA A CA    1 
ATOM   2215 C C     . ALA A 1 311 ? 18.727 0.536  19.277 1.00 16.59 ? 302 ALA A C     1 
ATOM   2216 O O     . ALA A 1 311 ? 17.552 0.231  19.493 1.00 18.49 ? 302 ALA A O     1 
ATOM   2217 C CB    . ALA A 1 311 ? 19.850 0.127  21.466 1.00 17.53 ? 302 ALA A CB    1 
ATOM   2218 N N     . TYR A 1 312 ? 19.060 1.576  18.528 1.00 15.66 ? 303 TYR A N     1 
ATOM   2219 C CA    . TYR A 1 312 ? 18.068 2.480  17.959 1.00 16.54 ? 303 TYR A CA    1 
ATOM   2220 C C     . TYR A 1 312 ? 17.740 2.069  16.522 1.00 15.49 ? 303 TYR A C     1 
ATOM   2221 O O     . TYR A 1 312 ? 18.654 1.912  15.702 1.00 18.34 ? 303 TYR A O     1 
ATOM   2222 C CB    . TYR A 1 312 ? 18.582 3.929  18.000 1.00 17.70 ? 303 TYR A CB    1 
ATOM   2223 C CG    . TYR A 1 312 ? 17.658 4.836  17.236 1.00 14.23 ? 303 TYR A CG    1 
ATOM   2224 C CD1   . TYR A 1 312 ? 16.322 4.938  17.598 1.00 16.21 ? 303 TYR A CD1   1 
ATOM   2225 C CD2   . TYR A 1 312 ? 18.119 5.579  16.170 1.00 15.77 ? 303 TYR A CD2   1 
ATOM   2226 C CE1   . TYR A 1 312 ? 15.444 5.736  16.894 1.00 16.85 ? 303 TYR A CE1   1 
ATOM   2227 C CE2   . TYR A 1 312 ? 17.252 6.398  15.461 1.00 18.06 ? 303 TYR A CE2   1 
ATOM   2228 C CZ    . TYR A 1 312 ? 15.925 6.448  15.810 1.00 19.89 ? 303 TYR A CZ    1 
ATOM   2229 O OH    . TYR A 1 312 ? 15.057 7.217  15.079 1.00 17.73 ? 303 TYR A OH    1 
ATOM   2230 N N     . GLN A 1 313 ? 16.439 1.952  16.220 1.00 17.76 ? 304 GLN A N     1 
ATOM   2231 C CA    . GLN A 1 313 ? 15.947 1.647  14.871 1.00 15.53 ? 304 GLN A CA    1 
ATOM   2232 C C     . GLN A 1 313 ? 15.842 2.933  14.060 1.00 15.29 ? 304 GLN A C     1 
ATOM   2233 O O     . GLN A 1 313 ? 14.759 3.479  13.848 1.00 22.38 ? 304 GLN A O     1 
ATOM   2234 C CB    . GLN A 1 313 ? 14.595 0.950  14.938 1.00 16.26 ? 304 GLN A CB    1 
ATOM   2235 C CG    . GLN A 1 313 ? 14.634 -0.324 15.745 1.00 21.50 ? 304 GLN A CG    1 
ATOM   2236 C CD    . GLN A 1 313 ? 13.288 -1.010 15.790 1.00 24.69 ? 304 GLN A CD    1 
ATOM   2237 O OE1   . GLN A 1 313 ? 12.378 -0.694 15.009 1.00 29.92 ? 304 GLN A OE1   1 
ATOM   2238 N NE2   . GLN A 1 313 ? 13.149 -1.956 16.717 1.00 28.60 ? 304 GLN A NE2   1 
ATOM   2239 N N     . GLY A 1 314 ? 16.977 3.400  13.554 1.00 15.63 ? 305 GLY A N     1 
ATOM   2240 C CA    . GLY A 1 314 ? 16.920 4.541  12.652 1.00 18.02 ? 305 GLY A CA    1 
ATOM   2241 C C     . GLY A 1 314 ? 18.276 5.223  12.509 1.00 16.28 ? 305 GLY A C     1 
ATOM   2242 O O     . GLY A 1 314 ? 19.321 4.627  12.760 1.00 17.87 ? 305 GLY A O     1 
ATOM   2243 N N     . THR A 1 315 ? 18.210 6.453  12.000 1.00 16.59 ? 306 THR A N     1 
ATOM   2244 C CA    . THR A 1 315 ? 19.397 7.216  11.652 1.00 16.16 ? 306 THR A CA    1 
ATOM   2245 C C     . THR A 1 315 ? 20.069 7.729  12.922 1.00 15.50 ? 306 THR A C     1 
ATOM   2246 O O     . THR A 1 315 ? 19.391 8.215  13.817 1.00 15.88 ? 306 THR A O     1 
ATOM   2247 C CB    . THR A 1 315 ? 18.985 8.390  10.764 1.00 16.14 ? 306 THR A CB    1 
ATOM   2248 O OG1   . THR A 1 315 ? 18.404 7.892  9.530  1.00 16.84 ? 306 THR A OG1   1 
ATOM   2249 C CG2   . THR A 1 315 ? 20.153 9.338  10.474 1.00 16.83 ? 306 THR A CG2   1 
ATOM   2250 N N     . PHE A 1 316 ? 21.398 7.672  12.966 1.00 15.73 ? 307 PHE A N     1 
ATOM   2251 C CA    . PHE A 1 316 ? 22.155 8.021  14.169 1.00 16.34 ? 307 PHE A CA    1 
ATOM   2252 C C     . PHE A 1 316 ? 23.189 9.093  13.846 1.00 17.31 ? 307 PHE A C     1 
ATOM   2253 O O     . PHE A 1 316 ? 24.001 8.929  12.924 1.00 15.74 ? 307 PHE A O     1 
ATOM   2254 C CB    . PHE A 1 316 ? 22.838 6.778  14.735 1.00 17.14 ? 307 PHE A CB    1 
ATOM   2255 C CG    . PHE A 1 316 ? 23.408 6.964  16.120 1.00 16.15 ? 307 PHE A CG    1 
ATOM   2256 C CD1   . PHE A 1 316 ? 22.601 6.762  17.240 1.00 16.97 ? 307 PHE A CD1   1 
ATOM   2257 C CD2   . PHE A 1 316 ? 24.741 7.321  16.293 1.00 17.99 ? 307 PHE A CD2   1 
ATOM   2258 C CE1   . PHE A 1 316 ? 23.117 6.905  18.529 1.00 16.00 ? 307 PHE A CE1   1 
ATOM   2259 C CE2   . PHE A 1 316 ? 25.264 7.492  17.584 1.00 18.61 ? 307 PHE A CE2   1 
ATOM   2260 C CZ    . PHE A 1 316 ? 24.443 7.268  18.701 1.00 16.82 ? 307 PHE A CZ    1 
ATOM   2261 N N     . ILE A 1 317 ? 23.157 10.188 14.610 1.00 14.96 ? 308 ILE A N     1 
ATOM   2262 C CA    . ILE A 1 317 ? 24.135 11.268 14.510 1.00 14.36 ? 308 ILE A CA    1 
ATOM   2263 C C     . ILE A 1 317 ? 25.014 11.223 15.755 1.00 17.67 ? 308 ILE A C     1 
ATOM   2264 O O     . ILE A 1 317 ? 24.508 11.338 16.879 1.00 15.71 ? 308 ILE A O     1 
ATOM   2265 C CB    . ILE A 1 317 ? 23.468 12.654 14.386 1.00 16.29 ? 308 ILE A CB    1 
ATOM   2266 C CG1   . ILE A 1 317 ? 22.353 12.658 13.326 1.00 16.06 ? 308 ILE A CG1   1 
ATOM   2267 C CG2   . ILE A 1 317 ? 24.549 13.725 14.140 1.00 14.97 ? 308 ILE A CG2   1 
ATOM   2268 C CD1   . ILE A 1 317 ? 21.803 14.074 12.969 1.00 18.89 ? 308 ILE A CD1   1 
ATOM   2269 N N     . CYS A 1 318 ? 26.325 11.072 15.560 1.00 16.12 ? 309 CYS A N     1 
ATOM   2270 C CA    . CYS A 1 318 ? 27.276 11.121 16.659 1.00 16.35 ? 309 CYS A CA    1 
ATOM   2271 C C     . CYS A 1 318 ? 27.897 12.508 16.746 1.00 16.67 ? 309 CYS A C     1 
ATOM   2272 O O     . CYS A 1 318 ? 28.056 13.211 15.741 1.00 20.47 ? 309 CYS A O     1 
ATOM   2273 C CB    . CYS A 1 318 ? 28.357 10.057 16.517 1.00 19.30 ? 309 CYS A CB    1 
ATOM   2274 S SG    . CYS A 1 318 ? 29.397 10.192 15.087 1.00 21.47 ? 309 CYS A SG    1 
ATOM   2275 N N     . SER A 1 319 ? 28.273 12.881 17.964 1.00 17.45 ? 310 SER A N     1 
ATOM   2276 C CA    . SER A 1 319 ? 28.674 14.247 18.252 1.00 16.48 ? 310 SER A CA    1 
ATOM   2277 C C     . SER A 1 319 ? 29.610 14.309 19.443 1.00 17.06 ? 310 SER A C     1 
ATOM   2278 O O     . SER A 1 319 ? 29.388 13.612 20.429 1.00 17.60 ? 310 SER A O     1 
ATOM   2279 C CB    . SER A 1 319 ? 27.444 15.097 18.565 1.00 17.20 ? 310 SER A CB    1 
ATOM   2280 O OG    . SER A 1 319 ? 27.835 16.249 19.299 1.00 19.11 ? 310 SER A OG    1 
ATOM   2281 N N     . GLY A 1 320 ? 30.629 15.171 19.355 1.00 17.45 ? 311 GLY A N     1 
ATOM   2282 C CA    . GLY A 1 320 ? 31.468 15.471 20.509 1.00 17.47 ? 311 GLY A CA    1 
ATOM   2283 C C     . GLY A 1 320 ? 32.926 15.108 20.293 1.00 22.00 ? 311 GLY A C     1 
ATOM   2284 O O     . GLY A 1 320 ? 33.304 13.941 20.414 1.00 22.93 ? 311 GLY A O     1 
ATOM   2285 N N     . GLY A 1 321 ? 33.755 16.102 19.977 1.00 17.82 ? 312 GLY A N     1 
ATOM   2286 C CA    . GLY A 1 321 ? 35.180 15.890 19.771 1.00 19.31 ? 312 GLY A CA    1 
ATOM   2287 C C     . GLY A 1 321 ? 35.566 15.160 18.502 1.00 21.01 ? 312 GLY A C     1 
ATOM   2288 O O     . GLY A 1 321 ? 36.720 14.737 18.380 1.00 23.71 ? 312 GLY A O     1 
ATOM   2289 N N     . TYR A 1 322 ? 34.657 14.998 17.543 1.00 20.62 ? 313 TYR A N     1 
ATOM   2290 C CA    . TYR A 1 322 ? 35.018 14.292 16.321 1.00 21.76 ? 313 TYR A CA    1 
ATOM   2291 C C     . TYR A 1 322 ? 35.971 15.129 15.488 1.00 24.77 ? 313 TYR A C     1 
ATOM   2292 O O     . TYR A 1 322 ? 35.881 16.359 15.448 1.00 21.60 ? 313 TYR A O     1 
ATOM   2293 C CB    . TYR A 1 322 ? 33.766 13.921 15.513 1.00 20.04 ? 313 TYR A CB    1 
ATOM   2294 C CG    . TYR A 1 322 ? 33.106 12.725 16.146 1.00 17.92 ? 313 TYR A CG    1 
ATOM   2295 C CD1   . TYR A 1 322 ? 32.159 12.885 17.154 1.00 19.37 ? 313 TYR A CD1   1 
ATOM   2296 C CD2   . TYR A 1 322 ? 33.476 11.421 15.782 1.00 21.97 ? 313 TYR A CD2   1 
ATOM   2297 C CE1   . TYR A 1 322 ? 31.603 11.799 17.780 1.00 22.31 ? 313 TYR A CE1   1 
ATOM   2298 C CE2   . TYR A 1 322 ? 32.906 10.318 16.403 1.00 26.91 ? 313 TYR A CE2   1 
ATOM   2299 C CZ    . TYR A 1 322 ? 31.963 10.518 17.391 1.00 22.58 ? 313 TYR A CZ    1 
ATOM   2300 O OH    . TYR A 1 322 ? 31.389 9.464  18.048 1.00 25.35 ? 313 TYR A OH    1 
ATOM   2301 N N     . THR A 1 323 ? 36.934 14.447 14.883 1.00 28.42 ? 314 THR A N     1 
ATOM   2302 C CA    . THR A 1 323 ? 37.869 15.015 13.931 1.00 26.55 ? 314 THR A CA    1 
ATOM   2303 C C     . THR A 1 323 ? 37.455 14.597 12.533 1.00 25.23 ? 314 THR A C     1 
ATOM   2304 O O     . THR A 1 323 ? 36.515 13.824 12.338 1.00 23.88 ? 314 THR A O     1 
ATOM   2305 C CB    . THR A 1 323 ? 39.286 14.524 14.236 1.00 22.04 ? 314 THR A CB    1 
ATOM   2306 O OG1   . THR A 1 323 ? 39.317 13.098 14.069 1.00 24.68 ? 314 THR A OG1   1 
ATOM   2307 C CG2   . THR A 1 323 ? 39.649 14.851 15.678 1.00 24.51 ? 314 THR A CG2   1 
ATOM   2308 N N     . ARG A 1 324 ? 38.188 15.092 11.538 1.00 21.37 ? 315 ARG A N     1 
ATOM   2309 C CA    . ARG A 1 324 ? 38.002 14.574 10.196 1.00 23.27 ? 315 ARG A CA    1 
ATOM   2310 C C     . ARG A 1 324 ? 38.198 13.061 10.166 1.00 26.33 ? 315 ARG A C     1 
ATOM   2311 O O     . ARG A 1 324 ? 37.341 12.313 9.683  1.00 22.04 ? 315 ARG A O     1 
ATOM   2312 C CB    . ARG A 1 324 ? 38.982 15.270 9.255  1.00 25.35 ? 315 ARG A CB    1 
ATOM   2313 C CG    . ARG A 1 324 ? 38.909 14.758 7.845  1.00 28.50 ? 315 ARG A CG    1 
ATOM   2314 C CD    . ARG A 1 324 ? 39.874 15.480 6.938  1.00 24.75 ? 315 ARG A CD    1 
ATOM   2315 N NE    . ARG A 1 324 ? 39.694 15.025 5.565  1.00 29.25 ? 315 ARG A NE    1 
ATOM   2316 C CZ    . ARG A 1 324 ? 40.255 13.937 5.055  1.00 31.52 ? 315 ARG A CZ    1 
ATOM   2317 N NH1   . ARG A 1 324 ? 41.092 13.196 5.762  1.00 35.03 ? 315 ARG A NH1   1 
ATOM   2318 N NH2   . ARG A 1 324 ? 39.966 13.585 3.807  1.00 34.15 ? 315 ARG A NH2   1 
ATOM   2319 N N     . GLU A 1 325 ? 39.307 12.591 10.737 1.00 26.12 ? 316 GLU A N     1 
ATOM   2320 C CA    . GLU A 1 325 ? 39.642 11.174 10.677 1.00 26.61 ? 316 GLU A CA    1 
ATOM   2321 C C     . GLU A 1 325 ? 38.643 10.329 11.463 1.00 24.67 ? 316 GLU A C     1 
ATOM   2322 O O     . GLU A 1 325 ? 38.258 9.245  11.015 1.00 23.89 ? 316 GLU A O     1 
ATOM   2323 C CB    . GLU A 1 325 ? 41.066 10.968 11.207 1.00 30.09 ? 316 GLU A CB    1 
ATOM   2324 C CG    . GLU A 1 325 ? 42.186 11.641 10.367 1.00 41.70 ? 316 GLU A CG    1 
ATOM   2325 C CD    . GLU A 1 325 ? 42.069 13.180 10.213 1.00 49.70 ? 316 GLU A CD    1 
ATOM   2326 O OE1   . GLU A 1 325 ? 41.772 13.893 11.224 1.00 36.38 ? 316 GLU A OE1   1 
ATOM   2327 O OE2   . GLU A 1 325 ? 42.281 13.669 9.061  1.00 40.45 ? 316 GLU A OE2   1 
ATOM   2328 N N     . LEU A 1 326 ? 38.210 10.806 12.633 1.00 24.24 ? 317 LEU A N     1 
ATOM   2329 C CA    . LEU A 1 326 ? 37.286 10.019 13.450 1.00 26.58 ? 317 LEU A CA    1 
ATOM   2330 C C     . LEU A 1 326 ? 35.880 10.027 12.866 1.00 25.82 ? 317 LEU A C     1 
ATOM   2331 O O     . LEU A 1 326 ? 35.132 9.053  13.034 1.00 23.77 ? 317 LEU A O     1 
ATOM   2332 C CB    . LEU A 1 326 ? 37.261 10.533 14.892 1.00 25.64 ? 317 LEU A CB    1 
ATOM   2333 C CG    . LEU A 1 326 ? 38.477 10.265 15.789 1.00 30.56 ? 317 LEU A CG    1 
ATOM   2334 C CD1   . LEU A 1 326 ? 38.454 11.172 17.016 1.00 33.65 ? 317 LEU A CD1   1 
ATOM   2335 C CD2   . LEU A 1 326 ? 38.549 8.802  16.203 1.00 34.14 ? 317 LEU A CD2   1 
ATOM   2336 N N     . GLY A 1 327 ? 35.500 11.111 12.187 1.00 21.58 ? 318 GLY A N     1 
ATOM   2337 C CA    . GLY A 1 327 ? 34.238 11.106 11.478 1.00 23.77 ? 318 GLY A CA    1 
ATOM   2338 C C     . GLY A 1 327 ? 34.247 10.120 10.329 1.00 20.47 ? 318 GLY A C     1 
ATOM   2339 O O     . GLY A 1 327 ? 33.284 9.372  10.133 1.00 22.72 ? 318 GLY A O     1 
ATOM   2340 N N     . ILE A 1 328 ? 35.341 10.094 9.557  1.00 21.52 ? 319 ILE A N     1 
ATOM   2341 C CA    . ILE A 1 328 ? 35.443 9.154  8.438  1.00 21.18 ? 319 ILE A CA    1 
ATOM   2342 C C     . ILE A 1 328 ? 35.317 7.725  8.950  1.00 22.95 ? 319 ILE A C     1 
ATOM   2343 O O     . ILE A 1 328 ? 34.555 6.914  8.403  1.00 24.19 ? 319 ILE A O     1 
ATOM   2344 C CB    . ILE A 1 328 ? 36.766 9.368  7.676  1.00 24.88 ? 319 ILE A CB    1 
ATOM   2345 C CG1   . ILE A 1 328 ? 36.728 10.673 6.887  1.00 24.10 ? 319 ILE A CG1   1 
ATOM   2346 C CG2   . ILE A 1 328 ? 37.043 8.187  6.751  1.00 29.76 ? 319 ILE A CG2   1 
