data_8QNY
# 
_entry.id   8QNY 
# 
_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   8QNY         pdb_00008qny 10.2210/pdb8qny/pdb 
WWPDB D_1292133637 ?            ?                   
# 
_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                        8QNY 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 8QNA unspecified 
PDB . 8QN1 unspecified 
PDB . 8QN9 unspecified 
PDB . 8QMX unspecified 
PDB . 8QN3 unspecified 
PDB . 8QNE unspecified 
PDB . 8QNK unspecified 
PDB . 8QNP unspecified 
PDB . 8QNM unspecified 
PDB . 8QNW unspecified 
PDB . 8QNX 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 2   ? ? ? ? 
2 non-polymer syn 'FLAVIN MONONUCLEOTIDE' 456.344   2   ? ? ? ? 
3 non-polymer syn 
;[[(2R,3S,4R,5R)-5-(5-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3-oxidanyl-4-phosphonooxy-oxolan-2-yl]methyl hydrogen phosphate
;
747.437   2   ? ? ? ? 
4 water       nat water 18.015    535 ? ? ? ? 
# 
_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,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN MONONUCLEOTIDE' FMN 
3 
;[[(2R,3S,4R,5R)-5-(5-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3-oxidanyl-4-phosphonooxy-oxolan-2-yl]methyl hydrogen phosphate
;
5J8 
4 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   SER n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  MET n 
1 11  ALA n 
1 12  SER n 
1 13  SER n 
1 14  ALA n 
1 15  GLN n 
1 16  ASP n 
1 17  GLY n 
1 18  ASN n 
1 19  ASN n 
1 20  PRO n 
1 21  LEU n 
1 22  PHE n 
1 23  SER n 
1 24  PRO n 
1 25  TYR n 
1 26  LYS n 
1 27  MET n 
1 28  GLY n 
1 29  LYS n 
1 30  PHE n 
1 31  ASN n 
1 32  LEU n 
1 33  SER n 
1 34  HIS n 
1 35  ARG n 
1 36  VAL n 
1 37  VAL n 
1 38  LEU n 
1 39  ALA n 
1 40  PRO n 
1 41  MET n 
1 42  THR n 
1 43  ARG n 
1 44  CYS n 
1 45  ARG n 
1 46  ALA n 
1 47  LEU n 
1 48  ASN n 
1 49  ASN n 
1 50  ILE n 
1 51  PRO n 
1 52  GLN n 
1 53  ALA n 
1 54  ALA n 
1 55  LEU n 
1 56  GLY n 
1 57  GLU n 
1 58  TYR n 
1 59  TYR n 
1 60  GLU n 
1 61  GLN n 
1 62  ARG n 
1 63  ALA n 
1 64  THR n 
1 65  ALA n 
1 66  GLY n 
1 67  GLY n 
1 68  PHE n 
1 69  LEU n 
1 70  ILE n 
1 71  THR n 
1 72  GLU n 
1 73  GLY n 
1 74  THR n 
1 75  MET n 
1 76  ILE n 
1 77  SER n 
1 78  PRO n 
1 79  THR n 
1 80  SER n 
1 81  ALA n 
1 82  GLY n 
1 83  PHE n 
1 84  PRO n 
1 85  HIS n 
1 86  VAL n 
1 87  PRO n 
1 88  GLY n 
1 89  ILE n 
1 90  PHE n 
1 91  THR n 
1 92  LYS n 
1 93  GLU n 
1 94  GLN n 
1 95  VAL n 
1 96  ARG n 
1 97  GLU n 
1 98  TRP n 
1 99  LYS n 
1 100 LYS n 
1 101 ILE n 
1 102 VAL n 
1 103 ASP n 
1 104 VAL n 
1 105 VAL n 
1 106 HIS n 
1 107 ALA n 
1 108 LYS n 
1 109 GLY n 
1 110 ALA n 
1 111 VAL n 
1 112 ILE n 
1 113 PHE n 
1 114 CYS n 
1 115 GLN n 
1 116 LEU n 
1 117 TRP n 
1 118 HIS n 
1 119 VAL n 
1 120 GLY n 
1 121 ARG n 
1 122 ALA n 
1 123 SER n 
1 124 HIS n 
1 125 GLU n 
1 126 VAL n 
1 127 TYR n 
1 128 GLN n 
1 129 PRO n 
1 130 ALA n 
1 131 GLY n 
1 132 ALA n 
1 133 ALA n 
1 134 PRO n 
1 135 ILE n 
1 136 SER n 
1 137 SER n 
1 138 THR n 
1 139 GLU n 
1 140 LYS n 
1 141 PRO n 
1 142 ILE n 
1 143 SER n 
1 144 ASN n 
1 145 ARG n 
1 146 TRP n 
1 147 ARG n 
1 148 ILE n 
1 149 LEU n 
1 150 MET n 
1 151 PRO n 
1 152 ASP n 
1 153 GLY n 
1 154 THR n 
1 155 HIS n 
1 156 GLY n 
1 157 ILE n 
1 158 TYR n 
1 159 PRO n 
1 160 LYS n 
1 161 PRO n 
1 162 ARG n 
1 163 ALA n 
1 164 ILE n 
1 165 GLY n 
1 166 THR n 
1 167 TYR n 
1 168 GLU n 
1 169 ILE n 
1 170 SER n 
1 171 GLN n 
1 172 VAL n 
1 173 VAL n 
1 174 GLU n 
1 175 ASP n 
1 176 TYR n 
1 177 ARG n 
1 178 ARG n 
1 179 SER n 
1 180 ALA n 
1 181 LEU n 
1 182 ASN n 
1 183 ALA n 
1 184 ILE n 
1 185 GLU n 
1 186 ALA n 
1 187 GLY n 
1 188 PHE n 
1 189 ASP n 
1 190 GLY n 
1 191 ILE n 
1 192 GLU n 
1 193 ILE n 
1 194 HIS n 
1 195 GLY n 
1 196 ALA n 
1 197 HIS n 
1 198 GLY n 
1 199 TYR n 
1 200 LEU n 
1 201 ILE n 
1 202 ASP n 
1 203 GLN n 
1 204 PHE n 
1 205 LEU n 
1 206 LYS n 
1 207 ASP n 
1 208 GLY n 
1 209 ILE n 
1 210 ASN n 
1 211 ASP n 
1 212 ARG n 
1 213 THR n 
1 214 ASP n 
1 215 GLU n 
1 216 TYR n 
1 217 GLY n 
1 218 GLY n 
1 219 SER n 
1 220 LEU n 
1 221 ALA n 
1 222 ASN n 
1 223 ARG n 
1 224 CYS n 
1 225 LYS n 
1 226 PHE n 
1 227 ILE n 
1 228 THR n 
1 229 GLN n 
1 230 VAL n 
1 231 VAL n 
1 232 GLN n 
1 233 ALA n 
1 234 VAL n 
1 235 VAL n 
1 236 SER n 
1 237 ALA n 
1 238 ILE n 
1 239 GLY n 
1 240 ALA n 
1 241 ASP n 
1 242 ARG n 
1 243 VAL n 
1 244 GLY n 
1 245 VAL n 
1 246 ARG n 
1 247 VAL n 
1 248 SER n 
1 249 PRO n 
1 250 ALA n 
1 251 ILE n 
1 252 ASP n 
1 253 HIS n 
1 254 LEU n 
1 255 ASP n 
1 256 ALA n 
1 257 MET n 
1 258 ASP n 
1 259 SER n 
1 260 ASN n 
1 261 PRO n 
1 262 LEU n 
1 263 SER n 
1 264 LEU n 
1 265 GLY n 
1 266 LEU n 
1 267 ALA n 
1 268 VAL n 
1 269 VAL n 
1 270 GLU n 
1 271 ARG n 
1 272 LEU n 
1 273 ASN n 
1 274 LYS n 
1 275 ILE n 
1 276 GLN n 
1 277 LEU n 
1 278 HIS n 
1 279 SER n 
1 280 GLY n 
1 281 SER n 
1 282 LYS n 
1 283 LEU n 
1 284 ALA n 
1 285 TYR n 
1 286 LEU n 
1 287 HIS n 
1 288 VAL n 
1 289 THR n 
1 290 GLN n 
1 291 PRO n 
1 292 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 
5J8 non-polymer         . 
;[[(2R,3S,4R,5R)-5-(5-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3-oxidanyl-4-phosphonooxy-oxolan-2-yl]methyl hydrogen phosphate
;
?                          'C21 H32 N7 O17 P3' 747.437 
ALA 'L-peptide linking' y ALANINE ?                          'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE ?                          'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                          'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                          'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE ?                          'C3 H7 N O2 S'      121.158 
FMN non-polymer         . 'FLAVIN MONONUCLEOTIDE' 'RIBOFLAVIN MONOPHOSPHATE' 'C17 H21 N4 O9 P'   456.344 
GLN 'L-peptide linking' y GLUTAMINE ?                          'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                          'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE ?                          'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE ?                          'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER ?                          'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                          'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE ?                          'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE ?                          'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE ?                          'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                          'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE ?                          'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE ?                          'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE ?                          'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                          'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE ?                          'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ?                          'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -8  ?   ?   ?   A . n 
A 1 2   ALA 2   -7  ?   ?   ?   A . n 
A 1 3   SER 3   -6  ?   ?   ?   A . n 
A 1 4   HIS 4   -5  ?   ?   ?   A . n 
A 1 5   HIS 5   -4  ?   ?   ?   A . n 
A 1 6   HIS 6   -3  ?   ?   ?   A . n 
A 1 7   HIS 7   -2  ?   ?   ?   A . n 
A 1 8   HIS 8   -1  ?   ?   ?   A . n 
A 1 9   HIS 9   0   ?   ?   ?   A . n 
A 1 10  MET 10  1   ?   ?   ?   A . n 
A 1 11  ALA 11  2   ?   ?   ?   A . n 
A 1 12  SER 12  3   ?   ?   ?   A . n 
A 1 13  SER 13  4   ?   ?   ?   A . n 
A 1 14  ALA 14  5   ?   ?   ?   A . n 
A 1 15  GLN 15  6   ?   ?   ?   A . n 
A 1 16  ASP 16  7   ?   ?   ?   A . n 
A 1 17  GLY 17  8   ?   ?   ?   A . n 
A 1 18  ASN 18  9   ?   ?   ?   A . n 
A 1 19  ASN 19  10  10  ASN ASN A . n 
A 1 20  PRO 20  11  11  PRO PRO A . n 
A 1 21  LEU 21  12  12  LEU LEU A . n 
A 1 22  PHE 22  13  13  PHE PHE A . n 
A 1 23  SER 23  14  14  SER SER A . n 
A 1 24  PRO 24  15  15  PRO PRO A . n 
A 1 25  TYR 25  16  16  TYR TYR A . n 
A 1 26  LYS 26  17  17  LYS LYS A . n 
A 1 27  MET 27  18  18  MET MET A . n 
A 1 28  GLY 28  19  19  GLY GLY A . n 
A 1 29  LYS 29  20  20  LYS LYS A . n 
A 1 30  PHE 30  21  21  PHE PHE A . n 
A 1 31  ASN 31  22  22  ASN ASN A . n 
A 1 32  LEU 32  23  23  LEU LEU A . n 
A 1 33  SER 33  24  24  SER SER A . n 
A 1 34  HIS 34  25  25  HIS HIS A . n 
A 1 35  ARG 35  26  26  ARG ARG A . n 
A 1 36  VAL 36  27  27  VAL VAL A . n 
A 1 37  VAL 37  28  28  VAL VAL A . n 
A 1 38  LEU 38  29  29  LEU LEU A . n 
A 1 39  ALA 39  30  30  ALA ALA A . n 
A 1 40  PRO 40  31  31  PRO PRO A . n 
A 1 41  MET 41  32  32  MET MET A . n 
A 1 42  THR 42  33  33  THR THR A . n 
A 1 43  ARG 43  34  34  ARG ARG A . n 
A 1 44  CYS 44  35  35  CYS CYS A . n 
A 1 45  ARG 45  36  36  ARG ARG A . n 
A 1 46  ALA 46  37  37  ALA ALA A . n 
A 1 47  LEU 47  38  38  LEU LEU A . n 
A 1 48  ASN 48  39  39  ASN ASN A . n 
A 1 49  ASN 49  40  40  ASN ASN A . n 
A 1 50  ILE 50  41  41  ILE ILE A . n 
A 1 51  PRO 51  42  42  PRO PRO A . n 
A 1 52  GLN 52  43  43  GLN GLN A . n 
A 1 53  ALA 53  44  44  ALA ALA A . n 
A 1 54  ALA 54  45  45  ALA ALA A . n 
A 1 55  LEU 55  46  46  LEU LEU A . n 
A 1 56  GLY 56  47  47  GLY GLY A . n 
A 1 57  GLU 57  48  48  GLU GLU A . n 
A 1 58  TYR 58  49  49  TYR TYR A . n 
A 1 59  TYR 59  50  50  TYR TYR A . n 
A 1 60  GLU 60  51  51  GLU GLU A . n 
A 1 61  GLN 61  52  52  GLN GLN A . n 
A 1 62  ARG 62  53  53  ARG ARG A . n 
A 1 63  ALA 63  54  54  ALA ALA A . n 
A 1 64  THR 64  55  55  THR THR A . n 
A 1 65  ALA 65  56  56  ALA ALA A . n 
A 1 66  GLY 66  57  57  GLY GLY A . n 
A 1 67  GLY 67  58  58  GLY GLY A . n 
A 1 68  PHE 68  59  59  PHE PHE A . n 
A 1 69  LEU 69  60  60  LEU LEU A . n 
A 1 70  ILE 70  61  61  ILE ILE A . n 
A 1 71  THR 71  62  62  THR THR A . n 
A 1 72  GLU 72  63  63  GLU GLU A . n 
A 1 73  GLY 73  64  64  GLY GLY A . n 
A 1 74  THR 74  65  65  THR THR A . n 
A 1 75  MET 75  66  66  MET MET A . n 
A 1 76  ILE 76  67  67  ILE ILE A . n 
A 1 77  SER 77  68  68  SER SER A . n 
A 1 78  PRO 78  69  69  PRO PRO A . n 
A 1 79  THR 79  70  70  THR THR A . n 
A 1 80  SER 80  71  71  SER SER A . n 
A 1 81  ALA 81  72  72  ALA ALA A . n 
A 1 82  GLY 82  73  73  GLY GLY A . n 
A 1 83  PHE 83  74  74  PHE PHE A . n 
A 1 84  PRO 84  75  75  PRO PRO A . n 
A 1 85  HIS 85  76  76  HIS HIS A . n 
A 1 86  VAL 86  77  77  VAL VAL A . n 
A 1 87  PRO 87  78  78  PRO PRO A . n 
A 1 88  GLY 88  79  79  GLY GLY A . n 
A 1 89  ILE 89  80  80  ILE ILE A . n 
A 1 90  PHE 90  81  81  PHE PHE A . n 
A 1 91  THR 91  82  82  THR THR A . n 
A 1 92  LYS 92  83  83  LYS LYS A . n 
A 1 93  GLU 93  84  84  GLU GLU A . n 
A 1 94  GLN 94  85  85  GLN GLN A . n 
A 1 95  VAL 95  86  86  VAL VAL A . n 
A 1 96  ARG 96  87  87  ARG ARG A . n 
A 1 97  GLU 97  88  88  GLU GLU A . n 
A 1 98  TRP 98  89  89  TRP TRP A . n 
A 1 99  LYS 99  90  90  LYS LYS A . n 
A 1 100 LYS 100 91  91  LYS LYS A . n 
A 1 101 ILE 101 92  92  ILE ILE A . n 
A 1 102 VAL 102 93  93  VAL VAL A . n 
A 1 103 ASP 103 94  94  ASP ASP A . n 
A 1 104 VAL 104 95  95  VAL VAL A . n 
A 1 105 VAL 105 96  96  VAL VAL A . n 
A 1 106 HIS 106 97  97  HIS HIS A . n 
A 1 107 ALA 107 98  98  ALA ALA A . n 
A 1 108 LYS 108 99  99  LYS LYS A . n 
A 1 109 GLY 109 100 100 GLY GLY A . n 
A 1 110 ALA 110 101 101 ALA ALA A . n 
A 1 111 VAL 111 102 102 VAL VAL A . n 
A 1 112 ILE 112 103 103 ILE ILE A . n 
A 1 113 PHE 113 104 104 PHE PHE A . n 
A 1 114 CYS 114 105 105 CYS CYS A . n 
A 1 115 GLN 115 106 106 GLN GLN A . n 
A 1 116 LEU 116 107 107 LEU LEU A . n 
A 1 117 TRP 117 108 108 TRP TRP A . n 
A 1 118 HIS 118 109 109 HIS HIS A . n 
A 1 119 VAL 119 110 110 VAL VAL A . n 
A 1 120 GLY 120 111 111 GLY GLY A . n 
A 1 121 ARG 121 112 112 ARG ARG A . n 
A 1 122 ALA 122 113 113 ALA ALA A . n 
A 1 123 SER 123 114 114 SER SER A . n 
A 1 124 HIS 124 115 115 HIS HIS A . n 
A 1 125 GLU 125 116 116 GLU GLU A . n 
A 1 126 VAL 126 117 117 VAL VAL A . n 
A 1 127 TYR 127 118 118 TYR TYR A . n 
A 1 128 GLN 128 119 119 GLN GLN A . n 
A 1 129 PRO 129 120 120 PRO PRO A . n 
A 1 130 ALA 130 121 121 ALA ALA A . n 
A 1 131 GLY 131 122 122 GLY GLY A . n 
A 1 132 ALA 132 123 123 ALA ALA A . n 
A 1 133 ALA 133 124 124 ALA ALA A . n 
A 1 134 PRO 134 125 125 PRO PRO A . n 
A 1 135 ILE 135 126 126 ILE ILE A . n 
A 1 136 SER 136 127 127 SER SER A . n 
A 1 137 SER 137 128 128 SER SER A . n 
A 1 138 THR 138 129 129 THR THR A . n 
A 1 139 GLU 139 130 130 GLU GLU A . n 
A 1 140 LYS 140 131 131 LYS LYS A . n 
A 1 141 PRO 141 132 132 PRO PRO A . n 
A 1 142 ILE 142 133 133 ILE ILE A . n 
A 1 143 SER 143 134 134 SER SER A . n 
A 1 144 ASN 144 135 135 ASN ASN A . n 
A 1 145 ARG 145 136 136 ARG ARG A . n 
A 1 146 TRP 146 137 137 TRP TRP A . n 
A 1 147 ARG 147 138 138 ARG ARG A . n 
A 1 148 ILE 148 139 139 ILE ILE A . n 
A 1 149 LEU 149 140 140 LEU LEU A . n 
A 1 150 MET 150 141 141 MET MET A . n 
A 1 151 PRO 151 142 142 PRO PRO A . n 
A 1 152 ASP 152 143 143 ASP ASP A . n 
A 1 153 GLY 153 144 144 GLY GLY A . n 
A 1 154 THR 154 145 145 THR THR A . n 
A 1 155 HIS 155 146 146 HIS HIS A . n 
A 1 156 GLY 156 147 147 GLY GLY A . n 
A 1 157 ILE 157 148 148 ILE ILE A . n 
A 1 158 TYR 158 149 149 TYR TYR A . n 
A 1 159 PRO 159 150 150 PRO PRO A . n 
A 1 160 LYS 160 151 151 LYS LYS A . n 
A 1 161 PRO 161 152 152 PRO PRO A . n 
A 1 162 ARG 162 153 153 ARG ARG A . n 
A 1 163 ALA 163 154 154 ALA ALA A . n 
A 1 164 ILE 164 155 155 ILE ILE A . n 
A 1 165 GLY 165 156 156 GLY GLY A . n 
A 1 166 THR 166 157 157 THR THR A . n 
A 1 167 TYR 167 158 158 TYR TYR A . n 
A 1 168 GLU 168 159 159 GLU GLU A . n 
A 1 169 ILE 169 160 160 ILE ILE A . n 
A 1 170 SER 170 161 161 SER SER A . n 
A 1 171 GLN 171 162 162 GLN GLN A . n 
A 1 172 VAL 172 163 163 VAL VAL A . n 
A 1 173 VAL 173 164 164 VAL VAL A . n 
A 1 174 GLU 174 165 165 GLU GLU A . n 
A 1 175 ASP 175 166 166 ASP ASP A . n 
A 1 176 TYR 176 167 167 TYR TYR A . n 
A 1 177 ARG 177 168 168 ARG ARG A . n 
A 1 178 ARG 178 169 169 ARG ARG A . n 
A 1 179 SER 179 170 170 SER SER A . n 
A 1 180 ALA 180 171 171 ALA ALA A . n 
A 1 181 LEU 181 172 172 LEU LEU A . n 
A 1 182 ASN 182 173 173 ASN ASN A . n 
A 1 183 ALA 183 174 174 ALA ALA A . n 
A 1 184 ILE 184 175 175 ILE ILE A . n 
A 1 185 GLU 185 176 176 GLU GLU A . n 
A 1 186 ALA 186 177 177 ALA ALA A . n 
A 1 187 GLY 187 178 178 GLY GLY A . n 
A 1 188 PHE 188 179 179 PHE PHE A . n 
A 1 189 ASP 189 180 180 ASP ASP A . n 
A 1 190 GLY 190 181 181 GLY GLY A . n 
A 1 191 ILE 191 182 182 ILE ILE A . n 
A 1 192 GLU 192 183 183 GLU GLU A . n 
A 1 193 ILE 193 184 184 ILE ILE A . n 
A 1 194 HIS 194 185 185 HIS HIS A . n 
A 1 195 GLY 195 186 186 GLY GLY A . n 
A 1 196 ALA 196 187 187 ALA ALA A . n 
A 1 197 HIS 197 188 188 HIS HIS A . n 
A 1 198 GLY 198 189 189 GLY GLY A . n 
A 1 199 TYR 199 190 190 TYR TYR A . n 
A 1 200 LEU 200 191 191 LEU LEU A . n 
A 1 201 ILE 201 192 192 ILE ILE A . n 
A 1 202 ASP 202 193 193 ASP ASP A . n 
A 1 203 GLN 203 194 194 GLN GLN A . n 
A 1 204 PHE 204 195 195 PHE PHE A . n 
A 1 205 LEU 205 196 196 LEU LEU A . n 
A 1 206 LYS 206 197 197 LYS LYS A . n 
A 1 207 ASP 207 198 198 ASP ASP A . n 
A 1 208 GLY 208 199 199 GLY GLY A . n 
A 1 209 ILE 209 200 200 ILE ILE A . n 
A 1 210 ASN 210 201 201 ASN ASN A . n 
A 1 211 ASP 211 202 202 ASP ASP A . n 
A 1 212 ARG 212 203 203 ARG ARG A . n 
A 1 213 THR 213 204 204 THR THR A . n 
A 1 214 ASP 214 205 205 ASP ASP A . n 
A 1 215 GLU 215 206 206 GLU GLU A . n 
A 1 216 TYR 216 207 207 TYR TYR A . n 
A 1 217 GLY 217 208 208 GLY GLY A . n 
A 1 218 GLY 218 209 209 GLY GLY A . n 
A 1 219 SER 219 210 210 SER SER A . n 
A 1 220 LEU 220 211 211 LEU LEU A . n 
A 1 221 ALA 221 212 212 ALA ALA A . n 
A 1 222 ASN 222 213 213 ASN ASN A . n 
A 1 223 ARG 223 214 214 ARG ARG A . n 
A 1 224 CYS 224 215 215 CYS CYS A . n 
A 1 225 LYS 225 216 216 LYS LYS A . n 
A 1 226 PHE 226 217 217 PHE PHE A . n 
A 1 227 ILE 227 218 218 ILE ILE A . n 
A 1 228 THR 228 219 219 THR THR A . n 
A 1 229 GLN 229 220 220 GLN GLN A . n 
A 1 230 VAL 230 221 221 VAL VAL A . n 
A 1 231 VAL 231 222 222 VAL VAL A . n 
A 1 232 GLN 232 223 223 GLN GLN A . n 
A 1 233 ALA 233 224 224 ALA ALA A . n 
A 1 234 VAL 234 225 225 VAL VAL A . n 
A 1 235 VAL 235 226 226 VAL VAL A . n 
A 1 236 SER 236 227 227 SER SER A . n 
A 1 237 ALA 237 228 228 ALA ALA A . n 
A 1 238 ILE 238 229 229 ILE ILE A . n 
A 1 239 GLY 239 230 230 GLY GLY A . n 
A 1 240 ALA 240 231 231 ALA ALA A . n 
A 1 241 ASP 241 232 232 ASP ASP A . n 
A 1 242 ARG 242 233 233 ARG ARG A . n 
A 1 243 VAL 243 234 234 VAL VAL A . n 
A 1 244 GLY 244 235 235 GLY GLY A . n 
A 1 245 VAL 245 236 236 VAL VAL A . n 
A 1 246 ARG 246 237 237 ARG ARG A . n 
A 1 247 VAL 247 238 238 VAL VAL A . n 
A 1 248 SER 248 239 239 SER SER A . n 
A 1 249 PRO 249 240 240 PRO PRO A . n 
A 1 250 ALA 250 241 241 ALA ALA A . n 
A 1 251 ILE 251 242 242 ILE ILE A . n 
A 1 252 ASP 252 243 243 ASP ASP A . n 
A 1 253 HIS 253 244 244 HIS HIS A . n 
A 1 254 LEU 254 245 245 LEU LEU A . n 
A 1 255 ASP 255 246 246 ASP ASP A . n 
A 1 256 ALA 256 247 247 ALA ALA A . n 
A 1 257 MET 257 248 248 MET MET A . n 
A 1 258 ASP 258 249 249 ASP ASP A . n 
A 1 259 SER 259 250 250 SER SER A . n 
A 1 260 ASN 260 251 251 ASN ASN A . n 
A 1 261 PRO 261 252 252 PRO PRO A . n 
A 1 262 LEU 262 253 253 LEU LEU A . n 
A 1 263 SER 263 254 254 SER SER A . n 
A 1 264 LEU 264 255 255 LEU LEU A . n 
A 1 265 GLY 265 256 256 GLY GLY A . n 
A 1 266 LEU 266 257 257 LEU LEU A . n 
A 1 267 ALA 267 258 258 ALA ALA A . n 
A 1 268 VAL 268 259 259 VAL VAL A . n 
A 1 269 VAL 269 260 260 VAL VAL A . n 
A 1 270 GLU 270 261 261 GLU GLU A . n 
A 1 271 ARG 271 262 262 ARG ARG A . n 
A 1 272 LEU 272 263 263 LEU LEU A . n 
A 1 273 ASN 273 264 264 ASN ASN A . n 
A 1 274 LYS 274 265 265 LYS LYS A . n 
A 1 275 ILE 275 266 266 ILE ILE A . n 
A 1 276 GLN 276 267 267 GLN GLN A . n 
A 1 277 LEU 277 268 268 LEU LEU A . n 
A 1 278 HIS 278 269 269 HIS HIS A . n 
A 1 279 SER 279 270 270 SER SER A . n 
A 1 280 GLY 280 271 271 GLY GLY A . n 
A 1 281 SER 281 272 272 SER SER A . n 
A 1 282 LYS 282 273 273 LYS LYS A . n 
A 1 283 LEU 283 274 274 LEU LEU A . n 
A 1 284 ALA 284 275 275 ALA ALA A . n 
A 1 285 TYR 285 276 276 TYR TYR A . n 
A 1 286 LEU 286 277 277 LEU LEU A . n 
A 1 287 HIS 287 278 278 HIS HIS A . n 
A 1 288 VAL 288 279 279 VAL VAL A . n 
A 1 289 THR 289 280 280 THR THR A . n 
A 1 290 GLN 290 281 281 GLN GLN A . n 
A 1 291 PRO 291 282 282 PRO PRO A . n 
A 1 292 GLY 292 283 283 GLY GLY A . n 
A 1 293 ASP 293 284 284 ASP ASP A . n 
A 1 294 GLY 294 285 285 GLY GLY A . n 
A 1 295 ARG 295 286 ?   ?   ?   A . n 
A 1 296 GLY 296 287 ?   ?   ?   A . n 
A 1 297 SER 297 288 288 SER SER A . n 
A 1 298 GLU 298 289 289 GLU GLU A . n 
A 1 299 GLU 299 290 290 GLU GLU A . n 
A 1 300 GLU 300 291 291 GLU GLU A . n 
A 1 301 GLU 301 292 292 GLU GLU A . n 
A 1 302 ALA 302 293 293 ALA ALA A . n 
A 1 303 ARG 303 294 294 ARG ARG A . n 
A 1 304 LEU 304 295 295 LEU LEU A . n 
A 1 305 MET 305 296 296 MET MET A . n 
A 1 306 ARG 306 297 297 ARG ARG A . n 
A 1 307 THR 307 298 298 THR THR A . n 
A 1 308 LEU 308 299 299 LEU LEU A . n 
A 1 309 ARG 309 300 300 ARG ARG A . n 
A 1 310 ASN 310 301 301 ASN ASN A . n 
A 1 311 ALA 311 302 302 ALA ALA A . n 
A 1 312 TYR 312 303 303 TYR TYR A . n 
A 1 313 GLN 313 304 304 GLN GLN A . n 
A 1 314 GLY 314 305 305 GLY GLY A . n 
A 1 315 THR 315 306 306 THR THR A . n 
A 1 316 PHE 316 307 307 PHE PHE A . n 
A 1 317 ILE 317 308 308 ILE ILE A . n 
A 1 318 CYS 318 309 309 CYS CYS A . n 
A 1 319 SER 319 310 310 SER SER A . n 
A 1 320 GLY 320 311 311 GLY GLY A . n 
A 1 321 GLY 321 312 312 GLY GLY A . n 
A 1 322 TYR 322 313 313 TYR TYR A . n 
A 1 323 THR 323 314 314 THR THR A . n 
A 1 324 ARG 324 315 315 ARG ARG A . n 
A 1 325 GLU 325 316 316 GLU GLU A . n 
A 1 326 LEU 326 317 317 LEU LEU A . n 
A 1 327 GLY 327 318 318 GLY GLY A . n 
A 1 328 ILE 328 319 319 ILE ILE A . n 
A 1 329 GLU 329 320 320 GLU GLU A . n 
A 1 330 ALA 330 321 321 ALA ALA A . n 
A 1 331 VAL 331 322 322 VAL VAL A . n 
A 1 332 ALA 332 323 323 ALA ALA A . n 
A 1 333 GLN 333 324 324 GLN GLN A . n 
A 1 334 GLY 334 325 325 GLY GLY A . n 
A 1 335 ASP 335 326 326 ASP ASP A . n 
A 1 336 ALA 336 327 327 ALA ALA A . n 
A 1 337 ASP 337 328 328 ASP ASP A . n 
A 1 338 LEU 338 329 329 LEU LEU A . n 
A 1 339 VAL 339 330 330 VAL VAL A . n 
A 1 340 SER 340 331 331 SER SER A . n 
A 1 341 TYR 341 332 332 TYR TYR A . n 
A 1 342 GLY 342 333 333 GLY GLY A . n 
A 1 343 ARG 343 334 334 ARG ARG A . n 
A 1 344 LEU 344 335 335 LEU LEU A . n 
A 1 345 PHE 345 336 336 PHE PHE A . n 
A 1 346 ILE 346 337 337 ILE ILE A . n 
A 1 347 SER 347 338 338 SER SER A . n 
A 1 348 ASN 348 339 339 ASN ASN A . n 
A 1 349 PRO 349 340 340 PRO PRO A . n 
A 1 350 ASP 350 341 341 ASP ASP A . n 
A 1 351 LEU 351 342 342 LEU LEU A . n 
A 1 352 VAL 352 343 343 VAL VAL A . n 
A 1 353 MET 353 344 344 MET MET A . n 
A 1 354 ARG 354 345 345 ARG ARG A . n 
A 1 355 ILE 355 346 346 ILE ILE A . n 
A 1 356 LYS 356 347 347 LYS LYS A . n 
A 1 357 LEU 357 348 348 LEU LEU A . n 
A 1 358 ASN 358 349 349 ASN ASN A . n 
A 1 359 ALA 359 350 350 ALA ALA A . n 
A 1 360 PRO 360 351 351 PRO PRO A . n 
A 1 361 LEU 361 352 352 LEU LEU A . n 
A 1 362 ASN 362 353 353 ASN ASN A . n 
A 1 363 LYS 363 354 354 LYS LYS A . n 
A 1 364 TYR 364 355 355 TYR TYR A . n 
A 1 365 ASN 365 356 356 ASN ASN A . n 
A 1 366 ARG 366 357 357 ARG ARG A . n 
A 1 367 LYS 367 358 358 LYS LYS A . n 
A 1 368 THR 368 359 359 THR THR A . n 
A 1 369 PHE 369 360 360 PHE PHE A . n 
A 1 370 TYR 370 361 361 TYR TYR A . n 
A 1 371 THR 371 362 362 THR THR A . n 
A 1 372 GLN 372 363 363 GLN GLN A . n 
A 1 373 ASP 373 364 364 ASP ASP A . n 
A 1 374 PRO 374 365 365 PRO PRO A . n 
A 1 375 VAL 375 366 366 VAL VAL A . n 
A 1 376 VAL 376 367 367 VAL VAL A . n 
A 1 377 GLY 377 368 368 GLY GLY A . n 
A 1 378 TYR 378 369 369 TYR TYR A . n 
A 1 379 THR 379 370 370 THR THR A . n 
A 1 380 ASP 380 371 371 ASP ASP A . n 
A 1 381 TYR 381 372 372 TYR TYR A . n 
A 1 382 PRO 382 373 373 PRO PRO A . n 
A 1 383 PHE 383 374 374 PHE PHE A . n 
A 1 384 LEU 384 375 375 LEU LEU A . n 
A 1 385 GLN 385 376 ?   ?   ?   A . n 
A 1 386 GLY 386 377 ?   ?   ?   A . n 
A 1 387 ASN 387 378 ?   ?   ?   A . n 
A 1 388 GLY 388 379 ?   ?   ?   A . n 
A 1 389 SER 389 380 ?   ?   ?   A . n 
A 1 390 ASN 390 381 ?   ?   ?   A . n 
A 1 391 GLY 391 382 ?   ?   ?   A . n 
A 1 392 PRO 392 383 ?   ?   ?   A . n 
A 1 393 LEU 393 384 ?   ?   ?   A . n 
A 1 394 SER 394 385 ?   ?   ?   A . n 
A 1 395 ARG 395 386 ?   ?   ?   A . n 
A 1 396 LEU 396 387 ?   ?   ?   A . n 
B 1 1   MET 1   -8  ?   ?   ?   B . n 
B 1 2   ALA 2   -7  ?   ?   ?   B . n 
B 1 3   SER 3   -6  ?   ?   ?   B . n 
B 1 4   HIS 4   -5  ?   ?   ?   B . n 
B 1 5   HIS 5   -4  ?   ?   ?   B . n 
B 1 6   HIS 6   -3  ?   ?   ?   B . n 
B 1 7   HIS 7   -2  ?   ?   ?   B . n 
B 1 8   HIS 8   -1  ?   ?   ?   B . n 
B 1 9   HIS 9   0   ?   ?   ?   B . n 
B 1 10  MET 10  1   ?   ?   ?   B . n 
B 1 11  ALA 11  2   ?   ?   ?   B . n 
B 1 12  SER 12  3   ?   ?   ?   B . n 
B 1 13  SER 13  4   ?   ?   ?   B . n 
B 1 14  ALA 14  5   ?   ?   ?   B . n 
B 1 15  GLN 15  6   ?   ?   ?   B . n 
B 1 16  ASP 16  7   ?   ?   ?   B . n 
B 1 17  GLY 17  8   ?   ?   ?   B . n 
B 1 18  ASN 18  9   ?   ?   ?   B . n 
B 1 19  ASN 19  10  10  ASN ASN B . n 
B 1 20  PRO 20  11  11  PRO PRO B . n 
B 1 21  LEU 21  12  12  LEU LEU B . n 
B 1 22  PHE 22  13  13  PHE PHE B . n 
B 1 23  SER 23  14  14  SER SER B . n 
B 1 24  PRO 24  15  15  PRO PRO B . n 
B 1 25  TYR 25  16  16  TYR TYR B . n 
B 1 26  LYS 26  17  17  LYS LYS B . n 
B 1 27  MET 27  18  18  MET MET B . n 
B 1 28  GLY 28  19  19  GLY GLY B . n 
B 1 29  LYS 29  20  20  LYS LYS B . n 
B 1 30  PHE 30  21  21  PHE PHE B . n 
B 1 31  ASN 31  22  22  ASN ASN B . n 
B 1 32  LEU 32  23  23  LEU LEU B . n 
B 1 33  SER 33  24  24  SER SER B . n 
B 1 34  HIS 34  25  25  HIS HIS B . n 
B 1 35  ARG 35  26  26  ARG ARG B . n 
B 1 36  VAL 36  27  27  VAL VAL B . n 
B 1 37  VAL 37  28  28  VAL VAL B . n 
B 1 38  LEU 38  29  29  LEU LEU B . n 
B 1 39  ALA 39  30  30  ALA ALA B . n 
B 1 40  PRO 40  31  31  PRO PRO B . n 
B 1 41  MET 41  32  32  MET MET B . n 
B 1 42  THR 42  33  33  THR THR B . n 
B 1 43  ARG 43  34  34  ARG ARG B . n 
B 1 44  CYS 44  35  35  CYS CYS B . n 
B 1 45  ARG 45  36  36  ARG ARG B . n 
B 1 46  ALA 46  37  37  ALA ALA B . n 
B 1 47  LEU 47  38  38  LEU LEU B . n 
B 1 48  ASN 48  39  39  ASN ASN B . n 
B 1 49  ASN 49  40  40  ASN ASN B . n 
B 1 50  ILE 50  41  41  ILE ILE B . n 
B 1 51  PRO 51  42  42  PRO PRO B . n 
B 1 52  GLN 52  43  43  GLN GLN B . n 
B 1 53  ALA 53  44  44  ALA ALA B . n 
B 1 54  ALA 54  45  45  ALA ALA B . n 
B 1 55  LEU 55  46  46  LEU LEU B . n 
B 1 56  GLY 56  47  47  GLY GLY B . n 
B 1 57  GLU 57  48  48  GLU GLU B . n 
B 1 58  TYR 58  49  49  TYR TYR B . n 
B 1 59  TYR 59  50  50  TYR TYR B . n 
B 1 60  GLU 60  51  51  GLU GLU B . n 
B 1 61  GLN 61  52  52  GLN GLN B . n 
B 1 62  ARG 62  53  53  ARG ARG B . n 
B 1 63  ALA 63  54  54  ALA ALA B . n 
B 1 64  THR 64  55  55  THR THR B . n 
B 1 65  ALA 65  56  56  ALA ALA B . n 
B 1 66  GLY 66  57  57  GLY GLY B . n 
B 1 67  GLY 67  58  58  GLY GLY B . n 
B 1 68  PHE 68  59  59  PHE PHE B . n 
B 1 69  LEU 69  60  60  LEU LEU B . n 
B 1 70  ILE 70  61  61  ILE ILE B . n 
B 1 71  THR 71  62  62  THR THR B . n 
B 1 72  GLU 72  63  63  GLU GLU B . n 
B 1 73  GLY 73  64  64  GLY GLY B . n 
B 1 74  THR 74  65  65  THR THR B . n 
B 1 75  MET 75  66  66  MET MET B . n 
B 1 76  ILE 76  67  67  ILE ILE B . n 
B 1 77  SER 77  68  68  SER SER B . n 
B 1 78  PRO 78  69  69  PRO PRO B . n 
B 1 79  THR 79  70  70  THR THR B . n 
B 1 80  SER 80  71  71  SER SER B . n 
B 1 81  ALA 81  72  72  ALA ALA B . n 
B 1 82  GLY 82  73  73  GLY GLY B . n 
B 1 83  PHE 83  74  74  PHE PHE B . n 
B 1 84  PRO 84  75  75  PRO PRO B . n 
B 1 85  HIS 85  76  76  HIS HIS B . n 
B 1 86  VAL 86  77  77  VAL VAL B . n 
B 1 87  PRO 87  78  78  PRO PRO B . n 
B 1 88  GLY 88  79  79  GLY GLY B . n 
B 1 89  ILE 89  80  80  ILE ILE B . n 
B 1 90  PHE 90  81  81  PHE PHE B . n 
B 1 91  THR 91  82  82  THR THR B . n 
B 1 92  LYS 92  83  83  LYS LYS B . n 
B 1 93  GLU 93  84  84  GLU GLU B . n 
B 1 94  GLN 94  85  85  GLN GLN B . n 
B 1 95  VAL 95  86  86  VAL VAL B . n 
B 1 96  ARG 96  87  87  ARG ARG B . n 
B 1 97  GLU 97  88  88  GLU GLU B . n 
B 1 98  TRP 98  89  89  TRP TRP B . n 
B 1 99  LYS 99  90  90  LYS LYS B . n 
B 1 100 LYS 100 91  91  LYS LYS B . n 
B 1 101 ILE 101 92  92  ILE ILE B . n 
B 1 102 VAL 102 93  93  VAL VAL B . n 
B 1 103 ASP 103 94  94  ASP ASP B . n 
B 1 104 VAL 104 95  95  VAL VAL B . n 
B 1 105 VAL 105 96  96  VAL VAL B . n 
B 1 106 HIS 106 97  97  HIS HIS B . n 
B 1 107 ALA 107 98  98  ALA ALA B . n 
B 1 108 LYS 108 99  99  LYS LYS B . n 
B 1 109 GLY 109 100 100 GLY GLY B . n 
B 1 110 ALA 110 101 101 ALA ALA B . n 
B 1 111 VAL 111 102 102 VAL VAL B . n 
B 1 112 ILE 112 103 103 ILE ILE B . n 
B 1 113 PHE 113 104 104 PHE PHE B . n 
B 1 114 CYS 114 105 105 CYS CYS B . n 
B 1 115 GLN 115 106 106 GLN GLN B . n 
B 1 116 LEU 116 107 107 LEU LEU B . n 
B 1 117 TRP 117 108 108 TRP TRP B . n 
B 1 118 HIS 118 109 109 HIS HIS B . n 
B 1 119 VAL 119 110 110 VAL VAL B . n 
B 1 120 GLY 120 111 111 GLY GLY B . n 
B 1 121 ARG 121 112 112 ARG ARG B . n 
B 1 122 ALA 122 113 113 ALA ALA B . n 
B 1 123 SER 123 114 114 SER SER B . n 
B 1 124 HIS 124 115 115 HIS HIS B . n 
B 1 125 GLU 125 116 116 GLU GLU B . n 
B 1 126 VAL 126 117 117 VAL VAL B . n 
B 1 127 TYR 127 118 118 TYR TYR B . n 
B 1 128 GLN 128 119 119 GLN GLN B . n 
B 1 129 PRO 129 120 120 PRO PRO B . n 
B 1 130 ALA 130 121 121 ALA ALA B . n 
B 1 131 GLY 131 122 122 GLY GLY B . n 
B 1 132 ALA 132 123 123 ALA ALA B . n 
B 1 133 ALA 133 124 124 ALA ALA B . n 
B 1 134 PRO 134 125 125 PRO PRO B . n 
B 1 135 ILE 135 126 126 ILE ILE B . n 
B 1 136 SER 136 127 127 SER SER B . n 
B 1 137 SER 137 128 128 SER SER B . n 
B 1 138 THR 138 129 129 THR THR B . n 
B 1 139 GLU 139 130 130 GLU GLU B . n 
B 1 140 LYS 140 131 131 LYS LYS B . n 
B 1 141 PRO 141 132 132 PRO PRO B . n 
B 1 142 ILE 142 133 133 ILE ILE B . n 
B 1 143 SER 143 134 134 SER SER B . n 
B 1 144 ASN 144 135 135 ASN ASN B . n 
B 1 145 ARG 145 136 136 ARG ARG B . n 
B 1 146 TRP 146 137 137 TRP TRP B . n 
B 1 147 ARG 147 138 138 ARG ARG B . n 
B 1 148 ILE 148 139 139 ILE ILE B . n 
B 1 149 LEU 149 140 140 LEU LEU B . n 
B 1 150 MET 150 141 141 MET MET B . n 
B 1 151 PRO 151 142 142 PRO PRO B . n 
B 1 152 ASP 152 143 143 ASP ASP B . n 
B 1 153 GLY 153 144 144 GLY GLY B . n 
B 1 154 THR 154 145 145 THR THR B . n 
B 1 155 HIS 155 146 146 HIS HIS B . n 
B 1 156 GLY 156 147 147 GLY GLY B . n 
B 1 157 ILE 157 148 148 ILE ILE B . n 
B 1 158 TYR 158 149 149 TYR TYR B . n 
B 1 159 PRO 159 150 150 PRO PRO B . n 
B 1 160 LYS 160 151 151 LYS LYS B . n 
B 1 161 PRO 161 152 152 PRO PRO B . n 
B 1 162 ARG 162 153 153 ARG ARG B . n 
B 1 163 ALA 163 154 154 ALA ALA B . n 
B 1 164 ILE 164 155 155 ILE ILE B . n 
B 1 165 GLY 165 156 156 GLY GLY B . n 
B 1 166 THR 166 157 157 THR THR B . n 
B 1 167 TYR 167 158 158 TYR TYR B . n 
B 1 168 GLU 168 159 159 GLU GLU B . n 
B 1 169 ILE 169 160 160 ILE ILE B . n 
B 1 170 SER 170 161 161 SER SER B . n 
B 1 171 GLN 171 162 162 GLN GLN B . n 
B 1 172 VAL 172 163 163 VAL VAL B . n 
B 1 173 VAL 173 164 164 VAL VAL B . n 
B 1 174 GLU 174 165 165 GLU GLU B . n 
B 1 175 ASP 175 166 166 ASP ASP B . n 
B 1 176 TYR 176 167 167 TYR TYR B . n 
B 1 177 ARG 177 168 168 ARG ARG B . n 
B 1 178 ARG 178 169 169 ARG ARG B . n 
B 1 179 SER 179 170 170 SER SER B . n 
B 1 180 ALA 180 171 171 ALA ALA B . n 
B 1 181 LEU 181 172 172 LEU LEU B . n 
B 1 182 ASN 182 173 173 ASN ASN B . n 
B 1 183 ALA 183 174 174 ALA ALA B . n 
B 1 184 ILE 184 175 175 ILE ILE B . n 
B 1 185 GLU 185 176 176 GLU GLU B . n 
B 1 186 ALA 186 177 177 ALA ALA B . n 
B 1 187 GLY 187 178 178 GLY GLY B . n 
B 1 188 PHE 188 179 179 PHE PHE B . n 
B 1 189 ASP 189 180 180 ASP ASP B . n 
B 1 190 GLY 190 181 181 GLY GLY B . n 
B 1 191 ILE 191 182 182 ILE ILE B . n 
B 1 192 GLU 192 183 183 GLU GLU B . n 
B 1 193 ILE 193 184 184 ILE ILE B . n 
B 1 194 HIS 194 185 185 HIS HIS B . n 
B 1 195 GLY 195 186 186 GLY GLY B . n 
B 1 196 ALA 196 187 187 ALA ALA B . n 
B 1 197 HIS 197 188 188 HIS HIS B . n 
B 1 198 GLY 198 189 189 GLY GLY B . n 
B 1 199 TYR 199 190 190 TYR TYR B . n 
B 1 200 LEU 200 191 191 LEU LEU B . n 
B 1 201 ILE 201 192 192 ILE ILE B . n 
B 1 202 ASP 202 193 193 ASP ASP B . n 
B 1 203 GLN 203 194 194 GLN GLN B . n 
B 1 204 PHE 204 195 195 PHE PHE B . n 
B 1 205 LEU 205 196 196 LEU LEU B . n 
B 1 206 LYS 206 197 197 LYS LYS B . n 
B 1 207 ASP 207 198 198 ASP ASP B . n 
B 1 208 GLY 208 199 199 GLY GLY B . n 
B 1 209 ILE 209 200 200 ILE ILE B . n 
B 1 210 ASN 210 201 201 ASN ASN B . n 
B 1 211 ASP 211 202 202 ASP ASP B . n 
B 1 212 ARG 212 203 203 ARG ARG B . n 
B 1 213 THR 213 204 204 THR THR B . n 
B 1 214 ASP 214 205 205 ASP ASP B . n 
B 1 215 GLU 215 206 206 GLU GLU B . n 
B 1 216 TYR 216 207 207 TYR TYR B . n 
B 1 217 GLY 217 208 208 GLY GLY B . n 
B 1 218 GLY 218 209 209 GLY GLY B . n 
B 1 219 SER 219 210 210 SER SER B . n 
B 1 220 LEU 220 211 211 LEU LEU B . n 
B 1 221 ALA 221 212 212 ALA ALA B . n 
B 1 222 ASN 222 213 213 ASN ASN B . n 
B 1 223 ARG 223 214 214 ARG ARG B . n 
B 1 224 CYS 224 215 215 CYS CYS B . n 
B 1 225 LYS 225 216 216 LYS LYS B . n 
B 1 226 PHE 226 217 217 PHE PHE B . n 
B 1 227 ILE 227 218 218 ILE ILE B . n 
B 1 228 THR 228 219 219 THR THR B . n 
B 1 229 GLN 229 220 220 GLN GLN B . n 
B 1 230 VAL 230 221 221 VAL VAL B . n 
B 1 231 VAL 231 222 222 VAL VAL B . n 
B 1 232 GLN 232 223 223 GLN GLN B . n 
B 1 233 ALA 233 224 224 ALA ALA B . n 
B 1 234 VAL 234 225 225 VAL VAL B . n 
B 1 235 VAL 235 226 226 VAL VAL B . n 
B 1 236 SER 236 227 227 SER SER B . n 
B 1 237 ALA 237 228 228 ALA ALA B . n 
B 1 238 ILE 238 229 229 ILE ILE B . n 
B 1 239 GLY 239 230 230 GLY GLY B . n 
B 1 240 ALA 240 231 231 ALA ALA B . n 
B 1 241 ASP 241 232 232 ASP ASP B . n 
B 1 242 ARG 242 233 233 ARG ARG B . n 
B 1 243 VAL 243 234 234 VAL VAL B . n 
B 1 244 GLY 244 235 235 GLY GLY B . n 
B 1 245 VAL 245 236 236 VAL VAL B . n 
B 1 246 ARG 246 237 237 ARG ARG B . n 
B 1 247 VAL 247 238 238 VAL VAL B . n 
B 1 248 SER 248 239 239 SER SER B . n 
B 1 249 PRO 249 240 240 PRO PRO B . n 
B 1 250 ALA 250 241 241 ALA ALA B . n 
B 1 251 ILE 251 242 242 ILE ILE B . n 
B 1 252 ASP 252 243 243 ASP ASP B . n 
B 1 253 HIS 253 244 244 HIS HIS B . n 
B 1 254 LEU 254 245 245 LEU LEU B . n 
B 1 255 ASP 255 246 246 ASP ASP B . n 
B 1 256 ALA 256 247 247 ALA ALA B . n 
B 1 257 MET 257 248 248 MET MET B . n 
B 1 258 ASP 258 249 249 ASP ASP B . n 
B 1 259 SER 259 250 250 SER SER B . n 
B 1 260 ASN 260 251 251 ASN ASN B . n 
B 1 261 PRO 261 252 252 PRO PRO B . n 
B 1 262 LEU 262 253 253 LEU LEU B . n 
B 1 263 SER 263 254 254 SER SER B . n 
B 1 264 LEU 264 255 255 LEU LEU B . n 
B 1 265 GLY 265 256 256 GLY GLY B . n 
B 1 266 LEU 266 257 257 LEU LEU B . n 
B 1 267 ALA 267 258 258 ALA ALA B . n 
B 1 268 VAL 268 259 259 VAL VAL B . n 
B 1 269 VAL 269 260 260 VAL VAL B . n 
B 1 270 GLU 270 261 261 GLU GLU B . n 
B 1 271 ARG 271 262 262 ARG ARG B . n 
B 1 272 LEU 272 263 263 LEU LEU B . n 
B 1 273 ASN 273 264 264 ASN ASN B . n 
B 1 274 LYS 274 265 265 LYS LYS B . n 
B 1 275 ILE 275 266 266 ILE ILE B . n 
B 1 276 GLN 276 267 267 GLN GLN B . n 
B 1 277 LEU 277 268 268 LEU LEU B . n 
B 1 278 HIS 278 269 269 HIS HIS B . n 
B 1 279 SER 279 270 270 SER SER B . n 
B 1 280 GLY 280 271 271 GLY GLY B . n 
B 1 281 SER 281 272 272 SER SER B . n 
B 1 282 LYS 282 273 273 LYS LYS B . n 
B 1 283 LEU 283 274 274 LEU LEU B . n 
B 1 284 ALA 284 275 275 ALA ALA B . n 
B 1 285 TYR 285 276 276 TYR TYR B . n 
B 1 286 LEU 286 277 277 LEU LEU B . n 
B 1 287 HIS 287 278 278 HIS HIS B . n 
B 1 288 VAL 288 279 279 VAL VAL B . n 
B 1 289 THR 289 280 280 THR THR B . n 
B 1 290 GLN 290 281 281 GLN GLN B . n 
B 1 291 PRO 291 282 282 PRO PRO B . n 
B 1 292 GLY 292 283 283 GLY GLY B . n 
B 1 293 ASP 293 284 284 ASP ASP B . n 
B 1 294 GLY 294 285 ?   ?   ?   B . n 
B 1 295 ARG 295 286 ?   ?   ?   B . n 
B 1 296 GLY 296 287 287 GLY GLY B . n 
B 1 297 SER 297 288 288 SER SER B . n 
B 1 298 GLU 298 289 289 GLU GLU B . n 
B 1 299 GLU 299 290 290 GLU GLU B . n 
B 1 300 GLU 300 291 291 GLU GLU B . n 
B 1 301 GLU 301 292 292 GLU GLU B . n 
B 1 302 ALA 302 293 293 ALA ALA B . n 
B 1 303 ARG 303 294 294 ARG ARG B . n 
B 1 304 LEU 304 295 295 LEU LEU B . n 
B 1 305 MET 305 296 296 MET MET B . n 
B 1 306 ARG 306 297 297 ARG ARG B . n 
B 1 307 THR 307 298 298 THR THR B . n 
B 1 308 LEU 308 299 299 LEU LEU B . n 
B 1 309 ARG 309 300 300 ARG ARG B . n 
B 1 310 ASN 310 301 301 ASN ASN B . n 
B 1 311 ALA 311 302 302 ALA ALA B . n 
B 1 312 TYR 312 303 303 TYR TYR B . n 
B 1 313 GLN 313 304 304 GLN GLN B . n 
B 1 314 GLY 314 305 305 GLY GLY B . n 
B 1 315 THR 315 306 306 THR THR B . n 
B 1 316 PHE 316 307 307 PHE PHE B . n 
B 1 317 ILE 317 308 308 ILE ILE B . n 
B 1 318 CYS 318 309 309 CYS CYS B . n 
B 1 319 SER 319 310 310 SER SER B . n 
B 1 320 GLY 320 311 311 GLY GLY B . n 
B 1 321 GLY 321 312 312 GLY GLY B . n 
B 1 322 TYR 322 313 313 TYR TYR B . n 
B 1 323 THR 323 314 314 THR THR B . n 
B 1 324 ARG 324 315 315 ARG ARG B . n 
B 1 325 GLU 325 316 316 GLU GLU B . n 
B 1 326 LEU 326 317 317 LEU LEU B . n 
B 1 327 GLY 327 318 318 GLY GLY B . n 
B 1 328 ILE 328 319 319 ILE ILE B . n 
B 1 329 GLU 329 320 320 GLU GLU B . n 
B 1 330 ALA 330 321 321 ALA ALA B . n 
B 1 331 VAL 331 322 322 VAL VAL B . n 
B 1 332 ALA 332 323 323 ALA ALA B . n 
B 1 333 GLN 333 324 324 GLN GLN B . n 
B 1 334 GLY 334 325 325 GLY GLY B . n 
B 1 335 ASP 335 326 326 ASP ASP B . n 
B 1 336 ALA 336 327 327 ALA ALA B . n 
B 1 337 ASP 337 328 328 ASP ASP B . n 
B 1 338 LEU 338 329 329 LEU LEU B . n 
B 1 339 VAL 339 330 330 VAL VAL B . n 
B 1 340 SER 340 331 331 SER SER B . n 
B 1 341 TYR 341 332 332 TYR TYR B . n 
B 1 342 GLY 342 333 333 GLY GLY B . n 
B 1 343 ARG 343 334 334 ARG ARG B . n 
B 1 344 LEU 344 335 335 LEU LEU B . n 
B 1 345 PHE 345 336 336 PHE PHE B . n 
B 1 346 ILE 346 337 337 ILE ILE B . n 
B 1 347 SER 347 338 338 SER SER B . n 
B 1 348 ASN 348 339 339 ASN ASN B . n 
B 1 349 PRO 349 340 340 PRO PRO B . n 
B 1 350 ASP 350 341 341 ASP ASP B . n 
B 1 351 LEU 351 342 342 LEU LEU B . n 
B 1 352 VAL 352 343 343 VAL VAL B . n 
B 1 353 MET 353 344 344 MET MET B . n 
B 1 354 ARG 354 345 345 ARG ARG B . n 
B 1 355 ILE 355 346 346 ILE ILE B . n 
B 1 356 LYS 356 347 347 LYS LYS B . n 
B 1 357 LEU 357 348 348 LEU LEU B . n 
B 1 358 ASN 358 349 349 ASN ASN B . n 
B 1 359 ALA 359 350 350 ALA ALA B . n 
B 1 360 PRO 360 351 351 PRO PRO B . n 
B 1 361 LEU 361 352 352 LEU LEU B . n 
B 1 362 ASN 362 353 353 ASN ASN B . n 
B 1 363 LYS 363 354 354 LYS LYS B . n 
B 1 364 TYR 364 355 355 TYR TYR B . n 
B 1 365 ASN 365 356 356 ASN ASN B . n 
B 1 366 ARG 366 357 357 ARG ARG B . n 
B 1 367 LYS 367 358 358 LYS LYS B . n 
B 1 368 THR 368 359 359 THR THR B . n 
B 1 369 PHE 369 360 360 PHE PHE B . n 
B 1 370 TYR 370 361 361 TYR TYR B . n 
B 1 371 THR 371 362 362 THR THR B . n 
B 1 372 GLN 372 363 363 GLN GLN B . n 
B 1 373 ASP 373 364 364 ASP ASP B . n 
B 1 374 PRO 374 365 365 PRO PRO B . n 
B 1 375 VAL 375 366 366 VAL VAL B . n 
B 1 376 VAL 376 367 367 VAL VAL B . n 
B 1 377 GLY 377 368 368 GLY GLY B . n 
B 1 378 TYR 378 369 369 TYR TYR B . n 
B 1 379 THR 379 370 370 THR THR B . n 
B 1 380 ASP 380 371 371 ASP ASP B . n 
B 1 381 TYR 381 372 372 TYR TYR B . n 
B 1 382 PRO 382 373 373 PRO PRO B . n 
B 1 383 PHE 383 374 374 PHE PHE B . n 
B 1 384 LEU 384 375 375 LEU LEU B . n 
B 1 385 GLN 385 376 ?   ?   ?   B . n 
B 1 386 GLY 386 377 ?   ?   ?   B . n 
B 1 387 ASN 387 378 ?   ?   ?   B . n 
B 1 388 GLY 388 379 ?   ?   ?   B . n 
B 1 389 SER 389 380 ?   ?   ?   B . n 
B 1 390 ASN 390 381 ?   ?   ?   B . n 
B 1 391 GLY 391 382 ?   ?   ?   B . n 
B 1 392 PRO 392 383 ?   ?   ?   B . n 
B 1 393 LEU 393 384 ?   ?   ?   B . n 
B 1 394 SER 394 385 ?   ?   ?   B . n 
B 1 395 ARG 395 386 ?   ?   ?   B . n 
B 1 396 LEU 396 387 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        5J8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   5J8 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 FMN 1   401 392 FMN FMN A . 
D 3 5J8 1   402 393 5J8 5J8 A . 
E 2 FMN 1   401 392 FMN FMN B . 
F 3 5J8 1   402 393 5J8 5J8 B . 
G 4 HOH 1   501 594 HOH HOH A . 
G 4 HOH 2   502 797 HOH HOH A . 
G 4 HOH 3   503 744 HOH HOH A . 
G 4 HOH 4   504 615 HOH HOH A . 
G 4 HOH 5   505 196 HOH HOH A . 
G 4 HOH 6   506 848 HOH HOH A . 
G 4 HOH 7   507 596 HOH HOH A . 
G 4 HOH 8   508 64  HOH HOH A . 
G 4 HOH 9   509 654 HOH HOH A . 
G 4 HOH 10  510 640 HOH HOH A . 
G 4 HOH 11  511 186 HOH HOH A . 
G 4 HOH 12  512 732 HOH HOH A . 
G 4 HOH 13  513 135 HOH HOH A . 
G 4 HOH 14  514 588 HOH HOH A . 
G 4 HOH 15  515 192 HOH HOH A . 
G 4 HOH 16  516 884 HOH HOH A . 
G 4 HOH 17  517 878 HOH HOH A . 
G 4 HOH 18  518 88  HOH HOH A . 
G 4 HOH 19  519 909 HOH HOH A . 
G 4 HOH 20  520 153 HOH HOH A . 
G 4 HOH 21  521 105 HOH HOH A . 
G 4 HOH 22  522 854 HOH HOH A . 
G 4 HOH 23  523 121 HOH HOH A . 
G 4 HOH 24  524 150 HOH HOH A . 
G 4 HOH 25  525 850 HOH HOH A . 
G 4 HOH 26  526 51  HOH HOH A . 
G 4 HOH 27  527 650 HOH HOH A . 
G 4 HOH 28  528 116 HOH HOH A . 
G 4 HOH 29  529 892 HOH HOH A . 
G 4 HOH 30  530 795 HOH HOH A . 
G 4 HOH 31  531 774 HOH HOH A . 
G 4 HOH 32  532 906 HOH HOH A . 
G 4 HOH 33  533 942 HOH HOH A . 
G 4 HOH 34  534 701 HOH HOH A . 
G 4 HOH 35  535 31  HOH HOH A . 
G 4 HOH 36  536 39  HOH HOH A . 
G 4 HOH 37  537 187 HOH HOH A . 
G 4 HOH 38  538 207 HOH HOH A . 
G 4 HOH 39  539 164 HOH HOH A . 
G 4 HOH 40  540 54  HOH HOH A . 
G 4 HOH 41  541 166 HOH HOH A . 
G 4 HOH 42  542 198 HOH HOH A . 
G 4 HOH 43  543 678 HOH HOH A . 
G 4 HOH 44  544 181 HOH HOH A . 
G 4 HOH 45  545 184 HOH HOH A . 
G 4 HOH 46  546 148 HOH HOH A . 
G 4 HOH 47  547 718 HOH HOH A . 
G 4 HOH 48  548 160 HOH HOH A . 
G 4 HOH 49  549 7   HOH HOH A . 
G 4 HOH 50  550 830 HOH HOH A . 
G 4 HOH 51  551 58  HOH HOH A . 
G 4 HOH 52  552 101 HOH HOH A . 
G 4 HOH 53  553 156 HOH HOH A . 
G 4 HOH 54  554 29  HOH HOH A . 
G 4 HOH 55  555 86  HOH HOH A . 
G 4 HOH 56  556 93  HOH HOH A . 
G 4 HOH 57  557 26  HOH HOH A . 
G 4 HOH 58  558 589 HOH HOH A . 
G 4 HOH 59  559 582 HOH HOH A . 
G 4 HOH 60  560 758 HOH HOH A . 
G 4 HOH 61  561 881 HOH HOH A . 
G 4 HOH 62  562 894 HOH HOH A . 
G 4 HOH 63  563 48  HOH HOH A . 
G 4 HOH 64  564 90  HOH HOH A . 
G 4 HOH 65  565 131 HOH HOH A . 
G 4 HOH 66  566 114 HOH HOH A . 
G 4 HOH 67  567 136 HOH HOH A . 
G 4 HOH 68  568 19  HOH HOH A . 
G 4 HOH 69  569 607 HOH HOH A . 
G 4 HOH 70  570 604 HOH HOH A . 
G 4 HOH 71  571 873 HOH HOH A . 
G 4 HOH 72  572 4   HOH HOH A . 
G 4 HOH 73  573 175 HOH HOH A . 
G 4 HOH 74  574 3   HOH HOH A . 
G 4 HOH 75  575 197 HOH HOH A . 
G 4 HOH 76  576 95  HOH HOH A . 
G 4 HOH 77  577 1   HOH HOH A . 
G 4 HOH 78  578 78  HOH HOH A . 
G 4 HOH 79  579 883 HOH HOH A . 
G 4 HOH 80  580 908 HOH HOH A . 
G 4 HOH 81  581 5   HOH HOH A . 
G 4 HOH 82  582 72  HOH HOH A . 
G 4 HOH 83  583 15  HOH HOH A . 
G 4 HOH 84  584 172 HOH HOH A . 
G 4 HOH 85  585 938 HOH HOH A . 
G 4 HOH 86  586 786 HOH HOH A . 
G 4 HOH 87  587 37  HOH HOH A . 
G 4 HOH 88  588 82  HOH HOH A . 
G 4 HOH 89  589 698 HOH HOH A . 
G 4 HOH 90  590 765 HOH HOH A . 
G 4 HOH 91  591 102 HOH HOH A . 
G 4 HOH 92  592 20  HOH HOH A . 
G 4 HOH 93  593 6   HOH HOH A . 
G 4 HOH 94  594 147 HOH HOH A . 
G 4 HOH 95  595 8   HOH HOH A . 
G 4 HOH 96  596 22  HOH HOH A . 
G 4 HOH 97  597 921 HOH HOH A . 
G 4 HOH 98  598 2   HOH HOH A . 
G 4 HOH 99  599 940 HOH HOH A . 
G 4 HOH 100 600 847 HOH HOH A . 
G 4 HOH 101 601 34  HOH HOH A . 
G 4 HOH 102 602 28  HOH HOH A . 
G 4 HOH 103 603 63  HOH HOH A . 
G 4 HOH 104 604 41  HOH HOH A . 
G 4 HOH 105 605 117 HOH HOH A . 
G 4 HOH 106 606 169 HOH HOH A . 
G 4 HOH 107 607 53  HOH HOH A . 
G 4 HOH 108 608 578 HOH HOH A . 
G 4 HOH 109 609 902 HOH HOH A . 
G 4 HOH 110 610 62  HOH HOH A . 
G 4 HOH 111 611 834 HOH HOH A . 
G 4 HOH 112 612 66  HOH HOH A . 
G 4 HOH 113 613 851 HOH HOH A . 
G 4 HOH 114 614 794 HOH HOH A . 
G 4 HOH 115 615 124 HOH HOH A . 
G 4 HOH 116 616 599 HOH HOH A . 
G 4 HOH 117 617 155 HOH HOH A . 
G 4 HOH 118 618 905 HOH HOH A . 
G 4 HOH 119 619 35  HOH HOH A . 
G 4 HOH 120 620 151 HOH HOH A . 
G 4 HOH 121 621 595 HOH HOH A . 
G 4 HOH 122 622 839 HOH HOH A . 
G 4 HOH 123 623 152 HOH HOH A . 
G 4 HOH 124 624 23  HOH HOH A . 
G 4 HOH 125 625 887 HOH HOH A . 
G 4 HOH 126 626 143 HOH HOH A . 
G 4 HOH 127 627 630 HOH HOH A . 
G 4 HOH 128 628 840 HOH HOH A . 
G 4 HOH 129 629 14  HOH HOH A . 
G 4 HOH 130 630 642 HOH HOH A . 
G 4 HOH 131 631 929 HOH HOH A . 
G 4 HOH 132 632 612 HOH HOH A . 
G 4 HOH 133 633 36  HOH HOH A . 
G 4 HOH 134 634 936 HOH HOH A . 
G 4 HOH 135 635 111 HOH HOH A . 
G 4 HOH 136 636 833 HOH HOH A . 
G 4 HOH 137 637 841 HOH HOH A . 
G 4 HOH 138 638 859 HOH HOH A . 
G 4 HOH 139 639 47  HOH HOH A . 
G 4 HOH 140 640 57  HOH HOH A . 
G 4 HOH 141 641 67  HOH HOH A . 
G 4 HOH 142 642 55  HOH HOH A . 
G 4 HOH 143 643 943 HOH HOH A . 
G 4 HOH 144 644 46  HOH HOH A . 
G 4 HOH 145 645 791 HOH HOH A . 
G 4 HOH 146 646 843 HOH HOH A . 
G 4 HOH 147 647 617 HOH HOH A . 
G 4 HOH 148 648 140 HOH HOH A . 
G 4 HOH 149 649 167 HOH HOH A . 
G 4 HOH 150 650 870 HOH HOH A . 
G 4 HOH 151 651 98  HOH HOH A . 
G 4 HOH 152 652 17  HOH HOH A . 
G 4 HOH 153 653 91  HOH HOH A . 
G 4 HOH 154 654 45  HOH HOH A . 
G 4 HOH 155 655 635 HOH HOH A . 
G 4 HOH 156 656 669 HOH HOH A . 
G 4 HOH 157 657 945 HOH HOH A . 
G 4 HOH 158 658 852 HOH HOH A . 
G 4 HOH 159 659 813 HOH HOH A . 
G 4 HOH 160 660 129 HOH HOH A . 
G 4 HOH 161 661 950 HOH HOH A . 
G 4 HOH 162 662 42  HOH HOH A . 
G 4 HOH 163 663 899 HOH HOH A . 
G 4 HOH 164 664 99  HOH HOH A . 
G 4 HOH 165 665 728 HOH HOH A . 
G 4 HOH 166 666 190 HOH HOH A . 
G 4 HOH 167 667 178 HOH HOH A . 
G 4 HOH 168 668 138 HOH HOH A . 
G 4 HOH 169 669 18  HOH HOH A . 
G 4 HOH 170 670 916 HOH HOH A . 
G 4 HOH 171 671 127 HOH HOH A . 
G 4 HOH 172 672 27  HOH HOH A . 
G 4 HOH 173 673 204 HOH HOH A . 
G 4 HOH 174 674 139 HOH HOH A . 
G 4 HOH 175 675 893 HOH HOH A . 
G 4 HOH 176 676 898 HOH HOH A . 
G 4 HOH 177 677 182 HOH HOH A . 
G 4 HOH 178 678 835 HOH HOH A . 
G 4 HOH 179 679 97  HOH HOH A . 
G 4 HOH 180 680 939 HOH HOH A . 
G 4 HOH 181 681 188 HOH HOH A . 
G 4 HOH 182 682 896 HOH HOH A . 
G 4 HOH 183 683 913 HOH HOH A . 
G 4 HOH 184 684 844 HOH HOH A . 
G 4 HOH 185 685 618 HOH HOH A . 
G 4 HOH 186 686 927 HOH HOH A . 
G 4 HOH 187 687 180 HOH HOH A . 
G 4 HOH 188 688 40  HOH HOH A . 
G 4 HOH 189 689 903 HOH HOH A . 
G 4 HOH 190 690 733 HOH HOH A . 
G 4 HOH 191 691 624 HOH HOH A . 
G 4 HOH 192 692 816 HOH HOH A . 
G 4 HOH 193 693 897 HOH HOH A . 
G 4 HOH 194 694 933 HOH HOH A . 
G 4 HOH 195 695 689 HOH HOH A . 
G 4 HOH 196 696 584 HOH HOH A . 
G 4 HOH 197 697 712 HOH HOH A . 
G 4 HOH 198 698 920 HOH HOH A . 
G 4 HOH 199 699 149 HOH HOH A . 
G 4 HOH 200 700 711 HOH HOH A . 
G 4 HOH 201 701 849 HOH HOH A . 
G 4 HOH 202 702 672 HOH HOH A . 
G 4 HOH 203 703 623 HOH HOH A . 
G 4 HOH 204 704 675 HOH HOH A . 
G 4 HOH 205 705 918 HOH HOH A . 
G 4 HOH 206 706 946 HOH HOH A . 
G 4 HOH 207 707 611 HOH HOH A . 
G 4 HOH 208 708 609 HOH HOH A . 
G 4 HOH 209 709 934 HOH HOH A . 
G 4 HOH 210 710 631 HOH HOH A . 
G 4 HOH 211 711 812 HOH HOH A . 
G 4 HOH 212 712 825 HOH HOH A . 
G 4 HOH 213 713 882 HOH HOH A . 
G 4 HOH 214 714 778 HOH HOH A . 
G 4 HOH 215 715 723 HOH HOH A . 
G 4 HOH 216 716 661 HOH HOH A . 
G 4 HOH 217 717 804 HOH HOH A . 
G 4 HOH 218 718 591 HOH HOH A . 
G 4 HOH 219 719 684 HOH HOH A . 
G 4 HOH 220 720 824 HOH HOH A . 
G 4 HOH 221 721 610 HOH HOH A . 
G 4 HOH 222 722 752 HOH HOH A . 
G 4 HOH 223 723 782 HOH HOH A . 
G 4 HOH 224 724 667 HOH HOH A . 
G 4 HOH 225 725 735 HOH HOH A . 
G 4 HOH 226 726 646 HOH HOH A . 
G 4 HOH 227 727 634 HOH HOH A . 
G 4 HOH 228 728 769 HOH HOH A . 
G 4 HOH 229 729 699 HOH HOH A . 
G 4 HOH 230 730 855 HOH HOH A . 
G 4 HOH 231 731 937 HOH HOH A . 
G 4 HOH 232 732 932 HOH HOH A . 
G 4 HOH 233 733 772 HOH HOH A . 
G 4 HOH 234 734 691 HOH HOH A . 
G 4 HOH 235 735 935 HOH HOH A . 
G 4 HOH 236 736 603 HOH HOH A . 
G 4 HOH 237 737 638 HOH HOH A . 
G 4 HOH 238 738 677 HOH HOH A . 
G 4 HOH 239 739 725 HOH HOH A . 
G 4 HOH 240 740 915 HOH HOH A . 
G 4 HOH 241 741 737 HOH HOH A . 
G 4 HOH 242 742 742 HOH HOH A . 
G 4 HOH 243 743 200 HOH HOH A . 
G 4 HOH 244 744 914 HOH HOH A . 
G 4 HOH 245 745 829 HOH HOH A . 
G 4 HOH 246 746 814 HOH HOH A . 
G 4 HOH 247 747 671 HOH HOH A . 
G 4 HOH 248 748 705 HOH HOH A . 
G 4 HOH 249 749 644 HOH HOH A . 
G 4 HOH 250 750 730 HOH HOH A . 
G 4 HOH 251 751 821 HOH HOH A . 
G 4 HOH 252 752 662 HOH HOH A . 
G 4 HOH 253 753 593 HOH HOH A . 
G 4 HOH 254 754 692 HOH HOH A . 
G 4 HOH 255 755 199 HOH HOH A . 
G 4 HOH 256 756 917 HOH HOH A . 
G 4 HOH 257 757 600 HOH HOH A . 
G 4 HOH 258 758 751 HOH HOH A . 
G 4 HOH 259 759 598 HOH HOH A . 
G 4 HOH 260 760 926 HOH HOH A . 
G 4 HOH 261 761 195 HOH HOH A . 
G 4 HOH 262 762 194 HOH HOH A . 
G 4 HOH 263 763 912 HOH HOH A . 
G 4 HOH 264 764 668 HOH HOH A . 
G 4 HOH 265 765 146 HOH HOH A . 
G 4 HOH 266 766 944 HOH HOH A . 
G 4 HOH 267 767 189 HOH HOH A . 
G 4 HOH 268 768 749 HOH HOH A . 
G 4 HOH 269 769 819 HOH HOH A . 
G 4 HOH 270 770 652 HOH HOH A . 
G 4 HOH 271 771 879 HOH HOH A . 
G 4 HOH 272 772 853 HOH HOH A . 
G 4 HOH 273 773 900 HOH HOH A . 
G 4 HOH 274 774 941 HOH HOH A . 
G 4 HOH 275 775 614 HOH HOH A . 
G 4 HOH 276 776 134 HOH HOH A . 
G 4 HOH 277 777 141 HOH HOH A . 
G 4 HOH 278 778 895 HOH HOH A . 
G 4 HOH 279 779 931 HOH HOH A . 
G 4 HOH 280 780 645 HOH HOH A . 
G 4 HOH 281 781 643 HOH HOH A . 
G 4 HOH 282 782 880 HOH HOH A . 
G 4 HOH 283 783 731 HOH HOH A . 
G 4 HOH 284 784 806 HOH HOH A . 
G 4 HOH 285 785 757 HOH HOH A . 
G 4 HOH 286 786 740 HOH HOH A . 
G 4 HOH 287 787 583 HOH HOH A . 
G 4 HOH 288 788 889 HOH HOH A . 
G 4 HOH 289 789 802 HOH HOH A . 
G 4 HOH 290 790 579 HOH HOH A . 
G 4 HOH 291 791 748 HOH HOH A . 
G 4 HOH 292 792 820 HOH HOH A . 
G 4 HOH 293 793 764 HOH HOH A . 
G 4 HOH 294 794 922 HOH HOH A . 
G 4 HOH 295 795 766 HOH HOH A . 
H 4 HOH 1   501 183 HOH HOH B . 
H 4 HOH 2   502 928 HOH HOH B . 
H 4 HOH 3   503 715 HOH HOH B . 
H 4 HOH 4   504 708 HOH HOH B . 
H 4 HOH 5   505 205 HOH HOH B . 
H 4 HOH 6   506 924 HOH HOH B . 
H 4 HOH 7   507 590 HOH HOH B . 
H 4 HOH 8   508 872 HOH HOH B . 
H 4 HOH 9   509 61  HOH HOH B . 
H 4 HOH 10  510 170 HOH HOH B . 
H 4 HOH 11  511 633 HOH HOH B . 
H 4 HOH 12  512 168 HOH HOH B . 
H 4 HOH 13  513 901 HOH HOH B . 
H 4 HOH 14  514 796 HOH HOH B . 
H 4 HOH 15  515 606 HOH HOH B . 
H 4 HOH 16  516 657 HOH HOH B . 
H 4 HOH 17  517 836 HOH HOH B . 
H 4 HOH 18  518 191 HOH HOH B . 
H 4 HOH 19  519 762 HOH HOH B . 
H 4 HOH 20  520 73  HOH HOH B . 
H 4 HOH 21  521 9   HOH HOH B . 
H 4 HOH 22  522 602 HOH HOH B . 
H 4 HOH 23  523 106 HOH HOH B . 
H 4 HOH 24  524 109 HOH HOH B . 
H 4 HOH 25  525 948 HOH HOH B . 
H 4 HOH 26  526 89  HOH HOH B . 
H 4 HOH 27  527 663 HOH HOH B . 
H 4 HOH 28  528 720 HOH HOH B . 
H 4 HOH 29  529 869 HOH HOH B . 
H 4 HOH 30  530 686 HOH HOH B . 
H 4 HOH 31  531 206 HOH HOH B . 
H 4 HOH 32  532 637 HOH HOH B . 
H 4 HOH 33  533 132 HOH HOH B . 
H 4 HOH 34  534 890 HOH HOH B . 
H 4 HOH 35  535 137 HOH HOH B . 
H 4 HOH 36  536 12  HOH HOH B . 
H 4 HOH 37  537 865 HOH HOH B . 
H 4 HOH 38  538 79  HOH HOH B . 
H 4 HOH 39  539 43  HOH HOH B . 
H 4 HOH 40  540 858 HOH HOH B . 
H 4 HOH 41  541 50  HOH HOH B . 
H 4 HOH 42  542 70  HOH HOH B . 
H 4 HOH 43  543 811 HOH HOH B . 
H 4 HOH 44  544 119 HOH HOH B . 
H 4 HOH 45  545 838 HOH HOH B . 
H 4 HOH 46  546 863 HOH HOH B . 
H 4 HOH 47  547 80  HOH HOH B . 
H 4 HOH 48  548 154 HOH HOH B . 
H 4 HOH 49  549 110 HOH HOH B . 
H 4 HOH 50  550 133 HOH HOH B . 
H 4 HOH 51  551 75  HOH HOH B . 
H 4 HOH 52  552 174 HOH HOH B . 
H 4 HOH 53  553 94  HOH HOH B . 
H 4 HOH 54  554 77  HOH HOH B . 
H 4 HOH 55  555 74  HOH HOH B . 
H 4 HOH 56  556 144 HOH HOH B . 
H 4 HOH 57  557 871 HOH HOH B . 
H 4 HOH 58  558 11  HOH HOH B . 
H 4 HOH 59  559 65  HOH HOH B . 
H 4 HOH 60  560 201 HOH HOH B . 
H 4 HOH 61  561 159 HOH HOH B . 
H 4 HOH 62  562 87  HOH HOH B . 
H 4 HOH 63  563 660 HOH HOH B . 
H 4 HOH 64  564 862 HOH HOH B . 
H 4 HOH 65  565 125 HOH HOH B . 
H 4 HOH 66  566 100 HOH HOH B . 
H 4 HOH 67  567 685 HOH HOH B . 
H 4 HOH 68  568 113 HOH HOH B . 
H 4 HOH 69  569 857 HOH HOH B . 
H 4 HOH 70  570 130 HOH HOH B . 
H 4 HOH 71  571 877 HOH HOH B . 
H 4 HOH 72  572 103 HOH HOH B . 
H 4 HOH 73  573 60  HOH HOH B . 
H 4 HOH 74  574 16  HOH HOH B . 
H 4 HOH 75  575 719 HOH HOH B . 
H 4 HOH 76  576 115 HOH HOH B . 
H 4 HOH 77  577 179 HOH HOH B . 
H 4 HOH 78  578 608 HOH HOH B . 
H 4 HOH 79  579 24  HOH HOH B . 
H 4 HOH 80  580 864 HOH HOH B . 
H 4 HOH 81  581 81  HOH HOH B . 
H 4 HOH 82  582 919 HOH HOH B . 
H 4 HOH 83  583 120 HOH HOH B . 
H 4 HOH 84  584 76  HOH HOH B . 
H 4 HOH 85  585 44  HOH HOH B . 
H 4 HOH 86  586 157 HOH HOH B . 
H 4 HOH 87  587 112 HOH HOH B . 
H 4 HOH 88  588 49  HOH HOH B . 
H 4 HOH 89  589 842 HOH HOH B . 
H 4 HOH 90  590 84  HOH HOH B . 
H 4 HOH 91  591 627 HOH HOH B . 
H 4 HOH 92  592 162 HOH HOH B . 
H 4 HOH 93  593 586 HOH HOH B . 
H 4 HOH 94  594 845 HOH HOH B . 
H 4 HOH 95  595 161 HOH HOH B . 
H 4 HOH 96  596 866 HOH HOH B . 
H 4 HOH 97  597 21  HOH HOH B . 
H 4 HOH 98  598 56  HOH HOH B . 
H 4 HOH 99  599 104 HOH HOH B . 
H 4 HOH 100 600 904 HOH HOH B . 
H 4 HOH 101 601 13  HOH HOH B . 
H 4 HOH 102 602 798 HOH HOH B . 
H 4 HOH 103 603 33  HOH HOH B . 
H 4 HOH 104 604 886 HOH HOH B . 
H 4 HOH 105 605 122 HOH HOH B . 
H 4 HOH 106 606 577 HOH HOH B . 
H 4 HOH 107 607 773 HOH HOH B . 
H 4 HOH 108 608 32  HOH HOH B . 
H 4 HOH 109 609 171 HOH HOH B . 
H 4 HOH 110 610 625 HOH HOH B . 
H 4 HOH 111 611 85  HOH HOH B . 
H 4 HOH 112 612 861 HOH HOH B . 
H 4 HOH 113 613 688 HOH HOH B . 
H 4 HOH 114 614 30  HOH HOH B . 
H 4 HOH 115 615 173 HOH HOH B . 
H 4 HOH 116 616 69  HOH HOH B . 
H 4 HOH 117 617 949 HOH HOH B . 
H 4 HOH 118 618 71  HOH HOH B . 
H 4 HOH 119 619 163 HOH HOH B . 
H 4 HOH 120 620 59  HOH HOH B . 
H 4 HOH 121 621 68  HOH HOH B . 
H 4 HOH 122 622 92  HOH HOH B . 
H 4 HOH 123 623 107 HOH HOH B . 
H 4 HOH 124 624 911 HOH HOH B . 
H 4 HOH 125 625 177 HOH HOH B . 
H 4 HOH 126 626 745 HOH HOH B . 
H 4 HOH 127 627 158 HOH HOH B . 
H 4 HOH 128 628 709 HOH HOH B . 
H 4 HOH 129 629 923 HOH HOH B . 
H 4 HOH 130 630 25  HOH HOH B . 
H 4 HOH 131 631 868 HOH HOH B . 
H 4 HOH 132 632 83  HOH HOH B . 
H 4 HOH 133 633 128 HOH HOH B . 
H 4 HOH 134 634 108 HOH HOH B . 
H 4 HOH 135 635 145 HOH HOH B . 
H 4 HOH 136 636 96  HOH HOH B . 
H 4 HOH 137 637 651 HOH HOH B . 
H 4 HOH 138 638 123 HOH HOH B . 
H 4 HOH 139 639 837 HOH HOH B . 
H 4 HOH 140 640 52  HOH HOH B . 
H 4 HOH 141 641 876 HOH HOH B . 
H 4 HOH 142 642 832 HOH HOH B . 
H 4 HOH 143 643 875 HOH HOH B . 
H 4 HOH 144 644 165 HOH HOH B . 
H 4 HOH 145 645 768 HOH HOH B . 
H 4 HOH 146 646 38  HOH HOH B . 
H 4 HOH 147 647 126 HOH HOH B . 
H 4 HOH 148 648 792 HOH HOH B . 
H 4 HOH 149 649 947 HOH HOH B . 
H 4 HOH 150 650 828 HOH HOH B . 
H 4 HOH 151 651 118 HOH HOH B . 
H 4 HOH 152 652 621 HOH HOH B . 
H 4 HOH 153 653 185 HOH HOH B . 
H 4 HOH 154 654 10  HOH HOH B . 
H 4 HOH 155 655 910 HOH HOH B . 
H 4 HOH 156 656 714 HOH HOH B . 
H 4 HOH 157 657 891 HOH HOH B . 
H 4 HOH 158 658 739 HOH HOH B . 
H 4 HOH 159 659 784 HOH HOH B . 
H 4 HOH 160 660 203 HOH HOH B . 
H 4 HOH 161 661 647 HOH HOH B . 
H 4 HOH 162 662 750 HOH HOH B . 
H 4 HOH 163 663 632 HOH HOH B . 
H 4 HOH 164 664 703 HOH HOH B . 
H 4 HOH 165 665 779 HOH HOH B . 