ATOM   2347 C CD1   . ILE A 1 328 ? 38.075 11.120 6.342  1.00 26.94 ? 319 ILE A CD1   1 
ATOM   2348 N N     . GLU A 1 329 ? 36.042 7.412  10.035 1.00 27.04 ? 320 GLU A N     1 
ATOM   2349 C CA    . GLU A 1 329 ? 36.012 6.073  10.623 1.00 25.78 ? 320 GLU A CA    1 
ATOM   2350 C C     . GLU A 1 329 ? 34.623 5.722  11.137 1.00 25.95 ? 320 GLU A C     1 
ATOM   2351 O O     . GLU A 1 329 ? 34.160 4.591  10.971 1.00 25.12 ? 320 GLU A O     1 
ATOM   2352 C CB    . GLU A 1 329 ? 37.027 5.972  11.757 1.00 31.52 ? 320 GLU A CB    1 
ATOM   2353 N N     . ALA A 1 330 ? 33.943 6.681  11.760 1.00 24.58 ? 321 ALA A N     1 
ATOM   2354 C CA    . ALA A 1 330 ? 32.623 6.400  12.321 1.00 24.40 ? 321 ALA A CA    1 
ATOM   2355 C C     . ALA A 1 330 ? 31.657 5.947  11.235 1.00 25.11 ? 321 ALA A C     1 
ATOM   2356 O O     . ALA A 1 330 ? 30.915 4.975  11.413 1.00 23.81 ? 321 ALA A O     1 
ATOM   2357 C CB    . ALA A 1 330 ? 32.086 7.641  13.038 1.00 23.96 ? 321 ALA A CB    1 
ATOM   2358 N N     . VAL A 1 331 ? 31.647 6.649  10.100 1.00 19.13 ? 322 VAL A N     1 
ATOM   2359 C CA    . VAL A 1 331 ? 30.742 6.273  9.019  1.00 19.93 ? 322 VAL A CA    1 
ATOM   2360 C C     . VAL A 1 331 ? 31.214 4.988  8.359  1.00 23.40 ? 322 VAL A C     1 
ATOM   2361 O O     . VAL A 1 331 ? 30.411 4.086  8.085  1.00 25.78 ? 322 VAL A O     1 
ATOM   2362 C CB    . VAL A 1 331 ? 30.612 7.423  8.007  1.00 19.97 ? 322 VAL A CB    1 
ATOM   2363 C CG1   . VAL A 1 331 ? 29.780 6.978  6.828  1.00 24.01 ? 322 VAL A CG1   1 
ATOM   2364 C CG2   . VAL A 1 331 ? 29.956 8.623  8.689  1.00 23.80 ? 322 VAL A CG2   1 
ATOM   2365 N N     . ALA A 1 332 ? 32.524 4.870  8.132  1.00 23.32 ? 323 ALA A N     1 
ATOM   2366 C CA    . ALA A 1 332 ? 33.067 3.717  7.423  1.00 25.67 ? 323 ALA A CA    1 
ATOM   2367 C C     . ALA A 1 332 ? 32.796 2.419  8.171  1.00 23.15 ? 323 ALA A C     1 
ATOM   2368 O O     . ALA A 1 332 ? 32.527 1.379  7.550  1.00 27.37 ? 323 ALA A O     1 
ATOM   2369 C CB    . ALA A 1 332 ? 34.569 3.895  7.200  1.00 30.88 ? 323 ALA A CB    1 
ATOM   2370 N N     . GLN A 1 333 ? 32.861 2.463  9.496  1.00 22.77 ? 324 GLN A N     1 
ATOM   2371 C CA    . GLN A 1 333 ? 32.673 1.304  10.363 1.00 23.34 ? 324 GLN A CA    1 
ATOM   2372 C C     . GLN A 1 333 ? 31.215 1.047  10.704 1.00 26.00 ? 324 GLN A C     1 
ATOM   2373 O O     . GLN A 1 333 ? 30.925 0.093  11.434 1.00 28.84 ? 324 GLN A O     1 
ATOM   2374 C CB    . GLN A 1 333 ? 33.466 1.501  11.653 1.00 28.22 ? 324 GLN A CB    1 
ATOM   2375 C CG    . GLN A 1 333 ? 34.965 1.518  11.419 1.00 29.80 ? 324 GLN A CG    1 
ATOM   2376 C CD    . GLN A 1 333 ? 35.764 1.796  12.669 1.00 44.74 ? 324 GLN A CD    1 
ATOM   2377 O OE1   . GLN A 1 333 ? 35.210 1.935  13.753 1.00 44.89 ? 324 GLN A OE1   1 
ATOM   2378 N NE2   . GLN A 1 333 ? 37.084 1.878  12.523 1.00 47.92 ? 324 GLN A NE2   1 
ATOM   2379 N N     . GLY A 1 334 ? 30.296 1.876  10.211 1.00 25.05 ? 325 GLY A N     1 
ATOM   2380 C CA    . GLY A 1 334 ? 28.898 1.723  10.536 1.00 23.88 ? 325 GLY A CA    1 
ATOM   2381 C C     . GLY A 1 334 ? 28.525 2.173  11.930 1.00 24.25 ? 325 GLY A C     1 
ATOM   2382 O O     . GLY A 1 334 ? 27.421 1.853  12.392 1.00 26.94 ? 325 GLY A O     1 
ATOM   2383 N N     . ASP A 1 335 ? 29.418 2.903  12.615 1.00 24.64 ? 326 ASP A N     1 
ATOM   2384 C CA    . ASP A 1 335 ? 29.160 3.383  13.973 1.00 21.97 ? 326 ASP A CA    1 
ATOM   2385 C C     . ASP A 1 335 ? 28.136 4.506  14.013 1.00 22.25 ? 326 ASP A C     1 
ATOM   2386 O O     . ASP A 1 335 ? 27.491 4.714  15.043 1.00 23.17 ? 326 ASP A O     1 
ATOM   2387 C CB    . ASP A 1 335 ? 30.434 3.916  14.616 1.00 26.30 ? 326 ASP A CB    1 
ATOM   2388 C CG    . ASP A 1 335 ? 31.491 2.844  14.816 1.00 44.39 ? 326 ASP A CG    1 
ATOM   2389 O OD1   . ASP A 1 335 ? 31.166 1.631  14.709 1.00 37.55 ? 326 ASP A OD1   1 
ATOM   2390 O OD2   . ASP A 1 335 ? 32.649 3.229  15.104 1.00 41.18 ? 326 ASP A OD2   1 
ATOM   2391 N N     . ALA A 1 336 ? 28.033 5.274  12.939 1.00 21.72 ? 327 ALA A N     1 
ATOM   2392 C CA    . ALA A 1 336 ? 27.100 6.379  12.863 1.00 18.13 ? 327 ALA A CA    1 
ATOM   2393 C C     . ALA A 1 336 ? 26.760 6.597  11.409 1.00 17.82 ? 327 ALA A C     1 
ATOM   2394 O O     . ALA A 1 336 ? 27.520 6.217  10.525 1.00 21.39 ? 327 ALA A O     1 
ATOM   2395 C CB    . ALA A 1 336 ? 27.686 7.665  13.446 1.00 19.05 ? 327 ALA A CB    1 
ATOM   2396 N N     . ASP A 1 337 ? 25.607 7.218  11.181 1.00 15.47 ? 328 ASP A N     1 
ATOM   2397 C CA    . ASP A 1 337 ? 25.227 7.611  9.829  1.00 15.90 ? 328 ASP A CA    1 
ATOM   2398 C C     . ASP A 1 337 ? 25.660 9.023  9.484  1.00 17.71 ? 328 ASP A C     1 
ATOM   2399 O O     . ASP A 1 337 ? 26.053 9.289  8.343  1.00 18.24 ? 328 ASP A O     1 
ATOM   2400 C CB    . ASP A 1 337 ? 23.723 7.472  9.662  1.00 18.45 ? 328 ASP A CB    1 
ATOM   2401 C CG    . ASP A 1 337 ? 23.254 6.071  9.992  1.00 24.26 ? 328 ASP A CG    1 
ATOM   2402 O OD1   . ASP A 1 337 ? 23.689 5.113  9.299  1.00 19.37 ? 328 ASP A OD1   1 
ATOM   2403 O OD2   . ASP A 1 337 ? 22.440 5.945  10.919 1.00 19.58 ? 328 ASP A OD2   1 
ATOM   2404 N N     . LEU A 1 338 ? 25.596 9.934  10.446 1.00 15.11 ? 329 LEU A N     1 
ATOM   2405 C CA    . LEU A 1 338 ? 25.960 11.327 10.258 1.00 14.61 ? 329 LEU A CA    1 
ATOM   2406 C C     . LEU A 1 338 ? 26.844 11.742 11.416 1.00 15.55 ? 329 LEU A C     1 
ATOM   2407 O O     . LEU A 1 338 ? 26.737 11.175 12.509 1.00 16.75 ? 329 LEU A O     1 
ATOM   2408 C CB    . LEU A 1 338 ? 24.726 12.242 10.229 1.00 18.56 ? 329 LEU A CB    1 
ATOM   2409 C CG    . LEU A 1 338 ? 23.645 11.837 9.230  1.00 18.40 ? 329 LEU A CG    1 
ATOM   2410 C CD1   . LEU A 1 338 ? 22.356 12.562 9.496  1.00 20.46 ? 329 LEU A CD1   1 
ATOM   2411 C CD2   . LEU A 1 338 ? 24.123 12.202 7.836  1.00 19.35 ? 329 LEU A CD2   1 
ATOM   2412 N N     . VAL A 1 339 ? 27.698 12.736 11.174 1.00 16.97 ? 330 VAL A N     1 
ATOM   2413 C CA    . VAL A 1 339 ? 28.642 13.224 12.176 1.00 16.63 ? 330 VAL A CA    1 
ATOM   2414 C C     . VAL A 1 339 ? 28.449 14.726 12.317 1.00 13.49 ? 330 VAL A C     1 
ATOM   2415 O O     . VAL A 1 339 ? 28.604 15.458 11.336 1.00 16.64 ? 330 VAL A O     1 
ATOM   2416 C CB    . VAL A 1 339 ? 30.100 12.894 11.795 1.00 16.89 ? 330 VAL A CB    1 
ATOM   2417 C CG1   . VAL A 1 339 ? 31.059 13.370 12.893 1.00 20.48 ? 330 VAL A CG1   1 
ATOM   2418 C CG2   . VAL A 1 339 ? 30.257 11.385 11.565 1.00 17.87 ? 330 VAL A CG2   1 
ATOM   2419 N N     . SER A 1 340 ? 28.138 15.204 13.529 1.00 14.39 ? 331 SER A N     1 
ATOM   2420 C CA    . SER A 1 340 ? 27.962 16.643 13.707 1.00 11.77 ? 331 SER A CA    1 
ATOM   2421 C C     . SER A 1 340 ? 29.203 17.261 14.333 1.00 15.94 ? 331 SER A C     1 
ATOM   2422 O O     . SER A 1 340 ? 29.863 16.659 15.190 1.00 18.42 ? 331 SER A O     1 
ATOM   2423 C CB    . SER A 1 340 ? 26.711 16.989 14.527 1.00 17.25 ? 331 SER A CB    1 
ATOM   2424 O OG    . SER A 1 340 ? 26.830 16.610 15.896 1.00 17.40 ? 331 SER A OG    1 
ATOM   2425 N N     . TYR A 1 341 ? 29.518 18.464 13.873 1.00 16.24 ? 332 TYR A N     1 
ATOM   2426 C CA    . TYR A 1 341 ? 30.660 19.229 14.338 1.00 17.16 ? 332 TYR A CA    1 
ATOM   2427 C C     . TYR A 1 341 ? 30.153 20.554 14.870 1.00 17.87 ? 332 TYR A C     1 
ATOM   2428 O O     . TYR A 1 341 ? 29.369 21.233 14.196 1.00 17.06 ? 332 TYR A O     1 
ATOM   2429 C CB    . TYR A 1 341 ? 31.668 19.475 13.202 1.00 17.32 ? 332 TYR A CB    1 
ATOM   2430 C CG    . TYR A 1 341 ? 32.304 18.212 12.668 1.00 17.80 ? 332 TYR A CG    1 
ATOM   2431 C CD1   . TYR A 1 341 ? 31.663 17.456 11.682 1.00 17.34 ? 332 TYR A CD1   1 
ATOM   2432 C CD2   . TYR A 1 341 ? 33.547 17.779 13.124 1.00 20.26 ? 332 TYR A CD2   1 
ATOM   2433 C CE1   . TYR A 1 341 ? 32.224 16.276 11.178 1.00 18.24 ? 332 TYR A CE1   1 
ATOM   2434 C CE2   . TYR A 1 341 ? 34.132 16.594 12.609 1.00 18.13 ? 332 TYR A CE2   1 
ATOM   2435 C CZ    . TYR A 1 341 ? 33.457 15.864 11.648 1.00 19.40 ? 332 TYR A CZ    1 
ATOM   2436 O OH    . TYR A 1 341 ? 34.002 14.704 11.144 1.00 21.51 ? 332 TYR A OH    1 
ATOM   2437 N N     . GLY A 1 342 ? 30.634 20.932 16.043 1.00 16.21 ? 333 GLY A N     1 
ATOM   2438 C CA    . GLY A 1 342 ? 30.271 22.202 16.654 1.00 17.45 ? 333 GLY A CA    1 
ATOM   2439 C C     . GLY A 1 342 ? 31.378 23.228 16.538 1.00 15.05 ? 333 GLY A C     1 
ATOM   2440 O O     . GLY A 1 342 ? 31.384 24.049 15.615 1.00 18.39 ? 333 GLY A O     1 
ATOM   2441 N N     . ARG A 1 343 ? 32.341 23.175 17.464 1.00 15.15 ? 334 ARG A N     1 
ATOM   2442 C CA    . ARG A 1 343 ? 33.317 24.256 17.553 1.00 16.70 ? 334 ARG A CA    1 
ATOM   2443 C C     . ARG A 1 343 ? 34.069 24.492 16.239 1.00 16.20 ? 334 ARG A C     1 
ATOM   2444 O O     . ARG A 1 343 ? 34.343 25.646 15.890 1.00 17.06 ? 334 ARG A O     1 
ATOM   2445 C CB    . ARG A 1 343 ? 34.295 23.976 18.687 1.00 17.29 ? 334 ARG A CB    1 
ATOM   2446 C CG    . ARG A 1 343 ? 33.659 24.248 20.030 1.00 18.11 ? 334 ARG A CG    1 
ATOM   2447 C CD    . ARG A 1 343 ? 34.488 23.572 21.125 1.00 18.35 ? 334 ARG A CD    1 
ATOM   2448 N NE    . ARG A 1 343 ? 34.296 22.127 21.179 1.00 17.76 ? 334 ARG A NE    1 
ATOM   2449 C CZ    . ARG A 1 343 ? 34.804 21.369 22.139 1.00 23.84 ? 334 ARG A CZ    1 
ATOM   2450 N NH1   . ARG A 1 343 ? 35.517 21.898 23.122 1.00 24.97 ? 334 ARG A NH1   1 
ATOM   2451 N NH2   . ARG A 1 343 ? 34.578 20.052 22.123 1.00 24.25 ? 334 ARG A NH2   1 
ATOM   2452 N N     . LEU A 1 344 ? 34.419 23.430 15.493 1.00 16.72 ? 335 LEU A N     1 
ATOM   2453 C CA    . LEU A 1 344 ? 35.134 23.650 14.233 1.00 16.78 ? 335 LEU A CA    1 
ATOM   2454 C C     . LEU A 1 344 ? 34.285 24.410 13.215 1.00 18.92 ? 335 LEU A C     1 
ATOM   2455 O O     . LEU A 1 344 ? 34.823 25.156 12.400 1.00 18.87 ? 335 LEU A O     1 
ATOM   2456 C CB    . LEU A 1 344 ? 35.608 22.314 13.647 1.00 16.02 ? 335 LEU A CB    1 
ATOM   2457 C CG    . LEU A 1 344 ? 36.842 21.694 14.299 1.00 21.80 ? 335 LEU A CG    1 
ATOM   2458 C CD1   . LEU A 1 344 ? 37.091 20.314 13.669 1.00 24.70 ? 335 LEU A CD1   1 
ATOM   2459 C CD2   . LEU A 1 344 ? 38.051 22.639 14.112 1.00 21.88 ? 335 LEU A CD2   1 
ATOM   2460 N N     . PHE A 1 345 ? 32.956 24.289 13.283 1.00 15.71 ? 336 PHE A N     1 
ATOM   2461 C CA    . PHE A 1 345 ? 32.092 25.083 12.408 1.00 17.20 ? 336 PHE A CA    1 
ATOM   2462 C C     . PHE A 1 345 ? 32.010 26.547 12.796 1.00 18.59 ? 336 PHE A C     1 
ATOM   2463 O O     . PHE A 1 345 ? 31.630 27.361 11.950 1.00 18.03 ? 336 PHE A O     1 
ATOM   2464 C CB    . PHE A 1 345 ? 30.681 24.500 12.380 1.00 15.52 ? 336 PHE A CB    1 
ATOM   2465 C CG    . PHE A 1 345 ? 30.302 23.827 11.086 1.00 15.53 ? 336 PHE A CG    1 
ATOM   2466 C CD1   . PHE A 1 345 ? 30.324 24.553 9.889  1.00 16.68 ? 336 PHE A CD1   1 
ATOM   2467 C CD2   . PHE A 1 345 ? 29.842 22.519 11.066 1.00 18.43 ? 336 PHE A CD2   1 
ATOM   2468 C CE1   . PHE A 1 345 ? 29.925 23.991 8.704  1.00 20.66 ? 336 PHE A CE1   1 
ATOM   2469 C CE2   . PHE A 1 345 ? 29.455 21.927 9.858  1.00 19.19 ? 336 PHE A CE2   1 
ATOM   2470 C CZ    . PHE A 1 345 ? 29.487 22.672 8.678  1.00 19.31 ? 336 PHE A CZ    1 
ATOM   2471 N N     . ILE A 1 346 ? 32.332 26.908 14.045 1.00 15.01 ? 337 ILE A N     1 
ATOM   2472 C CA    . ILE A 1 346 ? 32.365 28.321 14.410 1.00 14.80 ? 337 ILE A CA    1 
ATOM   2473 C C     . ILE A 1 346 ? 33.382 29.054 13.548 1.00 14.53 ? 337 ILE A C     1 
ATOM   2474 O O     . ILE A 1 346 ? 33.092 30.098 12.956 1.00 17.32 ? 337 ILE A O     1 
ATOM   2475 C CB    . ILE A 1 346 ? 32.691 28.479 15.907 1.00 15.77 ? 337 ILE A CB    1 
ATOM   2476 C CG1   . ILE A 1 346 ? 31.526 27.920 16.701 1.00 16.85 ? 337 ILE A CG1   1 
ATOM   2477 C CG2   . ILE A 1 346 ? 32.965 29.937 16.238 1.00 17.78 ? 337 ILE A CG2   1 
ATOM   2478 C CD1   . ILE A 1 346 ? 31.754 27.903 18.238 1.00 20.02 ? 337 ILE A CD1   1 
ATOM   2479 N N     . SER A 1 347 ? 34.577 28.486 13.422 1.00 17.53 ? 338 SER A N     1 