H 4 HOH 166 666 741 HOH HOH B . 
H 4 HOH 167 667 648 HOH HOH B . 
H 4 HOH 168 668 747 HOH HOH B . 
H 4 HOH 169 669 790 HOH HOH B . 
H 4 HOH 170 670 770 HOH HOH B . 
H 4 HOH 171 671 856 HOH HOH B . 
H 4 HOH 172 672 710 HOH HOH B . 
H 4 HOH 173 673 680 HOH HOH B . 
H 4 HOH 174 674 826 HOH HOH B . 
H 4 HOH 175 675 666 HOH HOH B . 
H 4 HOH 176 676 659 HOH HOH B . 
H 4 HOH 177 677 874 HOH HOH B . 
H 4 HOH 178 678 613 HOH HOH B . 
H 4 HOH 179 679 867 HOH HOH B . 
H 4 HOH 180 680 803 HOH HOH B . 
H 4 HOH 181 681 800 HOH HOH B . 
H 4 HOH 182 682 587 HOH HOH B . 
H 4 HOH 183 683 810 HOH HOH B . 
H 4 HOH 184 684 616 HOH HOH B . 
H 4 HOH 185 685 641 HOH HOH B . 
H 4 HOH 186 686 793 HOH HOH B . 
H 4 HOH 187 687 755 HOH HOH B . 
H 4 HOH 188 688 622 HOH HOH B . 
H 4 HOH 189 689 888 HOH HOH B . 
H 4 HOH 190 690 673 HOH HOH B . 
H 4 HOH 191 691 597 HOH HOH B . 
H 4 HOH 192 692 756 HOH HOH B . 
H 4 HOH 193 693 722 HOH HOH B . 
H 4 HOH 194 694 831 HOH HOH B . 
H 4 HOH 195 695 694 HOH HOH B . 
H 4 HOH 196 696 785 HOH HOH B . 
H 4 HOH 197 697 771 HOH HOH B . 
H 4 HOH 198 698 653 HOH HOH B . 
H 4 HOH 199 699 704 HOH HOH B . 
H 4 HOH 200 700 176 HOH HOH B . 
H 4 HOH 201 701 907 HOH HOH B . 
H 4 HOH 202 702 193 HOH HOH B . 
H 4 HOH 203 703 665 HOH HOH B . 
H 4 HOH 204 704 809 HOH HOH B . 
H 4 HOH 205 705 721 HOH HOH B . 
H 4 HOH 206 706 639 HOH HOH B . 
H 4 HOH 207 707 724 HOH HOH B . 
H 4 HOH 208 708 605 HOH HOH B . 
H 4 HOH 209 709 827 HOH HOH B . 
H 4 HOH 210 710 743 HOH HOH B . 
H 4 HOH 211 711 885 HOH HOH B . 
H 4 HOH 212 712 807 HOH HOH B . 
H 4 HOH 213 713 202 HOH HOH B . 
H 4 HOH 214 714 679 HOH HOH B . 
H 4 HOH 215 715 822 HOH HOH B . 
H 4 HOH 216 716 799 HOH HOH B . 
H 4 HOH 217 717 808 HOH HOH B . 
H 4 HOH 218 718 682 HOH HOH B . 
H 4 HOH 219 719 925 HOH HOH B . 
H 4 HOH 220 720 142 HOH HOH B . 
H 4 HOH 221 721 670 HOH HOH B . 
H 4 HOH 222 722 601 HOH HOH B . 
H 4 HOH 223 723 681 HOH HOH B . 
H 4 HOH 224 724 700 HOH HOH B . 
H 4 HOH 225 725 702 HOH HOH B . 
H 4 HOH 226 726 687 HOH HOH B . 
H 4 HOH 227 727 697 HOH HOH B . 
H 4 HOH 228 728 716 HOH HOH B . 
H 4 HOH 229 729 580 HOH HOH B . 
H 4 HOH 230 730 860 HOH HOH B . 
H 4 HOH 231 731 818 HOH HOH B . 
H 4 HOH 232 732 805 HOH HOH B . 
H 4 HOH 233 733 676 HOH HOH B . 
H 4 HOH 234 734 775 HOH HOH B . 
H 4 HOH 235 735 846 HOH HOH B . 
H 4 HOH 236 736 592 HOH HOH B . 
H 4 HOH 237 737 683 HOH HOH B . 
H 4 HOH 238 738 696 HOH HOH B . 
H 4 HOH 239 739 788 HOH HOH B . 
H 4 HOH 240 740 930 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 17  ? CG    ? A LYS 26  CG    
2   1 Y 1 A LYS 17  ? CD    ? A LYS 26  CD    
3   1 Y 1 A LYS 17  ? CE    ? A LYS 26  CE    
4   1 Y 1 A LYS 17  ? NZ    ? A LYS 26  NZ    
5   1 Y 1 A LYS 20  ? CG    ? A LYS 29  CG    
6   1 Y 1 A LYS 20  ? CD    ? A LYS 29  CD    
7   1 Y 1 A LYS 20  ? CE    ? A LYS 29  CE    
8   1 Y 1 A LYS 20  ? NZ    ? A LYS 29  NZ    
9   1 Y 1 A LYS 90  ? CG    ? A LYS 99  CG    
10  1 Y 1 A LYS 90  ? CD    ? A LYS 99  CD    
11  1 Y 1 A LYS 90  ? CE    ? A LYS 99  CE    
12  1 Y 1 A LYS 90  ? NZ    ? A LYS 99  NZ    
13  1 Y 1 A ARG 136 ? CG    ? A ARG 145 CG    
14  1 Y 1 A ARG 136 ? CD    ? A ARG 145 CD    
15  1 Y 1 A ARG 136 ? NE    ? A ARG 145 NE    
16  1 Y 1 A ARG 136 ? CZ    ? A ARG 145 CZ    
17  1 Y 1 A ARG 136 ? NH1   ? A ARG 145 NH1   
18  1 Y 1 A ARG 136 ? NH2   ? A ARG 145 NH2   
19  1 Y 1 A ASP 284 ? CG    ? A ASP 293 CG    
20  1 Y 1 A ASP 284 ? OD1   ? A ASP 293 OD1   
21  1 Y 1 A ASP 284 ? OD2   ? A ASP 293 OD2   
22  1 Y 1 A SER 288 ? OG    ? A SER 297 OG    
23  1 Y 1 A GLU 289 ? CG    ? A GLU 298 CG    
24  1 Y 1 A GLU 289 ? CD    ? A GLU 298 CD    
25  1 Y 1 A GLU 289 ? OE1   ? A GLU 298 OE1   
26  1 Y 1 A GLU 289 ? OE2   ? A GLU 298 OE2   
27  1 Y 1 A GLU 290 ? CG    ? A GLU 299 CG    
28  1 Y 1 A GLU 290 ? CD    ? A GLU 299 CD    
29  1 Y 1 A GLU 290 ? OE1   ? A GLU 299 OE1   
30  1 Y 1 A GLU 290 ? OE2   ? A GLU 299 OE2   
31  1 Y 1 A GLU 291 ? CG    ? A GLU 300 CG    
32  1 Y 1 A GLU 291 ? CD    ? A GLU 300 CD    
33  1 Y 1 A GLU 291 ? OE1   ? A GLU 300 OE1   
34  1 Y 1 A GLU 291 ? OE2   ? A GLU 300 OE2   
35  1 Y 1 A GLU 292 ? CG    ? A GLU 301 CG    
36  1 Y 1 A GLU 292 ? CD    ? A GLU 301 CD    
37  1 Y 1 A GLU 292 ? OE1   ? A GLU 301 OE1   
38  1 Y 1 A GLU 292 ? OE2   ? A GLU 301 OE2   
39  1 Y 1 A GLU 316 ? CG    ? A GLU 325 CG    
40  1 Y 1 A GLU 316 ? CD    ? A GLU 325 CD    
41  1 Y 1 A GLU 316 ? OE1   ? A GLU 325 OE1   
42  1 Y 1 A GLU 316 ? OE2   ? A GLU 325 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 ARG 357 ? CG    ? A ARG 366 CG    
48  1 Y 1 A ARG 357 ? CD    ? A ARG 366 CD    
49  1 Y 1 A ARG 357 ? NE    ? A ARG 366 NE    
50  1 Y 1 A ARG 357 ? CZ    ? A ARG 366 CZ    
51  1 Y 1 A ARG 357 ? NH1   ? A ARG 366 NH1   
52  1 Y 1 A ARG 357 ? NH2   ? A ARG 366 NH2   
53  1 Y 1 B LYS 17  ? CG    ? B LYS 26  CG    
54  1 Y 1 B LYS 17  ? CD    ? B LYS 26  CD    
55  1 Y 1 B LYS 17  ? CE    ? B LYS 26  CE    
56  1 Y 1 B LYS 17  ? NZ    ? B LYS 26  NZ    
57  1 Y 1 B GLU 48  ? CG    ? B GLU 57  CG    
58  1 Y 1 B GLU 48  ? CD    ? B GLU 57  CD    
59  1 Y 1 B GLU 48  ? OE1   ? B GLU 57  OE1   
60  1 Y 1 B GLU 48  ? OE2   ? B GLU 57  OE2   
61  1 Y 1 B GLU 116 ? CG    ? B GLU 125 CG    
62  1 Y 1 B GLU 116 ? CD    ? B GLU 125 CD    
63  1 Y 1 B GLU 116 ? OE1   ? B GLU 125 OE1   
64  1 Y 1 B GLU 116 ? OE2   ? B GLU 125 OE2   
65  1 Y 1 B ARG 136 ? CG    ? B ARG 145 CG    
66  1 Y 1 B ARG 136 ? CD    ? B ARG 145 CD    
67  1 Y 1 B ARG 136 ? NE    ? B ARG 145 NE    
68  1 Y 1 B ARG 136 ? CZ    ? B ARG 145 CZ    
69  1 Y 1 B ARG 136 ? NH1   ? B ARG 145 NH1   
70  1 Y 1 B ARG 136 ? NH2   ? B ARG 145 NH2   
71  1 Y 1 B ARG 169 ? CG    ? B ARG 178 CG    
72  1 Y 1 B ARG 169 ? CD    ? B ARG 178 CD    
73  1 Y 1 B ARG 169 ? NE    ? B ARG 178 NE    
74  1 Y 1 B ARG 169 ? CZ    ? B ARG 178 CZ    
75  1 Y 1 B ARG 169 ? NH1   ? B ARG 178 NH1   
76  1 Y 1 B ARG 169 ? NH2   ? B ARG 178 NH2   
77  1 Y 1 B ASP 284 ? CG    ? B ASP 293 CG    
78  1 Y 1 B ASP 284 ? OD1   ? B ASP 293 OD1   
79  1 Y 1 B ASP 284 ? OD2   ? B ASP 293 OD2   
80  1 Y 1 B SER 288 ? OG    ? B SER 297 OG    
81  1 Y 1 B GLU 289 ? CG    ? B GLU 298 CG    
82  1 Y 1 B GLU 289 ? CD    ? B GLU 298 CD    
83  1 Y 1 B GLU 289 ? OE1   ? B GLU 298 OE1   
84  1 Y 1 B GLU 289 ? OE2   ? B GLU 298 OE2   
85  1 Y 1 B GLU 290 ? CG    ? B GLU 299 CG    
86  1 Y 1 B GLU 290 ? CD    ? B GLU 299 CD    
87  1 Y 1 B GLU 290 ? OE1   ? B GLU 299 OE1   
88  1 Y 1 B GLU 290 ? OE2   ? B GLU 299 OE2   
89  1 Y 1 B GLU 291 ? CG    ? B GLU 300 CG    
90  1 Y 1 B GLU 291 ? CD    ? B GLU 300 CD    
91  1 Y 1 B GLU 291 ? OE1   ? B GLU 300 OE1   
92  1 Y 1 B GLU 291 ? OE2   ? B GLU 300 OE2   
93  1 Y 1 B GLU 292 ? CG    ? B GLU 301 CG    
94  1 Y 1 B GLU 292 ? CD    ? B GLU 301 CD    
95  1 Y 1 B GLU 292 ? OE1   ? B GLU 301 OE1   
96  1 Y 1 B GLU 292 ? OE2   ? B GLU 301 OE2   
97  1 Y 1 B GLU 320 ? CG    ? B GLU 329 CG    
98  1 Y 1 B GLU 320 ? CD    ? B GLU 329 CD    
99  1 Y 1 B GLU 320 ? OE1   ? B GLU 329 OE1   
100 1 Y 1 B GLU 320 ? OE2   ? B GLU 329 OE2   
101 1 Y 1 B ARG 357 ? CG    ? B ARG 366 CG    
102 1 Y 1 B ARG 357 ? CD    ? B ARG 366 CD    
103 1 Y 1 B ARG 357 ? NE    ? B ARG 366 NE    
104 1 Y 1 B ARG 357 ? CZ    ? B ARG 366 CZ    
105 1 Y 1 B ARG 357 ? NH1   ? B ARG 366 NH1   
106 1 Y 1 B ARG 357 ? NH2   ? B ARG 366 NH2   
107 1 Y 1 B LYS 358 ? CG    ? B LYS 367 CG    
108 1 Y 1 B LYS 358 ? CD    ? B LYS 367 CD    
109 1 Y 1 B LYS 358 ? CE    ? B LYS 367 CE    
110 1 Y 1 B LYS 358 ? NZ    ? B LYS 367 NZ    
111 1 N 1 A 5J8 402 ? C4    ? D 5J8 1   C4    
112 1 N 1 A 5J8 402 ? C5    ? D 5J8 1   C5    
113 1 N 1 A 5J8 402 ? C6    ? D 5J8 1   C6    
114 1 N 1 A 5J8 402 ? C8    ? D 5J8 1   C8    
115 1 N 1 A 5J8 402 ? N1    ? D 5J8 1   N1    
116 1 N 1 A 5J8 402 ? N3    ? D 5J8 1   N3    
117 1 N 1 A 5J8 402 ? "C5'" ? D 5J8 1   "C5'" 
118 1 N 1 A 5J8 402 ? "C4'" ? D 5J8 1   "C4'" 
119 1 N 1 A 5J8 402 ? "O4'" ? D 5J8 1   "O4'" 
120 1 N 1 A 5J8 402 ? "C3'" ? D 5J8 1   "C3'" 
121 1 N 1 A 5J8 402 ? "O3'" ? D 5J8 1   "O3'" 
122 1 N 1 A 5J8 402 ? "C2'" ? D 5J8 1   "C2'" 
123 1 N 1 A 5J8 402 ? "O2'" ? D 5J8 1   "O2'" 
124 1 N 1 A 5J8 402 ? "P2'" ? D 5J8 1   "P2'" 
125 1 N 1 A 5J8 402 ? OP1   ? D 5J8 1   OP1   
126 1 N 1 A 5J8 402 ? OP3   ? D 5J8 1   OP3   
127 1 N 1 A 5J8 402 ? OP2   ? D 5J8 1   OP2   
128 1 N 1 A 5J8 402 ? "C1'" ? D 5J8 1   "C1'" 
129 1 N 1 A 5J8 402 ? N9    ? D 5J8 1   N9    
130 1 N 1 A 5J8 402 ? N7    ? D 5J8 1   N7    
131 1 N 1 A 5J8 402 ? C2    ? D 5J8 1   C2    
132 1 N 1 A 5J8 402 ? N6    ? D 5J8 1   N6    
133 1 N 1 B 5J8 402 ? C4    ? F 5J8 1   C4    
134 1 N 1 B 5J8 402 ? C5    ? F 5J8 1   C5    
135 1 N 1 B 5J8 402 ? C6    ? F 5J8 1   C6    
136 1 N 1 B 5J8 402 ? C8    ? F 5J8 1   C8    
137 1 N 1 B 5J8 402 ? N1    ? F 5J8 1   N1    
138 1 N 1 B 5J8 402 ? N3    ? F 5J8 1   N3    
139 1 N 1 B 5J8 402 ? "C5'" ? F 5J8 1   "C5'" 
140 1 N 1 B 5J8 402 ? "C4'" ? F 5J8 1   "C4'" 
141 1 N 1 B 5J8 402 ? "O4'" ? F 5J8 1   "O4'" 
142 1 N 1 B 5J8 402 ? "C3'" ? F 5J8 1   "C3'" 
143 1 N 1 B 5J8 402 ? "O3'" ? F 5J8 1   "O3'" 
144 1 N 1 B 5J8 402 ? "C2'" ? F 5J8 1   "C2'" 
145 1 N 1 B 5J8 402 ? "O2'" ? F 5J8 1   "O2'" 
146 1 N 1 B 5J8 402 ? "P2'" ? F 5J8 1   "P2'" 
147 1 N 1 B 5J8 402 ? OP1   ? F 5J8 1   OP1   
148 1 N 1 B 5J8 402 ? OP3   ? F 5J8 1   OP3   
149 1 N 1 B 5J8 402 ? OP2   ? F 5J8 1   OP2   
150 1 N 1 B 5J8 402 ? "C1'" ? F 5J8 1   "C1'" 
151 1 N 1 B 5J8 402 ? N9    ? F 5J8 1   N9    
152 1 N 1 B 5J8 402 ? N7    ? F 5J8 1   N7    
153 1 N 1 B 5J8 402 ? C2    ? F 5J8 1   C2    
154 1 N 1 B 5J8 402 ? N6    ? F 5J8 1   N6    
# 
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                   98.99 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QNY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.736 
_cell.length_a_esd                 ? 
_cell.length_b                     91.727 
_cell.length_b_esd                 ? 
_cell.length_c                     89.770 
_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                         8QNY 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8QNY 
_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             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.96 
_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, 14% PEG8000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-22 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.96770 
_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                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.96770 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QNY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.65 
_reflns.d_resolution_low                               49.13 
_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                                     632860 
_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                           87.00 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.5 
_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                                   0.995 
_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                                    1.65 
_reflns_shell.d_res_low                                     1.67 
_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                             10981 
_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                                  0.483 
_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                                 8QNY 
_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                            1.65 
_refine.ls_d_res_low                             49.13 
_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                     83146 
_refine.ls_number_reflns_R_free                  4225 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    87.00 
_refine.ls_percent_reflns_R_free                 5.08 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1835 
_refine.ls_R_factor_R_free                       0.2162 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1818 
_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                          1.37 
_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                 22.39 
_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                            0.21 
_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        5556 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         114 
_refine_hist.number_atoms_solvent             545 
_refine_hist.number_atoms_total               6215 
_refine_hist.d_res_high                       1.65 
_refine_hist.d_res_low                        49.13 
# 
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' ? 0.013  ? 5839 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.254  ? 7966 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.093 ? 2098 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.076  ? 879  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.013  ? 1025 ? 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' 1.65 1.67  . . 73  1373 45.00 . . . . 0.3365 . . . . . . . . . . . 0.3440 
'X-RAY DIFFRACTION' 1.67 1.69  . . 81  1488 50.00 . . . . 0.3004 . . . . . . . . . . . 0.3050 
'X-RAY DIFFRACTION' 1.69 1.71  . . 89  1630 54.00 . . . . 0.2888 . . . . . . . . . . . 0.3448 
'X-RAY DIFFRACTION' 1.71 1.73  . . 96  1817 61.00 . . . . 0.2771 . . . . . . . . . . . 0.3047 
'X-RAY DIFFRACTION' 1.73 1.75  . . 96  2067 69.00 . . . . 0.2581 . . . . . . . . . . . 0.2856 
'X-RAY DIFFRACTION' 1.75 1.78  . . 128 2329 77.00 . . . . 0.2499 . . . . . . . . . . . 0.2976 
'X-RAY DIFFRACTION' 1.78 1.80  . . 144 2749 91.00 . . . . 0.2431 . . . . . . . . . . . 0.2633 
'X-RAY DIFFRACTION' 1.80 1.83  . . 161 2840 94.00 . . . . 0.2370 . . . . . . . . . . . 0.2829 
'X-RAY DIFFRACTION' 1.83 1.86  . . 156 2874 96.00 . . . . 0.2216 . . . . . . . . . . . 0.2614 
'X-RAY DIFFRACTION' 1.86 1.89  . . 150 2873 96.00 . . . . 0.2148 . . . . . . . . . . . 0.2631 
'X-RAY DIFFRACTION' 1.89 1.92  . . 162 2927 96.00 . . . . 0.2003 . . . . . . . . . . . 0.2632 
'X-RAY DIFFRACTION' 1.92 1.96  . . 148 2851 96.00 . . . . 0.2063 . . . . . . . . . . . 0.2435 
'X-RAY DIFFRACTION' 1.96 1.99  . . 164 2929 96.00 . . . . 0.2080 . . . . . . . . . . . 0.2354 
'X-RAY DIFFRACTION' 1.99 2.03  . . 155 2841 96.00 . . . . 0.2110 . . . . . . . . . . . 0.2588 
'X-RAY DIFFRACTION' 2.03 2.08  . . 178 2881 96.00 . . . . 0.2006 . . . . . . . . . . . 0.2530 
'X-RAY DIFFRACTION' 2.08 2.13  . . 138 2882 95.00 . . . . 0.1805 . . . . . . . . . . . 0.2221 
'X-RAY DIFFRACTION' 2.13 2.18  . . 154 2874 95.00 . . . . 0.1791 . . . . . . . . . . . 0.2103 
'X-RAY DIFFRACTION' 2.18 2.24  . . 156 2856 95.00 . . . . 0.1860 . . . . . . . . . . . 0.2315 
'X-RAY DIFFRACTION' 2.24 2.31  . . 140 2871 95.00 . . . . 0.1869 . . . . . . . . . . . 0.2295 
'X-RAY DIFFRACTION' 2.31 2.38  . . 150 2902 95.00 . . . . 0.1836 . . . . . . . . . . . 0.2366 
'X-RAY DIFFRACTION' 2.38 2.46  . . 153 2816 94.00 . . . . 0.1793 . . . . . . . . . . . 0.2419 
'X-RAY DIFFRACTION' 2.46 2.56  . . 155 2811 93.00 . . . . 0.1792 . . . . . . . . . . . 0.2087 
'X-RAY DIFFRACTION' 2.56 2.68  . . 172 2811 93.00 . . . . 0.1804 . . . . . . . . . . . 0.2128 
'X-RAY DIFFRACTION' 2.68 2.82  . . 133 2749 90.00 . . . . 0.1823 . . . . . . . . . . . 0.2134 
'X-RAY DIFFRACTION' 2.82 3.00  . . 128 2667 87.00 . . . . 0.1847 . . . . . . . . . . . 0.2379 
'X-RAY DIFFRACTION' 3.00 3.23  . . 118 2244 74.00 . . . . 0.1778 . . . . . . . . . . . 0.2153 
'X-RAY DIFFRACTION' 3.23 3.55  . . 163 2856 94.00 . . . . 0.1671 . . . . . . . . . . . 0.1908 
'X-RAY DIFFRACTION' 3.55 4.07  . . 157 3000 99.00 . . . . 0.1459 . . . . . . . . . . . 0.1706 
'X-RAY DIFFRACTION' 4.07 5.12  . . 181 3026 99.00 . . . . 0.1348 . . . . . . . . . . . 0.1596 
'X-RAY DIFFRACTION' 5.13 49.13 . . 146 3087 99.00 . . . . 0.1766 . . . . . . . . . . . 0.2029 
# 
_struct.entry_id                     8QNY 
_struct.title                        'OPR3 variant with redesigned loop 6 (8aa) in complex with NADPH4' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8QNY 
_struct_keywords.text            'Old Yellow Enzyme, ene-reductase, flavoenzyme, NADPH, FLAVOPROTEIN' 
_struct_keywords.pdbx_keywords   FLAVOPROTEIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    OPR3_SOLLC 
_struct_ref.pdbx_db_accession          Q9FEW9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTSAGFPHVPGI
FTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRAIGTYEI
SQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGADRVGVRVSP
AIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPRYVAYGQTEAGRLGSEEEEARLMRTLRNAYQGTFICSG
GYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLSRL
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8QNY A 10 ? 396 ? Q9FEW9 1 ? 396 ? 1 387 
2 1 8QNY B 10 ? 396 ? Q9FEW9 1 ? 396 ? 1 387 
# 
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 8QNY MET A 1   ? UNP Q9FEW9 ?   ?   'initiating methionine' -8  1  
1 8QNY ALA A 2   ? UNP Q9FEW9 ?   ?   'expression tag'        -7  2  
1 8QNY SER A 3   ? UNP Q9FEW9 ?   ?   'expression tag'        -6  3  
1 8QNY HIS A 4   ? UNP Q9FEW9 ?   ?   'expression tag'        -5  4  
1 8QNY HIS A 5   ? UNP Q9FEW9 ?   ?   'expression tag'        -4  5  
1 8QNY HIS A 6   ? UNP Q9FEW9 ?   ?   'expression tag'        -3  6  
1 8QNY HIS A 7   ? UNP Q9FEW9 ?   ?   'expression tag'        -2  7  
1 8QNY HIS A 8   ? UNP Q9FEW9 ?   ?   'expression tag'        -1  8  
1 8QNY HIS A 9   ? UNP Q9FEW9 ?   ?   'expression tag'        0   9  
1 8QNY GLY A 292 ? UNP Q9FEW9 ARG 283 'engineered mutation'   283 10 
1 8QNY ASP A 293 ? UNP Q9FEW9 TYR 284 'engineered mutation'   284 11 
1 8QNY GLY A 294 ? UNP Q9FEW9 VAL 285 'engineered mutation'   285 12 
1 8QNY ARG A 295 ? UNP Q9FEW9 ALA 286 'engineered mutation'   286 13 
1 8QNY ?   A ?   ? UNP Q9FEW9 TYR 287 deletion                ?   14 
1 8QNY ?   A ?   ? UNP Q9FEW9 GLY 288 deletion                ?   15 
1 8QNY ?   A ?   ? UNP Q9FEW9 GLN 289 deletion                ?   16 
1 8QNY ?   A ?   ? UNP Q9FEW9 THR 290 deletion                ?   17 
1 8QNY ?   A ?   ? UNP Q9FEW9 GLU 291 deletion                ?   18 
1 8QNY ?   A ?   ? UNP Q9FEW9 ALA 292 deletion                ?   19 
1 8QNY ?   A ?   ? UNP Q9FEW9 GLY 293 deletion                ?   20 
1 8QNY ?   A ?   ? UNP Q9FEW9 ARG 294 deletion                ?   21 
1 8QNY ?   A ?   ? UNP Q9FEW9 LEU 295 deletion                ?   22 
2 8QNY MET B 1   ? UNP Q9FEW9 ?   ?   'initiating methionine' -8  23 
2 8QNY ALA B 2   ? UNP Q9FEW9 ?   ?   'expression tag'        -7  24 
2 8QNY SER B 3   ? UNP Q9FEW9 ?   ?   'expression tag'        -6  25 
2 8QNY HIS B 4   ? UNP Q9FEW9 ?   ?   'expression tag'        -5  26 
2 8QNY HIS B 5   ? UNP Q9FEW9 ?   ?   'expression tag'        -4  27 
2 8QNY HIS B 6   ? UNP Q9FEW9 ?   ?   'expression tag'        -3  28 
2 8QNY HIS B 7   ? UNP Q9FEW9 ?   ?   'expression tag'        -2  29 
2 8QNY HIS B 8   ? UNP Q9FEW9 ?   ?   'expression tag'        -1  30 
2 8QNY HIS B 9   ? UNP Q9FEW9 ?   ?   'expression tag'        0   31 
2 8QNY GLY B 292 ? UNP Q9FEW9 ARG 283 'engineered mutation'   283 32 
2 8QNY ASP B 293 ? UNP Q9FEW9 TYR 284 'engineered mutation'   284 33 
2 8QNY GLY B 294 ? UNP Q9FEW9 VAL 285 'engineered mutation'   285 34 
2 8QNY ARG B 295 ? UNP Q9FEW9 ALA 286 'engineered mutation'   286 35 
2 8QNY ?   B ?   ? UNP Q9FEW9 TYR 287 deletion                ?   36 
2 8QNY ?   B ?   ? UNP Q9FEW9 GLY 288 deletion                ?   37 
2 8QNY ?   B ?   ? UNP Q9FEW9 GLN 289 deletion                ?   38 
2 8QNY ?   B ?   ? UNP Q9FEW9 THR 290 deletion                ?   39 
2 8QNY ?   B ?   ? UNP Q9FEW9 GLU 291 deletion                ?   40 
2 8QNY ?   B ?   ? UNP Q9FEW9 ALA 292 deletion                ?   41 
2 8QNY ?   B ?   ? UNP Q9FEW9 GLY 293 deletion                ?   42 
2 8QNY ?   B ?   ? UNP Q9FEW9 ARG 294 deletion                ?   43 
2 8QNY ?   B ?   ? UNP Q9FEW9 LEU 295 deletion                ?   44 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 19  ? SER A 23  ? ASN A 10  SER A 14  5 ? 5  
HELX_P HELX_P2  AA2 ALA A 46  ? ILE A 50  ? ALA A 37  ILE A 41  5 ? 5  
HELX_P HELX_P3  AA3 GLN A 52  ? ALA A 63  ? GLN A 43  ALA A 54  1 ? 12 
HELX_P HELX_P4  AA4 THR A 91  ? LYS A 108 ? THR A 82  LYS A 99  1 ? 18 
HELX_P HELX_P5  AA5 HIS A 124 ? ALA A 132 ? HIS A 115 ALA A 123 5 ? 9  
HELX_P HELX_P6  AA6 GLY A 165 ? GLY A 187 ? GLY A 156 GLY A 178 1 ? 23 
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 ? GLY A 239 ? SER A 210 GLY A 230 1 ? 21 
HELX_P HELX_P9  AA9 ASN A 260 ? GLY A 280 ? ASN A 251 GLY A 271 1 ? 21 
HELX_P HELX_P10 AB1 GLU A 298 ? TYR A 312 ? GLU A 289 TYR A 303 1 ? 15 
HELX_P HELX_P11 AB2 THR A 323 ? GLN A 333 ? THR A 314 GLN A 324 1 ? 11 
HELX_P HELX_P12 AB3 GLY A 342 ? ASN A 348 ? GLY A 333 ASN A 339 1 ? 7  
HELX_P HELX_P13 AB4 ASP A 350 ? ASN A 358 ? ASP A 341 ASN A 349 1 ? 9  
HELX_P HELX_P14 AB5 ASN A 365 ? PHE A 369 ? ASN A 356 PHE A 360 5 ? 5  
HELX_P HELX_P15 AB6 ASN B 19  ? SER B 23  ? ASN B 10  SER B 14  5 ? 5  
HELX_P HELX_P16 AB7 ALA B 46  ? ILE B 50  ? ALA B 37  ILE B 41  5 ? 5  
HELX_P HELX_P17 AB8 GLN B 52  ? ALA B 63  ? GLN B 43  ALA B 54  1 ? 12 
HELX_P HELX_P18 AB9 THR B 91  ? LYS B 108 ? THR B 82  LYS B 99  1 ? 18 
HELX_P HELX_P19 AC1 HIS B 124 ? ALA B 132 ? HIS B 115 ALA B 123 5 ? 9  
HELX_P HELX_P20 AC2 GLY B 165 ? GLY B 187 ? GLY B 156 GLY B 178 1 ? 23 
HELX_P HELX_P21 AC3 TYR B 199 ? LYS B 206 ? TYR B 190 LYS B 197 1 ? 8  
HELX_P HELX_P22 AC4 SER B 219 ? CYS B 224 ? SER B 210 CYS B 215 1 ? 6  
HELX_P HELX_P23 AC5 CYS B 224 ? GLY B 239 ? CYS B 215 GLY B 230 1 ? 16 
HELX_P HELX_P24 AC6 ASN B 260 ? GLY B 280 ? ASN B 251 GLY B 271 1 ? 21 
HELX_P HELX_P25 AC7 SER B 297 ? TYR B 312 ? SER B 288 TYR B 303 1 ? 16 
HELX_P HELX_P26 AC8 THR B 323 ? GLN B 333 ? THR B 314 GLN B 324 1 ? 11 
HELX_P HELX_P27 AC9 GLY B 342 ? ASN B 348 ? GLY B 333 ASN B 339 1 ? 7  
HELX_P HELX_P28 AD1 ASP B 350 ? ASN B 358 ? ASP B 341 ASN B 349 1 ? 9  
HELX_P HELX_P29 AD2 ASN B 365 ? PHE B 369 ? ASN B 356 PHE B 360 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 9 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 9 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? parallel      
AA2 8 9 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? parallel      
AA6 6 7 ? parallel      
AA6 7 8 ? parallel      
AA6 8 9 ? parallel      
AA7 1 2 ? parallel      
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 25  ? MET A 27  ? TYR A 16  MET A 18  
AA1 2 PHE A 30  ? LEU A 32  ? PHE A 21  LEU A 23  
AA2 1 VAL A 36  ? LEU A 38  ? VAL A 27  LEU A 29  
AA2 2 PHE A 68  ? MET A 75  ? PHE A 59  MET A 66  
AA2 3 VAL A 111 ? TRP A 117 ? VAL A 102 TRP A 108 
AA2 4 GLY A 190 ? GLY A 195 ? GLY A 181 GLY A 186 
AA2 5 VAL A 243 ? VAL A 247 ? VAL A 234 VAL A 238 
AA2 6 TYR A 285 ? THR A 289 ? TYR A 276 THR A 280 
AA2 7 PHE A 316 ? SER A 319 ? PHE A 307 SER A 310 
AA2 8 LEU A 338 ? TYR A 341 ? LEU A 329 TYR A 332 
AA2 9 VAL A 36  ? LEU A 38  ? VAL A 27  LEU A 29  
AA3 1 ILE A 135 ? SER A 136 ? ILE A 126 SER A 127 
AA3 2 ARG A 162 ? ALA A 163 ? ARG A 153 ALA A 154 
AA4 1 ILE A 148 ? LEU A 149 ? ILE A 139 LEU A 140 
AA4 2 HIS A 155 ? GLY A 156 ? HIS A 146 GLY A 147 
AA5 1 TYR B 25  ? MET B 27  ? TYR B 16  MET B 18  
AA5 2 PHE B 30  ? LEU B 32  ? PHE B 21  LEU B 23  
AA6 1 VAL B 36  ? LEU B 38  ? VAL B 27  LEU B 29  
AA6 2 PHE B 68  ? MET B 75  ? PHE B 59  MET B 66  
AA6 3 VAL B 111 ? TRP B 117 ? VAL B 102 TRP B 108 
AA6 4 GLY B 190 ? GLY B 195 ? GLY B 181 GLY B 186 
AA6 5 VAL B 243 ? VAL B 247 ? VAL B 234 VAL B 238 
AA6 6 TYR B 285 ? THR B 289 ? TYR B 276 THR B 280 
AA6 7 PHE B 316 ? SER B 319 ? PHE B 307 SER B 310 
AA6 8 LEU B 338 ? TYR B 341 ? LEU B 329 TYR B 332 
AA6 9 VAL B 36  ? LEU B 38  ? VAL B 27  LEU B 29  
AA7 1 ILE B 135 ? SER B 136 ? ILE B 126 SER B 127 
AA7 2 ARG B 162 ? ALA B 163 ? ARG B 153 ALA B 154 
AA8 1 ILE B 148 ? LEU B 149 ? ILE B 139 LEU B 140 
AA8 2 HIS B 155 ? GLY B 156 ? HIS B 146 GLY B 147 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TYR A 25  ? N TYR A 16  O LEU A 32  ? O LEU A 23  
AA2 1 2 N LEU A 38  ? N LEU A 29  O PHE A 68  ? O PHE A 59  
AA2 2 3 N LEU A 69  ? N LEU A 60  O VAL A 111 ? O VAL A 102 
AA2 3 4 N LEU A 116 ? N LEU A 107 O GLU A 192 ? O GLU A 183 
AA2 4 5 N ILE A 193 ? N ILE A 184 O ARG A 246 ? O ARG A 237 
AA2 5 6 N VAL A 245 ? N VAL A 236 O HIS A 287 ? O HIS A 278 
AA2 6 7 N LEU A 286 ? N LEU A 277 O ILE A 317 ? O ILE A 308 
AA2 7 8 N CYS A 318 ? N CYS A 309 O SER A 340 ? O SER A 331 
AA2 8 9 O VAL A 339 ? O VAL A 330 N VAL A 37  ? N VAL A 28  
AA3 1 2 N SER A 136 ? N SER A 127 O ARG A 162 ? O ARG A 153 
AA4 1 2 N ILE A 148 ? N ILE A 139 O GLY A 156 ? O GLY A 147 
AA5 1 2 N TYR B 25  ? N TYR B 16  O LEU B 32  ? O LEU B 23  
AA6 1 2 N LEU B 38  ? N LEU B 29  O PHE B 68  ? O PHE B 59  
AA6 2 3 N THR B 74  ? N THR B 65  O TRP B 117 ? O TRP B 108 
AA6 3 4 N LEU B 116 ? N LEU B 107 O GLU B 192 ? O GLU B 183 
AA6 4 5 N ILE B 191 ? N ILE B 182 O GLY B 244 ? O GLY B 235 
AA6 5 6 N VAL B 245 ? N VAL B 236 O HIS B 287 ? O HIS B 278 
AA6 6 7 N LEU B 286 ? N LEU B 277 O ILE B 317 ? O ILE B 308 
AA6 7 8 N CYS B 318 ? N CYS B 309 O SER B 340 ? O SER B 331 
AA6 8 9 O TYR B 341 ? O TYR B 332 N VAL B 37  ? N VAL B 28  
AA7 1 2 N SER B 136 ? N SER B 127 O ARG B 162 ? O ARG B 153 
AA8 1 2 N ILE B 148 ? N ILE B 139 O GLY B 156 ? O GLY B 147 
# 
_pdbx_entry_details.entry_id                   8QNY 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O B HOH 707 ? ? O B HOH 734 ? ? 2.08 
2 1 O B HOH 591 ? ? O B HOH 707 ? ? 2.09 
3 1 O A HOH 646 ? ? O A HOH 749 ? ? 2.13 
4 1 O A HOH 560 ? ? O A HOH 590 ? ? 2.14 
5 1 O A HOH 512 ? ? O A HOH 742 ? ? 2.15 
6 1 O B HOH 692 ? ? O B HOH 697 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     558 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     690 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_554 
_pdbx_validate_symm_contact.dist              2.18 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CD 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LYS 
_pdbx_validate_rmsd_angle.auth_seq_id_1              354 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LYS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              354 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NZ 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LYS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              354 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                125.69 
_pdbx_validate_rmsd_angle.angle_target_value         111.70 
_pdbx_validate_rmsd_angle.angle_deviation            13.99 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.30 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ILE A 80  ? ? -142.58 31.81   
2  1 ASP A 205 ? ? -108.09 -161.64 
3  1 ALA A 247 ? ? -110.32 76.28   
4  1 ASP A 341 ? ? -98.35  42.84   
5  1 VAL A 366 ? ? -123.90 -57.54  
6  1 TYR A 369 ? ? -130.53 -66.13  
7  1 CYS B 35  ? ? 73.84   33.31   
8  1 GLU B 63  ? ? -47.42  151.72  
9  1 ILE B 80  ? ? -142.78 35.34   
10 1 ASP B 205 ? ? -99.68  -157.94 
11 1 ASP B 341 ? ? -93.50  42.11   
12 1 VAL B 366 ? ? -125.81 -52.03  
13 1 TYR B 369 ? ? -124.50 -69.68  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -8  ? A MET 1   
2  1 Y 1 A ALA -7  ? A ALA 2   
3  1 Y 1 A SER -6  ? A SER 3   
4  1 Y 1 A HIS -5  ? A HIS 4   
5  1 Y 1 A HIS -4  ? A HIS 5   
6  1 Y 1 A HIS -3  ? A HIS 6   
7  1 Y 1 A HIS -2  ? A HIS 7   
8  1 Y 1 A HIS -1  ? A HIS 8   
9  1 Y 1 A HIS 0   ? A HIS 9   
10 1 Y 1 A MET 1   ? A MET 10  
11 1 Y 1 A ALA 2   ? A ALA 11  
12 1 Y 1 A SER 3   ? A SER 12  
13 1 Y 1 A SER 4   ? A SER 13  
14 1 Y 1 A ALA 5   ? A ALA 14  
15 1 Y 1 A GLN 6   ? A GLN 15  
16 1 Y 1 A ASP 7   ? A ASP 16  
17 1 Y 1 A GLY 8   ? A GLY 17  
18 1 Y 1 A ASN 9   ? A ASN 18  
19 1 Y 1 A ARG 286 ? A ARG 295 
20 1 Y 1 A GLY 287 ? A GLY 296 
21 1 Y 1 A GLN 376 ? A GLN 385 
22 1 Y 1 A GLY 377 ? A GLY 386 
23 1 Y 1 A ASN 378 ? A ASN 387 
24 1 Y 1 A GLY 379 ? A GLY 388 
25 1 Y 1 A SER 380 ? A SER 389 
26 1 Y 1 A ASN 381 ? A ASN 390 
27 1 Y 1 A GLY 382 ? A GLY 391 
28 1 Y 1 A PRO 383 ? A PRO 392 
29 1 Y 1 A LEU 384 ? A LEU 393 
30 1 Y 1 A SER 385 ? A SER 394 
31 1 Y 1 A ARG 386 ? A ARG 395 
32 1 Y 1 A LEU 387 ? A LEU 396 
33 1 Y 1 B MET -8  ? B MET 1   
34 1 Y 1 B ALA -7  ? B ALA 2   
35 1 Y 1 B SER -6  ? B SER 3   
36 1 Y 1 B HIS -5  ? B HIS 4   
37 1 Y 1 B HIS -4  ? B HIS 5   
38 1 Y 1 B HIS -3  ? B HIS 6   
39 1 Y 1 B HIS -2  ? B HIS 7   
40 1 Y 1 B HIS -1  ? B HIS 8   
41 1 Y 1 B HIS 0   ? B HIS 9   
42 1 Y 1 B MET 1   ? B MET 10  
43 1 Y 1 B ALA 2   ? B ALA 11  
44 1 Y 1 B SER 3   ? B SER 12  
45 1 Y 1 B SER 4   ? B SER 13  
46 1 Y 1 B ALA 5   ? B ALA 14  
47 1 Y 1 B GLN 6   ? B GLN 15  
48 1 Y 1 B ASP 7   ? B ASP 16  
49 1 Y 1 B GLY 8   ? B GLY 17  
50 1 Y 1 B ASN 9   ? B ASN 18  
51 1 Y 1 B GLY 285 ? B GLY 294 
52 1 Y 1 B ARG 286 ? B ARG 295 
53 1 Y 1 B GLN 376 ? B GLN 385 
54 1 Y 1 B GLY 377 ? B GLY 386 
55 1 Y 1 B ASN 378 ? B ASN 387 
56 1 Y 1 B GLY 379 ? B GLY 388 
57 1 Y 1 B SER 380 ? B SER 389 
58 1 Y 1 B ASN 381 ? B ASN 390 
59 1 Y 1 B GLY 382 ? B GLY 391 
60 1 Y 1 B PRO 383 ? B PRO 392 
61 1 Y 1 B LEU 384 ? B LEU 393 
62 1 Y 1 B SER 385 ? B SER 394 
63 1 Y 1 B ARG 386 ? B ARG 395 
64 1 Y 1 B LEU 387 ? B 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 
5J8 C4     C Y N 1   
5J8 C5     C Y N 2   
5J8 C6     C Y N 3   
5J8 C8     C Y N 4   
5J8 N1     N Y N 5   
5J8 N3     N Y N 6   
5J8 NBU    N N N 7   
5J8 CBT    C N N 8   
5J8 OBV    O N N 9   
5J8 CBR    C N N 10  
5J8 CBQ    C N N 11  
5J8 CBS    C N N 12  
5J8 CBN    C N N 13  
5J8 CBO    C N N 14  
5J8 NBP    N N N 15  
5J8 CBM    C N R 16  
5J8 OBG    O N N 17  
5J8 CBF    C N R 18  
5J8 OBI    O N N 19  
5J8 CBE    C N S 20  
5J8 OBJ    O N N 21  
5J8 CBH    C N R 22  
5J8 CBK    C N N 23  
5J8 OBL    O N N 24  
5J8 PAA    P N N 25  
5J8 OAC    O N N 26  
5J8 OAB    O N N 27  
5J8 OAD    O N N 28  
5J8 PAE    P N N 29  
5J8 OAG    O N N 30  
5J8 OAF    O N N 31  
5J8 "O5'"  O N N 32  
5J8 "C5'"  C N N 33  
5J8 "C4'"  C N R 34  
5J8 "O4'"  O N N 35  
5J8 "C3'"  C N R 36  
5J8 "O3'"  O N N 37  
5J8 "C2'"  C N R 38  
5J8 "O2'"  O N N 39  
5J8 "P2'"  P N N 40  
5J8 OP1    O N N 41  
5J8 OP3    O N N 42  
5J8 OP2    O N N 43  
5J8 "C1'"  C N R 44  
5J8 N9     N Y N 45  
5J8 N7     N Y N 46  
5J8 C2     C Y N 47  
5J8 N6     N N N 48  
5J8 H1     H N N 49  
5J8 H2     H N N 50  
5J8 H3     H N N 51  
5J8 H5     H N N 52  
5J8 H7     H N N 53  
5J8 H8     H N N 54  
5J8 H9     H N N 55  
5J8 H10    H N N 56  
5J8 H11    H N N 57  
5J8 H12    H N N 58  
5J8 H13    H N N 59  
5J8 H14    H N N 60  
5J8 H15    H N N 61  
5J8 H16    H N N 62  
5J8 H17    H N N 63  
5J8 H18    H N N 64  
5J8 H19    H N N 65  
5J8 H20    H N N 66  
5J8 H21    H N N 67  
5J8 H22    H N N 68  
5J8 H23    H N N 69  
5J8 H24    H N N 70  
5J8 H25    H N N 71  
5J8 H26    H N N 72  
5J8 H27    H N N 73  
5J8 H28    H N N 74  
5J8 H29    H N N 75  
5J8 H30    H N N 76  
5J8 H31    H N N 77  
5J8 H32    H N N 78  
5J8 H4     H N N 79  
5J8 H6     H N N 80  
ALA N      N N N 81  
ALA CA     C N S 82  
ALA C      C N N 83  
ALA O      O N N 84  
ALA CB     C N N 85  
ALA OXT    O N N 86  
ALA H      H N N 87  
ALA H2     H N N 88  
ALA HA     H N N 89  
ALA HB1    H N N 90  
ALA HB2    H N N 91  
ALA HB3    H N N 92  
ALA HXT    H N N 93  
ARG N      N N N 94  
ARG CA     C N S 95  
ARG C      C N N 96  
ARG O      O N N 97  
ARG CB     C N N 98  
ARG CG     C N N 99  
ARG CD     C N N 100 
ARG NE     N N N 101 
ARG CZ     C N N 102 
ARG NH1    N N N 103 
ARG NH2    N N N 104 
ARG OXT    O N N 105 
ARG H      H N N 106 
ARG H2     H N N 107 
ARG HA     H N N 108 
ARG HB2    H N N 109 
ARG HB3    H N N 110 
ARG HG2    H N N 111 
ARG HG3    H N N 112 
ARG HD2    H N N 113 
ARG HD3    H N N 114 
ARG HE     H N N 115 
ARG HH11   H N N 116 
ARG HH12   H N N 117 
ARG HH21   H N N 118 
ARG HH22   H N N 119 
ARG HXT    H N N 120 
ASN N      N N N 121 
ASN CA     C N S 122 
ASN C      C N N 123 
ASN O      O N N 124 
ASN CB     C N N 125 
ASN CG     C N N 126 
ASN OD1    O N N 127 
ASN ND2    N N N 128 
ASN OXT    O N N 129 
ASN H      H N N 130 
ASN H2     H N N 131 
ASN HA     H N N 132 
ASN HB2    H N N 133 
ASN HB3    H N N 134 
ASN HD21   H N N 135 
ASN HD22   H N N 136 
ASN HXT    H N N 137 
ASP N      N N N 138 
ASP CA     C N S 139 
ASP C      C N N 140 
ASP O      O N N 141 
ASP CB     C N N 142 
ASP CG     C N N 143 
ASP OD1    O N N 144 
ASP OD2    O N N 145 
ASP OXT    O N N 146 
ASP H      H N N 147 
ASP H2     H N N 148 
ASP HA     H N N 149 
ASP HB2    H N N 150 
ASP HB3    H N N 151 
ASP HD2    H N N 152 
ASP HXT    H N N 153 
CYS N      N N N 154 
CYS CA     C N R 155 
CYS C      C N N 156 
CYS O      O N N 157 
CYS CB     C N N 158 
CYS SG     S N N 159 
CYS OXT    O N N 160 
CYS H      H N N 161 
CYS H2     H N N 162 
CYS HA     H N N 163 
CYS HB2    H N N 164 
CYS HB3    H N N 165 
CYS HG     H N N 166 
CYS HXT    H N N 167 
FMN N1     N N N 168 
FMN C2     C N N 169 
FMN O2     O N N 170 
FMN N3     N N N 171 
FMN C4     C N N 172 
FMN O4     O N N 173 
FMN C4A    C N N 174 
FMN N5     N N N 175 
FMN C5A    C Y N 176 
FMN C6     C Y N 177 
FMN C7     C Y N 178 
FMN C7M    C N N 179 
FMN C8     C Y N 180 
FMN C8M    C N N 181 
FMN C9     C Y N 182 
FMN C9A    C Y N 183 
FMN N10    N N N 184 
FMN C10    C N N 185 
FMN "C1'"  C N N 186 
FMN "C2'"  C N S 187 
FMN "O2'"  O N N 188 
FMN "C3'"  C N S 189 
FMN "O3'"  O N N 190 
FMN "C4'"  C N R 191 
FMN "O4'"  O N N 192 
FMN "C5'"  C N N 193 
FMN "O5'"  O N N 194 
FMN P      P N N 195 
FMN O1P    O N N 196 
FMN O2P    O N N 197 
FMN O3P    O N N 198 
FMN HN3    H N N 199 
FMN H6     H N N 200 
FMN HM71   H N N 201 
FMN HM72   H N N 202 
FMN HM73   H N N 203 
FMN HM81   H N N 204 
FMN HM82   H N N 205 
FMN HM83   H N N 206 
FMN H9     H N N 207 
FMN "H1'1" H N N 208 
FMN "H1'2" H N N 209 
FMN "H2'"  H N N 210 
FMN "HO2'" H N N 211 
FMN "H3'"  H N N 212 
FMN "HO3'" H N N 213 
FMN "H4'"  H N N 214 
FMN "HO4'" H N N 215 
FMN "H5'1" H N N 216 
FMN "H5'2" H N N 217 
FMN HOP2   H N N 218 
FMN HOP3   H N N 219 
GLN N      N N N 220 
GLN CA     C N S 221 
GLN C      C N N 222 
GLN O      O N N 223 
GLN CB     C N N 224 
GLN CG     C N N 225 
GLN CD     C N N 226 
GLN OE1    O N N 227 
GLN NE2    N N N 228 
GLN OXT    O N N 229 
GLN H      H N N 230 
GLN H2     H N N 231 
GLN HA     H N N 232 
GLN HB2    H N N 233 
GLN HB3    H N N 234 
GLN HG2    H N N 235 
GLN HG3    H N N 236 
GLN HE21   H N N 237 
GLN HE22   H N N 238 
GLN HXT    H N N 239 
GLU N      N N N 240 
GLU CA     C N S 241 
GLU C      C N N 242 
GLU O      O N N 243 
GLU CB     C N N 244 
GLU CG     C N N 245 
GLU CD     C N N 246 
GLU OE1    O N N 247 
GLU OE2    O N N 248 
GLU OXT    O N N 249 
GLU H      H N N 250 
GLU H2     H N N 251 
GLU HA     H N N 252 
GLU HB2    H N N 253 
GLU HB3    H N N 254 
GLU HG2    H N N 255 
GLU HG3    H N N 256 
GLU HE2    H N N 257 
GLU HXT    H N N 258 
GLY N      N N N 259 
GLY CA     C N N 260 
GLY C      C N N 261 
GLY O      O N N 262 
GLY OXT    O N N 263 
GLY H      H N N 264 
GLY H2     H N N 265 
GLY HA2    H N N 266 
GLY HA3    H N N 267 
GLY HXT    H N N 268 
HIS N      N N N 269 
HIS CA     C N S 270 
HIS C      C N N 271 
HIS O      O N N 272 
HIS CB     C N N 273 
HIS CG     C Y N 274 
HIS ND1    N Y N 275 
HIS CD2    C Y N 276 
HIS CE1    C Y N 277 
HIS NE2    N Y N 278 
HIS OXT    O N N 279 
HIS H      H N N 280 
HIS H2     H N N 281 
HIS HA     H N N 282 
HIS HB2    H N N 283 
HIS HB3    H N N 284 
HIS HD1    H N N 285 
HIS HD2    H N N 286 
HIS HE1    H N N 287 
HIS HE2    H N N 288 
HIS HXT    H N N 289 
HOH O      O N N 290 
HOH H1     H N N 291 
HOH H2     H N N 292 
ILE N      N N N 293 
ILE CA     C N S 294 
ILE C      C N N 295 
ILE O      O N N 296 
ILE CB     C N S 297 
ILE CG1    C N N 298 
ILE CG2    C N N 299 
ILE CD1    C N N 300 
ILE OXT    O N N 301 
ILE H      H N N 302 
ILE H2     H N N 303 
ILE HA     H N N 304 
ILE HB     H N N 305 
ILE HG12   H N N 306 
ILE HG13   H N N 307 
ILE HG21   H N N 308 
ILE HG22   H N N 309 
ILE HG23   H N N 310 
ILE HD11   H N N 311 
ILE HD12   H N N 312 
ILE HD13   H N N 313 
ILE HXT    H N N 314 
LEU N      N N N 315 
LEU CA     C N S 316 
LEU C      C N N 317 
LEU O      O N N 318 
LEU CB     C N N 319 
LEU CG     C N N 320 
LEU CD1    C N N 321 
LEU CD2    C N N 322 
LEU OXT    O N N 323 
LEU H      H N N 324 
LEU H2     H N N 325 
LEU HA     H N N 326 
LEU HB2    H N N 327 
LEU HB3    H N N 328 
LEU HG     H N N 329 
LEU HD11   H N N 330 
LEU HD12   H N N 331 
LEU HD13   H N N 332 
LEU HD21   H N N 333 
LEU HD22   H N N 334 
LEU HD23   H N N 335 
LEU HXT    H N N 336 
LYS N      N N N 337 
LYS CA     C N S 338 
LYS C      C N N 339 
LYS O      O N N 340 
LYS CB     C N N 341 
LYS CG     C N N 342 
LYS CD     C N N 343 
LYS CE     C N N 344 
LYS NZ     N N N 345 
LYS OXT    O N N 346 
LYS H      H N N 347 
LYS H2     H N N 348 
LYS HA     H N N 349 
LYS HB2    H N N 350 
LYS HB3    H N N 351 
LYS HG2    H N N 352 
LYS HG3    H N N 353 
LYS HD2    H N N 354 
LYS HD3    H N N 355 
LYS HE2    H N N 356 
LYS HE3    H N N 357 
LYS HZ1    H N N 358 
LYS HZ2    H N N 359 
LYS HZ3    H N N 360 
LYS HXT    H N N 361 
MET N      N N N 362 
MET CA     C N S 363 
MET C      C N N 364 
MET O      O N N 365 
MET CB     C N N 366 
MET CG     C N N 367 
MET SD     S N N 368 
MET CE     C N N 369 
MET OXT    O N N 370 
MET H      H N N 371 
MET H2     H N N 372 
MET HA     H N N 373 
MET HB2    H N N 374 
MET HB3    H N N 375 
MET HG2    H N N 376 
MET HG3    H N N 377 
MET HE1    H N N 378 
MET HE2    H N N 379 
MET HE3    H N N 380 
MET HXT    H N N 381 
PHE N      N N N 382 
PHE CA     C N S 383 
PHE C      C N N 384 
PHE O      O N N 385 
PHE CB     C N N 386 
PHE CG     C Y N 387 
PHE CD1    C Y N 388 
PHE CD2    C Y N 389 
PHE CE1    C Y N 390 
PHE CE2    C Y N 391 
PHE CZ     C Y N 392 
PHE OXT    O N N 393 
PHE H      H N N 394 
PHE H2     H N N 395 
PHE HA     H N N 396 
PHE HB2    H N N 397 
PHE HB3    H N N 398 
PHE HD1    H N N 399 
PHE HD2    H N N 400 
PHE HE1    H N N 401 
PHE HE2    H N N 402 
PHE HZ     H N N 403 
PHE HXT    H N N 404 
PRO N      N N N 405 
PRO CA     C N S 406 
PRO C      C N N 407 
PRO O      O N N 408 
PRO CB     C N N 409 
PRO CG     C N N 410 
PRO CD     C N N 411 
PRO OXT    O N N 412 
PRO H      H N N 413 
PRO HA     H N N 414 
PRO HB2    H N N 415 
PRO HB3    H N N 416 
PRO HG2    H N N 417 
PRO HG3    H N N 418 
PRO HD2    H N N 419 
PRO HD3    H N N 420 
PRO HXT    H N N 421 
SER N      N N N 422 
SER CA     C N S 423 
SER C      C N N 424 
SER O      O N N 425 
SER CB     C N N 426 
SER OG     O N N 427 
SER OXT    O N N 428 
SER H      H N N 429 
SER H2     H N N 430 
SER HA     H N N 431 
SER HB2    H N N 432 
SER HB3    H N N 433 
SER HG     H N N 434 
SER HXT    H N N 435 
THR N      N N N 436 
THR CA     C N S 437 
THR C      C N N 438 
THR O      O N N 439 
THR CB     C N R 440 
THR OG1    O N N 441 
THR CG2    C N N 442 
THR OXT    O N N 443 
THR H      H N N 444 
THR H2     H N N 445 
THR HA     H N N 446 
THR HB     H N N 447 
THR HG1    H N N 448 
THR HG21   H N N 449 
THR HG22   H N N 450 
THR HG23   H N N 451 
THR HXT    H N N 452 
TRP N      N N N 453 
TRP CA     C N S 454 
TRP C      C N N 455 
TRP O      O N N 456 
TRP CB     C N N 457 
TRP CG     C Y N 458 
TRP CD1    C Y N 459 
TRP CD2    C Y N 460 
TRP NE1    N Y N 461 
TRP CE2    C Y N 462 
TRP CE3    C Y N 463 
TRP CZ2    C Y N 464 
TRP CZ3    C Y N 465 
TRP CH2    C Y N 466 
TRP OXT    O N N 467 
TRP H      H N N 468 
TRP H2     H N N 469 
TRP HA     H N N 470 
TRP HB2    H N N 471 
TRP HB3    H N N 472 
TRP HD1    H N N 473 
TRP HE1    H N N 474 
TRP HE3    H N N 475 
TRP HZ2    H N N 476 
TRP HZ3    H N N 477 
TRP HH2    H N N 478 
TRP HXT    H N N 479 
TYR N      N N N 480 
TYR CA     C N S 481 
TYR C      C N N 482 
TYR O      O N N 483 
TYR CB     C N N 484 
TYR CG     C Y N 485 
TYR CD1    C Y N 486 
TYR CD2    C Y N 487 
TYR CE1    C Y N 488 
TYR CE2    C Y N 489 
TYR CZ     C Y N 490 
TYR OH     O N N 491 
TYR OXT    O N N 492 
TYR H      H N N 493 
TYR H2     H N N 494 
TYR HA     H N N 495 
TYR HB2    H N N 496 
TYR HB3    H N N 497 
TYR HD1    H N N 498 
TYR HD2    H N N 499 
TYR HE1    H N N 500 
TYR HE2    H N N 501 
TYR HH     H N N 502 
TYR HXT    H N N 503 
VAL N      N N N 504 
VAL CA     C N S 505 
VAL C      C N N 506 
VAL O      O N N 507 
VAL CB     C N N 508 
VAL CG1    C N N 509 
VAL CG2    C N N 510 
VAL OXT    O N N 511 
VAL H      H N N 512 
VAL H2     H N N 513 
VAL HA     H N N 514 
VAL HB     H N N 515 
VAL HG11   H N N 516 
VAL HG12   H N N 517 
VAL HG13   H N N 518 
VAL HG21   H N N 519 
VAL HG22   H N N 520 
VAL HG23   H N N 521 
VAL HXT    H N N 522 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
5J8 OP3   "P2'"  doub N N 1   
5J8 OP2   "P2'"  sing N N 2   
5J8 OP1   "P2'"  sing N N 3   
5J8 "P2'" "O2'"  sing N N 4   
5J8 "O2'" "C2'"  sing N N 5   
5J8 "C2'" "C3'"  sing N N 6   
5J8 "C2'" "C1'"  sing N N 7   
5J8 OAC   PAA    doub N N 8   
5J8 C2    N1     sing Y N 9   
5J8 C2    N3     doub Y N 10  
5J8 N1    C6     doub Y N 11  
5J8 OAG   PAE    doub N N 12  
5J8 "C3'" "O3'"  sing N N 13  
5J8 "C3'" "C4'"  sing N N 14  
5J8 N3    C4     sing Y N 15  
5J8 C6    N6     sing N N 16  
5J8 C6    C5     sing Y N 17  
5J8 OBV   CBT    doub N N 18  
5J8 CBS   CBR    sing N N 19  
5J8 CBS   CBN    sing N N 20  
5J8 CBR   CBT    sing N N 21  
5J8 CBR   CBQ    doub N N 22  
5J8 C4    C5     doub Y N 23  
5J8 C4    N9     sing Y N 24  
5J8 CBN   CBO    sing N N 25  
5J8 C5    N7     sing Y N 26  
5J8 CBT   NBU    sing N N 27  
5J8 CBO   NBP    sing N N 28  
5J8 OBI   CBF    sing N N 29  
5J8 "O5'" PAE    sing N N 30  
5J8 "O5'" "C5'"  sing N N 31  
5J8 N9    "C1'"  sing N N 32  
5J8 N9    C8     sing Y N 33  
5J8 "C1'" "O4'"  sing N N 34  
5J8 N7    C8     doub Y N 35  
5J8 NBP   CBQ    sing N N 36  
5J8 NBP   CBM    sing N N 37  
5J8 PAE   OAD    sing N N 38  
5J8 PAE   OAF    sing N N 39  
5J8 PAA   OAD    sing N N 40  
5J8 PAA   OBL    sing N N 41  
5J8 PAA   OAB    sing N N 42  
5J8 CBF   CBM    sing N N 43  
5J8 CBF   CBE    sing N N 44  
5J8 "C4'" "C5'"  sing N N 45  
5J8 "C4'" "O4'"  sing N N 46  
5J8 OBL   CBK    sing N N 47  
5J8 CBM   OBG    sing N N 48  
5J8 CBE   OBJ    sing N N 49  
5J8 CBE   CBH    sing N N 50  
5J8 OBG   CBH    sing N N 51  
5J8 CBK   CBH    sing N N 52  
5J8 C8    H1     sing N N 53  
5J8 NBU   H2     sing N N 54  
5J8 NBU   H3     sing N N 55  
5J8 CBQ   H5     sing N N 56  
5J8 CBS   H7     sing N N 57  
5J8 CBS   H8     sing N N 58  
5J8 CBN   H9     sing N N 59  
5J8 CBO   H10    sing N N 60  
5J8 CBM   H11    sing N N 61  
5J8 CBF   H12    sing N N 62  
5J8 OBI   H13    sing N N 63  
5J8 CBE   H14    sing N N 64  
5J8 OBJ   H15    sing N N 65  
5J8 CBH   H16    sing N N 66  
5J8 CBK   H17    sing N N 67  
5J8 CBK   H18    sing N N 68  
5J8 OAB   H19    sing N N 69  
5J8 OAF   H20    sing N N 70  
5J8 "C5'" H21    sing N N 71  
5J8 "C5'" H22    sing N N 72  
5J8 "C4'" H23    sing N N 73  
5J8 "C3'" H24    sing N N 74  
5J8 "O3'" H25    sing N N 75  
5J8 "C2'" H26    sing N N 76  
5J8 OP1   H27    sing N N 77  
5J8 OP2   H28    sing N N 78  
5J8 "C1'" H29    sing N N 79  
5J8 C2    H30    sing N N 80  
5J8 N6    H31    sing N N 81  
5J8 N6    H32    sing N N 82  
5J8 CBN   H4     sing N N 83  
5J8 CBO   H6     sing N N 84  
ALA N     CA     sing N N 85  
ALA N     H      sing N N 86  
ALA N     H2     sing N N 87  
ALA CA    C      sing N N 88  
ALA CA    CB     sing N N 89  
ALA CA    HA     sing N N 90  
ALA C     O      doub N N 91  
ALA C     OXT    sing N N 92  
ALA CB    HB1    sing N N 93  
ALA CB    HB2    sing N N 94  
ALA CB    HB3    sing N N 95  
ALA OXT   HXT    sing N N 96  
ARG N     CA     sing N N 97  
ARG N     H      sing N N 98  
ARG N     H2     sing N N 99  
ARG CA    C      sing N N 100 
ARG CA    CB     sing N N 101 
ARG CA    HA     sing N N 102 
ARG C     O      doub N N 103 
ARG C     OXT    sing N N 104 
ARG CB    CG     sing N N 105 
ARG CB    HB2    sing N N 106 
ARG CB    HB3    sing N N 107 
ARG CG    CD     sing N N 108 
ARG CG    HG2    sing N N 109 
ARG CG    HG3    sing N N 110 
ARG CD    NE     sing N N 111 
ARG CD    HD2    sing N N 112 
ARG CD    HD3    sing N N 113 
ARG NE    CZ     sing N N 114 
ARG NE    HE     sing N N 115 
ARG CZ    NH1    sing N N 116 
ARG CZ    NH2    doub N N 117 
ARG NH1   HH11   sing N N 118 
ARG NH1   HH12   sing N N 119 
ARG NH2   HH21   sing N N 120 
ARG NH2   HH22   sing N N 121 
ARG OXT   HXT    sing N N 122 
ASN N     CA     sing N N 123 
ASN N     H      sing N N 124 
ASN N     H2     sing N N 125 
ASN CA    C      sing N N 126 
ASN CA    CB     sing N N 127 
ASN CA    HA     sing N N 128 
ASN C     O      doub N N 129 
ASN C     OXT    sing N N 130 
ASN CB    CG     sing N N 131 
ASN CB    HB2    sing N N 132 
ASN CB    HB3    sing N N 133 
ASN CG    OD1    doub N N 134 
ASN CG    ND2    sing N N 135 
ASN ND2   HD21   sing N N 136 
ASN ND2   HD22   sing N N 137 
ASN OXT   HXT    sing N N 138 
ASP N     CA     sing N N 139 
ASP N     H      sing N N 140 
ASP N     H2     sing N N 141 
ASP CA    C      sing N N 142 
ASP CA    CB     sing N N 143 
ASP CA    HA     sing N N 144 
ASP C     O      doub N N 145 
ASP C     OXT    sing N N 146 
ASP CB    CG     sing N N 147 
ASP CB    HB2    sing N N 148 
ASP CB    HB3    sing N N 149 
ASP CG    OD1    doub N N 150 
ASP CG    OD2    sing N N 151 
ASP OD2   HD2    sing N N 152 
ASP OXT   HXT    sing N N 153 
CYS N     CA     sing N N 154 
CYS N     H      sing N N 155 
CYS N     H2     sing N N 156 
CYS CA    C      sing N N 157 
CYS CA    CB     sing N N 158 
CYS CA    HA     sing N N 159 
CYS C     O      doub N N 160 
CYS C     OXT    sing N N 161 
CYS CB    SG     sing N N 162 
CYS CB    HB2    sing N N 163 
CYS CB    HB3    sing N N 164 
CYS SG    HG     sing N N 165 
CYS OXT   HXT    sing N N 166 
FMN N1    C2     sing N N 167 
FMN N1    C10    doub N N 168 
FMN C2    O2     doub N N 169 
FMN C2    N3     sing N N 170 
FMN N3    C4     sing N N 171 
FMN N3    HN3    sing N N 172 
FMN C4    O4     doub N N 173 
FMN C4    C4A    sing N N 174 
FMN C4A   N5     doub N N 175 
FMN C4A   C10    sing N N 176 
FMN N5    C5A    sing N N 177 
FMN C5A   C6     doub Y N 178 
FMN C5A   C9A    sing Y N 179 
FMN C6    C7     sing Y N 180 
FMN C6    H6     sing N N 181 
FMN C7    C7M    sing N N 182 
FMN C7    C8     doub Y N 183 
FMN C7M   HM71   sing N N 184 
FMN C7M   HM72   sing N N 185 
FMN C7M   HM73   sing N N 186 
FMN C8    C8M    sing N N 187 
FMN C8    C9     sing Y N 188 
FMN C8M   HM81   sing N N 189 
FMN C8M   HM82   sing N N 190 
FMN C8M   HM83   sing N N 191 
FMN C9    C9A    doub Y N 192 
FMN C9    H9     sing N N 193 
FMN C9A   N10    sing N N 194 
FMN N10   C10    sing N N 195 
FMN N10   "C1'"  sing N N 196 
FMN "C1'" "C2'"  sing N N 197 
FMN "C1'" "H1'1" sing N N 198 
FMN "C1'" "H1'2" sing N N 199 
FMN "C2'" "O2'"  sing N N 200 
FMN "C2'" "C3'"  sing N N 201 
FMN "C2'" "H2'"  sing N N 202 
FMN "O2'" "HO2'" sing N N 203 
FMN "C3'" "O3'"  sing N N 204 
FMN "C3'" "C4'"  sing N N 205 
FMN "C3'" "H3'"  sing N N 206 
FMN "O3'" "HO3'" sing N N 207 
FMN "C4'" "O4'"  sing N N 208 
FMN "C4'" "C5'"  sing N N 209 
FMN "C4'" "H4'"  sing N N 210 
FMN "O4'" "HO4'" sing N N 211 
FMN "C5'" "O5'"  sing N N 212 
FMN "C5'" "H5'1" sing N N 213 
FMN "C5'" "H5'2" sing N N 214 
FMN "O5'" P      sing N N 215 
FMN P     O1P    doub N N 216 
FMN P     O2P    sing N N 217 
FMN P     O3P    sing N N 218 
FMN O2P   HOP2   sing N N 219 
FMN O3P   HOP3   sing N N 220 
GLN N     CA     sing N N 221 
GLN N     H      sing N N 222 
GLN N     H2     sing N N 223 
GLN CA    C      sing N N 224 
GLN CA    CB     sing N N 225 
GLN CA    HA     sing N N 226 
GLN C     O      doub N N 227 
GLN C     OXT    sing N N 228 
GLN CB    CG     sing N N 229 
GLN CB    HB2    sing N N 230 
GLN CB    HB3    sing N N 231 
GLN CG    CD     sing N N 232 
GLN CG    HG2    sing N N 233 
GLN CG    HG3    sing N N 234 
GLN CD    OE1    doub N N 235 
GLN CD    NE2    sing N N 236 
GLN NE2   HE21   sing N N 237 
GLN NE2   HE22   sing N N 238 
GLN OXT   HXT    sing N N 239 
GLU N     CA     sing N N 240 
GLU N     H      sing N N 241 
GLU N     H2     sing N N 242 
GLU CA    C      sing N N 243 
GLU CA    CB     sing N N 244 
GLU CA    HA     sing N N 245 
GLU C     O      doub N N 246 
GLU C     OXT    sing N N 247 
GLU CB    CG     sing N N 248 
GLU CB    HB2    sing N N 249 
GLU CB    HB3    sing N N 250 
GLU CG    CD     sing N N 251 
GLU CG    HG2    sing N N 252 
GLU CG    HG3    sing N N 253 
GLU CD    OE1    doub N N 254 
GLU CD    OE2    sing N N 255 
GLU OE2   HE2    sing N N 256 
GLU OXT   HXT    sing N N 257 
GLY N     CA     sing N N 258 
GLY N     H      sing N N 259 
GLY N     H2     sing N N 260 
GLY CA    C      sing N N 261 
GLY CA    HA2    sing N N 262 
GLY CA    HA3    sing N N 263 
GLY C     O      doub N N 264 
GLY C     OXT    sing N N 265 
GLY OXT   HXT    sing N N 266 
HIS N     CA     sing N N 267 
HIS N     H      sing N N 268 
HIS N     H2     sing N N 269 
HIS CA    C      sing N N 270 
HIS CA    CB     sing N N 271 
HIS CA    HA     sing N N 272 
HIS C     O      doub N N 273 
HIS C     OXT    sing N N 274 
HIS CB    CG     sing N N 275 
HIS CB    HB2    sing N N 276 
HIS CB    HB3    sing N N 277 
HIS CG    ND1    sing Y N 278 
HIS CG    CD2    doub Y N 279 
HIS ND1   CE1    doub Y N 280 
HIS ND1   HD1    sing N N 281 
HIS CD2   NE2    sing Y N 282 
HIS CD2   HD2    sing N N 283 
HIS CE1   NE2    sing Y N 284 
HIS CE1   HE1    sing N N 285 
HIS NE2   HE2    sing N N 286 
HIS OXT   HXT    sing N N 287 
HOH O     H1     sing N N 288 
HOH O     H2     sing N N 289 
ILE N     CA     sing N N 290 
ILE N     H      sing N N 291 
ILE N     H2     sing N N 292 
ILE CA    C      sing N N 293 
ILE CA    CB     sing N N 294 
ILE CA    HA     sing N N 295 
ILE C     O      doub N N 296 
ILE C     OXT    sing N N 297 
ILE CB    CG1    sing N N 298 
ILE CB    CG2    sing N N 299 
ILE CB    HB     sing N N 300 
ILE CG1   CD1    sing N N 301 
ILE CG1   HG12   sing N N 302 
ILE CG1   HG13   sing N N 303 
ILE CG2   HG21   sing N N 304 
ILE CG2   HG22   sing N N 305 
ILE CG2   HG23   sing N N 306 
ILE CD1   HD11   sing N N 307 
ILE CD1   HD12   sing N N 308 
ILE CD1   HD13   sing N N 309 
ILE OXT   HXT    sing N N 310 
LEU N     CA     sing N N 311 
LEU N     H      sing N N 312 
LEU N     H2     sing N N 313 
LEU CA    C      sing N N 314 
LEU CA    CB     sing N N 315 
LEU CA    HA     sing N N 316 
LEU C     O      doub N N 317 
LEU C     OXT    sing N N 318 
LEU CB    CG     sing N N 319 
LEU CB    HB2    sing N N 320 
LEU CB    HB3    sing N N 321 
LEU CG    CD1    sing N N 322 
LEU CG    CD2    sing N N 323 
LEU CG    HG     sing N N 324 
LEU CD1   HD11   sing N N 325 
LEU CD1   HD12   sing N N 326 
LEU CD1   HD13   sing N N 327 
LEU CD2   HD21   sing N N 328 
LEU CD2   HD22   sing N N 329 
LEU CD2   HD23   sing N N 330 
LEU OXT   HXT    sing N N 331 
LYS N     CA     sing N N 332 
LYS N     H      sing N N 333 
LYS N     H2     sing N N 334 
LYS CA    C      sing N N 335 
LYS CA    CB     sing N N 336 
LYS CA    HA     sing N N 337 
LYS C     O      doub N N 338 
LYS C     OXT    sing N N 339 
LYS CB    CG     sing N N 340 
LYS CB    HB2    sing N N 341 
LYS CB    HB3    sing N N 342 
LYS CG    CD     sing N N 343 
LYS CG    HG2    sing N N 344 
LYS CG    HG3    sing N N 345 
LYS CD    CE     sing N N 346 
LYS CD    HD2    sing N N 347 
LYS CD    HD3    sing N N 348 
LYS CE    NZ     sing N N 349 
LYS CE    HE2    sing N N 350 
LYS CE    HE3    sing N N 351 
LYS NZ    HZ1    sing N N 352 
LYS NZ    HZ2    sing N N 353 
LYS NZ    HZ3    sing N N 354 
LYS OXT   HXT    sing N N 355 
MET N     CA     sing N N 356 
MET N     H      sing N N 357 
MET N     H2     sing N N 358 
MET CA    C      sing N N 359 
MET CA    CB     sing N N 360 
MET CA    HA     sing N N 361 
MET C     O      doub N N 362 
MET C     OXT    sing N N 363 
MET CB    CG     sing N N 364 
MET CB    HB2    sing N N 365 
MET CB    HB3    sing N N 366 
MET CG    SD     sing N N 367 
MET CG    HG2    sing N N 368 
MET CG    HG3    sing N N 369 
MET SD    CE     sing N N 370 
MET CE    HE1    sing N N 371 
MET CE    HE2    sing N N 372 
MET CE    HE3    sing N N 373 
MET OXT   HXT    sing N N 374 
PHE N     CA     sing N N 375 
PHE N     H      sing N N 376 
PHE N     H2     sing N N 377 
PHE CA    C      sing N N 378 
PHE CA    CB     sing N N 379 
PHE CA    HA     sing N N 380 
PHE C     O      doub N N 381 
PHE C     OXT    sing N N 382 
PHE CB    CG     sing N N 383 
PHE CB    HB2    sing N N 384 
PHE CB    HB3    sing N N 385 
PHE CG    CD1    doub Y N 386 
PHE CG    CD2    sing Y N 387 
PHE CD1   CE1    sing Y N 388 
PHE CD1   HD1    sing N N 389 
PHE CD2   CE2    doub Y N 390 
PHE CD2   HD2    sing N N 391 
PHE CE1   CZ     doub Y N 392 
PHE CE1   HE1    sing N N 393 
PHE CE2   CZ     sing Y N 394 
PHE CE2   HE2    sing N N 395 
PHE CZ    HZ     sing N N 396 
PHE OXT   HXT    sing N N 397 
PRO N     CA     sing N N 398 
PRO N     CD     sing N N 399 
PRO N     H      sing N N 400 
PRO CA    C      sing N N 401 
PRO CA    CB     sing N N 402 
PRO CA    HA     sing N N 403 
PRO C     O      doub N N 404 
PRO C     OXT    sing N N 405 
PRO CB    CG     sing N N 406 
PRO CB    HB2    sing N N 407 
PRO CB    HB3    sing N N 408 
PRO CG    CD     sing N N 409 
PRO CG    HG2    sing N N 410 
PRO CG    HG3    sing N N 411 
PRO CD    HD2    sing N N 412 
PRO CD    HD3    sing N N 413 
PRO OXT   HXT    sing N N 414 
SER N     CA     sing N N 415 
SER N     H      sing N N 416 
SER N     H2     sing N N 417 
SER CA    C      sing N N 418 
SER CA    CB     sing N N 419 
SER CA    HA     sing N N 420 
SER C     O      doub N N 421 
SER C     OXT    sing N N 422 
SER CB    OG     sing N N 423 
SER CB    HB2    sing N N 424 
SER CB    HB3    sing N N 425 
SER OG    HG     sing N N 426 
SER OXT   HXT    sing N N 427 
THR N     CA     sing N N 428 
THR N     H      sing N N 429 
THR N     H2     sing N N 430 
THR CA    C      sing N N 431 
THR CA    CB     sing N N 432 
THR CA    HA     sing N N 433 
THR C     O      doub N N 434 
THR C     OXT    sing N N 435 
THR CB    OG1    sing N N 436 
THR CB    CG2    sing N N 437 
THR CB    HB     sing N N 438 
THR OG1   HG1    sing N N 439 
THR CG2   HG21   sing N N 440 
THR CG2   HG22   sing N N 441 
THR CG2   HG23   sing N N 442 
THR OXT   HXT    sing N N 443 
TRP N     CA     sing N N 444 
TRP N     H      sing N N 445 
TRP N     H2     sing N N 446 
TRP CA    C      sing N N 447 
TRP CA    CB     sing N N 448 
TRP CA    HA     sing N N 449 
TRP C     O      doub N N 450 
TRP C     OXT    sing N N 451 
TRP CB    CG     sing N N 452 
TRP CB    HB2    sing N N 453 
TRP CB    HB3    sing N N 454 
TRP CG    CD1    doub Y N 455 
TRP CG    CD2    sing Y N 456 
TRP CD1   NE1    sing Y N 457 
TRP CD1   HD1    sing N N 458 
TRP CD2   CE2    doub Y N 459 
TRP CD2   CE3    sing Y N 460 
TRP NE1   CE2    sing Y N 461 
TRP NE1   HE1    sing N N 462 
TRP CE2   CZ2    sing Y N 463 
TRP CE3   CZ3    doub Y N 464 
TRP CE3   HE3    sing N N 465 