ATOM   2480 C CA    . SER A 1 347 ? 35.692 29.204 12.829 1.00 15.80 ? 338 SER A CA    1 
ATOM   2481 C C     . SER A 1 347 ? 36.014 28.740 11.422 1.00 17.16 ? 338 SER A C     1 
ATOM   2482 O O     . SER A 1 347 ? 36.914 29.298 10.776 1.00 19.52 ? 338 SER A O     1 
ATOM   2483 C CB    . SER A 1 347 ? 36.925 29.059 13.718 1.00 17.84 ? 338 SER A CB    1 
ATOM   2484 O OG    . SER A 1 347 ? 37.202 27.686 13.989 1.00 17.62 ? 338 SER A OG    1 
ATOM   2485 N N     . ASN A 1 348 ? 35.301 27.743 10.922 1.00 16.80 ? 339 ASN A N     1 
ATOM   2486 C CA    . ASN A 1 348 ? 35.512 27.237 9.569  1.00 16.15 ? 339 ASN A CA    1 
ATOM   2487 C C     . ASN A 1 348 ? 34.171 27.215 8.860  1.00 17.94 ? 339 ASN A C     1 
ATOM   2488 O O     . ASN A 1 348 ? 33.476 26.188 8.860  1.00 18.66 ? 339 ASN A O     1 
ATOM   2489 C CB    . ASN A 1 348 ? 36.156 25.856 9.600  1.00 17.75 ? 339 ASN A CB    1 
ATOM   2490 C CG    . ASN A 1 348 ? 37.532 25.903 10.213 1.00 18.54 ? 339 ASN A CG    1 
ATOM   2491 O OD1   . ASN A 1 348 ? 38.511 26.192 9.529  1.00 19.23 ? 339 ASN A OD1   1 
ATOM   2492 N ND2   . ASN A 1 348 ? 37.604 25.689 11.519 1.00 15.92 ? 339 ASN A ND2   1 
ATOM   2493 N N     . PRO A 1 349 ? 33.752 28.339 8.270  1.00 18.06 ? 340 PRO A N     1 
ATOM   2494 C CA    . PRO A 1 349 ? 32.419 28.350 7.656  1.00 19.42 ? 340 PRO A CA    1 
ATOM   2495 C C     . PRO A 1 349 ? 32.306 27.317 6.564  1.00 17.78 ? 340 PRO A C     1 
ATOM   2496 O O     . PRO A 1 349 ? 31.248 26.689 6.423  1.00 18.88 ? 340 PRO A O     1 
ATOM   2497 C CB    . PRO A 1 349 ? 32.286 29.778 7.102  1.00 17.97 ? 340 PRO A CB    1 
ATOM   2498 C CG    . PRO A 1 349 ? 33.721 30.259 6.958  1.00 18.86 ? 340 PRO A CG    1 
ATOM   2499 C CD    . PRO A 1 349 ? 34.429 29.642 8.147  1.00 16.08 ? 340 PRO A CD    1 
ATOM   2500 N N     . ASP A 1 350 ? 33.394 27.091 5.831  1.00 17.33 ? 341 ASP A N     1 
ATOM   2501 C CA    . ASP A 1 350 ? 33.470 26.034 4.816  1.00 16.76 ? 341 ASP A CA    1 
ATOM   2502 C C     . ASP A 1 350 ? 34.075 24.748 5.365  1.00 18.21 ? 341 ASP A C     1 
ATOM   2503 O O     . ASP A 1 350 ? 34.887 24.082 4.695  1.00 18.42 ? 341 ASP A O     1 
ATOM   2504 C CB    . ASP A 1 350 ? 34.253 26.548 3.612  1.00 18.87 ? 341 ASP A CB    1 
ATOM   2505 C CG    . ASP A 1 350 ? 35.595 27.183 3.983  1.00 23.84 ? 341 ASP A CG    1 
ATOM   2506 O OD1   . ASP A 1 350 ? 35.930 27.372 5.175  1.00 21.90 ? 341 ASP A OD1   1 
ATOM   2507 O OD2   . ASP A 1 350 ? 36.338 27.515 3.035  1.00 25.91 ? 341 ASP A OD2   1 
ATOM   2508 N N     . LEU A 1 351 ? 33.664 24.350 6.580  1.00 17.36 ? 342 LEU A N     1 
ATOM   2509 C CA    . LEU A 1 351 ? 34.203 23.137 7.180  1.00 16.72 ? 342 LEU A CA    1 
ATOM   2510 C C     . LEU A 1 351 ? 33.982 21.936 6.278  1.00 19.09 ? 342 LEU A C     1 
ATOM   2511 O O     . LEU A 1 351 ? 34.850 21.060 6.176  1.00 18.05 ? 342 LEU A O     1 
ATOM   2512 C CB    . LEU A 1 351 ? 33.567 22.877 8.556  1.00 17.74 ? 342 LEU A CB    1 
ATOM   2513 C CG    . LEU A 1 351 ? 34.100 21.630 9.258  1.00 16.04 ? 342 LEU A CG    1 
ATOM   2514 C CD1   . LEU A 1 351 ? 35.622 21.735 9.572  1.00 19.01 ? 342 LEU A CD1   1 
ATOM   2515 C CD2   . LEU A 1 351 ? 33.327 21.394 10.566 1.00 18.47 ? 342 LEU A CD2   1 
ATOM   2516 N N     . VAL A 1 352 ? 32.824 21.868 5.612  1.00 18.24 ? 343 VAL A N     1 
ATOM   2517 C CA    . VAL A 1 352 ? 32.548 20.713 4.763  1.00 19.01 ? 343 VAL A CA    1 
ATOM   2518 C C     . VAL A 1 352 ? 33.622 20.605 3.690  1.00 20.43 ? 343 VAL A C     1 
ATOM   2519 O O     . VAL A 1 352 ? 34.199 19.533 3.459  1.00 18.68 ? 343 VAL A O     1 
ATOM   2520 C CB    . VAL A 1 352 ? 31.141 20.812 4.142  1.00 18.44 ? 343 VAL A CB    1 
ATOM   2521 C CG1   . VAL A 1 352 ? 30.898 19.607 3.209  1.00 19.00 ? 343 VAL A CG1   1 
ATOM   2522 C CG2   . VAL A 1 352 ? 30.034 20.849 5.202  1.00 17.69 ? 343 VAL A CG2   1 
ATOM   2523 N N     . MET A 1 353 ? 33.916 21.734 3.036  1.00 18.77 ? 344 MET A N     1 
ATOM   2524 C CA    . MET A 1 353 ? 34.915 21.768 1.981  1.00 24.06 ? 344 MET A CA    1 
ATOM   2525 C C     . MET A 1 353 ? 36.303 21.477 2.530  1.00 21.47 ? 344 MET A C     1 
ATOM   2526 O O     . MET A 1 353 ? 37.070 20.730 1.922  1.00 20.48 ? 344 MET A O     1 
ATOM   2527 C CB    . MET A 1 353 ? 34.886 23.131 1.278  1.00 26.11 ? 344 MET A CB    1 
ATOM   2528 C CG    . MET A 1 353 ? 35.771 23.252 0.042  1.00 31.99 ? 344 MET A CG    1 
ATOM   2529 S SD    . MET A 1 353 ? 35.490 22.064 -1.315 1.00 46.36 ? 344 MET A SD    1 
ATOM   2530 C CE    . MET A 1 353 ? 33.721 21.692 -1.187 1.00 35.83 ? 344 MET A CE    1 
ATOM   2531 N N     . ARG A 1 354 ? 36.643 22.034 3.692  1.00 17.78 ? 345 ARG A N     1 
ATOM   2532 C CA    . ARG A 1 354 ? 37.947 21.743 4.255  1.00 20.20 ? 345 ARG A CA    1 
ATOM   2533 C C     . ARG A 1 354 ? 38.093 20.264 4.563  1.00 21.96 ? 345 ARG A C     1 
ATOM   2534 O O     . ARG A 1 354 ? 39.174 19.693 4.390  1.00 23.47 ? 345 ARG A O     1 
ATOM   2535 C CB    . ARG A 1 354 ? 38.162 22.586 5.509  1.00 18.09 ? 345 ARG A CB    1 
ATOM   2536 C CG    . ARG A 1 354 ? 38.228 24.035 5.188  1.00 17.31 ? 345 ARG A CG    1 
ATOM   2537 C CD    . ARG A 1 354 ? 38.503 24.845 6.457  1.00 18.89 ? 345 ARG A CD    1 
ATOM   2538 N NE    . ARG A 1 354 ? 38.333 26.260 6.163  1.00 20.84 ? 345 ARG A NE    1 
ATOM   2539 C CZ    . ARG A 1 354 ? 39.273 27.181 6.332  1.00 22.35 ? 345 ARG A CZ    1 
ATOM   2540 N NH1   . ARG A 1 354 ? 40.475 26.866 6.789  1.00 24.39 ? 345 ARG A NH1   1 
ATOM   2541 N NH2   . ARG A 1 354 ? 38.998 28.449 6.029  1.00 27.25 ? 345 ARG A NH2   1 
ATOM   2542 N N     . ILE A 1 355 ? 37.016 19.623 5.026  1.00 18.70 ? 346 ILE A N     1 
ATOM   2543 C CA    . ILE A 1 355 ? 37.088 18.196 5.308  1.00 20.64 ? 346 ILE A CA    1 
ATOM   2544 C C     . ILE A 1 355 ? 37.253 17.415 4.010  1.00 22.49 ? 346 ILE A C     1 
ATOM   2545 O O     . ILE A 1 355 ? 38.067 16.481 3.931  1.00 24.27 ? 346 ILE A O     1 
ATOM   2546 C CB    . ILE A 1 355 ? 35.848 17.762 6.116  1.00 19.83 ? 346 ILE A CB    1 
ATOM   2547 C CG1   . ILE A 1 355 ? 35.990 18.271 7.552  1.00 17.58 ? 346 ILE A CG1   1 
ATOM   2548 C CG2   . ILE A 1 355 ? 35.695 16.234 6.141  1.00 25.46 ? 346 ILE A CG2   1 
ATOM   2549 C CD1   . ILE A 1 355 ? 34.785 17.893 8.431  1.00 24.34 ? 346 ILE A CD1   1 
ATOM   2550 N N     . LYS A 1 356 ? 36.519 17.810 2.972  1.00 20.94 ? 347 LYS A N     1 
ATOM   2551 C CA    . LYS A 1 356 ? 36.625 17.156 1.665  1.00 23.91 ? 347 LYS A CA    1 
ATOM   2552 C C     . LYS A 1 356 ? 38.043 17.236 1.109  1.00 26.21 ? 347 LYS A C     1 
ATOM   2553 O O     . LYS A 1 356 ? 38.571 16.255 0.564  1.00 25.71 ? 347 LYS A O     1 
ATOM   2554 C CB    . LYS A 1 356 ? 35.645 17.802 0.695  1.00 25.27 ? 347 LYS A CB    1 
ATOM   2555 C CG    . LYS A 1 356 ? 35.739 17.254 -0.715 1.00 30.74 ? 347 LYS A CG    1 
ATOM   2556 C CD    . LYS A 1 356 ? 34.874 16.046 -0.848 1.00 37.70 ? 347 LYS A CD    1 
ATOM   2557 C CE    . LYS A 1 356 ? 33.935 16.185 -2.039 1.00 52.32 ? 347 LYS A CE    1 
ATOM   2558 N NZ    . LYS A 1 356 ? 33.759 14.871 -2.716 1.00 50.83 ? 347 LYS A NZ    1 
ATOM   2559 N N     . LEU A 1 357 ? 38.671 18.399 1.220  1.00 24.48 ? 348 LEU A N     1 
ATOM   2560 C CA    . LEU A 1 357 ? 40.010 18.621 0.688  1.00 23.70 ? 348 LEU A CA    1 
ATOM   2561 C C     . LEU A 1 357 ? 41.120 18.262 1.663  1.00 25.62 ? 348 LEU A C     1 
ATOM   2562 O O     . LEU A 1 357 ? 42.296 18.309 1.277  1.00 26.51 ? 348 LEU A O     1 
ATOM   2563 C CB    . LEU A 1 357 ? 40.167 20.085 0.297  1.00 24.19 ? 348 LEU A CB    1 
ATOM   2564 C CG    . LEU A 1 357 ? 39.206 20.643 -0.736 1.00 27.93 ? 348 LEU A CG    1 
ATOM   2565 C CD1   . LEU A 1 357 ? 39.547 22.096 -0.924 1.00 28.75 ? 348 LEU A CD1   1 
ATOM   2566 C CD2   . LEU A 1 357 ? 39.344 19.887 -2.044 1.00 29.88 ? 348 LEU A CD2   1 
ATOM   2567 N N     . ASN A 1 358 ? 40.787 17.943 2.918  1.00 22.48 ? 349 ASN A N     1 
ATOM   2568 C CA    . ASN A 1 358 ? 41.765 17.797 3.988  1.00 24.09 ? 349 ASN A CA    1 
ATOM   2569 C C     . ASN A 1 358 ? 42.649 19.040 4.091  1.00 25.04 ? 349 ASN A C     1 
ATOM   2570 O O     . ASN A 1 358 ? 43.870 18.963 4.233  1.00 26.43 ? 349 ASN A O     1 
ATOM   2571 C CB    . ASN A 1 358 ? 42.595 16.526 3.812  1.00 30.02 ? 349 ASN A CB    1 
ATOM   2572 C CG    . ASN A 1 358 ? 43.325 16.136 5.082  1.00 28.35 ? 349 ASN A CG    1 
ATOM   2573 O OD1   . ASN A 1 358 ? 42.984 16.593 6.176  1.00 28.34 ? 349 ASN A OD1   1 
ATOM   2574 N ND2   . ASN A 1 358 ? 44.343 15.299 4.943  1.00 36.09 ? 349 ASN A ND2   1 
ATOM   2575 N N     . ALA A 1 359 ? 41.997 20.214 4.028  1.00 23.56 ? 350 ALA A N     1 
ATOM   2576 C CA    . ALA A 1 359 ? 42.669 21.496 4.175  1.00 19.84 ? 350 ALA A CA    1 
ATOM   2577 C C     . ALA A 1 359 ? 42.838 21.835 5.653  1.00 24.65 ? 350 ALA A C     1 
ATOM   2578 O O     . ALA A 1 359 ? 42.060 21.380 6.487  1.00 22.63 ? 350 ALA A O     1 
ATOM   2579 C CB    . ALA A 1 359 ? 41.873 22.596 3.489  1.00 25.32 ? 350 ALA A CB    1 
ATOM   2580 N N     . PRO A 1 360 ? 43.851 22.628 6.004  1.00 26.36 ? 351 PRO A N     1 
ATOM   2581 C CA    . PRO A 1 360 ? 44.043 22.988 7.417  1.00 26.44 ? 351 PRO A CA    1 
ATOM   2582 C C     . PRO A 1 360 ? 42.859 23.772 7.977  1.00 25.07 ? 351 PRO A C     1 
ATOM   2583 O O     . PRO A 1 360 ? 42.198 24.538 7.277  1.00 26.25 ? 351 PRO A O     1 
ATOM   2584 C CB    . PRO A 1 360 ? 45.319 23.843 7.403  1.00 33.08 ? 351 PRO A CB    1 
ATOM   2585 C CG    . PRO A 1 360 ? 46.013 23.477 6.106  1.00 37.16 ? 351 PRO A CG    1 
ATOM   2586 C CD    . PRO A 1 360 ? 44.912 23.173 5.133  1.00 30.05 ? 351 PRO A CD    1 
ATOM   2587 N N     . LEU A 1 361 ? 42.601 23.563 9.257  1.00 20.26 ? 352 LEU A N     1 
ATOM   2588 C CA    . LEU A 1 361 ? 41.454 24.157 9.921  1.00 17.93 ? 352 LEU A CA    1 
ATOM   2589 C C     . LEU A 1 361 ? 41.889 25.386 10.704 1.00 16.95 ? 352 LEU A C     1 
ATOM   2590 O O     . LEU A 1 361 ? 43.000 25.429 11.236 1.00 17.97 ? 352 LEU A O     1 
ATOM   2591 C CB    . LEU A 1 361 ? 40.813 23.147 10.863 1.00 20.84 ? 352 LEU A CB    1 
ATOM   2592 C CG    . LEU A 1 361 ? 40.377 21.872 10.144 1.00 17.63 ? 352 LEU A CG    1 
ATOM   2593 C CD1   . LEU A 1 361 ? 39.834 20.856 11.135 1.00 27.73 ? 352 LEU A CD1   1 
ATOM   2594 C CD2   . LEU A 1 361 ? 39.346 22.193 9.066  1.00 22.84 ? 352 LEU A CD2   1 
ATOM   2595 N N     . ASN A 1 362 ? 41.012 26.381 10.779 1.00 16.81 ? 353 ASN A N     1 
ATOM   2596 C CA    . ASN A 1 362 ? 41.351 27.609 11.485 1.00 17.02 ? 353 ASN A CA    1 
ATOM   2597 C C     . ASN A 1 362 ? 40.812 27.573 12.908 1.00 18.66 ? 353 ASN A C     1 
ATOM   2598 O O     . ASN A 1 362 ? 39.763 26.998 13.180 1.00 17.50 ? 353 ASN A O     1 
ATOM   2599 C CB    . ASN A 1 362 ? 40.812 28.853 10.777 1.00 18.91 ? 353 ASN A CB    1 
ATOM   2600 C CG    . ASN A 1 362 ? 41.517 29.137 9.441  1.00 21.60 ? 353 ASN A CG    1 
ATOM   2601 O OD1   . ASN A 1 362 ? 42.604 28.632 9.161  1.00 25.05 ? 353 ASN A OD1   1 
ATOM   2602 N ND2   . ASN A 1 362 ? 40.894 29.959 8.624  1.00 25.91 ? 353 ASN A ND2   1 
ATOM   2603 N N     . LYS A 1 363 ? 41.547 28.206 13.818 1.00 15.84 ? 354 LYS A N     1 
ATOM   2604 C CA    . LYS A 1 363 ? 41.166 28.227 15.227 1.00 17.38 ? 354 LYS A CA    1 
ATOM   2605 C C     . LYS A 1 363 ? 39.947 29.107 15.452 1.00 14.91 ? 354 LYS A C     1 
ATOM   2606 O O     . LYS A 1 363 ? 39.653 30.023 14.675 1.00 18.69 ? 354 LYS A O     1 
ATOM   2607 C CB    . LYS A 1 363 ? 42.314 28.736 16.095 1.00 18.65 ? 354 LYS A CB    1 
ATOM   2608 C CG    . LYS A 1 363 ? 42.747 30.184 15.804 1.00 21.42 ? 354 LYS A CG    1 
ATOM   2609 C CD    . LYS A 1 363 ? 43.797 30.650 16.849 1.00 28.08 ? 354 LYS A CD    1 
ATOM   2610 C CE    . LYS A 1 363 ? 43.145 31.154 18.122 1.00 27.90 ? 354 LYS A CE    1 
ATOM   2611 N NZ    . LYS A 1 363 ? 44.129 31.232 19.243 1.00 31.81 ? 354 LYS A NZ    1 
ATOM   2612 N N     . TYR A 1 364 ? 39.256 28.846 16.557 1.00 17.66 ? 355 TYR A N     1 
ATOM   2613 C CA    . TYR A 1 364 ? 38.144 29.674 16.990 1.00 19.64 ? 355 TYR A CA    1 
ATOM   2614 C C     . TYR A 1 364 ? 38.550 30.536 18.181 1.00 20.64 ? 355 TYR A C     1 
ATOM   2615 O O     . TYR A 1 364 ? 39.461 30.199 18.950 1.00 21.46 ? 355 TYR A O     1 
ATOM   2616 C CB    . TYR A 1 364 ? 36.911 28.819 17.342 1.00 18.81 ? 355 TYR A CB    1 
ATOM   2617 C CG    . TYR A 1 364 ? 37.198 27.565 18.129 1.00 20.68 ? 355 TYR A CG    1 
ATOM   2618 C CD1   . TYR A 1 364 ? 37.420 27.624 19.509 1.00 21.69 ? 355 TYR A CD1   1 
ATOM   2619 C CD2   . TYR A 1 364 ? 37.217 26.317 17.506 1.00 18.05 ? 355 TYR A CD2   1 
ATOM   2620 C CE1   . TYR A 1 364 ? 37.687 26.464 20.251 1.00 23.07 ? 355 TYR A CE1   1 
ATOM   2621 C CE2   . TYR A 1 364 ? 37.469 25.160 18.236 1.00 21.01 ? 355 TYR A CE2   1 
ATOM   2622 C CZ    . TYR A 1 364 ? 37.707 25.239 19.588 1.00 23.58 ? 355 TYR A CZ    1 
ATOM   2623 O OH    . TYR A 1 364 ? 37.952 24.068 20.269 1.00 24.48 ? 355 TYR A OH    1 
ATOM   2624 N N     . ASN A 1 365 ? 37.882 31.675 18.310 1.00 19.17 ? 356 ASN A N     1 
ATOM   2625 C CA    . ASN A 1 365 ? 38.122 32.598 19.420 1.00 23.77 ? 356 ASN A CA    1 
ATOM   2626 C C     . ASN A 1 365 ? 37.016 32.381 20.453 1.00 23.08 ? 356 ASN A C     1 
ATOM   2627 O O     . ASN A 1 365 ? 35.870 32.801 20.263 1.00 20.48 ? 356 ASN A O     1 
ATOM   2628 C CB    . ASN A 1 365 ? 38.159 34.034 18.915 1.00 22.48 ? 356 ASN A CB    1 
ATOM   2629 C CG    . ASN A 1 365 ? 39.119 34.233 17.710 1.00 28.14 ? 356 ASN A CG    1 
ATOM   2630 O OD1   . ASN A 1 365 ? 40.220 33.686 17.674 1.00 30.70 ? 356 ASN A OD1   1 
ATOM   2631 N ND2   . ASN A 1 365 ? 38.675 34.998 16.717 1.00 30.21 ? 356 ASN A ND2   1 
ATOM   2632 N N     . ARG A 1 366 ? 37.359 31.706 21.557 1.00 19.84 ? 357 ARG A N     1 
ATOM   2633 C CA    . ARG A 1 366 ? 36.375 31.397 22.588 1.00 18.75 ? 357 ARG A CA    1 
ATOM   2634 C C     . ARG A 1 366 ? 35.731 32.658 23.171 1.00 18.33 ? 357 ARG A C     1 
ATOM   2635 O O     . ARG A 1 366 ? 34.566 32.632 23.587 1.00 19.13 ? 357 ARG A O     1 
ATOM   2636 C CB    . ARG A 1 366 ? 37.045 30.570 23.693 1.00 24.60 ? 357 ARG A CB    1 
ATOM   2637 C CG    . ARG A 1 366 ? 37.573 29.198 23.190 1.00 27.03 ? 357 ARG A CG    1 
ATOM   2638 C CD    . ARG A 1 366 ? 38.747 28.631 24.049 1.00 31.27 ? 357 ARG A CD    1 
ATOM   2639 N NE    . ARG A 1 366 ? 39.863 29.569 24.144 1.00 35.30 ? 357 ARG A NE    1 
ATOM   2640 C CZ    . ARG A 1 366 ? 40.888 29.446 24.979 1.00 38.91 ? 357 ARG A CZ    1 
ATOM   2641 N NH1   . ARG A 1 366 ? 41.005 28.401 25.779 1.00 36.90 ? 357 ARG A NH1   1 
ATOM   2642 N NH2   . ARG A 1 366 ? 41.827 30.390 24.997 1.00 37.13 ? 357 ARG A NH2   1 
ATOM   2643 N N     . LYS A 1 367 ? 36.380 33.705 23.217 1.00 21.34 ? 358 LYS A N     1 
ATOM   2644 C CA    . LYS A 1 367 ? 35.861 34.934 23.804 1.00 23.99 ? 358 LYS A CA    1 
ATOM   2645 C C     . LYS A 1 367 ? 34.630 35.460 23.068 1.00 21.83 ? 358 LYS A C     1 
ATOM   2646 O O     . LYS A 1 367 ? 33.870 36.253 23.653 1.00 22.47 ? 358 LYS A O     1 
ATOM   2647 C CB    . LYS A 1 367 ? 36.949 36.009 23.824 1.00 26.22 ? 358 LYS A CB    1 
ATOM   2648 C CG    . LYS A 1 367 ? 38.109 35.702 24.759 1.00 34.45 ? 358 LYS A CG    1 
ATOM   2649 C CD    . LYS A 1 367 ? 39.102 36.851 24.804 1.00 38.89 ? 358 LYS A CD    1 
ATOM   2650 C CE    . LYS A 1 367 ? 40.195 36.597 25.828 1.00 50.03 ? 358 LYS A CE    1 
ATOM   2651 N NZ    . LYS A 1 367 ? 41.127 35.522 25.391 1.00 56.97 ? 358 LYS A NZ    1 
ATOM   2652 N N     . THR A 1 368 ? 34.517 35.172 21.846 1.00 19.02 ? 359 THR A N     1 
ATOM   2653 C CA    . THR A 1 368 ? 33.377 35.692 21.098 1.00 18.66 ? 359 THR A CA    1 
ATOM   2654 C C     . THR A 1 368 ? 32.357 34.602 20.755 1.00 18.59 ? 359 THR A C     1 
ATOM   2655 O O     . THR A 1 368 ? 31.567 34.765 19.817 1.00 16.80 ? 359 THR A O     1 
ATOM   2656 C CB    . THR A 1 368 ? 33.837 36.431 19.838 1.00 20.43 ? 359 THR A CB    1 
ATOM   2657 O OG1   . THR A 1 368 ? 34.735 35.624 19.066 1.00 18.78 ? 359 THR A OG1   1 
ATOM   2658 C CG2   . THR A 1 368 ? 34.555 37.746 20.235 1.00 21.48 ? 359 THR A CG2   1 
ATOM   2659 N N     . PHE A 1 369 ? 32.336 33.506 21.522 1.00 16.31 ? 360 PHE A N     1 
ATOM   2660 C CA    . PHE A 1 369 ? 31.282 32.509 21.363 1.00 15.61 ? 360 PHE A CA    1 
ATOM   2661 C C     . PHE A 1 369 ? 29.905 33.107 21.631 1.00 15.00 ? 360 PHE A C     1 
ATOM   2662 O O     . PHE A 1 369 ? 28.937 32.788 20.927 1.00 15.94 ? 360 PHE A O     1 
ATOM   2663 C CB    . PHE A 1 369 ? 31.514 31.337 22.327 1.00 18.19 ? 360 PHE A CB    1 
ATOM   2664 C CG    . PHE A 1 369 ? 32.514 30.313 21.859 1.00 17.96 ? 360 PHE A CG    1 
ATOM   2665 C CD1   . PHE A 1 369 ? 33.263 30.484 20.704 1.00 20.79 ? 360 PHE A CD1   1 
ATOM   2666 C CD2   . PHE A 1 369 ? 32.718 29.168 22.630 1.00 20.59 ? 360 PHE A CD2   1 
ATOM   2667 C CE1   . PHE A 1 369 ? 34.181 29.510 20.283 1.00 21.77 ? 360 PHE A CE1   1 
ATOM   2668 C CE2   . PHE A 1 369 ? 33.645 28.187 22.209 1.00 20.25 ? 360 PHE A CE2   1 
ATOM   2669 C CZ    . PHE A 1 369 ? 34.379 28.380 21.054 1.00 23.17 ? 360 PHE A CZ    1 
ATOM   2670 N N     . TYR A 1 370 ? 29.777 33.935 22.679 1.00 17.76 ? 361 TYR A N     1 
ATOM   2671 C CA    . TYR A 1 370 ? 28.473 34.317 23.216 1.00 14.46 ? 361 TYR A CA    1 
ATOM   2672 C C     . TYR A 1 370 ? 28.277 35.828 23.267 1.00 18.07 ? 361 TYR A C     1 
ATOM   2673 O O     . TYR A 1 370 ? 27.374 36.304 23.954 1.00 18.78 ? 361 TYR A O     1 
ATOM   2674 C CB    . TYR A 1 370 ? 28.264 33.743 24.615 1.00 15.86 ? 361 TYR A CB    1 
ATOM   2675 C CG    . TYR A 1 370 ? 28.407 32.251 24.725 1.00 16.69 ? 361 TYR A CG    1 
ATOM   2676 C CD1   . TYR A 1 370 ? 27.531 31.397 24.075 1.00 19.58 ? 361 TYR A CD1   1 
ATOM   2677 C CD2   . TYR A 1 370 ? 29.390 31.698 25.536 1.00 21.20 ? 361 TYR A CD2   1 
ATOM   2678 C CE1   . TYR A 1 370 ? 27.631 30.026 24.220 1.00 22.89 ? 361 TYR A CE1   1 
ATOM   2679 C CE2   . TYR A 1 370 ? 29.508 30.325 25.677 1.00 25.33 ? 361 TYR A CE2   1 
ATOM   2680 C CZ    . TYR A 1 370 ? 28.621 29.499 25.016 1.00 27.69 ? 361 TYR A CZ    1 
ATOM   2681 O OH    . TYR A 1 370 ? 28.729 28.131 25.175 1.00 25.54 ? 361 TYR A OH    1 
ATOM   2682 N N     . THR A 1 371 ? 29.112 36.582 22.568 1.00 18.07 ? 362 THR A N     1 
ATOM   2683 C CA    . THR A 1 371 ? 28.978 38.030 22.499 1.00 22.06 ? 362 THR A CA    1 
ATOM   2684 C C     . THR A 1 371 ? 27.916 38.415 21.467 1.00 20.68 ? 362 THR A C     1 
ATOM   2685 O O     . THR A 1 371 ? 27.348 37.570 20.777 1.00 18.60 ? 362 THR A O     1 
ATOM   2686 C CB    . THR A 1 371 ? 30.322 38.649 22.155 1.00 16.12 ? 362 THR A CB    1 
ATOM   2687 O OG1   . THR A 1 371 ? 30.885 37.929 21.043 1.00 18.80 ? 362 THR A OG1   1 
ATOM   2688 C CG2   . THR A 1 371 ? 31.287 38.571 23.360 1.00 23.36 ? 362 THR A CG2   1 
ATOM   2689 N N     . GLN A 1 372 ? 27.605 39.712 21.391 1.00 18.83 ? 363 GLN A N     1 
ATOM   2690 C CA    . GLN A 1 372 ? 26.429 40.149 20.637 1.00 15.49 ? 363 GLN A CA    1 
ATOM   2691 C C     . GLN A 1 372 ? 26.736 40.797 19.297 1.00 17.99 ? 363 GLN A C     1 
ATOM   2692 O O     . GLN A 1 372 ? 25.797 41.087 18.539 1.00 19.62 ? 363 GLN A O     1 
ATOM   2693 C CB    . GLN A 1 372 ? 25.602 41.127 21.494 1.00 18.25 ? 363 GLN A CB    1 
ATOM   2694 C CG    . GLN A 1 372 ? 24.655 40.460 22.447 1.00 19.34 ? 363 GLN A CG    1 
ATOM   2695 C CD    . GLN A 1 372 ? 25.404 39.623 23.448 1.00 22.53 ? 363 GLN A CD    1 
ATOM   2696 O OE1   . GLN A 1 372 ? 26.092 40.156 24.332 1.00 20.62 ? 363 GLN A OE1   1 
ATOM   2697 N NE2   . GLN A 1 372 ? 25.310 38.303 23.302 1.00 18.58 ? 363 GLN A NE2   1 
ATOM   2698 N N     . ASP A 1 373 ? 28.005 41.004 18.969 1.00 20.77 ? 364 ASP A N     1 
ATOM   2699 C CA    . ASP A 1 373 ? 28.318 41.671 17.718 1.00 21.18 ? 364 ASP A CA    1 
ATOM   2700 C C     . ASP A 1 373 ? 27.820 40.833 16.541 1.00 18.76 ? 364 ASP A C     1 
ATOM   2701 O O     . ASP A 1 373 ? 28.020 39.616 16.513 1.00 18.55 ? 364 ASP A O     1 
ATOM   2702 C CB    . ASP A 1 373 ? 29.824 41.921 17.599 1.00 21.81 ? 364 ASP A CB    1 
ATOM   2703 C CG    . ASP A 1 373 ? 30.140 42.984 16.555 1.00 22.71 ? 364 ASP A CG    1 
ATOM   2704 O OD1   . ASP A 1 373 ? 30.214 42.657 15.364 1.00 22.21 ? 364 ASP A OD1   1 
ATOM   2705 O OD2   . ASP A 1 373 ? 30.262 44.167 16.931 1.00 25.97 ? 364 ASP A OD2   1 
ATOM   2706 N N     . PRO A 1 374 ? 27.187 41.456 15.540 1.00 19.48 ? 365 PRO A N     1 
ATOM   2707 C CA    . PRO A 1 374 ? 26.652 40.698 14.404 1.00 21.55 ? 365 PRO A CA    1 
ATOM   2708 C C     . PRO A 1 374 ? 27.720 40.180 13.452 1.00 21.55 ? 365 PRO A C     1 
ATOM   2709 O O     . PRO A 1 374 ? 27.402 39.329 12.604 1.00 20.30 ? 365 PRO A O     1 
ATOM   2710 C CB    . PRO A 1 374 ? 25.751 41.720 13.695 1.00 21.87 ? 365 PRO A CB    1 
ATOM   2711 C CG    . PRO A 1 374 ? 26.334 43.038 14.084 1.00 22.12 ? 365 PRO A CG    1 
ATOM   2712 C CD    . PRO A 1 374 ? 26.836 42.886 15.484 1.00 22.50 ? 365 PRO A CD    1 
ATOM   2713 N N     . VAL A 1 375 ? 28.958 40.682 13.543 1.00 18.35 ? 366 VAL A N     1 
ATOM   2714 C CA    . VAL A 1 375 ? 30.045 40.287 12.652 1.00 19.12 ? 366 VAL A CA    1 
ATOM   2715 C C     . VAL A 1 375 ? 31.200 39.658 13.435 1.00 19.66 ? 366 VAL A C     1 
ATOM   2716 O O     . VAL A 1 375 ? 31.643 38.546 13.121 1.00 20.97 ? 366 VAL A O     1 
ATOM   2717 C CB    . VAL A 1 375 ? 30.559 41.506 11.868 1.00 21.38 ? 366 VAL A CB    1 
ATOM   2718 C CG1   . VAL A 1 375 ? 31.761 41.114 10.991 1.00 21.63 ? 366 VAL A CG1   1 
ATOM   2719 C CG2   . VAL A 1 375 ? 29.440 42.112 11.021 1.00 23.72 ? 366 VAL A CG2   1 
ATOM   2720 N N     . VAL A 1 376 ? 31.720 40.382 14.435 1.00 19.10 ? 367 VAL A N     1 
ATOM   2721 C CA    . VAL A 1 376 ? 32.996 40.019 15.072 1.00 17.72 ? 367 VAL A CA    1 
ATOM   2722 C C     . VAL A 1 376 ? 32.884 38.684 15.801 1.00 18.64 ? 367 VAL A C     1 
ATOM   2723 O O     . VAL A 1 376 ? 32.037 38.513 16.687 1.00 20.59 ? 367 VAL A O     1 
ATOM   2724 C CB    . VAL A 1 376 ? 33.444 41.115 16.040 1.00 22.65 ? 367 VAL A CB    1 
ATOM   2725 C CG1   . VAL A 1 376 ? 34.634 40.628 16.838 1.00 21.76 ? 367 VAL A CG1   1 
ATOM   2726 C CG2   . VAL A 1 376 ? 33.814 42.356 15.262 1.00 23.27 ? 367 VAL A CG2   1 
ATOM   2727 N N     . GLY A 1 377 ? 33.736 37.730 15.420 1.00 20.03 ? 368 GLY A N     1 
ATOM   2728 C CA    . GLY A 1 377 ? 33.660 36.383 15.968 1.00 20.66 ? 368 GLY A CA    1 
ATOM   2729 C C     . GLY A 1 377 ? 32.432 35.611 15.539 1.00 19.15 ? 368 GLY A C     1 
ATOM   2730 O O     . GLY A 1 377 ? 32.120 34.575 16.133 1.00 18.81 ? 368 GLY A O     1 
ATOM   2731 N N     . TYR A 1 378 ? 31.729 36.069 14.506 1.00 17.60 ? 369 TYR A N     1 
ATOM   2732 C CA    . TYR A 1 378 ? 30.483 35.412 14.127 1.00 18.81 ? 369 TYR A CA    1 
ATOM   2733 C C     . TYR A 1 378 ? 30.492 35.119 12.621 1.00 18.17 ? 369 TYR A C     1 
ATOM   2734 O O     . TYR A 1 378 ? 30.459 33.945 12.205 1.00 17.78 ? 369 TYR A O     1 
ATOM   2735 C CB    . TYR A 1 378 ? 29.283 36.281 14.527 1.00 18.63 ? 369 TYR A CB    1 
ATOM   2736 C CG    . TYR A 1 378 ? 27.923 35.594 14.478 1.00 18.38 ? 369 TYR A CG    1 
ATOM   2737 C CD1   . TYR A 1 378 ? 27.707 34.366 15.107 1.00 15.88 ? 369 TYR A CD1   1 
ATOM   2738 C CD2   . TYR A 1 378 ? 26.856 36.187 13.794 1.00 18.09 ? 369 TYR A CD2   1 
ATOM   2739 C CE1   . TYR A 1 378 ? 26.459 33.735 15.041 1.00 15.63 ? 369 TYR A CE1   1 
ATOM   2740 C CE2   . TYR A 1 378 ? 25.608 35.581 13.740 1.00 19.70 ? 369 TYR A CE2   1 
ATOM   2741 C CZ    . TYR A 1 378 ? 25.413 34.366 14.375 1.00 19.18 ? 369 TYR A CZ    1 
ATOM   2742 O OH    . TYR A 1 378 ? 24.190 33.746 14.318 1.00 23.45 ? 369 TYR A OH    1 
ATOM   2743 N N     . THR A 1 379 ? 30.563 36.164 11.787 1.00 18.97 ? 370 THR A N     1 
ATOM   2744 C CA    . THR A 1 379 ? 30.590 35.964 10.344 1.00 19.36 ? 370 THR A CA    1 