TRP CZ2   CH2    doub Y N 466 
TRP CZ2   HZ2    sing N N 467 
TRP CZ3   CH2    sing Y N 468 
TRP CZ3   HZ3    sing N N 469 
TRP CH2   HH2    sing N N 470 
TRP OXT   HXT    sing N N 471 
TYR N     CA     sing N N 472 
TYR N     H      sing N N 473 
TYR N     H2     sing N N 474 
TYR CA    C      sing N N 475 
TYR CA    CB     sing N N 476 
TYR CA    HA     sing N N 477 
TYR C     O      doub N N 478 
TYR C     OXT    sing N N 479 
TYR CB    CG     sing N N 480 
TYR CB    HB2    sing N N 481 
TYR CB    HB3    sing N N 482 
TYR CG    CD1    doub Y N 483 
TYR CG    CD2    sing Y N 484 
TYR CD1   CE1    sing Y N 485 
TYR CD1   HD1    sing N N 486 
TYR CD2   CE2    doub Y N 487 
TYR CD2   HD2    sing N N 488 
TYR CE1   CZ     doub Y N 489 
TYR CE1   HE1    sing N N 490 
TYR CE2   CZ     sing Y N 491 
TYR CE2   HE2    sing N N 492 
TYR CZ    OH     sing N N 493 
TYR OH    HH     sing N N 494 
TYR OXT   HXT    sing N N 495 
VAL N     CA     sing N N 496 
VAL N     H      sing N N 497 
VAL N     H2     sing N N 498 
VAL CA    C      sing N N 499 
VAL CA    CB     sing N N 500 
VAL CA    HA     sing N N 501 
VAL C     O      doub N N 502 
VAL C     OXT    sing N N 503 
VAL CB    CG1    sing N N 504 
VAL CB    CG2    sing N N 505 
VAL CB    HB     sing N N 506 
VAL CG1   HG11   sing N N 507 
VAL CG1   HG12   sing N N 508 
VAL CG1   HG13   sing N N 509 
VAL CG2   HG21   sing N N 510 
VAL CG2   HG22   sing N N 511 
VAL CG2   HG23   sing N N 512 
VAL OXT   HXT    sing N N 513 
# 
_pdbx_audit_support.funding_organization   'Austrian Science Fund' 
_pdbx_audit_support.country                Austria 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2hs6 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8QNY 
_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]   0.020106 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003181 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010902 
_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]   0.011278 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . ASN A 1 19  ? -0.025 -18.204 9.470   1.00 32.48 ? 10  ASN A N     1 
ATOM   2    C CA    . ASN A 1 19  ? 1.279  -17.684 9.048   1.00 26.28 ? 10  ASN A CA    1 
ATOM   3    C C     . ASN A 1 19  ? 1.389  -16.195 9.367   1.00 23.10 ? 10  ASN A C     1 
ATOM   4    O O     . ASN A 1 19  ? 0.811  -15.347 8.659   1.00 25.29 ? 10  ASN A O     1 
ATOM   5    C CB    . ASN A 1 19  ? 1.522  -17.922 7.534   1.00 25.66 ? 10  ASN A CB    1 
ATOM   6    C CG    . ASN A 1 19  ? 2.975  -17.602 7.095   1.00 27.25 ? 10  ASN A CG    1 
ATOM   7    O OD1   . ASN A 1 19  ? 3.705  -16.885 7.768   1.00 25.34 ? 10  ASN A OD1   1 
ATOM   8    N ND2   . ASN A 1 19  ? 3.374  -18.141 5.957   1.00 22.94 ? 10  ASN A ND2   1 
ATOM   9    N N     . PRO A 1 20  ? 2.141  -15.864 10.424  1.00 24.74 ? 11  PRO A N     1 
ATOM   10   C CA    . PRO A 1 20  ? 2.287  -14.451 10.795  1.00 24.29 ? 11  PRO A CA    1 
ATOM   11   C C     . PRO A 1 20  ? 2.986  -13.630 9.738   1.00 23.16 ? 11  PRO A C     1 
ATOM   12   O O     . PRO A 1 20  ? 2.844  -12.406 9.762   1.00 19.88 ? 11  PRO A O     1 
ATOM   13   C CB    . PRO A 1 20  ? 3.093  -14.505 12.103  1.00 25.32 ? 11  PRO A CB    1 
ATOM   14   C CG    . PRO A 1 20  ? 3.809  -15.790 12.042  1.00 29.57 ? 11  PRO A CG    1 
ATOM   15   C CD    . PRO A 1 20  ? 2.925  -16.748 11.301  1.00 29.48 ? 11  PRO A CD    1 
ATOM   16   N N     . LEU A 1 21  ? 3.721  -14.248 8.796   1.00 18.73 ? 12  LEU A N     1 
ATOM   17   C CA    . LEU A 1 21  ? 4.274  -13.459 7.690   1.00 24.26 ? 12  LEU A CA    1 
ATOM   18   C C     . LEU A 1 21  ? 3.181  -12.818 6.864   1.00 22.31 ? 12  LEU A C     1 
ATOM   19   O O     . LEU A 1 21  ? 3.422  -11.789 6.211   1.00 23.72 ? 12  LEU A O     1 
ATOM   20   C CB    . LEU A 1 21  ? 5.161  -14.309 6.776   1.00 23.03 ? 12  LEU A CB    1 
ATOM   21   C CG    . LEU A 1 21  ? 6.545  -14.591 7.343   1.00 19.16 ? 12  LEU A CG    1 
ATOM   22   C CD1   . LEU A 1 21  ? 7.440  -15.304 6.336   1.00 21.89 ? 12  LEU A CD1   1 
ATOM   23   C CD2   . LEU A 1 21  ? 7.149  -13.298 7.774   1.00 24.13 ? 12  LEU A CD2   1 
ATOM   24   N N     . PHE A 1 22  ? 1.976  -13.365 6.911   1.00 19.05 ? 13  PHE A N     1 
ATOM   25   C CA    . PHE A 1 22  ? 0.873  -12.842 6.121   1.00 21.88 ? 13  PHE A CA    1 
ATOM   26   C C     . PHE A 1 22  ? -0.168 -12.117 6.956   1.00 22.79 ? 13  PHE A C     1 
ATOM   27   O O     . PHE A 1 22  ? -1.298 -11.929 6.514   1.00 27.32 ? 13  PHE A O     1 
ATOM   28   C CB    . PHE A 1 22  ? 0.284  -13.964 5.274   1.00 22.96 ? 13  PHE A CB    1 
ATOM   29   C CG    . PHE A 1 22  ? 1.205  -14.326 4.178   1.00 25.19 ? 13  PHE A CG    1 
ATOM   30   C CD1   . PHE A 1 22  ? 2.208  -15.263 4.396   1.00 22.52 ? 13  PHE A CD1   1 
ATOM   31   C CD2   . PHE A 1 22  ? 1.211  -13.587 2.999   1.00 27.43 ? 13  PHE A CD2   1 
ATOM   32   C CE1   . PHE A 1 22  ? 3.143  -15.534 3.405   1.00 26.36 ? 13  PHE A CE1   1 
ATOM   33   C CE2   . PHE A 1 22  ? 2.153  -13.879 1.997   1.00 25.32 ? 13  PHE A CE2   1 
ATOM   34   C CZ    . PHE A 1 22  ? 3.116  -14.848 2.228   1.00 23.32 ? 13  PHE A CZ    1 
ATOM   35   N N     . SER A 1 23  ? 0.258  -11.573 8.151   1.00 25.11 ? 14  SER A N     1 
ATOM   36   C CA    . SER A 1 23  ? -0.619 -10.616 8.808   1.00 23.96 ? 14  SER A CA    1 
ATOM   37   C C     . SER A 1 23  ? -0.272 -9.185  8.404   1.00 25.94 ? 14  SER A C     1 
ATOM   38   O O     . SER A 1 23  ? 0.902  -8.859  8.177   1.00 25.53 ? 14  SER A O     1 
ATOM   39   C CB    . SER A 1 23  ? -0.518 -10.760 10.323  1.00 27.64 ? 14  SER A CB    1 
ATOM   40   O OG    . SER A 1 23  ? 0.813  -10.613 10.737  1.00 26.15 ? 14  SER A OG    1 
ATOM   41   N N     . PRO A 1 24  ? -1.291 -8.324  8.314   1.00 23.61 ? 15  PRO A N     1 
ATOM   42   C CA    . PRO A 1 24  ? -1.066 -6.946  7.864   1.00 24.84 ? 15  PRO A CA    1 
ATOM   43   C C     . PRO A 1 24  ? -0.191 -6.196  8.848   1.00 23.04 ? 15  PRO A C     1 
ATOM   44   O O     . PRO A 1 24  ? -0.153 -6.509  10.044  1.00 22.80 ? 15  PRO A O     1 
ATOM   45   C CB    . PRO A 1 24  ? -2.475 -6.347  7.829   1.00 25.29 ? 15  PRO A CB    1 
ATOM   46   C CG    . PRO A 1 24  ? -3.217 -7.120  8.828   1.00 29.01 ? 15  PRO A CG    1 
ATOM   47   C CD    . PRO A 1 24  ? -2.696 -8.544  8.682   1.00 30.14 ? 15  PRO A CD    1 
ATOM   48   N N     . TYR A 1 25  ? 0.489  -5.177  8.327   1.00 20.16 ? 16  TYR A N     1 
ATOM   49   C CA    . TYR A 1 25  ? 1.390  -4.358  9.109   1.00 18.48 ? 16  TYR A CA    1 
ATOM   50   C C     . TYR A 1 25  ? 1.308  -2.932  8.597   1.00 21.36 ? 16  TYR A C     1 
ATOM   51   O O     . TYR A 1 25  ? 1.402  -2.693  7.388   1.00 20.06 ? 16  TYR A O     1 
ATOM   52   C CB    . TYR A 1 25  ? 2.848  -4.852  9.039   1.00 20.16 ? 16  TYR A CB    1 
ATOM   53   C CG    . TYR A 1 25  ? 3.678  -4.066  10.036  1.00 18.44 ? 16  TYR A CG    1 
ATOM   54   C CD1   . TYR A 1 25  ? 3.581  -4.332  11.383  1.00 20.83 ? 16  TYR A CD1   1 
ATOM   55   C CD2   . TYR A 1 25  ? 4.514  -3.028  9.627   1.00 20.89 ? 16  TYR A CD2   1 
ATOM   56   C CE1   . TYR A 1 25  ? 4.297  -3.604  12.317  1.00 20.80 ? 16  TYR A CE1   1 
ATOM   57   C CE2   . TYR A 1 25  ? 5.233  -2.274  10.561  1.00 23.24 ? 16  TYR A CE2   1 
ATOM   58   C CZ    . TYR A 1 25  ? 5.115  -2.574  11.905  1.00 19.25 ? 16  TYR A CZ    1 
ATOM   59   O OH    . TYR A 1 25  ? 5.825  -1.864  12.838  1.00 19.51 ? 16  TYR A OH    1 
ATOM   60   N N     . LYS A 1 26  ? 1.117  -2.007  9.525   1.00 18.32 ? 17  LYS A N     1 
ATOM   61   C CA    . LYS A 1 26  ? 1.094  -0.569  9.265   1.00 21.76 ? 17  LYS A CA    1 
ATOM   62   C C     . LYS A 1 26  ? 2.514  -0.025  9.337   1.00 26.35 ? 17  LYS A C     1 
ATOM   63   O O     . LYS A 1 26  ? 3.036  0.271   10.421  1.00 24.03 ? 17  LYS A O     1 
ATOM   64   C CB    . LYS A 1 26  ? 0.189  0.125   10.282  1.00 28.54 ? 17  LYS A CB    1 
ATOM   65   N N     . MET A 1 27  ? 3.146  0.131   8.184   1.00 19.72 ? 18  MET A N     1 
ATOM   66   C CA    . MET A 1 27  ? 4.418  0.838   8.132   1.00 22.97 ? 18  MET A CA    1 
ATOM   67   C C     . MET A 1 27  ? 4.119  2.324   7.961   1.00 29.76 ? 18  MET A C     1 
ATOM   68   O O     . MET A 1 27  ? 4.220  2.886   6.869   1.00 25.37 ? 18  MET A O     1 
ATOM   69   C CB    . MET A 1 27  ? 5.282  0.313   6.993   1.00 24.42 ? 18  MET A CB    1 
ATOM   70   C CG    . MET A 1 27  ? 6.659  0.878   6.997   1.00 24.94 ? 18  MET A CG    1 
ATOM   71   S SD    . MET A 1 27  ? 7.656  -0.010  5.808   1.00 25.65 ? 18  MET A SD    1 
ATOM   72   C CE    . MET A 1 27  ? 7.173  0.835   4.294   1.00 20.35 ? 18  MET A CE    1 
ATOM   73   N N     . GLY A 1 28  ? 3.658  2.928   9.064   1.00 30.07 ? 19  GLY A N     1 
ATOM   74   C CA    . GLY A 1 28  ? 3.308  4.349   9.064   1.00 29.10 ? 19  GLY A CA    1 
ATOM   75   C C     . GLY A 1 28  ? 2.067  4.584   8.237   1.00 29.97 ? 19  GLY A C     1 
ATOM   76   O O     . GLY A 1 28  ? 1.030  3.938   8.441   1.00 33.11 ? 19  GLY A O     1 
ATOM   77   N N     . LYS A 1 29  ? 2.177  5.489   7.260   1.00 30.41 ? 20  LYS A N     1 
ATOM   78   C CA    . LYS A 1 29  ? 1.100  5.703   6.309   1.00 27.74 ? 20  LYS A CA    1 
ATOM   79   C C     . LYS A 1 29  ? 0.869  4.499   5.390   1.00 32.10 ? 20  LYS A C     1 
ATOM   80   O O     . LYS A 1 29  ? -0.185 4.419   4.751   1.00 26.89 ? 20  LYS A O     1 
ATOM   81   C CB    . LYS A 1 29  ? 1.390  6.960   5.467   1.00 25.60 ? 20  LYS A CB    1 
ATOM   82   N N     . PHE A 1 30  ? 1.791  3.541   5.320   1.00 25.00 ? 21  PHE A N     1 
ATOM   83   C CA    . PHE A 1 30  ? 1.696  2.479   4.317   1.00 26.21 ? 21  PHE A CA    1 
ATOM   84   C C     . PHE A 1 30  ? 1.116  1.218   4.949   1.00 27.87 ? 21  PHE A C     1 
ATOM   85   O O     . PHE A 1 30  ? 1.674  0.670   5.911   1.00 24.56 ? 21  PHE A O     1 
ATOM   86   C CB    . PHE A 1 30  ? 3.060  2.226   3.675   1.00 25.24 ? 21  PHE A CB    1 
ATOM   87   C CG    . PHE A 1 30  ? 3.682  3.470   3.101   1.00 22.61 ? 21  PHE A CG    1 
ATOM   88   C CD1   . PHE A 1 30  ? 3.207  4.010   1.912   1.00 23.45 ? 21  PHE A CD1   1 
ATOM   89   C CD2   . PHE A 1 30  ? 4.717  4.117   3.763   1.00 29.66 ? 21  PHE A CD2   1 
ATOM   90   C CE1   . PHE A 1 30  ? 3.759  5.174   1.392   1.00 20.70 ? 21  PHE A CE1   1 
ATOM   91   C CE2   . PHE A 1 30  ? 5.263  5.286   3.258   1.00 26.45 ? 21  PHE A CE2   1 
ATOM   92   C CZ    . PHE A 1 30  ? 4.788  5.798   2.058   1.00 21.80 ? 21  PHE A CZ    1 
ATOM   93   N N     . ASN A 1 31  ? -0.025 0.772   4.439   1.00 22.73 ? 22  ASN A N     1 
ATOM   94   C CA    . ASN A 1 31  ? -0.685 -0.396  5.010   1.00 23.47 ? 22  ASN A CA    1 
ATOM   95   C C     . ASN A 1 31  ? -0.274 -1.629  4.209   1.00 23.05 ? 22  ASN A C     1 
ATOM   96   O O     . ASN A 1 31  ? -0.827 -1.899  3.137   1.00 29.03 ? 22  ASN A O     1 
ATOM   97   C CB    . ASN A 1 31  ? -2.193 -0.196  5.033   1.00 29.07 ? 22  ASN A CB    1 
ATOM   98   C CG    . ASN A 1 31  ? -2.593 0.914   5.966   1.00 29.76 ? 22  ASN A CG    1 
ATOM   99   O OD1   . ASN A 1 31  ? -2.567 0.738   7.193   1.00 32.11 ? 22  ASN A OD1   1 
ATOM   100  N ND2   . ASN A 1 31  ? -2.935 2.077   5.402   1.00 32.91 ? 22  ASN A ND2   1 
ATOM   101  N N     . LEU A 1 32  ? 0.672  -2.394  4.750   1.00 20.14 ? 23  LEU A N     1 
ATOM   102  C CA    . LEU A 1 32  ? 1.217  -3.563  4.066   1.00 20.60 ? 23  LEU A CA    1 
ATOM   103  C C     . LEU A 1 32  ? 0.357  -4.801  4.307   1.00 18.76 ? 23  LEU A C     1 
ATOM   104  O O     . LEU A 1 32  ? -0.177 -5.007  5.408   1.00 19.67 ? 23  LEU A O     1 
ATOM   105  C CB    . LEU A 1 32  ? 2.645  -3.816  4.558   1.00 19.61 ? 23  LEU A CB    1 
ATOM   106  C CG    . LEU A 1 32  ? 3.613  -2.632  4.377   1.00 17.77 ? 23  LEU A CG    1 
ATOM   107  C CD1   . LEU A 1 32  ? 5.006  -3.092  4.805   1.00 21.81 ? 23  LEU A CD1   1 
ATOM   108  C CD2   . LEU A 1 32  ? 3.640  -2.130  2.905   1.00 17.97 ? 23  LEU A CD2   1 
ATOM   109  N N     . SER A 1 33  ? 0.227  -5.641  3.271   1.00 18.78 ? 24  SER A N     1 
ATOM   110  C CA    A SER A 1 33  ? -0.638 -6.811  3.367   0.50 16.34 ? 24  SER A CA    1 
ATOM   111  C CA    B SER A 1 33  ? -0.538 -6.811  3.367   0.50 16.41 ? 24  SER A CA    1 
ATOM   112  C C     . SER A 1 33  ? 0.096  -8.041  3.897   1.00 19.65 ? 24  SER A C     1 
ATOM   113  O O     . SER A 1 33  ? -0.546 -8.993  4.333   1.00 19.83 ? 24  SER A O     1 
ATOM   114  C CB    A SER A 1 33  ? -1.302 -7.076  1.998   0.50 21.82 ? 24  SER A CB    1 
ATOM   115  C CB    B SER A 1 33  ? -1.202 -7.076  1.998   0.50 21.81 ? 24  SER A CB    1 
ATOM   116  O OG    A SER A 1 33  ? -0.410 -7.712  1.100   0.50 18.38 ? 24  SER A OG    1 
ATOM   117  O OG    B SER A 1 33  ? -2.132 -6.061  1.664   0.50 24.79 ? 24  SER A OG    1 
ATOM   118  N N     . HIS A 1 34  ? 1.426  -8.016  3.936   1.00 17.23 ? 25  HIS A N     1 
ATOM   119  C CA    . HIS A 1 34  ? 2.247  -9.135  4.377   1.00 14.19 ? 25  HIS A CA    1 
ATOM   120  C C     . HIS A 1 34  ? 3.617  -8.560  4.691   1.00 14.03 ? 25  HIS A C     1 
ATOM   121  O O     . HIS A 1 34  ? 3.930  -7.422  4.317   1.00 16.69 ? 25  HIS A O     1 
ATOM   122  C CB    . HIS A 1 34  ? 2.335  -10.242 3.298   1.00 15.04 ? 25  HIS A CB    1 
ATOM   123  C CG    . HIS A 1 34  ? 2.988  -9.786  2.019   1.00 17.35 ? 25  HIS A CG    1 
ATOM   124  N ND1   . HIS A 1 34  ? 4.356  -9.654  1.890   1.00 17.62 ? 25  HIS A ND1   1 
ATOM   125  C CD2   . HIS A 1 34  ? 2.463  -9.465  0.808   1.00 14.82 ? 25  HIS A CD2   1 
ATOM   126  C CE1   . HIS A 1 34  ? 4.646  -9.277  0.653   1.00 18.58 ? 25  HIS A CE1   1 
ATOM   127  N NE2   . HIS A 1 34  ? 3.515  -9.150  -0.024  1.00 16.84 ? 25  HIS A NE2   1 
ATOM   128  N N     . ARG A 1 35  ? 4.460  -9.382  5.321   1.00 15.32 ? 26  ARG A N     1 
ATOM   129  C CA    . ARG A 1 35  ? 5.688  -8.869  5.904   1.00 14.12 ? 26  ARG A CA    1 
ATOM   130  C C     . ARG A 1 35  ? 6.940  -9.307  5.147   1.00 15.46 ? 26  ARG A C     1 
ATOM   131  O O     . ARG A 1 35  ? 8.045  -9.108  5.657   1.00 16.75 ? 26  ARG A O     1 
ATOM   132  C CB    . ARG A 1 35  ? 5.768  -9.276  7.368   1.00 15.41 ? 26  ARG A CB    1 
ATOM   133  C CG    . ARG A 1 35  ? 4.737  -8.495  8.192   1.00 24.94 ? 26  ARG A CG    1 
ATOM   134  C CD    . ARG A 1 35  ? 4.229  -9.349  9.253   1.00 23.16 ? 26  ARG A CD    1 
ATOM   135  N NE    . ARG A 1 35  ? 3.118  -8.736  9.978   1.00 24.03 ? 26  ARG A NE    1 
ATOM   136  C CZ    . ARG A 1 35  ? 3.236  -8.124  11.146  1.00 22.21 ? 26  ARG A CZ    1 
ATOM   137  N NH1   . ARG A 1 35  ? 4.417  -7.833  11.657  1.00 18.45 ? 26  ARG A NH1   1 
ATOM   138  N NH2   . ARG A 1 35  ? 2.140  -7.830  11.835  1.00 23.88 ? 26  ARG A NH2   1 
ATOM   139  N N     . VAL A 1 36  ? 6.797  -9.872  3.941   1.00 14.33 ? 27  VAL A N     1 
ATOM   140  C CA    . VAL A 1 36  ? 7.947  -10.317 3.154   1.00 13.13 ? 27  VAL A CA    1 
ATOM   141  C C     . VAL A 1 36  ? 8.436  -9.120  2.341   1.00 14.01 ? 27  VAL A C     1 
ATOM   142  O O     . VAL A 1 36  ? 7.690  -8.595  1.500   1.00 13.90 ? 27  VAL A O     1 
ATOM   143  C CB    . VAL A 1 36  ? 7.572  -11.494 2.231   1.00 13.51 ? 27  VAL A CB    1 
ATOM   144  C CG1   . VAL A 1 36  ? 8.749  -11.913 1.373   1.00 14.03 ? 27  VAL A CG1   1 
ATOM   145  C CG2   . VAL A 1 36  ? 7.029  -12.693 3.059   1.00 14.33 ? 27  VAL A CG2   1 
ATOM   146  N N     . VAL A 1 37  ? 9.697  -8.722  2.534   1.00 14.69 ? 28  VAL A N     1 
ATOM   147  C CA    . VAL A 1 37  ? 10.215 -7.502  1.901   1.00 14.92 ? 28  VAL A CA    1 
ATOM   148  C C     . VAL A 1 37  ? 11.289 -7.855  0.869   1.00 12.80 ? 28  VAL A C     1 
ATOM   149  O O     . VAL A 1 37  ? 12.096 -8.761  1.088   1.00 14.90 ? 28  VAL A O     1 
ATOM   150  C CB    . VAL A 1 37  ? 10.770 -6.528  2.952   1.00 14.75 ? 28  VAL A CB    1 
ATOM   151  C CG1   . VAL A 1 37  ? 11.434 -5.289  2.245   1.00 13.85 ? 28  VAL A CG1   1 
ATOM   152  C CG2   . VAL A 1 37  ? 9.637  -6.106  3.947   1.00 15.95 ? 28  VAL A CG2   1 
ATOM   153  N N     . LEU A 1 38  ? 11.277 -7.188  -0.285  1.00 14.06 ? 29  LEU A N     1 
ATOM   154  C CA    . LEU A 1 38  ? 12.393 -7.345  -1.225  1.00 15.05 ? 29  LEU A CA    1 
ATOM   155  C C     . LEU A 1 38  ? 13.567 -6.515  -0.694  1.00 13.61 ? 29  LEU A C     1 
ATOM   156  O O     . LEU A 1 38  ? 13.487 -5.272  -0.623  1.00 13.97 ? 29  LEU A O     1 
ATOM   157  C CB    . LEU A 1 38  ? 11.997 -6.906  -2.631  1.00 11.96 ? 29  LEU A CB    1 
ATOM   158  C CG    . LEU A 1 38  ? 13.182 -6.762  -3.600  1.00 14.60 ? 29  LEU A CG    1 
ATOM   159  C CD1   . LEU A 1 38  ? 13.875 -8.107  -3.823  1.00 12.19 ? 29  LEU A CD1   1 
ATOM   160  C CD2   . LEU A 1 38  ? 12.697 -6.178  -4.969  1.00 13.65 ? 29  LEU A CD2   1 
ATOM   161  N N     . ALA A 1 39  ? 14.665 -7.185  -0.316  1.00 11.35 ? 30  ALA A N     1 
ATOM   162  C CA    . ALA A 1 39  ? 15.858 -6.469  0.115   1.00 11.61 ? 30  ALA A CA    1 
ATOM   163  C C     . ALA A 1 39  ? 16.505 -5.725  -1.066  1.00 13.77 ? 30  ALA A C     1 
ATOM   164  O O     . ALA A 1 39  ? 16.393 -6.160  -2.230  1.00 12.78 ? 30  ALA A O     1 
ATOM   165  C CB    . ALA A 1 39  ? 16.886 -7.445  0.713   1.00 14.75 ? 30  ALA A CB    1 
ATOM   166  N N     . PRO A 1 40  ? 17.164 -4.598  -0.790  1.00 13.97 ? 31  PRO A N     1 
ATOM   167  C CA    . PRO A 1 40  ? 17.853 -3.843  -1.848  1.00 12.31 ? 31  PRO A CA    1 
ATOM   168  C C     . PRO A 1 40  ? 18.993 -4.674  -2.417  1.00 11.69 ? 31  PRO A C     1 
ATOM   169  O O     . PRO A 1 40  ? 19.854 -5.155  -1.683  1.00 12.78 ? 31  PRO A O     1 
ATOM   170  C CB    . PRO A 1 40  ? 18.403 -2.617  -1.106  1.00 13.78 ? 31  PRO A CB    1 
ATOM   171  C CG    . PRO A 1 40  ? 18.585 -3.108  0.331   1.00 12.48 ? 31  PRO A CG    1 
ATOM   172  C CD    . PRO A 1 40  ? 17.422 -4.041  0.539   1.00 12.86 ? 31  PRO A CD    1 
ATOM   173  N N     . MET A 1 41  ? 19.028 -4.810  -3.738  1.00 10.40 ? 32  MET A N     1 
ATOM   174  C CA    . MET A 1 41  ? 20.151 -5.520  -4.360  1.00 10.29 ? 32  MET A CA    1 
ATOM   175  C C     . MET A 1 41  ? 20.588 -4.871  -5.668  1.00 13.25 ? 32  MET A C     1 
ATOM   176  O O     . MET A 1 41  ? 19.809 -4.768  -6.594  1.00 12.46 ? 32  MET A O     1 
ATOM   177  C CB    . MET A 1 41  ? 19.932 -7.025  -4.559  1.00 15.10 ? 32  MET A CB    1 
ATOM   178  C CG    . MET A 1 41  ? 19.300 -7.801  -3.379  1.00 14.86 ? 32  MET A CG    1 
ATOM   179  S SD    . MET A 1 41  ? 18.994 -9.513  -3.818  1.00 17.38 ? 32  MET A SD    1 
ATOM   180  C CE    . MET A 1 41  ? 17.277 -9.319  -4.293  1.00 16.48 ? 32  MET A CE    1 
ATOM   181  N N     . THR A 1 42  ? 21.861 -4.506  -5.706  1.00 12.36 ? 33  THR A N     1 
ATOM   182  C CA    . THR A 1 42  ? 22.569 -4.062  -6.905  1.00 13.31 ? 33  THR A CA    1 
ATOM   183  C C     . THR A 1 42  ? 22.610 -5.201  -7.940  1.00 13.70 ? 33  THR A C     1 
ATOM   184  O O     . THR A 1 42  ? 23.072 -6.306  -7.633  1.00 13.14 ? 33  THR A O     1 
ATOM   185  C CB    . THR A 1 42  ? 23.991 -3.685  -6.499  1.00 15.88 ? 33  THR A CB    1 
ATOM   186  O OG1   . THR A 1 42  ? 23.966 -2.572  -5.603  1.00 15.10 ? 33  THR A OG1   1 
ATOM   187  C CG2   . THR A 1 42  ? 24.820 -3.313  -7.725  1.00 14.20 ? 33  THR A CG2   1 
ATOM   188  N N     . ARG A 1 43  ? 22.127 -4.931  -9.155  1.00 13.97 ? 34  ARG A N     1 
ATOM   189  C CA    . ARG A 1 43  ? 22.138 -5.932  -10.226 1.00 11.19 ? 34  ARG A CA    1 
ATOM   190  C C     . ARG A 1 43  ? 22.801 -5.432  -11.502 1.00 14.43 ? 34  ARG A C     1 
ATOM   191  O O     . ARG A 1 43  ? 23.084 -6.252  -12.372 1.00 15.98 ? 34  ARG A O     1 
ATOM   192  C CB    . ARG A 1 43  ? 20.718 -6.408  -10.567 1.00 13.60 ? 34  ARG A CB    1 
ATOM   193  C CG    . ARG A 1 43  ? 19.925 -6.932  -9.345  1.00 11.72 ? 34  ARG A CG    1 
ATOM   194  C CD    . ARG A 1 43  ? 20.627 -8.153  -8.679  1.00 13.18 ? 34  ARG A CD    1 
ATOM   195  N NE    . ARG A 1 43  ? 20.951 -9.209  -9.633  1.00 14.89 ? 34  ARG A NE    1 
ATOM   196  C CZ    . ARG A 1 43  ? 20.045 -10.015 -10.175 1.00 17.20 ? 34  ARG A CZ    1 
ATOM   197  N NH1   . ARG A 1 43  ? 18.764 -9.932  -9.844  1.00 14.18 ? 34  ARG A NH1   1 
ATOM   198  N NH2   . ARG A 1 43  ? 20.424 -10.880 -11.126 1.00 16.60 ? 34  ARG A NH2   1 
ATOM   199  N N     . CYS A 1 44  ? 23.078 -4.128  -11.621 1.00 12.65 ? 35  CYS A N     1 
ATOM   200  C CA    . CYS A 1 44  ? 23.962 -3.583  -12.661 1.00 13.01 ? 35  CYS A CA    1 
ATOM   201  C C     . CYS A 1 44  ? 23.347 -3.690  -14.047 1.00 14.74 ? 35  CYS A C     1 
ATOM   202  O O     . CYS A 1 44  ? 24.077 -3.896  -15.030 1.00 15.31 ? 35  CYS A O     1 
ATOM   203  C CB    . CYS A 1 44  ? 25.341 -4.267  -12.672 1.00 12.29 ? 35  CYS A CB    1 
ATOM   204  S SG    . CYS A 1 44  ? 26.140 -4.226  -11.036 1.00 15.02 ? 35  CYS A SG    1 
ATOM   205  N N     . ARG A 1 45  ? 22.024 -3.552  -14.145 1.00 13.22 ? 36  ARG A N     1 
ATOM   206  C CA    . ARG A 1 45  ? 21.393 -3.478  -15.459 1.00 14.23 ? 36  ARG A CA    1 
ATOM   207  C C     . ARG A 1 45  ? 21.033 -2.066  -15.879 1.00 15.45 ? 36  ARG A C     1 
ATOM   208  O O     . ARG A 1 45  ? 20.487 -1.889  -16.968 1.00 14.79 ? 36  ARG A O     1 
ATOM   209  C CB    . ARG A 1 45  ? 20.148 -4.379  -15.502 1.00 16.10 ? 36  ARG A CB    1 
ATOM   210  C CG    . ARG A 1 45  ? 20.473 -5.807  -16.022 1.00 15.33 ? 36  ARG A CG    1 
ATOM   211  C CD    . ARG A 1 45  ? 21.128 -6.720  -14.910 1.00 15.31 ? 36  ARG A CD    1 
ATOM   212  N NE    . ARG A 1 45  ? 21.190 -8.153  -15.258 1.00 15.26 ? 36  ARG A NE    1 
ATOM   213  C CZ    . ARG A 1 45  ? 21.717 -9.088  -14.459 1.00 18.94 ? 36  ARG A CZ    1 
ATOM   214  N NH1   . ARG A 1 45  ? 22.237 -8.781  -13.287 1.00 14.76 ? 36  ARG A NH1   1 
ATOM   215  N NH2   . ARG A 1 45  ? 21.723 -10.376 -14.845 1.00 14.49 ? 36  ARG A NH2   1 
ATOM   216  N N     . ALA A 1 46  ? 21.292 -1.052  -15.047 1.00 15.27 ? 37  ALA A N     1 
ATOM   217  C CA    . ALA A 1 46  ? 20.879 0.310   -15.375 1.00 14.08 ? 37  ALA A CA    1 
ATOM   218  C C     . ALA A 1 46  ? 22.012 0.950   -16.169 1.00 16.56 ? 37  ALA A C     1 
ATOM   219  O O     . ALA A 1 46  ? 22.806 1.727   -15.653 1.00 14.78 ? 37  ALA A O     1 
ATOM   220  C CB    . ALA A 1 46  ? 20.530 1.094   -14.112 1.00 14.33 ? 37  ALA A CB    1 
ATOM   221  N N     . LEU A 1 47  ? 22.106 0.556   -17.454 1.00 15.02 ? 38  LEU A N     1 
ATOM   222  C CA    . LEU A 1 47  ? 23.224 0.996   -18.293 1.00 17.01 ? 38  LEU A CA    1 
ATOM   223  C C     . LEU A 1 47  ? 23.411 2.511   -18.279 1.00 17.11 ? 38  LEU A C     1 
ATOM   224  O O     . LEU A 1 47  ? 22.450 3.289   -18.391 1.00 16.46 ? 38  LEU A O     1 
ATOM   225  C CB    . LEU A 1 47  ? 23.020 0.507   -19.724 1.00 17.67 ? 38  LEU A CB    1 
ATOM   226  C CG    . LEU A 1 47  ? 22.657 -0.965  -19.820 1.00 16.34 ? 38  LEU A CG    1 
ATOM   227  C CD1   . LEU A 1 47  ? 22.391 -1.435  -21.304 1.00 18.00 ? 38  LEU A CD1   1 
ATOM   228  C CD2   . LEU A 1 47  ? 23.716 -1.823  -19.132 1.00 19.18 ? 38  LEU A CD2   1 
ATOM   229  N N     . ASN A 1 48  ? 24.682 2.932   -18.170 1.00 18.96 ? 39  ASN A N     1 
ATOM   230  C CA    . ASN A 1 48  ? 25.067 4.354   -18.085 1.00 19.97 ? 39  ASN A CA    1 
ATOM   231  C C     . ASN A 1 48  ? 24.379 5.095   -16.939 1.00 17.97 ? 39  ASN A C     1 
ATOM   232  O O     . ASN A 1 48  ? 24.113 6.293   -17.047 1.00 16.56 ? 39  ASN A O     1 
ATOM   233  C CB    . ASN A 1 48  ? 24.755 5.084   -19.389 1.00 19.70 ? 39  ASN A CB    1 
ATOM   234  C CG    . ASN A 1 48  ? 25.734 4.752   -20.477 1.00 31.36 ? 39  ASN A CG    1 
ATOM   235  O OD1   . ASN A 1 48  ? 26.831 4.215   -20.232 1.00 27.34 ? 39  ASN A OD1   1 
ATOM   236  N ND2   . ASN A 1 48  ? 25.327 5.022   -21.695 1.00 29.67 ? 39  ASN A ND2   1 
ATOM   237  N N     . ASN A 1 49  ? 24.075 4.376   -15.856 1.00 17.01 ? 40  ASN A N     1 
ATOM   238  C CA    . ASN A 1 49  ? 23.426 4.879   -14.648 1.00 16.44 ? 40  ASN A CA    1 
ATOM   239  C C     . ASN A 1 49  ? 22.003 5.359   -14.890 1.00 16.95 ? 40  ASN A C     1 
ATOM   240  O O     . ASN A 1 49  ? 21.424 6.026   -14.042 1.00 16.77 ? 40  ASN A O     1 
ATOM   241  C CB    . ASN A 1 49  ? 24.243 5.979   -13.966 1.00 18.95 ? 40  ASN A CB    1 
ATOM   242  C CG    . ASN A 1 49  ? 25.705 5.594   -13.813 1.00 21.48 ? 40  ASN A CG    1 
ATOM   243  O OD1   . ASN A 1 49  ? 26.591 6.301   -14.298 1.00 23.35 ? 40  ASN A OD1   1 
ATOM   244  N ND2   . ASN A 1 49  ? 25.969 4.461   -13.153 1.00 16.14 ? 40  ASN A ND2   1 
ATOM   245  N N     . ILE A 1 50  ? 21.407 4.986   -16.008 1.00 16.49 ? 41  ILE A N     1 
ATOM   246  C CA    . ILE A 1 50  ? 20.021 5.338   -16.321 1.00 16.48 ? 41  ILE A CA    1 
ATOM   247  C C     . ILE A 1 50  ? 19.141 4.115   -16.088 1.00 16.88 ? 41  ILE A C     1 
ATOM   248  O O     . ILE A 1 50  ? 19.440 3.044   -16.651 1.00 18.11 ? 41  ILE A O     1 
ATOM   249  C CB    . ILE A 1 50  ? 19.900 5.839   -17.774 1.00 18.71 ? 41  ILE A CB    1 
ATOM   250  C CG1   . ILE A 1 50  ? 20.930 6.938   -18.065 1.00 18.36 ? 41  ILE A CG1   1 
ATOM   251  C CG2   . ILE A 1 50  ? 18.454 6.233   -18.126 1.00 20.30 ? 41  ILE A CG2   1 
ATOM   252  C CD1   . ILE A 1 50  ? 20.954 7.334   -19.530 1.00 28.99 ? 41  ILE A CD1   1 
ATOM   253  N N     . PRO A 1 51  ? 18.084 4.218   -15.263 1.00 16.73 ? 42  PRO A N     1 
ATOM   254  C CA    . PRO A 1 51  ? 17.120 3.127   -15.139 1.00 16.25 ? 42  PRO A CA    1 
ATOM   255  C C     . PRO A 1 51  ? 16.592 2.699   -16.497 1.00 21.14 ? 42  PRO A C     1 
ATOM   256  O O     . PRO A 1 51  ? 16.299 3.528   -17.376 1.00 19.71 ? 42  PRO A O     1 
ATOM   257  C CB    . PRO A 1 51  ? 16.022 3.727   -14.254 1.00 17.89 ? 42  PRO A CB    1 
ATOM   258  C CG    . PRO A 1 51  ? 16.706 4.793   -13.451 1.00 16.73 ? 42  PRO A CG    1 
ATOM   259  C CD    . PRO A 1 51  ? 17.780 5.339   -14.347 1.00 15.25 ? 42  PRO A CD    1 
ATOM   260  N N     . GLN A 1 52  ? 16.542 1.384   -16.691 1.00 19.82 ? 43  GLN A N     1 
ATOM   261  C CA    . GLN A 1 52  ? 16.149 0.804   -17.976 1.00 19.49 ? 43  GLN A CA    1 
ATOM   262  C C     . GLN A 1 52  ? 14.812 0.079   -17.857 1.00 21.43 ? 43  GLN A C     1 
ATOM   263  O O     . GLN A 1 52  ? 14.395 -0.306  -16.772 1.00 17.99 ? 43  GLN A O     1 
ATOM   264  C CB    . GLN A 1 52  ? 17.229 -0.172  -18.462 1.00 21.22 ? 43  GLN A CB    1 
ATOM   265  C CG    . GLN A 1 52  ? 18.610 0.485   -18.504 1.00 19.14 ? 43  GLN A CG    1 
ATOM   266  C CD    . GLN A 1 52  ? 18.809 1.350   -19.724 1.00 23.73 ? 43  GLN A CD    1 
ATOM   267  O OE1   . GLN A 1 52  ? 18.404 0.964   -20.828 1.00 28.64 ? 43  GLN A OE1   1 
ATOM   268  N NE2   . GLN A 1 52  ? 19.400 2.532   -19.544 1.00 23.19 ? 43  GLN A NE2   1 
ATOM   269  N N     . ALA A 1 53  ? 14.160 -0.165  -19.004 1.00 22.90 ? 44  ALA A N     1 
ATOM   270  C CA    . ALA A 1 53  ? 12.915 -0.945  -18.982 1.00 20.01 ? 44  ALA A CA    1 
ATOM   271  C C     . ALA A 1 53  ? 13.096 -2.306  -18.331 1.00 20.57 ? 44  ALA A C     1 
ATOM   272  O O     . ALA A 1 53  ? 12.145 -2.839  -17.759 1.00 20.73 ? 44  ALA A O     1 
ATOM   273  C CB    . ALA A 1 53  ? 12.366 -1.145  -20.405 1.00 23.09 ? 44  ALA A CB    1 
ATOM   274  N N     . ALA A 1 54  ? 14.280 -2.910  -18.439 1.00 20.07 ? 45  ALA A N     1 
ATOM   275  C CA    . ALA A 1 54  ? 14.469 -4.207  -17.797 1.00 19.92 ? 45  ALA A CA    1 
ATOM   276  C C     . ALA A 1 54  ? 14.257 -4.090  -16.295 1.00 17.76 ? 45  ALA A C     1 
ATOM   277  O O     . ALA A 1 54  ? 13.694 -4.998  -15.680 1.00 19.13 ? 45  ALA A O     1 
ATOM   278  C CB    . ALA A 1 54  ? 15.853 -4.777  -18.114 1.00 21.80 ? 45  ALA A CB    1 
ATOM   279  N N     . LEU A 1 55  ? 14.665 -2.967  -15.681 1.00 17.45 ? 46  LEU A N     1 
ATOM   280  C CA    . LEU A 1 55  ? 14.396 -2.826  -14.241 1.00 16.21 ? 46  LEU A CA    1 
ATOM   281  C C     . LEU A 1 55  ? 12.902 -2.845  -13.988 1.00 18.37 ? 46  LEU A C     1 
ATOM   282  O O     . LEU A 1 55  ? 12.432 -3.452  -13.024 1.00 17.25 ? 46  LEU A O     1 
ATOM   283  C CB    . LEU A 1 55  ? 15.001 -1.545  -13.645 1.00 14.26 ? 46  LEU A CB    1 
ATOM   284  C CG    . LEU A 1 55  ? 16.477 -1.533  -13.259 1.00 13.21 ? 46  LEU A CG    1 
ATOM   285  C CD1   . LEU A 1 55  ? 17.365 -1.744  -14.493 1.00 15.80 ? 46  LEU A CD1   1 
ATOM   286  C CD2   . LEU A 1 55  ? 16.813 -0.224  -12.569 1.00 17.53 ? 46  LEU A CD2   1 
ATOM   287  N N     . GLY A 1 56  ? 12.134 -2.174  -14.846 1.00 18.94 ? 47  GLY A N     1 
ATOM   288  C CA    . GLY A 1 56  ? 10.694 -2.161  -14.652 1.00 21.08 ? 47  GLY A CA    1 
ATOM   289  C C     . GLY A 1 56  ? 10.109 -3.560  -14.714 1.00 20.26 ? 47  GLY A C     1 
ATOM   290  O O     . GLY A 1 56  ? 9.249  -3.916  -13.916 1.00 18.84 ? 47  GLY A O     1 
ATOM   291  N N     . GLU A 1 57  ? 10.621 -4.395  -15.612 1.00 18.96 ? 48  GLU A N     1 
ATOM   292  C CA    . GLU A 1 57  ? 10.096 -5.751  -15.677 1.00 19.70 ? 48  GLU A CA    1 
ATOM   293  C C     . GLU A 1 57  ? 10.469 -6.540  -14.430 1.00 17.37 ? 48  GLU A C     1 
ATOM   294  O O     . GLU A 1 57  ? 9.644  -7.276  -13.878 1.00 17.86 ? 48  GLU A O     1 
ATOM   295  C CB    . GLU A 1 57  ? 10.615 -6.454  -16.921 1.00 22.63 ? 48  GLU A CB    1 
ATOM   296  C CG    . GLU A 1 57  ? 10.190 -7.885  -16.967 1.00 24.27 ? 48  GLU A CG    1 
ATOM   297  C CD    . GLU A 1 57  ? 10.409 -8.513  -18.333 1.00 43.48 ? 48  GLU A CD    1 
ATOM   298  O OE1   . GLU A 1 57  ? 10.993 -7.824  -19.209 1.00 44.55 ? 48  GLU A OE1   1 
ATOM   299  O OE2   . GLU A 1 57  ? 10.002 -9.691  -18.518 1.00 45.03 ? 48  GLU A OE2   1 
ATOM   300  N N     . TYR A 1 58  ? 11.714 -6.383  -13.985 1.00 17.04 ? 49  TYR A N     1 
ATOM   301  C CA    . TYR A 1 58  ? 12.230 -7.094  -12.819 1.00 15.29 ? 49  TYR A CA    1 
ATOM   302  C C     . TYR A 1 58  ? 11.451 -6.731  -11.560 1.00 15.94 ? 49  TYR A C     1 
ATOM   303  O O     . TYR A 1 58  ? 11.010 -7.613  -10.828 1.00 15.04 ? 49  TYR A O     1 
ATOM   304  C CB    . TYR A 1 58  ? 13.705 -6.747  -12.651 1.00 15.83 ? 49  TYR A CB    1 
ATOM   305  C CG    . TYR A 1 58  ? 14.391 -7.180  -11.341 1.00 14.15 ? 49  TYR A CG    1 
ATOM   306  C CD1   . TYR A 1 58  ? 14.930 -8.464  -11.207 1.00 16.59 ? 49  TYR A CD1   1 
ATOM   307  C CD2   . TYR A 1 58  ? 14.642 -6.263  -10.324 1.00 16.77 ? 49  TYR A CD2   1 
ATOM   308  C CE1   . TYR A 1 58  ? 15.630 -8.837  -10.066 1.00 14.83 ? 49  TYR A CE1   1 
ATOM   309  C CE2   . TYR A 1 58  ? 15.356 -6.632  -9.159  1.00 13.78 ? 49  TYR A CE2   1 
ATOM   310  C CZ    . TYR A 1 58  ? 15.840 -7.930  -9.062  1.00 14.75 ? 49  TYR A CZ    1 
ATOM   311  O OH    . TYR A 1 58  ? 16.556 -8.341  -7.965  1.00 18.91 ? 49  TYR A OH    1 
ATOM   312  N N     . TYR A 1 59  ? 11.259 -5.428  -11.296 1.00 15.74 ? 50  TYR A N     1 
ATOM   313  C CA    . TYR A 1 59  ? 10.515 -5.062  -10.084 1.00 15.58 ? 50  TYR A CA    1 
ATOM   314  C C     . TYR A 1 59  ? 9.039  -5.442  -10.206 1.00 15.63 ? 50  TYR A C     1 
ATOM   315  O O     . TYR A 1 59  ? 8.413  -5.856  -9.220  1.00 17.21 ? 50  TYR A O     1 
ATOM   316  C CB    . TYR A 1 59  ? 10.672 -3.571  -9.764  1.00 17.17 ? 50  TYR A CB    1 
ATOM   317  C CG    . TYR A 1 59  ? 12.044 -3.271  -9.221  1.00 16.25 ? 50  TYR A CG    1 
ATOM   318  C CD1   . TYR A 1 59  ? 12.466 -3.776  -7.975  1.00 16.65 ? 50  TYR A CD1   1 
ATOM   319  C CD2   . TYR A 1 59  ? 12.932 -2.540  -9.955  1.00 16.27 ? 50  TYR A CD2   1 
ATOM   320  C CE1   . TYR A 1 59  ? 13.740 -3.520  -7.505  1.00 16.43 ? 50  TYR A CE1   1 
ATOM   321  C CE2   . TYR A 1 59  ? 14.208 -2.271  -9.496  1.00 15.05 ? 50  TYR A CE2   1 
ATOM   322  C CZ    . TYR A 1 59  ? 14.601 -2.744  -8.285  1.00 14.49 ? 50  TYR A CZ    1 
ATOM   323  O OH    . TYR A 1 59  ? 15.874 -2.439  -7.906  1.00 14.39 ? 50  TYR A OH    1 
ATOM   324  N N     . GLU A 1 60  ? 8.475  -5.328  -11.410 1.00 17.79 ? 51  GLU A N     1 
ATOM   325  C CA    . GLU A 1 60  ? 7.080  -5.702  -11.596 1.00 15.60 ? 51  GLU A CA    1 
ATOM   326  C C     . GLU A 1 60  ? 6.887  -7.184  -11.315 1.00 16.60 ? 51  GLU A C     1 
ATOM   327  O O     . GLU A 1 60  ? 5.880  -7.586  -10.738 1.00 18.20 ? 51  GLU A O     1 
ATOM   328  C CB    . GLU A 1 60  ? 6.634  -5.363  -13.018 1.00 18.85 ? 51  GLU A CB    1 
ATOM   329  C CG    . GLU A 1 60  ? 5.148  -5.593  -13.240 1.00 18.66 ? 51  GLU A CG    1 
ATOM   330  C CD    . GLU A 1 60  ? 4.745  -5.379  -14.713 1.00 29.76 ? 51  GLU A CD    1 
ATOM   331  O OE1   . GLU A 1 60  ? 5.529  -5.761  -15.627 1.00 35.16 ? 51  GLU A OE1   1 
ATOM   332  O OE2   . GLU A 1 60  ? 3.685  -4.762  -14.951 1.00 31.33 ? 51  GLU A OE2   1 
ATOM   333  N N     . GLN A 1 61  ? 7.853  -8.018  -11.716 1.00 16.96 ? 52  GLN A N     1 
ATOM   334  C CA    . GLN A 1 61  ? 7.736  -9.452  -11.464 1.00 16.32 ? 52  GLN A CA    1 
ATOM   335  C C     . GLN A 1 61  ? 7.613  -9.736  -9.977  1.00 17.16 ? 52  GLN A C     1 
ATOM   336  O O     . GLN A 1 61  ? 6.952  -10.695 -9.554  1.00 16.43 ? 52  GLN A O     1 
ATOM   337  C CB    . GLN A 1 61  ? 8.971  -10.150 -12.001 1.00 16.36 ? 52  GLN A CB    1 
ATOM   338  C CG    . GLN A 1 61  ? 8.938  -10.306 -13.522 1.00 18.61 ? 52  GLN A CG    1 
ATOM   339  C CD    . GLN A 1 61  ? 10.087 -11.126 -14.038 1.00 17.21 ? 52  GLN A CD    1 
ATOM   340  O OE1   . GLN A 1 61  ? 11.085 -11.303 -13.345 1.00 19.71 ? 52  GLN A OE1   1 
ATOM   341  N NE2   . GLN A 1 61  ? 9.939  -11.668 -15.263 1.00 19.25 ? 52  GLN A NE2   1 
ATOM   342  N N     . ARG A 1 62  ? 8.329  -8.970  -9.188  1.00 15.93 ? 53  ARG A N     1 
ATOM   343  C CA    . ARG A 1 62  ? 8.456  -9.240  -7.765  1.00 17.98 ? 53  ARG A CA    1 
ATOM   344  C C     . ARG A 1 62  ? 7.389  -8.552  -6.947  1.00 16.35 ? 53  ARG A C     1 
ATOM   345  O O     . ARG A 1 62  ? 7.163  -8.930  -5.782  1.00 16.85 ? 53  ARG A O     1 
ATOM   346  C CB    . ARG A 1 62  ? 9.865  -8.834  -7.321  1.00 16.70 ? 53  ARG A CB    1 
ATOM   347  C CG    . ARG A 1 62  ? 10.861 -9.950  -7.695  1.00 13.33 ? 53  ARG A CG    1 
ATOM   348  C CD    . ARG A 1 62  ? 12.317 -9.498  -8.033  1.00 14.56 ? 53  ARG A CD    1 
ATOM   349  N NE    . ARG A 1 62  ? 13.027 -10.665 -8.564  1.00 17.02 ? 53  ARG A NE    1 
ATOM   350  C CZ    . ARG A 1 62  ? 12.915 -11.093 -9.816  1.00 20.13 ? 53  ARG A CZ    1 
ATOM   351  N NH1   . ARG A 1 62  ? 12.256 -10.389 -10.734 1.00 15.53 ? 53  ARG A NH1   1 
ATOM   352  N NH2   . ARG A 1 62  ? 13.459 -12.264 -10.157 1.00 16.40 ? 53  ARG A NH2   1 
ATOM   353  N N     . ALA A 1 63  ? 6.727  -7.556  -7.537  1.00 16.68 ? 54  ALA A N     1 
ATOM   354  C CA    . ALA A 1 63  ? 5.704  -6.769  -6.854  1.00 16.52 ? 54  ALA A CA    1 
ATOM   355  C C     . ALA A 1 63  ? 4.463  -7.584  -6.520  1.00 15.63 ? 54  ALA A C     1 
ATOM   356  O O     . ALA A 1 63  ? 4.010  -8.427  -7.297  1.00 17.98 ? 54  ALA A O     1 
ATOM   357  C CB    . ALA A 1 63  ? 5.294  -5.588  -7.745  1.00 16.41 ? 54  ALA A CB    1 
ATOM   358  N N     . THR A 1 64  ? 3.882  -7.293  -5.360  1.00 14.79 ? 55  THR A N     1 
ATOM   359  C CA    . THR A 1 64  ? 2.630  -7.903  -4.955  1.00 15.42 ? 55  THR A CA    1 
ATOM   360  C C     . THR A 1 64  ? 1.765  -6.809  -4.352  1.00 19.26 ? 55  THR A C     1 
ATOM   361  O O     . THR A 1 64  ? 2.257  -5.740  -3.963  1.00 18.36 ? 55  THR A O     1 
ATOM   362  C CB    . THR A 1 64  ? 2.836  -9.048  -3.938  1.00 17.70 ? 55  THR A CB    1 
ATOM   363  O OG1   . THR A 1 64  ? 3.539  -8.547  -2.780  1.00 17.73 ? 55  THR A OG1   1 
ATOM   364  C CG2   . THR A 1 64  ? 3.583  -10.238 -4.552  1.00 19.59 ? 55  THR A CG2   1 
ATOM   365  N N     . ALA A 1 65  ? 0.463  -7.074  -4.304  1.00 17.34 ? 56  ALA A N     1 
ATOM   366  C CA    . ALA A 1 65  ? -0.465 -6.110  -3.749  1.00 20.78 ? 56  ALA A CA    1 
ATOM   367  C C     . ALA A 1 65  ? -0.220 -5.987  -2.247  1.00 18.62 ? 56  ALA A C     1 
ATOM   368  O O     . ALA A 1 65  ? -0.367 -6.950  -1.489  1.00 21.48 ? 56  ALA A O     1 
ATOM   369  C CB    . ALA A 1 65  ? -1.901 -6.535  -4.034  1.00 22.02 ? 56  ALA A CB    1 
ATOM   370  N N     . GLY A 1 66  ? 0.168  -4.802  -1.828  1.00 18.58 ? 57  GLY A N     1 
ATOM   371  C CA    . GLY A 1 66  ? 0.446  -4.566  -0.413  1.00 17.73 ? 57  GLY A CA    1 
ATOM   372  C C     . GLY A 1 66  ? 1.817  -4.991  0.026   1.00 19.31 ? 57  GLY A C     1 
ATOM   373  O O     . GLY A 1 66  ? 2.102  -4.947  1.231   1.00 19.68 ? 57  GLY A O     1 
ATOM   374  N N     . GLY A 1 67  ? 2.662  -5.433  -0.903  1.00 15.99 ? 58  GLY A N     1 
ATOM   375  C CA    . GLY A 1 67  ? 4.004  -5.848  -0.564  1.00 13.93 ? 58  GLY A CA    1 
ATOM   376  C C     . GLY A 1 67  ? 5.000  -4.708  -0.740  1.00 16.35 ? 58  GLY A C     1 
ATOM   377  O O     . GLY A 1 67  ? 4.805  -3.794  -1.561  1.00 15.62 ? 58  GLY A O     1 
ATOM   378  N N     . PHE A 1 68  ? 6.055  -4.744  0.080   1.00 18.06 ? 59  PHE A N     1 
ATOM   379  C CA    . PHE A 1 68  ? 7.035  -3.673  0.166   1.00 16.57 ? 59  PHE A CA    1 
ATOM   380  C C     . PHE A 1 68  ? 8.303  -4.059  -0.604  1.00 16.55 ? 59  PHE A C     1 
ATOM   381  O O     . PHE A 1 68  ? 8.853  -5.149  -0.393  1.00 14.49 ? 59  PHE A O     1 
ATOM   382  C CB    . PHE A 1 68  ? 7.338  -3.384  1.629   1.00 17.38 ? 59  PHE A CB    1 
ATOM   383  C CG    . PHE A 1 68  ? 8.359  -2.281  1.852   1.00 14.17 ? 59  PHE A CG    1 
ATOM   384  C CD1   . PHE A 1 68  ? 8.445  -1.198  1.001   1.00 16.78 ? 59  PHE A CD1   1 
ATOM   385  C CD2   . PHE A 1 68  ? 9.230  -2.339  2.947   1.00 16.70 ? 59  PHE A CD2   1 
ATOM   386  C CE1   . PHE A 1 68  ? 9.417  -0.194  1.189   1.00 13.27 ? 59  PHE A CE1   1 
ATOM   387  C CE2   . PHE A 1 68  ? 10.188 -1.298  3.172   1.00 12.67 ? 59  PHE A CE2   1 
ATOM   388  C CZ    . PHE A 1 68  ? 10.281 -0.235  2.278   1.00 15.21 ? 59  PHE A CZ    1 
ATOM   389  N N     . LEU A 1 69  ? 8.760  -3.167  -1.486  1.00 13.55 ? 60  LEU A N     1 
ATOM   390  C CA    . LEU A 1 69  ? 9.995  -3.377  -2.240  1.00 12.43 ? 60  LEU A CA    1 
ATOM   391  C C     . LEU A 1 69  ? 11.012 -2.285  -1.948  1.00 11.72 ? 60  LEU A C     1 
ATOM   392  O O     . LEU A 1 69  ? 10.667 -1.099  -1.836  1.00 14.10 ? 60  LEU A O     1 
ATOM   393  C CB    . LEU A 1 69  ? 9.727  -3.404  -3.718  1.00 13.19 ? 60  LEU A CB    1 
ATOM   394  C CG    . LEU A 1 69  ? 8.608  -4.296  -4.272  1.00 13.36 ? 60  LEU A CG    1 
ATOM   395  C CD1   . LEU A 1 69  ? 8.384  -3.998  -5.763  1.00 19.71 ? 60  LEU A CD1   1 
ATOM   396  C CD2   . LEU A 1 69  ? 8.892  -5.783  -4.075  1.00 18.46 ? 60  LEU A CD2   1 
ATOM   397  N N     . ILE A 1 70  ? 12.271 -2.698  -1.824  1.00 13.77 ? 61  ILE A N     1 
ATOM   398  C CA    . ILE A 1 70  ? 13.353 -1.685  -1.685  1.00 12.71 ? 61  ILE A CA    1 
ATOM   399  C C     . ILE A 1 70  ? 14.252 -1.839  -2.911  1.00 13.69 ? 61  ILE A C     1 
ATOM   400  O O     . ILE A 1 70  ? 14.618 -2.962  -3.241  1.00 13.80 ? 61  ILE A O     1 
ATOM   401  C CB    . ILE A 1 70  ? 14.149 -1.826  -0.376  1.00 11.33 ? 61  ILE A CB    1 
ATOM   402  C CG1   . ILE A 1 70  ? 13.226 -1.892  0.842   1.00 15.93 ? 61  ILE A CG1   1 
ATOM   403  C CG2   . ILE A 1 70  ? 15.164 -0.705  -0.240  1.00 12.96 ? 61  ILE A CG2   1 
ATOM   404  C CD1   . ILE A 1 70  ? 13.925 -2.314  2.106   1.00 12.70 ? 61  ILE A CD1   1 
ATOM   405  N N     . THR A 1 71  ? 14.572 -0.729  -3.556  1.00 11.96 ? 62  THR A N     1 
ATOM   406  C CA    . THR A 1 71  ? 15.343 -0.843  -4.804  1.00 12.17 ? 62  THR A CA    1 
ATOM   407  C C     . THR A 1 71  ? 16.821 -1.096  -4.555  1.00 13.04 ? 62  THR A C     1 
ATOM   408  O O     . THR A 1 71  ? 17.290 -0.874  -3.461  1.00 14.53 ? 62  THR A O     1 
ATOM   409  C CB    . THR A 1 71  ? 15.397 0.470   -5.608  1.00 13.57 ? 62  THR A CB    1 
ATOM   410  O OG1   . THR A 1 71  ? 16.142 1.453   -4.892  1.00 14.27 ? 62  THR A OG1   1 
ATOM   411  C CG2   . THR A 1 71  ? 14.027 0.988   -5.980  1.00 15.27 ? 62  THR A CG2   1 
ATOM   412  N N     . GLU A 1 72  ? 17.496 -1.496  -5.608  1.00 14.73 ? 63  GLU A N     1 
ATOM   413  C CA    . GLU A 1 72  ? 18.963 -1.561  -5.556  1.00 13.18 ? 63  GLU A CA    1 
ATOM   414  C C     . GLU A 1 72  ? 19.505 -0.200  -5.132  1.00 15.35 ? 63  GLU A C     1 
ATOM   415  O O     . GLU A 1 72  ? 18.816 0.812   -5.305  1.00 11.78 ? 63  GLU A O     1 
ATOM   416  C CB    . GLU A 1 72  ? 19.456 -1.826  -6.971  1.00 12.55 ? 63  GLU A CB    1 
ATOM   417  C CG    . GLU A 1 72  ? 18.973 -0.817  -7.996  1.00 14.75 ? 63  GLU A CG    1 
ATOM   418  C CD    . GLU A 1 72  ? 18.717 -1.367  -9.391  1.00 19.06 ? 63  GLU A CD    1 
ATOM   419  O OE1   . GLU A 1 72  ? 19.649 -1.385  -10.207 1.00 16.28 ? 63  GLU A OE1   1 
ATOM   420  O OE2   . GLU A 1 72  ? 17.590 -1.779  -9.652  1.00 19.55 ? 63  GLU A OE2   1 
ATOM   421  N N     . GLY A 1 73  ? 20.706 -0.205  -4.584  1.00 11.46 ? 64  GLY A N     1 
ATOM   422  C CA    . GLY A 1 73  ? 21.356 1.061   -4.257  1.00 11.85 ? 64  GLY A CA    1 
ATOM   423  C C     . GLY A 1 73  ? 21.362 1.993   -5.456  1.00 12.31 ? 64  GLY A C     1 
ATOM   424  O O     . GLY A 1 73  ? 21.659 1.533   -6.560  1.00 12.05 ? 64  GLY A O     1 
ATOM   425  N N     . THR A 1 74  ? 21.083 3.264   -5.199  1.00 13.11 ? 65  THR A N     1 
ATOM   426  C CA    . THR A 1 74  ? 20.940 4.258   -6.275  1.00 11.02 ? 65  THR A CA    1 
ATOM   427  C C     . THR A 1 74  ? 21.882 5.432   -5.974  1.00 13.33 ? 65  THR A C     1 
ATOM   428  O O     . THR A 1 74  ? 21.887 5.921   -4.858  1.00 14.60 ? 65  THR A O     1 
ATOM   429  C CB    . THR A 1 74  ? 19.452 4.613   -6.427  1.00 14.93 ? 65  THR A CB    1 
ATOM   430  O OG1   . THR A 1 74  ? 18.716 3.432   -6.737  1.00 16.48 ? 65  THR A OG1   1 
ATOM   431  C CG2   . THR A 1 74  ? 19.192 5.670   -7.476  1.00 13.79 ? 65  THR A CG2   1 
ATOM   432  N N     . MET A 1 75  ? 22.595 5.854   -6.908  1.00 13.64 ? 66  MET A N     1 
ATOM   433  C CA    . MET A 1 75  ? 23.548 6.969   -6.852  1.00 12.44 ? 66  MET A CA    1 
ATOM   434  C C     . MET A 1 75  ? 22.909 8.288   -6.394  1.00 12.88 ? 66  MET A C     1 
ATOM   435  O O     . MET A 1 75  ? 21.802 8.575   -6.822  1.00 14.48 ? 66  MET A O     1 
ATOM   436  C CB    . MET A 1 75  ? 24.204 7.165   -8.219  1.00 14.71 ? 66  MET A CB    1 
ATOM   437  C CG    . MET A 1 75  ? 25.129 6.032   -8.634  1.00 13.79 ? 66  MET A CG    1 
ATOM   438  S SD    . MET A 1 75  ? 25.813 6.261   -10.285 1.00 16.88 ? 66  MET A SD    1 
ATOM   439  C CE    . MET A 1 75  ? 26.971 7.596   -9.990  1.00 16.25 ? 66  MET A CE    1 
ATOM   440  N N     . ILE A 1 76  ? 23.643 9.010   -5.565  1.00 15.08 ? 67  ILE A N     1 
ATOM   441  C CA    . ILE A 1 76  ? 23.147 10.344  -5.119  1.00 16.53 ? 67  ILE A CA    1 
ATOM   442  C C     . ILE A 1 76  ? 23.971 11.439  -5.793  1.00 18.78 ? 67  ILE A C     1 
ATOM   443  O O     . ILE A 1 76  ? 23.623 12.601  -5.620  1.00 19.00 ? 67  ILE A O     1 
ATOM   444  C CB    . ILE A 1 76  ? 23.256 10.496  -3.594  1.00 15.33 ? 67  ILE A CB    1 
ATOM   445  C CG1   . ILE A 1 76  ? 24.715 10.443  -3.131  1.00 14.93 ? 67  ILE A CG1   1 
ATOM   446  C CG2   . ILE A 1 76  ? 22.397 9.462   -2.885  1.00 14.35 ? 67  ILE A CG2   1 
ATOM   447  C CD1   . ILE A 1 76  ? 24.934 10.942  -1.729  1.00 17.88 ? 67  ILE A CD1   1 
ATOM   448  N N     . SER A 1 77  ? 25.027 11.053  -6.509  1.00 16.36 ? 68  SER A N     1 
ATOM   449  C CA    . SER A 1 77  ? 25.956 12.036  -7.102  1.00 17.84 ? 68  SER A CA    1 
ATOM   450  C C     . SER A 1 77  ? 26.843 11.341  -8.134  1.00 17.87 ? 68  SER A C     1 
ATOM   451  O O     . SER A 1 77  ? 26.972 10.132  -8.087  1.00 16.70 ? 68  SER A O     1 
ATOM   452  C CB    . SER A 1 77  ? 26.840 12.634  -6.059  1.00 19.98 ? 68  SER A CB    1 
ATOM   453  O OG    . SER A 1 77  ? 27.906 11.771  -5.738  1.00 20.11 ? 68  SER A OG    1 
ATOM   454  N N     . PRO A 1 78  ? 27.469 12.093  -9.053  1.00 17.06 ? 69  PRO A N     1 
ATOM   455  C CA    . PRO A 1 78  ? 28.411 11.489  -9.984  1.00 18.87 ? 69  PRO A CA    1 
ATOM   456  C C     . PRO A 1 78  ? 29.592 10.783  -9.291  1.00 20.40 ? 69  PRO A C     1 
ATOM   457  O O     . PRO A 1 78  ? 30.226 9.989   -9.925  1.00 16.54 ? 69  PRO A O     1 
ATOM   458  C CB    . PRO A 1 78  ? 28.909 12.709  -10.777 1.00 20.57 ? 69  PRO A CB    1 
ATOM   459  C CG    . PRO A 1 78  ? 27.763 13.677  -10.716 1.00 22.30 ? 69  PRO A CG    1 
ATOM   460  C CD    . PRO A 1 78  ? 27.231 13.513  -9.310  1.00 21.04 ? 69  PRO A CD    1 
ATOM   461  N N     . THR A 1 79  ? 29.863 11.118  -8.026  1.00 16.54 ? 70  THR A N     1 
ATOM   462  C CA    . THR A 1 79  ? 31.029 10.517  -7.392  1.00 17.27 ? 70  THR A CA    1 
ATOM   463  C C     . THR A 1 79  ? 30.655 9.361   -6.466  1.00 16.25 ? 70  THR A C     1 
ATOM   464  O O     . THR A 1 79  ? 31.508 8.853   -5.726  1.00 17.76 ? 70  THR A O     1 
ATOM   465  C CB    . THR A 1 79  ? 31.804 11.585  -6.620  1.00 18.48 ? 70  THR A CB    1 
ATOM   466  O OG1   . THR A 1 79  ? 30.884 12.323  -5.796  1.00 23.13 ? 70  THR A OG1   1 
ATOM   467  C CG2   . THR A 1 79  ? 32.530 12.532  -7.597  1.00 27.77 ? 70  THR A CG2   1 
ATOM   468  N N     . SER A 1 80  ? 29.400 8.942   -6.479  1.00 17.40 ? 71  SER A N     1 
ATOM   469  C CA    . SER A 1 80  ? 28.913 8.051   -5.437  1.00 16.22 ? 71  SER A CA    1 
ATOM   470  C C     . SER A 1 80  ? 28.946 6.569   -5.820  1.00 15.95 ? 71  SER A C     1 
ATOM   471  O O     . SER A 1 80  ? 28.521 5.738   -5.018  1.00 16.11 ? 71  SER A O     1 
ATOM   472  C CB    . SER A 1 80  ? 27.489 8.445   -5.052  1.00 15.86 ? 71  SER A CB    1 
ATOM   473  O OG    . SER A 1 80  ? 26.659 8.260   -6.168  1.00 21.53 ? 71  SER A OG    1 
ATOM   474  N N     . ALA A 1 81  ? 29.464 6.217   -6.999  1.00 15.19 ? 72  ALA A N     1 
ATOM   475  C CA    . ALA A 1 81  ? 29.355 4.859   -7.482  1.00 15.06 ? 72  ALA A CA    1 
ATOM   476  C C     . ALA A 1 81  ? 30.669 4.098   -7.365  1.00 14.22 ? 72  ALA A C     1 
ATOM   477  O O     . ALA A 1 81  ? 31.765 4.669   -7.488  1.00 15.29 ? 72  ALA A O     1 
ATOM   478  C CB    . ALA A 1 81  ? 28.894 4.855   -8.936  1.00 16.19 ? 72  ALA A CB    1 
ATOM   479  N N     . GLY A 1 82  ? 30.524 2.777   -7.177  1.00 13.98 ? 73  GLY A N     1 
ATOM   480  C CA    . GLY A 1 82  ? 31.637 1.853   -7.144  1.00 14.84 ? 73  GLY A CA    1 
ATOM   481  C C     . GLY A 1 82  ? 31.307 0.518   -7.788  1.00 16.14 ? 73  GLY A C     1 
ATOM   482  O O     . GLY A 1 82  ? 31.989 -0.471  -7.521  1.00 15.72 ? 73  GLY A O     1 
ATOM   483  N N     . PHE A 1 83  ? 30.239 0.466   -8.580  1.00 14.82 ? 74  PHE A N     1 
ATOM   484  C CA    . PHE A 1 83  ? 29.812 -0.685  -9.369  1.00 11.73 ? 74  PHE A CA    1 
ATOM   485  C C     . PHE A 1 83  ? 29.450 -0.178  -10.756 1.00 13.20 ? 74  PHE A C     1 
ATOM   486  O O     . PHE A 1 83  ? 29.115 0.998   -10.916 1.00 15.47 ? 74  PHE A O     1 
ATOM   487  C CB    . PHE A 1 83  ? 28.576 -1.359  -8.761  1.00 14.88 ? 74  PHE A CB    1 
ATOM   488  C CG    . PHE A 1 83  ? 28.885 -2.398  -7.687  1.00 11.93 ? 74  PHE A CG    1 
ATOM   489  C CD1   . PHE A 1 83  ? 29.272 -2.013  -6.399  1.00 14.44 ? 74  PHE A CD1   1 
ATOM   490  C CD2   . PHE A 1 83  ? 28.783 -3.753  -7.977  1.00 12.79 ? 74  PHE A CD2   1 
ATOM   491  C CE1   . PHE A 1 83  ? 29.553 -2.992  -5.412  1.00 15.28 ? 74  PHE A CE1   1 
ATOM   492  C CE2   . PHE A 1 83  ? 29.058 -4.716  -7.006  1.00 16.17 ? 74  PHE A CE2   1 
ATOM   493  C CZ    . PHE A 1 83  ? 29.429 -4.348  -5.750  1.00 13.59 ? 74  PHE A CZ    1 
ATOM   494  N N     . PRO A 1 84  ? 29.463 -1.028  -11.765 1.00 13.81 ? 75  PRO A N     1 
ATOM   495  C CA    . PRO A 1 84  ? 29.103 -0.557  -13.110 1.00 14.86 ? 75  PRO A CA    1 
ATOM   496  C C     . PRO A 1 84  ? 27.588 -0.565  -13.283 1.00 15.13 ? 75  PRO A C     1 
ATOM   497  O O     . PRO A 1 84  ? 26.907 -1.434  -12.743 1.00 14.28 ? 75  PRO A O     1 
ATOM   498  C CB    . PRO A 1 84  ? 29.770 -1.595  -14.022 1.00 15.28 ? 75  PRO A CB    1 
ATOM   499  C CG    . PRO A 1 84  ? 29.703 -2.897  -13.185 1.00 16.95 ? 75  PRO A CG    1 
ATOM   500  C CD    . PRO A 1 84  ? 29.843 -2.459  -11.740 1.00 16.38 ? 75  PRO A CD    1 
ATOM   501  N N     . HIS A 1 85  ? 27.076 0.413   -14.049 1.00 17.33 ? 76  HIS A N     1 
ATOM   502  C CA    . HIS A 1 85  ? 25.692 0.416   -14.544 1.00 12.70 ? 76  HIS A CA    1 
ATOM   503  C C     . HIS A 1 85  ? 24.691 0.281   -13.394 1.00 16.56 ? 76  HIS A C     1 
ATOM   504  O O     . HIS A 1 85  ? 23.703 -0.450  -13.484 1.00 15.60 ? 76  HIS A O     1 
ATOM   505  C CB    . HIS A 1 85  ? 25.487 -0.699  -15.587 1.00 16.60 ? 76  HIS A CB    1 
ATOM   506  C CG    . HIS A 1 85  ? 26.502 -0.647  -16.675 1.00 18.02 ? 76  HIS A CG    1 
ATOM   507  N ND1   . HIS A 1 85  ? 26.646 0.463   -17.473 1.00 19.96 ? 76  HIS A ND1   1 
ATOM   508  C CD2   . HIS A 1 85  ? 27.488 -1.503  -17.026 1.00 19.26 ? 76  HIS A CD2   1 
ATOM   509  C CE1   . HIS A 1 85  ? 27.667 0.282   -18.294 1.00 21.31 ? 76  HIS A CE1   1 
ATOM   510  N NE2   . HIS A 1 85  ? 28.180 -0.914  -18.061 1.00 24.67 ? 76  HIS A NE2   1 
ATOM   511  N N     . VAL A 1 86  ? 24.973 0.975   -12.295 1.00 15.61 ? 77  VAL A N     1 
ATOM   512  C CA    . VAL A 1 86  ? 23.994 1.128   -11.217 1.00 14.89 ? 77  VAL A CA    1 
ATOM   513  C C     . VAL A 1 86  ? 23.192 2.408   -11.464 1.00 17.25 ? 77  VAL A C     1 
ATOM   514  O O     . VAL A 1 86  ? 23.738 3.402   -11.969 1.00 15.11 ? 77  VAL A O     1 
ATOM   515  C CB    . VAL A 1 86  ? 24.687 1.123   -9.844  1.00 16.61 ? 77  VAL A CB    1 
ATOM   516  C CG1   . VAL A 1 86  ? 25.423 -0.214  -9.655  1.00 14.28 ? 77  VAL A CG1   1 
ATOM   517  C CG2   . VAL A 1 86  ? 25.645 2.299   -9.703  1.00 17.51 ? 77  VAL A CG2   1 
ATOM   518  N N     . PRO A 1 87  ? 21.910 2.447   -11.086 1.00 15.85 ? 78  PRO A N     1 
ATOM   519  C CA    . PRO A 1 87  ? 21.079 3.614   -11.423 1.00 14.58 ? 78  PRO A CA    1 
ATOM   520  C C     . PRO A 1 87  ? 21.441 4.774   -10.530 1.00 15.23 ? 78  PRO A C     1 
ATOM   521  O O     . PRO A 1 87  ? 21.871 4.583   -9.395  1.00 14.56 ? 78  PRO A O     1 
ATOM   522  C CB    . PRO A 1 87  ? 19.648 3.135   -11.127 1.00 15.98 ? 78  PRO A CB    1 
ATOM   523  C CG    . PRO A 1 87  ? 19.807 2.069   -10.084 1.00 15.35 ? 78  PRO A CG    1 
ATOM   524  C CD    . PRO A 1 87  ? 21.159 1.401   -10.373 1.00 15.14 ? 78  PRO A CD    1 
ATOM   525  N N     . GLY A 1 88  ? 21.253 5.985   -11.044 1.00 14.20 ? 79  GLY A N     1 
ATOM   526  C CA    . GLY A 1 88  ? 21.284 7.183   -10.234 1.00 16.03 ? 79  GLY A CA    1 
ATOM   527  C C     . GLY A 1 88  ? 19.891 7.788   -10.076 1.00 14.44 ? 79  GLY A C     1 
ATOM   528  O O     . GLY A 1 88  ? 18.931 7.352   -10.706 1.00 17.79 ? 79  GLY A O     1 
ATOM   529  N N     . ILE A 1 89  ? 19.793 8.787   -9.191  1.00 14.60 ? 80  ILE A N     1 
ATOM   530  C CA    . ILE A 1 89  ? 18.562 9.570   -9.068  1.00 14.57 ? 80  ILE A CA    1 
ATOM   531  C C     . ILE A 1 89  ? 18.958 11.025  -8.802  1.00 18.59 ? 80  ILE A C     1 
ATOM   532  O O     . ILE A 1 89  ? 18.236 11.785  -8.143  1.00 19.33 ? 80  ILE A O     1 
ATOM   533  C CB    . ILE A 1 89  ? 17.612 8.979   -7.995  1.00 19.23 ? 80  ILE A CB    1 
ATOM   534  C CG1   . ILE A 1 89  ? 16.188 9.581   -8.125  1.00 19.95 ? 80  ILE A CG1   1 
ATOM   535  C CG2   . ILE A 1 89  ? 18.156 9.170   -6.590  1.00 12.91 ? 80  ILE A CG2   1 
ATOM   536  C CD1   . ILE A 1 89  ? 15.081 8.578   -7.912  1.00 21.96 ? 80  ILE A CD1   1 
ATOM   537  N N     . PHE A 1 90  ? 20.108 11.434  -9.358  1.00 16.75 ? 81  PHE A N     1 
ATOM   538  C CA    . PHE A 1 90  ? 20.573 12.808  -9.220  1.00 19.08 ? 81  PHE A CA    1 
ATOM   539  C C     . PHE A 1 90  ? 20.346 13.646  -10.479 1.00 20.90 ? 81  PHE A C     1 
ATOM   540  O O     . PHE A 1 90  ? 20.534 14.866  -10.424 1.00 21.50 ? 81  PHE A O     1 
ATOM   541  C CB    . PHE A 1 90  ? 22.069 12.852  -8.802  1.00 17.75 ? 81  PHE A CB    1 
ATOM   542  C CG    . PHE A 1 90  ? 23.012 12.115  -9.725  1.00 17.79 ? 81  PHE A CG    1 
ATOM   543  C CD1   . PHE A 1 90  ? 23.253 10.744  -9.563  1.00 15.84 ? 81  PHE A CD1   1 
ATOM   544  C CD2   . PHE A 1 90  ? 23.664 12.785  -10.780 1.00 17.96 ? 81  PHE A CD2   1 
ATOM   545  C CE1   . PHE A 1 90  ? 24.132 10.072  -10.400 1.00 17.64 ? 81  PHE A CE1   1 
ATOM   546  C CE2   . PHE A 1 90  ? 24.556 12.098  -11.628 1.00 18.78 ? 81  PHE A CE2   1 
ATOM   547  C CZ    . PHE A 1 90  ? 24.771 10.731  -11.457 1.00 19.97 ? 81  PHE A CZ    1 
ATOM   548  N N     . THR A 1 91  ? 19.916 13.046  -11.590 1.00 18.51 ? 82  THR A N     1 
ATOM   549  C CA    . THR A 1 91  ? 19.558 13.827  -12.776 1.00 21.89 ? 82  THR A CA    1 
ATOM   550  C C     . THR A 1 91  ? 18.066 13.724  -13.070 1.00 23.36 ? 82  THR A C     1 
ATOM   551  O O     . THR A 1 91  ? 17.393 12.749  -12.695 1.00 18.75 ? 82  THR A O     1 
ATOM   552  C CB    . THR A 1 91  ? 20.337 13.383  -14.018 1.00 20.89 ? 82  THR A CB    1 
ATOM   553  O OG1   . THR A 1 91  ? 19.849 12.110  -14.479 1.00 20.39 ? 82  THR A OG1   1 
ATOM   554  C CG2   . THR A 1 91  ? 21.835 13.277  -13.721 1.00 22.20 ? 82  THR A CG2   1 
ATOM   555  N N     . LYS A 1 92  ? 17.560 14.754  -13.770 1.00 22.68 ? 83  LYS A N     1 
ATOM   556  C CA    . LYS A 1 92  ? 16.159 14.748  -14.202 1.00 22.06 ? 83  LYS A CA    1 
ATOM   557  C C     . LYS A 1 92  ? 15.903 13.643  -15.224 1.00 18.95 ? 83  LYS A C     1 
ATOM   558  O O     . LYS A 1 92  ? 14.817 13.046  -15.244 1.00 20.46 ? 83  LYS A O     1 
ATOM   559  C CB    . LYS A 1 92  ? 15.782 16.123  -14.765 1.00 30.80 ? 83  LYS A CB    1 
ATOM   560  C CG    . LYS A 1 92  ? 15.929 17.260  -13.725 1.00 34.15 ? 83  LYS A CG    1 
ATOM   561  C CD    . LYS A 1 92  ? 14.847 17.177  -12.627 1.00 35.83 ? 83  LYS A CD    1 
ATOM   562  C CE    . LYS A 1 92  ? 15.419 17.464  -11.242 1.00 35.61 ? 83  LYS A CE    1 
ATOM   563  N NZ    . LYS A 1 92  ? 14.394 17.456  -10.156 1.00 37.27 ? 83  LYS A NZ    1 
ATOM   564  N N     . GLU A 1 93  ? 16.898 13.301  -16.028 1.00 21.00 ? 84  GLU A N     1 
ATOM   565  C CA    . GLU A 1 93  ? 16.746 12.149  -16.916 1.00 20.94 ? 84  GLU A CA    1 
ATOM   566  C C     . GLU A 1 93  ? 16.524 10.860  -16.113 1.00 18.95 ? 84  GLU A C     1 
ATOM   567  O O     . GLU A 1 93  ? 15.669 10.036  -16.458 1.00 18.39 ? 84  GLU A O     1 
ATOM   568  C CB    . GLU A 1 93  ? 17.979 12.014  -17.817 1.00 24.74 ? 84  GLU A CB    1 
ATOM   569  C CG    . GLU A 1 93  ? 17.945 10.763  -18.684 1.00 25.99 ? 84  GLU A CG    1 
ATOM   570  C CD    . GLU A 1 93  ? 19.236 10.546  -19.464 1.00 34.22 ? 84  GLU A CD    1 
ATOM   571  O OE1   . GLU A 1 93  ? 20.302 11.031  -19.014 1.00 31.47 ? 84  GLU A OE1   1 
ATOM   572  O OE2   . GLU A 1 93  ? 19.184 9.878   -20.517 1.00 37.17 ? 84  GLU A OE2   1 
ATOM   573  N N     . GLN A 1 94  ? 17.273 10.681  -15.029 1.00 17.16 ? 85  GLN A N     1 
ATOM   574  C CA    . GLN A 1 94  ? 17.076 9.481   -14.223 1.00 17.04 ? 85  GLN A CA    1 
ATOM   575  C C     . GLN A 1 94  ? 15.715 9.512   -13.568 1.00 16.03 ? 85  GLN A C     1 
ATOM   576  O O     . GLN A 1 94  ? 15.055 8.482   -13.459 1.00 18.27 ? 85  GLN A O     1 
ATOM   577  C CB    . GLN A 1 94  ? 18.176 9.374   -13.182 1.00 16.12 ? 85  GLN A CB    1 
ATOM   578  C CG    . GLN A 1 94  ? 19.513 9.022   -13.807 1.00 15.51 ? 85  GLN A CG    1 
ATOM   579  C CD    . GLN A 1 94  ? 20.671 9.511   -12.961 1.00 21.10 ? 85  GLN A CD    1 
ATOM   580  O OE1   . GLN A 1 94  ? 20.488 10.248  -11.967 1.00 17.88 ? 85  GLN A OE1   1 
ATOM   581  N NE2   . GLN A 1 94  ? 21.889 9.091   -13.338 1.00 20.44 ? 85  GLN A NE2   1 
ATOM   582  N N     . VAL A 1 95  ? 15.290 10.688  -13.083 1.00 16.80 ? 86  VAL A N     1 
ATOM   583  C CA    . VAL A 1 95  ? 13.981 10.775  -12.449 1.00 15.36 ? 86  VAL A CA    1 
ATOM   584  C C     . VAL A 1 95  ? 12.894 10.350  -13.430 1.00 18.47 ? 86  VAL A C     1 
ATOM   585  O O     . VAL A 1 95  ? 12.005 9.561   -13.085 1.00 18.80 ? 86  VAL A O     1 
ATOM   586  C CB    . VAL A 1 95  ? 13.745 12.198  -11.902 1.00 17.89 ? 86  VAL A CB    1 
ATOM   587  C CG1   . VAL A 1 95  ? 12.285 12.409  -11.535 1.00 17.51 ? 86  VAL A CG1   1 
ATOM   588  C CG2   . VAL A 1 95  ? 14.703 12.496  -10.708 1.00 15.93 ? 86  VAL A CG2   1 
ATOM   589  N N     . ARG A 1 96  ? 12.977 10.839  -14.685 1.00 18.02 ? 87  ARG A N     1 
ATOM   590  C CA    A ARG A 1 96  ? 11.988 10.475  -15.700 0.50 19.70 ? 87  ARG A CA    1 
ATOM   591  C CA    B ARG A 1 96  ? 11.999 10.470  -15.710 0.50 19.70 ? 87  ARG A CA    1 
ATOM   592  C C     . ARG A 1 96  ? 11.943 8.970   -15.924 1.00 16.93 ? 87  ARG A C     1 
ATOM   593  O O     . ARG A 1 96  ? 10.865 8.388   -16.050 1.00 20.21 ? 87  ARG A O     1 
ATOM   594  C CB    A ARG A 1 96  ? 12.293 11.210  -17.015 0.50 21.37 ? 87  ARG A CB    1 
ATOM   595  C CB    B ARG A 1 96  ? 12.339 11.138  -17.042 0.50 21.37 ? 87  ARG A CB    1 
ATOM   596  C CG    A ARG A 1 96  ? 12.156 12.724  -16.901 0.50 23.69 ? 87  ARG A CG    1 
ATOM   597  C CG    B ARG A 1 96  ? 12.000 12.599  -17.194 0.50 23.86 ? 87  ARG A CG    1 
ATOM   598  C CD    A ARG A 1 96  ? 12.027 13.429  -18.257 0.50 24.94 ? 87  ARG A CD    1 
ATOM   599  C CD    B ARG A 1 96  ? 12.535 13.173  -18.527 0.50 25.13 ? 87  ARG A CD    1 
ATOM   600  N NE    A ARG A 1 96  ? 13.285 13.425  -18.999 0.50 24.82 ? 87  ARG A NE    1 
ATOM   601  N NE    B ARG A 1 96  ? 13.441 12.272  -19.242 0.50 25.95 ? 87  ARG A NE    1 
ATOM   602  C CZ    A ARG A 1 96  ? 14.271 14.293  -18.836 0.50 22.55 ? 87  ARG A CZ    1 
ATOM   603  C CZ    B ARG A 1 96  ? 13.059 11.247  -19.990 0.50 23.87 ? 87  ARG A CZ    1 
ATOM   604  N NH1   A ARG A 1 96  ? 14.184 15.284  -17.967 0.50 22.35 ? 87  ARG A NH1   1 
ATOM   605  N NH1   B ARG A 1 96  ? 11.781 10.963  -20.170 0.50 27.95 ? 87  ARG A NH1   1 
ATOM   606  N NH2   A ARG A 1 96  ? 15.371 14.167  -19.569 0.50 25.87 ? 87  ARG A NH2   1 
ATOM   607  N NH2   B ARG A 1 96  ? 13.985 10.474  -20.552 0.50 27.06 ? 87  ARG A NH2   1 
ATOM   608  N N     . GLU A 1 97  ? 13.103 8.315   -15.978 1.00 15.70 ? 88  GLU A N     1 
ATOM   609  C CA    . GLU A 1 97  ? 13.084 6.877   -16.225 1.00 18.50 ? 88  GLU A CA    1 
ATOM   610  C C     . GLU A 1 97  ? 12.626 6.088   -15.002 1.00 16.17 ? 88  GLU A C     1 
ATOM   611  O O     . GLU A 1 97  ? 11.992 5.034   -15.141 1.00 18.51 ? 88  GLU A O     1 
ATOM   612  C CB    . GLU A 1 97  ? 14.464 6.435   -16.687 1.00 17.59 ? 88  GLU A CB    1 
ATOM   613  C CG    . GLU A 1 97  ? 14.892 7.136   -17.993 1.00 18.05 ? 88  GLU A CG    1 
ATOM   614  C CD    . GLU A 1 97  ? 13.866 6.989   -19.135 1.00 29.60 ? 88  GLU A CD    1 
ATOM   615  O OE1   . GLU A 1 97  ? 13.390 5.867   -19.391 1.00 29.80 ? 88  GLU A OE1   1 
ATOM   616  O OE2   . GLU A 1 97  ? 13.550 8.002   -19.793 1.00 31.17 ? 88  GLU A OE2   1 
ATOM   617  N N     . TRP A 1 98  ? 12.991 6.535   -13.799 1.00 15.61 ? 89  TRP A N     1 
ATOM   618  C CA    . TRP A 1 98  ? 12.496 5.887   -12.578 1.00 19.76 ? 89  TRP A CA    1 
ATOM   619  C C     . TRP A 1 98  ? 10.980 5.980   -12.478 1.00 18.16 ? 89  TRP A C     1 
ATOM   620  O O     . TRP A 1 98  ? 10.316 5.066   -11.974 1.00 17.04 ? 89  TRP A O     1 
ATOM   621  C CB    . TRP A 1 98  ? 13.101 6.550   -11.353 1.00 14.67 ? 89  TRP A CB    1 
ATOM   622  C CG    . TRP A 1 98  ? 14.391 5.947   -10.840 1.00 18.24 ? 89  TRP A CG    1 
ATOM   623  C CD1   . TRP A 1 98  ? 15.569 6.606   -10.657 1.00 15.55 ? 89  TRP A CD1   1 
ATOM   624  C CD2   . TRP A 1 98  ? 14.626 4.578   -10.442 1.00 15.25 ? 89  TRP A CD2   1 
ATOM   625  N NE1   . TRP A 1 98  ? 16.521 5.746   -10.127 1.00 13.42 ? 89  TRP A NE1   1 
ATOM   626  C CE2   . TRP A 1 98  ? 15.975 4.498   -10.010 1.00 16.70 ? 89  TRP A CE2   1 
ATOM   627  C CE3   . TRP A 1 98  ? 13.832 3.426   -10.388 1.00 13.77 ? 89  TRP A CE3   1 
ATOM   628  C CZ2   . TRP A 1 98  ? 16.543 3.319   -9.542  1.00 13.29 ? 89  TRP A CZ2   1 
ATOM   629  C CZ3   . TRP A 1 98  ? 14.393 2.250   -9.888  1.00 17.18 ? 89  TRP A CZ3   1 
ATOM   630  C CH2   . TRP A 1 98  ? 15.738 2.216   -9.468  1.00 14.03 ? 89  TRP A CH2   1 
ATOM   631  N N     . LYS A 1 99  ? 10.420 7.107   -12.900 1.00 18.49 ? 90  LYS A N     1 
ATOM   632  C CA    . LYS A 1 99  ? 8.974  7.296   -12.799 1.00 19.82 ? 90  LYS A CA    1 
ATOM   633  C C     . LYS A 1 99  ? 8.231  6.191   -13.548 1.00 20.47 ? 90  LYS A C     1 
ATOM   634  O O     . LYS A 1 99  ? 7.192  5.713   -13.084 1.00 19.28 ? 90  LYS A O     1 
ATOM   635  C CB    . LYS A 1 99  ? 8.590  8.706   -13.308 1.00 21.25 ? 90  LYS A CB    1 
ATOM   636  N N     . LYS A 1 100 ? 8.782  5.730   -14.680 1.00 18.31 ? 91  LYS A N     1 
ATOM   637  C CA    . LYS A 1 100 ? 8.147  4.664   -15.442 1.00 19.57 ? 91  LYS A CA    1 
ATOM   638  C C     . LYS A 1 100 ? 8.170  3.348   -14.692 1.00 25.07 ? 91  LYS A C     1 
ATOM   639  O O     . LYS A 1 100 ? 7.221  2.571   -14.784 1.00 25.29 ? 91  LYS A O     1 
ATOM   640  C CB    . LYS A 1 100 ? 8.835  4.491   -16.788 1.00 21.24 ? 91  LYS A CB    1 
ATOM   641  C CG    . LYS A 1 100 ? 8.757  5.738   -17.638 1.00 25.88 ? 91  LYS A CG    1 
ATOM   642  C CD    . LYS A 1 100 ? 9.881  5.776   -18.654 1.00 28.38 ? 91  LYS A CD    1 
ATOM   643  C CE    . LYS A 1 100 ? 9.699  6.968   -19.562 1.00 33.66 ? 91  LYS A CE    1 
ATOM   644  N NZ    . LYS A 1 100 ? 10.329 6.712   -20.882 1.00 40.83 ? 91  LYS A NZ    1 
ATOM   645  N N     . ILE A 1 101 ? 9.266  3.064   -13.984 1.00 18.85 ? 92  ILE A N     1 
ATOM   646  C CA    . ILE A 1 101 ? 9.354  1.854   -13.162 1.00 16.30 ? 92  ILE A CA    1 
ATOM   647  C C     . ILE A 1 101 ? 8.394  1.928   -11.974 1.00 17.14 ? 92  ILE A C     1 
ATOM   648  O O     . ILE A 1 101 ? 7.695  0.961   -11.635 1.00 17.71 ? 92  ILE A O     1 
ATOM   649  C CB    . ILE A 1 101 ? 10.807 1.674   -12.686 1.00 17.70 ? 92  ILE A CB    1 
ATOM   650  C CG1   . ILE A 1 101 ? 11.700 1.316   -13.872 1.00 20.52 ? 92  ILE A CG1   1 
ATOM   651  C CG2   . ILE A 1 101 ? 10.889 0.588   -11.642 1.00 13.56 ? 92  ILE A CG2   1 
ATOM   652  C CD1   . ILE A 1 101 ? 13.031 1.976   -13.857 1.00 15.41 ? 92  ILE A CD1   1 
ATOM   653  N N     . VAL A 1 102 ? 8.385  3.061   -11.291 1.00 16.01 ? 93  VAL A N     1 
ATOM   654  C CA    . VAL A 1 102 ? 7.538  3.206   -10.121 1.00 19.90 ? 93  VAL A CA    1 
ATOM   655  C C     . VAL A 1 102 ? 6.074  3.037   -10.512 1.00 22.57 ? 93  VAL A C     1 
ATOM   656  O O     . VAL A 1 102 ? 5.299  2.404   -9.791  1.00 20.88 ? 93  VAL A O     1 
ATOM   657  C CB    . VAL A 1 102 ? 7.789  4.570   -9.445  1.00 17.99 ? 93  VAL A CB    1 
ATOM   658  C CG1   . VAL A 1 102 ? 6.749  4.794   -8.349  1.00 19.79 ? 93  VAL A CG1   1 
ATOM   659  C CG2   . VAL A 1 102 ? 9.224  4.659   -8.904  1.00 19.12 ? 93  VAL A CG2   1 
ATOM   660  N N     . ASP A 1 103 ? 5.681  3.580   -11.672 1.00 20.65 ? 94  ASP A N     1 
ATOM   661  C CA    . ASP A 1 103 ? 4.279  3.492   -12.097 1.00 23.03 ? 94  ASP A CA    1 
ATOM   662  C C     . ASP A 1 103 ? 3.862  2.052   -12.285 1.00 19.24 ? 94  ASP A C     1 
ATOM   663  O O     . ASP A 1 103 ? 2.763  1.649   -11.884 1.00 20.50 ? 94  ASP A O     1 
ATOM   664  C CB    . ASP A 1 103 ? 4.062  4.261   -13.406 1.00 21.51 ? 94  ASP A CB    1 
ATOM   665  C CG    . ASP A 1 103 ? 4.088  5.766   -13.199 1.00 28.16 ? 94  ASP A CG    1 
ATOM   666  O OD1   . ASP A 1 103 ? 3.983  6.210   -12.030 1.00 30.60 ? 94  ASP A OD1   1 
ATOM   667  O OD2   . ASP A 1 103 ? 4.222  6.498   -14.207 1.00 31.76 ? 94  ASP A OD2   1 
ATOM   668  N N     . VAL A 1 104 ? 4.744  1.257   -12.891 1.00 16.63 ? 95  VAL A N     1 
ATOM   669  C CA    . VAL A 1 104 ? 4.476  -0.151  -13.127 1.00 17.09 ? 95  VAL A CA    1 
ATOM   670  C C     . VAL A 1 104 ? 4.321  -0.900  -11.809 1.00 21.81 ? 95  VAL A C     1 
ATOM   671  O O     . VAL A 1 104 ? 3.380  -1.690  -11.623 1.00 23.42 ? 95  VAL A O     1 
ATOM   672  C CB    . VAL A 1 104 ? 5.606  -0.710  -14.016 1.00 23.65 ? 95  VAL A CB    1 
ATOM   673  C CG1   . VAL A 1 104 ? 5.545  -2.184  -14.106 1.00 24.09 ? 95  VAL A CG1   1 
ATOM   674  C CG2   . VAL A 1 104 ? 5.487  -0.107  -15.396 1.00 23.53 ? 95  VAL A CG2   1 
ATOM   675  N N     . VAL A 1 105 ? 5.206  -0.621  -10.850 1.00 17.17 ? 96  VAL A N     1 
ATOM   676  C CA    . VAL A 1 105 ? 5.138  -1.273  -9.539  1.00 20.84 ? 96  VAL A CA    1 
ATOM   677  C C     . VAL A 1 105 ? 3.890  -0.834  -8.768  1.00 19.58 ? 96  VAL A C     1 
ATOM   678  O O     . VAL A 1 105 ? 3.201  -1.656  -8.140  1.00 17.48 ? 96  VAL A O     1 
ATOM   679  C CB    . VAL A 1 105 ? 6.438  -0.968  -8.773  1.00 21.08 ? 96  VAL A CB    1 
ATOM   680  C CG1   . VAL A 1 105 ? 6.319  -1.266  -7.283  1.00 21.23 ? 96  VAL A CG1   1 
ATOM   681  C CG2   . VAL A 1 105 ? 7.564  -1.759  -9.417  1.00 22.31 ? 96  VAL A CG2   1 
ATOM   682  N N     . HIS A 1 106 ? 3.546  0.447   -8.849  1.00 17.51 ? 97  HIS A N     1 
ATOM   683  C CA    . HIS A 1 106 ? 2.342  0.929   -8.165  1.00 18.45 ? 97  HIS A CA    1 
ATOM   684  C C     . HIS A 1 106 ? 1.065  0.376   -8.796  1.00 21.55 ? 97  HIS A C     1 
ATOM   685  O O     . HIS A 1 106 ? 0.072  0.158   -8.089  1.00 19.78 ? 97  HIS A O     1 
ATOM   686  C CB    . HIS A 1 106 ? 2.340  2.450   -8.185  1.00 18.68 ? 97  HIS A CB    1 
ATOM   687  C CG    . HIS A 1 106 ? 3.191  3.063   -7.131  1.00 15.34 ? 97  HIS A CG    1 
ATOM   688  N ND1   . HIS A 1 106 ? 3.556  4.396   -7.157  1.00 17.40 ? 97  HIS A ND1   1 
ATOM   689  C CD2   . HIS A 1 106 ? 3.662  2.561   -5.961  1.00 16.15 ? 97  HIS A CD2   1 
ATOM   690  C CE1   . HIS A 1 106 ? 4.256  4.674   -6.069  1.00 19.56 ? 97  HIS A CE1   1 
ATOM   691  N NE2   . HIS A 1 106 ? 4.337  3.573   -5.333  1.00 18.77 ? 97  HIS A NE2   1 
ATOM   692  N N     . ALA A 1 107 ? 1.098  0.069   -10.091 1.00 18.93 ? 98  ALA A N     1 
ATOM   693  C CA    . ALA A 1 107 ? -0.032 -0.602  -10.731 1.00 19.10 ? 98  ALA A CA    1 
ATOM   694  C C     . ALA A 1 107 ? -0.286 -1.998  -10.165 1.00 21.75 ? 98  ALA A C     1 
ATOM   695  O O     . ALA A 1 107 ? -1.419 -2.484  -10.239 1.00 21.73 ? 98  ALA A O     1 
ATOM   696  C CB    . ALA A 1 107 ? 0.194  -0.681  -12.255 1.00 19.36 ? 98  ALA A CB    1 
ATOM   697  N N     . LYS A 1 108 ? 0.713  -2.656  -9.579  1.00 21.41 ? 99  LYS A N     1 
ATOM   698  C CA    . LYS A 1 108 ? 0.476  -3.929  -8.899  1.00 21.34 ? 99  LYS A CA    1 
ATOM   699  C C     . LYS A 1 108 ? 0.116  -3.767  -7.427  1.00 23.10 ? 99  LYS A C     1 
ATOM   700  O O     . LYS A 1 108 ? -0.135 -4.772  -6.753  1.00 23.53 ? 99  LYS A O     1 
ATOM   701  C CB    . LYS A 1 108 ? 1.707  -4.835  -9.019  1.00 22.17 ? 99  LYS A CB    1 
ATOM   702  C CG    . LYS A 1 108 ? 2.098  -5.076  -10.481 1.00 27.07 ? 99  LYS A CG    1 
ATOM   703  C CD    . LYS A 1 108 ? 2.942  -6.307  -10.653 1.00 32.24 ? 99  LYS A CD    1 
ATOM   704  C CE    . LYS A 1 108 ? 2.187  -7.600  -10.423 1.00 34.13 ? 99  LYS A CE    1 
ATOM   705  N NZ    . LYS A 1 108 ? 3.156  -8.756  -10.482 1.00 30.25 ? 99  LYS A NZ    1 
ATOM   706  N N     . GLY A 1 109 ? 0.066  -2.544  -6.910  1.00 19.17 ? 100 GLY A N     1 
ATOM   707  C CA    . GLY A 1 109 ? -0.329 -2.344  -5.541  1.00 19.92 ? 100 GLY A CA    1 
ATOM   708  C C     . GLY A 1 109 ? 0.795  -2.463  -4.532  1.00 19.89 ? 100 GLY A C     1 
ATOM   709  O O     . GLY A 1 109 ? 0.528  -2.599  -3.324  1.00 17.89 ? 100 GLY A O     1 
ATOM   710  N N     . ALA A 1 110 ? 2.040  -2.398  -4.980  1.00 13.65 ? 101 ALA A N     1 
ATOM   711  C CA    . ALA A 1 110 ? 3.194  -2.472  -4.099  1.00 17.47 ? 101 ALA A CA    1 
ATOM   712  C C     . ALA A 1 110 ? 3.567  -1.092  -3.579  1.00 17.14 ? 101 ALA A C     1 
ATOM   713  O O     . ALA A 1 110 ? 3.191  -0.052  -4.140  1.00 22.15 ? 101 ALA A O     1 
ATOM   714  C CB    . ALA A 1 110 ? 4.405  -3.050  -4.829  1.00 17.97 ? 101 ALA A CB    1 
ATOM   715  N N     . VAL A 1 111 ? 4.341  -1.095  -2.505  1.00 16.32 ? 102 VAL A N     1 
ATOM   716  C CA    . VAL A 1 111 ? 4.978  0.095   -1.968  1.00 12.99 ? 102 VAL A CA    1 
ATOM   717  C C     . VAL A 1 111 ? 6.456  -0.033  -2.305  1.00 13.02 ? 102 VAL A C     1 
ATOM   718  O O     . VAL A 1 111 ? 7.006  -1.131  -2.198  1.00 16.47 ? 102 VAL A O     1 
ATOM   719  C CB    . VAL A 1 111 ? 4.767  0.172   -0.438  1.00 15.68 ? 102 VAL A CB    1 
ATOM   720  C CG1   . VAL A 1 111 ? 5.475  1.372   0.137   1.00 16.36 ? 102 VAL A CG1   1 
ATOM   721  C CG2   . VAL A 1 111 ? 3.275  0.221   -0.076  1.00 18.32 ? 102 VAL A CG2   1 
ATOM   722  N N     . ILE A 1 112 ? 7.094  1.054   -2.747  1.00 15.08 ? 103 ILE A N     1 
ATOM   723  C CA    . ILE A 1 112 ? 8.483  0.949   -3.167  1.00 14.06 ? 103 ILE A CA    1 
ATOM   724  C C     . ILE A 1 112 ? 9.279  2.136   -2.638  1.00 15.34 ? 103 ILE A C     1 
ATOM   725  O O     . ILE A 1 112 ? 8.865  3.298   -2.773  1.00 17.10 ? 103 ILE A O     1 
ATOM   726  C CB    . ILE A 1 112 ? 8.606  0.801   -4.708  1.00 17.22 ? 103 ILE A CB    1 
ATOM   727  C CG1   . ILE A 1 112 ? 10.056 0.564   -5.113  1.00 15.31 ? 103 ILE A CG1   1 
ATOM   728  C CG2   . ILE A 1 112 ? 7.950  1.961   -5.486  1.00 14.46 ? 103 ILE A CG2   1 
ATOM   729  C CD1   . ILE A 1 112 ? 10.162 -0.082  -6.501  1.00 18.91 ? 103 ILE A CD1   1 
ATOM   730  N N     . PHE A 1 113 ? 10.410 1.836   -1.994  1.00 14.05 ? 104 PHE A N     1 
ATOM   731  C CA    . PHE A 1 113 ? 11.366 2.844   -1.556  1.00 13.49 ? 104 PHE A CA    1 
ATOM   732  C C     . PHE A 1 113 ? 12.621 2.716   -2.394  1.00 12.97 ? 104 PHE A C     1 
ATOM   733  O O     . PHE A 1 113 ? 13.051 1.592   -2.714  1.00 14.12 ? 104 PHE A O     1 
ATOM   734  C CB    . PHE A 1 113 ? 11.797 2.660   -0.091  1.00 12.21 ? 104 PHE A CB    1 
ATOM   735  C CG    . PHE A 1 113 ? 10.843 3.226   0.944   1.00 11.76 ? 104 PHE A CG    1 
ATOM   736  C CD1   . PHE A 1 113 ? 9.487  3.392   0.687   1.00 14.47 ? 104 PHE A CD1   1 
ATOM   737  C CD2   . PHE A 1 113 ? 11.328 3.513   2.222   1.00 15.96 ? 104 PHE A CD2   1 
ATOM   738  C CE1   . PHE A 1 113 ? 8.636  3.886   1.722   1.00 15.16 ? 104 PHE A CE1   1 
ATOM   739  C CE2   . PHE A 1 113 ? 10.511 4.001   3.229   1.00 13.60 ? 104 PHE A CE2   1 
ATOM   740  C CZ    . PHE A 1 113 ? 9.153  4.178   2.969   1.00 15.60 ? 104 PHE A CZ    1 
ATOM   741  N N     . CYS A 1 114 ? 13.230 3.861   -2.663  1.00 11.79 ? 105 CYS A N     1 
ATOM   742  C CA    . CYS A 1 114 ? 14.514 3.939   -3.345  1.00 16.20 ? 105 CYS A CA    1 
ATOM   743  C C     . CYS A 1 114 ? 15.648 4.003   -2.331  1.00 13.68 ? 105 CYS A C     1 
ATOM   744  O O     . CYS A 1 114 ? 15.693 4.922   -1.505  1.00 14.76 ? 105 CYS A O     1 
ATOM   745  C CB    . CYS A 1 114 ? 14.546 5.195   -4.218  1.00 17.72 ? 105 CYS A CB    1 
ATOM   746  S SG    . CYS A 1 114 ? 16.116 5.379   -5.134  1.00 17.85 ? 105 CYS A SG    1 
ATOM   747  N N     . GLN A 1 115 ? 16.621 3.097   -2.458  1.00 12.89 ? 106 GLN A N     1 
ATOM   748  C CA    . GLN A 1 115 ? 17.771 3.099   -1.561  1.00 14.60 ? 106 GLN A CA    1 
ATOM   749  C C     . GLN A 1 115 ? 18.845 4.076   -2.050  1.00 15.62 ? 106 GLN A C     1 
ATOM   750  O O     . GLN A 1 115 ? 19.384 3.906   -3.153  1.00 14.15 ? 106 GLN A O     1 
ATOM   751  C CB    . GLN A 1 115 ? 18.366 1.698   -1.431  1.00 11.96 ? 106 GLN A CB    1 
ATOM   752  C CG    . GLN A 1 115 ? 19.435 1.704   -0.314  1.00 11.77 ? 106 GLN A CG    1 
ATOM   753  C CD    . GLN A 1 115 ? 20.250 0.439   -0.198  1.00 14.95 ? 106 GLN A CD    1 
ATOM   754  O OE1   . GLN A 1 115 ? 21.001 0.093   -1.130  1.00 14.41 ? 106 GLN A OE1   1 
ATOM   755  N NE2   . GLN A 1 115 ? 20.199 -0.208  0.977   1.00 12.42 ? 106 GLN A NE2   1 
ATOM   756  N N     . LEU A 1 116 ? 19.181 5.086   -1.238  1.00 11.71 ? 107 LEU A N     1 
ATOM   757  C CA    . LEU A 1 116 ? 20.192 6.082   -1.620  1.00 12.06 ? 107 LEU A CA    1 
ATOM   758  C C     . LEU A 1 116 ? 21.571 5.608   -1.171  1.00 13.69 ? 107 LEU A C     1 
ATOM   759  O O     . LEU A 1 116 ? 21.781 5.340   0.019   1.00 12.14 ? 107 LEU A O     1 
ATOM   760  C CB    . LEU A 1 116 ? 19.877 7.440   -0.985  1.00 14.36 ? 107 LEU A CB    1 
ATOM   761  C CG    . LEU A 1 116 ? 18.494 7.995   -1.347  1.00 13.51 ? 107 LEU A CG    1 
ATOM   762  C CD1   . LEU A 1 116 ? 18.349 9.380   -0.673  1.00 15.41 ? 107 LEU A CD1   1 
ATOM   763  C CD2   . LEU A 1 116 ? 18.312 8.113   -2.832  1.00 15.40 ? 107 LEU A CD2   1 
ATOM   764  N N     . TRP A 1 117 ? 22.517 5.530   -2.102  1.00 11.71 ? 108 TRP A N     1 
ATOM   765  C CA    . TRP A 1 117 ? 23.767 4.800   -1.909  1.00 15.39 ? 108 TRP A CA    1 
ATOM   766  C C     . TRP A 1 117 ? 24.971 5.647   -2.303  1.00 16.27 ? 108 TRP A C     1 
ATOM   767  O O     . TRP A 1 117 ? 25.081 6.067   -3.461  1.00 15.02 ? 108 TRP A O     1 
ATOM   768  C CB    . TRP A 1 117 ? 23.740 3.545   -2.788  1.00 13.17 ? 108 TRP A CB    1 
ATOM   769  C CG    . TRP A 1 117 ? 24.868 2.537   -2.601  1.00 14.62 ? 108 TRP A CG    1 
ATOM   770  C CD1   . TRP A 1 117 ? 25.640 2.336   -1.506  1.00 15.21 ? 108 TRP A CD1   1 
ATOM   771  C CD2   . TRP A 1 117 ? 25.291 1.583   -3.582  1.00 11.62 ? 108 TRP A CD2   1 
ATOM   772  N NE1   . TRP A 1 117 ? 26.541 1.306   -1.746  1.00 13.01 ? 108 TRP A NE1   1 
ATOM   773  C CE2   . TRP A 1 117 ? 26.334 0.826   -3.008  1.00 15.72 ? 108 TRP A CE2   1 
ATOM   774  C CE3   . TRP A 1 117 ? 24.863 1.283   -4.880  1.00 13.80 ? 108 TRP A CE3   1 
ATOM   775  C CZ2   . TRP A 1 117 ? 26.948 -0.230  -3.669  1.00 12.70 ? 108 TRP A CZ2   1 
ATOM   776  C CZ3   . TRP A 1 117 ? 25.477 0.229   -5.560  1.00 14.03 ? 108 TRP A CZ3   1 
ATOM   777  C CH2   . TRP A 1 117 ? 26.535 -0.489  -4.963  1.00 14.12 ? 108 TRP A CH2   1 
ATOM   778  N N     . HIS A 1 118 ? 25.908 5.816   -1.381  1.00 14.04 ? 109 HIS A N     1 
ATOM   779  C CA    . HIS A 1 118 ? 27.214 6.363   -1.711  1.00 15.00 ? 109 HIS A CA    1 
ATOM   780  C C     . HIS A 1 118 ? 28.249 5.367   -1.217  1.00 15.63 ? 109 HIS A C     1 
ATOM   781  O O     . HIS A 1 118 ? 28.255 5.021   -0.031  1.00 14.46 ? 109 HIS A O     1 
ATOM   782  C CB    . HIS A 1 118 ? 27.436 7.732   -1.055  1.00 14.98 ? 109 HIS A CB    1 
ATOM   783  C CG    . HIS A 1 118 ? 28.623 8.479   -1.581  1.00 14.57 ? 109 HIS A CG    1 
ATOM   784  N ND1   . HIS A 1 118 ? 29.887 7.935   -1.625  1.00 13.19 ? 109 HIS A ND1   1 
ATOM   785  C CD2   . HIS A 1 118 ? 28.750 9.761   -2.006  1.00 15.34 ? 109 HIS A CD2   1 
ATOM   786  C CE1   . HIS A 1 118 ? 30.729 8.818   -2.134  1.00 14.35 ? 109 HIS A CE1   1 
ATOM   787  N NE2   . HIS A 1 118 ? 30.073 9.947   -2.337  1.00 17.84 ? 109 HIS A NE2   1 
ATOM   788  N N     . VAL A 1 119 ? 29.139 4.939   -2.119  1.00 12.33 ? 110 VAL A N     1 
ATOM   789  C CA    . VAL A 1 119 ? 30.126 3.924   -1.766  1.00 14.82 ? 110 VAL A CA    1 
ATOM   790  C C     . VAL A 1 119 ? 31.335 4.438   -1.012  1.00 16.91 ? 110 VAL A C     1 
ATOM   791  O O     . VAL A 1 119 ? 32.074 3.609   -0.480  1.00 13.16 ? 110 VAL A O     1 
ATOM   792  C CB    . VAL A 1 119 ? 30.675 3.188   -3.006  1.00 14.79 ? 110 VAL A CB    1 
ATOM   793  C CG1   . VAL A 1 119 ? 29.520 2.403   -3.702  1.00 14.11 ? 110 VAL A CG1   1 
ATOM   794  C CG2   . VAL A 1 119 ? 31.415 4.156   -3.969  1.00 13.18 ? 110 VAL A CG2   1 
ATOM   795  N N     . GLY A 1 120 ? 31.546 5.760   -0.934  1.00 14.01 ? 111 GLY A N     1 
ATOM   796  C CA    . GLY A 1 120 ? 32.743 6.290   -0.287  1.00 14.38 ? 111 GLY A CA    1 
ATOM   797  C C     . GLY A 1 120 ? 33.996 5.692   -0.925  1.00 16.74 ? 111 GLY A C     1 
ATOM   798  O O     . GLY A 1 120 ? 34.154 5.724   -2.155  1.00 14.05 ? 111 GLY A O     1 
ATOM   799  N N     . ARG A 1 121 ? 34.884 5.113   -0.084  1.00 11.35 ? 112 ARG A N     1 
ATOM   800  C CA    . ARG A 1 121 ? 36.184 4.649   -0.569  1.00 15.32 ? 112 ARG A CA    1 
ATOM   801  C C     . ARG A 1 121 ? 36.108 3.337   -1.361  1.00 16.51 ? 112 ARG A C     1 
ATOM   802  O O     . ARG A 1 121 ? 37.126 2.924   -1.942  1.00 14.67 ? 112 ARG A O     1 
ATOM   803  C CB    . ARG A 1 121 ? 37.145 4.471   0.611   1.00 15.32 ? 112 ARG A CB    1 
ATOM   804  C CG    . ARG A 1 121 ? 36.875 3.206   1.406   1.00 13.10 ? 112 ARG A CG    1 
ATOM   805  C CD    . ARG A 1 121 ? 37.718 3.165   2.692   1.00 13.77 ? 112 ARG A CD    1 
ATOM   806  N NE    . ARG A 1 121 ? 37.396 1.976   3.468   1.00 13.58 ? 112 ARG A NE    1 
ATOM   807  C CZ    . ARG A 1 121 ? 38.232 1.447   4.352   1.00 17.21 ? 112 ARG A CZ    1 
ATOM   808  N NH1   . ARG A 1 121 ? 39.417 1.991   4.582   1.00 14.89 ? 112 ARG A NH1   1 
ATOM   809  N NH2   . ARG A 1 121 ? 37.862 0.369   5.041   1.00 14.31 ? 112 ARG A NH2   1 
ATOM   810  N N     . ALA A 1 122 ? 34.938 2.702   -1.432  1.00 14.53 ? 113 ALA A N     1 
ATOM   811  C CA    . ALA A 1 122 ? 34.755 1.429   -2.149  1.00 13.90 ? 113 ALA A CA    1 
ATOM   812  C C     . ALA A 1 122 ? 34.442 1.749   -3.611  1.00 13.71 ? 113 ALA A C     1 
ATOM   813  O O     . ALA A 1 122 ? 33.334 1.543   -4.117  1.00 12.29 ? 113 ALA A O     1 
ATOM   814  C CB    . ALA A 1 122 ? 33.663 0.589   -1.479  1.00 17.24 ? 113 ALA A CB    1 
ATOM   815  N N     . SER A 1 123 ? 35.437 2.335   -4.278  1.00 16.32 ? 114 SER A N     1 
ATOM   816  C CA    . SER A 1 123 ? 35.293 2.744   -5.687  1.00 16.31 ? 114 SER A CA    1 
ATOM   817  C C     . SER A 1 123 ? 36.636 2.534   -6.372  1.00 15.89 ? 114 SER A C     1 
ATOM   818  O O     . SER A 1 123 ? 37.532 1.894   -5.815  1.00 15.40 ? 114 SER A O     1 
ATOM   819  C CB    . SER A 1 123 ? 34.829 4.203   -5.819  1.00 14.15 ? 114 SER A CB    1 
ATOM   820  O OG    . SER A 1 123 ? 34.391 4.468   -7.176  1.00 16.07 ? 114 SER A OG    1 
ATOM   821  N N     . HIS A 1 124 ? 36.779 3.119   -7.557  1.00 15.82 ? 115 HIS A N     1 
ATOM   822  C CA    . HIS A 1 124 ? 37.951 2.949   -8.406  1.00 15.39 ? 115 HIS A CA    1 
ATOM   823  C C     . HIS A 1 124 ? 37.982 4.106   -9.413  1.00 15.50 ? 115 HIS A C     1 
ATOM   824  O O     . HIS A 1 124 ? 36.959 4.736   -9.708  1.00 14.19 ? 115 HIS A O     1 
ATOM   825  C CB    . HIS A 1 124 ? 37.908 1.569   -9.100  1.00 14.45 ? 115 HIS A CB    1 
ATOM   826  C CG    . HIS A 1 124 ? 39.162 1.230   -9.857  1.00 18.99 ? 115 HIS A CG    1 
ATOM   827  N ND1   . HIS A 1 124 ? 39.446 1.755   -11.106 1.00 21.04 ? 115 HIS A ND1   1 
ATOM   828  C CD2   . HIS A 1 124 ? 40.190 0.397   -9.554  1.00 17.36 ? 115 HIS A CD2   1 
ATOM   829  C CE1   . HIS A 1 124 ? 40.606 1.281   -11.524 1.00 22.68 ? 115 HIS A CE1   1 
ATOM   830  N NE2   . HIS A 1 124 ? 41.069 0.438   -10.613 1.00 20.01 ? 115 HIS A NE2   1 
ATOM   831  N N     . GLU A 1 125 ? 39.177 4.449   -9.884  1.00 15.10 ? 116 GLU A N     1 
ATOM   832  C CA    . GLU A 1 125 ? 39.249 5.514   -10.893 1.00 17.73 ? 116 GLU A CA    1 
ATOM   833  C C     . GLU A 1 125 ? 38.259 5.292   -12.047 1.00 20.02 ? 116 GLU A C     1 
ATOM   834  O O     . GLU A 1 125 ? 37.649 6.247   -12.549 1.00 20.38 ? 116 GLU A O     1 
ATOM   835  C CB    . GLU A 1 125 ? 40.677 5.633   -11.452 1.00 24.42 ? 116 GLU A CB    1 
ATOM   836  C CG    . GLU A 1 125 ? 41.945 5.804   -10.502 1.00 30.92 ? 116 GLU A CG    1 
ATOM   837  C CD    . GLU A 1 125 ? 42.110 4.886   -9.257  1.00 31.29 ? 116 GLU A CD    1 
ATOM   838  O OE1   . GLU A 1 125 ? 41.736 3.678   -9.231  1.00 24.86 ? 116 GLU A OE1   1 
ATOM   839  O OE2   . GLU A 1 125 ? 42.751 5.395   -8.300  1.00 39.97 ? 116 GLU A OE2   1 
ATOM   840  N N     . VAL A 1 126 ? 38.074 4.038   -12.480 1.00 17.25 ? 117 VAL A N     1 
ATOM   841  C CA    . VAL A 1 126 ? 37.209 3.766   -13.636 1.00 19.06 ? 117 VAL A CA    1 
ATOM   842  C C     . VAL A 1 126 ? 35.772 4.207   -13.357 1.00 19.81 ? 117 VAL A C     1 
ATOM   843  O O     . VAL A 1 126 ? 35.037 4.556   -14.290 1.00 17.11 ? 117 VAL A O     1 
ATOM   844  C CB    . VAL A 1 126 ? 37.301 2.275   -14.050 1.00 18.12 ? 117 VAL A CB    1 
ATOM   845  C CG1   . VAL A 1 126 ? 36.484 1.360   -13.097 1.00 19.58 ? 117 VAL A CG1   1 
ATOM   846  C CG2   . VAL A 1 126 ? 36.831 2.070   -15.509 1.00 20.80 ? 117 VAL A CG2   1 
ATOM   847  N N     . TYR A 1 127 ? 35.384 4.305   -12.087 1.00 17.29 ? 118 TYR A N     1 
ATOM   848  C CA    . TYR A 1 127 ? 34.028 4.677   -11.718 1.00 16.38 ? 118 TYR A CA    1 
ATOM   849  C C     . TYR A 1 127 ? 33.881 6.139   -11.331 1.00 15.67 ? 118 TYR A C     1 
ATOM   850  O O     . TYR A 1 127 ? 32.766 6.549   -11.028 1.00 17.56 ? 118 TYR A O     1 
ATOM   851  C CB    . TYR A 1 127 ? 33.510 3.824   -10.526 1.00 15.68 ? 118 TYR A CB    1 
ATOM   852  C CG    . TYR A 1 127 ? 33.395 2.378   -10.844 1.00 14.07 ? 118 TYR A CG    1 
ATOM   853  C CD1   . TYR A 1 127 ? 32.638 1.959   -11.939 1.00 15.02 ? 118 TYR A CD1   1 
ATOM   854  C CD2   . TYR A 1 127 ? 34.054 1.414   -10.087 1.00 13.87 ? 118 TYR A CD2   1 
ATOM   855  C CE1   . TYR A 1 127 ? 32.524 0.654   -12.269 1.00 12.54 ? 118 TYR A CE1   1 
ATOM   856  C CE2   . TYR A 1 127 ? 33.971 0.046   -10.446 1.00 15.64 ? 118 TYR A CE2   1 
ATOM   857  C CZ    . TYR A 1 127 ? 33.184 -0.323  -11.526 1.00 14.39 ? 118 TYR A CZ    1 
ATOM   858  O OH    . TYR A 1 127 ? 33.013 -1.651  -11.926 1.00 15.44 ? 118 TYR A OH    1 
ATOM   859  N N     . GLN A 1 128 ? 34.982 6.918   -11.275 1.00 14.55 ? 119 GLN A N     1 
ATOM   860  C CA    . GLN A 1 128 ? 34.929 8.300   -10.791 1.00 18.30 ? 119 GLN A CA    1 
ATOM   861  C C     . GLN A 1 128 ? 35.062 9.286   -11.950 1.00 23.81 ? 119 GLN A C     1 
ATOM   862  O O     . GLN A 1 128 ? 35.819 9.032   -12.891 1.00 22.67 ? 119 GLN A O     1 
ATOM   863  C CB    . GLN A 1 128 ? 36.058 8.572   -9.793  1.00 18.36 ? 119 GLN A CB    1 
ATOM   864  C CG    . GLN A 1 128 ? 35.879 7.878   -8.488  1.00 17.79 ? 119 GLN A CG    1 
ATOM   865  C CD    . GLN A 1 128 ? 34.675 8.408   -7.795  1.00 17.69 ? 119 GLN A CD    1 
ATOM   866  O OE1   . GLN A 1 128 ? 34.428 9.615   -7.825  1.00 21.89 ? 119 GLN A OE1   1 
ATOM   867  N NE2   . GLN A 1 128 ? 33.917 7.529   -7.128  1.00 18.16 ? 119 GLN A NE2   1 
ATOM   868  N N     . PRO A 1 129 ? 34.390 10.439  -11.896 1.00 21.28 ? 120 PRO A N     1 
ATOM   869  C CA    . PRO A 1 129 ? 34.598 11.443  -12.956 1.00 22.59 ? 120 PRO A CA    1 
ATOM   870  C C     . PRO A 1 129 ? 36.062 11.859  -13.019 1.00 24.05 ? 120 PRO A C     1 
ATOM   871  O O     . PRO A 1 129 ? 36.724 12.037  -11.996 1.00 27.06 ? 120 PRO A O     1 
ATOM   872  C CB    . PRO A 1 129 ? 33.687 12.611  -12.554 1.00 25.87 ? 120 PRO A CB    1 
ATOM   873  C CG    . PRO A 1 129 ? 32.772 12.079  -11.452 1.00 27.86 ? 120 PRO A CG    1 
ATOM   874  C CD    . PRO A 1 129 ? 33.481 10.910  -10.836 1.00 22.70 ? 120 PRO A CD    1 
ATOM   875  N N     . ALA A 1 130 ? 36.577 11.975  -14.242 1.00 29.54 ? 121 ALA A N     1 
ATOM   876  C CA    . ALA A 1 130 ? 37.969 12.358  -14.477 1.00 29.81 ? 121 ALA A CA    1 
ATOM   877  C C     . ALA A 1 130 ? 38.942 11.437  -13.746 1.00 28.34 ? 121 ALA A C     1 
ATOM   878  O O     . ALA A 1 130 ? 40.057 11.847  -13.416 1.00 31.47 ? 121 ALA A O     1 
ATOM   879  C CB    . ALA A 1 130 ? 38.221 13.822  -14.081 1.00 32.38 ? 121 ALA A CB    1 
ATOM   880  N N     . GLY A 1 131 ? 38.525 10.188  -13.493 1.00 24.81 ? 122 GLY A N     1 
ATOM   881  C CA    . GLY A 1 131 ? 39.318 9.235   -12.742 1.00 22.48 ? 122 GLY A CA    1 
ATOM   882  C C     . GLY A 1 131 ? 39.811 9.763   -11.401 1.00 26.62 ? 122 GLY A C     1 
ATOM   883  O O     . GLY A 1 131 ? 40.900 9.387   -10.961 1.00 24.45 ? 122 GLY A O     1 
ATOM   884  N N     . ALA A 1 132 ? 39.046 10.646  -10.763 1.00 26.35 ? 123 ALA A N     1 
ATOM   885  C CA    . ALA A 1 132 ? 39.447 11.234  -9.483  1.00 25.25 ? 123 ALA A CA    1 
ATOM   886  C C     . ALA A 1 132 ? 39.407 10.210  -8.347  1.00 24.93 ? 123 ALA A C     1 
ATOM   887  O O     . ALA A 1 132 ? 38.795 9.153   -8.455  1.00 26.75 ? 123 ALA A O     1 
ATOM   888  C CB    . ALA A 1 132 ? 38.541 12.401  -9.124  1.00 26.68 ? 123 ALA A CB    1 
ATOM   889  N N     . ALA A 1 133 ? 40.079 10.541  -7.240  1.00 23.47 ? 124 ALA A N     1 
ATOM   890  C CA    . ALA A 1 133 ? 40.073 9.665   -6.071  1.00 26.19 ? 124 ALA A CA    1 
ATOM   891  C C     . ALA A 1 133 ? 38.685 9.605   -5.428  1.00 21.00 ? 124 ALA A C     1 
ATOM   892  O O     . ALA A 1 133 ? 38.011 10.625  -5.291  1.00 22.54 ? 124 ALA A O     1 
ATOM   893  C CB    . ALA A 1 133 ? 41.084 10.136  -5.023  1.00 24.75 ? 124 ALA A CB    1 
ATOM   894  N N     . PRO A 1 134 ? 38.249 8.428   -5.004  1.00 17.82 ? 125 PRO A N     1 
ATOM   895  C CA    . PRO A 1 134 ? 37.024 8.319   -4.183  1.00 16.31 ? 125 PRO A CA    1 
ATOM   896  C C     . PRO A 1 134 ? 37.190 9.055   -2.858  1.00 16.09 ? 125 PRO A C     1 
ATOM   897  O O     . PRO A 1 134 ? 38.309 9.281   -2.406  1.00 18.94 ? 125 PRO A O     1 
ATOM   898  C CB    . PRO A 1 134 ? 36.889 6.812   -3.939  1.00 17.93 ? 125 PRO A CB    1 
ATOM   899  C CG    . PRO A 1 134 ? 38.126 6.191   -4.406  1.00 26.47 ? 125 PRO A CG    1 
ATOM   900  C CD    . PRO A 1 134 ? 39.007 7.178   -5.095  1.00 21.70 ? 125 PRO A CD    1 
ATOM   901  N N     . ILE A 1 135 ? 36.056 9.410   -2.215  1.00 16.30 ? 126 ILE A N     1 
ATOM   902  C CA    . ILE A 1 135 ? 36.058 10.141  -0.936  1.00 16.80 ? 126 ILE A CA    1 
ATOM   903  C C     . ILE A 1 135 ? 35.756 9.204   0.230   1.00 15.61 ? 126 ILE A C     1 
ATOM   904  O O     . ILE A 1 135 ? 35.142 8.138   0.066   1.00 15.67 ? 126 ILE A O     1 
ATOM   905  C CB    . ILE A 1 135 ? 35.050 11.309  -0.950  1.00 16.86 ? 126 ILE A CB    1 
ATOM   906  C CG1   . ILE A 1 135 ? 33.643 10.807  -1.348  1.00 13.05 ? 126 ILE A CG1   1 
ATOM   907  C CG2   . ILE A 1 135 ? 35.514 12.378  -1.954  1.00 19.44 ? 126 ILE A CG2   1 
ATOM   908  C CD1   . ILE A 1 135 ? 32.541 11.614  -0.637  1.00 19.06 ? 126 ILE A CD1   1 
ATOM   909  N N     . SER A 1 136 ? 36.152 9.615   1.438   1.00 16.81 ? 127 SER A N     1 
ATOM   910  C CA    . SER A 1 136 ? 35.890 8.812   2.638   1.00 13.76 ? 127 SER A CA    1 
ATOM   911  C C     . SER A 1 136 ? 36.060 9.672   3.881   1.00 16.22 ? 127 SER A C     1 
ATOM   912  O O     . SER A 1 136 ? 36.400 10.856  3.804   1.00 16.59 ? 127 SER A O     1 
ATOM   913  C CB    . SER A 1 136 ? 36.801 7.574   2.670   1.00 15.32 ? 127 SER A CB    1 
ATOM   914  O OG    . SER A 1 136 ? 36.443 6.665   3.741   1.00 18.54 ? 127 SER A OG    1 
ATOM   915  N N     . SER A 1 137 ? 35.805 9.059   5.033   1.00 17.05 ? 128 SER A N     1 
ATOM   916  C CA    . SER A 1 137 ? 36.167 9.663   6.320   1.00 14.40 ? 128 SER A CA    1 
ATOM   917  C C     . SER A 1 137 ? 37.680 9.742   6.510   1.00 16.41 ? 128 SER A C     1 
ATOM   918  O O     . SER A 1 137 ? 38.153 10.560  7.313   1.00 19.71 ? 128 SER A O     1 
ATOM   919  C CB    . SER A 1 137 ? 35.571 8.842   7.454   1.00 17.04 ? 128 SER A CB    1 
ATOM   920  O OG    . SER A 1 137 ? 36.038 7.516   7.334   1.00 17.20 ? 128 SER A OG    1 
ATOM   921  N N     . THR A 1 138 ? 38.430 8.936   5.748   1.00 21.03 ? 129 THR A N     1 
ATOM   922  C CA    . THR A 1 138 ? 39.788 8.509   6.040   1.00 16.57 ? 129 THR A CA    1 
ATOM   923  C C     . THR A 1 138 ? 40.603 8.525   4.749   1.00 21.67 ? 129 THR A C     1 
ATOM   924  O O     . THR A 1 138 ? 40.054 8.562   3.643   1.00 16.67 ? 129 THR A O     1 
ATOM   925  C CB    . THR A 1 138 ? 39.813 7.078   6.635   1.00 22.88 ? 129 THR A CB    1 
ATOM   926  O OG1   . THR A 1 138 ? 41.143 6.769   7.052   1.00 25.90 ? 129 THR A OG1   1 
ATOM   927  C CG2   . THR A 1 138 ? 39.360 5.999   5.566   1.00 22.81 ? 129 THR A CG2   1 
ATOM   928  N N     . GLU A 1 139 ? 41.927 8.520   4.890   1.00 22.15 ? 130 GLU A N     1 
ATOM   929  C CA    . GLU A 1 139 ? 42.785 8.267   3.731   1.00 20.29 ? 130 GLU A CA    1 
ATOM   930  C C     . GLU A 1 139 ? 43.190 6.809   3.587   1.00 22.60 ? 130 GLU A C     1 
ATOM   931  O O     . GLU A 1 139 ? 43.903 6.475   2.634   1.00 23.15 ? 130 GLU A O     1 
ATOM   932  C CB    . GLU A 1 139 ? 44.054 9.125   3.786   1.00 22.78 ? 130 GLU A CB    1 
ATOM   933  C CG    . GLU A 1 139 ? 43.778 10.586  3.538   1.00 26.11 ? 130 GLU A CG    1 
ATOM   934  C CD    . GLU A 1 139 ? 44.981 11.492  3.829   1.00 44.40 ? 130 GLU A CD    1 
ATOM   935  O OE1   . GLU A 1 139 ? 46.007 10.994  4.349   1.00 43.13 ? 130 GLU A OE1   1 
ATOM   936  O OE2   . GLU A 1 139 ? 44.900 12.707  3.521   1.00 41.25 ? 130 GLU A OE2   1 
ATOM   937  N N     . LYS A 1 140 ? 42.760 5.950   4.476   1.00 20.49 ? 131 LYS A N     1 
ATOM   938  C CA    . LYS A 1 140 ? 43.143 4.543   4.409   1.00 19.17 ? 131 LYS A CA    1 
ATOM   939  C C     . LYS A 1 140 ? 42.354 3.829   3.322   1.00 20.00 ? 131 LYS A C     1 
ATOM   940  O O     . LYS A 1 140 ? 41.122 3.907   3.313   1.00 18.69 ? 131 LYS A O     1 
ATOM   941  C CB    . LYS A 1 140 ? 42.903 3.840   5.737   1.00 27.18 ? 131 LYS A CB    1 
ATOM   942  C CG    . LYS A 1 140 ? 43.573 4.512   6.915   1.00 30.25 ? 131 LYS A CG    1 
ATOM   943  C CD    . LYS A 1 140 ? 43.211 3.781   8.188   1.00 35.30 ? 131 LYS A CD    1 
ATOM   944  C CE    . LYS A 1 140 ? 41.698 3.697   8.333   1.00 29.58 ? 131 LYS A CE    1 
ATOM   945  N NZ    . LYS A 1 140 ? 41.335 3.988   9.727   1.00 32.76 ? 131 LYS A NZ    1 
ATOM   946  N N     . PRO A 1 141 ? 43.015 3.131   2.409   1.00 25.17 ? 132 PRO A N     1 
ATOM   947  C CA    . PRO A 1 141 ? 42.288 2.314   1.441   1.00 20.18 ? 132 PRO A CA    1 
ATOM   948  C C     . PRO A 1 141 ? 41.760 1.040   2.079   1.00 19.34 ? 132 PRO A C     1 
ATOM   949  O O     . PRO A 1 141 ? 42.252 0.560   3.098   1.00 21.85 ? 132 PRO A O     1 
ATOM   950  C CB    . PRO A 1 141 ? 43.352 1.991   0.382   1.00 22.69 ? 132 PRO A CB    1 
ATOM   951  C CG    . PRO A 1 141 ? 44.625 2.027   1.107   1.00 25.60 ? 132 PRO A CG    1 
ATOM   952  C CD    . PRO A 1 141 ? 44.473 2.933   2.310   1.00 22.96 ? 132 PRO A CD    1 
ATOM   953  N N     . ILE A 1 142 ? 40.741 0.473   1.433   1.00 17.73 ? 133 ILE A N     1 
ATOM   954  C CA    . ILE A 1 142 ? 40.340 -0.887  1.750   1.00 18.99 ? 133 ILE A CA    1 
ATOM   955  C C     . ILE A 1 142 ? 41.536 -1.807  1.541   1.00 21.29 ? 133 ILE A C     1 
ATOM   956  O O     . ILE A 1 142 ? 42.301 -1.634  0.590   1.00 22.34 ? 133 ILE A O     1 
ATOM   957  C CB    . ILE A 1 142 ? 39.162 -1.278  0.846   1.00 18.96 ? 133 ILE A CB    1 
ATOM   958  C CG1   . ILE A 1 142 ? 37.936 -0.423  1.207   1.00 16.00 ? 133 ILE A CG1   1 
ATOM   959  C CG2   . ILE A 1 142 ? 38.842 -2.770  0.955   1.00 18.68 ? 133 ILE A CG2   1 
ATOM   960  C CD1   . ILE A 1 142 ? 36.889 -0.469  0.129   1.00 16.88 ? 133 ILE A CD1   1 
ATOM   961  N N     . SER A 1 143 ? 41.726 -2.775  2.435   1.00 21.12 ? 134 SER A N     1 
ATOM   962  C CA    . SER A 1 143 ? 42.935 -3.583  2.310   1.00 24.64 ? 134 SER A CA    1 
ATOM   963  C C     . SER A 1 143 ? 42.866 -4.471  1.075   1.00 21.64 ? 134 SER A C     1 
ATOM   964  O O     . SER A 1 143 ? 41.806 -4.720  0.499   1.00 21.11 ? 134 SER A O     1 
ATOM   965  C CB    . SER A 1 143 ? 43.135 -4.471  3.528   1.00 23.68 ? 134 SER A CB    1 
ATOM   966  O OG    . SER A 1 143 ? 42.079 -5.392  3.618   1.00 28.23 ? 134 SER A OG    1 
ATOM   967  N N     . ASN A 1 144 ? 44.025 -5.005  0.713   1.00 24.47 ? 135 ASN A N     1 
ATOM   968  C CA    . ASN A 1 144 ? 44.171 -5.818  -0.484  1.00 27.27 ? 135 ASN A CA    1 
ATOM   969  C C     . ASN A 1 144 ? 43.488 -7.182  -0.378  1.00 27.82 ? 135 ASN A C     1 
ATOM   970  O O     . ASN A 1 144 ? 43.449 -7.897  -1.386  1.00 32.78 ? 135 ASN A O     1 
ATOM   971  C CB    . ASN A 1 144 ? 45.669 -5.954  -0.799  1.00 26.95 ? 135 ASN A CB    1 
ATOM   972  C CG    . ASN A 1 144 ? 46.328 -4.609  -1.154  1.00 29.12 ? 135 ASN A CG    1 
ATOM   973  O OD1   . ASN A 1 144 ? 47.084 -4.043  -0.360  1.00 35.06 ? 135 ASN A OD1   1 
ATOM   974  N ND2   . ASN A 1 144 ? 46.037 -4.093  -2.346  1.00 29.50 ? 135 ASN A ND2   1 
ATOM   975  N N     . ARG A 1 145 ? 42.917 -7.541  0.781   1.00 22.76 ? 136 ARG A N     1 
ATOM   976  C CA    . ARG A 1 145 ? 42.073 -8.722  0.931   1.00 25.25 ? 136 ARG A CA    1 
ATOM   977  C C     . ARG A 1 145 ? 40.796 -8.634  0.106   1.00 28.06 ? 136 ARG A C     1 
ATOM   978  O O     . ARG A 1 145 ? 40.148 -9.658  -0.143  1.00 25.01 ? 136 ARG A O     1 
ATOM   979  C CB    . ARG A 1 145 ? 41.683 -8.908  2.394   1.00 24.32 ? 136 ARG A CB    1 
ATOM   980  N N     . TRP A 1 146 ? 40.392 -7.429  -0.262  1.00 21.36 ? 137 TRP A N     1 
ATOM   981  C CA    . TRP A 1 146 ? 39.185 -7.187  -1.039  1.00 23.72 ? 137 TRP A CA    1 
ATOM   982  C C     . TRP A 1 146 ? 39.592 -6.630  -2.387  1.00 18.12 ? 137 TRP A C     1 
ATOM   983  O O     . TRP A 1 146 ? 40.509 -5.808  -2.455  1.00 19.18 ? 137 TRP A O     1 
ATOM   984  C CB    . TRP A 1 146 ? 38.294 -6.166  -0.332  1.00 20.29 ? 137 TRP A CB    1 
ATOM   985  C CG    . TRP A 1 146 ? 38.075 -6.521  1.045   1.00 25.88 ? 137 TRP A CG    1 
ATOM   986  C CD1   . TRP A 1 146 ? 38.846 -6.201  2.126   1.00 21.83 ? 137 TRP A CD1   1 
ATOM   987  C CD2   . TRP A 1 146 ? 37.012 -7.319  1.523   1.00 23.47 ? 137 TRP A CD2   1 
ATOM   988  N NE1   . TRP A 1 146 ? 38.298 -6.748  3.268   1.00 25.30 ? 137 TRP A NE1   1 
ATOM   989  C CE2   . TRP A 1 146 ? 37.171 -7.440  2.919   1.00 24.37 ? 137 TRP A CE2   1 
ATOM   990  C CE3   . TRP A 1 146 ? 35.931 -7.932  0.909   1.00 18.77 ? 137 TRP A CE3   1 
ATOM   991  C CZ2   . TRP A 1 146 ? 36.287 -8.158  3.703   1.00 22.69 ? 137 TRP A CZ2   1 
ATOM   992  C CZ3   . TRP A 1 146 ? 35.035 -8.636  1.698   1.00 23.92 ? 137 TRP A CZ3   1 
ATOM   993  C CH2   . TRP A 1 146 ? 35.225 -8.743  3.070   1.00 23.06 ? 137 TRP A CH2   1 
ATOM   994  N N     . ARG A 1 147 ? 38.920 -7.079  -3.453  1.00 16.95 ? 138 ARG A N     1 
ATOM   995  C CA    . ARG A 1 147 ? 39.105 -6.567  -4.804  1.00 17.73 ? 138 ARG A CA    1 
ATOM   996  C C     . ARG A 1 147 ? 37.774 -6.066  -5.366  1.00 16.12 ? 138 ARG A C     1 
ATOM   997  O O     . ARG A 1 147 ? 36.718 -6.610  -5.063  1.00 19.41 ? 138 ARG A O     1 
ATOM   998  C CB    . ARG A 1 147 ? 39.671 -7.653  -5.759  1.00 22.87 ? 138 ARG A CB    1 
ATOM   999  C CG    . ARG A 1 147 ? 41.055 -8.242  -5.465  1.00 29.79 ? 138 ARG A CG    1 
ATOM   1000 C CD    . ARG A 1 147 ? 42.042 -7.306  -4.803  1.00 35.78 ? 138 ARG A CD    1 
ATOM   1001 N NE    . ARG A 1 147 ? 43.050 -8.048  -4.036  1.00 39.52 ? 138 ARG A NE    1 
ATOM   1002 C CZ    . ARG A 1 147 ? 44.218 -8.477  -4.504  1.00 42.63 ? 138 ARG A CZ    1 
ATOM   1003 N NH1   . ARG A 1 147 ? 44.586 -8.264  -5.763  1.00 45.00 ? 138 ARG A NH1   1 
ATOM   1004 N NH2   . ARG A 1 147 ? 45.028 -9.159  -3.692  1.00 42.21 ? 138 ARG A NH2   1 
ATOM   1005 N N     . ILE A 1 148 ? 37.824 -5.022  -6.180  1.00 17.06 ? 139 ILE A N     1 
ATOM   1006 C CA    . ILE A 1 148 ? 36.616 -4.383  -6.699  1.00 15.11 ? 139 ILE A CA    1 
ATOM   1007 C C     . ILE A 1 148 ? 36.310 -4.972  -8.074  1.00 16.45 ? 139 ILE A C     1 
ATOM   1008 O O     . ILE A 1 148 ? 37.219 -5.218  -8.883  1.00 17.59 ? 139 ILE A O     1 
ATOM   1009 C CB    . ILE A 1 148 ? 36.780 -2.843  -6.771  1.00 15.03 ? 139 ILE A CB    1 
ATOM   1010 C CG1   . ILE A 1 148 ? 35.449 -2.136  -7.086  1.00 15.33 ? 139 ILE A CG1   1 
ATOM   1011 C CG2   . ILE A 1 148 ? 37.822 -2.417  -7.831  1.00 11.04 ? 139 ILE A CG2   1 
ATOM   1012 C CD1   . ILE A 1 148 ? 35.584 -0.606  -7.074  1.00 13.71 ? 139 ILE A CD1   1 
ATOM   1013 N N     . LEU A 1 149 ? 35.043 -5.278  -8.313  1.00 16.86 ? 140 LEU A N     1 
ATOM   1014 C CA    . LEU A 1 149 ? 34.628 -5.750  -9.632  1.00 17.71 ? 140 LEU A CA    1 
ATOM   1015 C C     . LEU A 1 149 ? 34.769 -4.609  -10.639 1.00 16.14 ? 140 LEU A C     1 
ATOM   1016 O O     . LEU A 1 149 ? 34.247 -3.521  -10.409 1.00 13.32 ? 140 LEU A O     1 
ATOM   1017 C CB    . LEU A 1 149 ? 33.170 -6.233  -9.566  1.00 17.65 ? 140 LEU A CB    1 
ATOM   1018 C CG    . LEU A 1 149 ? 32.507 -6.626  -10.891 1.00 18.19 ? 140 LEU A CG    1 
ATOM   1019 C CD1   . LEU A 1 149 ? 33.190 -7.879  -11.449 1.00 18.91 ? 140 LEU A CD1   1 
ATOM   1020 C CD2   . LEU A 1 149 ? 30.969 -6.868  -10.696 1.00 15.98 ? 140 LEU A CD2   1 
ATOM   1021 N N     . MET A 1 150 ? 35.487 -4.839  -11.753 1.00 17.68 ? 141 MET A N     1 
ATOM   1022 C CA    . MET A 1 150 ? 35.638 -3.812  -12.797 1.00 16.18 ? 141 MET A CA    1 
ATOM   1023 C C     . MET A 1 150 ? 34.591 -3.938  -13.901 1.00 17.54 ? 141 MET A C     1 
ATOM   1024 O O     . MET A 1 150 ? 33.924 -4.966  -14.027 1.00 16.60 ? 141 MET A O     1 
ATOM   1025 C CB    . MET A 1 150 ? 37.057 -3.852  -13.402 1.00 15.70 ? 141 MET A CB    1 
ATOM   1026 C CG    . MET A 1 150 ? 38.075 -3.936  -12.298 1.00 18.92 ? 141 MET A CG    1 
ATOM   1027 S SD    . MET A 1 150 ? 38.361 -2.180  -11.841 1.00 19.28 ? 141 MET A SD    1 
ATOM   1028 C CE    . MET A 1 150 ? 38.726 -1.404  -13.400 1.00 22.67 ? 141 MET A CE    1 
ATOM   1029 N N     . PRO A 1 151 ? 34.408 -2.893  -14.730 1.00 16.15 ? 142 PRO A N     1 
ATOM   1030 C CA    . PRO A 1 151 ? 33.382 -2.985  -15.779 1.00 16.03 ? 142 PRO A CA    1 
ATOM   1031 C C     . PRO A 1 151 ? 33.628 -4.119  -16.765 1.00 17.66 ? 142 PRO A C     1 
ATOM   1032 O O     . PRO A 1 151 ? 32.675 -4.634  -17.361 1.00 21.42 ? 142 PRO A O     1 
ATOM   1033 C CB    . PRO A 1 151 ? 33.439 -1.612  -16.474 1.00 18.12 ? 142 PRO A CB    1 
ATOM   1034 C CG    . PRO A 1 151 ? 34.082 -0.685  -15.525 1.00 19.01 ? 142 PRO A CG    1 
ATOM   1035 C CD    . PRO A 1 151 ? 34.896 -1.511  -14.543 1.00 17.20 ? 142 PRO A CD    1 
ATOM   1036 N N     . ASP A 1 152 ? 34.854 -4.590  -16.905 1.00 15.54 ? 143 ASP A N     1 
ATOM   1037 C CA    . ASP A 1 152 ? 35.094 -5.683  -17.830 1.00 19.12 ? 143 ASP A CA    1 
ATOM   1038 C C     . ASP A 1 152 ? 35.008 -7.054  -17.170 1.00 20.19 ? 143 ASP A C     1 
ATOM   1039 O O     . ASP A 1 152 ? 35.338 -8.055  -17.810 1.00 21.20 ? 143 ASP A O     1 
ATOM   1040 C CB    . ASP A 1 152 ? 36.444 -5.497  -18.523 1.00 17.48 ? 143 ASP A CB    1 
ATOM   1041 C CG    . ASP A 1 152 ? 37.620 -5.609  -17.570 1.00 24.17 ? 143 ASP A CG    1 
ATOM   1042 O OD1   . ASP A 1 152 ? 37.430 -5.946  -16.364 1.00 23.32 ? 143 ASP A OD1   1 
ATOM   1043 O OD2   . ASP A 1 152 ? 38.746 -5.317  -18.030 1.00 23.20 ? 143 ASP A OD2   1 
ATOM   1044 N N     . GLY A 1 153 ? 34.591 -7.122  -15.908 1.00 16.57 ? 144 GLY A N     1 
ATOM   1045 C CA    . GLY A 1 153 ? 34.439 -8.390  -15.225 1.00 17.66 ? 144 GLY A CA    1 
ATOM   1046 C C     . GLY A 1 153 ? 35.680 -8.873  -14.506 1.00 20.48 ? 144 GLY A C     1 
ATOM   1047 O O     . GLY A 1 153 ? 35.599 -9.862  -13.759 1.00 22.88 ? 144 GLY A O     1 
ATOM   1048 N N     . THR A 1 154 ? 36.820 -8.219  -14.697 1.00 19.24 ? 145 THR A N     1 
ATOM   1049 C CA    . THR A 1 154 ? 37.992 -8.538  -13.899 1.00 18.98 ? 145 THR A CA    1 
ATOM   1050 C C     . THR A 1 154 ? 37.843 -7.894  -12.532 1.00 18.64 ? 145 THR A C     1 
ATOM   1051 O O     . THR A 1 154 ? 36.852 -7.219  -12.244 1.00 17.27 ? 145 THR A O     1 
ATOM   1052 C CB    . THR A 1 154 ? 39.264 -8.043  -14.566 1.00 18.45 ? 145 THR A CB    1 
ATOM   1053 O OG1   . THR A 1 154 ? 39.223 -6.619  -14.734 1.00 21.50 ? 145 THR A OG1   1 
ATOM   1054 C CG2   . THR A 1 154 ? 39.425 -8.679  -15.971 1.00 23.60 ? 145 THR A CG2   1 
ATOM   1055 N N     . HIS A 1 155 ? 38.850 -8.080  -11.686 1.00 18.68 ? 146 HIS A N     1 
ATOM   1056 C CA    . HIS A 1 155 ? 38.842 -7.473  -10.359 1.00 21.70 ? 146 HIS A CA    1 
ATOM   1057 C C     . HIS A 1 155 ? 40.056 -6.580  -10.214 1.00 26.34 ? 146 HIS A C     1 
ATOM   1058 O O     . HIS A 1 155 ? 41.136 -6.914  -10.713 1.00 26.59 ? 146 HIS A O     1 
ATOM   1059 C CB    . HIS A 1 155 ? 38.799 -8.546  -9.292  1.00 20.75 ? 146 HIS A CB    1 
ATOM   1060 C CG    . HIS A 1 155 ? 37.469 -9.223  -9.235  1.00 29.18 ? 146 HIS A CG    1 
ATOM   1061 N ND1   . HIS A 1 155 ? 37.134 -10.277 -10.060 1.00 26.31 ? 146 HIS A ND1   1 
ATOM   1062 C CD2   . HIS A 1 155 ? 36.356 -8.935  -8.516  1.00 27.92 ? 146 HIS A CD2   1 
ATOM   1063 C CE1   . HIS A 1 155 ? 35.882 -10.631 -9.827  1.00 31.15 ? 146 HIS A CE1   1 
ATOM   1064 N NE2   . HIS A 1 155 ? 35.388 -9.836  -8.892  1.00 33.45 ? 146 HIS A NE2   1 
ATOM   1065 N N     . GLY A 1 156 ? 39.858 -5.423  -9.578  1.00 19.49 ? 147 GLY A N     1 
ATOM   1066 C CA    . GLY A 1 156 ? 40.887 -4.414  -9.466  1.00 18.30 ? 147 GLY A CA    1 
ATOM   1067 C C     . GLY A 1 156 ? 41.194 -4.062  -8.015  1.00 18.12 ? 147 GLY A C     1 
ATOM   1068 O O     . GLY A 1 156 ? 40.616 -4.616  -7.068  1.00 20.87 ? 147 GLY A O     1 
ATOM   1069 N N     . ILE A 1 157 ? 42.147 -3.143  -7.862  1.00 16.04 ? 148 ILE A N     1 
ATOM   1070 C CA    . ILE A 1 157 ? 42.623 -2.732  -6.527  1.00 20.39 ? 148 ILE A CA    1 
ATOM   1071 C C     . ILE A 1 157 ? 41.855 -1.500  -6.077  1.00 17.89 ? 148 ILE A C     1 
ATOM   1072 O O     . ILE A 1 157 ? 41.789 -0.509  -6.812  1.00 18.42 ? 148 ILE A O     1 
ATOM   1073 C CB    . ILE A 1 157 ? 44.136 -2.417  -6.543  1.00 21.78 ? 148 ILE A CB    1 
ATOM   1074 C CG1   . ILE A 1 157 ? 45.001 -3.581  -7.045  1.00 26.41 ? 148 ILE A CG1   1 
ATOM   1075 C CG2   . ILE A 1 157 ? 44.607 -1.947  -5.154  1.00 19.84 ? 148 ILE A CG2   1 
ATOM   1076 C CD1   . ILE A 1 157 ? 44.516 -4.883  -6.676  1.00 29.52 ? 148 ILE A CD1   1 
ATOM   1077 N N     . TYR A 1 158 ? 41.344 -1.526  -4.832  1.00 19.50 ? 149 TYR A N     1 
ATOM   1078 C CA    . TYR A 1 158 ? 40.735 -0.318  -4.243  1.00 19.84 ? 149 TYR A CA    1 
ATOM   1079 C C     . TYR A 1 158 ? 41.804 0.739   -3.993  1.00 18.26 ? 149 TYR A C     1 
ATOM   1080 O O     . TYR A 1 158 ? 42.820 0.437   -3.347  1.00 20.82 ? 149 TYR A O     1 
ATOM   1081 C CB    . TYR A 1 158 ? 40.033 -0.633  -2.924  1.00 17.22 ? 149 TYR A CB    1 
ATOM   1082 C CG    . TYR A 1 158 ? 38.765 -1.453  -3.056  1.00 12.77 ? 149 TYR A CG    1 
ATOM   1083 C CD1   . TYR A 1 158 ? 37.587 -0.869  -3.471  1.00 14.48 ? 149 TYR A CD1   1 
ATOM   1084 C CD2   . TYR A 1 158 ? 38.763 -2.805  -2.744  1.00 15.48 ? 149 TYR A CD2   1 
ATOM   1085 C CE1   . TYR A 1 158 ? 36.426 -1.611  -3.564  1.00 16.01 ? 149 TYR A CE1   1 
ATOM   1086 C CE2   . TYR A 1 158 ? 37.617 -3.564  -2.851  1.00 13.63 ? 149 TYR A CE2   1 
ATOM   1087 C CZ    . TYR A 1 158 ? 36.449 -2.958  -3.244  1.00 13.57 ? 149 TYR A CZ    1 
ATOM   1088 O OH    . TYR A 1 158 ? 35.311 -3.726  -3.372  1.00 17.90 ? 149 TYR A OH    1 
ATOM   1089 N N     . PRO A 1 159 ? 41.621 1.962   -4.483  1.00 20.79 ? 150 PRO A N     1 
ATOM   1090 C CA    . PRO A 1 159 ? 42.665 2.990   -4.375  1.00 20.18 ? 150 PRO A CA    1 
ATOM   1091 C C     . PRO A 1 159 ? 42.600 3.713   -3.037  1.00 22.82 ? 150 PRO A C     1 
ATOM   1092 O O     . PRO A 1 159 ? 41.648 3.582   -2.268  1.00 17.82 ? 150 PRO A O     1 
ATOM   1093 C CB    . PRO A 1 159 ? 42.329 3.969   -5.507  1.00 20.81 ? 150 PRO A CB    1 
ATOM   1094 C CG    . PRO A 1 159 ? 40.800 3.848   -5.631  1.00 19.39 ? 150 PRO A CG    1 
ATOM   1095 C CD    . PRO A 1 159 ? 40.525 2.374   -5.386  1.00 20.53 ? 150 PRO A CD    1 
ATOM   1096 N N     . LYS A 1 160 ? 43.605 4.542   -2.817  1.00 23.21 ? 151 LYS A N     1 
ATOM   1097 C CA    . LYS A 1 160 ? 43.624 5.431   -1.661  1.00 21.28 ? 151 LYS A CA    1 
ATOM   1098 C C     . LYS A 1 160 ? 42.554 6.515   -1.780  1.00 19.52 ? 151 LYS A C     1 
ATOM   1099 O O     . LYS A 1 160 ? 42.546 7.261   -2.762  1.00 20.91 ? 151 LYS A O     1 
ATOM   1100 C CB    . LYS A 1 160 ? 45.007 6.055   -1.562  1.00 21.36 ? 151 LYS A CB    1 
ATOM   1101 C CG    . LYS A 1 160 ? 45.212 6.891   -0.330  1.00 28.68 ? 151 LYS A CG    1 
ATOM   1102 C CD    . LYS A 1 160 ? 46.663 7.338   -0.234  1.00 31.24 ? 151 LYS A CD    1 
ATOM   1103 C CE    . LYS A 1 160 ? 46.955 7.907   1.147   1.00 30.71 ? 151 LYS A CE    1 
ATOM   1104 N NZ    . LYS A 1 160 ? 46.648 6.877   2.201   1.00 36.19 ? 151 LYS A NZ    1 
ATOM   1105 N N     . PRO A 1 161 ? 41.641 6.637   -0.830  1.00 19.19 ? 152 PRO A N     1 
ATOM   1106 C CA    . PRO A 1 161 ? 40.637 7.702   -0.905  1.00 19.41 ? 152 PRO A CA    1 
ATOM   1107 C C     . PRO A 1 161 ? 41.177 9.023   -0.383  1.00 20.17 ? 152 PRO A C     1 
ATOM   1108 O O     . PRO A 1 161 ? 42.212 9.098   0.283   1.00 21.83 ? 152 PRO A O     1 
ATOM   1109 C CB    . PRO A 1 161 ? 39.516 7.190   0.008   1.00 17.89 ? 152 PRO A CB    1 
ATOM   1110 C CG    . PRO A 1 161 ? 40.259 6.342   1.071   1.00 19.41 ? 152 PRO A CG    1 
ATOM   1111 C CD    . PRO A 1 161 ? 41.456 5.739   0.334   1.00 20.23 ? 152 PRO A CD    1 
ATOM   1112 N N     . ARG A 1 162 ? 40.375 10.056  -0.605  1.00 19.49 ? 153 ARG A N     1 
ATOM   1113 C CA    . ARG A 1 162 ? 40.605 11.404  -0.103  1.00 21.58 ? 153 ARG A CA    1 
ATOM   1114 C C     . ARG A 1 162 ? 39.689 11.655  1.091   1.00 19.85 ? 153 ARG A C     1 
ATOM   1115 O O     . ARG A 1 162 ? 38.470 11.526  0.968   1.00 18.77 ? 153 ARG A O     1 
ATOM   1116 C CB    . ARG A 1 162 ? 40.308 12.397  -1.229  1.00 23.14 ? 153 ARG A CB    1 
ATOM   1117 C CG    . ARG A 1 162 ? 40.306 13.826  -0.837  1.00 27.11 ? 153 ARG A CG    1 
ATOM   1118 C CD    . ARG A 1 162 ? 40.251 14.690  -2.088  1.00 21.83 ? 153 ARG A CD    1 
ATOM   1119 N NE    . ARG A 1 162 ? 38.984 14.667  -2.824  1.00 22.42 ? 153 ARG A NE    1 
ATOM   1120 C CZ    . ARG A 1 162 ? 37.872 15.281  -2.422  1.00 22.08 ? 153 ARG A CZ    1 
ATOM   1121 N NH1   . ARG A 1 162 ? 37.813 15.916  -1.255  1.00 24.19 ? 153 ARG A NH1   1 
ATOM   1122 N NH2   . ARG A 1 162 ? 36.790 15.252  -3.206  1.00 23.19 ? 153 ARG A NH2   1 
ATOM   1123 N N     . ALA A 1 163 ? 40.268 12.011  2.241   1.00 20.95 ? 154 ALA A N     1 
ATOM   1124 C CA    . ALA A 1 163 ? 39.484 12.260  3.443   1.00 21.11 ? 154 ALA A CA    1 
ATOM   1125 C C     . ALA A 1 163 ? 38.845 13.643  3.354   1.00 19.64 ? 154 ALA A C     1 
ATOM   1126 O O     . ALA A 1 163 ? 39.549 14.641  3.165   1.00 21.96 ? 154 ALA A O     1 
ATOM   1127 C CB    . ALA A 1 163 ? 40.359 12.157  4.686   1.00 17.05 ? 154 ALA A CB    1 
ATOM   1128 N N     . ILE A 1 164 ? 37.520 13.713  3.489   1.00 16.55 ? 155 ILE A N     1 
ATOM   1129 C CA    . ILE A 1 164 ? 36.820 14.960  3.207   1.00 15.82 ? 155 ILE A CA    1 
ATOM   1130 C C     . ILE A 1 164 ? 36.721 15.808  4.470   1.00 16.53 ? 155 ILE A C     1 
ATOM   1131 O O     . ILE A 1 164 ? 36.707 15.306  5.605   1.00 16.60 ? 155 ILE A O     1 
ATOM   1132 C CB    . ILE A 1 164 ? 35.435 14.713  2.570   1.00 18.69 ? 155 ILE A CB    1 
ATOM   1133 C CG1   . ILE A 1 164 ? 34.554 13.838  3.461   1.00 16.06 ? 155 ILE A CG1   1 
ATOM   1134 C CG2   . ILE A 1 164 ? 35.622 14.052  1.166   1.00 15.85 ? 155 ILE A CG2   1 
ATOM   1135 C CD1   . ILE A 1 164 ? 33.083 13.826  3.052   1.00 15.33 ? 155 ILE A CD1   1 
ATOM   1136 N N     . GLY A 1 165 ? 36.660 17.124  4.264   1.00 17.20 ? 156 GLY A N     1 
ATOM   1137 C CA    . GLY A 1 165 ? 36.517 18.063  5.359   1.00 19.87 ? 156 GLY A CA    1 
ATOM   1138 C C     . GLY A 1 165 ? 35.060 18.289  5.684   1.00 18.60 ? 156 GLY A C     1 
ATOM   1139 O O     . GLY A 1 165 ? 34.163 17.692  5.089   1.00 18.71 ? 156 GLY A O     1 
ATOM   1140 N N     . THR A 1 166 ? 34.803 19.176  6.653   1.00 16.16 ? 157 THR A N     1 
ATOM   1141 C CA    . THR A 1 166 ? 33.420 19.227  7.104   1.00 14.37 ? 157 THR A CA    1 
ATOM   1142 C C     . THR A 1 166 ? 32.531 19.993  6.127   1.00 16.06 ? 157 THR A C     1 
ATOM   1143 O O     . THR A 1 166 ? 31.318 19.745  6.067   1.00 16.39 ? 157 THR A O     1 
ATOM   1144 C CB    . THR A 1 166 ? 33.326 19.833  8.503   1.00 18.50 ? 157 THR A CB    1 
ATOM   1145 O OG1   . THR A 1 166 ? 33.757 21.202  8.470   1.00 17.01 ? 157 THR A OG1   1 
ATOM   1146 C CG2   . THR A 1 166 ? 34.149 19.014  9.502   1.00 20.27 ? 157 THR A CG2   1 
ATOM   1147 N N     . TYR A 1 167 ? 33.088 20.922  5.354   1.00 16.55 ? 158 TYR A N     1 
ATOM   1148 C CA    . TYR A 1 167 ? 32.275 21.562  4.325   1.00 18.92 ? 158 TYR A CA    1 
ATOM   1149 C C     . TYR A 1 167 ? 31.824 20.535  3.289   1.00 16.14 ? 158 TYR A C     1 
ATOM   1150 O O     . TYR A 1 167 ? 30.639 20.467  2.933   1.00 17.76 ? 158 TYR A O     1 
ATOM   1151 C CB    . TYR A 1 167 ? 33.061 22.679  3.658   1.00 17.24 ? 158 TYR A CB    1 
ATOM   1152 C CG    . TYR A 1 167 ? 32.291 23.335  2.535   1.00 21.13 ? 158 TYR A CG    1 
ATOM   1153 C CD1   . TYR A 1 167 ? 31.180 24.129  2.811   1.00 20.14 ? 158 TYR A CD1   1 
ATOM   1154 C CD2   . TYR A 1 167 ? 32.643 23.127  1.198   1.00 16.94 ? 158 TYR A CD2   1 
ATOM   1155 C CE1   . TYR A 1 167 ? 30.466 24.750  1.778   1.00 23.92 ? 158 TYR A CE1   1 
ATOM   1156 C CE2   . TYR A 1 167 ? 31.937 23.716  0.182   1.00 19.52 ? 158 TYR A CE2   1 
ATOM   1157 C CZ    . TYR A 1 167 ? 30.849 24.520  0.476   1.00 21.26 ? 158 TYR A CZ    1 
ATOM   1158 O OH    . TYR A 1 167 ? 30.183 25.127  -0.564  1.00 23.55 ? 158 TYR A OH    1 
ATOM   1159 N N     . GLU A 1 168 ? 32.753 19.695  2.826   1.00 18.21 ? 159 GLU A N     1 
ATOM   1160 C CA    . GLU A 1 168 ? 32.385 18.669  1.849   1.00 18.82 ? 159 GLU A CA    1 
ATOM   1161 C C     . GLU A 1 168 ? 31.411 17.651  2.451   1.00 17.02 ? 159 GLU A C     1 
ATOM   1162 O O     . GLU A 1 168 ? 30.523 17.157  1.741   1.00 17.88 ? 159 GLU A O     1 
ATOM   1163 C CB    . GLU A 1 168 ? 33.652 17.986  1.303   1.00 15.63 ? 159 GLU A CB    1 
ATOM   1164 C CG    . GLU A 1 168 ? 33.363 16.939  0.243   1.00 16.78 ? 159 GLU A CG    1 
ATOM   1165 C CD    . GLU A 1 168 ? 34.530 16.699  -0.724  1.00 25.01 ? 159 GLU A CD    1 
ATOM   1166 O OE1   . GLU A 1 168 ? 35.672 17.193  -0.479  1.00 23.67 ? 159 GLU A OE1   1 
ATOM   1167 O OE2   . GLU A 1 168 ? 34.318 15.896  -1.668  1.00 19.78 ? 159 GLU A OE2   1 
ATOM   1168 N N     . ILE A 1 169 ? 31.524 17.362  3.763   1.00 14.58 ? 160 ILE A N     1 
ATOM   1169 C CA    . ILE A 1 169 ? 30.521 16.534  4.423   1.00 14.60 ? 160 ILE A CA    1 
ATOM   1170 C C     . ILE A 1 169 ? 29.141 17.165  4.279   1.00 17.44 ? 160 ILE A C     1 
ATOM   1171 O O     . ILE A 1 169 ? 28.175 16.500  3.894   1.00 15.67 ? 160 ILE A O     1 
ATOM   1172 C CB    . ILE A 1 169 ? 30.884 16.312  5.908   1.00 15.77 ? 160 ILE A CB    1 
ATOM   1173 C CG1   . ILE A 1 169 ? 32.043 15.327  6.010   1.00 16.29 ? 160 ILE A CG1   1 
ATOM   1174 C CG2   . ILE A 1 169 ? 29.663 15.810  6.685   1.00 17.02 ? 160 ILE A CG2   1 
ATOM   1175 C CD1   . ILE A 1 169 ? 32.656 15.289  7.458   1.00 15.92 ? 160 ILE A CD1   1 
ATOM   1176 N N     . SER A 1 170 ? 29.028 18.471  4.571   1.00 15.96 ? 161 SER A N     1 
ATOM   1177 C CA    . SER A 1 170 ? 27.732 19.125  4.410   1.00 17.36 ? 161 SER A CA    1 
ATOM   1178 C C     . SER A 1 170 ? 27.241 19.071  2.957   1.00 17.57 ? 161 SER A C     1 
ATOM   1179 O O     . SER A 1 170 ? 26.027 19.067  2.712   1.00 17.80 ? 161 SER A O     1 
ATOM   1180 C CB    . SER A 1 170 ? 27.813 20.570  4.935   1.00 19.61 ? 161 SER A CB    1 
ATOM   1181 O OG    . SER A 1 170 ? 28.479 21.422  3.983   1.00 22.21 ? 161 SER A OG    1 
ATOM   1182 N N     . GLN A 1 171 ? 28.162 19.029  1.988   1.00 15.29 ? 162 GLN A N     1 
ATOM   1183 C CA    . GLN A 1 171 ? 27.789 18.943  0.579   1.00 17.76 ? 162 GLN A CA    1 
ATOM   1184 C C     . GLN A 1 171 ? 27.241 17.561  0.243   1.00 16.98 ? 162 GLN A C     1 
ATOM   1185 O O     . GLN A 1 171 ? 26.258 17.436  -0.494  1.00 14.77 ? 162 GLN A O     1 
ATOM   1186 C CB    . GLN A 1 171 ? 28.987 19.256  -0.312  1.00 18.35 ? 162 GLN A CB    1 
ATOM   1187 C CG    . GLN A 1 171 ? 29.410 20.720  -0.311  1.00 20.71 ? 162 GLN A CG    1 
ATOM   1188 C CD    . GLN A 1 171 ? 30.514 20.927  -1.315  1.00 27.93 ? 162 GLN A CD    1 
ATOM   1189 O OE1   . GLN A 1 171 ? 31.577 20.305  -1.207  1.00 25.32 ? 162 GLN A OE1   1 
ATOM   1190 N NE2   . GLN A 1 171 ? 30.251 21.757  -2.338  1.00 28.67 ? 162 GLN A NE2   1 
ATOM   1191 N N     . VAL A 1 172 ? 27.849 16.513  0.799   1.00 14.88 ? 163 VAL A N     1 
ATOM   1192 C CA    . VAL A 1 172 ? 27.341 15.160  0.574   1.00 14.34 ? 163 VAL A CA    1 