ATOM   2745 C C     . THR A 1 379 ? 31.906 36.387 9.710  1.00 19.56 ? 370 THR A C     1 
ATOM   2746 O O     . THR A 1 379 ? 32.022 36.333 8.476  1.00 23.09 ? 370 THR A O     1 
ATOM   2747 C CB    . THR A 1 379 ? 29.444 36.721 9.655  1.00 18.87 ? 370 THR A CB    1 
ATOM   2748 O OG1   . THR A 1 379 ? 29.568 38.110 9.950  1.00 22.89 ? 370 THR A OG1   1 
ATOM   2749 C CG2   . THR A 1 379 ? 28.086 36.227 10.131 1.00 21.87 ? 370 THR A CG2   1 
ATOM   2750 N N     . ASP A 1 380 ? 32.901 36.789 10.509 1.00 20.11 ? 371 ASP A N     1 
ATOM   2751 C CA    . ASP A 1 380 ? 34.155 37.285 9.951  1.00 19.60 ? 371 ASP A CA    1 
ATOM   2752 C C     . ASP A 1 380 ? 35.259 36.234 9.909  1.00 24.05 ? 371 ASP A C     1 
ATOM   2753 O O     . ASP A 1 380 ? 36.395 36.570 9.581  1.00 26.03 ? 371 ASP A O     1 
ATOM   2754 C CB    . ASP A 1 380 ? 34.630 38.526 10.721 1.00 22.42 ? 371 ASP A CB    1 
ATOM   2755 C CG    . ASP A 1 380 ? 34.864 38.274 12.209 1.00 23.90 ? 371 ASP A CG    1 
ATOM   2756 O OD1   . ASP A 1 380 ? 34.591 37.171 12.734 1.00 26.51 ? 371 ASP A OD1   1 
ATOM   2757 O OD2   . ASP A 1 380 ? 35.351 39.226 12.875 1.00 30.64 ? 371 ASP A OD2   1 
ATOM   2758 N N     . TYR A 1 381 ? 34.970 34.984 10.227 1.00 19.28 ? 372 TYR A N     1 
ATOM   2759 C CA    . TYR A 1 381 ? 35.966 33.941 9.986  1.00 18.71 ? 372 TYR A CA    1 
ATOM   2760 C C     . TYR A 1 381 ? 36.027 33.657 8.487  1.00 19.82 ? 372 TYR A C     1 
ATOM   2761 O O     . TYR A 1 381 ? 34.990 33.365 7.870  1.00 21.71 ? 372 TYR A O     1 
ATOM   2762 C CB    . TYR A 1 381 ? 35.594 32.670 10.728 1.00 20.35 ? 372 TYR A CB    1 
ATOM   2763 C CG    . TYR A 1 381 ? 35.710 32.721 12.224 1.00 17.86 ? 372 TYR A CG    1 
ATOM   2764 C CD1   . TYR A 1 381 ? 36.953 32.564 12.850 1.00 19.85 ? 372 TYR A CD1   1 
ATOM   2765 C CD2   . TYR A 1 381 ? 34.582 32.860 13.033 1.00 16.53 ? 372 TYR A CD2   1 
ATOM   2766 C CE1   . TYR A 1 381 ? 37.078 32.563 14.238 1.00 22.36 ? 372 TYR A CE1   1 
ATOM   2767 C CE2   . TYR A 1 381 ? 34.690 32.863 14.441 1.00 17.95 ? 372 TYR A CE2   1 
ATOM   2768 C CZ    . TYR A 1 381 ? 35.940 32.699 15.032 1.00 19.32 ? 372 TYR A CZ    1 
ATOM   2769 O OH    . TYR A 1 381 ? 36.052 32.688 16.401 1.00 22.75 ? 372 TYR A OH    1 
ATOM   2770 N N     . PRO A 1 382 ? 37.196 33.722 7.867  1.00 22.10 ? 373 PRO A N     1 
ATOM   2771 C CA    . PRO A 1 382 ? 37.259 33.613 6.408  1.00 22.17 ? 373 PRO A CA    1 
ATOM   2772 C C     . PRO A 1 382 ? 37.089 32.197 5.869  1.00 24.09 ? 373 PRO A C     1 
ATOM   2773 O O     . PRO A 1 382 ? 37.313 31.187 6.540  1.00 22.26 ? 373 PRO A O     1 
ATOM   2774 C CB    . PRO A 1 382 ? 38.655 34.157 6.073  1.00 25.63 ? 373 PRO A CB    1 
ATOM   2775 C CG    . PRO A 1 382 ? 39.431 33.995 7.283  1.00 29.44 ? 373 PRO A CG    1 
ATOM   2776 C CD    . PRO A 1 382 ? 38.475 34.162 8.446  1.00 27.06 ? 373 PRO A CD    1 
ATOM   2777 N N     . PHE A 1 383 ? 36.698 32.160 4.607  1.00 22.00 ? 374 PHE A N     1 
ATOM   2778 C CA    . PHE A 1 383 ? 36.709 30.953 3.797  1.00 21.26 ? 374 PHE A CA    1 
ATOM   2779 C C     . PHE A 1 383 ? 38.130 30.642 3.351  1.00 25.30 ? 374 PHE A C     1 
ATOM   2780 O O     . PHE A 1 383 ? 39.036 31.469 3.464  1.00 26.81 ? 374 PHE A O     1 
ATOM   2781 C CB    . PHE A 1 383 ? 35.796 31.133 2.583  1.00 21.19 ? 374 PHE A CB    1 
ATOM   2782 C CG    . PHE A 1 383 ? 34.346 31.158 2.939  1.00 24.38 ? 374 PHE A CG    1 
ATOM   2783 C CD1   . PHE A 1 383 ? 33.754 32.328 3.408  1.00 28.19 ? 374 PHE A CD1   1 
ATOM   2784 C CD2   . PHE A 1 383 ? 33.578 30.012 2.833  1.00 24.21 ? 374 PHE A CD2   1 
ATOM   2785 C CE1   . PHE A 1 383 ? 32.413 32.348 3.751  1.00 26.20 ? 374 PHE A CE1   1 
ATOM   2786 C CE2   . PHE A 1 383 ? 32.225 30.035 3.188  1.00 26.42 ? 374 PHE A CE2   1 
ATOM   2787 C CZ    . PHE A 1 383 ? 31.655 31.198 3.634  1.00 26.19 ? 374 PHE A CZ    1 
ATOM   2788 N N     . LEU A 1 384 ? 38.321 29.423 2.844  1.00 22.66 ? 375 LEU A N     1 
ATOM   2789 C CA    . LEU A 1 384 ? 39.577 29.076 2.193  1.00 27.98 ? 375 LEU A CA    1 
ATOM   2790 C C     . LEU A 1 384 ? 39.866 30.059 1.069  1.00 30.92 ? 375 LEU A C     1 
ATOM   2791 O O     . LEU A 1 384 ? 38.964 30.445 0.320  1.00 32.62 ? 375 LEU A O     1 
ATOM   2792 C CB    . LEU A 1 384 ? 39.493 27.664 1.621  1.00 32.57 ? 375 LEU A CB    1 
ATOM   2793 C CG    . LEU A 1 384 ? 39.612 26.469 2.539  1.00 29.84 ? 375 LEU A CG    1 
ATOM   2794 C CD1   . LEU A 1 384 ? 39.558 25.213 1.695  1.00 32.20 ? 375 LEU A CD1   1 
ATOM   2795 C CD2   . LEU A 1 384 ? 40.939 26.530 3.320  1.00 32.75 ? 375 LEU A CD2   1 
ATOM   2796 N N     . GLN A 1 385 ? 41.128 30.466 0.951  1.00 35.46 ? 376 GLN A N     1 
ATOM   2797 C CA    . GLN A 1 385 ? 41.499 31.467 -0.056 1.00 44.82 ? 376 GLN A CA    1 
ATOM   2798 C C     . GLN A 1 385 ? 41.354 30.944 -1.492 1.00 46.08 ? 376 GLN A C     1 
ATOM   2799 O O     . GLN A 1 385 ? 41.180 29.745 -1.726 1.00 46.75 ? 376 GLN A O     1 
ATOM   2800 C CB    . GLN A 1 385 ? 42.932 31.954 0.178  1.00 48.93 ? 376 GLN A CB    1 
HETATM 2801 N N1    . FMN B 2 .   ? 24.373 21.998 22.005 1.00 13.80 ? 401 FMN A N1    1 
HETATM 2802 C C2    . FMN B 2 .   ? 23.012 22.013 21.926 1.00 14.24 ? 401 FMN A C2    1 
HETATM 2803 O O2    . FMN B 2 .   ? 22.351 20.963 21.908 1.00 14.85 ? 401 FMN A O2    1 
HETATM 2804 N N3    . FMN B 2 .   ? 22.365 23.212 21.831 1.00 13.95 ? 401 FMN A N3    1 
HETATM 2805 C C4    . FMN B 2 .   ? 23.023 24.428 21.861 1.00 17.24 ? 401 FMN A C4    1 
HETATM 2806 O O4    . FMN B 2 .   ? 22.382 25.482 21.751 1.00 16.48 ? 401 FMN A O4    1 
HETATM 2807 C C4A   . FMN B 2 .   ? 24.411 24.414 21.978 1.00 14.77 ? 401 FMN A C4A   1 
HETATM 2808 N N5    . FMN B 2 .   ? 25.131 25.587 22.023 1.00 17.52 ? 401 FMN A N5    1 
HETATM 2809 C C5A   . FMN B 2 .   ? 26.498 25.532 22.010 1.00 16.62 ? 401 FMN A C5A   1 
HETATM 2810 C C6    . FMN B 2 .   ? 27.214 26.718 21.971 1.00 15.55 ? 401 FMN A C6    1 
HETATM 2811 C C7    . FMN B 2 .   ? 28.585 26.679 21.974 1.00 15.39 ? 401 FMN A C7    1 
HETATM 2812 C C7M   . FMN B 2 .   ? 29.330 27.989 21.963 1.00 21.37 ? 401 FMN A C7M   1 
HETATM 2813 C C8    . FMN B 2 .   ? 29.267 25.484 22.030 1.00 19.04 ? 401 FMN A C8    1 
HETATM 2814 C C8M   . FMN B 2 .   ? 30.768 25.473 22.071 1.00 25.42 ? 401 FMN A C8M   1 
HETATM 2815 C C9    . FMN B 2 .   ? 28.552 24.288 22.072 1.00 19.79 ? 401 FMN A C9    1 
HETATM 2816 C C9A   . FMN B 2 .   ? 27.158 24.313 22.026 1.00 16.47 ? 401 FMN A C9A   1 
HETATM 2817 N N10   . FMN B 2 .   ? 26.436 23.134 22.069 1.00 14.85 ? 401 FMN A N10   1 
HETATM 2818 C C10   . FMN B 2 .   ? 25.068 23.189 22.017 1.00 14.56 ? 401 FMN A C10   1 
HETATM 2819 C "C1'" . FMN B 2 .   ? 27.140 21.808 22.059 1.00 15.12 ? 401 FMN A "C1'" 1 
HETATM 2820 C "C2'" . FMN B 2 .   ? 27.550 21.474 20.607 1.00 16.24 ? 401 FMN A "C2'" 1 
HETATM 2821 O "O2'" . FMN B 2 .   ? 26.389 21.280 19.816 1.00 15.09 ? 401 FMN A "O2'" 1 
HETATM 2822 C "C3'" . FMN B 2 .   ? 28.466 20.238 20.456 1.00 15.06 ? 401 FMN A "C3'" 1 
HETATM 2823 O "O3'" . FMN B 2 .   ? 27.723 19.126 20.913 1.00 18.18 ? 401 FMN A "O3'" 1 
HETATM 2824 C "C4'" . FMN B 2 .   ? 29.694 20.350 21.350 1.00 18.98 ? 401 FMN A "C4'" 1 
HETATM 2825 O "O4'" . FMN B 2 .   ? 30.370 21.568 21.084 1.00 19.71 ? 401 FMN A "O4'" 1 
HETATM 2826 C "C5'" . FMN B 2 .   ? 30.632 19.166 21.109 1.00 21.07 ? 401 FMN A "C5'" 1 
HETATM 2827 O "O5'" . FMN B 2 .   ? 30.928 19.041 19.723 1.00 18.07 ? 401 FMN A "O5'" 1 
HETATM 2828 P P     . FMN B 2 .   ? 32.311 19.594 19.099 1.00 17.08 ? 401 FMN A P     1 
HETATM 2829 O O1P   . FMN B 2 .   ? 33.471 18.899 19.785 1.00 19.25 ? 401 FMN A O1P   1 
HETATM 2830 O O2P   . FMN B 2 .   ? 32.365 21.075 19.312 1.00 16.93 ? 401 FMN A O2P   1 
HETATM 2831 O O3P   . FMN B 2 .   ? 32.271 19.255 17.639 1.00 17.42 ? 401 FMN A O3P   1 
HETATM 2832 C C1    . MPD C 3 .   ? 25.107 26.420 25.447 0.88 32.77 ? 402 MPD A C1    1 
HETATM 2833 C C2    . MPD C 3 .   ? 25.847 25.412 26.321 0.88 28.88 ? 402 MPD A C2    1 
HETATM 2834 O O2    . MPD C 3 .   ? 24.858 24.523 26.848 0.88 29.15 ? 402 MPD A O2    1 
HETATM 2835 C CM    . MPD C 3 .   ? 26.572 26.165 27.437 0.88 41.87 ? 402 MPD A CM    1 
HETATM 2836 C C3    . MPD C 3 .   ? 26.873 24.602 25.509 0.88 36.76 ? 402 MPD A C3    1 
HETATM 2837 C C4    . MPD C 3 .   ? 27.766 23.704 26.366 0.88 35.57 ? 402 MPD A C4    1 
HETATM 2838 O O4    . MPD C 3 .   ? 26.928 22.991 27.273 0.88 42.33 ? 402 MPD A O4    1 
HETATM 2839 C C5    . MPD C 3 .   ? 28.568 22.716 25.538 0.88 36.55 ? 402 MPD A C5    1 
HETATM 2840 S S     . SO4 D 4 .   ? 40.609 32.967 22.790 0.74 34.81 ? 403 SO4 A S     1 
HETATM 2841 O O1    . SO4 D 4 .   ? 41.777 33.426 21.973 0.74 39.10 ? 403 SO4 A O1    1 
HETATM 2842 O O2    . SO4 D 4 .   ? 40.327 31.527 22.446 0.74 28.07 ? 403 SO4 A O2    1 
HETATM 2843 O O3    . SO4 D 4 .   ? 39.433 33.875 22.522 0.74 31.71 ? 403 SO4 A O3    1 
HETATM 2844 O O4    . SO4 D 4 .   ? 40.933 33.042 24.241 0.74 35.07 ? 403 SO4 A O4    1 
HETATM 2845 O O     . HOH E 5 .   ? 15.334 9.410  -2.330 1.00 42.86 ? 501 HOH A O     1 
HETATM 2846 O O     . HOH E 5 .   ? 9.015  41.797 19.884 1.00 45.76 ? 502 HOH A O     1 
HETATM 2847 O O     . HOH E 5 .   ? 23.981 27.916 31.783 1.00 27.30 ? 503 HOH A O     1 
HETATM 2848 O O     . HOH E 5 .   ? 43.164 34.221 25.385 1.00 43.35 ? 504 HOH A O     1 
HETATM 2849 O O     . HOH E 5 .   ? 33.569 10.448 29.371 1.00 42.28 ? 505 HOH A O     1 
HETATM 2850 O O     . HOH E 5 .   ? 3.373  7.035  18.500 1.00 36.16 ? 506 HOH A O     1 
HETATM 2851 O O     . HOH E 5 .   ? 27.129 27.124 34.287 1.00 28.90 ? 507 HOH A O     1 
HETATM 2852 O O     . HOH E 5 .   ? 32.916 5.629  15.591 1.00 31.31 ? 508 HOH A O     1 
HETATM 2853 O O     . HOH E 5 .   ? 24.922 13.174 32.642 1.00 33.70 ? 509 HOH A O     1 
HETATM 2854 O O     . HOH E 5 .   ? 42.555 30.673 21.781 1.00 46.08 ? 510 HOH A O     1 
HETATM 2855 O O     . HOH E 5 .   ? 27.080 38.534 38.223 1.00 45.11 ? 511 HOH A O     1 
HETATM 2856 O O     . HOH E 5 .   ? 15.146 46.550 22.273 1.00 32.07 ? 512 HOH A O     1 
HETATM 2857 O O     . HOH E 5 .   ? 29.067 14.781 -1.188 1.00 41.63 ? 513 HOH A O     1 
HETATM 2858 O O     . HOH E 5 .   ? 20.336 29.904 -4.939 1.00 27.74 ? 514 HOH A O     1 
HETATM 2859 O O     . HOH E 5 .   ? 10.321 43.803 17.720 1.00 40.34 ? 515 HOH A O     1 
HETATM 2860 O O     . HOH E 5 .   ? 12.374 35.365 2.667  1.00 34.72 ? 516 HOH A O     1 
HETATM 2861 O O     . HOH E 5 .   ? 15.459 39.506 11.133 1.00 33.89 ? 517 HOH A O     1 
HETATM 2862 O O     . HOH E 5 .   ? 36.142 12.812 27.154 1.00 38.38 ? 518 HOH A O     1 
HETATM 2863 O O     . HOH E 5 .   ? 8.003  26.911 31.055 1.00 28.10 ? 519 HOH A O     1 
HETATM 2864 O O     . HOH E 5 .   ? 42.149 34.063 19.315 1.00 38.10 ? 520 HOH A O     1 
HETATM 2865 O O     . HOH E 5 .   ? 0.267  10.773 34.517 1.00 27.68 ? 521 HOH A O     1 
HETATM 2866 O O     . HOH E 5 .   ? 2.996  23.558 38.691 1.00 24.69 ? 522 HOH A O     1 
HETATM 2867 O O     . HOH E 5 .   ? 13.232 36.814 26.936 1.00 29.56 ? 523 HOH A O     1 
HETATM 2868 O O     . HOH E 5 .   ? 28.992 17.971 17.757 1.00 19.63 ? 524 HOH A O     1 
HETATM 2869 O O     . HOH E 5 .   ? 25.228 28.139 15.740 1.00 18.78 ? 525 HOH A O     1 
HETATM 2870 O O     . HOH E 5 .   ? 5.812  23.265 43.249 1.00 39.23 ? 526 HOH A O     1 
HETATM 2871 O O     . HOH E 5 .   ? 14.910 29.724 48.832 1.00 25.24 ? 527 HOH A O     1 
HETATM 2872 O O     . HOH E 5 .   ? 27.961 18.131 23.488 1.00 19.61 ? 528 HOH A O     1 
HETATM 2873 O O     . HOH E 5 .   ? 27.725 43.379 36.960 1.00 44.78 ? 529 HOH A O     1 
HETATM 2874 O O     . HOH E 5 .   ? -0.650 13.450 37.520 1.00 24.17 ? 530 HOH A O     1 
HETATM 2875 O O     . HOH E 5 .   ? 25.018 26.237 30.284 1.00 30.32 ? 531 HOH A O     1 
HETATM 2876 O O     . HOH E 5 .   ? 36.304 18.667 16.585 1.00 25.07 ? 532 HOH A O     1 