ATOM   1193 C C     . VAL A 1 172 ? 25.967 14.995  1.213   1.00 15.37 ? 163 VAL A C     1 
ATOM   1194 O O     . VAL A 1 172 ? 25.079 14.330  0.662   1.00 14.11 ? 163 VAL A O     1 
ATOM   1195 C CB    . VAL A 1 172 ? 28.352 14.129  1.128   1.00 16.45 ? 163 VAL A CB    1 
ATOM   1196 C CG1   . VAL A 1 172 ? 27.783 12.701  1.095   1.00 16.38 ? 163 VAL A CG1   1 
ATOM   1197 C CG2   . VAL A 1 172 ? 29.663 14.242  0.334   1.00 13.74 ? 163 VAL A CG2   1 
ATOM   1198 N N     . VAL A 1 173 ? 25.792 15.541  2.419   1.00 13.29 ? 164 VAL A N     1 
ATOM   1199 C CA    . VAL A 1 173 ? 24.473 15.529  3.046   1.00 14.52 ? 164 VAL A CA    1 
ATOM   1200 C C     . VAL A 1 173 ? 23.442 16.167  2.107   1.00 14.83 ? 164 VAL A C     1 
ATOM   1201 O O     . VAL A 1 173 ? 22.322 15.660  1.924   1.00 14.61 ? 164 VAL A O     1 
ATOM   1202 C CB    . VAL A 1 173 ? 24.542 16.257  4.414   1.00 15.34 ? 164 VAL A CB    1 
ATOM   1203 C CG1   . VAL A 1 173 ? 23.131 16.472  4.977   1.00 18.18 ? 164 VAL A CG1   1 
ATOM   1204 C CG2   . VAL A 1 173 ? 25.441 15.497  5.437   1.00 16.33 ? 164 VAL A CG2   1 
ATOM   1205 N N     . GLU A 1 174 ? 23.816 17.268  1.460   1.00 15.46 ? 165 GLU A N     1 
ATOM   1206 C CA    . GLU A 1 174 ? 22.894 17.916  0.534   1.00 17.77 ? 165 GLU A CA    1 
ATOM   1207 C C     . GLU A 1 174 ? 22.620 17.025  -0.690  1.00 16.44 ? 165 GLU A C     1 
ATOM   1208 O O     . GLU A 1 174 ? 21.499 17.005  -1.215  1.00 16.13 ? 165 GLU A O     1 
ATOM   1209 C CB    . GLU A 1 174 ? 23.477 19.281  0.138   1.00 17.97 ? 165 GLU A CB    1 
ATOM   1210 C CG    . GLU A 1 174 ? 22.668 20.038  -0.932  1.00 27.27 ? 165 GLU A CG    1 
ATOM   1211 C CD    . GLU A 1 174 ? 21.268 20.492  -0.460  1.00 31.95 ? 165 GLU A CD    1 
ATOM   1212 O OE1   . GLU A 1 174 ? 20.988 20.516  0.762   1.00 27.16 ? 165 GLU A OE1   1 
ATOM   1213 O OE2   . GLU A 1 174 ? 20.448 20.842  -1.339  1.00 37.83 ? 165 GLU A OE2   1 
ATOM   1214 N N     . ASP A 1 175 ? 23.614 16.261  -1.134  1.00 15.60 ? 166 ASP A N     1 
ATOM   1215 C CA    . ASP A 1 175 ? 23.381 15.283  -2.193  1.00 19.22 ? 166 ASP A CA    1 
ATOM   1216 C C     . ASP A 1 175 ? 22.321 14.253  -1.783  1.00 16.40 ? 166 ASP A C     1 
ATOM   1217 O O     . ASP A 1 175 ? 21.474 13.864  -2.601  1.00 15.15 ? 166 ASP A O     1 
ATOM   1218 C CB    . ASP A 1 175 ? 24.700 14.594  -2.557  1.00 18.18 ? 166 ASP A CB    1 
ATOM   1219 C CG    . ASP A 1 175 ? 25.625 15.481  -3.388  1.00 21.27 ? 166 ASP A CG    1 
ATOM   1220 O OD1   . ASP A 1 175 ? 25.157 16.482  -3.999  1.00 25.56 ? 166 ASP A OD1   1 
ATOM   1221 O OD2   . ASP A 1 175 ? 26.845 15.227  -3.383  1.00 24.13 ? 166 ASP A OD2   1 
ATOM   1222 N N     . TYR A 1 176 ? 22.366 13.777  -0.528  1.00 11.53 ? 167 TYR A N     1 
ATOM   1223 C CA    . TYR A 1 176 ? 21.306 12.897  -0.047  1.00 11.24 ? 167 TYR A CA    1 
ATOM   1224 C C     . TYR A 1 176 ? 19.962 13.609  -0.059  1.00 16.34 ? 167 TYR A C     1 
ATOM   1225 O O     . TYR A 1 176 ? 18.959 13.035  -0.496  1.00 14.77 ? 167 TYR A O     1 
ATOM   1226 C CB    . TYR A 1 176 ? 21.618 12.410  1.364   1.00 13.19 ? 167 TYR A CB    1 
ATOM   1227 C CG    . TYR A 1 176 ? 22.605 11.251  1.422   1.00 11.44 ? 167 TYR A CG    1 
ATOM   1228 C CD1   . TYR A 1 176 ? 22.190 9.929   1.190   1.00 12.61 ? 167 TYR A CD1   1 
ATOM   1229 C CD2   . TYR A 1 176 ? 23.929 11.479  1.850   1.00 13.64 ? 167 TYR A CD2   1 
ATOM   1230 C CE1   . TYR A 1 176 ? 23.101 8.863   1.308   1.00 15.02 ? 167 TYR A CE1   1 
ATOM   1231 C CE2   . TYR A 1 176 ? 24.838 10.442  1.958   1.00 16.73 ? 167 TYR A CE2   1 
ATOM   1232 C CZ    . TYR A 1 176 ? 24.416 9.130   1.684   1.00 13.43 ? 167 TYR A CZ    1 
ATOM   1233 O OH    . TYR A 1 176 ? 25.314 8.108   1.834   1.00 16.24 ? 167 TYR A OH    1 
ATOM   1234 N N     . ARG A 1 177 ? 19.929 14.862  0.424   1.00 17.34 ? 168 ARG A N     1 
ATOM   1235 C CA    . ARG A 1 177 ? 18.670 15.613  0.484   1.00 15.88 ? 168 ARG A CA    1 
ATOM   1236 C C     . ARG A 1 177 ? 18.068 15.784  -0.913  1.00 16.61 ? 168 ARG A C     1 
ATOM   1237 O O     . ARG A 1 177 ? 16.874 15.521  -1.109  1.00 16.49 ? 168 ARG A O     1 
ATOM   1238 C CB    . ARG A 1 177 ? 18.886 16.971  1.163   1.00 18.26 ? 168 ARG A CB    1 
ATOM   1239 C CG    . ARG A 1 177 ? 17.577 17.587  1.710   1.00 20.37 ? 168 ARG A CG    1 
ATOM   1240 C CD    . ARG A 1 177 ? 17.764 19.073  2.119   1.00 24.80 ? 168 ARG A CD    1 
ATOM   1241 N NE    . ARG A 1 177 ? 18.095 19.892  0.963   1.00 28.47 ? 168 ARG A NE    1 
ATOM   1242 C CZ    . ARG A 1 177 ? 17.202 20.444  0.147   1.00 35.25 ? 168 ARG A CZ    1 
ATOM   1243 N NH1   . ARG A 1 177 ? 15.908 20.420  0.420   1.00 30.68 ? 168 ARG A NH1   1 
ATOM   1244 N NH2   . ARG A 1 177 ? 17.618 21.018  -0.980  1.00 31.70 ? 168 ARG A NH2   1 
ATOM   1245 N N     . ARG A 1 178 ? 18.897 16.182  -1.911  1.00 13.49 ? 169 ARG A N     1 
ATOM   1246 C CA    . ARG A 1 178 ? 18.387 16.396  -3.270  1.00 15.67 ? 169 ARG A CA    1 
ATOM   1247 C C     . ARG A 1 178 ? 17.912 15.087  -3.893  1.00 17.09 ? 169 ARG A C     1 
ATOM   1248 O O     . ARG A 1 178 ? 16.898 15.047  -4.617  1.00 16.72 ? 169 ARG A O     1 
ATOM   1249 C CB    . ARG A 1 178 ? 19.453 17.052  -4.179  1.00 16.28 ? 169 ARG A CB    1 
ATOM   1250 C CG    . ARG A 1 178 ? 20.134 18.253  -3.574  1.00 30.71 ? 169 ARG A CG    1 
ATOM   1251 C CD    . ARG A 1 178 ? 21.080 18.914  -4.574  1.00 39.36 ? 169 ARG A CD    1 
ATOM   1252 N NE    . ARG A 1 178 ? 20.958 20.365  -4.545  1.00 47.42 ? 169 ARG A NE    1 
ATOM   1253 C CZ    . ARG A 1 178 ? 21.946 21.203  -4.834  1.00 60.51 ? 169 ARG A CZ    1 
ATOM   1254 N NH1   . ARG A 1 178 ? 23.154 20.763  -5.156  1.00 61.92 ? 169 ARG A NH1   1 
ATOM   1255 N NH2   . ARG A 1 178 ? 21.712 22.515  -4.820  1.00 61.20 ? 169 ARG A NH2   1 
ATOM   1256 N N     . SER A 1 179 ? 18.641 14.002  -3.643  1.00 16.21 ? 170 SER A N     1 
ATOM   1257 C CA    . SER A 1 179 ? 18.207 12.722  -4.186  1.00 13.64 ? 170 SER A CA    1 
ATOM   1258 C C     . SER A 1 179 ? 16.905 12.257  -3.555  1.00 15.89 ? 170 SER A C     1 
ATOM   1259 O O     . SER A 1 179 ? 16.081 11.617  -4.221  1.00 17.50 ? 170 SER A O     1 
ATOM   1260 C CB    . SER A 1 179 ? 19.295 11.659  -3.992  1.00 16.54 ? 170 SER A CB    1 
ATOM   1261 O OG    . SER A 1 179 ? 20.389 11.941  -4.836  1.00 18.52 ? 170 SER A OG    1 
ATOM   1262 N N     . ALA A 1 180 ? 16.709 12.534  -2.263  1.00 13.60 ? 171 ALA A N     1 
ATOM   1263 C CA    . ALA A 1 180 ? 15.452 12.169  -1.626  1.00 18.08 ? 171 ALA A CA    1 
ATOM   1264 C C     . ALA A 1 180 ? 14.294 12.909  -2.276  1.00 16.25 ? 171 ALA A C     1 
ATOM   1265 O O     . ALA A 1 180 ? 13.236 12.327  -2.533  1.00 15.47 ? 171 ALA A O     1 
ATOM   1266 C CB    . ALA A 1 180 ? 15.515 12.498  -0.134  1.00 15.57 ? 171 ALA A CB    1 
ATOM   1267 N N     . LEU A 1 181 ? 14.477 14.209  -2.522  1.00 16.50 ? 172 LEU A N     1 
ATOM   1268 C CA    . LEU A 1 181 ? 13.441 14.987  -3.204  1.00 18.74 ? 172 LEU A CA    1 
ATOM   1269 C C     . LEU A 1 181 ? 13.199 14.450  -4.603  1.00 15.64 ? 172 LEU A C     1 
ATOM   1270 O O     . LEU A 1 181 ? 12.049 14.370  -5.069  1.00 17.27 ? 172 LEU A O     1 
ATOM   1271 C CB    . LEU A 1 181 ? 13.858 16.459  -3.259  1.00 17.50 ? 172 LEU A CB    1 
ATOM   1272 C CG    . LEU A 1 181 ? 13.769 17.169  -1.889  1.00 18.19 ? 172 LEU A CG    1 
ATOM   1273 C CD1   . LEU A 1 181 ? 14.342 18.619  -1.980  1.00 23.37 ? 172 LEU A CD1   1 
ATOM   1274 C CD2   . LEU A 1 181 ? 12.321 17.208  -1.463  1.00 22.42 ? 172 LEU A CD2   1 
ATOM   1275 N N     . ASN A 1 182 ? 14.274 14.062  -5.290  1.00 15.89 ? 173 ASN A N     1 
ATOM   1276 C CA    . ASN A 1 182 ? 14.136 13.512  -6.640  1.00 14.13 ? 173 ASN A CA    1 
ATOM   1277 C C     . ASN A 1 182 ? 13.358 12.214  -6.619  1.00 13.47 ? 173 ASN A C     1 
ATOM   1278 O O     . ASN A 1 182 ? 12.567 11.923  -7.533  1.00 15.95 ? 173 ASN A O     1 
ATOM   1279 C CB    . ASN A 1 182 ? 15.514 13.277  -7.243  1.00 16.71 ? 173 ASN A CB    1 
ATOM   1280 C CG    . ASN A 1 182 ? 16.095 14.508  -7.836  1.00 24.26 ? 173 ASN A CG    1 
ATOM   1281 O OD1   . ASN A 1 182 ? 15.444 15.560  -7.883  1.00 22.13 ? 173 ASN A OD1   1 
ATOM   1282 N ND2   . ASN A 1 182 ? 17.338 14.403  -8.312  1.00 23.00 ? 173 ASN A ND2   1 
ATOM   1283 N N     . ALA A 1 183 ? 13.644 11.368  -5.615  1.00 14.16 ? 174 ALA A N     1 
ATOM   1284 C CA    . ALA A 1 183 ? 12.899 10.122  -5.492  1.00 13.36 ? 174 ALA A CA    1 
ATOM   1285 C C     . ALA A 1 183 ? 11.411 10.400  -5.334  1.00 14.81 ? 174 ALA A C     1 
ATOM   1286 O O     . ALA A 1 183 ? 10.583 9.750   -5.983  1.00 16.89 ? 174 ALA A O     1 
ATOM   1287 C CB    . ALA A 1 183 ? 13.411 9.295   -4.320  1.00 16.15 ? 174 ALA A CB    1 
ATOM   1288 N N     . ILE A 1 184 ? 11.060 11.400  -4.510  1.00 15.30 ? 175 ILE A N     1 
ATOM   1289 C CA    . ILE A 1 184 ? 9.658  11.733  -4.317  1.00 14.99 ? 175 ILE A CA    1 
ATOM   1290 C C     . ILE A 1 184 ? 9.054  12.200  -5.630  1.00 19.32 ? 175 ILE A C     1 
ATOM   1291 O O     . ILE A 1 184 ? 7.924  11.833  -5.978  1.00 17.62 ? 175 ILE A O     1 
ATOM   1292 C CB    . ILE A 1 184 ? 9.491  12.790  -3.211  1.00 20.91 ? 175 ILE A CB    1 
ATOM   1293 C CG1   . ILE A 1 184 ? 9.833  12.188  -1.844  1.00 20.58 ? 175 ILE A CG1   1 
ATOM   1294 C CG2   . ILE A 1 184 ? 8.041  13.349  -3.228  1.00 24.95 ? 175 ILE A CG2   1 
ATOM   1295 C CD1   . ILE A 1 184 ? 9.109  10.945  -1.555  1.00 20.36 ? 175 ILE A CD1   1 
ATOM   1296 N N     . GLU A 1 185 ? 9.823  12.980  -6.393  1.00 21.27 ? 176 GLU A N     1 
ATOM   1297 C CA    . GLU A 1 185 ? 9.364  13.461  -7.681  1.00 20.24 ? 176 GLU A CA    1 
ATOM   1298 C C     . GLU A 1 185 ? 9.117  12.311  -8.654  1.00 21.60 ? 176 GLU A C     1 
ATOM   1299 O O     . GLU A 1 185 ? 8.209  12.379  -9.508  1.00 23.28 ? 176 GLU A O     1 
ATOM   1300 C CB    . GLU A 1 185 ? 10.391 14.453  -8.228  1.00 22.92 ? 176 GLU A CB    1 
ATOM   1301 C CG    . GLU A 1 185 ? 9.935  15.152  -9.519  1.00 25.06 ? 176 GLU A CG    1 
ATOM   1302 C CD    . GLU A 1 185 ? 10.991 16.077  -10.082 1.00 36.78 ? 176 GLU A CD    1 
ATOM   1303 O OE1   . GLU A 1 185 ? 11.814 16.590  -9.293  1.00 40.03 ? 176 GLU A OE1   1 
ATOM   1304 O OE2   . GLU A 1 185 ? 11.002 16.291  -11.315 1.00 40.98 ? 176 GLU A OE2   1 
ATOM   1305 N N     . ALA A 1 186 ? 9.950  11.273  -8.598  1.00 18.17 ? 177 ALA A N     1 
ATOM   1306 C CA    . ALA A 1 186 ? 9.734  10.109  -9.444  1.00 17.49 ? 177 ALA A CA    1 
ATOM   1307 C C     . ALA A 1 186 ? 8.529  9.283   -9.009  1.00 17.10 ? 177 ALA A C     1 
ATOM   1308 O O     . ALA A 1 186 ? 8.110  8.389   -9.755  1.00 20.64 ? 177 ALA A O     1 
ATOM   1309 C CB    . ALA A 1 186 ? 10.992 9.219   -9.473  1.00 16.81 ? 177 ALA A CB    1 
ATOM   1310 N N     . GLY A 1 187 ? 7.984  9.524   -7.820  1.00 16.45 ? 178 GLY A N     1 
ATOM   1311 C CA    . GLY A 1 187 ? 6.826  8.798   -7.344  1.00 18.86 ? 178 GLY A CA    1 
ATOM   1312 C C     . GLY A 1 187 ? 7.114  7.734   -6.304  1.00 18.28 ? 178 GLY A C     1 
ATOM   1313 O O     . GLY A 1 187 ? 6.173  7.084   -5.837  1.00 17.53 ? 178 GLY A O     1 
ATOM   1314 N N     . PHE A 1 188 ? 8.379  7.539   -5.930  1.00 15.79 ? 179 PHE A N     1 
ATOM   1315 C CA    . PHE A 1 188 ? 8.708  6.611   -4.860  1.00 17.57 ? 179 PHE A CA    1 
ATOM   1316 C C     . PHE A 1 188 ? 7.901  6.951   -3.607  1.00 19.96 ? 179 PHE A C     1 
ATOM   1317 O O     . PHE A 1 188 ? 7.611  8.113   -3.336  1.00 16.62 ? 179 PHE A O     1 
ATOM   1318 C CB    . PHE A 1 188 ? 10.200 6.705   -4.560  1.00 14.59 ? 179 PHE A CB    1 
ATOM   1319 C CG    . PHE A 1 188 ? 11.036 5.939   -5.532  1.00 16.31 ? 179 PHE A CG    1 
ATOM   1320 C CD1   . PHE A 1 188 ? 11.118 4.553   -5.452  1.00 16.25 ? 179 PHE A CD1   1 
ATOM   1321 C CD2   . PHE A 1 188 ? 11.703 6.609   -6.538  1.00 17.30 ? 179 PHE A CD2   1 
ATOM   1322 C CE1   . PHE A 1 188 ? 11.898 3.840   -6.370  1.00 14.56 ? 179 PHE A CE1   1 
ATOM   1323 C CE2   . PHE A 1 188 ? 12.492 5.907   -7.468  1.00 15.43 ? 179 PHE A CE2   1 
ATOM   1324 C CZ    . PHE A 1 188 ? 12.562 4.518   -7.368  1.00 14.76 ? 179 PHE A CZ    1 
ATOM   1325 N N     . ASP A 1 189 ? 7.525  5.916   -2.856  1.00 15.18 ? 180 ASP A N     1 
ATOM   1326 C CA    . ASP A 1 189 ? 6.828  6.135   -1.585  1.00 15.06 ? 180 ASP A CA    1 
ATOM   1327 C C     . ASP A 1 189 ? 7.775  6.655   -0.507  1.00 19.15 ? 180 ASP A C     1 
ATOM   1328 O O     . ASP A 1 189 ? 7.342  7.333   0.438   1.00 18.86 ? 180 ASP A O     1 
ATOM   1329 C CB    . ASP A 1 189 ? 6.180  4.812   -1.178  1.00 14.88 ? 180 ASP A CB    1 
ATOM   1330 C CG    . ASP A 1 189 ? 5.170  4.364   -2.208  1.00 20.56 ? 180 ASP A CG    1 
ATOM   1331 O OD1   . ASP A 1 189 ? 4.158  5.099   -2.350  1.00 22.70 ? 180 ASP A OD1   1 
ATOM   1332 O OD2   . ASP A 1 189 ? 5.407  3.376   -2.940  1.00 17.42 ? 180 ASP A OD2   1 
ATOM   1333 N N     . GLY A 1 190 ? 9.061  6.345   -0.629  1.00 17.81 ? 181 GLY A N     1 
ATOM   1334 C CA    . GLY A 1 190 ? 10.044 6.822   0.324   1.00 12.75 ? 181 GLY A CA    1 
ATOM   1335 C C     . GLY A 1 190 ? 11.434 6.430   -0.142  1.00 14.29 ? 181 GLY A C     1 
ATOM   1336 O O     . GLY A 1 190 ? 11.631 5.973   -1.282  1.00 12.61 ? 181 GLY A O     1 
ATOM   1337 N N     . ILE A 1 191 ? 12.390 6.599   0.756   1.00 15.15 ? 182 ILE A N     1 
ATOM   1338 C CA    . ILE A 1 191 ? 13.797 6.298   0.473   1.00 10.45 ? 182 ILE A CA    1 
ATOM   1339 C C     . ILE A 1 191 ? 14.362 5.529   1.648   1.00 16.84 ? 182 ILE A C     1 
ATOM   1340 O O     . ILE A 1 191 ? 13.894 5.652   2.787   1.00 14.50 ? 182 ILE A O     1 
ATOM   1341 C CB    . ILE A 1 191 ? 14.640 7.564   0.190   1.00 14.85 ? 182 ILE A CB    1 
ATOM   1342 C CG1   . ILE A 1 191 ? 14.681 8.482   1.409   1.00 12.91 ? 182 ILE A CG1   1 
ATOM   1343 C CG2   . ILE A 1 191 ? 14.051 8.341   -0.975  1.00 14.06 ? 182 ILE A CG2   1 
ATOM   1344 C CD1   . ILE A 1 191 ? 15.918 8.267   2.244   1.00 16.28 ? 182 ILE A CD1   1 
ATOM   1345 N N     . GLU A 1 192 ? 15.389 4.727   1.379   1.00 13.15 ? 183 GLU A N     1 
ATOM   1346 C CA    . GLU A 1 192 ? 16.163 4.103   2.437   1.00 12.77 ? 183 GLU A CA    1 
ATOM   1347 C C     . GLU A 1 192 ? 17.578 4.671   2.410   1.00 14.21 ? 183 GLU A C     1 
ATOM   1348 O O     . GLU A 1 192 ? 18.218 4.695   1.363   1.00 14.04 ? 183 GLU A O     1 
ATOM   1349 C CB    . GLU A 1 192 ? 16.192 2.578   2.269   1.00 13.84 ? 183 GLU A CB    1 
ATOM   1350 C CG    . GLU A 1 192 ? 17.025 1.880   3.358   1.00 13.58 ? 183 GLU A CG    1 
ATOM   1351 C CD    . GLU A 1 192 ? 16.951 0.357   3.255   1.00 15.87 ? 183 GLU A CD    1 
ATOM   1352 O OE1   . GLU A 1 192 ? 15.965 -0.217  3.711   1.00 13.18 ? 183 GLU A OE1   1 
ATOM   1353 O OE2   . GLU A 1 192 ? 17.855 -0.280  2.683   1.00 15.28 ? 183 GLU A OE2   1 
ATOM   1354 N N     . ILE A 1 193 ? 18.101 5.038   3.568   1.00 13.41 ? 184 ILE A N     1 
ATOM   1355 C CA    . ILE A 1 193 ? 19.498 5.444   3.656   1.00 11.88 ? 184 ILE A CA    1 
ATOM   1356 C C     . ILE A 1 193 ? 20.377 4.199   3.758   1.00 14.49 ? 184 ILE A C     1 
ATOM   1357 O O     . ILE A 1 193 ? 20.278 3.455   4.739   1.00 15.33 ? 184 ILE A O     1 
ATOM   1358 C CB    . ILE A 1 193 ? 19.706 6.361   4.864   1.00 11.73 ? 184 ILE A CB    1 
ATOM   1359 C CG1   . ILE A 1 193 ? 18.924 7.682   4.699   1.00 12.38 ? 184 ILE A CG1   1 
ATOM   1360 C CG2   . ILE A 1 193 ? 21.190 6.587   5.104   1.00 15.09 ? 184 ILE A CG2   1 
ATOM   1361 C CD1   . ILE A 1 193 ? 19.329 8.470   3.423   1.00 13.73 ? 184 ILE A CD1   1 
ATOM   1362 N N     . HIS A 1 194 ? 21.269 3.992   2.781   1.00 13.67 ? 185 HIS A N     1 
ATOM   1363 C CA    . HIS A 1 194 ? 22.189 2.855   2.820   1.00 14.68 ? 185 HIS A CA    1 
ATOM   1364 C C     . HIS A 1 194 ? 23.316 3.187   3.778   1.00 14.04 ? 185 HIS A C     1 
ATOM   1365 O O     . HIS A 1 194 ? 24.274 3.863   3.405   1.00 15.28 ? 185 HIS A O     1 
ATOM   1366 C CB    . HIS A 1 194 ? 22.770 2.542   1.436   1.00 12.39 ? 185 HIS A CB    1 
ATOM   1367 C CG    . HIS A 1 194 ? 23.545 1.255   1.379   1.00 16.29 ? 185 HIS A CG    1 
ATOM   1368 N ND1   . HIS A 1 194 ? 24.112 0.648   2.487   1.00 15.45 ? 185 HIS A ND1   1 
ATOM   1369 C CD2   . HIS A 1 194 ? 23.805 0.436   0.332   1.00 13.12 ? 185 HIS A CD2   1 
ATOM   1370 C CE1   . HIS A 1 194 ? 24.672 -0.499  2.120   1.00 12.81 ? 185 HIS A CE1   1 
ATOM   1371 N NE2   . HIS A 1 194 ? 24.536 -0.624  0.812   1.00 15.06 ? 185 HIS A NE2   1 
ATOM   1372 N N     . GLY A 1 195 ? 23.250 2.677   4.998   1.00 11.18 ? 186 GLY A N     1 
ATOM   1373 C CA    . GLY A 1 195 ? 24.331 2.979   5.916   1.00 12.68 ? 186 GLY A CA    1 
ATOM   1374 C C     . GLY A 1 195 ? 25.088 1.734   6.341   1.00 14.88 ? 186 GLY A C     1 
ATOM   1375 O O     . GLY A 1 195 ? 25.655 1.681   7.448   1.00 15.82 ? 186 GLY A O     1 
ATOM   1376 N N     . ALA A 1 196 ? 25.148 0.752   5.434   1.00 13.69 ? 187 ALA A N     1 
ATOM   1377 C CA    . ALA A 1 196 ? 25.628 -0.592  5.756   1.00 12.38 ? 187 ALA A CA    1 
ATOM   1378 C C     . ALA A 1 196 ? 26.873 -0.931  4.917   1.00 13.16 ? 187 ALA A C     1 
ATOM   1379 O O     . ALA A 1 196 ? 27.279 -0.160  4.057   1.00 12.86 ? 187 ALA A O     1 
ATOM   1380 C CB    . ALA A 1 196 ? 24.501 -1.597  5.503   1.00 14.37 ? 187 ALA A CB    1 
ATOM   1381 N N     . HIS A 1 197 ? 27.452 -2.117  5.189   1.00 13.69 ? 188 HIS A N     1 
ATOM   1382 C CA    . HIS A 1 197 ? 28.338 -2.862  4.283   1.00 16.00 ? 188 HIS A CA    1 
ATOM   1383 C C     . HIS A 1 197 ? 29.641 -2.148  3.970   1.00 15.76 ? 188 HIS A C     1 
ATOM   1384 O O     . HIS A 1 197 ? 30.230 -2.384  2.913   1.00 13.96 ? 188 HIS A O     1 
ATOM   1385 C CB    . HIS A 1 197 ? 27.620 -3.212  2.973   1.00 13.59 ? 188 HIS A CB    1 
ATOM   1386 C CG    . HIS A 1 197 ? 26.429 -4.092  3.162   1.00 14.27 ? 188 HIS A CG    1 
ATOM   1387 N ND1   . HIS A 1 197 ? 25.229 -3.875  2.518   1.00 16.45 ? 188 HIS A ND1   1 
ATOM   1388 C CD2   . HIS A 1 197 ? 26.240 -5.181  3.948   1.00 16.46 ? 188 HIS A CD2   1 
ATOM   1389 C CE1   . HIS A 1 197 ? 24.363 -4.810  2.871   1.00 18.25 ? 188 HIS A CE1   1 
ATOM   1390 N NE2   . HIS A 1 197 ? 24.955 -5.622  3.733   1.00 18.92 ? 188 HIS A NE2   1 
ATOM   1391 N N     . GLY A 1 198 ? 30.096 -1.279  4.865   1.00 12.30 ? 189 GLY A N     1 
ATOM   1392 C CA    . GLY A 1 198 ? 31.371 -0.610  4.688   1.00 14.34 ? 189 GLY A CA    1 
ATOM   1393 C C     . GLY A 1 198 ? 31.404 0.445   3.619   1.00 14.19 ? 189 GLY A C     1 
ATOM   1394 O O     . GLY A 1 198 ? 32.495 0.847   3.180   1.00 13.05 ? 189 GLY A O     1 
ATOM   1395 N N     . TYR A 1 199 ? 30.252 0.927   3.201   1.00 11.33 ? 190 TYR A N     1 
ATOM   1396 C CA    . TYR A 1 199 ? 30.198 2.075   2.295   1.00 13.39 ? 190 TYR A CA    1 
ATOM   1397 C C     . TYR A 1 199 ? 30.333 3.408   3.063   1.00 13.51 ? 190 TYR A C     1 
ATOM   1398 O O     . TYR A 1 199 ? 30.793 3.410   4.206   1.00 13.39 ? 190 TYR A O     1 
ATOM   1399 C CB    . TYR A 1 199 ? 28.909 1.937   1.473   1.00 10.72 ? 190 TYR A CB    1 
ATOM   1400 C CG    . TYR A 1 199 ? 29.015 0.716   0.547   1.00 12.92 ? 190 TYR A CG    1 
ATOM   1401 C CD1   . TYR A 1 199 ? 30.046 0.617   -0.379  1.00 15.60 ? 190 TYR A CD1   1 
ATOM   1402 C CD2   . TYR A 1 199 ? 28.111 -0.352  0.631   1.00 11.97 ? 190 TYR A CD2   1 
ATOM   1403 C CE1   . TYR A 1 199 ? 30.160 -0.535  -1.210  1.00 13.41 ? 190 TYR A CE1   1 
ATOM   1404 C CE2   . TYR A 1 199 ? 28.206 -1.461  -0.198  1.00 15.19 ? 190 TYR A CE2   1 
ATOM   1405 C CZ    . TYR A 1 199 ? 29.228 -1.543  -1.117  1.00 15.65 ? 190 TYR A CZ    1 
ATOM   1406 O OH    . TYR A 1 199 ? 29.285 -2.670  -1.933  1.00 14.51 ? 190 TYR A OH    1 
ATOM   1407 N N     . LEU A 1 200 ? 29.996 4.548   2.445   1.00 13.47 ? 191 LEU A N     1 
ATOM   1408 C CA    . LEU A 1 200 ? 30.486 5.835   2.955   1.00 13.39 ? 191 LEU A CA    1 
ATOM   1409 C C     . LEU A 1 200 ? 30.010 6.077   4.386   1.00 12.50 ? 191 LEU A C     1 
ATOM   1410 O O     . LEU A 1 200 ? 30.807 6.420   5.266   1.00 14.28 ? 191 LEU A O     1 
ATOM   1411 C CB    . LEU A 1 200 ? 30.048 6.970   2.011   1.00 15.68 ? 191 LEU A CB    1 
ATOM   1412 C CG    . LEU A 1 200 ? 30.439 8.358   2.587   1.00 18.49 ? 191 LEU A CG    1 
ATOM   1413 C CD1   . LEU A 1 200 ? 31.974 8.564   2.660   1.00 14.37 ? 191 LEU A CD1   1 
ATOM   1414 C CD2   . LEU A 1 200 ? 29.800 9.477   1.765   1.00 14.44 ? 191 LEU A CD2   1 
ATOM   1415 N N     . ILE A 1 201 ? 28.713 5.849   4.660   1.00 12.93 ? 192 ILE A N     1 
ATOM   1416 C CA    . ILE A 1 201 ? 28.215 6.095   6.014   1.00 14.50 ? 192 ILE A CA    1 
ATOM   1417 C C     . ILE A 1 201 ? 28.881 5.156   7.025   1.00 13.41 ? 192 ILE A C     1 
ATOM   1418 O O     . ILE A 1 201 ? 29.325 5.582   8.098   1.00 13.11 ? 192 ILE A O     1 
ATOM   1419 C CB    . ILE A 1 201 ? 26.675 5.979   6.052   1.00 12.05 ? 192 ILE A CB    1 
ATOM   1420 C CG1   . ILE A 1 201 ? 26.074 7.177   5.310   1.00 15.50 ? 192 ILE A CG1   1 
ATOM   1421 C CG2   . ILE A 1 201 ? 26.226 5.966   7.525   1.00 13.41 ? 192 ILE A CG2   1 
ATOM   1422 C CD1   . ILE A 1 201 ? 24.542 7.028   5.020   1.00 17.43 ? 192 ILE A CD1   1 
ATOM   1423 N N     . ASP A 1 202 ? 29.057 3.891   6.652   1.00 14.68 ? 193 ASP A N     1 
ATOM   1424 C CA    . ASP A 1 202 ? 29.721 2.937   7.540   1.00 14.59 ? 193 ASP A CA    1 
ATOM   1425 C C     . ASP A 1 202 ? 31.197 3.293   7.731   1.00 15.42 ? 193 ASP A C     1 
ATOM   1426 O O     . ASP A 1 202 ? 31.787 2.996   8.785   1.00 15.89 ? 193 ASP A O     1 
ATOM   1427 C CB    . ASP A 1 202 ? 29.569 1.531   6.948   1.00 16.69 ? 193 ASP A CB    1 
ATOM   1428 C CG    . ASP A 1 202 ? 29.420 0.458   8.010   1.00 19.52 ? 193 ASP A CG    1 
ATOM   1429 O OD1   . ASP A 1 202 ? 29.005 0.795   9.137   1.00 16.36 ? 193 ASP A OD1   1 
ATOM   1430 O OD2   . ASP A 1 202 ? 29.707 -0.729  7.714   1.00 21.52 ? 193 ASP A OD2   1 
ATOM   1431 N N     . GLN A 1 203 ? 31.802 3.963   6.752   1.00 12.71 ? 194 GLN A N     1 
ATOM   1432 C CA    . GLN A 1 203 ? 33.184 4.415   6.915   1.00 13.40 ? 194 GLN A CA    1 
ATOM   1433 C C     . GLN A 1 203 ? 33.319 5.517   7.961   1.00 17.10 ? 194 GLN A C     1 
ATOM   1434 O O     . GLN A 1 203 ? 34.411 5.680   8.523   1.00 15.25 ? 194 GLN A O     1 
ATOM   1435 C CB    . GLN A 1 203 ? 33.770 4.879   5.564   1.00 14.06 ? 194 GLN A CB    1 
ATOM   1436 C CG    . GLN A 1 203 ? 33.944 3.741   4.567   1.00 11.20 ? 194 GLN A CG    1 
ATOM   1437 C CD    . GLN A 1 203 ? 33.800 4.249   3.132   1.00 13.72 ? 194 GLN A CD    1 
ATOM   1438 O OE1   . GLN A 1 203 ? 34.279 5.353   2.794   1.00 13.28 ? 194 GLN A OE1   1 
ATOM   1439 N NE2   . GLN A 1 203 ? 33.234 3.415   2.262   1.00 14.30 ? 194 GLN A NE2   1 
ATOM   1440 N N     . PHE A 1 204 ? 32.239 6.268   8.245   1.00 14.18 ? 195 PHE A N     1 
ATOM   1441 C CA    . PHE A 1 204 ? 32.223 7.179   9.395   1.00 14.97 ? 195 PHE A CA    1 
ATOM   1442 C C     . PHE A 1 204 ? 31.849 6.450   10.689  1.00 13.31 ? 195 PHE A C     1 
ATOM   1443 O O     . PHE A 1 204 ? 32.383 6.768   11.752  1.00 15.69 ? 195 PHE A O     1 
ATOM   1444 C CB    . PHE A 1 204 ? 31.251 8.327   9.131   1.00 15.18 ? 195 PHE A CB    1 
ATOM   1445 C CG    . PHE A 1 204 ? 31.841 9.431   8.291   1.00 16.76 ? 195 PHE A CG    1 
ATOM   1446 C CD1   . PHE A 1 204 ? 31.824 9.316   6.915   1.00 13.77 ? 195 PHE A CD1   1 
ATOM   1447 C CD2   . PHE A 1 204 ? 32.450 10.548  8.872   1.00 17.73 ? 195 PHE A CD2   1 
ATOM   1448 C CE1   . PHE A 1 204 ? 32.358 10.296  6.115   1.00 16.14 ? 195 PHE A CE1   1 
ATOM   1449 C CE2   . PHE A 1 204 ? 32.997 11.533  8.093   1.00 21.03 ? 195 PHE A CE2   1 
ATOM   1450 C CZ    . PHE A 1 204 ? 32.961 11.402  6.681   1.00 20.01 ? 195 PHE A CZ    1 
ATOM   1451 N N     . LEU A 1 205 ? 30.935 5.475   10.618  1.00 15.78 ? 196 LEU A N     1 
ATOM   1452 C CA    . LEU A 1 205 ? 30.453 4.792   11.836  1.00 13.19 ? 196 LEU A CA    1 
ATOM   1453 C C     . LEU A 1 205 ? 31.525 3.918   12.479  1.00 18.02 ? 196 LEU A C     1 
ATOM   1454 O O     . LEU A 1 205 ? 31.659 3.902   13.712  1.00 16.03 ? 196 LEU A O     1 
ATOM   1455 C CB    . LEU A 1 205 ? 29.237 3.931   11.481  1.00 11.31 ? 196 LEU A CB    1 
ATOM   1456 C CG    . LEU A 1 205 ? 27.881 4.546   11.248  1.00 12.42 ? 196 LEU A CG    1 
ATOM   1457 C CD1   . LEU A 1 205 ? 26.915 3.433   10.850  1.00 14.45 ? 196 LEU A CD1   1 
ATOM   1458 C CD2   . LEU A 1 205 ? 27.353 5.293   12.532  1.00 13.60 ? 196 LEU A CD2   1 
ATOM   1459 N N     . LYS A 1 206 ? 32.255 3.135   11.690  1.00 17.85 ? 197 LYS A N     1 
ATOM   1460 C CA    . LYS A 1 206 ? 33.081 2.082   12.279  1.00 19.15 ? 197 LYS A CA    1 
ATOM   1461 C C     . LYS A 1 206 ? 34.431 2.622   12.750  1.00 18.03 ? 197 LYS A C     1 
ATOM   1462 O O     . LYS A 1 206 ? 35.110 3.347   12.026  1.00 17.74 ? 197 LYS A O     1 
ATOM   1463 C CB    . LYS A 1 206 ? 33.284 0.930   11.289  1.00 17.51 ? 197 LYS A CB    1 
ATOM   1464 C CG    . LYS A 1 206 ? 31.956 0.343   10.792  1.00 22.46 ? 197 LYS A CG    1 
ATOM   1465 C CD    . LYS A 1 206 ? 31.424 -0.713  11.736  1.00 22.52 ? 197 LYS A CD    1 
ATOM   1466 C CE    . LYS A 1 206 ? 30.043 -1.218  11.327  1.00 22.10 ? 197 LYS A CE    1 
ATOM   1467 N NZ    . LYS A 1 206 ? 30.163 -2.235  10.203  1.00 23.92 ? 197 LYS A NZ    1 
ATOM   1468 N N     . ASP A 1 207 ? 34.850 2.227   13.952  1.00 19.47 ? 198 ASP A N     1 
ATOM   1469 C CA    . ASP A 1 207 ? 36.144 2.735   14.417  1.00 21.63 ? 198 ASP A CA    1 
ATOM   1470 C C     . ASP A 1 207 ? 37.322 1.981   13.809  1.00 17.69 ? 198 ASP A C     1 
ATOM   1471 O O     . ASP A 1 207 ? 38.467 2.440   13.934  1.00 23.59 ? 198 ASP A O     1 
ATOM   1472 C CB    . ASP A 1 207 ? 36.238 2.739   15.960  1.00 21.84 ? 198 ASP A CB    1 
ATOM   1473 C CG    . ASP A 1 207 ? 36.114 1.358   16.594  1.00 22.79 ? 198 ASP A CG    1 
ATOM   1474 O OD1   . ASP A 1 207 ? 36.007 0.337   15.912  1.00 21.34 ? 198 ASP A OD1   1 
ATOM   1475 O OD2   . ASP A 1 207 ? 36.125 1.299   17.854  1.00 29.05 ? 198 ASP A OD2   1 
ATOM   1476 N N     . GLY A 1 208 ? 37.069 0.863   13.133  1.00 20.51 ? 199 GLY A N     1 
ATOM   1477 C CA    . GLY A 1 208 ? 38.095 0.258   12.312  1.00 21.82 ? 199 GLY A CA    1 
ATOM   1478 C C     . GLY A 1 208 ? 38.460 1.061   11.081  1.00 25.79 ? 199 GLY A C     1 
ATOM   1479 O O     . GLY A 1 208 ? 39.474 0.751   10.440  1.00 25.15 ? 199 GLY A O     1 
ATOM   1480 N N     . ILE A 1 209 ? 37.648 2.055   10.711  1.00 18.87 ? 200 ILE A N     1 
ATOM   1481 C CA    . ILE A 1 209 ? 37.886 2.875   9.526   1.00 17.94 ? 200 ILE A CA    1 
ATOM   1482 C C     . ILE A 1 209 ? 38.109 4.328   9.904   1.00 20.89 ? 200 ILE A C     1 
ATOM   1483 O O     . ILE A 1 209 ? 39.065 4.973   9.457   1.00 25.31 ? 200 ILE A O     1 
ATOM   1484 C CB    . ILE A 1 209 ? 36.720 2.763   8.510   1.00 19.04 ? 200 ILE A CB    1 
ATOM   1485 C CG1   . ILE A 1 209 ? 36.517 1.308   8.034   1.00 21.31 ? 200 ILE A CG1   1 
ATOM   1486 C CG2   . ILE A 1 209 ? 36.950 3.763   7.347   1.00 18.99 ? 200 ILE A CG2   1 
ATOM   1487 C CD1   . ILE A 1 209 ? 35.271 1.067   7.112   1.00 14.38 ? 200 ILE A CD1   1 
ATOM   1488 N N     . ASN A 1 210 ? 37.228 4.865   10.720  1.00 19.32 ? 201 ASN A N     1 
ATOM   1489 C CA    . ASN A 1 210 ? 37.190 6.284   11.007  1.00 19.84 ? 201 ASN A CA    1 
ATOM   1490 C C     . ASN A 1 210 ? 38.313 6.590   12.000  1.00 22.50 ? 201 ASN A C     1 
ATOM   1491 O O     . ASN A 1 210 ? 38.194 6.331   13.203  1.00 24.52 ? 201 ASN A O     1 
ATOM   1492 C CB    . ASN A 1 210 ? 35.802 6.646   11.511  1.00 17.38 ? 201 ASN A CB    1 
ATOM   1493 C CG    . ASN A 1 210 ? 35.651 8.121   11.794  1.00 20.50 ? 201 ASN A CG    1 
ATOM   1494 O OD1   . ASN A 1 210 ? 36.633 8.846   11.911  1.00 22.43 ? 201 ASN A OD1   1 
ATOM   1495 N ND2   . ASN A 1 210 ? 34.423 8.570   11.904  1.00 15.48 ? 201 ASN A ND2   1 
ATOM   1496 N N     . ASP A 1 211 ? 39.411 7.144   11.474  1.00 23.80 ? 202 ASP A N     1 
ATOM   1497 C CA    . ASP A 1 211 ? 40.544 7.628   12.256  1.00 26.75 ? 202 ASP A CA    1 
ATOM   1498 C C     . ASP A 1 211 ? 40.613 9.158   12.309  1.00 28.22 ? 202 ASP A C     1 
ATOM   1499 O O     . ASP A 1 211 ? 41.700 9.729   12.471  1.00 26.75 ? 202 ASP A O     1 
ATOM   1500 C CB    . ASP A 1 211 ? 41.853 7.051   11.696  1.00 24.56 ? 202 ASP A CB    1 
ATOM   1501 C CG    . ASP A 1 211 ? 42.077 7.376   10.194  1.00 30.76 ? 202 ASP A CG    1 
ATOM   1502 O OD1   . ASP A 1 211 ? 41.219 8.009   9.520   1.00 26.16 ? 202 ASP A OD1   1 
ATOM   1503 O OD2   . ASP A 1 211 ? 43.130 6.948   9.666   1.00 31.59 ? 202 ASP A OD2   1 
ATOM   1504 N N     . ARG A 1 212 ? 39.468 9.839   12.196  1.00 22.21 ? 203 ARG A N     1 
ATOM   1505 C CA    . ARG A 1 212 ? 39.450 11.303  12.218  1.00 22.74 ? 203 ARG A CA    1 
ATOM   1506 C C     . ARG A 1 212 ? 39.692 11.871  13.615  1.00 22.41 ? 203 ARG A C     1 
ATOM   1507 O O     . ARG A 1 212 ? 39.345 11.267  14.629  1.00 23.84 ? 203 ARG A O     1 
ATOM   1508 C CB    . ARG A 1 212 ? 38.105 11.822  11.721  1.00 19.83 ? 203 ARG A CB    1 
ATOM   1509 C CG    . ARG A 1 212 ? 37.737 11.355  10.303  1.00 17.92 ? 203 ARG A CG    1 
ATOM   1510 C CD    . ARG A 1 212 ? 36.329 11.830  9.961   1.00 20.81 ? 203 ARG A CD    1 
ATOM   1511 N NE    . ARG A 1 212 ? 36.287 13.277  9.730   1.00 18.28 ? 203 ARG A NE    1 
ATOM   1512 C CZ    . ARG A 1 212 ? 36.385 13.846  8.535   1.00 17.32 ? 203 ARG A CZ    1 
ATOM   1513 N NH1   . ARG A 1 212 ? 36.625 13.126  7.436   1.00 16.15 ? 203 ARG A NH1   1 
ATOM   1514 N NH2   . ARG A 1 212 ? 36.227 15.164  8.436   1.00 19.82 ? 203 ARG A NH2   1 
ATOM   1515 N N     . THR A 1 213 ? 40.229 13.093  13.653  1.00 23.93 ? 204 THR A N     1 
ATOM   1516 C CA    . THR A 1 213 ? 40.478 13.804  14.902  1.00 23.06 ? 204 THR A CA    1 
ATOM   1517 C C     . THR A 1 213 ? 39.654 15.083  14.988  1.00 27.78 ? 204 THR A C     1 
ATOM   1518 O O     . THR A 1 213 ? 39.969 15.981  15.774  1.00 27.46 ? 204 THR A O     1 
ATOM   1519 C CB    . THR A 1 213 ? 41.964 14.135  15.064  1.00 26.49 ? 204 THR A CB    1 
ATOM   1520 O OG1   . THR A 1 213 ? 42.421 14.868  13.918  1.00 29.48 ? 204 THR A OG1   1 
ATOM   1521 C CG2   . THR A 1 213 ? 42.777 12.874  15.235  1.00 30.17 ? 204 THR A CG2   1 
ATOM   1522 N N     . ASP A 1 214 ? 38.620 15.202  14.177  1.00 25.16 ? 205 ASP A N     1 
ATOM   1523 C CA    . ASP A 1 214 ? 37.775 16.364  14.276  1.00 20.59 ? 205 ASP A CA    1 
ATOM   1524 C C     . ASP A 1 214 ? 36.455 15.916  14.890  1.00 21.78 ? 205 ASP A C     1 
ATOM   1525 O O     . ASP A 1 214 ? 36.365 14.819  15.483  1.00 22.33 ? 205 ASP A O     1 
ATOM   1526 C CB    . ASP A 1 214 ? 37.636 17.014  12.890  1.00 18.03 ? 205 ASP A CB    1 
ATOM   1527 C CG    . ASP A 1 214 ? 36.866 16.157  11.887  1.00 21.69 ? 205 ASP A CG    1 
ATOM   1528 O OD1   . ASP A 1 214 ? 36.548 14.982  12.165  1.00 18.14 ? 205 ASP A OD1   1 
ATOM   1529 O OD2   . ASP A 1 214 ? 36.558 16.698  10.798  1.00 22.19 ? 205 ASP A OD2   1 
ATOM   1530 N N     . GLU A 1 215 ? 35.429 16.728  14.724  1.00 17.95 ? 206 GLU A N     1 
ATOM   1531 C CA    . GLU A 1 215 ? 34.154 16.428  15.359  1.00 22.84 ? 206 GLU A CA    1 
ATOM   1532 C C     . GLU A 1 215 ? 33.402 15.262  14.720  1.00 21.59 ? 206 GLU A C     1 
ATOM   1533 O O     . GLU A 1 215 ? 32.319 14.903  15.221  1.00 19.75 ? 206 GLU A O     1 
ATOM   1534 C CB    . GLU A 1 215 ? 33.300 17.692  15.384  1.00 24.79 ? 206 GLU A CB    1 
ATOM   1535 C CG    . GLU A 1 215 ? 32.770 18.072  14.075  1.00 23.70 ? 206 GLU A CG    1 
ATOM   1536 C CD    . GLU A 1 215 ? 33.595 19.193  13.454  1.00 34.55 ? 206 GLU A CD    1 
ATOM   1537 O OE1   . GLU A 1 215 ? 34.850 19.186  13.616  1.00 32.16 ? 206 GLU A OE1   1 
ATOM   1538 O OE2   . GLU A 1 215 ? 32.992 20.099  12.817  1.00 37.92 ? 206 GLU A OE2   1 
ATOM   1539 N N     . TYR A 1 216 ? 33.952 14.627  13.682  1.00 19.36 ? 207 TYR A N     1 
ATOM   1540 C CA    . TYR A 1 216 ? 33.308 13.462  13.083  1.00 18.37 ? 207 TYR A CA    1 
ATOM   1541 C C     . TYR A 1 216 ? 34.002 12.165  13.454  1.00 18.94 ? 207 TYR A C     1 
ATOM   1542 O O     . TYR A 1 216 ? 33.655 11.099  12.915  1.00 20.51 ? 207 TYR A O     1 
ATOM   1543 C CB    . TYR A 1 216 ? 33.229 13.632  11.550  1.00 14.88 ? 207 TYR A CB    1 
ATOM   1544 C CG    . TYR A 1 216 ? 32.169 14.616  11.156  1.00 16.50 ? 207 TYR A CG    1 
ATOM   1545 C CD1   . TYR A 1 216 ? 32.430 15.979  11.143  1.00 21.26 ? 207 TYR A CD1   1 
ATOM   1546 C CD2   . TYR A 1 216 ? 30.881 14.182  10.830  1.00 18.28 ? 207 TYR A CD2   1 
ATOM   1547 C CE1   . TYR A 1 216 ? 31.435 16.903  10.789  1.00 20.68 ? 207 TYR A CE1   1 
ATOM   1548 C CE2   . TYR A 1 216 ? 29.903 15.069  10.501  1.00 20.01 ? 207 TYR A CE2   1 
ATOM   1549 C CZ    . TYR A 1 216 ? 30.175 16.433  10.478  1.00 21.39 ? 207 TYR A CZ    1 
ATOM   1550 O OH    . TYR A 1 216 ? 29.166 17.296  10.109  1.00 20.63 ? 207 TYR A OH    1 
ATOM   1551 N N     . GLY A 1 217 ? 34.985 12.215  14.356  1.00 21.70 ? 208 GLY A N     1 
ATOM   1552 C CA    . GLY A 1 217 ? 35.701 11.012  14.721  1.00 19.02 ? 208 GLY A CA    1 
ATOM   1553 C C     . GLY A 1 217 ? 35.998 10.945  16.203  1.00 20.79 ? 208 GLY A C     1 
ATOM   1554 O O     . GLY A 1 217 ? 35.853 11.917  16.933  1.00 23.74 ? 208 GLY A O     1 
ATOM   1555 N N     . GLY A 1 218 ? 36.429 9.752   16.618  1.00 23.67 ? 209 GLY A N     1 
ATOM   1556 C CA    . GLY A 1 218 ? 36.786 9.485   17.993  1.00 28.29 ? 209 GLY A CA    1 
ATOM   1557 C C     . GLY A 1 218 ? 35.616 8.828   18.688  1.00 30.55 ? 209 GLY A C     1 
ATOM   1558 O O     . GLY A 1 218 ? 35.326 7.650   18.431  1.00 30.53 ? 209 GLY A O     1 
ATOM   1559 N N     . SER A 1 219 ? 34.894 9.610   19.497  1.00 25.41 ? 210 SER A N     1 
ATOM   1560 C CA    . SER A 1 219 ? 33.790 9.095   20.299  1.00 23.18 ? 210 SER A CA    1 
ATOM   1561 C C     . SER A 1 219 ? 32.699 8.507   19.423  1.00 27.12 ? 210 SER A C     1 
ATOM   1562 O O     . SER A 1 219 ? 32.598 8.788   18.212  1.00 21.53 ? 210 SER A O     1 
ATOM   1563 C CB    . SER A 1 219 ? 33.164 10.193  21.153  1.00 23.33 ? 210 SER A CB    1 
ATOM   1564 O OG    . SER A 1 219 ? 32.664 11.240  20.333  1.00 22.66 ? 210 SER A OG    1 
ATOM   1565 N N     . LEU A 1 220 ? 31.877 7.679   20.073  1.00 25.19 ? 211 LEU A N     1 
ATOM   1566 C CA    . LEU A 1 220 ? 30.635 7.162   19.506  1.00 23.83 ? 211 LEU A CA    1 
ATOM   1567 C C     . LEU A 1 220 ? 29.788 8.291   18.928  1.00 23.16 ? 211 LEU A C     1 
ATOM   1568 O O     . LEU A 1 220 ? 29.348 8.227   17.767  1.00 19.32 ? 211 LEU A O     1 
ATOM   1569 C CB    . LEU A 1 220 ? 29.893 6.422   20.629  1.00 30.27 ? 211 LEU A CB    1 
ATOM   1570 C CG    . LEU A 1 220 ? 30.139 4.928   20.732  1.00 28.70 ? 211 LEU A CG    1 
ATOM   1571 C CD1   . LEU A 1 220 ? 29.215 4.246   21.802  1.00 18.74 ? 211 LEU A CD1   1 
ATOM   1572 C CD2   . LEU A 1 220 ? 29.940 4.314   19.330  1.00 32.36 ? 211 LEU A CD2   1 
ATOM   1573 N N     . ALA A 1 221 ? 29.579 9.356   19.728  1.00 23.96 ? 212 ALA A N     1 
ATOM   1574 C CA    . ALA A 1 221 ? 28.765 10.481  19.281  1.00 21.70 ? 212 ALA A CA    1 
ATOM   1575 C C     . ALA A 1 221 ? 29.331 11.100  18.012  1.00 21.04 ? 212 ALA A C     1 
ATOM   1576 O O     . ALA A 1 221 ? 28.589 11.429  17.088  1.00 20.91 ? 212 ALA A O     1 
ATOM   1577 C CB    . ALA A 1 221 ? 28.682 11.555  20.380  1.00 24.86 ? 212 ALA A CB    1 
ATOM   1578 N N     . ASN A 1 222 ? 30.647 11.299  17.964  1.00 19.59 ? 213 ASN A N     1 
ATOM   1579 C CA    . ASN A 1 222 ? 31.222 11.932  16.800  1.00 19.61 ? 213 ASN A CA    1 
ATOM   1580 C C     . ASN A 1 222 ? 31.084 11.023  15.585  1.00 17.24 ? 213 ASN A C     1 
ATOM   1581 O O     . ASN A 1 222 ? 30.775 11.492  14.486  1.00 16.91 ? 213 ASN A O     1 
ATOM   1582 C CB    . ASN A 1 222 ? 32.684 12.282  17.066  1.00 20.06 ? 213 ASN A CB    1 
ATOM   1583 C CG    . ASN A 1 222 ? 32.837 13.495  17.969  1.00 23.28 ? 213 ASN A CG    1 
ATOM   1584 O OD1   . ASN A 1 222 ? 31.836 14.051  18.432  1.00 22.05 ? 213 ASN A OD1   1 
ATOM   1585 N ND2   . ASN A 1 222 ? 34.088 13.910  18.229  1.00 21.25 ? 213 ASN A ND2   1 
ATOM   1586 N N     . ARG A 1 223 ? 31.277 9.718   15.780  1.00 17.09 ? 214 ARG A N     1 
ATOM   1587 C CA    . ARG A 1 223 ? 31.151 8.802   14.648  1.00 17.63 ? 214 ARG A CA    1 
ATOM   1588 C C     . ARG A 1 223 ? 29.721 8.653   14.186  1.00 14.55 ? 214 ARG A C     1 
ATOM   1589 O O     . ARG A 1 223 ? 29.504 8.374   12.998  1.00 19.19 ? 214 ARG A O     1 
ATOM   1590 C CB    . ARG A 1 223 ? 31.769 7.457   15.001  1.00 18.65 ? 214 ARG A CB    1 
ATOM   1591 C CG    . ARG A 1 223 ? 33.266 7.625   15.074  1.00 20.94 ? 214 ARG A CG    1 
ATOM   1592 C CD    . ARG A 1 223 ? 34.018 6.457   15.653  1.00 29.44 ? 214 ARG A CD    1 
ATOM   1593 N NE    . ARG A 1 223 ? 33.275 5.210   15.706  1.00 34.85 ? 214 ARG A NE    1 
ATOM   1594 C CZ    . ARG A 1 223 ? 33.123 4.497   16.813  1.00 29.66 ? 214 ARG A CZ    1 
ATOM   1595 N NH1   . ARG A 1 223 ? 33.589 4.920   17.976  1.00 32.84 ? 214 ARG A NH1   1 
ATOM   1596 N NH2   . ARG A 1 223 ? 32.485 3.333   16.754  1.00 26.11 ? 214 ARG A NH2   1 
ATOM   1597 N N     . CYS A 1 224 ? 28.742 8.910   15.051  1.00 16.61 ? 215 CYS A N     1 
ATOM   1598 C CA    . CYS A 1 224 ? 27.361 8.872   14.604  1.00 18.03 ? 215 CYS A CA    1 
ATOM   1599 C C     . CYS A 1 224 ? 26.882 10.187  14.011  1.00 17.21 ? 215 CYS A C     1 
ATOM   1600 O O     . CYS A 1 224 ? 25.746 10.241  13.525  1.00 16.39 ? 215 CYS A O     1 
ATOM   1601 C CB    . CYS A 1 224 ? 26.453 8.472   15.756  1.00 17.18 ? 215 CYS A CB    1 
ATOM   1602 S SG    . CYS A 1 224 ? 26.755 6.775   16.282  1.00 22.85 ? 215 CYS A SG    1 
ATOM   1603 N N     . LYS A 1 225 ? 27.721 11.227  14.010  1.00 16.58 ? 216 LYS A N     1 
ATOM   1604 C CA    . LYS A 1 225 ? 27.291 12.534  13.508  1.00 12.91 ? 216 LYS A CA    1 
ATOM   1605 C C     . LYS A 1 225 ? 26.884 12.465  12.046  1.00 16.29 ? 216 LYS A C     1 
ATOM   1606 O O     . LYS A 1 225 ? 25.847 13.016  11.654  1.00 16.15 ? 216 LYS A O     1 
ATOM   1607 C CB    . LYS A 1 225 ? 28.416 13.550  13.689  1.00 20.71 ? 216 LYS A CB    1 
ATOM   1608 C CG    . LYS A 1 225 ? 28.024 15.018  13.514  1.00 26.15 ? 216 LYS A CG    1 
ATOM   1609 C CD    . LYS A 1 225 ? 29.073 15.952  14.203  1.00 27.44 ? 216 LYS A CD    1 
ATOM   1610 C CE    . LYS A 1 225 ? 28.949 15.898  15.739  1.00 33.16 ? 216 LYS A CE    1 
ATOM   1611 N NZ    . LYS A 1 225 ? 30.188 16.230  16.528  1.00 30.67 ? 216 LYS A NZ    1 
ATOM   1612 N N     . PHE A 1 226 ? 27.726 11.852  11.208  1.00 13.96 ? 217 PHE A N     1 
ATOM   1613 C CA    . PHE A 1 226 ? 27.415 11.813  9.776   1.00 16.13 ? 217 PHE A CA    1 
ATOM   1614 C C     . PHE A 1 226 ? 26.044 11.181  9.513   1.00 15.29 ? 217 PHE A C     1 
ATOM   1615 O O     . PHE A 1 226 ? 25.201 11.769  8.821   1.00 14.91 ? 217 PHE A O     1 
ATOM   1616 C CB    . PHE A 1 226 ? 28.492 11.065  8.991   1.00 17.41 ? 217 PHE A CB    1 
ATOM   1617 C CG    . PHE A 1 226 ? 28.324 11.187  7.490   1.00 18.07 ? 217 PHE A CG    1 
ATOM   1618 C CD1   . PHE A 1 226 ? 28.247 12.414  6.894   1.00 19.49 ? 217 PHE A CD1   1 
ATOM   1619 C CD2   . PHE A 1 226 ? 28.202 10.058  6.686   1.00 15.38 ? 217 PHE A CD2   1 
ATOM   1620 C CE1   . PHE A 1 226 ? 28.092 12.534  5.507   1.00 21.16 ? 217 PHE A CE1   1 
ATOM   1621 C CE2   . PHE A 1 226 ? 28.039 10.179  5.298   1.00 13.23 ? 217 PHE A CE2   1 
ATOM   1622 C CZ    . PHE A 1 226 ? 28.009 11.414  4.718   1.00 15.20 ? 217 PHE A CZ    1 
ATOM   1623 N N     . ILE A 1 227 ? 25.785 9.994   10.066  1.00 14.75 ? 218 ILE A N     1 
ATOM   1624 C CA    . ILE A 1 227 ? 24.521 9.329   9.724   1.00 12.64 ? 218 ILE A CA    1 
ATOM   1625 C C     . ILE A 1 227 ? 23.352 10.140  10.255  1.00 14.60 ? 218 ILE A C     1 
ATOM   1626 O O     . ILE A 1 227 ? 22.316 10.275  9.591   1.00 15.95 ? 218 ILE A O     1 
ATOM   1627 C CB    . ILE A 1 227 ? 24.466 7.850   10.199  1.00 13.01 ? 218 ILE A CB    1 
ATOM   1628 C CG1   . ILE A 1 227 ? 23.256 7.136   9.557   1.00 12.83 ? 218 ILE A CG1   1 
ATOM   1629 C CG2   . ILE A 1 227 ? 24.471 7.732   11.736  1.00 13.39 ? 218 ILE A CG2   1 
ATOM   1630 C CD1   . ILE A 1 227 ? 23.254 5.587   9.796   1.00 16.48 ? 218 ILE A CD1   1 
ATOM   1631 N N     . THR A 1 228 ? 23.519 10.725  11.432  1.00 14.56 ? 219 THR A N     1 
ATOM   1632 C CA    . THR A 1 228 ? 22.483 11.582  12.002  1.00 19.46 ? 219 THR A CA    1 
ATOM   1633 C C     . THR A 1 228 ? 22.162 12.752  11.075  1.00 15.76 ? 219 THR A C     1 
ATOM   1634 O O     . THR A 1 228 ? 20.983 13.031  10.797  1.00 16.92 ? 219 THR A O     1 
ATOM   1635 C CB    . THR A 1 228 ? 22.937 12.077  13.374  1.00 19.16 ? 219 THR A CB    1 
ATOM   1636 O OG1   . THR A 1 228 ? 23.125 10.940  14.222  1.00 19.50 ? 219 THR A OG1   1 
ATOM   1637 C CG2   . THR A 1 228 ? 21.892 12.980  13.985  1.00 22.48 ? 219 THR A CG2   1 
ATOM   1638 N N     . GLN A 1 229 ? 23.200 13.437  10.572  1.00 18.03 ? 220 GLN A N     1 
ATOM   1639 C CA    . GLN A 1 229 ? 22.987 14.583  9.692   1.00 16.57 ? 220 GLN A CA    1 
ATOM   1640 C C     . GLN A 1 229 ? 22.340 14.174  8.377   1.00 17.77 ? 220 GLN A C     1 
ATOM   1641 O O     . GLN A 1 229 ? 21.477 14.885  7.861   1.00 18.47 ? 220 GLN A O     1 
ATOM   1642 C CB    . GLN A 1 229 ? 24.303 15.317  9.458   1.00 20.95 ? 220 GLN A CB    1 
ATOM   1643 C CG    . GLN A 1 229 ? 24.709 16.086  10.689  1.00 22.01 ? 220 GLN A CG    1 
ATOM   1644 C CD    . GLN A 1 229 ? 26.126 16.626  10.646  1.00 26.04 ? 220 GLN A CD    1 
ATOM   1645 O OE1   . GLN A 1 229 ? 26.839 16.484  9.653   1.00 27.00 ? 220 GLN A OE1   1 
ATOM   1646 N NE2   . GLN A 1 229 ? 26.547 17.246  11.750  1.00 29.24 ? 220 GLN A NE2   1 
ATOM   1647 N N     . VAL A 1 230 ? 22.737 13.028  7.815   1.00 16.20 ? 221 VAL A N     1 
ATOM   1648 C CA    . VAL A 1 230 ? 22.072 12.537  6.608   1.00 17.80 ? 221 VAL A CA    1 
ATOM   1649 C C     . VAL A 1 230 ? 20.592 12.285  6.867   1.00 15.24 ? 221 VAL A C     1 
ATOM   1650 O O     . VAL A 1 230 ? 19.724 12.687  6.084   1.00 14.23 ? 221 VAL A O     1 
ATOM   1651 C CB    . VAL A 1 230 ? 22.776 11.265  6.103   1.00 14.48 ? 221 VAL A CB    1 
ATOM   1652 C CG1   . VAL A 1 230 ? 21.981 10.634  4.983   1.00 13.80 ? 221 VAL A CG1   1 
ATOM   1653 C CG2   . VAL A 1 230 ? 24.186 11.595  5.649   1.00 14.68 ? 221 VAL A CG2   1 
ATOM   1654 N N     . VAL A 1 231 ? 20.283 11.566  7.952   1.00 16.44 ? 222 VAL A N     1 
ATOM   1655 C CA    . VAL A 1 231 ? 18.897 11.201  8.233   1.00 16.08 ? 222 VAL A CA    1 
ATOM   1656 C C     . VAL A 1 231 ? 18.071 12.445  8.540   1.00 15.98 ? 222 VAL A C     1 
ATOM   1657 O O     . VAL A 1 231 ? 16.961 12.602  8.018   1.00 18.37 ? 222 VAL A O     1 
ATOM   1658 C CB    . VAL A 1 231 ? 18.843 10.154  9.369   1.00 15.55 ? 222 VAL A CB    1 
ATOM   1659 C CG1   . VAL A 1 231 ? 17.380 9.898   9.816   1.00 17.01 ? 222 VAL A CG1   1 
ATOM   1660 C CG2   . VAL A 1 231 ? 19.475 8.781   8.895   1.00 11.19 ? 222 VAL A CG2   1 
ATOM   1661 N N     . GLN A 1 232 ? 18.620 13.372  9.331   1.00 14.14 ? 223 GLN A N     1 
ATOM   1662 C CA    A GLN A 1 232 ? 17.878 14.594  9.624   0.50 17.31 ? 223 GLN A CA    1 
ATOM   1663 C CA    B GLN A 1 232 ? 17.922 14.624  9.630   0.50 17.31 ? 223 GLN A CA    1 
ATOM   1664 C C     . GLN A 1 232 ? 17.601 15.385  8.356   1.00 19.36 ? 223 GLN A C     1 
ATOM   1665 O O     . GLN A 1 232 ? 16.491 15.909  8.187   1.00 21.52 ? 223 GLN A O     1 
ATOM   1666 C CB    A GLN A 1 232 ? 18.621 15.464  10.631  0.50 19.64 ? 223 GLN A CB    1 
ATOM   1667 C CB    B GLN A 1 232 ? 18.780 15.493  10.550  0.50 19.51 ? 223 GLN A CB    1 
ATOM   1668 C CG    A GLN A 1 232 ? 17.830 16.728  10.983  0.50 19.31 ? 223 GLN A CG    1 
ATOM   1669 C CG    B GLN A 1 232 ? 18.703 15.127  12.016  0.50 18.27 ? 223 GLN A CG    1 
ATOM   1670 C CD    A GLN A 1 232 ? 16.418 16.452  11.503  0.50 18.89 ? 223 GLN A CD    1 
ATOM   1671 C CD    B GLN A 1 232 ? 19.711 15.903  12.857  0.50 22.18 ? 223 GLN A CD    1 
ATOM   1672 O OE1   A GLN A 1 232 ? 16.240 15.867  12.572  0.50 22.41 ? 223 GLN A OE1   1 
ATOM   1673 O OE1   B GLN A 1 232 ? 20.857 16.083  12.449  0.50 20.63 ? 223 GLN A OE1   1 
ATOM   1674 N NE2   A GLN A 1 232 ? 15.413 16.913  10.768  0.50 21.14 ? 223 GLN A NE2   1 
ATOM   1675 N NE2   B GLN A 1 232 ? 19.280 16.383  14.021  0.50 21.51 ? 223 GLN A NE2   1 
ATOM   1676 N N     . ALA A 1 233 ? 18.578 15.463  7.453   1.00 16.26 ? 224 ALA A N     1 
ATOM   1677 C CA    . ALA A 1 233 ? 18.382 16.170  6.190   1.00 18.37 ? 224 ALA A CA    1 
ATOM   1678 C C     . ALA A 1 233 ? 17.251 15.550  5.387   1.00 17.89 ? 224 ALA A C     1 
ATOM   1679 O O     . ALA A 1 233 ? 16.368 16.259  4.904   1.00 18.82 ? 224 ALA A O     1 
ATOM   1680 C CB    . ALA A 1 233 ? 19.682 16.158  5.379   1.00 16.29 ? 224 ALA A CB    1 
ATOM   1681 N N     . VAL A 1 234 ? 17.249 14.219  5.227   1.00 14.99 ? 225 VAL A N     1 
ATOM   1682 C CA    . VAL A 1 234 ? 16.196 13.659  4.384   1.00 17.73 ? 225 VAL A CA    1 
ATOM   1683 C C     . VAL A 1 234 ? 14.843 13.700  5.097   1.00 21.67 ? 225 VAL A C     1 
ATOM   1684 O O     . VAL A 1 234 ? 13.805 13.899  4.438   1.00 21.26 ? 225 VAL A O     1 
ATOM   1685 C CB    . VAL A 1 234 ? 16.562 12.250  3.880   1.00 16.96 ? 225 VAL A CB    1 
ATOM   1686 C CG1   . VAL A 1 234 ? 17.751 12.360  2.882   1.00 13.50 ? 225 VAL A CG1   1 
ATOM   1687 C CG2   . VAL A 1 234 ? 16.883 11.270  5.033   1.00 16.53 ? 225 VAL A CG2   1 
ATOM   1688 N N     . VAL A 1 235 ? 14.821 13.541  6.433   1.00 16.56 ? 226 VAL A N     1 
ATOM   1689 C CA    . VAL A 1 235 ? 13.556 13.655  7.168   1.00 19.97 ? 226 VAL A CA    1 
ATOM   1690 C C     . VAL A 1 235 ? 12.978 15.050  6.991   1.00 18.12 ? 226 VAL A C     1 
ATOM   1691 O O     . VAL A 1 235 ? 11.782 15.218  6.707   1.00 22.47 ? 226 VAL A O     1 
ATOM   1692 C CB    . VAL A 1 235 ? 13.753 13.312  8.652   1.00 17.98 ? 226 VAL A CB    1 
ATOM   1693 C CG1   . VAL A 1 235 ? 12.564 13.848  9.501   1.00 18.69 ? 226 VAL A CG1   1 
ATOM   1694 C CG2   . VAL A 1 235 ? 13.896 11.791  8.800   1.00 15.64 ? 226 VAL A CG2   1 
ATOM   1695 N N     . SER A 1 236 ? 13.823 16.065  7.117   1.00 21.34 ? 227 SER A N     1 
ATOM   1696 C CA    . SER A 1 236 ? 13.363 17.433  6.927   1.00 19.94 ? 227 SER A CA    1 
ATOM   1697 C C     . SER A 1 236 ? 12.869 17.681  5.506   1.00 21.33 ? 227 SER A C     1 
ATOM   1698 O O     . SER A 1 236 ? 11.962 18.489  5.309   1.00 26.47 ? 227 SER A O     1 
ATOM   1699 C CB    . SER A 1 236 ? 14.481 18.394  7.287   1.00 22.75 ? 227 SER A CB    1 
ATOM   1700 O OG    . SER A 1 236 ? 14.648 18.339  8.698   1.00 31.55 ? 227 SER A OG    1 
ATOM   1701 N N     . ALA A 1 237 ? 13.401 16.962  4.514   1.00 20.52 ? 228 ALA A N     1 
ATOM   1702 C CA    . ALA A 1 237 ? 12.979 17.201  3.138   1.00 22.13 ? 228 ALA A CA    1 
ATOM   1703 C C     . ALA A 1 237 ? 11.682 16.482  2.783   1.00 22.39 ? 228 ALA A C     1 
ATOM   1704 O O     . ALA A 1 237 ? 10.852 17.033  2.052   1.00 18.43 ? 228 ALA A O     1 
ATOM   1705 C CB    . ALA A 1 237 ? 14.084 16.789  2.170   1.00 21.47 ? 228 ALA A CB    1 
ATOM   1706 N N     . ILE A 1 238 ? 11.480 15.241  3.228   1.00 20.50 ? 229 ILE A N     1 
ATOM   1707 C CA    . ILE A 1 238 ? 10.381 14.439  2.702   1.00 20.61 ? 229 ILE A CA    1 
ATOM   1708 C C     . ILE A 1 238 ? 9.486  13.856  3.780   1.00 17.55 ? 229 ILE A C     1 
ATOM   1709 O O     . ILE A 1 238 ? 8.475  13.248  3.449   1.00 18.92 ? 229 ILE A O     1 
ATOM   1710 C CB    . ILE A 1 238 ? 10.882 13.314  1.765   1.00 18.95 ? 229 ILE A CB    1 
ATOM   1711 C CG1   . ILE A 1 238 ? 11.573 12.193  2.546   1.00 16.50 ? 229 ILE A CG1   1 
ATOM   1712 C CG2   . ILE A 1 238 ? 11.805 13.902  0.611   1.00 21.32 ? 229 ILE A CG2   1 
ATOM   1713 C CD1   . ILE A 1 238 ? 11.806 10.957  1.687   1.00 19.06 ? 229 ILE A CD1   1 
ATOM   1714 N N     . GLY A 1 239 ? 9.820  14.024  5.061   1.00 17.71 ? 230 GLY A N     1 
ATOM   1715 C CA    . GLY A 1 239 ? 9.006  13.515  6.169   1.00 20.32 ? 230 GLY A CA    1 
ATOM   1716 C C     . GLY A 1 239 ? 9.602  12.237  6.727   1.00 20.34 ? 230 GLY A C     1 
ATOM   1717 O O     . GLY A 1 239 ? 10.050 11.393  5.940   1.00 18.52 ? 230 GLY A O     1 
ATOM   1718 N N     . ALA A 1 240 ? 9.661  12.094  8.059   1.00 15.65 ? 231 ALA A N     1 
ATOM   1719 C CA    . ALA A 1 240 ? 10.277 10.905  8.650   1.00 19.19 ? 231 ALA A CA    1 
ATOM   1720 C C     . ALA A 1 240 ? 9.584  9.621   8.208   1.00 20.68 ? 231 ALA A C     1 
ATOM   1721 O O     . ALA A 1 240 ? 10.247 8.600   8.005   1.00 18.51 ? 231 ALA A O     1 
ATOM   1722 C CB    . ALA A 1 240 ? 10.276 11.031  10.173  1.00 18.38 ? 231 ALA A CB    1 
ATOM   1723 N N     . ASP A 1 241 ? 8.268  9.659   7.989   1.00 20.95 ? 232 ASP A N     1 
ATOM   1724 C CA    . ASP A 1 241 ? 7.515  8.460   7.677   1.00 17.45 ? 232 ASP A CA    1 
ATOM   1725 C C     . ASP A 1 241 ? 7.810  7.911   6.287   1.00 16.38 ? 232 ASP A C     1 
ATOM   1726 O O     . ASP A 1 241 ? 7.385  6.794   5.991   1.00 18.92 ? 232 ASP A O     1 
ATOM   1727 C CB    . ASP A 1 241 ? 6.023  8.750   7.793   1.00 22.77 ? 232 ASP A CB    1 
ATOM   1728 C CG    . ASP A 1 241 ? 5.555  9.730   6.752   1.00 26.42 ? 232 ASP A CG    1 
ATOM   1729 O OD1   . ASP A 1 241 ? 6.096  10.857  6.679   1.00 29.54 ? 232 ASP A OD1   1 
ATOM   1730 O OD2   . ASP A 1 241 ? 4.643  9.371   5.988   1.00 43.39 ? 232 ASP A OD2   1 
ATOM   1731 N N     . ARG A 1 242 ? 8.539  8.657   5.452   1.00 16.38 ? 233 ARG A N     1 
ATOM   1732 C CA    . ARG A 1 242 ? 9.000  8.175   4.159   1.00 17.29 ? 233 ARG A CA    1 
ATOM   1733 C C     . ARG A 1 242 ? 10.492 7.822   4.184   1.00 16.50 ? 233 ARG A C     1 
ATOM   1734 O O     . ARG A 1 242 ? 11.116 7.767   3.129   1.00 15.04 ? 233 ARG A O     1 
ATOM   1735 C CB    . ARG A 1 242 ? 8.723  9.232   3.070   1.00 15.37 ? 233 ARG A CB    1 
ATOM   1736 C CG    . ARG A 1 242 ? 7.226  9.503   2.785   1.00 18.60 ? 233 ARG A CG    1 
ATOM   1737 C CD    . ARG A 1 242 ? 7.041  10.542  1.683   1.00 19.99 ? 233 ARG A CD    1 
ATOM   1738 N NE    . ARG A 1 242 ? 5.625  10.833  1.443   1.00 27.32 ? 233 ARG A NE    1 
ATOM   1739 C CZ    . ARG A 1 242 ? 4.767  10.037  0.807   1.00 32.42 ? 233 ARG A CZ    1 
ATOM   1740 N NH1   . ARG A 1 242 ? 5.135  8.861   0.299   1.00 26.06 ? 233 ARG A NH1   1 
ATOM   1741 N NH2   . ARG A 1 242 ? 3.498  10.422  0.676   1.00 31.14 ? 233 ARG A NH2   1 
ATOM   1742 N N     . VAL A 1 243 ? 11.109 7.685   5.365   1.00 15.27 ? 234 VAL A N     1 
ATOM   1743 C CA    . VAL A 1 243 ? 12.562 7.476   5.447   1.00 14.41 ? 234 VAL A CA    1 
ATOM   1744 C C     . VAL A 1 243 ? 12.839 6.177   6.199   1.00 15.77 ? 234 VAL A C     1 
ATOM   1745 O O     . VAL A 1 243 ? 12.400 6.011   7.344   1.00 16.93 ? 234 VAL A O     1 
ATOM   1746 C CB    . VAL A 1 243 ? 13.270 8.654   6.138   1.00 17.86 ? 234 VAL A CB    1 
ATOM   1747 C CG1   . VAL A 1 243 ? 14.765 8.341   6.378   1.00 19.21 ? 234 VAL A CG1   1 
ATOM   1748 C CG2   . VAL A 1 243 ? 13.116 9.953   5.360   1.00 16.25 ? 234 VAL A CG2   1 
ATOM   1749 N N     . GLY A 1 244 ? 13.585 5.253   5.566   1.00 12.08 ? 235 GLY A N     1 
ATOM   1750 C CA    . GLY A 1 244 ? 14.043 4.069   6.294   1.00 14.41 ? 235 GLY A CA    1 
ATOM   1751 C C     . GLY A 1 244 ? 15.553 4.165   6.445   1.00 13.50 ? 235 GLY A C     1 
ATOM   1752 O O     . GLY A 1 244 ? 16.175 4.887   5.679   1.00 13.67 ? 235 GLY A O     1 
ATOM   1753 N N     . VAL A 1 245 ? 16.176 3.462   7.398   1.00 13.16 ? 236 VAL A N     1 
ATOM   1754 C CA    . VAL A 1 245 ? 17.630 3.542   7.556   1.00 11.06 ? 236 VAL A CA    1 
ATOM   1755 C C     . VAL A 1 245 ? 18.173 2.134   7.683   1.00 15.35 ? 236 VAL A C     1 
ATOM   1756 O O     . VAL A 1 245 ? 17.684 1.372   8.527   1.00 13.21 ? 236 VAL A O     1 
ATOM   1757 C CB    . VAL A 1 245 ? 18.003 4.346   8.801   1.00 10.24 ? 236 VAL A CB    1 
ATOM   1758 C CG1   . VAL A 1 245 ? 19.509 4.538   8.903   1.00 15.67 ? 236 VAL A CG1   1 
ATOM   1759 C CG2   . VAL A 1 245 ? 17.245 5.677   8.812   1.00 13.27 ? 236 VAL A CG2   1 
ATOM   1760 N N     . ARG A 1 246 ? 19.169 1.782   6.856   1.00 12.17 ? 237 ARG A N     1 
ATOM   1761 C CA    . ARG A 1 246 ? 19.758 0.444   6.917   1.00 11.09 ? 237 ARG A CA    1 
ATOM   1762 C C     . ARG A 1 246 ? 21.170 0.492   7.471   1.00 15.13 ? 237 ARG A C     1 
ATOM   1763 O O     . ARG A 1 246 ? 22.016 1.236   6.966   1.00 14.70 ? 237 ARG A O     1 
ATOM   1764 C CB    . ARG A 1 246 ? 19.792 -0.254  5.561   1.00 12.54 ? 237 ARG A CB    1 
ATOM   1765 C CG    . ARG A 1 246 ? 20.052 -1.731  5.663   1.00 10.40 ? 237 ARG A CG    1 
ATOM   1766 C CD    . ARG A 1 246 ? 20.032 -2.380  4.260   1.00 13.19 ? 237 ARG A CD    1 
ATOM   1767 N NE    . ARG A 1 246 ? 19.561 -3.758  4.390   1.00 14.38 ? 237 ARG A NE    1 
ATOM   1768 C CZ    . ARG A 1 246 ? 19.840 -4.754  3.561   1.00 13.82 ? 237 ARG A CZ    1 
ATOM   1769 N NH1   . ARG A 1 246 ? 20.704 -4.604  2.571   1.00 12.58 ? 237 ARG A NH1   1 
ATOM   1770 N NH2   . ARG A 1 246 ? 19.217 -5.922  3.722   1.00 15.86 ? 237 ARG A NH2   1 
ATOM   1771 N N     . VAL A 1 247 ? 21.442 -0.348  8.477   1.00 14.10 ? 238 VAL A N     1 
ATOM   1772 C CA    . VAL A 1 247 ? 22.789 -0.476  9.017   1.00 15.23 ? 238 VAL A CA    1 
ATOM   1773 C C     . VAL A 1 247 ? 23.146 -1.957  9.184   1.00 13.57 ? 238 VAL A C     1 
ATOM   1774 O O     . VAL A 1 247 ? 22.281 -2.834  9.200   1.00 13.63 ? 238 VAL A O     1 
ATOM   1775 C CB    . VAL A 1 247 ? 22.938 0.261   10.355  1.00 13.50 ? 238 VAL A CB    1 
ATOM   1776 C CG1   . VAL A 1 247 ? 22.764 1.785   10.172  1.00 15.72 ? 238 VAL A CG1   1 
ATOM   1777 C CG2   . VAL A 1 247 ? 21.926 -0.251  11.374  1.00 14.92 ? 238 VAL A CG2   1 
ATOM   1778 N N     . SER A 1 248 ? 24.449 -2.213  9.374   1.00 13.27 ? 239 SER A N     1 
ATOM   1779 C CA    . SER A 1 248 ? 24.981 -3.571  9.537   1.00 14.33 ? 239 SER A CA    1 
ATOM   1780 C C     . SER A 1 248 ? 26.145 -3.529  10.528  1.00 17.10 ? 239 SER A C     1 
ATOM   1781 O O     . SER A 1 248 ? 27.316 -3.683  10.154  1.00 18.35 ? 239 SER A O     1 
ATOM   1782 C CB    . SER A 1 248 ? 25.403 -4.166  8.182   1.00 15.63 ? 239 SER A CB    1 
ATOM   1783 O OG    . SER A 1 248 ? 26.384 -3.342  7.519   1.00 15.10 ? 239 SER A OG    1 
ATOM   1784 N N     . PRO A 1 249 ? 25.850 -3.315  11.821  1.00 13.89 ? 240 PRO A N     1 
ATOM   1785 C CA    . PRO A 1 249 ? 26.949 -3.159  12.795  1.00 13.87 ? 240 PRO A CA    1 
ATOM   1786 C C     . PRO A 1 249 ? 27.883 -4.361  12.826  1.00 14.15 ? 240 PRO A C     1 
ATOM   1787 O O     . PRO A 1 249 ? 29.067 -4.206  13.130  1.00 19.46 ? 240 PRO A O     1 
ATOM   1788 C CB    . PRO A 1 249 ? 26.234 -2.984  14.136  1.00 16.19 ? 240 PRO A CB    1 
ATOM   1789 C CG    . PRO A 1 249 ? 24.759 -2.852  13.840  1.00 20.87 ? 240 PRO A CG    1 
ATOM   1790 C CD    . PRO A 1 249 ? 24.518 -3.393  12.452  1.00 17.25 ? 240 PRO A CD    1 
ATOM   1791 N N     . ALA A 1 250 ? 27.405 -5.549  12.486  1.00 16.93 ? 241 ALA A N     1 
ATOM   1792 C CA    . ALA A 1 250 ? 28.222 -6.740  12.665  1.00 22.21 ? 241 ALA A CA    1 
ATOM   1793 C C     . ALA A 1 250 ? 28.630 -7.396  11.355  1.00 19.08 ? 241 ALA A C     1 
ATOM   1794 O O     . ALA A 1 250 ? 29.017 -8.561  11.371  1.00 22.75 ? 241 ALA A O     1 
ATOM   1795 C CB    . ALA A 1 250 ? 27.496 -7.763  13.548  1.00 27.68 ? 241 ALA A CB    1 
ATOM   1796 N N     . ILE A 1 251 ? 28.538 -6.690  10.212  1.00 16.34 ? 242 ILE A N     1 
ATOM   1797 C CA    . ILE A 1 251 ? 29.085 -7.182  8.945   1.00 16.60 ? 242 ILE A CA    1 
ATOM   1798 C C     . ILE A 1 251 ? 30.403 -6.454  8.729   1.00 19.15 ? 242 ILE A C     1 
ATOM   1799 O O     . ILE A 1 251 ? 30.440 -5.216  8.793   1.00 19.09 ? 242 ILE A O     1 
ATOM   1800 C CB    . ILE A 1 251 ? 28.105 -6.929  7.786   1.00 16.02 ? 242 ILE A CB    1 
ATOM   1801 C CG1   . ILE A 1 251 ? 26.838 -7.761  7.981   1.00 16.10 ? 242 ILE A CG1   1 
ATOM   1802 C CG2   . ILE A 1 251 ? 28.774 -7.219  6.385   1.00 18.11 ? 242 ILE A CG2   1 
ATOM   1803 C CD1   . ILE A 1 251 ? 25.799 -7.723  6.811   1.00 16.33 ? 242 ILE A CD1   1 
ATOM   1804 N N     . ASP A 1 252 ? 31.492 -7.199  8.491   1.00 21.09 ? 243 ASP A N     1 
ATOM   1805 C CA    . ASP A 1 252 ? 32.792 -6.544  8.373   1.00 24.66 ? 243 ASP A CA    1 
ATOM   1806 C C     . ASP A 1 252 ? 33.246 -6.404  6.931   1.00 26.98 ? 243 ASP A C     1 
ATOM   1807 O O     . ASP A 1 252 ? 34.452 -6.280  6.676   1.00 26.87 ? 243 ASP A O     1 
ATOM   1808 C CB    . ASP A 1 252 ? 33.875 -7.273  9.176   1.00 27.94 ? 243 ASP A CB    1 
ATOM   1809 C CG    . ASP A 1 252 ? 33.912 -8.764  8.905   1.00 40.40 ? 243 ASP A CG    1 
ATOM   1810 O OD1   . ASP A 1 252 ? 33.618 -9.177  7.748   1.00 42.40 ? 243 ASP A OD1   1 
ATOM   1811 O OD2   . ASP A 1 252 ? 34.256 -9.521  9.851   1.00 49.55 ? 243 ASP A OD2   1 
ATOM   1812 N N     . HIS A 1 253 ? 32.295 -6.402  6.000   1.00 24.00 ? 244 HIS A N     1 
ATOM   1813 C CA    . HIS A 1 253 ? 32.563 -6.266  4.575   1.00 23.84 ? 244 HIS A CA    1 
ATOM   1814 C C     . HIS A 1 253 ? 33.415 -5.034  4.278   1.00 22.03 ? 244 HIS A C     1 
ATOM   1815 O O     . HIS A 1 253 ? 33.222 -3.972  4.873   1.00 19.26 ? 244 HIS A O     1 
ATOM   1816 C CB    . HIS A 1 253 ? 31.215 -6.185  3.864   1.00 23.13 ? 244 HIS A CB    1 
ATOM   1817 C CG    . HIS A 1 253 ? 31.312 -6.115  2.375   1.00 19.76 ? 244 HIS A CG    1 
ATOM   1818 N ND1   . HIS A 1 253 ? 31.821 -7.146  1.613   1.00 23.28 ? 244 HIS A ND1   1 
ATOM   1819 C CD2   . HIS A 1 253 ? 30.957 -5.139  1.506   1.00 16.43 ? 244 HIS A CD2   1 
ATOM   1820 C CE1   . HIS A 1 253 ? 31.764 -6.814  0.332   1.00 22.81 ? 244 HIS A CE1   1 
ATOM   1821 N NE2   . HIS A 1 253 ? 31.250 -5.599  0.240   1.00 18.67 ? 244 HIS A NE2   1 
ATOM   1822 N N     . LEU A 1 254 ? 34.393 -5.199  3.373   1.00 18.31 ? 245 LEU A N     1 
ATOM   1823 C CA    . LEU A 1 254 ? 35.294 -4.118  2.952   1.00 16.60 ? 245 LEU A CA    1 
ATOM   1824 C C     . LEU A 1 254 ? 36.020 -3.465  4.127   1.00 20.92 ? 245 LEU A C     1 
ATOM   1825 O O     . LEU A 1 254 ? 36.161 -2.242  4.166   1.00 17.14 ? 245 LEU A O     1 
ATOM   1826 C CB    . LEU A 1 254 ? 34.548 -3.053  2.174   1.00 16.21 ? 245 LEU A CB    1 
ATOM   1827 C CG    . LEU A 1 254 ? 33.833 -3.608  0.966   1.00 18.88 ? 245 LEU A CG    1 
ATOM   1828 C CD1   . LEU A 1 254 ? 32.952 -2.476  0.435   1.00 17.83 ? 245 LEU A CD1   1 
ATOM   1829 C CD2   . LEU A 1 254 ? 34.819 -4.179  -0.061  1.00 19.34 ? 245 LEU A CD2   1 
ATOM   1830 N N     . ASP A 1 255 ? 36.478 -4.285  5.092   1.00 18.70 ? 246 ASP A N     1 
ATOM   1831 C CA    . ASP A 1 255 ? 37.327 -3.825  6.194   1.00 19.39 ? 246 ASP A CA    1 
ATOM   1832 C C     . ASP A 1 255 ? 36.585 -2.940  7.162   1.00 25.19 ? 246 ASP A C     1 
ATOM   1833 O O     . ASP A 1 255 ? 37.157 -1.986  7.676   1.00 30.30 ? 246 ASP A O     1 
ATOM   1834 C CB    . ASP A 1 255 ? 38.534 -3.028  5.722   1.00 28.02 ? 246 ASP A CB    1 
ATOM   1835 C CG    . ASP A 1 255 ? 39.644 -3.875  5.288   1.00 30.43 ? 246 ASP A CG    1 
ATOM   1836 O OD1   . ASP A 1 255 ? 39.560 -5.110  5.494   1.00 35.41 ? 246 ASP A OD1   1 
ATOM   1837 O OD2   . ASP A 1 255 ? 40.599 -3.268  4.754   1.00 36.21 ? 246 ASP A OD2   1 
ATOM   1838 N N     . ALA A 1 256 ? 35.309 -3.208  7.366   1.00 14.33 ? 247 ALA A N     1 
ATOM   1839 C CA    . ALA A 1 256 ? 34.415 -2.319  8.097   1.00 20.87 ? 247 ALA A CA    1 
ATOM   1840 C C     . ALA A 1 256 ? 34.059 -2.976  9.420   1.00 22.64 ? 247 ALA A C     1 
ATOM   1841 O O     . ALA A 1 256 ? 32.941 -3.435  9.624   1.00 25.54 ? 247 ALA A O     1 
ATOM   1842 C CB    . ALA A 1 256 ? 33.151 -2.023  7.288   1.00 20.80 ? 247 ALA A CB    1 
ATOM   1843 N N     . MET A 1 257 ? 34.994 -2.941  10.353  1.00 18.94 ? 248 MET A N     1 
ATOM   1844 C CA    . MET A 1 257 ? 34.809 -3.559  11.652  1.00 21.10 ? 248 MET A CA    1 
ATOM   1845 C C     . MET A 1 257 ? 34.736 -2.496  12.735  1.00 19.47 ? 248 MET A C     1 
ATOM   1846 O O     . MET A 1 257 ? 35.390 -1.450  12.649  1.00 17.39 ? 248 MET A O     1 
ATOM   1847 C CB    . MET A 1 257 ? 35.953 -4.524  11.936  1.00 25.37 ? 248 MET A CB    1 
ATOM   1848 C CG    . MET A 1 257 ? 35.672 -5.536  13.027  1.00 39.22 ? 248 MET A CG    1 
ATOM   1849 S SD    . MET A 1 257 ? 36.908 -6.854  12.928  1.00 74.69 ? 248 MET A SD    1 
ATOM   1850 C CE    . MET A 1 257 ? 36.828 -7.272  11.176  1.00 44.81 ? 248 MET A CE    1 
ATOM   1851 N N     . ASP A 1 258 ? 33.951 -2.772  13.776  1.00 21.87 ? 249 ASP A N     1 
ATOM   1852 C CA    . ASP A 1 258 ? 33.963 -1.930  14.962  1.00 20.69 ? 249 ASP A CA    1 
ATOM   1853 C C     . ASP A 1 258 ? 34.365 -2.747  16.183  1.00 22.15 ? 249 ASP A C     1 
ATOM   1854 O O     . ASP A 1 258 ? 34.063 -3.936  16.278  1.00 20.99 ? 249 ASP A O     1 
ATOM   1855 C CB    . ASP A 1 258 ? 32.596 -1.262  15.223  1.00 19.58 ? 249 ASP A CB    1 
ATOM   1856 C CG    . ASP A 1 258 ? 32.700 -0.083  16.205  1.00 21.75 ? 249 ASP A CG    1 
ATOM   1857 O OD1   . ASP A 1 258 ? 32.995 1.080   15.785  1.00 22.02 ? 249 ASP A OD1   1 
ATOM   1858 O OD2   . ASP A 1 258 ? 32.520 -0.311  17.439  1.00 22.04 ? 249 ASP A OD2   1 
ATOM   1859 N N     . SER A 1 259 ? 35.043 -2.089  17.116  1.00 21.15 ? 250 SER A N     1 
ATOM   1860 C CA    . SER A 1 259 ? 35.501 -2.782  18.311  1.00 23.49 ? 250 SER A CA    1 
ATOM   1861 C C     . SER A 1 259 ? 34.347 -3.168  19.225  1.00 23.94 ? 250 SER A C     1 
ATOM   1862 O O     . SER A 1 259 ? 34.500 -4.064  20.065  1.00 25.66 ? 250 SER A O     1 
ATOM   1863 C CB    . SER A 1 259 ? 36.491 -1.902  19.049  1.00 26.60 ? 250 SER A CB    1 
ATOM   1864 O OG    . SER A 1 259 ? 35.816 -0.754  19.486  1.00 24.89 ? 250 SER A OG    1 
ATOM   1865 N N     . ASN A 1 260 ? 33.199 -2.533  19.090  1.00 18.02 ? 251 ASN A N     1 
ATOM   1866 C CA    . ASN A 1 260 ? 32.042 -2.842  19.936  1.00 20.88 ? 251 ASN A CA    1 
ATOM   1867 C C     . ASN A 1 260 ? 30.792 -2.715  19.078  1.00 23.33 ? 251 ASN A C     1 
ATOM   1868 O O     . ASN A 1 260 ? 30.115 -1.680  19.109  1.00 23.23 ? 251 ASN A O     1 
ATOM   1869 C CB    . ASN A 1 260 ? 31.994 -1.895  21.145  1.00 21.47 ? 251 ASN A CB    1 
ATOM   1870 C CG    . ASN A 1 260 ? 30.990 -2.326  22.204  1.00 23.27 ? 251 ASN A CG    1 
ATOM   1871 O OD1   . ASN A 1 260 ? 30.120 -3.176  21.957  1.00 22.43 ? 251 ASN A OD1   1 
ATOM   1872 N ND2   . ASN A 1 260 ? 31.120 -1.750  23.407  1.00 30.13 ? 251 ASN A ND2   1 
ATOM   1873 N N     . PRO A 1 261 ? 30.485 -3.737  18.252  1.00 21.89 ? 252 PRO A N     1 
ATOM   1874 C CA    . PRO A 1 261 ? 29.339 -3.613  17.324  1.00 20.44 ? 252 PRO A CA    1 
ATOM   1875 C C     . PRO A 1 261 ? 28.027 -3.326  18.014  1.00 20.50 ? 252 PRO A C     1 
ATOM   1876 O O     . PRO A 1 261 ? 27.258 -2.495  17.536  1.00 17.53 ? 252 PRO A O     1 
ATOM   1877 C CB    . PRO A 1 261 ? 29.314 -4.970  16.594  1.00 20.71 ? 252 PRO A CB    1 
ATOM   1878 C CG    . PRO A 1 261 ? 30.769 -5.419  16.628  1.00 20.51 ? 252 PRO A CG    1 
ATOM   1879 C CD    . PRO A 1 261 ? 31.239 -4.982  18.022  1.00 23.90 ? 252 PRO A CD    1 
ATOM   1880 N N     . LEU A 1 262 ? 27.724 -4.004  19.114  1.00 19.91 ? 253 LEU A N     1 
ATOM   1881 C CA    . LEU A 1 262 ? 26.425 -3.789  19.737  1.00 17.91 ? 253 LEU A CA    1 
ATOM   1882 C C     . LEU A 1 262 ? 26.288 -2.355  20.263  1.00 15.91 ? 253 LEU A C     1 
ATOM   1883 O O     . LEU A 1 262 ? 25.226 -1.740  20.158  1.00 19.72 ? 253 LEU A O     1 
ATOM   1884 C CB    . LEU A 1 262 ? 26.218 -4.843  20.826  1.00 23.18 ? 253 LEU A CB    1 
ATOM   1885 C CG    . LEU A 1 262 ? 24.981 -4.635  21.678  1.00 26.93 ? 253 LEU A CG    1 
ATOM   1886 C CD1   . LEU A 1 262 ? 23.764 -4.875  20.750  1.00 29.42 ? 253 LEU A CD1   1 
ATOM   1887 C CD2   . LEU A 1 262 ? 25.006 -5.675  22.799  1.00 23.69 ? 253 LEU A CD2   1 
ATOM   1888 N N     . SER A 1 263 ? 27.347 -1.810  20.836  1.00 16.35 ? 254 SER A N     1 
ATOM   1889 C CA    . SER A 1 263 ? 27.288 -0.452  21.338  1.00 18.55 ? 254 SER A CA    1 
ATOM   1890 C C     . SER A 1 263 ? 27.196 0.555   20.194  1.00 18.09 ? 254 SER A C     1 
ATOM   1891 O O     . SER A 1 263 ? 26.515 1.583   20.323  1.00 16.94 ? 254 SER A O     1 
ATOM   1892 C CB    . SER A 1 263 ? 28.516 -0.199  22.215  1.00 26.94 ? 254 SER A CB    1 
ATOM   1893 O OG    . SER A 1 263 ? 28.691 1.156   22.472  1.00 26.56 ? 254 SER A OG    1 
ATOM   1894 N N     . LEU A 1 264 ? 27.928 0.308   19.094  1.00 17.51 ? 255 LEU A N     1 
ATOM   1895 C CA    . LEU A 1 264 ? 27.756 1.161   17.919  1.00 14.50 ? 255 LEU A CA    1 
ATOM   1896 C C     . LEU A 1 264 ? 26.320 1.106   17.420  1.00 16.69 ? 255 LEU A C     1 
ATOM   1897 O O     . LEU A 1 264 ? 25.704 2.146   17.151  1.00 16.17 ? 255 LEU A O     1 
ATOM   1898 C CB    . LEU A 1 264 ? 28.718 0.757   16.797  1.00 15.41 ? 255 LEU A CB    1 
ATOM   1899 C CG    . LEU A 1 264 ? 28.534 1.538   15.456  1.00 15.72 ? 255 LEU A CG    1 
ATOM   1900 C CD1   . LEU A 1 264 ? 28.877 3.012   15.597  1.00 16.67 ? 255 LEU A CD1   1 
ATOM   1901 C CD2   . LEU A 1 264 ? 29.443 0.881   14.451  1.00 17.70 ? 255 LEU A CD2   1 
ATOM   1902 N N     . GLY A 1 265 ? 25.767 -0.096  17.305  1.00 15.77 ? 256 GLY A N     1 
ATOM   1903 C CA    . GLY A 1 265 ? 24.373 -0.217  16.901  1.00 13.09 ? 256 GLY A CA    1 
ATOM   1904 C C     . GLY A 1 265 ? 23.432 0.497   17.863  1.00 19.29 ? 256 GLY A C     1 
ATOM   1905 O O     . GLY A 1 265 ? 22.499 1.191   17.441  1.00 16.41 ? 256 GLY A O     1 
ATOM   1906 N N     . LEU A 1 266 ? 23.681 0.363   19.176  1.00 15.32 ? 257 LEU A N     1 
ATOM   1907 C CA    . LEU A 1 266 ? 22.783 1.012   20.130  1.00 14.64 ? 257 LEU A CA    1 
ATOM   1908 C C     . LEU A 1 266 ? 22.917 2.530   20.072  1.00 17.75 ? 257 LEU A C     1 
ATOM   1909 O O     . LEU A 1 266 ? 21.931 3.234   20.311  1.00 15.36 ? 257 LEU A O     1 
ATOM   1910 C CB    . LEU A 1 266 ? 23.047 0.507   21.546  1.00 13.47 ? 257 LEU A CB    1 
ATOM   1911 C CG    . LEU A 1 266 ? 22.549 -0.890  21.824  1.00 21.04 ? 257 LEU A CG    1 
ATOM   1912 C CD1   . LEU A 1 266 ? 22.940 -1.354  23.276  1.00 15.28 ? 257 LEU A CD1   1 
ATOM   1913 C CD2   . LEU A 1 266 ? 21.028 -0.868  21.641  1.00 18.78 ? 257 LEU A CD2   1 
ATOM   1914 N N     . ALA A 1 267 ? 24.122 3.042   19.736  1.00 18.71 ? 258 ALA A N     1 
ATOM   1915 C CA    . ALA A 1 267 ? 24.315 4.487   19.586  1.00 19.57 ? 258 ALA A CA    1 
ATOM   1916 C C     . ALA A 1 267 ? 23.599 5.004   18.355  1.00 17.84 ? 258 ALA A C     1 
ATOM   1917 O O     . ALA A 1 267 ? 23.021 6.091   18.383  1.00 17.37 ? 258 ALA A O     1 
ATOM   1918 C CB    . ALA A 1 267 ? 25.803 4.862   19.511  1.00 21.37 ? 258 ALA A CB    1 
ATOM   1919 N N     . VAL A 1 268 ? 23.575 4.226   17.275  1.00 16.83 ? 259 VAL A N     1 
ATOM   1920 C CA    . VAL A 1 268 ? 22.816 4.675   16.113  1.00 16.01 ? 259 VAL A CA    1 
ATOM   1921 C C     . VAL A 1 268 ? 21.329 4.727   16.453  1.00 14.21 ? 259 VAL A C     1 
ATOM   1922 O O     . VAL A 1 268 ? 20.636 5.680   16.105  1.00 17.19 ? 259 VAL A O     1 
ATOM   1923 C CB    . VAL A 1 268 ? 23.067 3.764   14.899  1.00 16.25 ? 259 VAL A CB    1 
ATOM   1924 C CG1   . VAL A 1 268 ? 22.143 4.208   13.733  1.00 17.58 ? 259 VAL A CG1   1 
ATOM   1925 C CG2   . VAL A 1 268 ? 24.519 3.858   14.473  1.00 16.64 ? 259 VAL A CG2   1 
ATOM   1926 N N     . VAL A 1 269 ? 20.828 3.696   17.132  1.00 15.70 ? 260 VAL A N     1 
ATOM   1927 C CA    . VAL A 1 269 ? 19.399 3.618   17.462  1.00 17.94 ? 260 VAL A CA    1 
ATOM   1928 C C     . VAL A 1 269 ? 18.979 4.786   18.347  1.00 17.33 ? 260 VAL A C     1 
ATOM   1929 O O     . VAL A 1 269 ? 17.875 5.328   18.209  1.00 17.75 ? 260 VAL A O     1 
ATOM   1930 C CB    . VAL A 1 269 ? 19.096 2.274   18.133  1.00 14.31 ? 260 VAL A CB    1 
ATOM   1931 C CG1   . VAL A 1 269 ? 17.770 2.331   18.977  1.00 17.27 ? 260 VAL A CG1   1 
ATOM   1932 C CG2   . VAL A 1 269 ? 19.008 1.159   17.088  1.00 14.10 ? 260 VAL A CG2   1 
ATOM   1933 N N     . GLU A 1 270 ? 19.824 5.145   19.319  1.00 17.88 ? 261 GLU A N     1 
ATOM   1934 C CA    . GLU A 1 270 ? 19.536 6.288   20.179  1.00 19.08 ? 261 GLU A CA    1 
ATOM   1935 C C     . GLU A 1 270 ? 19.396 7.567   19.363  1.00 18.13 ? 261 GLU A C     1 
ATOM   1936 O O     . GLU A 1 270 ? 18.502 8.377   19.606  1.00 18.34 ? 261 GLU A O     1 
ATOM   1937 C CB    . GLU A 1 270 ? 20.639 6.423   21.240  1.00 24.75 ? 261 GLU A CB    1 
ATOM   1938 C CG    . GLU A 1 270 ? 20.584 7.737   22.027  1.00 29.54 ? 261 GLU A CG    1 
ATOM   1939 C CD    . GLU A 1 270 ? 21.797 7.976   22.947  1.00 43.78 ? 261 GLU A CD    1 
ATOM   1940 O OE1   . GLU A 1 270 ? 21.891 7.350   24.034  1.00 48.86 ? 261 GLU A OE1   1 
ATOM   1941 O OE2   . GLU A 1 270 ? 22.625 8.855   22.614  1.00 44.84 ? 261 GLU A OE2   1 
ATOM   1942 N N     . ARG A 1 271 ? 20.271 7.771   18.392  1.00 18.87 ? 262 ARG A N     1 
ATOM   1943 C CA    . ARG A 1 271 ? 20.160 8.958   17.554  1.00 18.06 ? 262 ARG A CA    1 
ATOM   1944 C C     . ARG A 1 271 ? 18.901 8.927   16.680  1.00 19.23 ? 262 ARG A C     1 
ATOM   1945 O O     . ARG A 1 271 ? 18.282 9.972   16.463  1.00 18.00 ? 262 ARG A O     1 
ATOM   1946 C CB    . ARG A 1 271 ? 21.444 9.118   16.755  1.00 20.41 ? 262 ARG A CB    1 
ATOM   1947 C CG    . ARG A 1 271 ? 22.430 9.980   17.593  1.00 27.34 ? 262 ARG A CG    1 
ATOM   1948 C CD    . ARG A 1 271 ? 23.754 9.315   17.736  1.00 31.95 ? 262 ARG A CD    1 
ATOM   1949 N NE    . ARG A 1 271 ? 24.546 9.806   18.861  1.00 34.77 ? 262 ARG A NE    1 
ATOM   1950 C CZ    . ARG A 1 271 ? 24.815 9.106   19.966  1.00 35.45 ? 262 ARG A CZ    1 
ATOM   1951 N NH1   . ARG A 1 271 ? 24.273 7.904   20.195  1.00 29.96 ? 262 ARG A NH1   1 
ATOM   1952 N NH2   . ARG A 1 271 ? 25.648 9.620   20.868  1.00 35.94 ? 262 ARG A NH2   1 
ATOM   1953 N N     . LEU A 1 272 ? 18.479 7.749   16.202  1.00 17.89 ? 263 LEU A N     1 
ATOM   1954 C CA    . LEU A 1 272 ? 17.215 7.680   15.464  1.00 16.92 ? 263 LEU A CA    1 
ATOM   1955 C C     . LEU A 1 272 ? 16.030 7.954   16.394  1.00 15.94 ? 263 LEU A C     1 
ATOM   1956 O O     . LEU A 1 272 ? 15.065 8.632   16.007  1.00 18.14 ? 263 LEU A O     1 
ATOM   1957 C CB    . LEU A 1 272 ? 17.054 6.311   14.786  1.00 16.17 ? 263 LEU A CB    1 
ATOM   1958 C CG    . LEU A 1 272 ? 18.204 5.926   13.849  1.00 17.29 ? 263 LEU A CG    1 
ATOM   1959 C CD1   . LEU A 1 272 ? 17.943 4.584   13.189  1.00 18.29 ? 263 LEU A CD1   1 
ATOM   1960 C CD2   . LEU A 1 272 ? 18.460 7.037   12.808  1.00 16.98 ? 263 LEU A CD2   1 
ATOM   1961 N N     . ASN A 1 273 ? 16.089 7.449   17.624  1.00 16.60 ? 264 ASN A N     1 
ATOM   1962 C CA    . ASN A 1 273 ? 14.984 7.688   18.544  1.00 17.08 ? 264 ASN A CA    1 
ATOM   1963 C C     . ASN A 1 273 ? 14.858 9.167   18.840  1.00 17.80 ? 264 ASN A C     1 
ATOM   1964 O O     . ASN A 1 273 ? 13.751 9.700   18.902  1.00 19.96 ? 264 ASN A O     1 
ATOM   1965 C CB    . ASN A 1 273 ? 15.175 6.926   19.846  1.00 17.59 ? 264 ASN A CB    1 
ATOM   1966 C CG    . ASN A 1 273 ? 14.891 5.435   19.702  1.00 16.58 ? 264 ASN A CG    1 
ATOM   1967 O OD1   . ASN A 1 273 ? 14.310 4.964   18.703  1.00 17.58 ? 264 ASN A OD1   1 
ATOM   1968 N ND2   . ASN A 1 273 ? 15.261 4.687   20.738  1.00 18.93 ? 264 ASN A ND2   1 
ATOM   1969 N N     . LYS A 1 274 ? 15.993 9.849   18.990  1.00 17.07 ? 265 LYS A N     1 
ATOM   1970 C CA    . LYS A 1 274 ? 15.974 11.299  19.231  1.00 19.74 ? 265 LYS A CA    1 
ATOM   1971 C C     . LYS A 1 274 ? 15.472 12.080  18.012  1.00 19.69 ? 265 LYS A C     1 
ATOM   1972 O O     . LYS A 1 274 ? 14.714 13.044  18.156  1.00 22.36 ? 265 LYS A O     1 
ATOM   1973 C CB    . LYS A 1 274 ? 17.370 11.754  19.623  1.00 21.63 ? 265 LYS A CB    1 
ATOM   1974 C CG    . LYS A 1 274 ? 17.808 11.200  20.972  1.00 31.08 ? 265 LYS A CG    1 
ATOM   1975 C CD    . LYS A 1 274 ? 17.617 12.207  22.099  1.00 41.57 ? 265 LYS A CD    1 
ATOM   1976 C CE    . LYS A 1 274 ? 18.870 12.295  22.971  1.00 51.02 ? 265 LYS A CE    1 
ATOM   1977 N NZ    . LYS A 1 274 ? 19.404 10.957  23.401  1.00 43.21 ? 265 LYS A NZ    1 
ATOM   1978 N N     . ILE A 1 275 ? 15.882 11.689  16.803  1.00 18.05 ? 266 ILE A N     1 
ATOM   1979 C CA    . ILE A 1 275 ? 15.375 12.377  15.612  1.00 20.68 ? 266 ILE A CA    1 
ATOM   1980 C C     . ILE A 1 275 ? 13.857 12.282  15.561  1.00 20.95 ? 266 ILE A C     1 
ATOM   1981 O O     . ILE A 1 275 ? 13.160 13.244  15.196  1.00 20.11 ? 266 ILE A O     1 
ATOM   1982 C CB    . ILE A 1 275 ? 16.016 11.789  14.339  1.00 21.29 ? 266 ILE A CB    1 
ATOM   1983 C CG1   . ILE A 1 275 ? 17.503 12.147  14.283  1.00 20.19 ? 266 ILE A CG1   1 
ATOM   1984 C CG2   . ILE A 1 275 ? 15.201 12.217  13.078  1.00 20.19 ? 266 ILE A CG2   1 
ATOM   1985 C CD1   . ILE A 1 275 ? 18.261 11.410  13.107  1.00 18.89 ? 266 ILE A CD1   1 
ATOM   1986 N N     . GLN A 1 276 ? 13.324 11.115  15.934  1.00 19.37 ? 267 GLN A N     1 
ATOM   1987 C CA    . GLN A 1 276 ? 11.884 10.919  15.981  1.00 17.28 ? 267 GLN A CA    1 
ATOM   1988 C C     . GLN A 1 276 ? 11.242 11.817  17.044  1.00 21.13 ? 267 GLN A C     1 
ATOM   1989 O O     . GLN A 1 276 ? 10.256 12.506  16.765  1.00 25.75 ? 267 GLN A O     1 
ATOM   1990 C CB    . GLN A 1 276 ? 11.575 9.452   16.259  1.00 19.92 ? 267 GLN A CB    1 
ATOM   1991 C CG    . GLN A 1 276 ? 11.976 8.578   15.089  1.00 15.77 ? 267 GLN A CG    1 
ATOM   1992 C CD    . GLN A 1 276 ? 11.675 7.100   15.264  1.00 17.83 ? 267 GLN A CD    1 
ATOM   1993 O OE1   . GLN A 1 276 ? 11.591 6.357   14.271  1.00 19.71 ? 267 GLN A OE1   1 
ATOM   1994 N NE2   . GLN A 1 276 ? 11.503 6.659   16.524  1.00 18.73 ? 267 GLN A NE2   1 
ATOM   1995 N N     . LEU A 1 277 ? 11.792 11.830  18.282  1.00 22.21 ? 268 LEU A N     1 
ATOM   1996 C CA    . LEU A 1 277 ? 11.217 12.738  19.283  1.00 27.26 ? 268 LEU A CA    1 
ATOM   1997 C C     . LEU A 1 277 ? 11.301 14.189  18.828  1.00 29.83 ? 268 LEU A C     1 
ATOM   1998 O O     . LEU A 1 277 ? 10.312 14.928  18.890  1.00 36.83 ? 268 LEU A O     1 
ATOM   1999 C CB    . LEU A 1 277 ? 11.914 12.540  20.630  1.00 33.64 ? 268 LEU A CB    1 
ATOM   2000 C CG    . LEU A 1 277 ? 11.691 11.157  21.255  1.00 33.61 ? 268 LEU A CG    1 
ATOM   2001 C CD1   . LEU A 1 277 ? 12.509 10.928  22.522  1.00 36.66 ? 268 LEU A CD1   1 
ATOM   2002 C CD2   . LEU A 1 277 ? 10.219 11.010  21.573  1.00 40.90 ? 268 LEU A CD2   1 
ATOM   2003 N N     . HIS A 1 278 ? 12.322 14.616  18.343  1.00 30.88 ? 269 HIS A N     1 
ATOM   2004 C CA    . HIS A 1 278 ? 12.381 16.025  17.958  1.00 35.21 ? 269 HIS A CA    1 
ATOM   2005 C C     . HIS A 1 278 ? 11.553 16.329  16.708  1.00 34.67 ? 269 HIS A C     1 
ATOM   2006 O O     . HIS A 1 278 ? 11.020 17.439  16.592  1.00 40.00 ? 269 HIS A O     1 
ATOM   2007 C CB    . HIS A 1 278 ? 13.846 16.459  17.784  1.00 34.29 ? 269 HIS A CB    1 
ATOM   2008 C CG    . HIS A 1 278 ? 14.693 16.220  19.008  1.00 41.85 ? 269 HIS A CG    1 
ATOM   2009 N ND1   . HIS A 1 278 ? 16.074 16.278  18.989  1.00 39.37 ? 269 HIS A ND1   1 
ATOM   2010 C CD2   . HIS A 1 278 ? 14.352 15.873  20.276  1.00 41.98 ? 269 HIS A CD2   1 
ATOM   2011 C CE1   . HIS A 1 278 ? 16.543 15.996  20.194  1.00 42.36 ? 269 HIS A CE1   1 
ATOM   2012 N NE2   . HIS A 1 278 ? 15.519 15.745  20.994  1.00 44.73 ? 269 HIS A NE2   1 
ATOM   2013 N N     . SER A 1 279 ? 11.416 15.371  15.782  1.00 34.10 ? 270 SER A N     1 
ATOM   2014 C CA    . SER A 1 279 ? 10.597 15.537  14.579  1.00 28.99 ? 270 SER A CA    1 
ATOM   2015 C C     . SER A 1 279 ? 9.105  15.510  14.859  1.00 33.75 ? 270 SER A C     1 
ATOM   2016 O O     . SER A 1 279 ? 8.324  15.986  14.023  1.00 38.94 ? 270 SER A O     1 
ATOM   2017 C CB    . SER A 1 279 ? 10.873 14.422  13.570  1.00 32.07 ? 270 SER A CB    1 
ATOM   2018 O OG    . SER A 1 279 ? 11.888 14.792  12.652  1.00 35.12 ? 270 SER A OG    1 
ATOM   2019 N N     . GLY A 1 280 ? 8.699  14.913  15.975  1.00 31.05 ? 271 GLY A N     1 
ATOM   2020 C CA    . GLY A 1 280 ? 7.306  14.612  16.239  1.00 32.46 ? 271 GLY A CA    1 
ATOM   2021 C C     . GLY A 1 280 ? 6.753  13.443  15.451  1.00 29.97 ? 271 GLY A C     1 
ATOM   2022 O O     . GLY A 1 280 ? 5.533  13.283  15.364  1.00 28.46 ? 271 GLY A O     1 
ATOM   2023 N N     . SER A 1 281 ? 7.611  12.598  14.886  1.00 27.85 ? 272 SER A N     1 
ATOM   2024 C CA    . SER A 1 281 ? 7.141  11.636  13.906  1.00 21.94 ? 272 SER A CA    1 
ATOM   2025 C C     . SER A 1 281 ? 8.090  10.442  13.896  1.00 26.67 ? 272 SER A C     1 
ATOM   2026 O O     . SER A 1 281 ? 9.258  10.572  14.258  1.00 33.27 ? 272 SER A O     1 
ATOM   2027 C CB    . SER A 1 281 ? 7.047  12.340  12.537  1.00 28.37 ? 272 SER A CB    1 
ATOM   2028 O OG    . SER A 1 281 ? 6.953  11.421  11.454  1.00 38.94 ? 272 SER A OG    1 
ATOM   2029 N N     . LYS A 1 282 ? 7.570  9.280   13.503  1.00 27.49 ? 273 LYS A N     1 
ATOM   2030 C CA    . LYS A 1 282 ? 8.347  8.054   13.351  1.00 21.70 ? 273 LYS A CA    1 
ATOM   2031 C C     . LYS A 1 282 ? 8.984  7.950   11.971  1.00 16.96 ? 273 LYS A C     1 
ATOM   2032 O O     . LYS A 1 282 ? 8.360  8.286   10.971  1.00 17.19 ? 273 LYS A O     1 
ATOM   2033 C CB    . LYS A 1 282 ? 7.449  6.832   13.559  1.00 24.33 ? 273 LYS A CB    1 
ATOM   2034 C CG    . LYS A 1 282 ? 6.842  6.832   14.913  1.00 31.66 ? 273 LYS A CG    1 
ATOM   2035 C CD    . LYS A 1 282 ? 7.924  6.507   15.897  1.00 27.36 ? 273 LYS A CD    1 
ATOM   2036 C CE    . LYS A 1 282 ? 7.433  5.515   16.937  1.00 33.45 ? 273 LYS A CE    1 
ATOM   2037 N NZ    . LYS A 1 282 ? 7.588  6.116   18.274  1.00 35.95 ? 273 LYS A NZ    1 
ATOM   2038 N N     . LEU A 1 283 ? 10.204 7.413   11.922  1.00 15.10 ? 274 LEU A N     1 
ATOM   2039 C CA    . LEU A 1 283 ? 10.775 6.906   10.665  1.00 17.07 ? 274 LEU A CA    1 
ATOM   2040 C C     . LEU A 1 283 ? 9.919  5.777   10.086  1.00 19.52 ? 274 LEU A C     1 
ATOM   2041 O O     . LEU A 1 283 ? 9.101  5.148   10.782  1.00 13.99 ? 274 LEU A O     1 
ATOM   2042 C CB    . LEU A 1 283 ? 12.204 6.396   10.906  1.00 14.68 ? 274 LEU A CB    1 
ATOM   2043 C CG    . LEU A 1 283 ? 13.220 7.491   11.284  1.00 18.68 ? 274 LEU A CG    1 
ATOM   2044 C CD1   . LEU A 1 283 ? 14.513 6.879   11.804  1.00 17.75 ? 274 LEU A CD1   1 
ATOM   2045 C CD2   . LEU A 1 283 ? 13.526 8.457   10.128  1.00 14.87 ? 274 LEU A CD2   1 
ATOM   2046 N N     . ALA A 1 284 ? 10.082 5.529   8.772   1.00 15.78 ? 275 ALA A N     1 
ATOM   2047 C CA    . ALA A 1 284 ? 9.431  4.360   8.193   1.00 12.77 ? 275 ALA A CA    1 
ATOM   2048 C C     . ALA A 1 284 ? 9.875  3.088   8.918   1.00 12.35 ? 275 ALA A C     1 
ATOM   2049 O O     . ALA A 1 284 ? 9.043  2.232   9.252   1.00 15.55 ? 275 ALA A O     1 
ATOM   2050 C CB    . ALA A 1 284 ? 9.716  4.255   6.680   1.00 14.44 ? 275 ALA A CB    1 
ATOM   2051 N N     . TYR A 1 285 ? 11.184 2.934   9.168   1.00 14.92 ? 276 TYR A N     1 
ATOM   2052 C CA    . TYR A 1 285 ? 11.725 1.722   9.799   1.00 14.12 ? 276 TYR A CA    1 
ATOM   2053 C C     . TYR A 1 285 ? 13.227 1.834   10.007  1.00 11.46 ? 276 TYR A C     1 
ATOM   2054 O O     . TYR A 1 285 ? 13.903 2.667   9.393   1.00 13.70 ? 276 TYR A O     1 
ATOM   2055 C CB    . TYR A 1 285 ? 11.479 0.480   8.956   1.00 11.26 ? 276 TYR A CB    1 
ATOM   2056 C CG    . TYR A 1 285 ? 12.049 0.615   7.555   1.00 13.15 ? 276 TYR A CG    1 
ATOM   2057 C CD1   . TYR A 1 285 ? 13.410 0.354   7.298   1.00 13.68 ? 276 TYR A CD1   1 
ATOM   2058 C CD2   . TYR A 1 285 ? 11.234 0.997   6.481   1.00 15.90 ? 276 TYR A CD2   1 
ATOM   2059 C CE1   . TYR A 1 285 ? 13.915 0.448   6.002   1.00 12.36 ? 276 TYR A CE1   1 
ATOM   2060 C CE2   . TYR A 1 285 ? 11.735 1.101   5.188   1.00 14.49 ? 276 TYR A CE2   1 
ATOM   2061 C CZ    . TYR A 1 285 ? 13.085 0.832   4.970   1.00 13.02 ? 276 TYR A CZ    1 
ATOM   2062 O OH    . TYR A 1 285 ? 13.601 0.936   3.716   1.00 15.89 ? 276 TYR A OH    1 
ATOM   2063 N N     . LEU A 1 286 ? 13.728 0.969   10.882  1.00 12.10 ? 277 LEU A N     1 
ATOM   2064 C CA    . LEU A 1 286 ? 15.144 0.652   11.005  1.00 14.34 ? 277 LEU A CA    1 
ATOM   2065 C C     . LEU A 1 286 ? 15.303 -0.745  10.423  1.00 15.78 ? 277 LEU A C     1 
ATOM   2066 O O     . LEU A 1 286 ? 14.505 -1.626  10.729  1.00 12.94 ? 277 LEU A O     1 
ATOM   2067 C CB    . LEU A 1 286 ? 15.575 0.697   12.481  1.00 12.59 ? 277 LEU A CB    1 
ATOM   2068 C CG    . LEU A 1 286 ? 16.963 0.164   12.756  1.00 13.61 ? 277 LEU A CG    1 
ATOM   2069 C CD1   . LEU A 1 286 ? 17.999 1.072   12.111  1.00 14.12 ? 277 LEU A CD1   1 
ATOM   2070 C CD2   . LEU A 1 286 ? 17.230 -0.004  14.286  1.00 18.05 ? 277 LEU A CD2   1 
ATOM   2071 N N     . HIS A 1 287 ? 16.312 -0.929  9.575   1.00 14.33 ? 278 HIS A N     1 
ATOM   2072 C CA    . HIS A 1 287 ? 16.529 -2.139  8.774   1.00 10.62 ? 278 HIS A CA    1 
ATOM   2073 C C     . HIS A 1 287 ? 17.931 -2.612  9.131   1.00 11.45 ? 278 HIS A C     1 
ATOM   2074 O O     . HIS A 1 287 ? 18.899 -1.944  8.796   1.00 14.86 ? 278 HIS A O     1 
ATOM   2075 C CB    . HIS A 1 287 ? 16.426 -1.763  7.294   1.00 9.29  ? 278 HIS A CB    1 
ATOM   2076 C CG    . HIS A 1 287 ? 16.473 -2.903  6.325   1.00 13.39 ? 278 HIS A CG    1 
ATOM   2077 N ND1   . HIS A 1 287 ? 16.338 -2.697  4.963   1.00 13.20 ? 278 HIS A ND1   1 
ATOM   2078 C CD2   . HIS A 1 287 ? 16.603 -4.239  6.497   1.00 12.50 ? 278 HIS A CD2   1 
ATOM   2079 C CE1   . HIS A 1 287 ? 16.387 -3.862  4.342   1.00 14.88 ? 278 HIS A CE1   1 
ATOM   2080 N NE2   . HIS A 1 287 ? 16.550 -4.811  5.245   1.00 15.35 ? 278 HIS A NE2   1 
ATOM   2081 N N     . VAL A 1 288 ? 18.044 -3.714  9.865   1.00 13.10 ? 279 VAL A N     1 
ATOM   2082 C CA    . VAL A 1 288 ? 19.341 -4.189  10.327  1.00 13.08 ? 279 VAL A CA    1 
ATOM   2083 C C     . VAL A 1 288 ? 19.665 -5.466  9.568   1.00 11.97 ? 279 VAL A C     1 
ATOM   2084 O O     . VAL A 1 288 ? 18.867 -6.404  9.550   1.00 13.45 ? 279 VAL A O     1 
ATOM   2085 C CB    . VAL A 1 288 ? 19.362 -4.428  11.847  1.00 15.31 ? 279 VAL A CB    1 
ATOM   2086 C CG1   . VAL A 1 288 ? 20.702 -5.075  12.215  1.00 12.30 ? 279 VAL A CG1   1 
ATOM   2087 C CG2   . VAL A 1 288 ? 19.182 -3.066  12.593  1.00 14.96 ? 279 VAL A CG2   1 
ATOM   2088 N N     . THR A 1 289 ? 20.854 -5.538  8.987   1.00 11.83 ? 280 THR A N     1 
ATOM   2089 C CA    . THR A 1 289 ? 21.221 -6.728  8.240   1.00 12.62 ? 280 THR A CA    1 
ATOM   2090 C C     . THR A 1 289 ? 22.495 -7.336  8.834   1.00 16.18 ? 280 THR A C     1 
ATOM   2091 O O     . THR A 1 289 ? 23.355 -6.611  9.362   1.00 15.95 ? 280 THR A O     1 
ATOM   2092 C CB    . THR A 1 289 ? 21.370 -6.386  6.742   1.00 16.78 ? 280 THR A CB    1 
ATOM   2093 O OG1   . THR A 1 289 ? 21.493 -7.609  5.995   1.00 18.49 ? 280 THR A OG1   1 
ATOM   2094 C CG2   . THR A 1 289 ? 22.567 -5.510  6.526   1.00 14.42 ? 280 THR A CG2   1 
ATOM   2095 N N     . GLN A 1 290 ? 22.545 -8.672  8.855   1.00 16.17 ? 281 GLN A N     1 
ATOM   2096 C CA    . GLN A 1 290 ? 23.556 -9.464  9.537   1.00 19.03 ? 281 GLN A CA    1 
ATOM   2097 C C     . GLN A 1 290 ? 24.218 -10.404 8.544   1.00 17.51 ? 281 GLN A C     1 
ATOM   2098 O O     . GLN A 1 290 ? 23.649 -10.697 7.490   1.00 16.60 ? 281 GLN A O     1 
ATOM   2099 C CB    . GLN A 1 290 ? 22.925 -10.302 10.670  1.00 18.84 ? 281 GLN A CB    1 
ATOM   2100 C CG    . GLN A 1 290 ? 21.981 -11.390 10.149  1.00 15.57 ? 281 GLN A CG    1 
ATOM   2101 C CD    . GLN A 1 290 ? 21.194 -12.117 11.244  1.00 18.61 ? 281 GLN A CD    1 
ATOM   2102 O OE1   . GLN A 1 290 ? 21.353 -11.843 12.430  1.00 19.91 ? 281 GLN A OE1   1 
ATOM   2103 N NE2   . GLN A 1 290 ? 20.373 -13.092 10.838  1.00 18.31 ? 281 GLN A NE2   1 
ATOM   2104 N N     . PRO A 1 291 ? 25.392 -10.949 8.869   1.00 17.51 ? 282 PRO A N     1 
ATOM   2105 C CA    . PRO A 1 291 ? 25.992 -11.952 7.982   1.00 19.89 ? 282 PRO A CA    1 
ATOM   2106 C C     . PRO A 1 291 ? 25.017 -13.095 7.714   1.00 23.70 ? 282 PRO A C     1 
ATOM   2107 O O     . PRO A 1 291 ? 24.324 -13.574 8.618   1.00 22.87 ? 282 PRO A O     1 
ATOM   2108 C CB    . PRO A 1 291 ? 27.211 -12.426 8.776   1.00 21.13 ? 282 PRO A CB    1 
ATOM   2109 C CG    . PRO A 1 291 ? 27.598 -11.232 9.615   1.00 19.69 ? 282 PRO A CG    1 
ATOM   2110 C CD    . PRO A 1 291 ? 26.218 -10.721 10.071  1.00 19.09 ? 282 PRO A CD    1 
ATOM   2111 N N     . GLY A 1 292 ? 24.941 -13.490 6.449   1.00 21.03 ? 283 GLY A N     1 
ATOM   2112 C CA    . GLY A 1 292 ? 24.081 -14.557 5.965   1.00 24.19 ? 283 GLY A CA    1 
ATOM   2113 C C     . GLY A 1 292 ? 24.354 -15.897 6.632   1.00 31.78 ? 283 GLY A C     1 
ATOM   2114 O O     . GLY A 1 292 ? 23.460 -16.435 7.286   1.00 29.99 ? 283 GLY A O     1 
ATOM   2115 N N     . ASP A 1 293 ? 25.563 -16.450 6.469   1.00 32.90 ? 284 ASP A N     1 
ATOM   2116 C CA    . ASP A 1 293 ? 25.934 -17.730 7.088   1.00 38.67 ? 284 ASP A CA    1 
ATOM   2117 C C     . ASP A 1 293 ? 26.282 -17.477 8.547   1.00 42.95 ? 284 ASP A C     1 
ATOM   2118 O O     . ASP A 1 293 ? 27.374 -16.996 8.858   1.00 48.37 ? 284 ASP A O     1 
ATOM   2119 C CB    . ASP A 1 293 ? 27.111 -18.374 6.367   1.00 32.87 ? 284 ASP A CB    1 
ATOM   2120 N N     . GLY A 1 294 ? 25.349 -17.795 9.444   1.00 42.01 ? 285 GLY A N     1 
ATOM   2121 C CA    . GLY A 1 294 ? 25.531 -17.581 10.874  1.00 47.42 ? 285 GLY A CA    1 
ATOM   2122 C C     . GLY A 1 294 ? 25.765 -18.864 11.663  1.00 56.93 ? 285 GLY A C     1 
ATOM   2123 O O     . GLY A 1 294 ? 25.147 -19.099 12.708  1.00 55.83 ? 285 GLY A O     1 
ATOM   2124 N N     . SER A 1 297 ? 27.825 -18.626 14.816  1.00 49.65 ? 288 SER A N     1 
ATOM   2125 C CA    . SER A 1 297 ? 27.518 -17.903 16.051  1.00 47.55 ? 288 SER A CA    1 
ATOM   2126 C C     . SER A 1 297 ? 26.052 -17.484 16.061  1.00 44.30 ? 288 SER A C     1 
ATOM   2127 O O     . SER A 1 297 ? 25.745 -16.300 16.206  1.00 47.15 ? 288 SER A O     1 
ATOM   2128 C CB    . SER A 1 297 ? 28.419 -16.673 16.203  1.00 44.38 ? 288 SER A CB    1 
ATOM   2129 N N     . GLU A 1 298 ? 25.157 -18.465 15.935  1.00 44.84 ? 289 GLU A N     1 
ATOM   2130 C CA    . GLU A 1 298 ? 23.746 -18.208 15.674  1.00 46.07 ? 289 GLU A CA    1 
ATOM   2131 C C     . GLU A 1 298 ? 23.075 -17.446 16.809  1.00 48.56 ? 289 GLU A C     1 
ATOM   2132 O O     . GLU A 1 298 ? 22.681 -16.288 16.635  1.00 49.39 ? 289 GLU A O     1 
ATOM   2133 C CB    . GLU A 1 298 ? 22.994 -19.517 15.424  1.00 43.20 ? 289 GLU A CB    1 
ATOM   2134 N N     . GLU A 1 299 ? 22.922 -18.087 17.970  1.00 44.22 ? 290 GLU A N     1 
ATOM   2135 C CA    . GLU A 1 299 ? 22.194 -17.450 19.063  1.00 49.03 ? 290 GLU A CA    1 
ATOM   2136 C C     . GLU A 1 299 ? 22.786 -16.096 19.449  1.00 44.47 ? 290 GLU A C     1 
ATOM   2137 O O     . GLU A 1 299 ? 22.060 -15.253 19.991  1.00 48.21 ? 290 GLU A O     1 
ATOM   2138 C CB    . GLU A 1 299 ? 22.148 -18.382 20.276  1.00 47.72 ? 290 GLU A CB    1 
ATOM   2139 N N     . GLU A 1 300 ? 24.076 -15.863 19.170  1.00 40.97 ? 291 GLU A N     1 
ATOM   2140 C CA    . GLU A 1 300 ? 24.695 -14.569 19.451  1.00 30.76 ? 291 GLU A CA    1 
ATOM   2141 C C     . GLU A 1 300 ? 24.379 -13.539 18.372  1.00 42.94 ? 291 GLU A C     1 
ATOM   2142 O O     . GLU A 1 300 ? 24.282 -12.336 18.653  1.00 40.49 ? 291 GLU A O     1 
ATOM   2143 C CB    . GLU A 1 300 ? 26.207 -14.717 19.543  1.00 29.43 ? 291 GLU A CB    1 
ATOM   2144 N N     . GLU A 1 301 ? 24.304 -13.969 17.114  1.00 41.93 ? 292 GLU A N     1 
ATOM   2145 C CA    . GLU A 1 301 ? 23.803 -13.058 16.098  1.00 36.04 ? 292 GLU A CA    1 
ATOM   2146 C C     . GLU A 1 301 ? 22.383 -12.641 16.442  1.00 34.73 ? 292 GLU A C     1 
ATOM   2147 O O     . GLU A 1 301 ? 21.993 -11.482 16.221  1.00 28.60 ? 292 GLU A O     1 
ATOM   2148 C CB    . GLU A 1 301 ? 23.868 -13.718 14.721  1.00 36.73 ? 292 GLU A CB    1 
ATOM   2149 N N     . ALA A 1 302 ? 21.623 -13.566 17.044  1.00 34.11 ? 293 ALA A N     1 
ATOM   2150 C CA    . ALA A 1 302 ? 20.264 -13.268 17.475  1.00 35.94 ? 293 ALA A CA    1 
ATOM   2151 C C     . ALA A 1 302 ? 20.252 -12.269 18.628  1.00 37.93 ? 293 ALA A C     1 
ATOM   2152 O O     . ALA A 1 302 ? 19.362 -11.410 18.692  1.00 36.16 ? 293 ALA A O     1 
ATOM   2153 C CB    . ALA A 1 302 ? 19.546 -14.559 17.852  1.00 37.83 ? 293 ALA A CB    1 
ATOM   2154 N N     . ARG A 1 303 ? 21.225 -12.366 19.545  1.00 37.53 ? 294 ARG A N     1 
ATOM   2155 C CA    . ARG A 1 303 ? 21.373 -11.381 20.613  1.00 38.91 ? 294 ARG A CA    1 
ATOM   2156 C C     . ARG A 1 303 ? 21.384 -9.982  20.045  1.00 30.00 ? 294 ARG A C     1 
ATOM   2157 O O     . ARG A 1 303 ? 20.552 -9.147  20.412  1.00 30.22 ? 294 ARG A O     1 
ATOM   2158 C CB    . ARG A 1 303 ? 22.672 -11.582 21.412  1.00 42.58 ? 294 ARG A CB    1 
ATOM   2159 C CG    . ARG A 1 303 ? 22.613 -12.458 22.670  1.00 37.87 ? 294 ARG A CG    1 
ATOM   2160 C CD    . ARG A 1 303 ? 24.003 -12.444 23.339  1.00 32.82 ? 294 ARG A CD    1 
ATOM   2161 N NE    . ARG A 1 303 ? 24.165 -13.488 24.341  1.00 40.42 ? 294 ARG A NE    1 
ATOM   2162 C CZ    . ARG A 1 303 ? 25.312 -13.769 24.950  1.00 44.69 ? 294 ARG A CZ    1 
ATOM   2163 N NH1   . ARG A 1 303 ? 26.392 -13.026 24.762  1.00 48.30 ? 294 ARG A NH1   1 
ATOM   2164 N NH2   . ARG A 1 303 ? 25.382 -14.831 25.760  1.00 40.98 ? 294 ARG A NH2   1 
ATOM   2165 N N     . LEU A 1 304 ? 22.355 -9.710  19.165  1.00 26.69 ? 295 LEU A N     1 
ATOM   2166 C CA    . LEU A 1 304 ? 22.475 -8.392  18.549  1.00 29.78 ? 295 LEU A CA    1 
ATOM   2167 C C     . LEU A 1 304 ? 21.165 -7.956  17.903  1.00 24.04 ? 295 LEU A C     1 
ATOM   2168 O O     . LEU A 1 304 ? 20.707 -6.822  18.095  1.00 22.09 ? 295 LEU A O     1 
ATOM   2169 C CB    . LEU A 1 304 ? 23.598 -8.382  17.509  1.00 24.48 ? 295 LEU A CB    1 
ATOM   2170 C CG    . LEU A 1 304 ? 23.868 -7.024  16.854  1.00 25.33 ? 295 LEU A CG    1 
ATOM   2171 C CD1   . LEU A 1 304 ? 25.364 -6.716  16.862  1.00 35.61 ? 295 LEU A CD1   1 
ATOM   2172 C CD2   . LEU A 1 304 ? 23.339 -6.979  15.430  1.00 32.79 ? 295 LEU A CD2   1 
ATOM   2173 N N     . MET A 1 305 ? 20.556 -8.831  17.113  1.00 19.74 ? 296 MET A N     1 
ATOM   2174 C CA    . MET A 1 305 ? 19.335 -8.427  16.429  1.00 23.37 ? 296 MET A CA    1 
ATOM   2175 C C     . MET A 1 305 ? 18.227 -8.061  17.424  1.00 19.65 ? 296 MET A C     1 
ATOM   2176 O O     . MET A 1 305 ? 17.582 -7.019  17.292  1.00 19.30 ? 296 MET A O     1 
ATOM   2177 C CB    . MET A 1 305 ? 18.913 -9.532  15.444  1.00 24.15 ? 296 MET A CB    1 
ATOM   2178 C CG    . MET A 1 305 ? 17.928 -9.016  14.412  1.00 26.93 ? 296 MET A CG    1 
ATOM   2179 S SD    . MET A 1 305 ? 18.610 -7.973  13.123  1.00 21.77 ? 296 MET A SD    1 
ATOM   2180 C CE    . MET A 1 305 ? 19.586 -9.040  12.031  1.00 21.85 ? 296 MET A CE    1 
ATOM   2181 N N     . ARG A 1 306 ? 18.009 -8.878  18.458  1.00 25.68 ? 297 ARG A N     1 
ATOM   2182 C CA    . ARG A 1 306 ? 16.912 -8.572  19.374  1.00 23.36 ? 297 ARG A CA    1 
ATOM   2183 C C     . ARG A 1 306 ? 17.202 -7.316  20.191  1.00 22.22 ? 297 ARG A C     1 
ATOM   2184 O O     . ARG A 1 306 ? 16.292 -6.510  20.436  1.00 23.71 ? 297 ARG A O     1 
ATOM   2185 C CB    . ARG A 1 306 ? 16.642 -9.778  20.272  1.00 28.50 ? 297 ARG A CB    1 
ATOM   2186 C CG    . ARG A 1 306 ? 15.256 -9.796  20.927  1.00 40.57 ? 297 ARG A CG    1 
ATOM   2187 C CD    . ARG A 1 306 ? 14.115 -9.532  19.917  1.00 35.34 ? 297 ARG A CD    1 
ATOM   2188 N NE    . ARG A 1 306 ? 13.033 -8.720  20.478  1.00 35.91 ? 297 ARG A NE    1 
ATOM   2189 C CZ    . ARG A 1 306 ? 11.884 -9.208  20.939  1.00 39.96 ? 297 ARG A CZ    1 
ATOM   2190 N NH1   . ARG A 1 306 ? 11.594 -10.502 20.855  1.00 34.92 ? 297 ARG A NH1   1 
ATOM   2191 N NH2   . ARG A 1 306 ? 10.980 -8.371  21.445  1.00 37.57 ? 297 ARG A NH2   1 
ATOM   2192 N N     . THR A 1 307 ? 18.472 -7.089  20.547  1.00 22.23 ? 298 THR A N     1 
ATOM   2193 C CA    . THR A 1 307 ? 18.845 -5.941  21.370  1.00 21.41 ? 298 THR A CA    1 
ATOM   2194 C C     . THR A 1 307 ? 18.623 -4.625  20.631  1.00 21.62 ? 298 THR A C     1 
ATOM   2195 O O     . THR A 1 307 ? 18.129 -3.648  21.217  1.00 17.91 ? 298 THR A O     1 
ATOM   2196 C CB    . THR A 1 307 ? 20.308 -6.078  21.812  1.00 25.15 ? 298 THR A CB    1 
ATOM   2197 O OG1   . THR A 1 307 ? 20.466 -7.307  22.534  1.00 31.75 ? 298 THR A OG1   1 
ATOM   2198 C CG2   . THR A 1 307 ? 20.725 -4.946  22.679  1.00 26.56 ? 298 THR A CG2   1 
ATOM   2199 N N     . LEU A 1 308 ? 18.989 -4.577  19.342  1.00 19.45 ? 299 LEU A N     1 
ATOM   2200 C CA    . LEU A 1 308 ? 18.730 -3.385  18.535  1.00 17.26 ? 299 LEU A CA    1 
ATOM   2201 C C     . LEU A 1 308 ? 17.229 -3.174  18.351  1.00 19.64 ? 299 LEU A C     1 
ATOM   2202 O O     . LEU A 1 308 ? 16.733 -2.049  18.504  1.00 17.63 ? 299 LEU A O     1 
ATOM   2203 C CB    . LEU A 1 308 ? 19.433 -3.494  17.180  1.00 20.56 ? 299 LEU A CB    1 
ATOM   2204 C CG    . LEU A 1 308 ? 20.965 -3.622  17.249  1.00 25.55 ? 299 LEU A CG    1 
ATOM   2205 C CD1   . LEU A 1 308 ? 21.604 -3.599  15.850  1.00 26.31 ? 299 LEU A CD1   1 
ATOM   2206 C CD2   . LEU A 1 308 ? 21.585 -2.523  18.109  1.00 20.72 ? 299 LEU A CD2   1 
ATOM   2207 N N     . ARG A 1 309 ? 16.488 -4.250  18.053  1.00 17.75 ? 300 ARG A N     1 
ATOM   2208 C CA    . ARG A 1 309 ? 15.040 -4.125  17.915  1.00 16.49 ? 300 ARG A CA    1 
ATOM   2209 C C     . ARG A 1 309 ? 14.419 -3.593  19.199  1.00 16.37 ? 300 ARG A C     1 
ATOM   2210 O O     . ARG A 1 309 ? 13.575 -2.691  19.172  1.00 18.41 ? 300 ARG A O     1 
ATOM   2211 C CB    . ARG A 1 309 ? 14.424 -5.478  17.546  1.00 18.03 ? 300 ARG A CB    1 
ATOM   2212 C CG    . ARG A 1 309 ? 12.941 -5.420  17.069  1.00 17.78 ? 300 ARG A CG    1 
ATOM   2213 C CD    . ARG A 1 309 ? 11.916 -5.390  18.239  1.00 17.10 ? 300 ARG A CD    1 
ATOM   2214 N NE    . ARG A 1 309 ? 10.664 -6.012  17.836  1.00 18.06 ? 300 ARG A NE    1 
ATOM   2215 C CZ    . ARG A 1 309 ? 9.824  -5.481  16.956  1.00 18.07 ? 300 ARG A CZ    1 
ATOM   2216 N NH1   . ARG A 1 309 ? 9.991  -4.245  16.490  1.00 18.10 ? 300 ARG A NH1   1 
ATOM   2217 N NH2   . ARG A 1 309 ? 8.805  -6.208  16.520  1.00 21.73 ? 300 ARG A NH2   1 
ATOM   2218 N N     . ASN A 1 310 ? 14.799 -4.169  20.338  1.00 15.25 ? 301 ASN A N     1 
ATOM   2219 C CA    . ASN A 1 310 ? 14.215 -3.735  21.611  1.00 15.84 ? 301 ASN A CA    1 
ATOM   2220 C C     . ASN A 1 310 ? 14.547 -2.295  21.942  1.00 16.89 ? 301 ASN A C     1 
ATOM   2221 O O     . ASN A 1 310 ? 13.776 -1.619  22.639  1.00 16.97 ? 301 ASN A O     1 
ATOM   2222 C CB    . ASN A 1 310 ? 14.717 -4.630  22.724  1.00 18.24 ? 301 ASN A CB    1 
ATOM   2223 C CG    . ASN A 1 310 ? 14.021 -5.945  22.739  1.00 18.09 ? 301 ASN A CG    1 
ATOM   2224 O OD1   . ASN A 1 310 ? 12.955 -6.100  22.150  1.00 22.22 ? 301 ASN A OD1   1 
ATOM   2225 N ND2   . ASN A 1 310 ? 14.606 -6.911  23.412  1.00 19.29 ? 301 ASN A ND2   1 
ATOM   2226 N N     . ALA A 1 311 ? 15.703 -1.816  21.485  1.00 13.75 ? 302 ALA A N     1 
ATOM   2227 C CA    . ALA A 1 311 ? 16.124 -0.451  21.754  1.00 14.20 ? 302 ALA A CA    1 
ATOM   2228 C C     . ALA A 1 311 ? 15.380 0.584   20.924  1.00 15.15 ? 302 ALA A C     1 
ATOM   2229 O O     . ALA A 1 311 ? 15.354 1.760   21.303  1.00 16.69 ? 302 ALA A O     1 
ATOM   2230 C CB    . ALA A 1 311 ? 17.622 -0.302  21.481  1.00 16.33 ? 302 ALA A CB    1 
ATOM   2231 N N     . TYR A 1 312 ? 14.890 0.201   19.745  1.00 13.47 ? 303 TYR A N     1 
ATOM   2232 C CA    . TYR A 1 312 ? 14.438 1.148   18.730  1.00 16.62 ? 303 TYR A CA    1 
ATOM   2233 C C     . TYR A 1 312 ? 12.921 1.367   18.822  1.00 17.20 ? 303 TYR A C     1 
ATOM   2234 O O     . TYR A 1 312 ? 12.148 0.407   18.797  1.00 17.92 ? 303 TYR A O     1 
ATOM   2235 C CB    . TYR A 1 312 ? 14.833 0.653   17.330  1.00 16.32 ? 303 TYR A CB    1 
ATOM   2236 C CG    . TYR A 1 312 ? 14.198 1.515   16.271  1.00 13.84 ? 303 TYR A CG    1 
ATOM   2237 C CD1   . TYR A 1 312 ? 14.368 2.880   16.299  1.00 15.06 ? 303 TYR A CD1   1 
ATOM   2238 C CD2   . TYR A 1 312 ? 13.377 0.965   15.305  1.00 15.83 ? 303 TYR A CD2   1 
ATOM   2239 C CE1   . TYR A 1 312 ? 13.757 3.716   15.345  1.00 16.47 ? 303 TYR A CE1   1 
ATOM   2240 C CE2   . TYR A 1 312 ? 12.720 1.787   14.349  1.00 15.03 ? 303 TYR A CE2   1 
ATOM   2241 C CZ    . TYR A 1 312 ? 12.916 3.176   14.418  1.00 15.02 ? 303 TYR A CZ    1 
ATOM   2242 O OH    . TYR A 1 312 ? 12.350 4.036   13.509  1.00 16.45 ? 303 TYR A OH    1 
ATOM   2243 N N     . GLN A 1 313 ? 12.498 2.633   18.918  1.00 15.88 ? 304 GLN A N     1 
ATOM   2244 C CA    . GLN A 1 313 ? 11.065 2.961   19.013  1.00 16.56 ? 304 GLN A CA    1 
ATOM   2245 C C     . GLN A 1 313 ? 10.455 3.025   17.609  1.00 16.23 ? 304 GLN A C     1 
ATOM   2246 O O     . GLN A 1 313 ? 10.189 4.092   17.055  1.00 19.86 ? 304 GLN A O     1 
ATOM   2247 C CB    . GLN A 1 313 ? 10.867 4.287   19.754  1.00 18.76 ? 304 GLN A CB    1 
ATOM   2248 C CG    . GLN A 1 313 ? 11.343 4.269   21.203  1.00 18.98 ? 304 GLN A CG    1 
ATOM   2249 C CD    . GLN A 1 313 ? 11.248 5.626   21.867  1.00 25.54 ? 304 GLN A CD    1 
ATOM   2250 O OE1   . GLN A 1 313 ? 10.538 6.507   21.402  1.00 21.13 ? 304 GLN A OE1   1 
ATOM   2251 N NE2   . GLN A 1 313 ? 11.975 5.794   22.959  1.00 23.26 ? 304 GLN A NE2   1 
ATOM   2252 N N     . GLY A 1 314 ? 10.192 1.866   17.026  1.00 16.93 ? 305 GLY A N     1 
ATOM   2253 C CA    . GLY A 1 314 ? 9.557  1.885   15.722  1.00 15.72 ? 305 GLY A CA    1 
ATOM   2254 C C     . GLY A 1 314 ? 9.644  0.537   15.037  1.00 15.19 ? 305 GLY A C     1 
ATOM   2255 O O     . GLY A 1 314 ? 9.926  -0.495  15.647  1.00 17.15 ? 305 GLY A O     1 
ATOM   2256 N N     . THR A 1 315 ? 9.324  0.587   13.763  1.00 18.23 ? 306 THR A N     1 
ATOM   2257 C CA    . THR A 1 315 ? 9.280  -0.581  12.906  1.00 14.63 ? 306 THR A CA    1 
ATOM   2258 C C     . THR A 1 315 ? 10.687 -1.114  12.633  1.00 13.89 ? 306 THR A C     1 
ATOM   2259 O O     . THR A 1 315 ? 11.617 -0.355  12.312  1.00 13.24 ? 306 THR A O     1 
ATOM   2260 C CB    . THR A 1 315 ? 8.587  -0.180  11.604  1.00 18.32 ? 306 THR A CB    1 
ATOM   2261 O OG1   . THR A 1 315 ? 7.216  0.128   11.900  1.00 18.52 ? 306 THR A OG1   1 
ATOM   2262 C CG2   . THR A 1 315 ? 8.676  -1.297  10.569  1.00 15.27 ? 306 THR A CG2   1 
ATOM   2263 N N     . PHE A 1 316 ? 10.838 -2.429  12.724  1.00 14.76 ? 307 PHE A N     1 
ATOM   2264 C CA    . PHE A 1 316 ? 12.135 -3.080  12.565  1.00 11.12 ? 307 PHE A CA    1 
ATOM   2265 C C     . PHE A 1 316 ? 12.070 -4.137  11.465  1.00 13.86 ? 307 PHE A C     1 
ATOM   2266 O O     . PHE A 1 316 ? 11.219 -5.036  11.511  1.00 12.05 ? 307 PHE A O     1 
ATOM   2267 C CB    . PHE A 1 316 ? 12.533 -3.733  13.911  1.00 15.31 ? 307 PHE A CB    1 
ATOM   2268 C CG    . PHE A 1 316 ? 13.976 -4.230  13.996  1.00 13.34 ? 307 PHE A CG    1 
ATOM   2269 C CD1   . PHE A 1 316 ? 14.985 -3.370  14.421  1.00 16.74 ? 307 PHE A CD1   1 
ATOM   2270 C CD2   . PHE A 1 316 ? 14.290 -5.566  13.697  1.00 18.34 ? 307 PHE A CD2   1 
ATOM   2271 C CE1   . PHE A 1 316 ? 16.293 -3.788  14.541  1.00 18.08 ? 307 PHE A CE1   1 
ATOM   2272 C CE2   . PHE A 1 316 ? 15.613 -6.010  13.787  1.00 17.92 ? 307 PHE A CE2   1 
ATOM   2273 C CZ    . PHE A 1 316 ? 16.618 -5.121  14.216  1.00 20.12 ? 307 PHE A CZ    1 
ATOM   2274 N N     . ILE A 1 317 ? 13.007 -4.065  10.520  1.00 14.38 ? 308 ILE A N     1 
ATOM   2275 C CA    . ILE A 1 317 ? 13.138 -5.045  9.439   1.00 13.18 ? 308 ILE A CA    1 
ATOM   2276 C C     . ILE A 1 317 ? 14.426 -5.810  9.702   1.00 13.86 ? 308 ILE A C     1 
ATOM   2277 O O     . ILE A 1 317 ? 15.495 -5.192  9.764   1.00 13.06 ? 308 ILE A O     1 
ATOM   2278 C CB    . ILE A 1 317 ? 13.239 -4.383  8.058   1.00 12.43 ? 308 ILE A CB    1 
ATOM   2279 C CG1   . ILE A 1 317 ? 12.064 -3.435  7.791   1.00 12.10 ? 308 ILE A CG1   1 
ATOM   2280 C CG2   . ILE A 1 317 ? 13.261 -5.481  6.981   1.00 11.77 ? 308 ILE A CG2   1 
ATOM   2281 C CD1   . ILE A 1 317 ? 12.059 -2.770  6.377   1.00 12.71 ? 308 ILE A CD1   1 
ATOM   2282 N N     . CYS A 1 318 ? 14.342 -7.131  9.818   1.00 17.07 ? 309 CYS A N     1 
ATOM   2283 C CA    . CYS A 1 318 ? 15.528 -7.966  9.970   1.00 14.37 ? 309 CYS A CA    1 
ATOM   2284 C C     . CYS A 1 318 ? 15.909 -8.566  8.626   1.00 15.65 ? 309 CYS A C     1 
ATOM   2285 O O     . CYS A 1 318 ? 15.065 -8.722  7.737   1.00 17.25 ? 309 CYS A O     1 
ATOM   2286 C CB    . CYS A 1 318 ? 15.315 -9.075  11.007  1.00 17.78 ? 309 CYS A CB    1 
ATOM   2287 S SG    . CYS A 1 318 ? 13.986 -10.193 10.611  1.00 17.57 ? 309 CYS A SG    1 
ATOM   2288 N N     . SER A 1 319 ? 17.197 -8.877  8.471   1.00 17.17 ? 310 SER A N     1 
ATOM   2289 C CA    . SER A 1 319 ? 17.718 -9.242  7.160   1.00 15.20 ? 310 SER A CA    1 
ATOM   2290 C C     . SER A 1 319 ? 19.009 -10.046 7.315   1.00 14.51 ? 310 SER A C     1 
ATOM   2291 O O     . SER A 1 319 ? 19.807 -9.774  8.207   1.00 15.01 ? 310 SER A O     1 
ATOM   2292 C CB    . SER A 1 319 ? 17.971 -7.986  6.322   1.00 14.95 ? 310 SER A CB    1 
ATOM   2293 O OG    . SER A 1 319 ? 18.938 -8.220  5.324   1.00 18.65 ? 310 SER A OG    1 
ATOM   2294 N N     . GLY A 1 320 ? 19.233 -10.995 6.405   1.00 13.54 ? 311 GLY A N     1 
ATOM   2295 C CA    . GLY A 1 320 ? 20.502 -11.704 6.355   1.00 14.33 ? 311 GLY A CA    1 
ATOM   2296 C C     . GLY A 1 320 ? 20.348 -13.178 6.711   1.00 15.04 ? 311 GLY A C     1 
ATOM   2297 O O     . GLY A 1 320 ? 20.234 -13.538 7.883   1.00 17.35 ? 311 GLY A O     1 
ATOM   2298 N N     . GLY A 1 321 ? 20.320 -14.020 5.687   1.00 17.16 ? 312 GLY A N     1 
ATOM   2299 C CA    . GLY A 1 321 ? 20.173 -15.466 5.880   1.00 17.11 ? 312 GLY A CA    1 
ATOM   2300 C C     . GLY A 1 321 ? 18.815 -15.942 6.373   1.00 20.09 ? 312 GLY A C     1 
ATOM   2301 O O     . GLY A 1 321 ? 18.701 -17.086 6.835   1.00 23.27 ? 312 GLY A O     1 
ATOM   2302 N N     . TYR A 1 322 ? 17.769 -15.123 6.299   1.00 16.04 ? 313 TYR A N     1 
ATOM   2303 C CA    . TYR A 1 322 ? 16.455 -15.601 6.713   1.00 18.26 ? 313 TYR A CA    1 
ATOM   2304 C C     . TYR A 1 322 ? 15.861 -16.588 5.710   1.00 19.46 ? 313 TYR A C     1 
ATOM   2305 O O     . TYR A 1 322 ? 16.026 -16.473 4.477   1.00 19.23 ? 313 TYR A O     1 
ATOM   2306 C CB    . TYR A 1 322 ? 15.502 -14.425 6.948   1.00 16.82 ? 313 TYR A CB    1 
ATOM   2307 C CG    . TYR A 1 322 ? 15.837 -13.775 8.282   1.00 13.81 ? 313 TYR A CG    1 
ATOM   2308 C CD1   . TYR A 1 322 ? 15.269 -14.236 9.485   1.00 17.92 ? 313 TYR A CD1   1 
ATOM   2309 C CD2   . TYR A 1 322 ? 16.817 -12.807 8.354   1.00 18.45 ? 313 TYR A CD2   1 
ATOM   2310 C CE1   . TYR A 1 322 ? 15.631 -13.663 10.733  1.00 19.40 ? 313 TYR A CE1   1 
ATOM   2311 C CE2   . TYR A 1 322 ? 17.189 -12.251 9.569   1.00 19.95 ? 313 TYR A CE2   1 
ATOM   2312 C CZ    . TYR A 1 322 ? 16.593 -12.662 10.749  1.00 17.65 ? 313 TYR A CZ    1 
ATOM   2313 O OH    . TYR A 1 322 ? 17.031 -12.046 11.915  1.00 18.03 ? 313 TYR A OH    1 
ATOM   2314 N N     . THR A 1 323 ? 15.209 -17.602 6.256   1.00 18.39 ? 314 THR A N     1 
ATOM   2315 C CA    . THR A 1 323 ? 14.488 -18.612 5.510   1.00 19.76 ? 314 THR A CA    1 
ATOM   2316 C C     . THR A 1 323 ? 13.013 -18.380 5.737   1.00 19.52 ? 314 THR A C     1 
ATOM   2317 O O     . THR A 1 323 ? 12.617 -17.526 6.543   1.00 19.31 ? 314 THR A O     1 
ATOM   2318 C CB    . THR A 1 323 ? 14.896 -20.012 5.979   1.00 20.73 ? 314 THR A CB    1 
ATOM   2319 O OG1   . THR A 1 323 ? 14.575 -20.139 7.386   1.00 21.87 ? 314 THR A OG1   1 
ATOM   2320 C CG2   . THR A 1 323 ? 16.389 -20.201 5.795   1.00 23.47 ? 314 THR A CG2   1 
ATOM   2321 N N     . ARG A 1 324 ? 12.190 -19.178 5.066   1.00 19.11 ? 315 ARG A N     1 
ATOM   2322 C CA    . ARG A 1 324 ? 10.763 -19.123 5.344   1.00 17.93 ? 315 ARG A CA    1 
ATOM   2323 C C     . ARG A 1 324 ? 10.513 -19.337 6.829   1.00 21.64 ? 315 ARG A C     1 
ATOM   2324 O O     . ARG A 1 324 ? 9.849  -18.526 7.478   1.00 19.89 ? 315 ARG A O     1 
ATOM   2325 C CB    . ARG A 1 324 ? 10.008 -20.172 4.536   1.00 18.53 ? 315 ARG A CB    1 
ATOM   2326 C CG    . ARG A 1 324 ? 8.551  -20.287 4.925   1.00 24.66 ? 315 ARG A CG    1 
ATOM   2327 C CD    . ARG A 1 324 ? 7.767  -21.162 3.967   1.00 24.99 ? 315 ARG A CD    1 
ATOM   2328 N NE    . ARG A 1 324 ? 6.348  -21.102 4.279   1.00 23.82 ? 315 ARG A NE    1 
ATOM   2329 C CZ    . ARG A 1 324 ? 5.784  -21.852 5.211   1.00 27.17 ? 315 ARG A CZ    1 
ATOM   2330 N NH1   . ARG A 1 324 ? 6.496  -22.705 5.928   1.00 25.48 ? 315 ARG A NH1   1 
ATOM   2331 N NH2   . ARG A 1 324 ? 4.474  -21.747 5.426   1.00 27.78 ? 315 ARG A NH2   1 
ATOM   2332 N N     . GLU A 1 325 ? 11.060 -20.418 7.388   1.00 18.15 ? 316 GLU A N     1 
ATOM   2333 C CA    . GLU A 1 325 ? 10.765 -20.744 8.791   1.00 18.29 ? 316 GLU A CA    1 
ATOM   2334 C C     . GLU A 1 325 ? 11.330 -19.704 9.757   1.00 18.72 ? 316 GLU A C     1 
ATOM   2335 O O     . GLU A 1 325 ? 10.668 -19.339 10.733  1.00 19.18 ? 316 GLU A O     1 
ATOM   2336 C CB    . GLU A 1 325 ? 11.286 -22.137 9.117   1.00 18.27 ? 316 GLU A CB    1 
ATOM   2337 N N     . LEU A 1 326 ? 12.561 -19.236 9.533   1.00 20.11 ? 317 LEU A N     1 
ATOM   2338 C CA    . LEU A 1 326 ? 13.142 -18.230 10.433  1.00 17.70 ? 317 LEU A CA    1 
ATOM   2339 C C     . LEU A 1 326 ? 12.425 -16.886 10.330  1.00 19.80 ? 317 LEU A C     1 
ATOM   2340 O O     . LEU A 1 326 ? 12.364 -16.136 11.307  1.00 17.89 ? 317 LEU A O     1 
ATOM   2341 C CB    . LEU A 1 326 ? 14.635 -18.049 10.139  1.00 16.62 ? 317 LEU A CB    1 
ATOM   2342 C CG    . LEU A 1 326 ? 15.626 -19.154 10.482  1.00 21.12 ? 317 LEU A CG    1 
ATOM   2343 C CD1   . LEU A 1 326 ? 17.043 -18.764 10.013  1.00 20.37 ? 317 LEU A CD1   1 
ATOM   2344 C CD2   . LEU A 1 326 ? 15.607 -19.456 11.978  1.00 25.74 ? 317 LEU A CD2   1 
ATOM   2345 N N     . GLY A 1 327 ? 11.893 -16.558 9.152   1.00 21.67 ? 318 GLY A N     1 
ATOM   2346 C CA    . GLY A 1 327 ? 11.075 -15.361 9.033   1.00 18.88 ? 318 GLY A CA    1 
ATOM   2347 C C     . GLY A 1 327 ? 9.780  -15.465 9.814   1.00 20.50 ? 318 GLY A C     1 
ATOM   2348 O O     . GLY A 1 327 ? 9.382  -14.515 10.493  1.00 19.95 ? 318 GLY A O     1 
ATOM   2349 N N     . ILE A 1 328 ? 9.111  -16.626 9.735   1.00 17.70 ? 319 ILE A N     1 
ATOM   2350 C CA    . ILE A 1 328 ? 7.886  -16.842 10.505  1.00 20.55 ? 319 ILE A CA    1 
ATOM   2351 C C     . ILE A 1 328 ? 8.181  -16.708 11.988  1.00 18.30 ? 319 ILE A C     1 
ATOM   2352 O O     . ILE A 1 328 ? 7.460  -16.039 12.737  1.00 20.11 ? 319 ILE A O     1 
ATOM   2353 C CB    . ILE A 1 328 ? 7.295  -18.224 10.177  1.00 24.23 ? 319 ILE A CB    1 
ATOM   2354 C CG1   . ILE A 1 328 ? 6.748  -18.242 8.748   1.00 23.04 ? 319 ILE A CG1   1 
ATOM   2355 C CG2   . ILE A 1 328 ? 6.248  -18.661 11.232  1.00 23.99 ? 319 ILE A CG2   1 
ATOM   2356 C CD1   . ILE A 1 328 ? 6.439  -19.652 8.235   1.00 23.05 ? 319 ILE A CD1   1 
ATOM   2357 N N     . GLU A 1 329 ? 9.254  -17.353 12.432  1.00 20.16 ? 320 GLU A N     1 
ATOM   2358 C CA    . GLU A 1 329 ? 9.589  -17.330 13.849  1.00 22.69 ? 320 GLU A CA    1 
ATOM   2359 C C     . GLU A 1 329 ? 9.897  -15.907 14.304  1.00 20.90 ? 320 GLU A C     1 
ATOM   2360 O O     . GLU A 1 329 ? 9.442  -15.463 15.357  1.00 23.00 ? 320 GLU A O     1 
ATOM   2361 C CB    . GLU A 1 329 ? 10.780 -18.260 14.093  1.00 23.86 ? 320 GLU A CB    1 
ATOM   2362 N N     . ALA A 1 330 ? 10.649 -15.166 13.483  1.00 20.33 ? 321 ALA A N     1 
ATOM   2363 C CA    . ALA A 1 330 ? 11.005 -13.787 13.798  1.00 18.52 ? 321 ALA A CA    1 
ATOM   2364 C C     . ALA A 1 330 ? 9.768  -12.927 14.049  1.00 19.74 ? 321 ALA A C     1 
ATOM   2365 O O     . ALA A 1 330 ? 9.718  -12.159 15.021  1.00 18.96 ? 321 ALA A O     1 
ATOM   2366 C CB    . ALA A 1 330 ? 11.854 -13.216 12.657  1.00 17.71 ? 321 ALA A CB    1 
ATOM   2367 N N     . VAL A 1 331 ? 8.769  -13.003 13.163  1.00 18.25 ? 322 VAL A N     1 
ATOM   2368 C CA    . VAL A 1 331 ? 7.576  -12.189 13.385  1.00 16.04 ? 322 VAL A CA    1 
ATOM   2369 C C     . VAL A 1 331 ? 6.747  -12.744 14.544  1.00 20.67 ? 322 VAL A C     1 
ATOM   2370 O O     . VAL A 1 331 ? 6.228  -11.989 15.377  1.00 22.06 ? 322 VAL A O     1 
ATOM   2371 C CB    . VAL A 1 331 ? 6.742  -12.107 12.101  1.00 22.30 ? 322 VAL A CB    1 
ATOM   2372 C CG1   . VAL A 1 331 ? 5.401  -11.406 12.380  1.00 21.01 ? 322 VAL A CG1   1 
ATOM   2373 C CG2   . VAL A 1 331 ? 7.560  -11.420 10.987  1.00 18.56 ? 322 VAL A CG2   1 
ATOM   2374 N N     . ALA A 1 332 ? 6.589  -14.069 14.593  1.00 20.45 ? 323 ALA A N     1 
ATOM   2375 C CA    . ALA A 1 332 ? 5.782  -14.677 15.645  1.00 22.26 ? 323 ALA A CA    1 
ATOM   2376 C C     . ALA A 1 332 ? 6.304  -14.332 17.037  1.00 23.74 ? 323 ALA A C     1 
ATOM   2377 O O     . ALA A 1 332 ? 5.500  -14.148 17.965  1.00 26.93 ? 323 ALA A O     1 
ATOM   2378 C CB    . ALA A 1 332 ? 5.721  -16.188 15.452  1.00 25.61 ? 323 ALA A CB    1 
ATOM   2379 N N     . GLN A 1 333 ? 7.638  -14.271 17.230  1.00 19.93 ? 324 GLN A N     1 
ATOM   2380 C CA    . GLN A 1 333 ? 8.179  -14.027 18.576  1.00 23.04 ? 324 GLN A CA    1 
ATOM   2381 C C     . GLN A 1 333 ? 8.277  -12.552 18.904  1.00 22.05 ? 324 GLN A C     1 
ATOM   2382 O O     . GLN A 1 333 ? 8.771  -12.209 19.984  1.00 21.47 ? 324 GLN A O     1 
ATOM   2383 C CB    . GLN A 1 333 ? 9.589  -14.615 18.791  1.00 25.16 ? 324 GLN A CB    1 
ATOM   2384 C CG    . GLN A 1 333 ? 9.990  -15.830 18.030  1.00 33.78 ? 324 GLN A CG    1 
ATOM   2385 C CD    . GLN A 1 333 ? 9.815  -17.125 18.751  1.00 41.55 ? 324 GLN A CD    1 
ATOM   2386 O OE1   . GLN A 1 333 ? 9.258  -17.181 19.855  1.00 52.83 ? 324 GLN A OE1   1 
ATOM   2387 N NE2   . GLN A 1 333 ? 10.317 -18.200 18.136  1.00 43.04 ? 324 GLN A NE2   1 
ATOM   2388 N N     . GLY A 1 334 ? 7.846  -11.671 17.996  1.00 19.33 ? 325 GLY A N     1 
ATOM   2389 C CA    . GLY A 1 334 ? 8.030  -10.249 18.176  1.00 21.86 ? 325 GLY A CA    1 
ATOM   2390 C C     . GLY A 1 334 ? 9.425  -9.730  17.911  1.00 21.37 ? 325 GLY A C     1 
ATOM   2391 O O     . GLY A 1 334 ? 9.717  -8.580  18.276  1.00 22.93 ? 325 GLY A O     1 
ATOM   2392 N N     . ASP A 1 335 ? 10.289 -10.533 17.290  1.00 16.20 ? 326 ASP A N     1 
ATOM   2393 C CA    . ASP A 1 335 ? 11.682 -10.161 17.062  1.00 20.87 ? 326 ASP A CA    1 
ATOM   2394 C C     . ASP A 1 335 ? 11.846 -9.142  15.939  1.00 17.65 ? 326 ASP A C     1 
ATOM   2395 O O     . ASP A 1 335 ? 12.889 -8.490  15.862  1.00 18.18 ? 326 ASP A O     1 
ATOM   2396 C CB    . ASP A 1 335 ? 12.511 -11.397 16.711  1.00 22.85 ? 326 ASP A CB    1 
ATOM   2397 C CG    . ASP A 1 335 ? 12.562 -12.399 17.837  1.00 29.46 ? 326 ASP A CG    1 
ATOM   2398 O OD1   . ASP A 1 335 ? 12.302 -11.992 18.980  1.00 32.62 ? 326 ASP A OD1   1 
ATOM   2399 O OD2   . ASP A 1 335 ? 12.867 -13.585 17.576  1.00 35.70 ? 326 ASP A OD2   1 
ATOM   2400 N N     . ALA A 1 336 ? 10.868 -9.042  15.043  1.00 18.83 ? 327 ALA A N     1 
ATOM   2401 C CA    . ALA A 1 336 ? 10.933 -8.161  13.885  1.00 15.46 ? 327 ALA A CA    1 
ATOM   2402 C C     . ALA A 1 336 ? 9.516  -7.928  13.431  1.00 15.87 ? 327 ALA A C     1 
ATOM   2403 O O     . ALA A 1 336 ? 8.638  -8.775  13.657  1.00 19.68 ? 327 ALA A O     1 
ATOM   2404 C CB    . ALA A 1 336 ? 11.746 -8.747  12.722  1.00 15.63 ? 327 ALA A CB    1 
ATOM   2405 N N     . ASP A 1 337 ? 9.304  -6.792  12.771  1.00 14.75 ? 328 ASP A N     1 
ATOM   2406 C CA    . ASP A 1 337 ? 8.012  -6.515  12.176  1.00 16.27 ? 328 ASP A CA    1 
ATOM   2407 C C     . ASP A 1 337 ? 7.978  -6.951  10.715  1.00 17.08 ? 328 ASP A C     1 