HETATM 2877 O O     . HOH E 5 .   ? 26.980 12.923 -2.602 1.00 36.40 ? 533 HOH A O     1 
HETATM 2878 O O     . HOH E 5 .   ? 5.588  26.730 32.726 1.00 36.40 ? 534 HOH A O     1 
HETATM 2879 O O     . HOH E 5 .   ? 18.590 5.930  4.896  1.00 41.96 ? 535 HOH A O     1 
HETATM 2880 O O     . HOH E 5 .   ? 36.558 35.916 13.924 1.00 35.10 ? 536 HOH A O     1 
HETATM 2881 O O     . HOH E 5 .   ? 5.475  3.599  36.111 1.00 44.99 ? 537 HOH A O     1 
HETATM 2882 O O     . HOH E 5 .   ? 33.960 33.154 17.911 1.00 19.60 ? 538 HOH A O     1 
HETATM 2883 O O     . HOH E 5 .   ? 26.473 39.647 10.172 1.00 29.84 ? 539 HOH A O     1 
HETATM 2884 O O     . HOH E 5 .   ? 16.186 9.174  8.960  1.00 21.49 ? 540 HOH A O     1 
HETATM 2885 O O     . HOH E 5 .   ? 14.039 21.721 1.923  1.00 30.46 ? 541 HOH A O     1 
HETATM 2886 O O     . HOH E 5 .   ? 33.229 2.427  17.536 1.00 48.91 ? 542 HOH A O     1 
HETATM 2887 O O     . HOH E 5 .   ? 38.287 30.867 8.958  1.00 26.13 ? 543 HOH A O     1 
HETATM 2888 O O     . HOH E 5 .   ? 19.407 4.765  36.243 1.00 34.11 ? 544 HOH A O     1 
HETATM 2889 O O     . HOH E 5 .   ? 24.036 15.219 40.280 1.00 41.40 ? 545 HOH A O     1 
HETATM 2890 O O     . HOH E 5 .   ? 37.912 38.233 8.216  1.00 47.10 ? 546 HOH A O     1 
HETATM 2891 O O     . HOH E 5 .   ? 25.287 4.986  7.210  1.00 21.50 ? 547 HOH A O     1 
HETATM 2892 O O     . HOH E 5 .   ? 29.466 26.926 2.767  1.00 34.53 ? 548 HOH A O     1 
HETATM 2893 O O     . HOH E 5 .   ? 12.916 32.588 29.780 1.00 19.62 ? 549 HOH A O     1 
HETATM 2894 O O     . HOH E 5 .   ? -6.393 23.199 30.534 1.00 30.14 ? 550 HOH A O     1 
HETATM 2895 O O     . HOH E 5 .   ? 2.491  5.742  35.211 1.00 43.36 ? 551 HOH A O     1 
HETATM 2896 O O     . HOH E 5 .   ? 21.395 31.969 -0.208 1.00 24.50 ? 552 HOH A O     1 
HETATM 2897 O O     . HOH E 5 .   ? 14.405 21.297 24.925 1.00 17.36 ? 553 HOH A O     1 
HETATM 2898 O O     . HOH E 5 .   ? 7.549  2.441  37.134 1.00 33.85 ? 554 HOH A O     1 
HETATM 2899 O O     . HOH E 5 .   ? 23.207 27.863 42.685 1.00 21.91 ? 555 HOH A O     1 
HETATM 2900 O O     . HOH E 5 .   ? 43.547 16.374 8.757  1.00 39.64 ? 556 HOH A O     1 
HETATM 2901 O O     . HOH E 5 .   ? 38.510 13.764 1.476  1.00 38.70 ? 557 HOH A O     1 
HETATM 2902 O O     . HOH E 5 .   ? 16.337 15.945 46.783 1.00 26.29 ? 558 HOH A O     1 
HETATM 2903 O O     . HOH E 5 .   ? 7.998  30.367 38.634 1.00 31.89 ? 559 HOH A O     1 
HETATM 2904 O O     . HOH E 5 .   ? 31.457 2.117  27.568 1.00 34.73 ? 560 HOH A O     1 
HETATM 2905 O O     . HOH E 5 .   ? 16.594 22.183 0.917  1.00 24.65 ? 561 HOH A O     1 
HETATM 2906 O O     . HOH E 5 .   ? 26.487 22.492 5.274  1.00 20.53 ? 562 HOH A O     1 
HETATM 2907 O O     . HOH E 5 .   ? 11.986 12.488 -0.578 1.00 33.03 ? 563 HOH A O     1 
HETATM 2908 O O     . HOH E 5 .   ? 0.322  18.936 23.747 1.00 26.06 ? 564 HOH A O     1 
HETATM 2909 O O     . HOH E 5 .   ? 31.554 39.709 19.175 1.00 25.03 ? 565 HOH A O     1 
HETATM 2910 O O     . HOH E 5 .   ? 25.592 6.329  0.054  1.00 36.62 ? 566 HOH A O     1 
HETATM 2911 O O     . HOH E 5 .   ? 21.322 38.374 6.344  1.00 33.73 ? 567 HOH A O     1 
HETATM 2912 O O     . HOH E 5 .   ? 44.437 33.211 21.860 1.00 34.12 ? 568 HOH A O     1 
HETATM 2913 O O     . HOH E 5 .   ? 18.402 17.379 0.746  1.00 38.01 ? 569 HOH A O     1 
HETATM 2914 O O     . HOH E 5 .   ? 2.148  14.847 40.894 1.00 26.18 ? 570 HOH A O     1 
HETATM 2915 O O     . HOH E 5 .   ? 34.307 38.103 25.535 1.00 42.91 ? 571 HOH A O     1 
HETATM 2916 O O     . HOH E 5 .   ? 14.376 23.722 47.300 1.00 34.21 ? 572 HOH A O     1 
HETATM 2917 O O     . HOH E 5 .   ? 35.571 27.241 0.486  1.00 33.10 ? 573 HOH A O     1 
HETATM 2918 O O     . HOH E 5 .   ? 8.257  5.914  29.935 1.00 31.64 ? 574 HOH A O     1 
HETATM 2919 O O     . HOH E 5 .   ? 14.080 9.807  40.284 1.00 28.81 ? 575 HOH A O     1 
HETATM 2920 O O     . HOH E 5 .   ? 23.643 32.213 30.336 1.00 19.81 ? 576 HOH A O     1 
HETATM 2921 O O     . HOH E 5 .   ? 41.140 19.013 7.375  1.00 31.14 ? 577 HOH A O     1 
HETATM 2922 O O     . HOH E 5 .   ? 11.327 26.850 44.829 1.00 39.35 ? 578 HOH A O     1 
HETATM 2923 O O     . HOH E 5 .   ? 20.076 -0.126 14.661 1.00 32.70 ? 579 HOH A O     1 
HETATM 2924 O O     . HOH E 5 .   ? 16.885 -0.085 24.389 1.00 26.45 ? 580 HOH A O     1 
HETATM 2925 O O     . HOH E 5 .   ? 10.785 20.806 4.135  1.00 27.93 ? 581 HOH A O     1 
HETATM 2926 O O     . HOH E 5 .   ? 36.990 38.512 14.894 1.00 38.95 ? 582 HOH A O     1 
HETATM 2927 O O     . HOH E 5 .   ? 29.961 8.420  24.296 1.00 23.35 ? 583 HOH A O     1 
HETATM 2928 O O     . HOH E 5 .   ? 19.121 -1.124 30.953 1.00 25.50 ? 584 HOH A O     1 
HETATM 2929 O O     . HOH E 5 .   ? 40.842 31.868 13.100 1.00 21.60 ? 585 HOH A O     1 
HETATM 2930 O O     . HOH E 5 .   ? 10.469 -0.188 22.118 1.00 37.13 ? 586 HOH A O     1 
HETATM 2931 O O     . HOH E 5 .   ? 27.484 8.065  36.815 1.00 43.32 ? 587 HOH A O     1 
HETATM 2932 O O     . HOH E 5 .   ? 43.713 25.942 5.532  1.00 39.77 ? 588 HOH A O     1 
HETATM 2933 O O     . HOH E 5 .   ? 16.238 38.669 29.829 1.00 26.61 ? 589 HOH A O     1 
HETATM 2934 O O     . HOH E 5 .   ? 23.998 31.317 15.575 1.00 22.98 ? 590 HOH A O     1 
HETATM 2935 O O     . HOH E 5 .   ? 31.053 26.748 25.311 1.00 41.49 ? 591 HOH A O     1 
HETATM 2936 O O     . HOH E 5 .   ? 35.735 8.085  21.838 1.00 33.41 ? 592 HOH A O     1 
HETATM 2937 O O     . HOH E 5 .   ? 14.023 31.259 43.064 1.00 28.08 ? 593 HOH A O     1 
HETATM 2938 O O     . HOH E 5 .   ? 44.701 23.496 12.090 1.00 19.59 ? 594 HOH A O     1 
HETATM 2939 O O     . HOH E 5 .   ? 29.489 45.086 19.366 1.00 33.69 ? 595 HOH A O     1 
HETATM 2940 O O     . HOH E 5 .   ? 32.324 -2.155 12.039 1.00 40.94 ? 596 HOH A O     1 
HETATM 2941 O O     . HOH E 5 .   ? 22.792 33.787 17.512 1.00 20.52 ? 597 HOH A O     1 
HETATM 2942 O O     . HOH E 5 .   ? 22.093 2.923  9.095  1.00 30.58 ? 598 HOH A O     1 
HETATM 2943 O O     . HOH E 5 .   ? 9.148  36.828 6.577  1.00 26.13 ? 599 HOH A O     1 
HETATM 2944 O O     . HOH E 5 .   ? 32.569 45.478 17.538 1.00 27.11 ? 600 HOH A O     1 
HETATM 2945 O O     . HOH E 5 .   ? 4.965  7.472  43.054 1.00 42.91 ? 601 HOH A O     1 
HETATM 2946 O O     . HOH E 5 .   ? 7.522  26.280 28.548 1.00 23.27 ? 602 HOH A O     1 
HETATM 2947 O O     . HOH E 5 .   ? 35.582 41.680 11.711 1.00 38.22 ? 603 HOH A O     1 
HETATM 2948 O O     . HOH E 5 .   ? 32.448 33.148 9.356  1.00 21.39 ? 604 HOH A O     1 
HETATM 2949 O O     . HOH E 5 .   ? 17.332 17.417 42.875 1.00 25.06 ? 605 HOH A O     1 
HETATM 2950 O O     . HOH E 5 .   ? 36.039 19.405 19.017 1.00 27.27 ? 606 HOH A O     1 
HETATM 2951 O O     . HOH E 5 .   ? 25.415 42.681 25.112 1.00 24.03 ? 607 HOH A O     1 
HETATM 2952 O O     . HOH E 5 .   ? 15.729 7.687  12.407 1.00 19.88 ? 608 HOH A O     1 
HETATM 2953 O O     . HOH E 5 .   ? 25.456 10.619 33.486 1.00 25.40 ? 609 HOH A O     1 
HETATM 2954 O O     . HOH E 5 .   ? 20.335 13.501 27.944 1.00 19.55 ? 610 HOH A O     1 
HETATM 2955 O O     . HOH E 5 .   ? 2.126  12.236 12.988 1.00 38.61 ? 611 HOH A O     1 
HETATM 2956 O O     . HOH E 5 .   ? 26.296 20.640 7.117  1.00 18.63 ? 612 HOH A O     1 
HETATM 2957 O O     . HOH E 5 .   ? 3.346  33.325 21.896 1.00 47.01 ? 613 HOH A O     1 
HETATM 2958 O O     . HOH E 5 .   ? 16.811 23.745 -1.431 1.00 29.27 ? 614 HOH A O     1 
HETATM 2959 O O     . HOH E 5 .   ? 17.744 5.785  40.516 1.00 32.72 ? 615 HOH A O     1 
HETATM 2960 O O     . HOH E 5 .   ? 36.595 36.883 17.499 1.00 30.76 ? 616 HOH A O     1 
HETATM 2961 O O     . HOH E 5 .   ? 4.614  24.728 40.810 1.00 33.24 ? 617 HOH A O     1 
HETATM 2962 O O     . HOH E 5 .   ? 21.531 28.513 31.092 1.00 21.24 ? 618 HOH A O     1 
HETATM 2963 O O     . HOH E 5 .   ? 31.233 44.576 13.692 1.00 23.94 ? 619 HOH A O     1 
HETATM 2964 O O     . HOH E 5 .   ? 23.899 15.920 30.176 1.00 24.49 ? 620 HOH A O     1 
HETATM 2965 O O     . HOH E 5 .   ? 22.927 -2.041 22.002 1.00 20.80 ? 621 HOH A O     1 
HETATM 2966 O O     . HOH E 5 .   ? 35.644 1.145  22.381 1.00 45.29 ? 622 HOH A O     1 
HETATM 2967 O O     . HOH E 5 .   ? 41.489 11.781 15.105 1.00 36.53 ? 623 HOH A O     1 
HETATM 2968 O O     . HOH E 5 .   ? 45.928 29.404 20.218 1.00 27.05 ? 624 HOH A O     1 
HETATM 2969 O O     . HOH E 5 .   ? 31.648 -1.174 8.045  1.00 45.54 ? 625 HOH A O     1 
HETATM 2970 O O     . HOH E 5 .   ? 25.209 28.936 40.996 1.00 21.59 ? 626 HOH A O     1 
HETATM 2971 O O     . HOH E 5 .   ? 0.401  12.850 40.057 1.00 27.50 ? 627 HOH A O     1 
HETATM 2972 O O     . HOH E 5 .   ? 41.005 8.485  25.711 1.00 48.49 ? 628 HOH A O     1 
HETATM 2973 O O     . HOH E 5 .   ? 8.690  38.244 19.253 1.00 28.18 ? 629 HOH A O     1 
HETATM 2974 O O     . HOH E 5 .   ? 20.687 29.652 21.377 1.00 17.54 ? 630 HOH A O     1 
HETATM 2975 O O     . HOH E 5 .   ? 33.030 8.120  20.942 1.00 27.93 ? 631 HOH A O     1 
HETATM 2976 O O     . HOH E 5 .   ? 18.942 26.224 39.442 1.00 17.95 ? 632 HOH A O     1 
HETATM 2977 O O     . HOH E 5 .   ? 27.716 4.213  8.652  1.00 25.53 ? 633 HOH A O     1 
HETATM 2978 O O     . HOH E 5 .   ? 17.417 34.622 39.985 1.00 26.64 ? 634 HOH A O     1 
HETATM 2979 O O     . HOH E 5 .   ? 6.747  10.733 9.074  1.00 34.78 ? 635 HOH A O     1 
HETATM 2980 O O     . HOH E 5 .   ? 43.241 13.641 13.537 1.00 39.08 ? 636 HOH A O     1 
HETATM 2981 O O     . HOH E 5 .   ? 24.186 25.713 14.931 1.00 17.56 ? 637 HOH A O     1 
HETATM 2982 O O     . HOH E 5 .   ? 33.685 30.982 25.608 1.00 42.82 ? 638 HOH A O     1 
HETATM 2983 O O     . HOH E 5 .   ? 30.365 24.375 5.218  1.00 18.90 ? 639 HOH A O     1 
HETATM 2984 O O     . HOH E 5 .   ? 28.915 5.156  17.361 1.00 30.24 ? 640 HOH A O     1 
HETATM 2985 O O     . HOH E 5 .   ? 23.575 41.728 26.873 1.00 20.03 ? 641 HOH A O     1 
HETATM 2986 O O     . HOH E 5 .   ? 2.297  13.989 24.472 1.00 24.40 ? 642 HOH A O     1 
HETATM 2987 O O     . HOH E 5 .   ? 5.756  15.169 7.975  1.00 34.58 ? 643 HOH A O     1 
HETATM 2988 O O     . HOH E 5 .   ? 12.871 9.973  42.982 1.00 37.46 ? 644 HOH A O     1 
HETATM 2989 O O     . HOH E 5 .   ? 15.895 28.561 25.539 1.00 18.57 ? 645 HOH A O     1 
HETATM 2990 O O     . HOH E 5 .   ? 35.475 10.561 23.141 1.00 36.54 ? 646 HOH A O     1 
HETATM 2991 O O     . HOH E 5 .   ? 39.605 33.937 2.357  1.00 40.22 ? 647 HOH A O     1 
HETATM 2992 O O     . HOH E 5 .   ? 2.134  27.572 13.543 1.00 38.38 ? 648 HOH A O     1 
HETATM 2993 O O     . HOH E 5 .   ? 31.181 31.992 14.028 1.00 17.88 ? 649 HOH A O     1 
HETATM 2994 O O     . HOH E 5 .   ? 27.657 19.927 -1.322 1.00 38.32 ? 650 HOH A O     1 
HETATM 2995 O O     . HOH E 5 .   ? 12.571 38.462 40.956 1.00 43.92 ? 651 HOH A O     1 
HETATM 2996 O O     . HOH E 5 .   ? 20.171 33.886 41.889 1.00 30.69 ? 652 HOH A O     1 
HETATM 2997 O O     . HOH E 5 .   ? 12.252 12.647 30.437 1.00 18.17 ? 653 HOH A O     1 
HETATM 2998 O O     . HOH E 5 .   ? 2.258  19.754 10.420 1.00 34.35 ? 654 HOH A O     1 
HETATM 2999 O O     . HOH E 5 .   ? 21.823 31.860 20.325 1.00 18.84 ? 655 HOH A O     1 
HETATM 3000 O O     . HOH E 5 .   ? 9.489  30.391 34.999 1.00 30.76 ? 656 HOH A O     1 
HETATM 3001 O O     . HOH E 5 .   ? 34.101 20.582 16.030 1.00 18.47 ? 657 HOH A O     1 
HETATM 3002 O O     . HOH E 5 .   ? 2.612  24.802 10.783 1.00 25.97 ? 658 HOH A O     1 
HETATM 3003 O O     . HOH E 5 .   ? 10.971 1.582  15.762 1.00 26.97 ? 659 HOH A O     1 
HETATM 3004 O O     . HOH E 5 .   ? 12.127 27.946 2.238  1.00 37.68 ? 660 HOH A O     1 
HETATM 3005 O O     . HOH E 5 .   ? 13.115 19.118 45.204 1.00 25.02 ? 661 HOH A O     1 
HETATM 3006 O O     . HOH E 5 .   ? 15.640 20.497 27.604 1.00 18.78 ? 662 HOH A O     1 
HETATM 3007 O O     . HOH E 5 .   ? 20.168 2.815  10.826 1.00 34.31 ? 663 HOH A O     1 
HETATM 3008 O O     . HOH E 5 .   ? 33.815 35.572 6.488  1.00 33.07 ? 664 HOH A O     1 
HETATM 3009 O O     . HOH E 5 .   ? 23.388 22.910 25.061 1.00 22.10 ? 665 HOH A O     1 