ATOM   2408 O O     . ASP A 1 337 ? 6.952  -7.443  10.237  1.00 16.25 ? 328 ASP A O     1 
ATOM   2409 C CB    . ASP A 1 337 ? 7.692  -5.037  12.321  1.00 18.09 ? 328 ASP A CB    1 
ATOM   2410 C CG    . ASP A 1 337 ? 7.816  -4.595  13.748  1.00 16.81 ? 328 ASP A CG    1 
ATOM   2411 O OD1   . ASP A 1 337 ? 7.031  -5.135  14.578  1.00 17.19 ? 328 ASP A OD1   1 
ATOM   2412 O OD2   . ASP A 1 337 ? 8.691  -3.759  14.032  1.00 19.13 ? 328 ASP A OD2   1 
ATOM   2413 N N     . LEU A 1 338 ? 9.087  -6.807  10.011  1.00 15.88 ? 329 LEU A N     1 
ATOM   2414 C CA    . LEU A 1 338 ? 9.158  -7.178  8.601   1.00 15.57 ? 329 LEU A CA    1 
ATOM   2415 C C     . LEU A 1 338 ? 10.449 -7.952  8.390   1.00 17.30 ? 329 LEU A C     1 
ATOM   2416 O O     . LEU A 1 338 ? 11.423 -7.736  9.100   1.00 15.36 ? 329 LEU A O     1 
ATOM   2417 C CB    . LEU A 1 338 ? 9.144  -5.918  7.705   1.00 14.50 ? 329 LEU A CB    1 
ATOM   2418 C CG    . LEU A 1 338 ? 7.957  -4.925  7.820   1.00 15.28 ? 329 LEU A CG    1 
ATOM   2419 C CD1   . LEU A 1 338 ? 8.215  -3.685  6.992   1.00 19.47 ? 329 LEU A CD1   1 
ATOM   2420 C CD2   . LEU A 1 338 ? 6.673  -5.586  7.373   1.00 16.68 ? 329 LEU A CD2   1 
ATOM   2421 N N     . VAL A 1 339 ? 10.468 -8.860  7.406   1.00 12.35 ? 330 VAL A N     1 
ATOM   2422 C CA    . VAL A 1 339 ? 11.665 -9.641  7.107   1.00 13.58 ? 330 VAL A CA    1 
ATOM   2423 C C     . VAL A 1 339 ? 12.039 -9.429  5.640   1.00 13.67 ? 330 VAL A C     1 
ATOM   2424 O O     . VAL A 1 339 ? 11.204 -9.621  4.761   1.00 15.28 ? 330 VAL A O     1 
ATOM   2425 C CB    . VAL A 1 339 ? 11.426 -11.140 7.391   1.00 19.30 ? 330 VAL A CB    1 
ATOM   2426 C CG1   . VAL A 1 339 ? 12.709 -11.934 7.148   1.00 14.49 ? 330 VAL A CG1   1 
ATOM   2427 C CG2   . VAL A 1 339 ? 10.962 -11.342 8.820   1.00 15.93 ? 330 VAL A CG2   1 
ATOM   2428 N N     . SER A 1 340 ? 13.275 -9.022  5.365   1.00 12.74 ? 331 SER A N     1 
ATOM   2429 C CA    . SER A 1 340 ? 13.657 -8.834  3.960   1.00 12.75 ? 331 SER A CA    1 
ATOM   2430 C C     . SER A 1 340 ? 14.489 -10.018 3.479   1.00 16.56 ? 331 SER A C     1 
ATOM   2431 O O     . SER A 1 340 ? 15.260 -10.613 4.245   1.00 15.74 ? 331 SER A O     1 
ATOM   2432 C CB    . SER A 1 340 ? 14.406 -7.515  3.719   1.00 15.75 ? 331 SER A CB    1 
ATOM   2433 O OG    . SER A 1 340 ? 15.672 -7.500  4.364   1.00 16.98 ? 331 SER A OG    1 
ATOM   2434 N N     . TYR A 1 341 ? 14.257 -10.388 2.226   1.00 14.46 ? 332 TYR A N     1 
ATOM   2435 C CA    . TYR A 1 341 ? 14.934 -11.485 1.544   1.00 12.09 ? 332 TYR A CA    1 
ATOM   2436 C C     . TYR A 1 341 ? 15.658 -10.931 0.330   1.00 13.62 ? 332 TYR A C     1 
ATOM   2437 O O     . TYR A 1 341 ? 15.094 -10.136 -0.415  1.00 13.72 ? 332 TYR A O     1 
ATOM   2438 C CB    . TYR A 1 341 ? 13.919 -12.548 1.111   1.00 13.31 ? 332 TYR A CB    1 
ATOM   2439 C CG    . TYR A 1 341 ? 13.237 -13.232 2.286   1.00 14.17 ? 332 TYR A CG    1 
ATOM   2440 C CD1   . TYR A 1 341 ? 12.135 -12.651 2.897   1.00 14.36 ? 332 TYR A CD1   1 
ATOM   2441 C CD2   . TYR A 1 341 ? 13.694 -14.459 2.756   1.00 16.35 ? 332 TYR A CD2   1 
ATOM   2442 C CE1   . TYR A 1 341 ? 11.507 -13.276 3.980   1.00 15.53 ? 332 TYR A CE1   1 
ATOM   2443 C CE2   . TYR A 1 341 ? 13.081 -15.099 3.820   1.00 18.38 ? 332 TYR A CE2   1 
ATOM   2444 C CZ    . TYR A 1 341 ? 11.990 -14.506 4.422   1.00 13.80 ? 332 TYR A CZ    1 
ATOM   2445 O OH    . TYR A 1 341 ? 11.383 -15.138 5.505   1.00 17.47 ? 332 TYR A OH    1 
ATOM   2446 N N     . GLY A 1 342 ? 16.920 -11.327 0.160   1.00 12.92 ? 333 GLY A N     1 
ATOM   2447 C CA    . GLY A 1 342 ? 17.719 -10.869 -0.958  1.00 14.04 ? 333 GLY A CA    1 
ATOM   2448 C C     . GLY A 1 342 ? 17.874 -11.973 -1.983  1.00 12.53 ? 333 GLY A C     1 
ATOM   2449 O O     . GLY A 1 342 ? 17.133 -12.032 -2.973  1.00 14.94 ? 333 GLY A O     1 
ATOM   2450 N N     . ARG A 1 343 ? 18.810 -12.881 -1.729  1.00 13.29 ? 334 ARG A N     1 
ATOM   2451 C CA    . ARG A 1 343 ? 19.194 -13.832 -2.766  1.00 17.36 ? 334 ARG A CA    1 
ATOM   2452 C C     . ARG A 1 343 ? 18.029 -14.697 -3.224  1.00 14.31 ? 334 ARG A C     1 
ATOM   2453 O O     . ARG A 1 343 ? 17.881 -14.954 -4.419  1.00 16.67 ? 334 ARG A O     1 
ATOM   2454 C CB    . ARG A 1 343 ? 20.358 -14.685 -2.281  1.00 14.72 ? 334 ARG A CB    1 
ATOM   2455 C CG    . ARG A 1 343 ? 21.654 -13.911 -2.294  1.00 16.82 ? 334 ARG A CG    1 
ATOM   2456 C CD    . ARG A 1 343 ? 22.718 -14.617 -1.477  1.00 20.70 ? 334 ARG A CD    1 
ATOM   2457 N NE    . ARG A 1 343 ? 22.461 -14.460 -0.058  1.00 18.08 ? 334 ARG A NE    1 
ATOM   2458 C CZ    . ARG A 1 343 ? 23.316 -14.844 0.877   1.00 21.57 ? 334 ARG A CZ    1 
ATOM   2459 N NH1   . ARG A 1 343 ? 24.444 -15.464 0.547   1.00 21.46 ? 334 ARG A NH1   1 
ATOM   2460 N NH2   . ARG A 1 343 ? 23.052 -14.569 2.165   1.00 19.50 ? 334 ARG A NH2   1 
ATOM   2461 N N     . LEU A 1 344 ? 17.170 -15.132 -2.306  1.00 12.43 ? 335 LEU A N     1 
ATOM   2462 C CA    . LEU A 1 344 ? 16.033 -15.954 -2.722  1.00 16.33 ? 335 LEU A CA    1 
ATOM   2463 C C     . LEU A 1 344 ? 15.087 -15.193 -3.637  1.00 19.09 ? 335 LEU A C     1 
ATOM   2464 O O     . LEU A 1 344 ? 14.452 -15.802 -4.497  1.00 15.49 ? 335 LEU A O     1 
ATOM   2465 C CB    . LEU A 1 344 ? 15.283 -16.461 -1.498  1.00 18.59 ? 335 LEU A CB    1 
ATOM   2466 C CG    . LEU A 1 344 ? 16.031 -17.618 -0.868  1.00 17.83 ? 335 LEU A CG    1 
ATOM   2467 C CD1   . LEU A 1 344 ? 15.334 -18.059 0.467   1.00 20.30 ? 335 LEU A CD1   1 
ATOM   2468 C CD2   . LEU A 1 344 ? 16.190 -18.754 -1.872  1.00 20.55 ? 335 LEU A CD2   1 
ATOM   2469 N N     . PHE A 1 345 ? 14.988 -13.868 -3.461  1.00 13.58 ? 336 PHE A N     1 
ATOM   2470 C CA    . PHE A 1 345 ? 14.148 -13.039 -4.337  1.00 14.60 ? 336 PHE A CA    1 
ATOM   2471 C C     . PHE A 1 345 ? 14.749 -12.888 -5.719  1.00 15.99 ? 336 PHE A C     1 
ATOM   2472 O O     . PHE A 1 345 ? 14.019 -12.612 -6.696  1.00 16.60 ? 336 PHE A O     1 
ATOM   2473 C CB    . PHE A 1 345 ? 13.944 -11.638 -3.704  1.00 14.35 ? 336 PHE A CB    1 
ATOM   2474 C CG    . PHE A 1 345 ? 12.475 -11.288 -3.432  1.00 12.11 ? 336 PHE A CG    1 
ATOM   2475 C CD1   . PHE A 1 345 ? 11.513 -11.474 -4.423  1.00 16.89 ? 336 PHE A CD1   1 
ATOM   2476 C CD2   . PHE A 1 345 ? 12.081 -10.770 -2.222  1.00 15.01 ? 336 PHE A CD2   1 
ATOM   2477 C CE1   . PHE A 1 345 ? 10.163 -11.154 -4.196  1.00 17.11 ? 336 PHE A CE1   1 
ATOM   2478 C CE2   . PHE A 1 345 ? 10.749 -10.433 -1.980  1.00 14.43 ? 336 PHE A CE2   1 
ATOM   2479 C CZ    . PHE A 1 345 ? 9.786  -10.611 -2.989  1.00 17.81 ? 336 PHE A CZ    1 
ATOM   2480 N N     . ILE A 1 346 ? 16.077 -13.005 -5.834  1.00 14.53 ? 337 ILE A N     1 
ATOM   2481 C CA    . ILE A 1 346 ? 16.689 -12.989 -7.158  1.00 13.01 ? 337 ILE A CA    1 
ATOM   2482 C C     . ILE A 1 346 ? 16.096 -14.094 -8.034  1.00 14.39 ? 337 ILE A C     1 
ATOM   2483 O O     . ILE A 1 346 ? 15.732 -13.868 -9.192  1.00 16.69 ? 337 ILE A O     1 
ATOM   2484 C CB    . ILE A 1 346 ? 18.222 -13.134 -7.047  1.00 14.49 ? 337 ILE A CB    1 
ATOM   2485 C CG1   . ILE A 1 346 ? 18.856 -11.816 -6.606  1.00 17.38 ? 337 ILE A CG1   1 
ATOM   2486 C CG2   . ILE A 1 346 ? 18.837 -13.456 -8.402  1.00 16.81 ? 337 ILE A CG2   1 
ATOM   2487 C CD1   . ILE A 1 346 ? 20.382 -11.898 -6.521  1.00 17.12 ? 337 ILE A CD1   1 
ATOM   2488 N N     . SER A 1 347 ? 16.043 -15.316 -7.518  1.00 15.39 ? 338 SER A N     1 
ATOM   2489 C CA    . SER A 1 347 ? 15.695 -16.476 -8.338  1.00 14.23 ? 338 SER A CA    1 
ATOM   2490 C C     . SER A 1 347 ? 14.230 -16.881 -8.201  1.00 14.66 ? 338 SER A C     1 
ATOM   2491 O O     . SER A 1 347 ? 13.777 -17.781 -8.902  1.00 15.35 ? 338 SER A O     1 
ATOM   2492 C CB    . SER A 1 347 ? 16.591 -17.635 -7.960  1.00 14.12 ? 338 SER A CB    1 
ATOM   2493 O OG    . SER A 1 347 ? 16.572 -17.821 -6.570  1.00 15.23 ? 338 SER A OG    1 
ATOM   2494 N N     . ASN A 1 348 ? 13.483 -16.255 -7.287  1.00 14.17 ? 339 ASN A N     1 
ATOM   2495 C CA    . ASN A 1 348 ? 12.063 -16.543 -7.108  1.00 17.11 ? 339 ASN A CA    1 
ATOM   2496 C C     . ASN A 1 348 ? 11.301 -15.241 -7.262  1.00 16.55 ? 339 ASN A C     1 
ATOM   2497 O O     . ASN A 1 348 ? 11.089 -14.534 -6.268  1.00 14.53 ? 339 ASN A O     1 
ATOM   2498 C CB    . ASN A 1 348 ? 11.820 -17.187 -5.747  1.00 15.27 ? 339 ASN A CB    1 
ATOM   2499 C CG    . ASN A 1 348 ? 12.522 -18.534 -5.663  1.00 14.55 ? 339 ASN A CG    1 
ATOM   2500 O OD1   . ASN A 1 348 ? 11.951 -19.544 -6.053  1.00 17.06 ? 339 ASN A OD1   1 
ATOM   2501 N ND2   . ASN A 1 348 ? 13.795 -18.528 -5.257  1.00 17.58 ? 339 ASN A ND2   1 
ATOM   2502 N N     . PRO A 1 349 ? 10.931 -14.845 -8.491  1.00 16.25 ? 340 PRO A N     1 
ATOM   2503 C CA    . PRO A 1 349 ? 10.184 -13.583 -8.625  1.00 18.10 ? 340 PRO A CA    1 
ATOM   2504 C C     . PRO A 1 349 ? 8.897  -13.602 -7.813  1.00 16.67 ? 340 PRO A C     1 
ATOM   2505 O O     . PRO A 1 349 ? 8.492  -12.561 -7.277  1.00 16.70 ? 340 PRO A O     1 
ATOM   2506 C CB    . PRO A 1 349 ? 9.905  -13.485 -10.132 1.00 16.91 ? 340 PRO A CB    1 
ATOM   2507 C CG    . PRO A 1 349 ? 10.002 -14.947 -10.646 1.00 18.00 ? 340 PRO A CG    1 
ATOM   2508 C CD    . PRO A 1 349 ? 11.038 -15.589 -9.779  1.00 19.27 ? 340 PRO A CD    1 
ATOM   2509 N N     . ASP A 1 350 ? 8.275  -14.775 -7.671  1.00 15.29 ? 341 ASP A N     1 
ATOM   2510 C CA    . ASP A 1 350 ? 7.072  -14.931 -6.852  1.00 16.25 ? 341 ASP A CA    1 
ATOM   2511 C C     . ASP A 1 350 ? 7.407  -15.480 -5.467  1.00 19.70 ? 341 ASP A C     1 
ATOM   2512 O O     . ASP A 1 350 ? 6.701  -16.344 -4.953  1.00 18.37 ? 341 ASP A O     1 
ATOM   2513 C CB    . ASP A 1 350 ? 6.035  -15.819 -7.549  1.00 17.44 ? 341 ASP A CB    1 
ATOM   2514 C CG    . ASP A 1 350 ? 6.615  -17.153 -8.096  1.00 20.43 ? 341 ASP A CG    1 
ATOM   2515 O OD1   . ASP A 1 350 ? 7.835  -17.387 -8.032  1.00 19.53 ? 341 ASP A OD1   1 
ATOM   2516 O OD2   . ASP A 1 350 ? 5.833  -17.981 -8.611  1.00 21.75 ? 341 ASP A OD2   1 
ATOM   2517 N N     . LEU A 1 351 ? 8.476  -14.977 -4.837  1.00 16.60 ? 342 LEU A N     1 
ATOM   2518 C CA    . LEU A 1 351 ? 8.877  -15.494 -3.531  1.00 15.76 ? 342 LEU A CA    1 
ATOM   2519 C C     . LEU A 1 351 ? 7.761  -15.335 -2.508  1.00 15.65 ? 342 LEU A C     1 
ATOM   2520 O O     . LEU A 1 351 ? 7.566  -16.217 -1.672  1.00 17.80 ? 342 LEU A O     1 
ATOM   2521 C CB    . LEU A 1 351 ? 10.135 -14.783 -3.028  1.00 16.00 ? 342 LEU A CB    1 
ATOM   2522 C CG    . LEU A 1 351 ? 10.713 -15.256 -1.675  1.00 13.28 ? 342 LEU A CG    1 
ATOM   2523 C CD1   . LEU A 1 351 ? 11.180 -16.711 -1.802  1.00 19.28 ? 342 LEU A CD1   1 
ATOM   2524 C CD2   . LEU A 1 351 ? 11.837 -14.313 -1.213  1.00 13.98 ? 342 LEU A CD2   1 
ATOM   2525 N N     . VAL A 1 352 ? 7.000  -14.230 -2.579  1.00 16.22 ? 343 VAL A N     1 
ATOM   2526 C CA    . VAL A 1 352 ? 5.914  -14.033 -1.611  1.00 17.57 ? 343 VAL A CA    1 
ATOM   2527 C C     . VAL A 1 352 ? 4.926  -15.184 -1.698  1.00 21.85 ? 343 VAL A C     1 
ATOM   2528 O O     . VAL A 1 352 ? 4.597  -15.819 -0.690  1.00 19.73 ? 343 VAL A O     1 
ATOM   2529 C CB    . VAL A 1 352 ? 5.200  -12.677 -1.791  1.00 18.17 ? 343 VAL A CB    1 
ATOM   2530 C CG1   . VAL A 1 352 ? 4.167  -12.451 -0.676  1.00 17.93 ? 343 VAL A CG1   1 
ATOM   2531 C CG2   . VAL A 1 352 ? 6.203  -11.459 -1.820  1.00 17.24 ? 343 VAL A CG2   1 
ATOM   2532 N N     . MET A 1 353 ? 4.442  -15.474 -2.898  1.00 18.20 ? 344 MET A N     1 
ATOM   2533 C CA    . MET A 1 353 ? 3.487  -16.562 -3.034  1.00 20.88 ? 344 MET A CA    1 
ATOM   2534 C C     . MET A 1 353 ? 4.126  -17.907 -2.675  1.00 20.18 ? 344 MET A C     1 
ATOM   2535 O O     . MET A 1 353 ? 3.464  -18.799 -2.123  1.00 19.93 ? 344 MET A O     1 
ATOM   2536 C CB    . MET A 1 353 ? 2.933  -16.567 -4.453  1.00 22.16 ? 344 MET A CB    1 
ATOM   2537 C CG    . MET A 1 353 ? 2.043  -17.739 -4.784  1.00 31.78 ? 344 MET A CG    1 
ATOM   2538 S SD    . MET A 1 353 ? 0.421  -17.502 -4.002  1.00 41.81 ? 344 MET A SD    1 
ATOM   2539 C CE    . MET A 1 353 ? 0.263  -15.702 -3.958  1.00 38.16 ? 344 MET A CE    1 
ATOM   2540 N N     . ARG A 1 354 ? 5.406  -18.089 -3.001  1.00 17.78 ? 345 ARG A N     1 
ATOM   2541 C CA    . ARG A 1 354 ? 6.052  -19.351 -2.642  1.00 18.94 ? 345 ARG A CA    1 
ATOM   2542 C C     . ARG A 1 354 ? 6.108  -19.528 -1.130  1.00 22.22 ? 345 ARG A C     1 
ATOM   2543 O O     . ARG A 1 354 ? 5.856  -20.624 -0.615  1.00 21.10 ? 345 ARG A O     1 
ATOM   2544 C CB    . ARG A 1 354 ? 7.451  -19.428 -3.263  1.00 16.44 ? 345 ARG A CB    1 
ATOM   2545 C CG    . ARG A 1 354 ? 7.404  -19.497 -4.796  1.00 20.38 ? 345 ARG A CG    1 
ATOM   2546 C CD    . ARG A 1 354 ? 8.728  -19.991 -5.361  1.00 21.29 ? 345 ARG A CD    1 
ATOM   2547 N NE    . ARG A 1 354 ? 8.840  -19.735 -6.789  1.00 18.87 ? 345 ARG A NE    1 
ATOM   2548 C CZ    . ARG A 1 354 ? 9.356  -20.587 -7.665  1.00 21.32 ? 345 ARG A CZ    1 
ATOM   2549 N NH1   . ARG A 1 354 ? 9.800  -21.780 -7.294  1.00 21.97 ? 345 ARG A NH1   1 
ATOM   2550 N NH2   . ARG A 1 354 ? 9.450  -20.224 -8.939  1.00 23.10 ? 345 ARG A NH2   1 
ATOM   2551 N N     . ILE A 1 355 ? 6.395  -18.446 -0.399  1.00 19.79 ? 346 ILE A N     1 
ATOM   2552 C CA    . ILE A 1 355 ? 6.417  -18.498 1.063   1.00 18.10 ? 346 ILE A CA    1 
ATOM   2553 C C     . ILE A 1 355 ? 5.018  -18.770 1.602   1.00 22.46 ? 346 ILE A C     1 
ATOM   2554 O O     . ILE A 1 355 ? 4.838  -19.595 2.508   1.00 24.47 ? 346 ILE A O     1 
ATOM   2555 C CB    . ILE A 1 355 ? 7.015  -17.192 1.624   1.00 18.13 ? 346 ILE A CB    1 
ATOM   2556 C CG1   . ILE A 1 355 ? 8.543  -17.197 1.430   1.00 19.29 ? 346 ILE A CG1   1 
ATOM   2557 C CG2   . ILE A 1 355 ? 6.668  -16.952 3.128   1.00 16.24 ? 346 ILE A CG2   1 
ATOM   2558 C CD1   . ILE A 1 355 ? 9.195  -15.930 1.823   1.00 16.29 ? 346 ILE A CD1   1 
ATOM   2559 N N     . LYS A 1 356 ? 4.001  -18.129 1.010   1.00 20.71 ? 347 LYS A N     1 
ATOM   2560 C CA    . LYS A 1 356 ? 2.615  -18.368 1.429   1.00 19.84 ? 347 LYS A CA    1 
ATOM   2561 C C     . LYS A 1 356 ? 2.211  -19.838 1.261   1.00 21.65 ? 347 LYS A C     1 
ATOM   2562 O O     . LYS A 1 356 ? 1.550  -20.420 2.131   1.00 24.19 ? 347 LYS A O     1 
ATOM   2563 C CB    . LYS A 1 356 ? 1.674  -17.491 0.616   1.00 22.36 ? 347 LYS A CB    1 
ATOM   2564 C CG    . LYS A 1 356 ? 0.221  -17.749 0.865   1.00 29.71 ? 347 LYS A CG    1 
ATOM   2565 C CD    . LYS A 1 356 ? -0.325 -16.778 1.859   1.00 35.76 ? 347 LYS A CD    1 
ATOM   2566 C CE    . LYS A 1 356 ? -1.853 -16.876 1.900   1.00 47.39 ? 347 LYS A CE    1 
ATOM   2567 N NZ    . LYS A 1 356 ? -2.469 -15.893 2.832   1.00 48.16 ? 347 LYS A NZ    1 
ATOM   2568 N N     . LEU A 1 357 ? 2.625  -20.453 0.169   1.00 20.54 ? 348 LEU A N     1 
ATOM   2569 C CA    . LEU A 1 357 ? 2.229  -21.816 -0.147  1.00 23.79 ? 348 LEU A CA    1 
ATOM   2570 C C     . LEU A 1 357 ? 3.188  -22.860 0.395   1.00 25.01 ? 348 LEU A C     1 
ATOM   2571 O O     . LEU A 1 357 ? 2.902  -24.060 0.283   1.00 24.04 ? 348 LEU A O     1 
ATOM   2572 C CB    . LEU A 1 357 ? 2.118  -21.985 -1.651  1.00 23.85 ? 348 LEU A CB    1 
ATOM   2573 C CG    . LEU A 1 357 ? 1.121  -21.077 -2.358  1.00 26.15 ? 348 LEU A CG    1 
ATOM   2574 C CD1   . LEU A 1 357 ? 1.185  -21.330 -3.831  1.00 26.56 ? 348 LEU A CD1   1 
ATOM   2575 C CD2   . LEU A 1 357 ? -0.268 -21.341 -1.841  1.00 29.36 ? 348 LEU A CD2   1 
ATOM   2576 N N     . ASN A 1 358 ? 4.297  -22.436 0.998   1.00 20.80 ? 349 ASN A N     1 
ATOM   2577 C CA    . ASN A 1 358 ? 5.426  -23.318 1.289   1.00 24.78 ? 349 ASN A CA    1 
ATOM   2578 C C     . ASN A 1 358 ? 5.809  -24.138 0.060   1.00 24.81 ? 349 ASN A C     1 
ATOM   2579 O O     . ASN A 1 358 ? 6.026  -25.349 0.143   1.00 22.54 ? 349 ASN A O     1 
ATOM   2580 C CB    . ASN A 1 358 ? 5.150  -24.250 2.479   1.00 22.03 ? 349 ASN A CB    1 
ATOM   2581 C CG    . ASN A 1 358 ? 6.427  -24.757 3.095   1.00 26.55 ? 349 ASN A CG    1 
ATOM   2582 O OD1   . ASN A 1 358 ? 7.498  -24.239 2.795   1.00 27.45 ? 349 ASN A OD1   1 
ATOM   2583 N ND2   . ASN A 1 358 ? 6.339  -25.796 3.915   1.00 27.90 ? 349 ASN A ND2   1 
ATOM   2584 N N     . ALA A 1 359 ? 5.878  -23.447 -1.115  1.00 22.89 ? 350 ALA A N     1 
ATOM   2585 C CA    . ALA A 1 359 ? 6.275  -24.045 -2.386  1.00 24.53 ? 350 ALA A CA    1 
ATOM   2586 C C     . ALA A 1 359 ? 7.798  -24.122 -2.479  1.00 23.39 ? 350 ALA A C     1 
ATOM   2587 O O     . ALA A 1 359 ? 8.501  -23.287 -1.908  1.00 22.61 ? 350 ALA A O     1 
ATOM   2588 C CB    . ALA A 1 359 ? 5.738  -23.231 -3.564  1.00 24.37 ? 350 ALA A CB    1 
ATOM   2589 N N     . PRO A 1 360 ? 8.341  -25.109 -3.190  1.00 19.57 ? 351 PRO A N     1 
ATOM   2590 C CA    . PRO A 1 360 ? 9.804  -25.211 -3.259  1.00 21.37 ? 351 PRO A CA    1 
ATOM   2591 C C     . PRO A 1 360 ? 10.409 -24.054 -4.041  1.00 21.81 ? 351 PRO A C     1 
ATOM   2592 O O     . PRO A 1 360 ? 9.838  -23.575 -5.032  1.00 21.56 ? 351 PRO A O     1 
ATOM   2593 C CB    . PRO A 1 360 ? 10.057 -26.566 -3.944  1.00 21.43 ? 351 PRO A CB    1 
ATOM   2594 C CG    . PRO A 1 360 ? 8.745  -27.021 -4.473  1.00 29.56 ? 351 PRO A CG    1 
ATOM   2595 C CD    . PRO A 1 360 ? 7.655  -26.287 -3.748  1.00 24.09 ? 351 PRO A CD    1 
ATOM   2596 N N     . LEU A 1 361 ? 11.591 -23.626 -3.589  1.00 18.09 ? 352 LEU A N     1 
ATOM   2597 C CA    . LEU A 1 361 ? 12.288 -22.458 -4.116  1.00 16.13 ? 352 LEU A CA    1 
ATOM   2598 C C     . LEU A 1 361 ? 13.334 -22.807 -5.178  1.00 18.22 ? 352 LEU A C     1 
ATOM   2599 O O     . LEU A 1 361 ? 13.939 -23.892 -5.167  1.00 17.94 ? 352 LEU A O     1 
ATOM   2600 C CB    . LEU A 1 361 ? 12.969 -21.715 -2.958  1.00 18.15 ? 352 LEU A CB    1 
ATOM   2601 C CG    . LEU A 1 361 ? 12.058 -21.330 -1.794  1.00 21.45 ? 352 LEU A CG    1 
ATOM   2602 C CD1   . LEU A 1 361 ? 12.855 -20.597 -0.712  1.00 23.99 ? 352 LEU A CD1   1 
ATOM   2603 C CD2   . LEU A 1 361 ? 10.919 -20.422 -2.277  1.00 21.11 ? 352 LEU A CD2   1 
ATOM   2604 N N     . ASN A 1 362 ? 13.522 -21.867 -6.106  1.00 13.55 ? 353 ASN A N     1 
ATOM   2605 C CA    . ASN A 1 362 ? 14.495 -21.959 -7.201  1.00 18.99 ? 353 ASN A CA    1 
ATOM   2606 C C     . ASN A 1 362 ? 15.886 -21.548 -6.753  1.00 20.68 ? 353 ASN A C     1 
ATOM   2607 O O     . ASN A 1 362 ? 16.038 -20.558 -6.025  1.00 15.66 ? 353 ASN A O     1 
ATOM   2608 C CB    . ASN A 1 362 ? 14.105 -21.005 -8.333  1.00 19.47 ? 353 ASN A CB    1 
ATOM   2609 C CG    . ASN A 1 362 ? 12.916 -21.468 -9.105  1.00 28.35 ? 353 ASN A CG    1 
ATOM   2610 O OD1   . ASN A 1 362 ? 12.420 -22.589 -8.908  1.00 22.62 ? 353 ASN A OD1   1 
ATOM   2611 N ND2   . ASN A 1 362 ? 12.452 -20.617 -10.029 1.00 31.95 ? 353 ASN A ND2   1 
ATOM   2612 N N     . LYS A 1 363 ? 16.910 -22.249 -7.261  1.00 17.94 ? 354 LYS A N     1 
ATOM   2613 C CA    . LYS A 1 363 ? 18.284 -21.824 -7.031  1.00 20.45 ? 354 LYS A CA    1 
ATOM   2614 C C     . LYS A 1 363 ? 18.595 -20.537 -7.806  1.00 16.64 ? 354 LYS A C     1 
ATOM   2615 O O     . LYS A 1 363 ? 17.980 -20.244 -8.835  1.00 18.25 ? 354 LYS A O     1 
ATOM   2616 C CB    . LYS A 1 363 ? 19.293 -22.899 -7.453  1.00 21.65 ? 354 LYS A CB    1 
ATOM   2617 C CG    . LYS A 1 363 ? 19.247 -23.244 -8.939  1.00 20.19 ? 354 LYS A CG    1 
ATOM   2618 C CD    . LYS A 1 363 ? 20.286 -24.375 -9.243  1.00 28.98 ? 354 LYS A CD    1 
ATOM   2619 C CE    . LYS A 1 363 ? 19.986 -25.544 -8.309  1.00 29.39 ? 354 LYS A CE    1 
ATOM   2620 N NZ    . LYS A 1 363 ? 20.785 -26.809 -8.206  1.00 30.19 ? 354 LYS A NZ    1 
ATOM   2621 N N     . TYR A 1 364 ? 19.566 -19.767 -7.294  1.00 20.22 ? 355 TYR A N     1 
ATOM   2622 C CA    . TYR A 1 364 ? 20.068 -18.588 -7.996  1.00 16.71 ? 355 TYR A CA    1 
ATOM   2623 C C     . TYR A 1 364 ? 21.468 -18.851 -8.547  1.00 18.69 ? 355 TYR A C     1 
ATOM   2624 O O     . TYR A 1 364 ? 22.191 -19.729 -8.069  1.00 21.46 ? 355 TYR A O     1 
ATOM   2625 C CB    . TYR A 1 364 ? 20.092 -17.354 -7.078  1.00 16.76 ? 355 TYR A CB    1 
ATOM   2626 C CG    . TYR A 1 364 ? 20.726 -17.602 -5.733  1.00 16.91 ? 355 TYR A CG    1 
ATOM   2627 C CD1   . TYR A 1 364 ? 22.105 -17.605 -5.597  1.00 18.52 ? 355 TYR A CD1   1 
ATOM   2628 C CD2   . TYR A 1 364 ? 19.943 -17.832 -4.594  1.00 20.19 ? 355 TYR A CD2   1 
ATOM   2629 C CE1   . TYR A 1 364 ? 22.701 -17.805 -4.340  1.00 18.62 ? 355 TYR A CE1   1 
ATOM   2630 C CE2   . TYR A 1 364 ? 20.530 -18.064 -3.354  1.00 20.40 ? 355 TYR A CE2   1 
ATOM   2631 C CZ    . TYR A 1 364 ? 21.900 -18.043 -3.239  1.00 21.04 ? 355 TYR A CZ    1 
ATOM   2632 O OH    . TYR A 1 364 ? 22.478 -18.249 -2.017  1.00 24.38 ? 355 TYR A OH    1 
ATOM   2633 N N     . ASN A 1 365 ? 21.845 -18.087 -9.576  1.00 21.13 ? 356 ASN A N     1 
ATOM   2634 C CA    A ASN A 1 365 ? 23.155 -18.224 -10.212 0.50 18.12 ? 356 ASN A CA    1 
ATOM   2635 C CA    B ASN A 1 365 ? 23.157 -18.222 -10.206 0.50 18.12 ? 356 ASN A CA    1 
ATOM   2636 C C     . ASN A 1 365 ? 23.968 -16.968 -9.927  1.00 18.51 ? 356 ASN A C     1 
ATOM   2637 O O     . ASN A 1 365 ? 23.700 -15.907 -10.509 1.00 16.68 ? 356 ASN A O     1 
ATOM   2638 C CB    A ASN A 1 365 ? 23.009 -18.463 -11.713 0.50 21.03 ? 356 ASN A CB    1 
ATOM   2639 C CB    B ASN A 1 365 ? 23.013 -18.466 -11.702 0.50 21.03 ? 356 ASN A CB    1 
ATOM   2640 C CG    A ASN A 1 365 ? 22.000 -19.562 -12.048 0.50 21.80 ? 356 ASN A CG    1 
ATOM   2641 C CG    B ASN A 1 365 ? 24.334 -18.372 -12.437 0.50 20.07 ? 356 ASN A CG    1 
ATOM   2642 O OD1   A ASN A 1 365 ? 22.158 -20.720 -11.647 0.50 21.09 ? 356 ASN A OD1   1 
ATOM   2643 O OD1   B ASN A 1 365 ? 25.400 -18.639 -11.876 0.50 22.48 ? 356 ASN A OD1   1 
ATOM   2644 N ND2   A ASN A 1 365 ? 20.979 -19.207 -12.827 0.50 21.56 ? 356 ASN A ND2   1 
ATOM   2645 N ND2   B ASN A 1 365 ? 24.266 -18.037 -13.715 0.50 22.80 ? 356 ASN A ND2   1 
ATOM   2646 N N     . ARG A 1 366 ? 24.963 -17.098 -9.037  1.00 17.78 ? 357 ARG A N     1 
ATOM   2647 C CA    . ARG A 1 366 ? 25.830 -15.982 -8.678  1.00 15.91 ? 357 ARG A CA    1 
ATOM   2648 C C     . ARG A 1 366 ? 26.493 -15.355 -9.898  1.00 15.52 ? 357 ARG A C     1 
ATOM   2649 O O     . ARG A 1 366 ? 26.728 -14.134 -9.920  1.00 16.88 ? 357 ARG A O     1 
ATOM   2650 C CB    . ARG A 1 366 ? 26.890 -16.462 -7.677  1.00 18.15 ? 357 ARG A CB    1 
ATOM   2651 N N     . LYS A 1 367 ? 26.773 -16.157 -10.935 1.00 17.01 ? 358 LYS A N     1 
ATOM   2652 C CA    . LYS A 1 367 ? 27.516 -15.640 -12.077 1.00 17.61 ? 358 LYS A CA    1 
ATOM   2653 C C     . LYS A 1 367 ? 26.778 -14.502 -12.776 1.00 16.87 ? 358 LYS A C     1 
ATOM   2654 O O     . LYS A 1 367 ? 27.421 -13.642 -13.389 1.00 20.40 ? 358 LYS A O     1 
ATOM   2655 C CB    . LYS A 1 367 ? 27.815 -16.787 -13.043 1.00 23.09 ? 358 LYS A CB    1 
ATOM   2656 C CG    . LYS A 1 367 ? 28.737 -17.827 -12.410 1.00 28.98 ? 358 LYS A CG    1 
ATOM   2657 C CD    . LYS A 1 367 ? 29.662 -18.489 -13.446 1.00 33.27 ? 358 LYS A CD    1 
ATOM   2658 C CE    . LYS A 1 367 ? 29.019 -19.739 -14.061 1.00 55.79 ? 358 LYS A CE    1 
ATOM   2659 N NZ    . LYS A 1 367 ? 29.961 -20.917 -14.197 1.00 52.90 ? 358 LYS A NZ    1 
ATOM   2660 N N     . THR A 1 368 ? 25.448 -14.457 -12.702 1.00 13.57 ? 359 THR A N     1 
ATOM   2661 C CA    . THR A 1 368 ? 24.708 -13.353 -13.316 1.00 17.53 ? 359 THR A CA    1 
ATOM   2662 C C     . THR A 1 368 ? 24.129 -12.356 -12.281 1.00 17.39 ? 359 THR A C     1 
ATOM   2663 O O     . THR A 1 368 ? 23.192 -11.610 -12.587 1.00 15.08 ? 359 THR A O     1 
ATOM   2664 C CB    . THR A 1 368 ? 23.610 -13.893 -14.247 1.00 17.72 ? 359 THR A CB    1 
ATOM   2665 O OG1   . THR A 1 368 ? 22.851 -14.924 -13.589 1.00 17.56 ? 359 THR A OG1   1 
ATOM   2666 C CG2   . THR A 1 368 ? 24.236 -14.466 -15.608 1.00 19.49 ? 359 THR A CG2   1 
ATOM   2667 N N     . PHE A 1 369 ? 24.665 -12.315 -11.068 1.00 15.90 ? 360 PHE A N     1 
ATOM   2668 C CA    . PHE A 1 369 ? 24.239 -11.264 -10.126 1.00 14.87 ? 360 PHE A CA    1 
ATOM   2669 C C     . PHE A 1 369 ? 24.495 -9.854  -10.694 1.00 16.54 ? 360 PHE A C     1 
ATOM   2670 O O     . PHE A 1 369 ? 23.659 -8.956  -10.548 1.00 13.32 ? 360 PHE A O     1 
ATOM   2671 C CB    . PHE A 1 369 ? 24.978 -11.406 -8.797  1.00 16.49 ? 360 PHE A CB    1 
ATOM   2672 C CG    . PHE A 1 369 ? 24.411 -12.442 -7.857  1.00 17.00 ? 360 PHE A CG    1 
ATOM   2673 C CD1   . PHE A 1 369 ? 23.302 -13.226 -8.200  1.00 17.58 ? 360 PHE A CD1   1 
ATOM   2674 C CD2   . PHE A 1 369 ? 25.019 -12.651 -6.638  1.00 18.52 ? 360 PHE A CD2   1 
ATOM   2675 C CE1   . PHE A 1 369 ? 22.801 -14.202 -7.291  1.00 19.08 ? 360 PHE A CE1   1 
ATOM   2676 C CE2   . PHE A 1 369 ? 24.527 -13.622 -5.745  1.00 14.55 ? 360 PHE A CE2   1 
ATOM   2677 C CZ    . PHE A 1 369 ? 23.417 -14.375 -6.061  1.00 15.84 ? 360 PHE A CZ    1 
ATOM   2678 N N     . TYR A 1 370 ? 25.665 -9.613  -11.303 1.00 15.60 ? 361 TYR A N     1 
ATOM   2679 C CA    . TYR A 1 370 ? 26.056 -8.240  -11.636 1.00 13.66 ? 361 TYR A CA    1 
ATOM   2680 C C     . TYR A 1 370 ? 26.399 -8.076  -13.121 1.00 16.18 ? 361 TYR A C     1 
ATOM   2681 O O     . TYR A 1 370 ? 27.103 -7.131  -13.492 1.00 19.58 ? 361 TYR A O     1 
ATOM   2682 C CB    . TYR A 1 370 ? 27.267 -7.775  -10.830 1.00 13.75 ? 361 TYR A CB    1 
ATOM   2683 C CG    . TYR A 1 370 ? 27.186 -7.939  -9.361  1.00 14.99 ? 361 TYR A CG    1 
ATOM   2684 C CD1   . TYR A 1 370 ? 26.246 -7.217  -8.603  1.00 13.38 ? 361 TYR A CD1   1 
ATOM   2685 C CD2   . TYR A 1 370 ? 28.020 -8.839  -8.693  1.00 20.67 ? 361 TYR A CD2   1 
ATOM   2686 C CE1   . TYR A 1 370 ? 26.188 -7.351  -7.212  1.00 18.31 ? 361 TYR A CE1   1 
ATOM   2687 C CE2   . TYR A 1 370 ? 27.950 -8.976  -7.290  1.00 18.67 ? 361 TYR A CE2   1 
ATOM   2688 C CZ    . TYR A 1 370 ? 27.026 -8.233  -6.577  1.00 15.49 ? 361 TYR A CZ    1 
ATOM   2689 O OH    . TYR A 1 370 ? 26.953 -8.342  -5.206  1.00 17.26 ? 361 TYR A OH    1 
ATOM   2690 N N     . THR A 1 371 ? 25.976 -9.004  -13.965 1.00 19.29 ? 362 THR A N     1 
ATOM   2691 C CA    . THR A 1 371 ? 26.132 -8.893  -15.405 1.00 21.56 ? 362 THR A CA    1 
ATOM   2692 C C     . THR A 1 371 ? 25.110 -7.904  -15.967 1.00 21.30 ? 362 THR A C     1 
ATOM   2693 O O     . THR A 1 371 ? 24.242 -7.417  -15.240 1.00 16.84 ? 362 THR A O     1 
ATOM   2694 C CB    . THR A 1 371 ? 25.986 -10.277 -16.025 1.00 15.43 ? 362 THR A CB    1 
ATOM   2695 O OG1   . THR A 1 371 ? 24.831 -10.939 -15.476 1.00 16.77 ? 362 THR A OG1   1 
ATOM   2696 C CG2   . THR A 1 371 ? 27.246 -11.105 -15.742 1.00 20.89 ? 362 THR A CG2   1 
ATOM   2697 N N     . GLN A 1 372 ? 25.210 -7.595  -17.283 1.00 16.54 ? 363 GLN A N     1 
ATOM   2698 C CA    . GLN A 1 372 ? 24.454 -6.486  -17.864 1.00 21.23 ? 363 GLN A CA    1 
ATOM   2699 C C     . GLN A 1 372 ? 23.250 -6.906  -18.698 1.00 18.74 ? 363 GLN A C     1 
ATOM   2700 O O     . GLN A 1 372 ? 22.525 -6.023  -19.163 1.00 19.32 ? 363 GLN A O     1 
ATOM   2701 C CB    . GLN A 1 372 ? 25.374 -5.583  -18.735 1.00 16.13 ? 363 GLN A CB    1 
ATOM   2702 C CG    . GLN A 1 372 ? 26.136 -4.528  -17.951 1.00 15.83 ? 363 GLN A CG    1 
ATOM   2703 C CD    . GLN A 1 372 ? 27.005 -5.183  -16.891 1.00 25.08 ? 363 GLN A CD    1 
ATOM   2704 O OE1   . GLN A 1 372 ? 28.042 -5.782  -17.191 1.00 19.95 ? 363 GLN A OE1   1 
ATOM   2705 N NE2   . GLN A 1 372 ? 26.556 -5.116  -15.669 1.00 17.77 ? 363 GLN A NE2   1 
ATOM   2706 N N     . ASP A 1 373 ? 23.028 -8.199  -18.906 1.00 18.20 ? 364 ASP A N     1 
ATOM   2707 C CA    . ASP A 1 373 ? 21.980 -8.653  -19.812 1.00 18.46 ? 364 ASP A CA    1 
ATOM   2708 C C     . ASP A 1 373 ? 20.615 -8.310  -19.248 1.00 21.81 ? 364 ASP A C     1 
ATOM   2709 O O     . ASP A 1 373 ? 20.342 -8.629  -18.087 1.00 20.55 ? 364 ASP A O     1 
ATOM   2710 C CB    . ASP A 1 373 ? 22.074 -10.152 -20.003 1.00 20.62 ? 364 ASP A CB    1 
ATOM   2711 C CG    . ASP A 1 373 ? 21.277 -10.647 -21.193 1.00 24.09 ? 364 ASP A CG    1 
ATOM   2712 O OD1   . ASP A 1 373 ? 20.025 -10.629 -21.161 1.00 19.10 ? 364 ASP A OD1   1 
ATOM   2713 O OD2   . ASP A 1 373 ? 21.935 -11.095 -22.162 1.00 26.11 ? 364 ASP A OD2   1 
ATOM   2714 N N     . PRO A 1 374 ? 19.721 -7.709  -20.036 1.00 19.88 ? 365 PRO A N     1 
ATOM   2715 C CA    . PRO A 1 374 ? 18.432 -7.268  -19.483 1.00 19.83 ? 365 PRO A CA    1 
ATOM   2716 C C     . PRO A 1 374 ? 17.478 -8.400  -19.153 1.00 20.36 ? 365 PRO A C     1 
ATOM   2717 O O     . PRO A 1 374 ? 16.431 -8.139  -18.538 1.00 19.32 ? 365 PRO A O     1 
ATOM   2718 C CB    . PRO A 1 374 ? 17.880 -6.349  -20.588 1.00 21.22 ? 365 PRO A CB    1 
ATOM   2719 C CG    . PRO A 1 374 ? 18.544 -6.863  -21.878 1.00 20.82 ? 365 PRO A CG    1 
ATOM   2720 C CD    . PRO A 1 374 ? 19.913 -7.290  -21.446 1.00 23.85 ? 365 PRO A CD    1 
ATOM   2721 N N     . VAL A 1 375 ? 17.795 -9.638  -19.544 1.00 19.55 ? 366 VAL A N     1 
ATOM   2722 C CA    . VAL A 1 375 ? 16.928 -10.798 -19.390 1.00 19.34 ? 366 VAL A CA    1 
ATOM   2723 C C     . VAL A 1 375 ? 17.673 -11.866 -18.610 1.00 18.79 ? 366 VAL A C     1 
ATOM   2724 O O     . VAL A 1 375 ? 17.190 -12.348 -17.577 1.00 18.56 ? 366 VAL A O     1 
ATOM   2725 C CB    . VAL A 1 375 ? 16.486 -11.371 -20.755 1.00 21.95 ? 366 VAL A CB    1 
ATOM   2726 C CG1   . VAL A 1 375 ? 15.688 -12.640 -20.547 1.00 23.14 ? 366 VAL A CG1   1 
ATOM   2727 C CG2   . VAL A 1 375 ? 15.686 -10.352 -21.552 1.00 20.54 ? 366 VAL A CG2   1 
ATOM   2728 N N     . VAL A 1 376 ? 18.836 -12.286 -19.121 1.00 20.87 ? 367 VAL A N     1 
ATOM   2729 C CA    . VAL A 1 376 ? 19.455 -13.516 -18.635 1.00 20.21 ? 367 VAL A CA    1 
ATOM   2730 C C     . VAL A 1 376 ? 19.939 -13.339 -17.204 1.00 19.17 ? 367 VAL A C     1 
ATOM   2731 O O     . VAL A 1 376 ? 20.779 -12.478 -16.917 1.00 18.15 ? 367 VAL A O     1 
ATOM   2732 C CB    . VAL A 1 376 ? 20.618 -13.967 -19.531 1.00 19.99 ? 367 VAL A CB    1 
ATOM   2733 C CG1   . VAL A 1 376 ? 21.332 -15.109 -18.854 1.00 21.03 ? 367 VAL A CG1   1 
ATOM   2734 C CG2   . VAL A 1 376 ? 20.116 -14.435 -20.901 1.00 24.43 ? 367 VAL A CG2   1 
ATOM   2735 N N     . GLY A 1 377 ? 19.455 -14.213 -16.319 1.00 18.99 ? 368 GLY A N     1 
ATOM   2736 C CA    . GLY A 1 377 ? 19.776 -14.155 -14.912 1.00 15.84 ? 368 GLY A CA    1 
ATOM   2737 C C     . GLY A 1 377 ? 19.162 -12.958 -14.222 1.00 19.65 ? 368 GLY A C     1 
ATOM   2738 O O     . GLY A 1 377 ? 19.637 -12.556 -13.160 1.00 15.15 ? 368 GLY A O     1 
ATOM   2739 N N     . TYR A 1 378 ? 18.149 -12.344 -14.828 1.00 20.52 ? 369 TYR A N     1 
ATOM   2740 C CA    . TYR A 1 378 ? 17.542 -11.137 -14.272 1.00 16.32 ? 369 TYR A CA    1 
ATOM   2741 C C     . TYR A 1 378 ? 16.033 -11.297 -14.235 1.00 17.48 ? 369 TYR A C     1 
ATOM   2742 O O     . TYR A 1 378 ? 15.430 -11.344 -13.154 1.00 18.29 ? 369 TYR A O     1 
ATOM   2743 C CB    . TYR A 1 378 ? 17.927 -9.918  -15.105 1.00 15.28 ? 369 TYR A CB    1 
ATOM   2744 C CG    . TYR A 1 378 ? 17.653 -8.595  -14.441 1.00 16.82 ? 369 TYR A CG    1 
ATOM   2745 C CD1   . TYR A 1 378 ? 18.052 -8.346  -13.130 1.00 16.82 ? 369 TYR A CD1   1 
ATOM   2746 C CD2   . TYR A 1 378 ? 17.013 -7.581  -15.147 1.00 16.56 ? 369 TYR A CD2   1 
ATOM   2747 C CE1   . TYR A 1 378 ? 17.801 -7.060  -12.493 1.00 14.59 ? 369 TYR A CE1   1 
ATOM   2748 C CE2   . TYR A 1 378 ? 16.778 -6.354  -14.571 1.00 15.89 ? 369 TYR A CE2   1 
ATOM   2749 C CZ    . TYR A 1 378 ? 17.149 -6.091  -13.253 1.00 16.64 ? 369 TYR A CZ    1 
ATOM   2750 O OH    . TYR A 1 378 ? 16.854 -4.849  -12.760 1.00 20.30 ? 369 TYR A OH    1 
ATOM   2751 N N     . THR A 1 379 ? 15.403 -11.376 -15.420 1.00 17.81 ? 370 THR A N     1 
ATOM   2752 C CA    . THR A 1 379 ? 13.956 -11.562 -15.497 1.00 18.16 ? 370 THR A CA    1 
ATOM   2753 C C     . THR A 1 379 ? 13.544 -12.940 -16.014 1.00 20.72 ? 370 THR A C     1 
ATOM   2754 O O     . THR A 1 379 ? 12.342 -13.191 -16.152 1.00 17.91 ? 370 THR A O     1 
ATOM   2755 C CB    . THR A 1 379 ? 13.319 -10.497 -16.400 1.00 19.29 ? 370 THR A CB    1 
ATOM   2756 O OG1   . THR A 1 379 ? 13.841 -10.647 -17.727 1.00 19.79 ? 370 THR A OG1   1 
ATOM   2757 C CG2   . THR A 1 379 ? 13.602 -9.068  -15.907 1.00 21.82 ? 370 THR A CG2   1 
ATOM   2758 N N     . ASP A 1 380 ? 14.482 -13.844 -16.315 1.00 17.65 ? 371 ASP A N     1 
ATOM   2759 C CA    . ASP A 1 380 ? 14.089 -15.152 -16.835 1.00 17.99 ? 371 ASP A CA    1 
ATOM   2760 C C     . ASP A 1 380 ? 14.098 -16.263 -15.794 1.00 22.07 ? 371 ASP A C     1 
ATOM   2761 O O     . ASP A 1 380 ? 14.024 -17.431 -16.163 1.00 19.87 ? 371 ASP A O     1 
ATOM   2762 C CB    . ASP A 1 380 ? 14.965 -15.548 -18.033 1.00 20.47 ? 371 ASP A CB    1 
ATOM   2763 C CG    . ASP A 1 380 ? 16.462 -15.672 -17.697 1.00 25.09 ? 371 ASP A CG    1 
ATOM   2764 O OD1   . ASP A 1 380 ? 16.890 -15.438 -16.550 1.00 21.93 ? 371 ASP A OD1   1 
ATOM   2765 O OD2   . ASP A 1 380 ? 17.221 -16.019 -18.638 1.00 28.58 ? 371 ASP A OD2   1 
ATOM   2766 N N     . TYR A 1 381 ? 14.187 -15.943 -14.508 1.00 21.99 ? 372 TYR A N     1 
ATOM   2767 C CA    . TYR A 1 381 ? 13.887 -16.946 -13.501 1.00 20.72 ? 372 TYR A CA    1 
ATOM   2768 C C     . TYR A 1 381 ? 12.387 -17.216 -13.522 1.00 22.49 ? 372 TYR A C     1 
ATOM   2769 O O     . TYR A 1 381 ? 11.594 -16.276 -13.391 1.00 22.09 ? 372 TYR A O     1 
ATOM   2770 C CB    . TYR A 1 381 ? 14.294 -16.475 -12.102 1.00 17.14 ? 372 TYR A CB    1 
ATOM   2771 C CG    . TYR A 1 381 ? 15.780 -16.443 -11.855 1.00 18.27 ? 372 TYR A CG    1 
ATOM   2772 C CD1   . TYR A 1 381 ? 16.461 -17.600 -11.557 1.00 17.51 ? 372 TYR A CD1   1 
ATOM   2773 C CD2   . TYR A 1 381 ? 16.486 -15.235 -11.851 1.00 15.95 ? 372 TYR A CD2   1 
ATOM   2774 C CE1   . TYR A 1 381 ? 17.834 -17.602 -11.249 1.00 20.52 ? 372 TYR A CE1   1 
ATOM   2775 C CE2   . TYR A 1 381 ? 17.892 -15.220 -11.568 1.00 18.79 ? 372 TYR A CE2   1 
ATOM   2776 C CZ    . TYR A 1 381 ? 18.535 -16.418 -11.253 1.00 18.51 ? 372 TYR A CZ    1 
ATOM   2777 O OH    . TYR A 1 381 ? 19.871 -16.452 -10.969 1.00 17.85 ? 372 TYR A OH    1 
ATOM   2778 N N     . PRO A 1 382 ? 11.965 -18.475 -13.589 1.00 28.96 ? 373 PRO A N     1 
ATOM   2779 C CA    . PRO A 1 382 ? 10.547 -18.774 -13.796 1.00 25.47 ? 373 PRO A CA    1 
ATOM   2780 C C     . PRO A 1 382 ? 9.696  -18.639 -12.547 1.00 24.13 ? 373 PRO A C     1 
ATOM   2781 O O     . PRO A 1 382 ? 10.137 -18.854 -11.408 1.00 23.06 ? 373 PRO A O     1 
ATOM   2782 C CB    . PRO A 1 382 ? 10.562 -20.236 -14.271 1.00 22.93 ? 373 PRO A CB    1 
ATOM   2783 C CG    . PRO A 1 382 ? 12.023 -20.583 -14.503 1.00 35.47 ? 373 PRO A CG    1 
ATOM   2784 C CD    . PRO A 1 382 ? 12.783 -19.699 -13.580 1.00 30.12 ? 373 PRO A CD    1 
ATOM   2785 N N     . PHE A 1 383 ? 8.434  -18.301 -12.796 1.00 23.20 ? 374 PHE A N     1 
ATOM   2786 C CA    . PHE A 1 383 ? 7.410  -18.379 -11.780 1.00 24.14 ? 374 PHE A CA    1 
ATOM   2787 C C     . PHE A 1 383 ? 7.074  -19.846 -11.490 1.00 25.18 ? 374 PHE A C     1 
ATOM   2788 O O     . PHE A 1 383 ? 7.437  -20.763 -12.234 1.00 28.76 ? 374 PHE A O     1 
ATOM   2789 C CB    . PHE A 1 383 ? 6.165  -17.604 -12.232 1.00 24.66 ? 374 PHE A CB    1 
ATOM   2790 C CG    . PHE A 1 383 ? 6.326  -16.104 -12.200 1.00 21.91 ? 374 PHE A CG    1 
ATOM   2791 C CD1   . PHE A 1 383 ? 7.018  -15.434 -13.193 1.00 28.23 ? 374 PHE A CD1   1 
ATOM   2792 C CD2   . PHE A 1 383 ? 5.752  -15.360 -11.172 1.00 24.81 ? 374 PHE A CD2   1 
ATOM   2793 C CE1   . PHE A 1 383 ? 7.150  -14.036 -13.155 1.00 23.79 ? 374 PHE A CE1   1 
ATOM   2794 C CE2   . PHE A 1 383 ? 5.892  -13.976 -11.131 1.00 23.20 ? 374 PHE A CE2   1 
ATOM   2795 C CZ    . PHE A 1 383 ? 6.586  -13.318 -12.120 1.00 25.97 ? 374 PHE A CZ    1 
ATOM   2796 N N     . LEU A 1 384 ? 6.350  -20.054 -10.392 1.00 23.89 ? 375 LEU A N     1 
ATOM   2797 C CA    . LEU A 1 384 ? 6.036  -21.382 -9.900  1.00 24.97 ? 375 LEU A CA    1 
ATOM   2798 C C     . LEU A 1 384 ? 5.106  -22.110 -10.858 1.00 27.48 ? 375 LEU A C     1 
ATOM   2799 O O     . LEU A 1 384 ? 4.533  -21.475 -11.739 1.00 32.30 ? 375 LEU A O     1 
ATOM   2800 C CB    . LEU A 1 384 ? 5.403  -21.255 -8.509  1.00 24.37 ? 375 LEU A CB    1 
ATOM   2801 C CG    . LEU A 1 384 ? 5.103  -22.493 -7.726  1.00 28.31 ? 375 LEU A CG    1 
ATOM   2802 C CD1   . LEU A 1 384 ? 6.396  -23.169 -7.367  1.00 26.70 ? 375 LEU A CD1   1 
ATOM   2803 C CD2   . LEU A 1 384 ? 4.378  -21.990 -6.501  1.00 30.34 ? 375 LEU A CD2   1 
ATOM   2804 N N     . ASN B 1 19  ? 38.815 13.947  60.943  1.00 39.19 ? 10  ASN B N     1 
ATOM   2805 C CA    . ASN B 1 19  ? 37.659 13.471  60.173  1.00 35.72 ? 10  ASN B CA    1 
ATOM   2806 C C     . ASN B 1 19  ? 37.458 11.984  60.402  1.00 28.00 ? 10  ASN B C     1 
ATOM   2807 O O     . ASN B 1 19  ? 38.212 11.171  59.886  1.00 31.13 ? 10  ASN B O     1 
ATOM   2808 C CB    . ASN B 1 19  ? 37.824 13.740  58.661  1.00 32.87 ? 10  ASN B CB    1 
ATOM   2809 C CG    . ASN B 1 19  ? 36.540 13.428  57.852  1.00 31.62 ? 10  ASN B CG    1 
ATOM   2810 O OD1   . ASN B 1 19  ? 35.647 12.711  58.314  1.00 27.03 ? 10  ASN B OD1   1 
ATOM   2811 N ND2   . ASN B 1 19  ? 36.464 13.961  56.637  1.00 28.48 ? 10  ASN B ND2   1 
ATOM   2812 N N     . PRO B 1 20  ? 36.429 11.630  61.172  1.00 30.27 ? 11  PRO B N     1 
ATOM   2813 C CA    . PRO B 1 20  ? 36.209 10.211  61.489  1.00 25.10 ? 11  PRO B CA    1 
ATOM   2814 C C     . PRO B 1 20  ? 35.826 9.371   60.281  1.00 23.79 ? 11  PRO B C     1 
ATOM   2815 O O     . PRO B 1 20  ? 35.905 8.146   60.367  1.00 25.74 ? 11  PRO B O     1 
ATOM   2816 C CB    . PRO B 1 20  ? 35.081 10.251  62.530  1.00 27.67 ? 11  PRO B CB    1 
ATOM   2817 C CG    . PRO B 1 20  ? 34.374 11.539  62.261  1.00 33.58 ? 11  PRO B CG    1 
ATOM   2818 C CD    . PRO B 1 20  ? 35.445 12.508  61.820  1.00 30.34 ? 11  PRO B CD    1 
ATOM   2819 N N     . LEU B 1 21  ? 35.406 9.976   59.168  1.00 21.22 ? 12  LEU B N     1 
ATOM   2820 C CA    . LEU B 1 21  ? 35.222 9.212   57.932  1.00 26.67 ? 12  LEU B CA    1 
ATOM   2821 C C     . LEU B 1 21  ? 36.507 8.573   57.456  1.00 27.10 ? 12  LEU B C     1 
ATOM   2822 O O     . LEU B 1 21  ? 36.454 7.589   56.711  1.00 24.85 ? 12  LEU B O     1 
ATOM   2823 C CB    . LEU B 1 21  ? 34.655 10.097  56.815  1.00 26.39 ? 12  LEU B CB    1 
ATOM   2824 C CG    . LEU B 1 21  ? 33.147 10.288  56.970  1.00 25.31 ? 12  LEU B CG    1 
ATOM   2825 C CD1   . LEU B 1 21  ? 32.573 11.134  55.832  1.00 26.55 ? 12  LEU B CD1   1 
ATOM   2826 C CD2   . LEU B 1 21  ? 32.458 8.955   57.034  1.00 23.16 ? 12  LEU B CD2   1 
ATOM   2827 N N     . PHE B 1 22  ? 37.661 9.091   57.881  1.00 24.70 ? 13  PHE B N     1 
ATOM   2828 C CA    . PHE B 1 22  ? 38.948 8.560   57.456  1.00 25.58 ? 13  PHE B CA    1 
ATOM   2829 C C     . PHE B 1 22  ? 39.696 7.875   58.582  1.00 26.63 ? 13  PHE B C     1 
ATOM   2830 O O     . PHE B 1 22  ? 40.923 7.721   58.522  1.00 30.78 ? 13  PHE B O     1 
ATOM   2831 C CB    . PHE B 1 22  ? 39.756 9.672   56.800  1.00 23.92 ? 13  PHE B CB    1 
ATOM   2832 C CG    . PHE B 1 22  ? 39.141 10.085  55.520  1.00 27.14 ? 13  PHE B CG    1 
ATOM   2833 C CD1   . PHE B 1 22  ? 39.368 9.351   54.372  1.00 24.58 ? 13  PHE B CD1   1 
ATOM   2834 C CD2   . PHE B 1 22  ? 38.222 11.118  55.490  1.00 25.08 ? 13  PHE B CD2   1 
ATOM   2835 C CE1   . PHE B 1 22  ? 38.735 9.685   53.179  1.00 23.35 ? 13  PHE B CE1   1 
ATOM   2836 C CE2   . PHE B 1 22  ? 37.582 11.456  54.296  1.00 30.16 ? 13  PHE B CE2   1 
ATOM   2837 C CZ    . PHE B 1 22  ? 37.836 10.723  53.143  1.00 23.85 ? 13  PHE B CZ    1 
ATOM   2838 N N     . SER B 1 23  ? 38.965 7.402   59.568  1.00 29.17 ? 14  SER B N     1 
ATOM   2839 C CA    . SER B 1 23  ? 39.525 6.482   60.540  1.00 28.13 ? 14  SER B CA    1 
ATOM   2840 C C     . SER B 1 23  ? 39.309 5.048   60.060  1.00 28.30 ? 14  SER B C     1 
ATOM   2841 O O     . SER B 1 23  ? 38.240 4.730   59.518  1.00 29.31 ? 14  SER B O     1 
ATOM   2842 C CB    . SER B 1 23  ? 38.877 6.695   61.897  1.00 27.83 ? 14  SER B CB    1 
ATOM   2843 O OG    . SER B 1 23  ? 37.515 6.304   61.851  1.00 32.32 ? 14  SER B OG    1 
ATOM   2844 N N     . PRO B 1 24  ? 40.326 4.189   60.187  1.00 30.26 ? 15  PRO B N     1 
ATOM   2845 C CA    . PRO B 1 24  ? 40.226 2.823   59.646  1.00 26.91 ? 15  PRO B CA    1 
ATOM   2846 C C     . PRO B 1 24  ? 39.134 2.024   60.338  1.00 27.27 ? 15  PRO B C     1 
ATOM   2847 O O     . PRO B 1 24  ? 38.693 2.348   61.444  1.00 26.33 ? 15  PRO B O     1 
ATOM   2848 C CB    . PRO B 1 24  ? 41.603 2.220   59.942  1.00 33.43 ? 15  PRO B CB    1 
ATOM   2849 C CG    . PRO B 1 24  ? 42.095 3.001   61.131  1.00 32.01 ? 15  PRO B CG    1 
ATOM   2850 C CD    . PRO B 1 24  ? 41.600 4.410   60.892  1.00 33.29 ? 15  PRO B CD    1 
ATOM   2851 N N     . TYR B 1 25  ? 38.720 0.951   59.670  1.00 28.44 ? 16  TYR B N     1 
ATOM   2852 C CA    . TYR B 1 25  ? 37.644 0.104   60.162  1.00 23.66 ? 16  TYR B CA    1 
ATOM   2853 C C     . TYR B 1 25  ? 37.858 -1.335  59.713  1.00 25.32 ? 16  TYR B C     1 
ATOM   2854 O O     . TYR B 1 25  ? 38.095 -1.592  58.532  1.00 25.97 ? 16  TYR B O     1 
ATOM   2855 C CB    . TYR B 1 25  ? 36.267 0.584   59.673  1.00 22.90 ? 16  TYR B CB    1 
ATOM   2856 C CG    . TYR B 1 25  ? 35.157 -0.189  60.353  1.00 22.37 ? 16  TYR B CG    1 
ATOM   2857 C CD1   . TYR B 1 25  ? 34.775 0.130   61.652  1.00 26.97 ? 16  TYR B CD1   1 
ATOM   2858 C CD2   . TYR B 1 25  ? 34.519 -1.264  59.724  1.00 24.24 ? 16  TYR B CD2   1 
ATOM   2859 C CE1   . TYR B 1 25  ? 33.785 -0.581  62.305  1.00 23.97 ? 16  TYR B CE1   1 
ATOM   2860 C CE2   . TYR B 1 25  ? 33.507 -1.994  60.380  1.00 23.98 ? 16  TYR B CE2   1 
ATOM   2861 C CZ    . TYR B 1 25  ? 33.158 -1.641  61.672  1.00 23.45 ? 16  TYR B CZ    1 
ATOM   2862 O OH    . TYR B 1 25  ? 32.174 -2.348  62.344  1.00 18.90 ? 16  TYR B OH    1 
ATOM   2863 N N     . LYS B 1 26  ? 37.726 -2.273  60.649  1.00 24.80 ? 17  LYS B N     1 
ATOM   2864 C CA    . LYS B 1 26  ? 37.837 -3.707  60.355  1.00 27.54 ? 17  LYS B CA    1 
ATOM   2865 C C     . LYS B 1 26  ? 36.448 -4.251  60.033  1.00 24.18 ? 17  LYS B C     1 
ATOM   2866 O O     . LYS B 1 26  ? 35.618 -4.455  60.923  1.00 27.52 ? 17  LYS B O     1 
ATOM   2867 C CB    . LYS B 1 26  ? 38.468 -4.445  61.535  1.00 30.18 ? 17  LYS B CB    1 
ATOM   2868 N N     . MET B 1 27  ? 36.169 -4.448  58.744  1.00 24.23 ? 18  MET B N     1 
ATOM   2869 C CA    . MET B 1 27  ? 34.937 -5.116  58.321  1.00 29.26 ? 18  MET B CA    1 
ATOM   2870 C C     . MET B 1 27  ? 35.171 -6.621  58.339  1.00 33.17 ? 18  MET B C     1 
ATOM   2871 O O     . MET B 1 27  ? 35.338 -7.262  57.300  1.00 31.51 ? 18  MET B O     1 
ATOM   2872 C CB    . MET B 1 27  ? 34.512 -4.695  56.919  1.00 29.04 ? 18  MET B CB    1 
ATOM   2873 C CG    . MET B 1 27  ? 33.013 -4.844  56.708  1.00 28.87 ? 18  MET B CG    1 
ATOM   2874 S SD    . MET B 1 27  ? 32.463 -4.140  55.149  1.00 30.78 ? 18  MET B SD    1 
ATOM   2875 C CE    . MET B 1 27  ? 33.538 -4.958  53.981  1.00 20.83 ? 18  MET B CE    1 
ATOM   2876 N N     . GLY B 1 28  ? 35.186 -7.192  59.542  1.00 37.28 ? 19  GLY B N     1 
ATOM   2877 C CA    . GLY B 1 28  ? 35.539 -8.602  59.646  1.00 36.83 ? 19  GLY B CA    1 
ATOM   2878 C C     . GLY B 1 28  ? 36.975 -8.782  59.208  1.00 33.18 ? 19  GLY B C     1 
ATOM   2879 O O     . GLY B 1 28  ? 37.888 -8.134  59.742  1.00 35.14 ? 19  GLY B O     1 
ATOM   2880 N N     . LYS B 1 29  ? 37.201 -9.602  58.182  1.00 28.89 ? 20  LYS B N     1 
ATOM   2881 C CA    . LYS B 1 29  ? 38.572 -9.787  57.732  1.00 32.31 ? 20  LYS B CA    1 
ATOM   2882 C C     . LYS B 1 29  ? 39.076 -8.672  56.817  1.00 33.67 ? 20  LYS B C     1 
ATOM   2883 O O     . LYS B 1 29  ? 40.278 -8.633  56.531  1.00 32.14 ? 20  LYS B O     1 
ATOM   2884 C CB    . LYS B 1 29  ? 38.716 -11.103 56.993  1.00 36.00 ? 20  LYS B CB    1 
ATOM   2885 C CG    . LYS B 1 29  ? 37.527 -11.422 56.137  1.00 36.58 ? 20  LYS B CG    1 
ATOM   2886 C CD    . LYS B 1 29  ? 37.690 -12.801 55.628  1.00 43.73 ? 20  LYS B CD    1 
ATOM   2887 C CE    . LYS B 1 29  ? 38.419 -12.816 54.327  1.00 43.21 ? 20  LYS B CE    1 
ATOM   2888 N NZ    . LYS B 1 29  ? 38.040 -14.097 53.738  1.00 42.36 ? 20  LYS B NZ    1 
ATOM   2889 N N     . PHE B 1 30  ? 38.216 -7.775  56.342  1.00 24.95 ? 21  PHE B N     1 
ATOM   2890 C CA    . PHE B 1 30  ? 38.656 -6.748  55.397  1.00 25.67 ? 21  PHE B CA    1 
ATOM   2891 C C     . PHE B 1 30  ? 39.010 -5.491  56.176  1.00 25.68 ? 21  PHE B C     1 
ATOM   2892 O O     . PHE B 1 30  ? 38.189 -4.971  56.942  1.00 26.98 ? 21  PHE B O     1 
ATOM   2893 C CB    . PHE B 1 30  ? 37.572 -6.471  54.354  1.00 26.30 ? 21  PHE B CB    1 
ATOM   2894 C CG    . PHE B 1 30  ? 37.138 -7.700  53.620  1.00 23.55 ? 21  PHE B CG    1 
ATOM   2895 C CD1   . PHE B 1 30  ? 37.978 -8.286  52.686  1.00 24.53 ? 21  PHE B CD1   1 
ATOM   2896 C CD2   . PHE B 1 30  ? 35.919 -8.299  53.886  1.00 28.64 ? 21  PHE B CD2   1 
ATOM   2897 C CE1   . PHE B 1 30  ? 37.601 -9.433  52.022  1.00 27.45 ? 21  PHE B CE1   1 
ATOM   2898 C CE2   . PHE B 1 30  ? 35.538 -9.455  53.214  1.00 28.31 ? 21  PHE B CE2   1 
ATOM   2899 C CZ    . PHE B 1 30  ? 36.379 -10.016 52.287  1.00 25.52 ? 21  PHE B CZ    1 
ATOM   2900 N N     . ASN B 1 31  ? 40.229 -5.011  56.012  1.00 23.36 ? 22  ASN B N     1 
ATOM   2901 C CA    . ASN B 1 31  ? 40.678 -3.839  56.754  1.00 26.63 ? 22  ASN B CA    1 
ATOM   2902 C C     . ASN B 1 31  ? 40.470 -2.606  55.876  1.00 28.89 ? 22  ASN B C     1 
ATOM   2903 O O     . ASN B 1 31  ? 41.219 -2.377  54.922  1.00 28.78 ? 22  ASN B O     1 
ATOM   2904 C CB    . ASN B 1 31  ? 42.129 -4.011  57.186  1.00 33.57 ? 22  ASN B CB    1 
ATOM   2905 C CG    . ASN B 1 31  ? 42.254 -4.967  58.352  1.00 34.79 ? 22  ASN B CG    1 
ATOM   2906 O OD1   . ASN B 1 31  ? 41.734 -4.701  59.439  1.00 39.30 ? 22  ASN B OD1   1 
ATOM   2907 N ND2   . ASN B 1 31  ? 42.927 -6.088  58.133  1.00 39.45 ? 22  ASN B ND2   1 
ATOM   2908 N N     . LEU B 1 32  ? 39.443 -1.819  56.196  1.00 23.96 ? 23  LEU B N     1 
ATOM   2909 C CA    . LEU B 1 32  ? 39.108 -0.640  55.405  1.00 20.96 ? 23  LEU B CA    1 
ATOM   2910 C C     . LEU B 1 32  ? 39.891 0.564   55.898  1.00 23.45 ? 23  LEU B C     1 
ATOM   2911 O O     . LEU B 1 32  ? 40.052 0.772   57.110  1.00 22.49 ? 23  LEU B O     1 
ATOM   2912 C CB    . LEU B 1 32  ? 37.613 -0.345  55.477  1.00 16.18 ? 23  LEU B CB    1 
ATOM   2913 C CG    . LEU B 1 32  ? 36.770 -1.526  54.980  1.00 21.51 ? 23  LEU B CG    1 
ATOM   2914 C CD1   . LEU B 1 32  ? 35.296 -1.180  55.017  1.00 21.10 ? 23  LEU B CD1   1 
ATOM   2915 C CD2   . LEU B 1 32  ? 37.173 -1.955  53.567  1.00 22.86 ? 23  LEU B CD2   1 
ATOM   2916 N N     . SER B 1 33  ? 40.363 1.364   54.952  1.00 22.15 ? 24  SER B N     1 
ATOM   2917 C CA    . SER B 1 33  ? 41.154 2.531   55.295  1.00 22.28 ? 24  SER B CA    1 
ATOM   2918 C C     . SER B 1 33  ? 40.303 3.781   55.549  1.00 25.67 ? 24  SER B C     1 
ATOM   2919 O O     . SER B 1 33  ? 40.820 4.758   56.115  1.00 25.16 ? 24  SER B O     1 
ATOM   2920 C CB    . SER B 1 33  ? 42.191 2.754   54.189  1.00 22.22 ? 24  SER B CB    1 
ATOM   2921 O OG    . SER B 1 33  ? 41.588 3.483   53.144  1.00 29.05 ? 24  SER B OG    1 
ATOM   2922 N N     . HIS B 1 34  ? 39.004 3.743   55.227  1.00 22.94 ? 25  HIS B N     1 
ATOM   2923 C CA    . HIS B 1 34  ? 38.087 4.868   55.385  1.00 20.53 ? 25  HIS B CA    1 
ATOM   2924 C C     . HIS B 1 34  ? 36.673 4.306   55.273  1.00 19.47 ? 25  HIS B C     1 
ATOM   2925 O O     . HIS B 1 34  ? 36.469 3.152   54.892  1.00 19.78 ? 25  HIS B O     1 
ATOM   2926 C CB    . HIS B 1 34  ? 38.334 5.976   54.340  1.00 20.20 ? 25  HIS B CB    1 
ATOM   2927 C CG    . HIS B 1 34  ? 38.093 5.546   52.933  1.00 20.41 ? 25  HIS B CG    1 
ATOM   2928 N ND1   . HIS B 1 34  ? 36.824 5.415   52.409  1.00 19.40 ? 25  HIS B ND1   1 
ATOM   2929 C CD2   . HIS B 1 34  ? 38.950 5.219   51.934  1.00 19.07 ? 25  HIS B CD2   1 
ATOM   2930 C CE1   . HIS B 1 34  ? 36.911 5.031   51.144  1.00 19.67 ? 25  HIS B CE1   1 
ATOM   2931 N NE2   . HIS B 1 34  ? 38.189 4.895   50.834  1.00 20.87 ? 25  HIS B NE2   1 
ATOM   2932 N N     . ARG B 1 35  ? 35.690 5.137   55.592  1.00 20.98 ? 26  ARG B N     1 
ATOM   2933 C CA    . ARG B 1 35  ? 34.345 4.630   55.774  1.00 19.32 ? 26  ARG B CA    1 
ATOM   2934 C C     . ARG B 1 35  ? 33.396 5.062   54.666  1.00 20.78 ? 26  ARG B C     1 
ATOM   2935 O O     . ARG B 1 35  ? 32.178 4.883   54.815  1.00 19.91 ? 26  ARG B O     1 
ATOM   2936 C CB    . ARG B 1 35  ? 33.805 5.050   57.138  1.00 22.48 ? 26  ARG B CB    1 
ATOM   2937 C CG    . ARG B 1 35  ? 34.472 4.265   58.280  1.00 27.34 ? 26  ARG B CG    1 
ATOM   2938 C CD    . ARG B 1 35  ? 34.918 5.149   59.337  1.00 31.52 ? 26  ARG B CD    1 
ATOM   2939 N NE    . ARG B 1 35  ? 35.719 4.453   60.342  1.00 26.34 ? 26  ARG B NE    1 
ATOM   2940 C CZ    . ARG B 1 35  ? 35.231 3.859   61.418  1.00 26.50 ? 26  ARG B CZ    1 
ATOM   2941 N NH1   . ARG B 1 35  ? 33.936 3.608   61.546  1.00 22.68 ? 26  ARG B NH1   1 
ATOM   2942 N NH2   . ARG B 1 35  ? 36.064 3.541   62.412  1.00 23.46 ? 26  ARG B NH2   1 
ATOM   2943 N N     . VAL B 1 36  ? 33.911 5.633   53.575  1.00 17.28 ? 27  VAL B N     1 
ATOM   2944 C CA    . VAL B 1 36  ? 33.066 6.088   52.481  1.00 18.02 ? 27  VAL B CA    1 
ATOM   2945 C C     . VAL B 1 36  ? 32.850 4.907   51.536  1.00 17.79 ? 27  VAL B C     1 
ATOM   2946 O O     . VAL B 1 36  ? 33.806 4.380   50.955  1.00 17.88 ? 27  VAL B O     1 
ATOM   2947 C CB    . VAL B 1 36  ? 33.679 7.302   51.752  1.00 19.85 ? 27  VAL B CB    1 
ATOM   2948 C CG1   . VAL B 1 36  ? 32.800 7.726   50.555  1.00 19.00 ? 27  VAL B CG1   1 
ATOM   2949 C CG2   . VAL B 1 36  ? 33.855 8.515   52.698  1.00 18.69 ? 27  VAL B CG2   1 
ATOM   2950 N N     . VAL B 1 37  ? 31.601 4.490   51.382  1.00 15.47 ? 28  VAL B N     1 
ATOM   2951 C CA    . VAL B 1 37  ? 31.271 3.284   50.604  1.00 14.89 ? 28  VAL B CA    1 
ATOM   2952 C C     . VAL B 1 37  ? 30.521 3.665   49.336  1.00 17.48 ? 28  VAL B C     1 
ATOM   2953 O O     . VAL B 1 37  ? 29.613 4.504   49.363  1.00 16.07 ? 28  VAL B O     1 
ATOM   2954 C CB    . VAL B 1 37  ? 30.421 2.304   51.431  1.00 14.33 ? 28  VAL B CB    1 
ATOM   2955 C CG1   . VAL B 1 37  ? 29.920 1.118   50.532  1.00 15.97 ? 28  VAL B CG1   1 
ATOM   2956 C CG2   . VAL B 1 37  ? 31.232 1.817   52.679  1.00 14.96 ? 28  VAL B CG2   1 
ATOM   2957 N N     . LEU B 1 38  ? 30.857 3.011   48.226  1.00 15.69 ? 29  LEU B N     1 
ATOM   2958 C CA    . LEU B 1 38  ? 30.072 3.196   47.003  1.00 16.11 ? 29  LEU B CA    1 
ATOM   2959 C C     . LEU B 1 38  ? 28.788 2.377   47.114  1.00 15.68 ? 29  LEU B C     1 
ATOM   2960 O O     . LEU B 1 38  ? 28.830 1.143   47.236  1.00 18.45 ? 29  LEU B O     1 
ATOM   2961 C CB    . LEU B 1 38  ? 30.889 2.789   45.784  1.00 14.08 ? 29  LEU B CB    1 
ATOM   2962 C CG    . LEU B 1 38  ? 30.078 2.661   44.467  1.00 17.23 ? 29  LEU B CG    1 
ATOM   2963 C CD1   . LEU B 1 38  ? 29.551 4.004   43.970  1.00 17.17 ? 29  LEU B CD1   1 
ATOM   2964 C CD2   . LEU B 1 38  ? 30.884 1.963   43.345  1.00 17.97 ? 29  LEU B CD2   1 
ATOM   2965 N N     . ALA B 1 39  ? 27.649 3.058   47.113  1.00 14.60 ? 30  ALA B N     1 
ATOM   2966 C CA    . ALA B 1 39  ? 26.380 2.348   47.170  1.00 15.47 ? 30  ALA B CA    1 
ATOM   2967 C C     . ALA B 1 39  ? 26.131 1.601   45.853  1.00 18.21 ? 30  ALA B C     1 
ATOM   2968 O O     . ALA B 1 39  ? 26.602 2.022   44.775  1.00 16.33 ? 30  ALA B O     1 
ATOM   2969 C CB    . ALA B 1 39  ? 25.219 3.318   47.445  1.00 15.61 ? 30  ALA B CB    1 
ATOM   2970 N N     . PRO B 1 40  ? 25.416 0.480   45.918  1.00 16.85 ? 31  PRO B N     1 
ATOM   2971 C CA    . PRO B 1 40  ? 25.063 -0.256  44.700  1.00 15.55 ? 31  PRO B CA    1 
ATOM   2972 C C     . PRO B 1 40  ? 24.155 0.574   43.816  1.00 13.53 ? 31  PRO B C     1 
ATOM   2973 O O     . PRO B 1 40  ? 23.139 1.088   44.270  1.00 16.38 ? 31  PRO B O     1 
ATOM   2974 C CB    . PRO B 1 40  ? 24.319 -1.482  45.242  1.00 17.03 ? 31  PRO B CB    1 
ATOM   2975 C CG    . PRO B 1 40  ? 23.718 -1.006  46.547  1.00 13.13 ? 31  PRO B CG    1 
ATOM   2976 C CD    . PRO B 1 40  ? 24.825 -0.134  47.114  1.00 15.27 ? 31  PRO B CD    1 
ATOM   2977 N N     . MET B 1 41  ? 24.512 0.677   42.528  1.00 15.86 ? 32  MET B N     1 
ATOM   2978 C CA    . MET B 1 41  ? 23.650 1.389   41.577  1.00 12.48 ? 32  MET B CA    1 
ATOM   2979 C C     . MET B 1 41  ? 23.635 0.754   40.191  1.00 12.17 ? 32  MET B C     1 
ATOM   2980 O O     . MET B 1 41  ? 24.666 0.665   39.544  1.00 15.20 ? 32  MET B O     1 
ATOM   2981 C CB    . MET B 1 41  ? 23.912 2.894   41.417  1.00 16.10 ? 32  MET B CB    1 
ATOM   2982 C CG    . MET B 1 41  ? 23.857 3.726   42.731  1.00 16.63 ? 32  MET B CG    1 
ATOM   2983 S SD    . MET B 1 41  ? 24.624 5.345   42.526  1.00 18.43 ? 32  MET B SD    1 
ATOM   2984 C CE    . MET B 1 41  ? 26.378 5.053   42.545  1.00 15.33 ? 32  MET B CE    1 
ATOM   2985 N N     . THR B 1 42  ? 22.453 0.304   39.812  1.00 14.57 ? 33  THR B N     1 
ATOM   2986 C CA    . THR B 1 42  ? 22.130 -0.121  38.453  1.00 12.78 ? 33  THR B CA    1 
ATOM   2987 C C     . THR B 1 42  ? 22.412 1.021   37.469  1.00 15.51 ? 33  THR B C     1 
ATOM   2988 O O     . THR B 1 42  ? 21.892 2.138   37.641  1.00 15.76 ? 33  THR B O     1 
ATOM   2989 C CB    . THR B 1 42  ? 20.647 -0.503  38.394  1.00 15.94 ? 33  THR B CB    1 
ATOM   2990 O OG1   . THR B 1 42  ? 20.352 -1.588  39.269  1.00 16.72 ? 33  THR B OG1   1 
ATOM   2991 C CG2   . THR B 1 42  ? 20.229 -0.894  36.979  1.00 15.12 ? 33  THR B CG2   1 
ATOM   2992 N N     . ARG B 1 43  ? 23.218 0.741   36.439  1.00 16.31 ? 34  ARG B N     1 
ATOM   2993 C CA    . ARG B 1 43  ? 23.550 1.744   35.412  1.00 12.05 ? 34  ARG B CA    1 
ATOM   2994 C C     . ARG B 1 43  ? 23.279 1.281   33.996  1.00 17.91 ? 34  ARG B C     1 
ATOM   2995 O O     . ARG B 1 43  ? 23.232 2.134   33.090  1.00 17.37 ? 34  ARG B O     1 
ATOM   2996 C CB    . ARG B 1 43  ? 25.028 2.178   35.496  1.00 14.79 ? 34  ARG B CB    1 
ATOM   2997 C CG    . ARG B 1 43  ? 25.414 2.734   36.886  1.00 11.72 ? 34  ARG B CG    1 
ATOM   2998 C CD    . ARG B 1 43  ? 24.489 3.955   37.235  1.00 13.32 ? 34  ARG B CD    1 
ATOM   2999 N NE    . ARG B 1 43  ? 24.492 5.042   36.252  1.00 14.02 ? 34  ARG B NE    1 
ATOM   3000 C CZ    . ARG B 1 43  ? 25.541 5.816   36.023  1.00 17.61 ? 34  ARG B CZ    1 
ATOM   3001 N NH1   . ARG B 1 43  ? 26.665 5.654   36.690  1.00 15.99 ? 34  ARG B NH1   1 
ATOM   3002 N NH2   . ARG B 1 43  ? 25.478 6.737   35.052  1.00 17.50 ? 34  ARG B NH2   1 
ATOM   3003 N N     . CYS B 1 44  ? 23.111 -0.030  33.772  1.00 18.45 ? 35  CYS B N     1 
ATOM   3004 C CA    . CYS B 1 44  ? 22.565 -0.583  32.531  1.00 15.42 ? 35  CYS B CA    1 
ATOM   3005 C C     . CYS B 1 44  ? 23.561 -0.507  31.389  1.00 16.24 ? 35  CYS B C     1 
ATOM   3006 O O     . CYS B 1 44  ? 23.165 -0.353  30.226  1.00 18.15 ? 35  CYS B O     1 
ATOM   3007 C CB    . CYS B 1 44  ? 21.254 0.093   32.119  1.00 17.83 ? 35  CYS B CB    1 
ATOM   3008 S SG    . CYS B 1 44  ? 19.975 0.065   33.408  1.00 17.31 ? 35  CYS B SG    1 
ATOM   3009 N N     . ARG B 1 45  ? 24.845 -0.642  31.710  1.00 16.47 ? 36  ARG B N     1 
ATOM   3010 C CA    . ARG B 1 45  ? 25.878 -0.685  30.689  1.00 17.25 ? 36  ARG B CA    1 
ATOM   3011 C C     . ARG B 1 45  ? 26.346 -2.105  30.394  1.00 18.26 ? 36  ARG B C     1 
ATOM   3012 O O     . ARG B 1 45  ? 27.170 -2.306  29.503  1.00 17.65 ? 36  ARG B O     1 
ATOM   3013 C CB    . ARG B 1 45  ? 27.053 0.198   31.100  1.00 16.11 ? 36  ARG B CB    1 
ATOM   3014 C CG    . ARG B 1 45  ? 26.940 1.632   30.482  1.00 18.03 ? 36  ARG B CG    1 