HETATM 3010 O O     . HOH E 5 .   ? 15.336 35.861 3.020  1.00 28.77 ? 666 HOH A O     1 
HETATM 3011 O O     . HOH E 5 .   ? 13.152 39.620 34.803 1.00 39.37 ? 667 HOH A O     1 
HETATM 3012 O O     . HOH E 5 .   ? 10.119 23.972 3.840  1.00 40.21 ? 668 HOH A O     1 
HETATM 3013 O O     . HOH E 5 .   ? 1.829  26.951 16.882 1.00 26.59 ? 669 HOH A O     1 
HETATM 3014 O O     . HOH E 5 .   ? 32.077 16.521 17.117 1.00 18.05 ? 670 HOH A O     1 
HETATM 3015 O O     . HOH E 5 .   ? -4.861 26.460 32.945 1.00 25.85 ? 671 HOH A O     1 
HETATM 3016 O O     . HOH E 5 .   ? 10.272 15.228 45.841 1.00 40.46 ? 672 HOH A O     1 
HETATM 3017 O O     . HOH E 5 .   ? -0.791 19.063 12.818 1.00 32.59 ? 673 HOH A O     1 
HETATM 3018 O O     . HOH E 5 .   ? 31.539 22.120 23.562 1.00 23.78 ? 674 HOH A O     1 
HETATM 3019 O O     . HOH E 5 .   ? 12.305 2.371  28.143 1.00 31.80 ? 675 HOH A O     1 
HETATM 3020 O O     . HOH E 5 .   ? 30.681 39.535 7.817  1.00 36.53 ? 676 HOH A O     1 
HETATM 3021 O O     . HOH E 5 .   ? 2.973  36.179 10.657 1.00 39.25 ? 677 HOH A O     1 
HETATM 3022 O O     . HOH E 5 .   ? 15.527 41.261 32.565 1.00 29.46 ? 678 HOH A O     1 
HETATM 3023 O O     . HOH E 5 .   ? 32.755 7.099  18.653 1.00 32.10 ? 679 HOH A O     1 
HETATM 3024 O O     . HOH E 5 .   ? 8.253  23.651 6.560  1.00 28.23 ? 680 HOH A O     1 
HETATM 3025 O O     . HOH E 5 .   ? 20.500 21.102 35.755 1.00 16.63 ? 681 HOH A O     1 
HETATM 3026 O O     . HOH E 5 .   ? 45.163 27.559 9.564  1.00 19.82 ? 682 HOH A O     1 
HETATM 3027 O O     . HOH E 5 .   ? -3.386 18.110 31.245 1.00 19.73 ? 683 HOH A O     1 
HETATM 3028 O O     . HOH E 5 .   ? 14.790 44.082 19.311 1.00 48.42 ? 684 HOH A O     1 
HETATM 3029 O O     . HOH E 5 .   ? 4.210  28.836 28.324 1.00 37.43 ? 685 HOH A O     1 
HETATM 3030 O O     . HOH E 5 .   ? 7.676  7.431  41.649 1.00 33.07 ? 686 HOH A O     1 
HETATM 3031 O O     . HOH E 5 .   ? 31.724 34.722 24.622 1.00 22.97 ? 687 HOH A O     1 
HETATM 3032 O O     . HOH E 5 .   ? 26.789 11.227 26.595 1.00 22.19 ? 688 HOH A O     1 
HETATM 3033 O O     . HOH E 5 .   ? 23.619 -1.296 14.189 1.00 33.28 ? 689 HOH A O     1 
HETATM 3034 O O     . HOH E 5 .   ? 20.797 -3.568 15.853 1.00 24.48 ? 690 HOH A O     1 
HETATM 3035 O O     . HOH E 5 .   ? -0.152 12.547 20.544 1.00 38.54 ? 691 HOH A O     1 
HETATM 3036 O O     . HOH E 5 .   ? 0.021  18.297 26.400 1.00 21.88 ? 692 HOH A O     1 
HETATM 3037 O O     . HOH E 5 .   ? 21.063 11.614 -1.125 1.00 28.53 ? 693 HOH A O     1 
HETATM 3038 O O     . HOH E 5 .   ? 5.888  30.385 29.531 1.00 30.16 ? 694 HOH A O     1 
HETATM 3039 O O     . HOH E 5 .   ? 21.085 3.727  14.865 1.00 21.36 ? 695 HOH A O     1 
HETATM 3040 O O     . HOH E 5 .   ? 15.547 7.457  40.531 1.00 29.46 ? 696 HOH A O     1 
HETATM 3041 O O     . HOH E 5 .   ? 10.793 35.943 27.894 1.00 29.42 ? 697 HOH A O     1 
HETATM 3042 O O     . HOH E 5 .   ? 11.071 1.364  34.656 1.00 21.88 ? 698 HOH A O     1 
HETATM 3043 O O     . HOH E 5 .   ? 27.400 23.751 -1.670 1.00 31.48 ? 699 HOH A O     1 
HETATM 3044 O O     . HOH E 5 .   ? 31.362 4.584  18.511 1.00 25.80 ? 700 HOH A O     1 
HETATM 3045 O O     . HOH E 5 .   ? 13.151 12.275 46.628 1.00 24.24 ? 701 HOH A O     1 
HETATM 3046 O O     . HOH E 5 .   ? 40.352 16.902 11.815 1.00 33.10 ? 702 HOH A O     1 
HETATM 3047 O O     . HOH E 5 .   ? 1.109  25.640 26.982 1.00 33.89 ? 703 HOH A O     1 
HETATM 3048 O O     . HOH E 5 .   ? 41.142 28.682 20.661 1.00 34.17 ? 704 HOH A O     1 
HETATM 3049 O O     . HOH E 5 .   ? 8.930  0.504  28.228 1.00 47.28 ? 705 HOH A O     1 
HETATM 3050 O O     . HOH E 5 .   ? 15.193 35.976 28.711 1.00 21.09 ? 706 HOH A O     1 
HETATM 3051 O O     . HOH E 5 .   ? 38.917 16.511 18.706 1.00 35.80 ? 707 HOH A O     1 
HETATM 3052 O O     . HOH E 5 .   ? 16.634 -1.497 21.556 1.00 35.50 ? 708 HOH A O     1 
HETATM 3053 O O     . HOH E 5 .   ? 36.571 34.649 3.237  1.00 30.09 ? 709 HOH A O     1 
HETATM 3054 O O     . HOH E 5 .   ? 16.181 6.920  6.399  1.00 45.08 ? 710 HOH A O     1 
HETATM 3055 O O     . HOH E 5 .   ? 39.308 32.351 26.472 1.00 47.82 ? 711 HOH A O     1 
HETATM 3056 O O     . HOH E 5 .   ? 4.577  28.416 23.328 1.00 37.72 ? 712 HOH A O     1 
HETATM 3057 O O     . HOH E 5 .   ? 21.542 15.856 -2.139 1.00 34.32 ? 713 HOH A O     1 
HETATM 3058 O O     . HOH E 5 .   ? 38.166 4.675  27.703 1.00 47.22 ? 714 HOH A O     1 
HETATM 3059 O O     . HOH E 5 .   ? 35.383 7.054  15.061 1.00 29.21 ? 715 HOH A O     1 
HETATM 3060 O O     . HOH E 5 .   ? 16.984 35.602 26.651 1.00 20.22 ? 716 HOH A O     1 
HETATM 3061 O O     . HOH E 5 .   ? 21.427 20.033 41.872 1.00 35.50 ? 717 HOH A O     1 
HETATM 3062 O O     . HOH E 5 .   ? 12.888 9.203  8.889  1.00 32.30 ? 718 HOH A O     1 
HETATM 3063 O O     . HOH E 5 .   ? 4.527  10.404 11.976 1.00 28.53 ? 719 HOH A O     1 
HETATM 3064 O O     . HOH E 5 .   ? 10.735 17.216 42.762 1.00 27.44 ? 720 HOH A O     1 
HETATM 3065 O O     . HOH E 5 .   ? 9.777  12.105 33.141 1.00 16.89 ? 721 HOH A O     1 
HETATM 3066 O O     . HOH E 5 .   ? 16.226 4.236  38.578 1.00 35.86 ? 722 HOH A O     1 
HETATM 3067 O O     . HOH E 5 .   ? 15.921 37.306 9.885  1.00 28.42 ? 723 HOH A O     1 
HETATM 3068 O O     . HOH E 5 .   ? 40.791 30.642 5.578  1.00 33.52 ? 724 HOH A O     1 
HETATM 3069 O O     . HOH E 5 .   ? 18.480 42.242 11.901 1.00 29.61 ? 725 HOH A O     1 
HETATM 3070 O O     . HOH E 5 .   ? 25.045 16.802 6.097  1.00 17.89 ? 726 HOH A O     1 
HETATM 3071 O O     . HOH E 5 .   ? 11.061 38.096 20.985 1.00 26.49 ? 727 HOH A O     1 
HETATM 3072 O O     . HOH E 5 .   ? 25.373 30.272 31.241 1.00 23.46 ? 728 HOH A O     1 
HETATM 3073 O O     . HOH E 5 .   ? 30.957 10.153 28.862 1.00 35.86 ? 729 HOH A O     1 
HETATM 3074 O O     . HOH E 5 .   ? 43.016 28.495 6.314  1.00 38.52 ? 730 HOH A O     1 
HETATM 3075 O O     . HOH E 5 .   ? 24.744 25.507 -3.311 1.00 33.80 ? 731 HOH A O     1 
HETATM 3076 O O     . HOH E 5 .   ? 17.685 18.715 28.467 1.00 16.29 ? 732 HOH A O     1 
HETATM 3077 O O     . HOH E 5 .   ? 9.844  8.296  43.069 1.00 42.02 ? 733 HOH A O     1 
HETATM 3078 O O     . HOH E 5 .   ? 18.334 29.675 26.615 1.00 18.18 ? 734 HOH A O     1 
HETATM 3079 O O     . HOH E 5 .   ? 28.854 30.077 32.646 1.00 44.42 ? 735 HOH A O     1 
HETATM 3080 O O     . HOH E 5 .   ? 15.919 16.237 -0.158 1.00 28.04 ? 736 HOH A O     1 
HETATM 3081 O O     . HOH E 5 .   ? 2.656  35.933 18.233 1.00 35.55 ? 737 HOH A O     1 
HETATM 3082 O O     . HOH E 5 .   ? -1.601 28.522 32.917 1.00 46.62 ? 738 HOH A O     1 
HETATM 3083 O O     . HOH E 5 .   ? 10.970 37.732 23.811 1.00 31.08 ? 739 HOH A O     1 
HETATM 3084 O O     . HOH E 5 .   ? 41.532 33.803 15.093 1.00 28.65 ? 740 HOH A O     1 
HETATM 3085 O O     . HOH E 5 .   ? 23.192 35.981 40.729 1.00 33.38 ? 741 HOH A O     1 
HETATM 3086 O O     . HOH E 5 .   ? 30.247 27.567 35.629 1.00 37.31 ? 742 HOH A O     1 
HETATM 3087 O O     . HOH E 5 .   ? 4.666  5.643  39.444 1.00 36.53 ? 743 HOH A O     1 
HETATM 3088 O O     . HOH E 5 .   ? -0.455 26.194 35.398 1.00 37.86 ? 744 HOH A O     1 
HETATM 3089 O O     . HOH E 5 .   ? 36.234 20.099 25.289 1.00 44.18 ? 745 HOH A O     1 
HETATM 3090 O O     . HOH E 5 .   ? 27.448 -2.685 22.084 1.00 31.61 ? 746 HOH A O     1 
HETATM 3091 O O     . HOH E 5 .   ? 9.894  1.623  12.984 1.00 46.17 ? 747 HOH A O     1 
HETATM 3092 O O     . HOH E 5 .   ? 23.479 40.653 16.714 1.00 21.31 ? 748 HOH A O     1 
HETATM 3093 O O     . HOH E 5 .   ? 1.287  10.909 31.928 1.00 32.04 ? 749 HOH A O     1 
HETATM 3094 O O     . HOH E 5 .   ? 28.085 37.293 26.606 1.00 31.23 ? 750 HOH A O     1 
HETATM 3095 O O     . HOH E 5 .   ? 29.022 41.719 22.969 1.00 31.62 ? 751 HOH A O     1 
HETATM 3096 O O     . HOH E 5 .   ? 11.336 13.910 6.340  1.00 35.47 ? 752 HOH A O     1 
HETATM 3097 O O     . HOH E 5 .   ? 19.307 9.952  -0.605 1.00 35.85 ? 753 HOH A O     1 
HETATM 3098 O O     . HOH E 5 .   ? 1.836  27.373 36.964 1.00 36.59 ? 754 HOH A O     1 
HETATM 3099 O O     . HOH E 5 .   ? 24.359 40.899 36.411 1.00 41.35 ? 755 HOH A O     1 
HETATM 3100 O O     . HOH E 5 .   ? 24.922 4.401  4.482  1.00 40.03 ? 756 HOH A O     1 
HETATM 3101 O O     . HOH E 5 .   ? 26.820 34.697 3.653  1.00 40.36 ? 757 HOH A O     1 
HETATM 3102 O O     . HOH E 5 .   ? 16.486 31.288 44.736 1.00 26.56 ? 758 HOH A O     1 
HETATM 3103 O O     . HOH E 5 .   ? 29.814 35.849 3.749  1.00 41.13 ? 759 HOH A O     1 
HETATM 3104 O O     . HOH E 5 .   ? 3.272  39.742 15.488 1.00 45.56 ? 760 HOH A O     1 
HETATM 3105 O O     . HOH E 5 .   ? 17.747 38.076 26.200 1.00 21.63 ? 761 HOH A O     1 
HETATM 3106 O O     . HOH E 5 .   ? 12.651 27.762 33.380 1.00 19.26 ? 762 HOH A O     1 
HETATM 3107 O O     . HOH E 5 .   ? 21.794 41.598 12.291 1.00 21.50 ? 763 HOH A O     1 
HETATM 3108 O O     . HOH E 5 .   ? 30.447 17.948 24.423 1.00 27.11 ? 764 HOH A O     1 
HETATM 3109 O O     . HOH E 5 .   ? -0.994 17.478 17.269 1.00 27.49 ? 765 HOH A O     1 
HETATM 3110 O O     . HOH E 5 .   ? 28.595 39.314 25.675 1.00 40.46 ? 766 HOH A O     1 
HETATM 3111 O O     . HOH E 5 .   ? 44.126 21.340 10.490 1.00 33.46 ? 767 HOH A O     1 
HETATM 3112 O O     . HOH E 5 .   ? 10.809 -3.013 25.421 1.00 47.92 ? 768 HOH A O     1 
HETATM 3113 O O     . HOH E 5 .   ? 25.738 -0.427 11.497 1.00 43.34 ? 769 HOH A O     1 
HETATM 3114 O O     . HOH E 5 .   ? 8.706  24.129 44.131 1.00 32.52 ? 770 HOH A O     1 
HETATM 3115 O O     . HOH E 5 .   ? -0.877 29.189 14.587 1.00 44.25 ? 771 HOH A O     1 
HETATM 3116 O O     . HOH E 5 .   ? 4.711  18.927 8.893  1.00 28.19 ? 772 HOH A O     1 
HETATM 3117 O O     . HOH E 5 .   ? 9.046  4.752  40.508 1.00 27.35 ? 773 HOH A O     1 
HETATM 3118 O O     . HOH E 5 .   ? 14.266 1.665  37.168 1.00 24.71 ? 774 HOH A O     1 
HETATM 3119 O O     . HOH E 5 .   ? 31.879 23.932 2.853  1.00 21.20 ? 775 HOH A O     1 
HETATM 3120 O O     . HOH E 5 .   ? 19.010 1.763  35.583 1.00 31.99 ? 776 HOH A O     1 
HETATM 3121 O O     . HOH E 5 .   ? 31.383 37.444 37.611 1.00 41.66 ? 777 HOH A O     1 
HETATM 3122 O O     . HOH E 5 .   ? 17.358 0.199  29.645 1.00 27.67 ? 778 HOH A O     1 
HETATM 3123 O O     . HOH E 5 .   ? 31.133 15.799 30.953 1.00 42.01 ? 779 HOH A O     1 
HETATM 3124 O O     . HOH E 5 .   ? 26.998 3.126  31.880 1.00 32.52 ? 780 HOH A O     1 
HETATM 3125 O O     . HOH E 5 .   ? 8.671  33.630 41.307 1.00 46.02 ? 781 HOH A O     1 
HETATM 3126 O O     . HOH E 5 .   ? 13.172 -1.311 21.273 1.00 35.01 ? 782 HOH A O     1 
HETATM 3127 O O     . HOH E 5 .   ? 20.895 6.161  2.718  1.00 29.92 ? 783 HOH A O     1 
HETATM 3128 O O     . HOH E 5 .   ? 2.617  31.649 17.982 1.00 37.44 ? 784 HOH A O     1 
HETATM 3129 O O     . HOH E 5 .   ? 4.371  38.310 17.453 1.00 29.68 ? 785 HOH A O     1 
HETATM 3130 O O     . HOH E 5 .   ? 12.725 25.053 49.113 1.00 43.00 ? 786 HOH A O     1 
HETATM 3131 O O     . HOH E 5 .   ? 3.736  7.808  23.049 1.00 31.27 ? 787 HOH A O     1 
HETATM 3132 O O     . HOH E 5 .   ? 15.531 43.626 16.803 1.00 44.60 ? 788 HOH A O     1 
HETATM 3133 O O     . HOH E 5 .   ? 6.176  6.851  28.520 1.00 28.55 ? 789 HOH A O     1 
HETATM 3134 O O     . HOH E 5 .   ? 43.575 28.029 27.489 1.00 27.81 ? 790 HOH A O     1 
HETATM 3135 O O     . HOH E 5 .   ? 26.162 -0.180 32.959 1.00 43.67 ? 791 HOH A O     1 
HETATM 3136 O O     . HOH E 5 .   ? 13.636 -0.983 11.761 1.00 46.25 ? 792 HOH A O     1 
HETATM 3137 O O     . HOH E 5 .   ? 27.811 40.372 27.767 1.00 43.05 ? 793 HOH A O     1 
HETATM 3138 O O     . HOH E 5 .   ? 30.704 7.040  16.186 1.00 33.03 ? 794 HOH A O     1 
HETATM 3139 O O     . HOH E 5 .   ? 18.530 35.839 5.963  1.00 34.18 ? 795 HOH A O     1 
HETATM 3140 O O     . HOH E 5 .   ? 21.811 -2.473 34.553 1.00 26.41 ? 796 HOH A O     1 
HETATM 3141 O O     . HOH E 5 .   ? 32.388 -4.320 25.155 1.00 39.52 ? 797 HOH A O     1 
HETATM 3142 O O     . HOH E 5 .   ? 6.905  30.262 35.279 1.00 37.99 ? 798 HOH A O     1 
HETATM 3143 O O     . HOH E 5 .   ? 7.977  2.601  12.007 1.00 37.73 ? 799 HOH A O     1 
HETATM 3144 O O     . HOH E 5 .   ? 26.307 29.952 46.150 1.00 42.85 ? 800 HOH A O     1 
HETATM 3145 O O     . HOH E 5 .   ? 25.131 -3.304 21.044 1.00 23.03 ? 801 HOH A O     1 
HETATM 3146 O O     . HOH E 5 .   ? 18.837 1.214  12.028 1.00 42.33 ? 802 HOH A O     1 
HETATM 3147 O O     . HOH E 5 .   ? 4.278  8.905  28.309 1.00 40.38 ? 803 HOH A O     1 
HETATM 3148 O O     . HOH E 5 .   ? 44.450 30.615 26.982 1.00 28.26 ? 804 HOH A O     1 
HETATM 3149 O O     . HOH E 5 .   ? 40.082 32.445 10.638 1.00 34.26 ? 805 HOH A O     1 
HETATM 3150 O O     . HOH E 5 .   ? 32.865 33.028 26.410 1.00 38.23 ? 806 HOH A O     1 
HETATM 3151 O O     . HOH E 5 .   ? 16.070 -0.727 27.326 1.00 33.71 ? 807 HOH A O     1 
HETATM 3152 O O     . HOH E 5 .   ? 15.935 39.994 25.626 1.00 33.61 ? 808 HOH A O     1 
HETATM 3153 O O     . HOH E 5 .   ? 29.810 -2.322 9.329  1.00 45.88 ? 809 HOH A O     1 
HETATM 3154 O O     . HOH E 5 .   ? 8.537  3.317  29.604 1.00 36.64 ? 810 HOH A O     1 
HETATM 3155 O O     . HOH E 5 .   ? 16.775 33.331 -0.713 1.00 36.11 ? 811 HOH A O     1 
HETATM 3156 O O     . HOH E 5 .   ? 35.682 12.319 -1.440 1.00 51.33 ? 812 HOH A O     1 
HETATM 3157 O O     . HOH E 5 .   ? -3.529 19.673 20.657 1.00 48.65 ? 813 HOH A O     1 
HETATM 3158 O O     . HOH E 5 .   ? 20.627 0.574  37.519 1.00 36.47 ? 814 HOH A O     1 
HETATM 3159 O O     . HOH E 5 .   ? 13.120 3.877  41.611 1.00 47.05 ? 815 HOH A O     1 
HETATM 3160 O O     . HOH E 5 .   ? 12.070 23.452 1.136  1.00 46.74 ? 816 HOH A O     1 
HETATM 3161 O O     . HOH E 5 .   ? 33.143 0.732  19.968 1.00 43.24 ? 817 HOH A O     1 
HETATM 3162 O O     . HOH E 5 .   ? 8.886  -0.820 20.073 1.00 40.33 ? 818 HOH A O     1 
HETATM 3163 O O     . HOH E 5 .   ? 23.697 28.078 -4.418 1.00 29.28 ? 819 HOH A O     1 
HETATM 3164 O O     . HOH E 5 .   ? 10.861 10.324 0.142  1.00 42.18 ? 820 HOH A O     1 
HETATM 3165 O O     . HOH E 5 .   ? 4.997  19.862 6.465  1.00 38.63 ? 821 HOH A O     1 
HETATM 3166 O O     . HOH E 5 .   ? 14.580 18.921 50.295 1.00 43.77 ? 822 HOH A O     1 
HETATM 3167 O O     . HOH E 5 .   ? 37.894 11.210 24.321 1.00 41.37 ? 823 HOH A O     1 
HETATM 3168 O O     . HOH E 5 .   ? 1.089  7.989  33.954 1.00 46.54 ? 824 HOH A O     1 
HETATM 3169 O O     . HOH E 5 .   ? 13.497 -0.055 28.095 1.00 34.88 ? 825 HOH A O     1 
HETATM 3170 O O     . HOH E 5 .   ? 32.236 20.023 24.897 1.00 42.38 ? 826 HOH A O     1 
HETATM 3171 O O     . HOH E 5 .   ? 11.193 2.851  30.233 1.00 31.87 ? 827 HOH A O     1 
HETATM 3172 O O     . HOH E 5 .   ? 2.653  25.739 8.438  1.00 37.58 ? 828 HOH A O     1 
HETATM 3173 O O     . HOH E 5 .   ? 7.543  2.827  39.703 1.00 40.95 ? 829 HOH A O     1 
HETATM 3174 O O     . HOH E 5 .   ? 5.262  29.287 33.293 1.00 43.55 ? 830 HOH A O     1 
HETATM 3175 O O     . HOH E 5 .   ? 41.285 26.652 22.320 1.00 30.40 ? 831 HOH A O     1 
HETATM 3176 O O     . HOH E 5 .   ? 34.918 39.861 23.756 1.00 41.93 ? 832 HOH A O     1 
HETATM 3177 O O     . HOH E 5 .   ? 3.519  9.671  24.903 1.00 33.60 ? 833 HOH A O     1 
HETATM 3178 O O     . HOH E 5 .   ? 1.529  27.394 39.463 1.00 49.47 ? 834 HOH A O     1 
HETATM 3179 O O     . HOH E 5 .   ? 8.679  0.481  35.958 1.00 28.12 ? 835 HOH A O     1 
HETATM 3180 O O     . HOH E 5 .   ? 21.784 0.163  13.276 1.00 42.42 ? 836 HOH A O     1 
HETATM 3181 O O     . HOH E 5 .   ? 35.117 25.520 24.238 1.00 42.88 ? 837 HOH A O     1 
HETATM 3182 O O     . HOH E 5 .   ? 9.785  26.645 2.195  1.00 48.38 ? 838 HOH A O     1 
HETATM 3183 O O     . HOH E 5 .   ? 15.505 46.823 19.476 1.00 37.63 ? 839 HOH A O     1 
HETATM 3184 O O     . HOH E 5 .   ? 13.093 9.892  -3.864 1.00 46.00 ? 840 HOH A O     1 
HETATM 3185 O O     . HOH E 5 .   ? 16.281 41.667 9.737  1.00 47.62 ? 841 HOH A O     1 
HETATM 3186 O O     . HOH E 5 .   ? 18.328 16.130 45.265 1.00 39.70 ? 842 HOH A O     1 
HETATM 3187 O O     . HOH E 5 .   ? 38.077 18.422 20.786 1.00 33.71 ? 843 HOH A O     1 
HETATM 3188 O O     . HOH E 5 .   ? 21.170 36.579 4.523  1.00 38.70 ? 844 HOH A O     1 
HETATM 3189 O O     . HOH E 5 .   ? 20.838 35.876 42.745 1.00 48.27 ? 845 HOH A O     1 
HETATM 3190 O O     . HOH E 5 .   ? 44.873 29.434 22.809 1.00 28.72 ? 846 HOH A O     1 
HETATM 3191 O O     . HOH E 5 .   ? 4.440  5.329  23.230 1.00 53.38 ? 847 HOH A O     1 
HETATM 3192 O O     . HOH E 5 .   ? 10.499 18.509 44.880 1.00 32.03 ? 848 HOH A O     1 
HETATM 3193 O O     . HOH E 5 .   ? 23.829 -1.127 38.499 1.00 38.37 ? 849 HOH A O     1 
HETATM 3194 O O     . HOH E 5 .   ? -2.488 29.727 31.265 1.00 40.57 ? 850 HOH A O     1 
HETATM 3195 O O     . HOH E 5 .   ? 14.590 40.908 37.410 1.00 51.84 ? 851 HOH A O     1 
HETATM 3196 O O     . HOH E 5 .   ? 6.368  21.784 5.423  1.00 40.08 ? 852 HOH A O     1 
HETATM 3197 O O     . HOH E 5 .   ? 28.629 5.319  35.990 1.00 51.83 ? 853 HOH A O     1 
HETATM 3198 O O     . HOH E 5 .   ? 17.683 37.705 7.771  1.00 36.08 ? 854 HOH A O     1 
HETATM 3199 O O     . HOH E 5 .   ? 29.275 9.700  26.619 1.00 28.30 ? 855 HOH A O     1 
HETATM 3200 O O     . HOH E 5 .   ? 14.359 33.089 40.854 1.00 38.15 ? 856 HOH A O     1 
HETATM 3201 O O     . HOH E 5 .   ? 37.056 6.868  19.525 1.00 48.22 ? 857 HOH A O     1 
HETATM 3202 O O     . HOH E 5 .   ? 32.668 28.088 26.089 1.00 45.77 ? 858 HOH A O     1 
HETATM 3203 O O     . HOH E 5 .   ? 15.242 31.476 -2.543 1.00 28.69 ? 859 HOH A O     1 
HETATM 3204 O O     . HOH E 5 .   ? 29.922 41.353 25.095 1.00 41.07 ? 860 HOH A O     1 
HETATM 3205 O O     . HOH E 5 .   ? 10.944 8.372  7.178  1.00 41.72 ? 861 HOH A O     1 
HETATM 3206 O O     . HOH E 5 .   ? 2.285  11.717 43.859 1.00 46.38 ? 862 HOH A O     1 
HETATM 3207 O O     . HOH E 5 .   ? 28.309 32.853 2.028  1.00 44.70 ? 863 HOH A O     1 
HETATM 3208 O O     . HOH E 5 .   ? 33.902 44.002 18.873 1.00 36.64 ? 864 HOH A O     1 
HETATM 3209 O O     . HOH E 5 .   ? 4.463  30.738 24.451 1.00 35.40 ? 865 HOH A O     1 
HETATM 3210 O O     . HOH E 5 .   ? 22.762 31.588 -2.783 1.00 43.09 ? 866 HOH A O     1 
HETATM 3211 O O     . HOH E 5 .   ? 39.249 40.197 11.855 1.00 48.54 ? 867 HOH A O     1 
HETATM 3212 O O     . HOH E 5 .   ? 39.223 11.829 -0.264 1.00 48.08 ? 868 HOH A O     1 
HETATM 3213 O O     . HOH E 5 .   ? -2.563 14.064 19.841 1.00 44.69 ? 869 HOH A O     1 
HETATM 3214 O O     . HOH E 5 .   ? 41.680 18.048 9.876  1.00 33.33 ? 870 HOH A O     1 
HETATM 3215 O O     . HOH E 5 .   ? 14.746 6.589  42.956 1.00 45.81 ? 871 HOH A O     1 
HETATM 3216 O O     . HOH E 5 .   ? 19.517 33.735 -1.246 1.00 35.17 ? 872 HOH A O     1 
HETATM 3217 O O     . HOH E 5 .   ? 35.935 3.874  17.713 1.00 44.25 ? 873 HOH A O     1 
HETATM 3218 O O     . HOH E 5 .   ? 12.403 -2.464 27.517 1.00 39.24 ? 874 HOH A O     1 
HETATM 3219 O O     . HOH E 5 .   ? 10.160 36.356 3.968  1.00 34.49 ? 875 HOH A O     1 
HETATM 3220 O O     . HOH E 5 .   ? 0.406  25.641 11.996 1.00 47.41 ? 876 HOH A O     1 
HETATM 3221 O O     . HOH E 5 .   ? 30.428 36.137 26.945 1.00 33.06 ? 877 HOH A O     1 
HETATM 3222 O O     . HOH E 5 .   ? 25.689 42.254 9.959  1.00 36.95 ? 878 HOH A O     1 
HETATM 3223 O O     . HOH E 5 .   ? 35.253 7.509  17.785 1.00 33.85 ? 879 HOH A O     1 
HETATM 3224 O O     . HOH E 5 .   ? 28.003 29.765 30.180 1.00 43.38 ? 880 HOH A O     1 
HETATM 3225 O O     . HOH E 5 .   ? -3.221 26.762 35.346 1.00 34.43 ? 881 HOH A O     1 
HETATM 3226 O O     . HOH E 5 .   ? 11.839 31.263 44.861 1.00 51.60 ? 882 HOH A O     1 
HETATM 3227 O O     . HOH E 5 .   ? 37.566 40.847 9.423  1.00 51.96 ? 883 HOH A O     1 
HETATM 3228 O O     . HOH E 5 .   ? 27.932 9.880  33.898 1.00 41.08 ? 884 HOH A O     1 
HETATM 3229 O O     . HOH E 5 .   ? 19.543 32.587 44.455 1.00 41.84 ? 885 HOH A O     1 
HETATM 3230 O O     . HOH E 5 .   ? 33.207 41.573 20.121 1.00 29.63 ? 886 HOH A O     1 
HETATM 3231 O O     . HOH E 5 .   ? 32.363 24.441 24.939 1.00 39.84 ? 887 HOH A O     1 
HETATM 3232 O O     . HOH E 5 .   ? 41.978 9.212  14.391 1.00 38.64 ? 888 HOH A O     1 
HETATM 3233 O O     . HOH E 5 .   ? 41.520 35.044 4.439  1.00 49.10 ? 889 HOH A O     1 
HETATM 3234 O O     . HOH E 5 .   ? 31.331 33.434 28.457 1.00 41.63 ? 890 HOH A O     1 
HETATM 3235 O O     . HOH E 5 .   ? 1.988  14.717 43.496 1.00 43.02 ? 891 HOH A O     1 
HETATM 3236 O O     . HOH E 5 .   ? 16.279 34.586 41.870 1.00 39.00 ? 892 HOH A O     1 
HETATM 3237 O O     . HOH E 5 .   ? 2.869  36.036 20.764 1.00 43.64 ? 893 HOH A O     1 
HETATM 3238 O O     . HOH E 5 .   ? 4.124  5.757  30.041 1.00 42.10 ? 894 HOH A O     1 
HETATM 3239 O O     . HOH E 5 .   ? 8.111  39.305 6.760  1.00 42.35 ? 895 HOH A O     1 
HETATM 3240 O O     . HOH E 5 .   ? 23.369 43.311 10.899 1.00 34.01 ? 896 HOH A O     1 
HETATM 3241 O O     . HOH E 5 .   ? 18.978 7.366  -1.563 1.00 43.32 ? 897 HOH A O     1 
HETATM 3242 O O     . HOH E 5 .   ? 9.346  36.627 25.751 1.00 34.24 ? 898 HOH A O     1 
HETATM 3243 O O     . HOH E 5 .   ? 18.812 38.870 28.491 1.00 23.65 ? 899 HOH A O     1 
HETATM 3244 O O     . HOH E 5 .   ? 13.419 1.244  39.734 1.00 33.58 ? 900 HOH A O     1 
HETATM 3245 O O     . HOH E 5 .   ? 32.079 38.180 27.419 1.00 46.99 ? 901 HOH A O     1 
HETATM 3246 O O     . HOH E 5 .   ? 11.593 -4.296 23.321 1.00 47.22 ? 902 HOH A O     1 
HETATM 3247 O O     . HOH E 5 .   ? 41.901 11.997 17.714 1.00 48.31 ? 903 HOH A O     1 
HETATM 3248 O O     . HOH E 5 .   ? 15.909 35.393 0.364  1.00 40.72 ? 904 HOH A O     1 
HETATM 3249 O O     . HOH E 5 .   ? 6.577  35.832 6.322  1.00 36.04 ? 905 HOH A O     1 
HETATM 3250 O O     . HOH E 5 .   ? 45.731 33.521 24.377 1.00 30.89 ? 906 HOH A O     1 
HETATM 3251 O O     . HOH E 5 .   ? 31.079 25.830 1.082  1.00 32.96 ? 907 HOH A O     1 
HETATM 3252 O O     . HOH E 5 .   ? 6.381  1.948  30.367 1.00 48.89 ? 908 HOH A O     1 
HETATM 3253 O O     . HOH E 5 .   ? 17.133 39.978 6.415  1.00 40.62 ? 909 HOH A O     1 
HETATM 3254 O O     . HOH E 5 .   ? 33.406 44.084 11.976 1.00 32.71 ? 910 HOH A O     1 
HETATM 3255 O O     . HOH E 5 .   ? 3.563  33.308 24.410 1.00 46.19 ? 911 HOH A O     1 
HETATM 3256 O O     . HOH E 5 .   ? 4.866  32.729 30.195 1.00 42.90 ? 912 HOH A O     1 
HETATM 3257 O O     . HOH E 5 .   ? 3.320  8.200  26.551 1.00 46.94 ? 913 HOH A O     1 
HETATM 3258 O O     . HOH E 5 .   ? 16.882 1.378  37.168 1.00 30.96 ? 914 HOH A O     1 
HETATM 3259 O O     . HOH E 5 .   ? 35.499 34.703 0.644  1.00 45.22 ? 915 HOH A O     1 
HETATM 3260 O O     . HOH E 5 .   ? 1.649  22.345 9.938  1.00 33.41 ? 916 HOH A O     1 
HETATM 3261 O O     . HOH E 5 .   ? 5.348  18.052 43.576 1.00 53.19 ? 917 HOH A O     1 
HETATM 3262 O O     . HOH E 5 .   ? 34.259 41.234 8.526  1.00 44.87 ? 918 HOH A O     1 
HETATM 3263 O O     . HOH E 5 .   ? 37.376 39.792 19.513 1.00 46.38 ? 919 HOH A O     1 
HETATM 3264 O O     . HOH E 5 .   ? -0.894 22.130 11.093 1.00 49.50 ? 920 HOH A O     1 
HETATM 3265 O O     . HOH E 5 .   ? 17.467 33.842 44.042 1.00 43.53 ? 921 HOH A O     1 
HETATM 3266 O O     . HOH E 5 .   ? 30.589 18.931 -0.900 1.00 49.42 ? 922 HOH A O     1 
HETATM 3267 O O     . HOH E 5 .   ? 11.280 0.220  39.917 1.00 44.70 ? 923 HOH A O     1 
HETATM 3268 O O     . HOH E 5 .   ? 4.528  35.518 23.858 1.00 47.66 ? 924 HOH A O     1 
HETATM 3269 O O     . HOH E 5 .   ? 8.554  -3.888 28.442 1.00 41.35 ? 925 HOH A O     1 
HETATM 3270 O O     . HOH E 5 .   ? 20.764 44.064 8.601  1.00 37.14 ? 926 HOH A O     1 
HETATM 3271 O O     . HOH E 5 .   ? 21.415 42.727 6.279  1.00 44.75 ? 927 HOH A O     1 
HETATM 3272 O O     . HOH E 5 .   ? 5.059  35.419 29.997 1.00 44.61 ? 928 HOH A O     1 
HETATM 3273 O O     . HOH E 5 .   ? 26.568 44.681 10.298 1.00 32.86 ? 929 HOH A O     1 
HETATM 3274 O O     . HOH E 5 .   ? 7.205  -0.193 33.908 1.00 44.18 ? 930 HOH A O     1 
# 