ATOM   3015 C CD    . ARG B 1 45  ? 25.948 2.521   31.292  1.00 17.01 ? 36  ARG B CD    1 
ATOM   3016 N NE    . ARG B 1 45  ? 25.992 3.940   30.911  1.00 16.77 ? 36  ARG B NE    1 
ATOM   3017 C CZ    . ARG B 1 45  ? 25.245 4.894   31.468  1.00 21.43 ? 36  ARG B CZ    1 
ATOM   3018 N NH1   . ARG B 1 45  ? 24.333 4.613   32.390  1.00 15.79 ? 36  ARG B NH1   1 
ATOM   3019 N NH2   . ARG B 1 45  ? 25.413 6.167   31.088  1.00 19.80 ? 36  ARG B NH2   1 
ATOM   3020 N N     . ALA B 1 46  ? 25.845 -3.100  31.122  1.00 19.31 ? 37  ALA B N     1 
ATOM   3021 C CA    . ALA B 1 46  ? 26.289 -4.482  30.946  1.00 17.75 ? 37  ALA B CA    1 
ATOM   3022 C C     . ALA B 1 46  ? 25.444 -5.140  29.852  1.00 20.04 ? 37  ALA B C     1 
ATOM   3023 O O     . ALA B 1 46  ? 24.546 -5.935  30.107  1.00 18.82 ? 37  ALA B O     1 
ATOM   3024 C CB    . ALA B 1 46  ? 26.208 -5.235  32.277  1.00 17.48 ? 37  ALA B CB    1 
ATOM   3025 N N     . LEU B 1 47  ? 25.744 -4.759  28.599  1.00 18.59 ? 38  LEU B N     1 
ATOM   3026 C CA    . LEU B 1 47  ? 24.940 -5.187  27.455  1.00 22.68 ? 38  LEU B CA    1 
ATOM   3027 C C     . LEU B 1 47  ? 24.745 -6.697  27.412  1.00 19.05 ? 38  LEU B C     1 
ATOM   3028 O O     . LEU B 1 47  ? 25.698 -7.466  27.589  1.00 21.48 ? 38  LEU B O     1 
ATOM   3029 C CB    . LEU B 1 47  ? 25.603 -4.710  26.168  1.00 19.81 ? 38  LEU B CB    1 
ATOM   3030 C CG    . LEU B 1 47  ? 25.925 -3.219  26.155  1.00 17.35 ? 38  LEU B CG    1 
ATOM   3031 C CD1   . LEU B 1 47  ? 26.524 -2.765  24.785  1.00 23.54 ? 38  LEU B CD1   1 
ATOM   3032 C CD2   . LEU B 1 47  ? 24.675 -2.389  26.455  1.00 22.37 ? 38  LEU B CD2   1 
ATOM   3033 N N     . ASN B 1 48  ? 23.494 -7.114  27.139  1.00 19.48 ? 39  ASN B N     1 
ATOM   3034 C CA    . ASN B 1 48  ? 23.078 -8.526  27.079  1.00 19.45 ? 39  ASN B CA    1 
ATOM   3035 C C     . ASN B 1 48  ? 23.390 -9.286  28.361  1.00 21.56 ? 39  ASN B C     1 
ATOM   3036 O O     . ASN B 1 48  ? 23.613 -10.506 28.324  1.00 19.46 ? 39  ASN B O     1 
ATOM   3037 C CB    . ASN B 1 48  ? 23.726 -9.247  25.894  1.00 22.24 ? 39  ASN B CB    1 
ATOM   3038 C CG    . ASN B 1 48  ? 23.261 -8.699  24.583  1.00 27.91 ? 39  ASN B CG    1 
ATOM   3039 O OD1   . ASN B 1 48  ? 24.072 -8.490  23.701  1.00 32.68 ? 39  ASN B OD1   1 
ATOM   3040 N ND2   . ASN B 1 48  ? 21.941 -8.479  24.437  1.00 22.34 ? 39  ASN B ND2   1 
ATOM   3041 N N     . ASN B 1 49  ? 23.401 -8.560  29.493  1.00 17.98 ? 40  ASN B N     1 
ATOM   3042 C CA    . ASN B 1 49  ? 23.667 -9.075  30.833  1.00 19.73 ? 40  ASN B CA    1 
ATOM   3043 C C     . ASN B 1 49  ? 25.092 -9.557  31.011  1.00 17.26 ? 40  ASN B C     1 
ATOM   3044 O O     . ASN B 1 49  ? 25.384 -10.282 31.970  1.00 19.76 ? 40  ASN B O     1 
ATOM   3045 C CB    . ASN B 1 49  ? 22.686 -10.183 31.229  1.00 19.63 ? 40  ASN B CB    1 
ATOM   3046 C CG    . ASN B 1 49  ? 21.236 -9.792  30.997  1.00 22.72 ? 40  ASN B CG    1 
ATOM   3047 O OD1   . ASN B 1 49  ? 20.455 -10.556 30.391  1.00 26.83 ? 40  ASN B OD1   1 
ATOM   3048 N ND2   . ASN B 1 49  ? 20.848 -8.623  31.494  1.00 19.88 ? 40  ASN B ND2   1 
ATOM   3049 N N     . ILE B 1 50  ? 26.001 -9.171  30.121  1.00 18.87 ? 41  ILE B N     1 
ATOM   3050 C CA    . ILE B 1 50  ? 27.409 -9.534  30.240  1.00 19.37 ? 41  ILE B CA    1 
ATOM   3051 C C     . ILE B 1 50  ? 28.160 -8.309  30.735  1.00 21.98 ? 41  ILE B C     1 
ATOM   3052 O O     . ILE B 1 50  ? 28.064 -7.242  30.096  1.00 20.05 ? 41  ILE B O     1 
ATOM   3053 C CB    . ILE B 1 50  ? 27.987 -10.024 28.903  1.00 21.78 ? 41  ILE B CB    1 
ATOM   3054 C CG1   . ILE B 1 50  ? 27.085 -11.121 28.318  1.00 25.97 ? 41  ILE B CG1   1 
ATOM   3055 C CG2   . ILE B 1 50  ? 29.463 -10.434 29.062  1.00 22.31 ? 41  ILE B CG2   1 
ATOM   3056 C CD1   . ILE B 1 50  ? 27.006 -12.351 29.171  1.00 28.73 ? 41  ILE B CD1   1 
ATOM   3057 N N     . PRO B 1 51  ? 28.897 -8.404  31.850  1.00 21.71 ? 42  PRO B N     1 
ATOM   3058 C CA    . PRO B 1 51  ? 29.756 -7.295  32.278  1.00 21.66 ? 42  PRO B CA    1 
ATOM   3059 C C     . PRO B 1 51  ? 30.707 -6.875  31.168  1.00 23.69 ? 42  PRO B C     1 
ATOM   3060 O O     . PRO B 1 51  ? 31.303 -7.708  30.471  1.00 23.54 ? 42  PRO B O     1 
ATOM   3061 C CB    . PRO B 1 51  ? 30.514 -7.867  33.479  1.00 23.09 ? 42  PRO B CB    1 
ATOM   3062 C CG    . PRO B 1 51  ? 29.686 -9.029  33.955  1.00 18.28 ? 42  PRO B CG    1 
ATOM   3063 C CD    . PRO B 1 51  ? 28.941 -9.559  32.775  1.00 19.03 ? 42  PRO B CD    1 
ATOM   3064 N N     . GLN B 1 52  ? 30.828 -5.566  30.990  1.00 19.24 ? 43  GLN B N     1 
ATOM   3065 C CA    . GLN B 1 52  ? 31.597 -5.014  29.888  1.00 22.09 ? 43  GLN B CA    1 
ATOM   3066 C C     . GLN B 1 52  ? 32.836 -4.316  30.411  1.00 24.14 ? 43  GLN B C     1 
ATOM   3067 O O     . GLN B 1 52  ? 32.910 -3.941  31.583  1.00 24.47 ? 43  GLN B O     1 
ATOM   3068 C CB    . GLN B 1 52  ? 30.744 -4.023  29.087  1.00 22.43 ? 43  GLN B CB    1 
ATOM   3069 C CG    . GLN B 1 52  ? 29.468 -4.645  28.531  1.00 21.22 ? 43  GLN B CG    1 
ATOM   3070 C CD    . GLN B 1 52  ? 29.744 -5.542  27.346  1.00 28.14 ? 43  GLN B CD    1 
ATOM   3071 O OE1   . GLN B 1 52  ? 30.558 -5.204  26.501  1.00 31.21 ? 43  GLN B OE1   1 
ATOM   3072 N NE2   . GLN B 1 52  ? 29.092 -6.713  27.301  1.00 22.45 ? 43  GLN B NE2   1 
ATOM   3073 N N     . ALA B 1 53  ? 33.797 -4.092  29.507  1.00 24.04 ? 44  ALA B N     1 
ATOM   3074 C CA    . ALA B 1 53  ? 34.977 -3.322  29.883  1.00 23.08 ? 44  ALA B CA    1 
ATOM   3075 C C     . ALA B 1 53  ? 34.603 -1.962  30.473  1.00 22.15 ? 44  ALA B C     1 
ATOM   3076 O O     . ALA B 1 53  ? 35.328 -1.441  31.332  1.00 22.53 ? 44  ALA B O     1 
ATOM   3077 C CB    . ALA B 1 53  ? 35.890 -3.121  28.670  1.00 23.25 ? 44  ALA B CB    1 
ATOM   3078 N N     . ALA B 1 54  ? 33.494 -1.365  30.015  1.00 22.36 ? 45  ALA B N     1 
ATOM   3079 C CA    . ALA B 1 54  ? 33.109 -0.054  30.540  1.00 20.99 ? 45  ALA B CA    1 
ATOM   3080 C C     . ALA B 1 54  ? 32.882 -0.127  32.041  1.00 20.08 ? 45  ALA B C     1 
ATOM   3081 O O     . ALA B 1 54  ? 33.249 0.796   32.774  1.00 19.86 ? 45  ALA B O     1 
ATOM   3082 C CB    . ALA B 1 54  ? 31.864 0.471   29.818  1.00 22.56 ? 45  ALA B CB    1 
ATOM   3083 N N     . LEU B 1 55  ? 32.303 -1.231  32.532  1.00 23.68 ? 46  LEU B N     1 
ATOM   3084 C CA    . LEU B 1 55  ? 32.142 -1.398  33.983  1.00 21.76 ? 46  LEU B CA    1 
ATOM   3085 C C     . LEU B 1 55  ? 33.493 -1.375  34.686  1.00 18.06 ? 46  LEU B C     1 
ATOM   3086 O O     . LEU B 1 55  ? 33.629 -0.814  35.780  1.00 19.82 ? 46  LEU B O     1 
ATOM   3087 C CB    . LEU B 1 55  ? 31.423 -2.716  34.301  1.00 17.47 ? 46  LEU B CB    1 
ATOM   3088 C CG    . LEU B 1 55  ? 29.905 -2.713  34.283  1.00 17.89 ? 46  LEU B CG    1 
ATOM   3089 C CD1   . LEU B 1 55  ? 29.371 -2.554  32.830  1.00 20.12 ? 46  LEU B CD1   1 
ATOM   3090 C CD2   . LEU B 1 55  ? 29.319 -4.000  34.893  1.00 19.58 ? 46  LEU B CD2   1 
ATOM   3091 N N     . GLY B 1 56  ? 34.495 -2.028  34.091  1.00 18.62 ? 47  GLY B N     1 
ATOM   3092 C CA    . GLY B 1 56  ? 35.824 -2.007  34.673  1.00 20.07 ? 47  GLY B CA    1 
ATOM   3093 C C     . GLY B 1 56  ? 36.350 -0.586  34.829  1.00 20.66 ? 47  GLY B C     1 
ATOM   3094 O O     . GLY B 1 56  ? 36.884 -0.222  35.878  1.00 19.09 ? 47  GLY B O     1 
ATOM   3095 N N     . GLU B 1 57  ? 36.187 0.238   33.782  1.00 16.42 ? 48  GLU B N     1 
ATOM   3096 C CA    . GLU B 1 57  ? 36.689 1.614   33.843  1.00 19.95 ? 48  GLU B CA    1 
ATOM   3097 C C     . GLU B 1 57  ? 35.955 2.407   34.907  1.00 17.99 ? 48  GLU B C     1 
ATOM   3098 O O     . GLU B 1 57  ? 36.551 3.235   35.603  1.00 20.27 ? 48  GLU B O     1 
ATOM   3099 C CB    . GLU B 1 57  ? 36.545 2.302   32.480  1.00 22.08 ? 48  GLU B CB    1 
ATOM   3100 N N     . TYR B 1 58  ? 34.647 2.191   35.009  1.00 17.19 ? 49  TYR B N     1 
ATOM   3101 C CA    . TYR B 1 58  ? 33.807 2.892   35.978  1.00 16.63 ? 49  TYR B CA    1 
ATOM   3102 C C     . TYR B 1 58  ? 34.196 2.548   37.416  1.00 17.89 ? 49  TYR B C     1 
ATOM   3103 O O     . TYR B 1 58  ? 34.417 3.440   38.241  1.00 14.92 ? 49  TYR B O     1 
ATOM   3104 C CB    . TYR B 1 58  ? 32.367 2.501   35.707  1.00 17.83 ? 49  TYR B CB    1 
ATOM   3105 C CG    . TYR B 1 58  ? 31.293 2.951   36.697  1.00 17.78 ? 49  TYR B CG    1 
ATOM   3106 C CD1   . TYR B 1 58  ? 30.744 4.239   36.640  1.00 19.53 ? 49  TYR B CD1   1 
ATOM   3107 C CD2   . TYR B 1 58  ? 30.767 2.054   37.624  1.00 20.64 ? 49  TYR B CD2   1 
ATOM   3108 C CE1   . TYR B 1 58  ? 29.726 4.612   37.496  1.00 16.33 ? 49  TYR B CE1   1 
ATOM   3109 C CE2   . TYR B 1 58  ? 29.731 2.429   38.514  1.00 16.04 ? 49  TYR B CE2   1 
ATOM   3110 C CZ    . TYR B 1 58  ? 29.219 3.713   38.423  1.00 16.91 ? 49  TYR B CZ    1 
ATOM   3111 O OH    . TYR B 1 58  ? 28.158 4.110   39.224  1.00 17.47 ? 49  TYR B OH    1 
ATOM   3112 N N     . TYR B 1 59  ? 34.316 1.251   37.731  1.00 16.84 ? 50  TYR B N     1 
ATOM   3113 C CA    . TYR B 1 59  ? 34.662 0.902   39.109  1.00 17.98 ? 50  TYR B CA    1 
ATOM   3114 C C     . TYR B 1 59  ? 36.104 1.283   39.442  1.00 18.75 ? 50  TYR B C     1 
ATOM   3115 O O     . TYR B 1 59  ? 36.393 1.689   40.568  1.00 19.97 ? 50  TYR B O     1 
ATOM   3116 C CB    . TYR B 1 59  ? 34.400 -0.585  39.367  1.00 18.93 ? 50  TYR B CB    1 
ATOM   3117 C CG    . TYR B 1 59  ? 32.925 -0.884  39.451  1.00 20.32 ? 50  TYR B CG    1 
ATOM   3118 C CD1   . TYR B 1 59  ? 32.125 -0.326  40.475  1.00 18.90 ? 50  TYR B CD1   1 
ATOM   3119 C CD2   . TYR B 1 59  ? 32.308 -1.690  38.512  1.00 20.07 ? 50  TYR B CD2   1 
ATOM   3120 C CE1   . TYR B 1 59  ? 30.759 -0.593  40.534  1.00 15.78 ? 50  TYR B CE1   1 
ATOM   3121 C CE2   . TYR B 1 59  ? 30.947 -1.954  38.578  1.00 19.80 ? 50  TYR B CE2   1 
ATOM   3122 C CZ    . TYR B 1 59  ? 30.184 -1.405  39.559  1.00 16.23 ? 50  TYR B CZ    1 
ATOM   3123 O OH    . TYR B 1 59  ? 28.842 -1.712  39.546  1.00 17.06 ? 50  TYR B OH    1 
ATOM   3124 N N     . GLU B 1 60  ? 37.031 1.091   38.508  1.00 18.32 ? 51  GLU B N     1 
ATOM   3125 C CA    . GLU B 1 60  ? 38.410 1.531   38.721  1.00 19.48 ? 51  GLU B CA    1 
ATOM   3126 C C     . GLU B 1 60  ? 38.475 3.029   39.023  1.00 20.73 ? 51  GLU B C     1 
ATOM   3127 O O     . GLU B 1 60  ? 39.242 3.462   39.893  1.00 19.59 ? 51  GLU B O     1 
ATOM   3128 C CB    . GLU B 1 60  ? 39.268 1.208   37.500  1.00 23.85 ? 51  GLU B CB    1 
ATOM   3129 C CG    . GLU B 1 60  ? 40.755 1.539   37.671  1.00 26.95 ? 51  GLU B CG    1 
ATOM   3130 C CD    . GLU B 1 60  ? 41.565 1.305   36.381  1.00 35.46 ? 51  GLU B CD    1 
ATOM   3131 O OE1   . GLU B 1 60  ? 41.044 1.591   35.273  1.00 37.08 ? 51  GLU B OE1   1 
ATOM   3132 O OE2   . GLU B 1 60  ? 42.705 0.785   36.477  1.00 35.03 ? 51  GLU B OE2   1 
ATOM   3133 N N     . GLN B 1 61  ? 37.670 3.835   38.317  1.00 21.47 ? 52  GLN B N     1 
ATOM   3134 C CA    . GLN B 1 61  ? 37.641 5.275   38.598  1.00 20.64 ? 52  GLN B CA    1 
ATOM   3135 C C     . GLN B 1 61  ? 37.340 5.542   40.067  1.00 22.59 ? 52  GLN B C     1 
ATOM   3136 O O     . GLN B 1 61  ? 37.908 6.450   40.674  1.00 21.72 ? 52  GLN B O     1 
ATOM   3137 C CB    . GLN B 1 61  ? 36.596 5.965   37.734  1.00 19.65 ? 52  GLN B CB    1 
ATOM   3138 C CG    . GLN B 1 61  ? 37.090 6.248   36.325  1.00 22.32 ? 52  GLN B CG    1 
ATOM   3139 C CD    . GLN B 1 61  ? 36.108 7.064   35.510  1.00 24.13 ? 52  GLN B CD    1 
ATOM   3140 O OE1   . GLN B 1 61  ? 34.926 7.174   35.853  1.00 21.88 ? 52  GLN B OE1   1 
ATOM   3141 N NE2   . GLN B 1 61  ? 36.586 7.618   34.401  1.00 24.19 ? 52  GLN B NE2   1 
ATOM   3142 N N     . ARG B 1 62  ? 36.434 4.771   40.639  1.00 19.08 ? 53  ARG B N     1 
ATOM   3143 C CA    . ARG B 1 62  ? 35.915 5.073   41.964  1.00 18.38 ? 53  ARG B CA    1 
ATOM   3144 C C     . ARG B 1 62  ? 36.627 4.313   43.063  1.00 20.63 ? 53  ARG B C     1 
ATOM   3145 O O     . ARG B 1 62  ? 36.454 4.656   44.237  1.00 20.93 ? 53  ARG B O     1 
ATOM   3146 C CB    . ARG B 1 62  ? 34.409 4.772   41.993  1.00 20.68 ? 53  ARG B CB    1 
ATOM   3147 C CG    . ARG B 1 62  ? 33.625 5.797   41.171  1.00 16.24 ? 53  ARG B CG    1 
ATOM   3148 C CD    . ARG B 1 62  ? 32.354 5.267   40.513  1.00 17.50 ? 53  ARG B CD    1 
ATOM   3149 N NE    . ARG B 1 62  ? 31.779 6.399   39.796  1.00 21.82 ? 53  ARG B NE    1 
ATOM   3150 C CZ    . ARG B 1 62  ? 32.238 6.845   38.636  1.00 21.51 ? 53  ARG B CZ    1 
ATOM   3151 N NH1   . ARG B 1 62  ? 33.123 6.156   37.938  1.00 21.56 ? 53  ARG B NH1   1 
ATOM   3152 N NH2   . ARG B 1 62  ? 31.826 8.028   38.180  1.00 20.02 ? 53  ARG B NH2   1 
ATOM   3153 N N     . ALA B 1 63  ? 37.434 3.315   42.694  1.00 21.28 ? 54  ALA B N     1 
ATOM   3154 C CA    . ALA B 1 63  ? 38.205 2.523   43.640  1.00 20.66 ? 54  ALA B CA    1 
ATOM   3155 C C     . ALA B 1 63  ? 39.286 3.354   44.328  1.00 19.95 ? 54  ALA B C     1 
ATOM   3156 O O     . ALA B 1 63  ? 39.987 4.156   43.710  1.00 23.70 ? 54  ALA B O     1 
ATOM   3157 C CB    . ALA B 1 63  ? 38.845 1.340   42.909  1.00 23.63 ? 54  ALA B CB    1 
ATOM   3158 N N     . THR B 1 64  ? 39.431 3.145   45.620  1.00 18.28 ? 55  THR B N     1 
ATOM   3159 C CA    . THR B 1 64  ? 40.493 3.754   46.394  1.00 21.05 ? 55  THR B CA    1 
ATOM   3160 C C     . THR B 1 64  ? 41.124 2.664   47.242  1.00 22.06 ? 55  THR B C     1 
ATOM   3161 O O     . THR B 1 64  ? 40.508 1.621   47.496  1.00 20.41 ? 55  THR B O     1 
ATOM   3162 C CB    . THR B 1 64  ? 39.992 4.875   47.340  1.00 20.50 ? 55  THR B CB    1 
ATOM   3163 O OG1   . THR B 1 64  ? 38.991 4.342   48.242  1.00 20.37 ? 55  THR B OG1   1 
ATOM   3164 C CG2   . THR B 1 64  ? 39.421 6.060   46.584  1.00 22.30 ? 55  THR B CG2   1 
ATOM   3165 N N     . ALA B 1 65  ? 42.337 2.951   47.720  1.00 21.47 ? 56  ALA B N     1 
ATOM   3166 C CA    . ALA B 1 65  ? 43.087 2.012   48.541  1.00 24.20 ? 56  ALA B CA    1 
ATOM   3167 C C     . ALA B 1 65  ? 42.398 1.832   49.884  1.00 20.03 ? 56  ALA B C     1 
ATOM   3168 O O     . ALA B 1 65  ? 42.274 2.784   50.656  1.00 26.56 ? 56  ALA B O     1 
ATOM   3169 C CB    . ALA B 1 65  ? 44.511 2.526   48.735  1.00 25.10 ? 56  ALA B CB    1 
ATOM   3170 N N     . GLY B 1 66  ? 41.925 0.625   50.157  1.00 21.00 ? 57  GLY B N     1 
ATOM   3171 C CA    . GLY B 1 66  ? 41.247 0.398   51.409  1.00 24.56 ? 57  GLY B CA    1 
ATOM   3172 C C     . GLY B 1 66  ? 39.813 0.866   51.426  1.00 22.12 ? 57  GLY B C     1 
ATOM   3173 O O     . GLY B 1 66  ? 39.202 0.914   52.497  1.00 22.43 ? 57  GLY B O     1 
ATOM   3174 N N     . GLY B 1 67  ? 39.264 1.206   50.268  1.00 19.37 ? 58  GLY B N     1 
ATOM   3175 C CA    . GLY B 1 67  ? 37.883 1.614   50.154  1.00 18.24 ? 58  GLY B CA    1 
ATOM   3176 C C     . GLY B 1 67  ? 36.990 0.470   49.702  1.00 18.27 ? 58  GLY B C     1 
ATOM   3177 O O     . GLY B 1 67  ? 37.406 -0.417  48.963  1.00 18.42 ? 58  GLY B O     1 
ATOM   3178 N N     . PHE B 1 68  ? 35.742 0.517   50.153  1.00 17.34 ? 59  PHE B N     1 
ATOM   3179 C CA    . PHE B 1 68  ? 34.771 -0.541  49.921  1.00 18.55 ? 59  PHE B CA    1 
ATOM   3180 C C     . PHE B 1 68  ? 33.815 -0.133  48.799  1.00 17.71 ? 59  PHE B C     1 
ATOM   3181 O O     . PHE B 1 68  ? 33.226 0.954   48.846  1.00 15.49 ? 59  PHE B O     1 
ATOM   3182 C CB    . PHE B 1 68  ? 34.003 -0.818  51.211  1.00 14.92 ? 59  PHE B CB    1 
ATOM   3183 C CG    . PHE B 1 68  ? 32.997 -1.938  51.094  1.00 15.76 ? 59  PHE B CG    1 
ATOM   3184 C CD1   . PHE B 1 68  ? 33.236 -3.025  50.264  1.00 18.30 ? 59  PHE B CD1   1 
ATOM   3185 C CD2   . PHE B 1 68  ? 31.795 -1.889  51.786  1.00 16.86 ? 59  PHE B CD2   1 
ATOM   3186 C CE1   . PHE B 1 68  ? 32.284 -4.033  50.144  1.00 15.92 ? 59  PHE B CE1   1 
ATOM   3187 C CE2   . PHE B 1 68  ? 30.846 -2.898  51.671  1.00 15.05 ? 59  PHE B CE2   1 
ATOM   3188 C CZ    . PHE B 1 68  ? 31.090 -3.975  50.847  1.00 14.63 ? 59  PHE B CZ    1 
ATOM   3189 N N     . LEU B 1 69  ? 33.675 -1.000  47.790  1.00 16.98 ? 60  LEU B N     1 
ATOM   3190 C CA    . LEU B 1 69  ? 32.700 -0.810  46.722  1.00 17.12 ? 60  LEU B CA    1 
ATOM   3191 C C     . LEU B 1 69  ? 31.660 -1.923  46.728  1.00 17.61 ? 60  LEU B C     1 
ATOM   3192 O O     . LEU B 1 69  ? 32.007 -3.099  46.889  1.00 16.55 ? 60  LEU B O     1 
ATOM   3193 C CB    . LEU B 1 69  ? 33.390 -0.811  45.366  1.00 17.76 ? 60  LEU B CB    1 
ATOM   3194 C CG    . LEU B 1 69  ? 34.630 0.066   45.209  1.00 22.37 ? 60  LEU B CG    1 
ATOM   3195 C CD1   . LEU B 1 69  ? 35.191 -0.104  43.795  1.00 24.03 ? 60  LEU B CD1   1 
ATOM   3196 C CD2   . LEU B 1 69  ? 34.272 1.507   45.500  1.00 22.85 ? 60  LEU B CD2   1 
ATOM   3197 N N     . ILE B 1 70  ? 30.395 -1.562  46.474  1.00 14.78 ? 61  ILE B N     1 
ATOM   3198 C CA    . ILE B 1 70  ? 29.331 -2.529  46.232  1.00 14.12 ? 61  ILE B CA    1 
ATOM   3199 C C     . ILE B 1 70  ? 28.860 -2.343  44.790  1.00 16.21 ? 61  ILE B C     1 
ATOM   3200 O O     . ILE B 1 70  ? 28.600 -1.202  44.365  1.00 15.80 ? 61  ILE B O     1 
ATOM   3201 C CB    . ILE B 1 70  ? 28.161 -2.326  47.215  1.00 14.05 ? 61  ILE B CB    1 
ATOM   3202 C CG1   . ILE B 1 70  ? 28.643 -2.319  48.689  1.00 18.89 ? 61  ILE B CG1   1 
ATOM   3203 C CG2   . ILE B 1 70  ? 27.087 -3.428  47.011  1.00 14.89 ? 61  ILE B CG2   1 
ATOM   3204 C CD1   . ILE B 1 70  ? 27.588 -1.800  49.665  1.00 11.87 ? 61  ILE B CD1   1 
ATOM   3205 N N     . THR B 1 71  ? 28.764 -3.443  44.036  1.00 14.45 ? 62  THR B N     1 
ATOM   3206 C CA    . THR B 1 71  ? 28.392 -3.320  42.626  1.00 13.73 ? 62  THR B CA    1 
ATOM   3207 C C     . THR B 1 71  ? 26.914 -3.018  42.466  1.00 14.55 ? 62  THR B C     1 
ATOM   3208 O O     . THR B 1 71  ? 26.093 -3.243  43.357  1.00 15.51 ? 62  THR B O     1 
ATOM   3209 C CB    . THR B 1 71  ? 28.642 -4.612  41.811  1.00 17.38 ? 62  THR B CB    1 
ATOM   3210 O OG1   . THR B 1 71  ? 27.721 -5.645  42.203  1.00 16.31 ? 62  THR B OG1   1 
ATOM   3211 C CG2   . THR B 1 71  ? 30.076 -5.100  41.915  1.00 16.76 ? 62  THR B CG2   1 
ATOM   3212 N N     . GLU B 1 72  ? 26.568 -2.590  41.257  1.00 15.75 ? 63  GLU B N     1 
ATOM   3213 C CA    . GLU B 1 72  ? 25.184 -2.607  40.804  1.00 13.96 ? 63  GLU B CA    1 
ATOM   3214 C C     . GLU B 1 72  ? 24.547 -3.962  41.108  1.00 16.08 ? 63  GLU B C     1 
ATOM   3215 O O     . GLU B 1 72  ? 25.234 -4.987  41.147  1.00 16.86 ? 63  GLU B O     1 
ATOM   3216 C CB    . GLU B 1 72  ? 25.140 -2.351  39.292  1.00 16.84 ? 63  GLU B CB    1 
ATOM   3217 C CG    . GLU B 1 72  ? 25.864 -3.429  38.464  1.00 20.06 ? 63  GLU B CG    1 
ATOM   3218 C CD    . GLU B 1 72  ? 26.582 -2.846  37.254  1.00 23.16 ? 63  GLU B CD    1 
ATOM   3219 O OE1   . GLU B 1 72  ? 27.730 -2.387  37.385  1.00 22.32 ? 63  GLU B OE1   1 
ATOM   3220 O OE2   . GLU B 1 72  ? 25.961 -2.790  36.169  1.00 22.59 ? 63  GLU B OE2   1 
ATOM   3221 N N     . GLY B 1 73  ? 23.222 -3.962  41.306  1.00 14.05 ? 64  GLY B N     1 
ATOM   3222 C CA    . GLY B 1 73  ? 22.457 -5.190  41.424  1.00 11.32 ? 64  GLY B CA    1 
ATOM   3223 C C     . GLY B 1 73  ? 22.758 -6.117  40.252  1.00 15.46 ? 64  GLY B C     1 
ATOM   3224 O O     . GLY B 1 73  ? 22.851 -5.670  39.105  1.00 14.81 ? 64  GLY B O     1 
ATOM   3225 N N     . THR B 1 74  ? 22.933 -7.410  40.546  1.00 14.23 ? 65  THR B N     1 
ATOM   3226 C CA    . THR B 1 74  ? 23.394 -8.389  39.581  1.00 15.69 ? 65  THR B CA    1 
ATOM   3227 C C     . THR B 1 74  ? 22.454 -9.594  39.597  1.00 16.11 ? 65  THR B C     1 
ATOM   3228 O O     . THR B 1 74  ? 22.077 -10.097 40.660  1.00 16.18 ? 65  THR B O     1 
ATOM   3229 C CB    . THR B 1 74  ? 24.839 -8.768  39.904  1.00 16.36 ? 65  THR B CB    1 
ATOM   3230 O OG1   . THR B 1 74  ? 25.677 -7.604  39.784  1.00 17.76 ? 65  THR B OG1   1 
ATOM   3231 C CG2   . THR B 1 74  ? 25.368 -9.910  39.046  1.00 16.32 ? 65  THR B CG2   1 
ATOM   3232 N N     . MET B 1 75  ? 22.065 -10.027 38.406  1.00 16.34 ? 66  MET B N     1 
ATOM   3233 C CA    . MET B 1 75  ? 21.086 -11.096 38.217  1.00 16.15 ? 66  MET B CA    1 
ATOM   3234 C C     . MET B 1 75  ? 21.551 -12.413 38.831  1.00 17.01 ? 66  MET B C     1 
ATOM   3235 O O     . MET B 1 75  ? 22.704 -12.823 38.651  1.00 16.51 ? 66  MET B O     1 
ATOM   3236 C CB    . MET B 1 75  ? 20.899 -11.310 36.710  1.00 15.82 ? 66  MET B CB    1 
ATOM   3237 C CG    . MET B 1 75  ? 20.260 -10.130 36.039  1.00 16.03 ? 66  MET B CG    1 
ATOM   3238 S SD    . MET B 1 75  ? 20.063 -10.413 34.244  1.00 20.05 ? 66  MET B SD    1 
ATOM   3239 C CE    . MET B 1 75  ? 18.883 -11.741 34.206  1.00 17.33 ? 66  MET B CE    1 
ATOM   3240 N N     . ILE B 1 76  ? 20.621 -13.109 39.491  1.00 18.04 ? 67  ILE B N     1 
ATOM   3241 C CA    . ILE B 1 76  ? 20.924 -14.440 40.022  1.00 16.67 ? 67  ILE B CA    1 
ATOM   3242 C C     . ILE B 1 76  ? 20.410 -15.548 39.122  1.00 19.47 ? 67  ILE B C     1 
ATOM   3243 O O     . ILE B 1 76  ? 20.702 -16.727 39.391  1.00 19.50 ? 67  ILE B O     1 
ATOM   3244 C CB    . ILE B 1 76  ? 20.355 -14.624 41.445  1.00 16.98 ? 67  ILE B CB    1 
ATOM   3245 C CG1   . ILE B 1 76  ? 18.803 -14.556 41.430  1.00 16.80 ? 67  ILE B CG1   1 
ATOM   3246 C CG2   . ILE B 1 76  ? 21.060 -13.634 42.381  1.00 15.88 ? 67  ILE B CG2   1 
ATOM   3247 C CD1   . ILE B 1 76  ? 18.123 -15.077 42.674  1.00 18.17 ? 67  ILE B CD1   1 
ATOM   3248 N N     . SER B 1 77  ? 19.661 -15.219 38.076  1.00 18.83 ? 68  SER B N     1 
ATOM   3249 C CA    . SER B 1 77  ? 19.024 -16.210 37.224  1.00 19.79 ? 68  SER B CA    1 
ATOM   3250 C C     . SER B 1 77  ? 18.456 -15.513 35.999  1.00 22.36 ? 68  SER B C     1 
ATOM   3251 O O     . SER B 1 77  ? 18.231 -14.301 36.021  1.00 19.19 ? 68  SER B O     1 
ATOM   3252 C CB    . SER B 1 77  ? 17.894 -16.935 37.954  1.00 20.08 ? 68  SER B CB    1 
ATOM   3253 O OG    . SER B 1 77  ? 16.762 -16.085 38.001  1.00 18.40 ? 68  SER B OG    1 
ATOM   3254 N N     . PRO B 1 78  ? 18.137 -16.279 34.957  1.00 18.92 ? 69  PRO B N     1 
ATOM   3255 C CA    . PRO B 1 78  ? 17.488 -15.676 33.778  1.00 19.73 ? 69  PRO B CA    1 
ATOM   3256 C C     . PRO B 1 78  ? 16.159 -14.994 34.054  1.00 19.14 ? 69  PRO B C     1 
ATOM   3257 O O     . PRO B 1 78  ? 15.765 -14.154 33.243  1.00 16.33 ? 69  PRO B O     1 
ATOM   3258 C CB    . PRO B 1 78  ? 17.306 -16.875 32.830  1.00 18.91 ? 69  PRO B CB    1 
ATOM   3259 C CG    . PRO B 1 78  ? 18.444 -17.762 33.149  1.00 22.18 ? 69  PRO B CG    1 
ATOM   3260 C CD    . PRO B 1 78  ? 18.553 -17.669 34.706  1.00 21.51 ? 69  PRO B CD    1 
ATOM   3261 N N     . THR B 1 79  ? 15.457 -15.295 35.158  1.00 19.03 ? 70  THR B N     1 
ATOM   3262 C CA    . THR B 1 79  ? 14.147 -14.706 35.458  1.00 18.01 ? 70  THR B CA    1 
ATOM   3263 C C     . THR B 1 79  ? 14.205 -13.566 36.482  1.00 16.66 ? 70  THR B C     1 
ATOM   3264 O O     . THR B 1 79  ? 13.153 -13.065 36.932  1.00 19.64 ? 70  THR B O     1 
ATOM   3265 C CB    . THR B 1 79  ? 13.214 -15.793 35.955  1.00 23.88 ? 70  THR B CB    1 
ATOM   3266 O OG1   . THR B 1 79  ? 13.915 -16.560 36.942  1.00 24.09 ? 70  THR B OG1   1 
ATOM   3267 C CG2   . THR B 1 79  ? 12.787 -16.708 34.747  1.00 28.53 ? 70  THR B CG2   1 
ATOM   3268 N N     . SER B 1 80  ? 15.389 -13.127 36.845  1.00 17.01 ? 71  SER B N     1 
ATOM   3269 C CA    . SER B 1 80  ? 15.544 -12.235 37.997  1.00 14.90 ? 71  SER B CA    1 
ATOM   3270 C C     . SER B 1 80  ? 15.643 -10.752 37.620  1.00 17.85 ? 71  SER B C     1 
ATOM   3271 O O     . SER B 1 80  ? 15.814 -9.914  38.511  1.00 16.84 ? 71  SER B O     1 
ATOM   3272 C CB    . SER B 1 80  ? 16.788 -12.645 38.775  1.00 17.80 ? 71  SER B CB    1 
ATOM   3273 O OG    . SER B 1 80  ? 17.915 -12.372 37.988  1.00 23.31 ? 71  SER B OG    1 
ATOM   3274 N N     . ALA B 1 81  ? 15.541 -10.404 36.334  1.00 17.80 ? 72  ALA B N     1 
ATOM   3275 C CA    . ALA B 1 81  ? 15.811 -9.048  35.883  1.00 14.18 ? 72  ALA B CA    1 
ATOM   3276 C C     . ALA B 1 81  ? 14.537 -8.275  35.540  1.00 15.23 ? 72  ALA B C     1 
ATOM   3277 O O     . ALA B 1 81  ? 13.528 -8.842  35.105  1.00 15.29 ? 72  ALA B O     1 
ATOM   3278 C CB    . ALA B 1 81  ? 16.757 -9.060  34.675  1.00 18.03 ? 72  ALA B CB    1 
ATOM   3279 N N     . GLY B 1 82  ? 14.604 -6.959  35.773  1.00 16.26 ? 73  GLY B N     1 
ATOM   3280 C CA    . GLY B 1 82  ? 13.569 -6.021  35.397  1.00 14.94 ? 73  GLY B CA    1 
ATOM   3281 C C     . GLY B 1 82  ? 14.111 -4.670  34.936  1.00 15.89 ? 73  GLY B C     1 
ATOM   3282 O O     . GLY B 1 82  ? 13.391 -3.669  35.001  1.00 17.85 ? 73  GLY B O     1 
ATOM   3283 N N     . PHE B 1 83  ? 15.392 -4.606  34.580  1.00 16.87 ? 74  PHE B N     1 
ATOM   3284 C CA    . PHE B 1 83  ? 16.018 -3.449  33.951  1.00 15.45 ? 74  PHE B CA    1 
ATOM   3285 C C     . PHE B 1 83  ? 16.749 -3.958  32.728  1.00 16.32 ? 74  PHE B C     1 
ATOM   3286 O O     . PHE B 1 83  ? 17.077 -5.146  32.645  1.00 18.80 ? 74  PHE B O     1 
ATOM   3287 C CB    . PHE B 1 83  ? 17.023 -2.740  34.876  1.00 18.09 ? 74  PHE B CB    1 
ATOM   3288 C CG    . PHE B 1 83  ? 16.400 -1.718  35.804  1.00 15.43 ? 74  PHE B CG    1 
ATOM   3289 C CD1   . PHE B 1 83  ? 15.612 -2.113  36.884  1.00 20.20 ? 74  PHE B CD1   1 
ATOM   3290 C CD2   . PHE B 1 83  ? 16.582 -0.356  35.584  1.00 18.45 ? 74  PHE B CD2   1 
ATOM   3291 C CE1   . PHE B 1 83  ? 15.020 -1.164  37.724  1.00 19.64 ? 74  PHE B CE1   1 
ATOM   3292 C CE2   . PHE B 1 83  ? 15.986 0.587   36.428  1.00 18.78 ? 74  PHE B CE2   1 
ATOM   3293 C CZ    . PHE B 1 83  ? 15.206 0.177   37.484  1.00 18.99 ? 74  PHE B CZ    1 
ATOM   3294 N N     . PRO B 1 84  ? 17.046 -3.090  31.777  1.00 14.63 ? 75  PRO B N     1 
ATOM   3295 C CA    . PRO B 1 84  ? 17.768 -3.535  30.585  1.00 16.06 ? 75  PRO B CA    1 
ATOM   3296 C C     . PRO B 1 84  ? 19.256 -3.558  30.883  1.00 14.15 ? 75  PRO B C     1 
ATOM   3297 O O     . PRO B 1 84  ? 19.766 -2.717  31.631  1.00 17.12 ? 75  PRO B O     1 
ATOM   3298 C CB    . PRO B 1 84  ? 17.418 -2.459  29.550  1.00 19.25 ? 75  PRO B CB    1 
ATOM   3299 C CG    . PRO B 1 84  ? 17.303 -1.181  30.431  1.00 16.58 ? 75  PRO B CG    1 
ATOM   3300 C CD    . PRO B 1 84  ? 16.674 -1.658  31.717  1.00 17.75 ? 75  PRO B CD    1 
ATOM   3301 N N     . HIS B 1 85  ? 19.940 -4.555  30.315  1.00 16.17 ? 76  HIS B N     1 
ATOM   3302 C CA    . HIS B 1 85  ? 21.403 -4.610  30.286  1.00 14.44 ? 76  HIS B CA    1 
ATOM   3303 C C     . HIS B 1 85  ? 22.010 -4.462  31.682  1.00 15.80 ? 76  HIS B C     1 
ATOM   3304 O O     . HIS B 1 85  ? 22.997 -3.760  31.870  1.00 16.04 ? 76  HIS B O     1 
ATOM   3305 C CB    . HIS B 1 85  ? 21.963 -3.551  29.337  1.00 20.02 ? 76  HIS B CB    1 
ATOM   3306 C CG    . HIS B 1 85  ? 21.379 -3.659  27.969  1.00 20.07 ? 76  HIS B CG    1 
ATOM   3307 N ND1   . HIS B 1 85  ? 21.563 -4.784  27.194  1.00 22.70 ? 76  HIS B ND1   1 
ATOM   3308 C CD2   . HIS B 1 85  ? 20.542 -2.850  27.279  1.00 23.75 ? 76  HIS B CD2   1 
ATOM   3309 C CE1   . HIS B 1 85  ? 20.878 -4.654  26.070  1.00 26.01 ? 76  HIS B CE1   1 
ATOM   3310 N NE2   . HIS B 1 85  ? 20.265 -3.482  26.088  1.00 28.22 ? 76  HIS B NE2   1 
ATOM   3311 N N     . VAL B 1 86  ? 21.438 -5.186  32.642  1.00 19.56 ? 77  VAL B N     1 
ATOM   3312 C CA    . VAL B 1 86  ? 22.025 -5.314  33.981  1.00 14.01 ? 77  VAL B CA    1 
ATOM   3313 C C     . VAL B 1 86  ? 22.868 -6.582  33.988  1.00 20.74 ? 77  VAL B C     1 
ATOM   3314 O O     . VAL B 1 86  ? 22.516 -7.564  33.307  1.00 18.98 ? 77  VAL B O     1 
ATOM   3315 C CB    . VAL B 1 86  ? 20.929 -5.338  35.059  1.00 19.35 ? 77  VAL B CB    1 
ATOM   3316 C CG1   . VAL B 1 86  ? 20.170 -4.026  35.038  1.00 18.83 ? 77  VAL B CG1   1 
ATOM   3317 C CG2   . VAL B 1 86  ? 19.987 -6.513  34.870  1.00 17.38 ? 77  VAL B CG2   1 
ATOM   3318 N N     . PRO B 1 87  ? 23.987 -6.624  34.708  1.00 17.59 ? 78  PRO B N     1 
ATOM   3319 C CA    . PRO B 1 87  ? 24.851 -7.804  34.603  1.00 20.62 ? 78  PRO B CA    1 
ATOM   3320 C C     . PRO B 1 87  ? 24.254 -8.953  35.386  1.00 18.64 ? 78  PRO B C     1 
ATOM   3321 O O     . PRO B 1 87  ? 23.499 -8.754  36.340  1.00 15.93 ? 78  PRO B O     1 
ATOM   3322 C CB    . PRO B 1 87  ? 26.180 -7.340  35.215  1.00 19.17 ? 78  PRO B CB    1 
ATOM   3323 C CG    . PRO B 1 87  ? 25.797 -6.239  36.184  1.00 19.15 ? 78  PRO B CG    1 
ATOM   3324 C CD    . PRO B 1 87  ? 24.591 -5.552  35.512  1.00 20.23 ? 78  PRO B CD    1 
ATOM   3325 N N     . GLY B 1 88  ? 24.573 -10.166 34.943  1.00 18.03 ? 79  GLY B N     1 
ATOM   3326 C CA    . GLY B 1 88  ? 24.307 -11.358 35.712  1.00 17.71 ? 79  GLY B CA    1 
ATOM   3327 C C     . GLY B 1 88  ? 25.593 -11.949 36.265  1.00 16.36 ? 79  GLY B C     1 
ATOM   3328 O O     . GLY B 1 88  ? 26.692 -11.502 35.972  1.00 20.96 ? 79  GLY B O     1 
ATOM   3329 N N     . ILE B 1 89  ? 25.426 -12.949 37.137  1.00 16.93 ? 80  ILE B N     1 
ATOM   3330 C CA    . ILE B 1 89  ? 26.562 -13.747 37.584  1.00 18.93 ? 80  ILE B CA    1 
ATOM   3331 C C     . ILE B 1 89  ? 26.096 -15.198 37.731  1.00 23.18 ? 80  ILE B C     1 
ATOM   3332 O O     . ILE B 1 89  ? 26.558 -15.934 38.609  1.00 23.86 ? 80  ILE B O     1 
ATOM   3333 C CB    . ILE B 1 89  ? 27.170 -13.162 38.884  1.00 20.74 ? 80  ILE B CB    1 
ATOM   3334 C CG1   . ILE B 1 89  ? 28.604 -13.679 39.108  1.00 22.64 ? 80  ILE B CG1   1 
ATOM   3335 C CG2   . ILE B 1 89  ? 26.259 -13.363 40.085  1.00 15.46 ? 80  ILE B CG2   1 
ATOM   3336 C CD1   . ILE B 1 89  ? 29.450 -12.792 39.920  1.00 22.63 ? 80  ILE B CD1   1 
ATOM   3337 N N     . PHE B 1 90  ? 25.188 -15.630 36.844  1.00 18.70 ? 81  PHE B N     1 
ATOM   3338 C CA    . PHE B 1 90  ? 24.687 -17.000 36.867  1.00 22.37 ? 81  PHE B CA    1 
ATOM   3339 C C     . PHE B 1 90  ? 25.246 -17.859 35.726  1.00 26.07 ? 81  PHE B C     1 
ATOM   3340 O O     . PHE B 1 90  ? 25.008 -19.072 35.714  1.00 27.13 ? 81  PHE B O     1 
ATOM   3341 C CB    . PHE B 1 90  ? 23.144 -17.015 36.862  1.00 17.62 ? 81  PHE B CB    1 
ATOM   3342 C CG    . PHE B 1 90  ? 22.511 -16.308 35.682  1.00 24.78 ? 81  PHE B CG    1 
ATOM   3343 C CD1   . PHE B 1 90  ? 22.234 -14.942 35.734  1.00 18.79 ? 81  PHE B CD1   1 
ATOM   3344 C CD2   . PHE B 1 90  ? 22.203 -16.998 34.517  1.00 23.72 ? 81  PHE B CD2   1 
ATOM   3345 C CE1   . PHE B 1 90  ? 21.654 -14.291 34.666  1.00 19.68 ? 81  PHE B CE1   1 
ATOM   3346 C CE2   . PHE B 1 90  ? 21.612 -16.347 33.433  1.00 24.29 ? 81  PHE B CE2   1 
ATOM   3347 C CZ    . PHE B 1 90  ? 21.343 -14.992 33.491  1.00 22.82 ? 81  PHE B CZ    1 
ATOM   3348 N N     . THR B 1 91  ? 26.031 -17.287 34.812  1.00 24.11 ? 82  THR B N     1 
ATOM   3349 C CA    . THR B 1 91  ? 26.713 -18.067 33.779  1.00 24.92 ? 82  THR B CA    1 
ATOM   3350 C C     . THR B 1 91  ? 28.224 -17.959 33.927  1.00 28.09 ? 82  THR B C     1 
ATOM   3351 O O     . THR B 1 91  ? 28.752 -16.979 34.465  1.00 24.38 ? 82  THR B O     1 
ATOM   3352 C CB    . THR B 1 91  ? 26.334 -17.610 32.360  1.00 23.69 ? 82  THR B CB    1 
ATOM   3353 O OG1   . THR B 1 91  ? 27.003 -16.376 32.057  1.00 24.38 ? 82  THR B OG1   1 
ATOM   3354 C CG2   . THR B 1 91  ? 24.847 -17.426 32.228  1.00 22.19 ? 82  THR B CG2   1 
ATOM   3355 N N     . LYS B 1 92  ? 28.924 -18.976 33.409  1.00 26.89 ? 83  LYS B N     1 
ATOM   3356 C CA    . LYS B 1 92  ? 30.384 -18.950 33.462  1.00 26.16 ? 83  LYS B CA    1 
ATOM   3357 C C     . LYS B 1 92  ? 30.947 -17.852 32.575  1.00 24.43 ? 83  LYS B C     1 
ATOM   3358 O O     . LYS B 1 92  ? 32.002 -17.292 32.889  1.00 25.30 ? 83  LYS B O     1 
ATOM   3359 C CB    . LYS B 1 92  ? 30.955 -20.315 33.086  1.00 32.58 ? 83  LYS B CB    1 
ATOM   3360 C CG    . LYS B 1 92  ? 30.629 -21.420 34.129  1.00 32.28 ? 83  LYS B CG    1 
ATOM   3361 C CD    . LYS B 1 92  ? 31.204 -21.108 35.537  1.00 34.09 ? 83  LYS B CD    1 
ATOM   3362 C CE    . LYS B 1 92  ? 30.290 -21.662 36.633  1.00 34.17 ? 83  LYS B CE    1 
ATOM   3363 N NZ    . LYS B 1 92  ? 30.981 -21.908 37.928  1.00 39.58 ? 83  LYS B NZ    1 
ATOM   3364 N N     . GLU B 1 93  ? 30.242 -17.512 31.491  1.00 21.34 ? 84  GLU B N     1 
ATOM   3365 C CA    . GLU B 1 93  ? 30.602 -16.353 30.678  1.00 25.26 ? 84  GLU B CA    1 
ATOM   3366 C C     . GLU B 1 93  ? 30.630 -15.086 31.538  1.00 24.40 ? 84  GLU B C     1 
ATOM   3367 O O     . GLU B 1 93  ? 31.600 -14.315 31.520  1.00 22.93 ? 84  GLU B O     1 
ATOM   3368 C CB    . GLU B 1 93  ? 29.589 -16.218 29.529  1.00 24.68 ? 84  GLU B CB    1 
ATOM   3369 C CG    . GLU B 1 93  ? 29.924 -15.092 28.554  1.00 28.88 ? 84  GLU B CG    1 
ATOM   3370 C CD    . GLU B 1 93  ? 28.870 -14.842 27.457  1.00 33.76 ? 84  GLU B CD    1 
ATOM   3371 O OE1   . GLU B 1 93  ? 27.697 -15.308 27.538  1.00 34.87 ? 84  GLU B OE1   1 
ATOM   3372 O OE2   . GLU B 1 93  ? 29.243 -14.151 26.492  1.00 37.19 ? 84  GLU B OE2   1 
ATOM   3373 N N     . GLN B 1 94  ? 29.586 -14.889 32.334  1.00 21.72 ? 85  GLN B N     1 
ATOM   3374 C CA    . GLN B 1 94  ? 29.514 -13.690 33.168  1.00 22.02 ? 85  GLN B CA    1 
ATOM   3375 C C     . GLN B 1 94  ? 30.621 -13.697 34.197  1.00 22.22 ? 85  GLN B C     1 
ATOM   3376 O O     . GLN B 1 94  ? 31.191 -12.648 34.511  1.00 21.79 ? 85  GLN B O     1 
ATOM   3377 C CB    . GLN B 1 94  ? 28.154 -13.596 33.853  1.00 20.95 ? 85  GLN B CB    1 
ATOM   3378 C CG    . GLN B 1 94  ? 27.047 -13.215 32.917  1.00 19.28 ? 85  GLN B CG    1 
ATOM   3379 C CD    . GLN B 1 94  ? 25.698 -13.759 33.326  1.00 22.44 ? 85  GLN B CD    1 
ATOM   3380 O OE1   . GLN B 1 94  ? 25.566 -14.501 34.318  1.00 23.00 ? 85  GLN B OE1   1 
ATOM   3381 N NE2   . GLN B 1 94  ? 24.662 -13.364 32.582  1.00 22.38 ? 85  GLN B NE2   1 
ATOM   3382 N N     . VAL B 1 95  ? 30.933 -14.883 34.741  1.00 22.87 ? 86  VAL B N     1 
ATOM   3383 C CA    . VAL B 1 95  ? 31.996 -14.996 35.728  1.00 17.49 ? 86  VAL B CA    1 
ATOM   3384 C C     . VAL B 1 95  ? 33.316 -14.561 35.128  1.00 21.58 ? 86  VAL B C     1 
ATOM   3385 O O     . VAL B 1 95  ? 34.083 -13.807 35.742  1.00 20.65 ? 86  VAL B O     1 
ATOM   3386 C CB    . VAL B 1 95  ? 32.077 -16.434 36.272  1.00 18.00 ? 86  VAL B CB    1 
ATOM   3387 C CG1   . VAL B 1 95  ? 33.290 -16.567 37.178  1.00 19.42 ? 86  VAL B CG1   1 
ATOM   3388 C CG2   . VAL B 1 95  ? 30.772 -16.825 37.036  1.00 25.11 ? 86  VAL B CG2   1 
ATOM   3389 N N     . ARG B 1 96  ? 33.606 -15.041 33.909  1.00 22.22 ? 87  ARG B N     1 
ATOM   3390 C CA    . ARG B 1 96  ? 34.857 -14.703 33.248  1.00 22.86 ? 87  ARG B CA    1 
ATOM   3391 C C     . ARG B 1 96  ? 34.997 -13.197 33.062  1.00 23.61 ? 87  ARG B C     1 
ATOM   3392 O O     . ARG B 1 96  ? 36.071 -12.636 33.292  1.00 23.78 ? 87  ARG B O     1 
ATOM   3393 C CB    . ARG B 1 96  ? 34.927 -15.400 31.887  1.00 27.36 ? 87  ARG B CB    1 
ATOM   3394 C CG    . ARG B 1 96  ? 35.010 -16.903 31.965  1.00 32.06 ? 87  ARG B CG    1 
ATOM   3395 C CD    . ARG B 1 96  ? 35.525 -17.453 30.642  1.00 35.09 ? 87  ARG B CD    1 
ATOM   3396 N NE    . ARG B 1 96  ? 34.502 -17.457 29.602  1.00 35.56 ? 87  ARG B NE    1 
ATOM   3397 C CZ    . ARG B 1 96  ? 33.548 -18.377 29.490  1.00 35.62 ? 87  ARG B CZ    1 
ATOM   3398 N NH1   . ARG B 1 96  ? 33.426 -19.358 30.368  1.00 36.96 ? 87  ARG B NH1   1 
ATOM   3399 N NH2   . ARG B 1 96  ? 32.707 -18.320 28.458  1.00 41.11 ? 87  ARG B NH2   1 
ATOM   3400 N N     . GLU B 1 97  ? 33.913 -12.519 32.676  1.00 23.13 ? 88  GLU B N     1 
ATOM   3401 C CA    . GLU B 1 97  ? 34.000 -11.079 32.466  1.00 22.85 ? 88  GLU B CA    1 
ATOM   3402 C C     . GLU B 1 97  ? 34.080 -10.309 33.783  1.00 22.67 ? 88  GLU B C     1 
ATOM   3403 O O     . GLU B 1 97  ? 34.789 -9.296  33.877  1.00 21.48 ? 88  GLU B O     1 
ATOM   3404 C CB    . GLU B 1 97  ? 32.819 -10.619 31.631  1.00 25.00 ? 88  GLU B CB    1 
ATOM   3405 C CG    . GLU B 1 97  ? 32.783 -11.328 30.274  1.00 25.98 ? 88  GLU B CG    1 
ATOM   3406 C CD    . GLU B 1 97  ? 34.107 -11.212 29.526  1.00 34.39 ? 88  GLU B CD    1 
ATOM   3407 O OE1   . GLU B 1 97  ? 34.702 -10.109 29.536  1.00 31.37 ? 88  GLU B OE1   1 
ATOM   3408 O OE2   . GLU B 1 97  ? 34.572 -12.235 28.947  1.00 35.90 ? 88  GLU B OE2   1 
ATOM   3409 N N     . TRP B 1 98  ? 33.346 -10.751 34.799  1.00 21.20 ? 89  TRP B N     1 
ATOM   3410 C CA    . TRP B 1 98  ? 33.436 -10.102 36.107  1.00 21.80 ? 89  TRP B CA    1 
ATOM   3411 C C     . TRP B 1 98  ? 34.843 -10.191 36.662  1.00 20.85 ? 89  TRP B C     1 
ATOM   3412 O O     . TRP B 1 98  ? 35.315 -9.268  37.335  1.00 20.21 ? 89  TRP B O     1 
ATOM   3413 C CB    . TRP B 1 98  ? 32.474 -10.764 37.081  1.00 17.57 ? 89  TRP B CB    1 
ATOM   3414 C CG    . TRP B 1 98  ? 31.098 -10.166 37.162  1.00 18.50 ? 89  TRP B CG    1 
ATOM   3415 C CD1   . TRP B 1 98  ? 29.924 -10.836 37.023  1.00 19.86 ? 89  TRP B CD1   1 
ATOM   3416 C CD2   . TRP B 1 98  ? 30.749 -8.808  37.481  1.00 16.52 ? 89  TRP B CD2   1 
ATOM   3417 N NE1   . TRP B 1 98  ? 28.864 -9.981  37.243  1.00 16.58 ? 89  TRP B NE1   1 
ATOM   3418 C CE2   . TRP B 1 98  ? 29.347 -8.737  37.515  1.00 16.18 ? 89  TRP B CE2   1 
ATOM   3419 C CE3   . TRP B 1 98  ? 31.487 -7.656  37.766  1.00 17.92 ? 89  TRP B CE3   1 
ATOM   3420 C CZ2   . TRP B 1 98  ? 28.665 -7.556  37.816  1.00 18.99 ? 89  TRP B CZ2   1 
ATOM   3421 C CZ3   . TRP B 1 98  ? 30.806 -6.491  38.081  1.00 19.34 ? 89  TRP B CZ3   1 
ATOM   3422 C CH2   . TRP B 1 98  ? 29.424 -6.448  38.086  1.00 18.01 ? 89  TRP B CH2   1 
ATOM   3423 N N     . LYS B 1 99  ? 35.528 -11.310 36.390  1.00 23.93 ? 90  LYS B N     1 
ATOM   3424 C CA    . LYS B 1 99  ? 36.876 -11.513 36.917  1.00 23.63 ? 90  LYS B CA    1 
ATOM   3425 C C     . LYS B 1 99  ? 37.822 -10.409 36.448  1.00 25.04 ? 90  LYS B C     1 
ATOM   3426 O O     . LYS B 1 99  ? 38.690 -9.948  37.206  1.00 20.46 ? 90  LYS B O     1 
ATOM   3427 C CB    . LYS B 1 99  ? 37.358 -12.913 36.504  1.00 23.91 ? 90  LYS B CB    1 
ATOM   3428 C CG    . LYS B 1 99  ? 38.772 -13.271 36.934  1.00 32.19 ? 90  LYS B CG    1 
ATOM   3429 C CD    . LYS B 1 99  ? 39.020 -14.770 36.740  1.00 40.02 ? 90  LYS B CD    1 
ATOM   3430 C CE    . LYS B 1 99  ? 40.292 -15.231 37.455  1.00 44.74 ? 90  LYS B CE    1 
ATOM   3431 N NZ    . LYS B 1 99  ? 40.726 -14.254 38.485  1.00 49.43 ? 90  LYS B NZ    1 
ATOM   3432 N N     . LYS B 1 100 ? 37.647 -9.946  35.205  1.00 21.37 ? 91  LYS B N     1 
ATOM   3433 C CA    . LYS B 1 100 ? 38.498 -8.878  34.694  1.00 23.08 ? 91  LYS B CA    1 
ATOM   3434 C C     . LYS B 1 100 ? 38.243 -7.563  35.416  1.00 22.23 ? 91  LYS B C     1 
ATOM   3435 O O     . LYS B 1 100 ? 39.157 -6.749  35.582  1.00 25.22 ? 91  LYS B O     1 
ATOM   3436 C CB    . LYS B 1 100 ? 38.254 -8.725  33.201  1.00 21.81 ? 91  LYS B CB    1 
ATOM   3437 C CG    . LYS B 1 100 ? 38.423 -10.057 32.480  1.00 21.28 ? 91  LYS B CG    1 
ATOM   3438 C CD    . LYS B 1 100 ? 37.893 -9.984  31.056  1.00 29.17 ? 91  LYS B CD    1 
ATOM   3439 C CE    . LYS B 1 100 ? 37.916 -11.352 30.400  1.00 34.97 ? 91  LYS B CE    1 
ATOM   3440 N NZ    . LYS B 1 100 ? 37.883 -11.240 28.900  1.00 39.52 ? 91  LYS B NZ    1 
ATOM   3441 N N     . ILE B 1 101 ? 36.994 -7.305  35.777  1.00 21.34 ? 92  ILE B N     1 
ATOM   3442 C CA    . ILE B 1 101 ? 36.669 -6.074  36.491  1.00 19.70 ? 92  ILE B CA    1 
ATOM   3443 C C     . ILE B 1 101 ? 37.196 -6.137  37.918  1.00 20.23 ? 92  ILE B C     1 
ATOM   3444 O O     . ILE B 1 101 ? 37.755 -5.164  38.439  1.00 22.02 ? 92  ILE B O     1 
ATOM   3445 C CB    . ILE B 1 101 ? 35.151 -5.873  36.443  1.00 20.48 ? 92  ILE B CB    1 
ATOM   3446 C CG1   . ILE B 1 101 ? 34.743 -5.600  34.991  1.00 20.80 ? 92  ILE B CG1   1 
ATOM   3447 C CG2   . ILE B 1 101 ? 34.720 -4.789  37.405  1.00 18.92 ? 92  ILE B CG2   1 
ATOM   3448 C CD1   . ILE B 1 101 ? 33.453 -6.258  34.614  1.00 20.33 ? 92  ILE B CD1   1 
ATOM   3449 N N     . VAL B 1 102 ? 37.006 -7.275  38.579  1.00 19.49 ? 93  VAL B N     1 
ATOM   3450 C CA    . VAL B 1 102 ? 37.442 -7.397  39.964  1.00 20.73 ? 93  VAL B CA    1 
ATOM   3451 C C     . VAL B 1 102 ? 38.953 -7.220  40.044  1.00 26.29 ? 93  VAL B C     1 
ATOM   3452 O O     . VAL B 1 102 ? 39.470 -6.518  40.931  1.00 23.62 ? 93  VAL B O     1 
ATOM   3453 C CB    . VAL B 1 102 ? 36.977 -8.750  40.550  1.00 22.25 ? 93  VAL B CB    1 
ATOM   3454 C CG1   . VAL B 1 102 ? 37.668 -9.015  41.852  1.00 25.01 ? 93  VAL B CG1   1 
ATOM   3455 C CG2   . VAL B 1 102 ? 35.441 -8.759  40.721  1.00 19.84 ? 93  VAL B CG2   1 
ATOM   3456 N N     . ASP B 1 103 ? 39.674 -7.773  39.057  1.00 23.89 ? 94  ASP B N     1 
ATOM   3457 C CA    . ASP B 1 103 ? 41.132 -7.666  39.038  1.00 25.49 ? 94  ASP B CA    1 
ATOM   3458 C C     . ASP B 1 103 ? 41.577 -6.217  38.966  1.00 23.40 ? 94  ASP B C     1 
ATOM   3459 O O     . ASP B 1 103 ? 42.491 -5.798  39.686  1.00 22.57 ? 94  ASP B O     1 
ATOM   3460 C CB    . ASP B 1 103 ? 41.705 -8.459  37.860  1.00 25.87 ? 94  ASP B CB    1 
ATOM   3461 C CG    . ASP B 1 103 ? 41.729 -9.958  38.134  1.00 32.94 ? 94  ASP B CG    1 
ATOM   3462 O OD1   . ASP B 1 103 ? 41.494 -10.348 39.305  1.00 37.85 ? 94  ASP B OD1   1 
ATOM   3463 O OD2   . ASP B 1 103 ? 41.983 -10.745 37.193  1.00 37.65 ? 94  ASP B OD2   1 
ATOM   3464 N N     . VAL B 1 104 ? 40.924 -5.433  38.117  1.00 24.28 ? 95  VAL B N     1 
ATOM   3465 C CA    . VAL B 1 104 ? 41.272 -4.019  37.978  1.00 23.54 ? 95  VAL B CA    1 
ATOM   3466 C C     . VAL B 1 104 ? 41.011 -3.259  39.273  1.00 24.51 ? 95  VAL B C     1 
ATOM   3467 O O     . VAL B 1 104 ? 41.810 -2.410  39.703  1.00 23.29 ? 95  VAL B O     1 
ATOM   3468 C CB    . VAL B 1 104 ? 40.483 -3.430  36.798  1.00 26.59 ? 95  VAL B CB    1 
ATOM   3469 C CG1   . VAL B 1 104 ? 40.720 -1.955  36.706  1.00 26.16 ? 95  VAL B CG1   1 
ATOM   3470 C CG2   . VAL B 1 104 ? 40.869 -4.146  35.521  1.00 29.52 ? 95  VAL B CG2   1 
ATOM   3471 N N     . VAL B 1 105 ? 39.887 -3.551  39.921  1.00 23.10 ? 96  VAL B N     1 
ATOM   3472 C CA    . VAL B 1 105 ? 39.554 -2.884  41.168  1.00 21.55 ? 96  VAL B CA    1 
ATOM   3473 C C     . VAL B 1 105 ? 40.508 -3.315  42.284  1.00 25.16 ? 96  VAL B C     1 
ATOM   3474 O O     . VAL B 1 105 ? 40.935 -2.503  43.124  1.00 19.79 ? 96  VAL B O     1 
ATOM   3475 C CB    . VAL B 1 105 ? 38.086 -3.204  41.493  1.00 27.67 ? 96  VAL B CB    1 
ATOM   3476 C CG1   . VAL B 1 105 ? 37.759 -2.965  42.966  1.00 25.96 ? 96  VAL B CG1   1 
ATOM   3477 C CG2   . VAL B 1 105 ? 37.168 -2.441  40.513  1.00 22.72 ? 96  VAL B CG2   1 
ATOM   3478 N N     . HIS B 1 106 ? 40.856 -4.596  42.314  1.00 22.51 ? 97  HIS B N     1 
ATOM   3479 C CA    . HIS B 1 106 ? 41.776 -5.077  43.339  1.00 24.13 ? 97  HIS B CA    1 
ATOM   3480 C C     . HIS B 1 106 ? 43.168 -4.476  43.168  1.00 23.00 ? 97  HIS B C     1 
ATOM   3481 O O     . HIS B 1 106 ? 43.845 -4.199  44.168  1.00 22.17 ? 97  HIS B O     1 
ATOM   3482 C CB    . HIS B 1 106 ? 41.819 -6.597  43.311  1.00 22.69 ? 97  HIS B CB    1 
ATOM   3483 C CG    . HIS B 1 106 ? 40.704 -7.236  44.073  1.00 20.25 ? 97  HIS B CG    1 
ATOM   3484 N ND1   . HIS B 1 106 ? 40.356 -8.557  43.914  1.00 22.04 ? 97  HIS B ND1   1 
ATOM   3485 C CD2   . HIS B 1 106 ? 39.884 -6.743  45.036  1.00 21.17 ? 97  HIS B CD2   1 
ATOM   3486 C CE1   . HIS B 1 106 ? 39.350 -8.846  44.725  1.00 25.03 ? 97  HIS B CE1   1 
ATOM   3487 N NE2   . HIS B 1 106 ? 39.040 -7.760  45.409  1.00 22.33 ? 97  HIS B NE2   1 
ATOM   3488 N N     . ALA B 1 107 ? 43.579 -4.191  41.933  1.00 22.11 ? 98  ALA B N     1 
ATOM   3489 C CA    . ALA B 1 107 ? 44.884 -3.570  41.731  1.00 24.45 ? 98  ALA B CA    1 
ATOM   3490 C C     . ALA B 1 107 ? 44.972 -2.174  42.350  1.00 24.51 ? 98  ALA B C     1 
ATOM   3491 O O     . ALA B 1 107 ? 46.074 -1.724  42.677  1.00 27.89 ? 98  ALA B O     1 
ATOM   3492 C CB    . ALA B 1 107 ? 45.196 -3.502  40.236  1.00 24.56 ? 98  ALA B CB    1 
ATOM   3493 N N     . LYS B 1 108 ? 43.841 -1.497  42.542  1.00 22.32 ? 99  LYS B N     1 
ATOM   3494 C CA    . LYS B 1 108 ? 43.780 -0.203  43.227  1.00 25.93 ? 99  LYS B CA    1 
ATOM   3495 C C     . LYS B 1 108 ? 43.678 -0.330  44.743  1.00 29.54 ? 99  LYS B C     1 
ATOM   3496 O O     . LYS B 1 108 ? 43.645 0.694   45.440  1.00 31.25 ? 99  LYS B O     1 
ATOM   3497 C CB    . LYS B 1 108 ? 42.575 0.598   42.710  1.00 23.83 ? 99  LYS B CB    1 
ATOM   3498 C CG    . LYS B 1 108 ? 42.626 1.017   41.245  1.00 29.65 ? 99  LYS B CG    1 
ATOM   3499 C CD    . LYS B 1 108 ? 43.570 2.199   41.051  1.00 35.06 ? 99  LYS B CD    1 
ATOM   3500 C CE    . LYS B 1 108 ? 42.890 3.384   40.372  1.00 40.82 ? 99  LYS B CE    1 
ATOM   3501 N NZ    . LYS B 1 108 ? 41.893 4.066   41.267  1.00 36.06 ? 99  LYS B NZ    1 
ATOM   3502 N N     . GLY B 1 109 ? 43.584 -1.542  45.274  1.00 23.40 ? 100 GLY B N     1 
ATOM   3503 C CA    . GLY B 1 109 ? 43.520 -1.722  46.703  1.00 23.60 ? 100 GLY B CA    1 
ATOM   3504 C C     . GLY B 1 109 ? 42.120 -1.733  47.287  1.00 23.28 ? 100 GLY B C     1 
ATOM   3505 O O     . GLY B 1 109 ? 41.977 -1.744  48.515  1.00 22.25 ? 100 GLY B O     1 
ATOM   3506 N N     . ALA B 1 110 ? 41.089 -1.758  46.459  1.00 21.12 ? 101 ALA B N     1 
ATOM   3507 C CA    . ALA B 1 110 ? 39.713 -1.704  46.945  1.00 20.04 ? 101 ALA B CA    1 
ATOM   3508 C C     . ALA B 1 110 ? 39.189 -3.091  47.316  1.00 22.53 ? 101 ALA B C     1 
ATOM   3509 O O     . ALA B 1 110 ? 39.631 -4.120  46.779  1.00 23.87 ? 101 ALA B O     1 
ATOM   3510 C CB    . ALA B 1 110 ? 38.798 -1.092  45.880  1.00 22.64 ? 101 ALA B CB    1 
ATOM   3511 N N     . VAL B 1 111 ? 38.209 -3.096  48.218  1.00 22.69 ? 102 VAL B N     1 
ATOM   3512 C CA    . VAL B 1 111 ? 37.391 -4.269  48.539  1.00 17.21 ? 102 VAL B CA    1 
ATOM   3513 C C     . VAL B 1 111 ? 36.095 -4.151  47.746  1.00 17.41 ? 102 VAL B C     1 
ATOM   3514 O O     . VAL B 1 111 ? 35.505 -3.066  47.686  1.00 20.93 ? 102 VAL B O     1 
ATOM   3515 C CB    . VAL B 1 111 ? 37.103 -4.326  50.050  1.00 20.92 ? 102 VAL B CB    1 
ATOM   3516 C CG1   . VAL B 1 111 ? 36.314 -5.615  50.418  1.00 19.79 ? 102 VAL B CG1   1 
ATOM   3517 C CG2   . VAL B 1 111 ? 38.428 -4.240  50.850  1.00 19.35 ? 102 VAL B CG2   1 
ATOM   3518 N N     . ILE B 1 112 ? 35.661 -5.220  47.088  1.00 17.75 ? 103 ILE B N     1 
ATOM   3519 C CA    . ILE B 1 112 ? 34.447 -5.115  46.279  1.00 16.99 ? 103 ILE B CA    1 
ATOM   3520 C C     . ILE B 1 112 ? 33.505 -6.279  46.576  1.00 17.38 ? 103 ILE B C     1 
ATOM   3521 O O     . ILE B 1 112 ? 33.901 -7.451  46.504  1.00 18.99 ? 103 ILE B O     1 
ATOM   3522 C CB    . ILE B 1 112 ? 34.777 -5.035  44.767  1.00 19.77 ? 103 ILE B CB    1 
ATOM   3523 C CG1   . ILE B 1 112 ? 33.496 -4.766  43.959  1.00 18.57 ? 103 ILE B CG1   1 
ATOM   3524 C CG2   . ILE B 1 112 ? 35.568 -6.281  44.277  1.00 16.49 ? 103 ILE B CG2   1 
ATOM   3525 C CD1   . ILE B 1 112 ? 33.784 -4.246  42.532  1.00 22.57 ? 103 ILE B CD1   1 
ATOM   3526 N N     . PHE B 1 113 ? 32.242 -5.966  46.860  1.00 15.36 ? 104 PHE B N     1 
ATOM   3527 C CA    . PHE B 1 113 ? 31.187 -6.967  46.997  1.00 14.43 ? 104 PHE B CA    1 
ATOM   3528 C C     . PHE B 1 113 ? 30.238 -6.881  45.808  1.00 17.77 ? 104 PHE B C     1 
ATOM   3529 O O     . PHE B 1 113 ? 29.950 -5.776  45.320  1.00 15.07 ? 104 PHE B O     1 
ATOM   3530 C CB    . PHE B 1 113 ? 30.342 -6.725  48.269  1.00 15.08 ? 104 PHE B CB    1 
ATOM   3531 C CG    . PHE B 1 113 ? 30.895 -7.331  49.543  1.00 15.73 ? 104 PHE B CG    1 
ATOM   3532 C CD1   . PHE B 1 113 ? 32.249 -7.494  49.746  1.00 18.32 ? 104 PHE B CD1   1 
ATOM   3533 C CD2   . PHE B 1 113 ? 30.013 -7.671  50.562  1.00 14.40 ? 104 PHE B CD2   1 
ATOM   3534 C CE1   . PHE B 1 113 ? 32.732 -8.022  50.968  1.00 17.90 ? 104 PHE B CE1   1 
ATOM   3535 C CE2   . PHE B 1 113 ? 30.481 -8.234  51.783  1.00 15.94 ? 104 PHE B CE2   1 
ATOM   3536 C CZ    . PHE B 1 113 ? 31.847 -8.398  51.955  1.00 16.58 ? 104 PHE B CZ    1 
ATOM   3537 N N     . CYS B 1 114 ? 29.705 -8.037  45.387  1.00 14.99 ? 105 CYS B N     1 
ATOM   3538 C CA    . CYS B 1 114 ? 28.709 -8.119  44.313  1.00 19.69 ? 105 CYS B CA    1 
ATOM   3539 C C     . CYS B 1 114 ? 27.315 -8.177  44.922  1.00 17.16 ? 105 CYS B C     1 
ATOM   3540 O O     . CYS B 1 114 ? 27.015 -9.089  45.694  1.00 16.93 ? 105 CYS B O     1 
ATOM   3541 C CB    . CYS B 1 114 ? 28.921 -9.369  43.451  1.00 18.89 ? 105 CYS B CB    1 
ATOM   3542 S SG    . CYS B 1 114 ? 27.729 -9.568  42.066  1.00 19.13 ? 105 CYS B SG    1 
ATOM   3543 N N     . GLN B 1 115 ? 26.446 -7.230  44.553  1.00 14.37 ? 106 GLN B N     1 
ATOM   3544 C CA    . GLN B 1 115 ? 25.073 -7.245  45.030  1.00 14.45 ? 106 GLN B CA    1 
ATOM   3545 C C     . GLN B 1 115 ? 24.200 -8.232  44.236  1.00 16.90 ? 106 GLN B C     1 
ATOM   3546 O O     . GLN B 1 115 ? 24.017 -8.088  43.016  1.00 15.21 ? 106 GLN B O     1 
ATOM   3547 C CB    . GLN B 1 115 ? 24.457 -5.851  44.958  1.00 13.92 ? 106 GLN B CB    1 
ATOM   3548 C CG    . GLN B 1 115 ? 23.123 -5.859  45.684  1.00 14.35 ? 106 GLN B CG    1 
ATOM   3549 C CD    . GLN B 1 115 ? 22.319 -4.599  45.528  1.00 18.14 ? 106 GLN B CD    1 
ATOM   3550 O OE1   . GLN B 1 115 ? 21.928 -4.205  44.401  1.00 16.92 ? 106 GLN B OE1   1 
ATOM   3551 N NE2   . GLN B 1 115 ? 22.012 -3.977  46.642  1.00 14.59 ? 106 GLN B NE2   1 
ATOM   3552 N N     . LEU B 1 116 ? 23.593 -9.199  44.936  1.00 13.41 ? 107 LEU B N     1 
ATOM   3553 C CA    . LEU B 1 116 ? 22.749 -10.209 44.289  1.00 16.30 ? 107 LEU B CA    1 
ATOM   3554 C C     . LEU B 1 116 ? 21.300 -9.738  44.246  1.00 18.44 ? 107 LEU B C     1 
ATOM   3555 O O     . LEU B 1 116 ? 20.714 -9.431  45.288  1.00 15.97 ? 107 LEU B O     1 
ATOM   3556 C CB    . LEU B 1 116 ? 22.846 -11.532 45.057  1.00 19.96 ? 107 LEU B CB    1 
ATOM   3557 C CG    . LEU B 1 116 ? 24.241 -12.111 45.151  1.00 15.09 ? 107 LEU B CG    1 
ATOM   3558 C CD1   . LEU B 1 116 ? 24.168 -13.550 45.792  1.00 16.25 ? 107 LEU B CD1   1 
ATOM   3559 C CD2   . LEU B 1 116 ? 24.837 -12.130 43.751  1.00 18.01 ? 107 LEU B CD2   1 
ATOM   3560 N N     . TRP B 1 117 ? 20.705 -9.717  43.052  1.00 12.81 ? 108 TRP B N     1 
ATOM   3561 C CA    . TRP B 1 117 ? 19.458 -8.979  42.847  1.00 15.88 ? 108 TRP B CA    1 
ATOM   3562 C C     . TRP B 1 117 ? 18.406 -9.800  42.099  1.00 18.74 ? 108 TRP B C     1 
ATOM   3563 O O     . TRP B 1 117 ? 18.625 -10.184 40.942  1.00 18.95 ? 108 TRP B O     1 
ATOM   3564 C CB    . TRP B 1 117 ? 19.773 -7.699  42.051  1.00 17.05 ? 108 TRP B CB    1 
ATOM   3565 C CG    . TRP B 1 117 ? 18.640 -6.712  41.876  1.00 14.94 ? 108 TRP B CG    1 
ATOM   3566 C CD1   . TRP B 1 117 ? 17.543 -6.576  42.659  1.00 16.46 ? 108 TRP B CD1   1 
ATOM   3567 C CD2   . TRP B 1 117 ? 18.511 -5.739  40.813  1.00 14.89 ? 108 TRP B CD2   1 
ATOM   3568 N NE1   . TRP B 1 117 ? 16.743 -5.553  42.177  1.00 17.67 ? 108 TRP B NE1   1 
ATOM   3569 C CE2   . TRP B 1 117 ? 17.316 -5.020  41.055  1.00 15.29 ? 108 TRP B CE2   1 
ATOM   3570 C CE3   . TRP B 1 117 ? 19.313 -5.383  39.716  1.00 16.59 ? 108 TRP B CE3   1 
ATOM   3571 C CZ2   . TRP B 1 117 ? 16.890 -3.948  40.237  1.00 15.79 ? 108 TRP B CZ2   1 
ATOM   3572 C CZ3   . TRP B 1 117 ? 18.904 -4.308  38.905  1.00 16.14 ? 108 TRP B CZ3   1 
ATOM   3573 C CH2   . TRP B 1 117 ? 17.678 -3.640  39.143  1.00 15.64 ? 108 TRP B CH2   1 
ATOM   3574 N N     . HIS B 1 118 ? 17.242 -10.003 42.720  1.00 16.92 ? 109 HIS B N     1 
ATOM   3575 C CA    . HIS B 1 118 ? 16.061 -10.544 42.047  1.00 17.47 ? 109 HIS B CA    1 
ATOM   3576 C C     . HIS B 1 118 ? 14.940 -9.525  42.195  1.00 16.35 ? 109 HIS B C     1 
ATOM   3577 O O     . HIS B 1 118 ? 14.584 -9.156  43.321  1.00 14.55 ? 109 HIS B O     1 
ATOM   3578 C CB    . HIS B 1 118 ? 15.628 -11.887 42.644  1.00 15.13 ? 109 HIS B CB    1 
ATOM   3579 C CG    . HIS B 1 118 ? 14.694 -12.670 41.771  1.00 16.22 ? 109 HIS B CG    1 
ATOM   3580 N ND1   . HIS B 1 118 ? 13.535 -12.141 41.256  1.00 15.43 ? 109 HIS B ND1   1 
ATOM   3581 C CD2   . HIS B 1 118 ? 14.745 -13.958 41.340  1.00 16.48 ? 109 HIS B CD2   1 
ATOM   3582 C CE1   . HIS B 1 118 ? 12.916 -13.057 40.524  1.00 18.49 ? 109 HIS B CE1   1 
ATOM   3583 N NE2   . HIS B 1 118 ? 13.624 -14.175 40.576  1.00 19.72 ? 109 HIS B NE2   1 
ATOM   3584 N N     . VAL B 1 119 ? 14.401 -9.064  41.054  1.00 16.35 ? 110 VAL B N     1 
ATOM   3585 C CA    . VAL B 1 119 ? 13.345 -8.061  41.074  1.00 14.87 ? 110 VAL B CA    1 
ATOM   3586 C C     . VAL B 1 119 ? 11.961 -8.590  41.411  1.00 15.56 ? 110 VAL B C     1 
ATOM   3587 O O     . VAL B 1 119 ? 11.070 -7.785  41.652  1.00 15.72 ? 110 VAL B O     1 
ATOM   3588 C CB    . VAL B 1 119 ? 13.180 -7.323  39.729  1.00 14.13 ? 110 VAL B CB    1 
ATOM   3589 C CG1   . VAL B 1 119 ? 14.431 -6.450  39.429  1.00 14.32 ? 110 VAL B CG1   1 
ATOM   3590 C CG2   . VAL B 1 119 ? 12.740 -8.311  38.580  1.00 15.30 ? 110 VAL B CG2   1 
ATOM   3591 N N     . GLY B 1 120 ? 11.744 -9.907  41.455  1.00 14.79 ? 111 GLY B N     1 
ATOM   3592 C CA    . GLY B 1 120 ? 10.388 -10.417 41.625  1.00 14.77 ? 111 GLY B CA    1 
ATOM   3593 C C     . GLY B 1 120 ? 9.400  -9.809  40.631  1.00 16.45 ? 111 GLY B C     1 
ATOM   3594 O O     . GLY B 1 120 ? 9.624  -9.827  39.404  1.00 18.71 ? 111 GLY B O     1 
ATOM   3595 N N     . ARG B 1 121 ? 8.304  -9.244  41.152  1.00 15.53 ? 112 ARG B N     1 
ATOM   3596 C CA    . ARG B 1 121 ? 7.206  -8.765  40.319  1.00 16.50 ? 112 ARG B CA    1 
ATOM   3597 C C     . ARG B 1 121 ? 7.515  -7.448  39.607  1.00 18.36 ? 112 ARG B C     1 
ATOM   3598 O O     . ARG B 1 121 ? 6.678  -7.004  38.805  1.00 16.75 ? 112 ARG B O     1 
ATOM   3599 C CB    . ARG B 1 121 ? 5.932  -8.597  41.154  1.00 15.92 ? 112 ARG B CB    1 
ATOM   3600 C CG    . ARG B 1 121 ? 5.948  -7.311  42.008  1.00 14.53 ? 112 ARG B CG    1 
ATOM   3601 C CD    . ARG B 1 121 ? 4.742  -7.262  43.004  1.00 14.50 ? 112 ARG B CD    1 
ATOM   3602 N NE    . ARG B 1 121 ? 4.692  -6.021  43.797  1.00 16.30 ? 112 ARG B NE    1 
ATOM   3603 C CZ    . ARG B 1 121 ? 3.615  -5.560  44.424  1.00 19.14 ? 112 ARG B CZ    1 
ATOM   3604 N NH1   . ARG B 1 121 ? 2.466  -6.207  44.390  1.00 18.85 ? 112 ARG B NH1   1 
ATOM   3605 N NH2   . ARG B 1 121 ? 3.694  -4.428  45.139  1.00 16.87 ? 112 ARG B NH2   1 
ATOM   3606 N N     . ALA B 1 122 ? 8.694  -6.857  39.848  1.00 15.82 ? 113 ALA B N     1 
ATOM   3607 C CA    . ALA B 1 122 ? 9.070  -5.552  39.278  1.00 17.28 ? 113 ALA B CA    1 
ATOM   3608 C C     . ALA B 1 122 ? 9.816  -5.842  37.976  1.00 15.22 ? 113 ALA B C     1 
ATOM   3609 O O     . ALA B 1 122 ? 11.035 -5.707  37.859  1.00 14.45 ? 113 ALA B O     1 
ATOM   3610 C CB    . ALA B 1 122 ? 9.897  -4.734  40.286  1.00 15.20 ? 113 ALA B CB    1 
ATOM   3611 N N     . SER B 1 123 ? 9.057  -6.387  37.031  1.00 18.31 ? 114 SER B N     1 
ATOM   3612 C CA    . SER B 1 123 ? 9.594  -6.832  35.753  1.00 16.61 ? 114 SER B CA    1 
ATOM   3613 C C     . SER B 1 123 ? 8.485  -6.681  34.717  1.00 18.88 ? 114 SER B C     1 
ATOM   3614 O O     . SER B 1 123 ? 7.437  -6.087  34.991  1.00 17.97 ? 114 SER B O     1 
ATOM   3615 C CB    . SER B 1 123 ? 10.082 -8.287  35.815  1.00 17.50 ? 114 SER B CB    1 
ATOM   3616 O OG    . SER B 1 123 ? 10.942 -8.582  34.717  1.00 18.34 ? 114 SER B OG    1 
ATOM   3617 N N     . HIS B 1 124 ? 8.714  -7.255  33.542  1.00 20.03 ? 115 HIS B N     1 
ATOM   3618 C CA    . HIS B 1 124 ? 7.846  -7.115  32.380  1.00 18.25 ? 115 HIS B CA    1 
ATOM   3619 C C     . HIS B 1 124 ? 8.158  -8.274  31.445  1.00 19.00 ? 115 HIS B C     1 
ATOM   3620 O O     . HIS B 1 124 ? 9.267  -8.835  31.455  1.00 18.76 ? 115 HIS B O     1 
ATOM   3621 C CB    . HIS B 1 124 ? 8.062  -5.747  31.699  1.00 22.17 ? 115 HIS B CB    1 
ATOM   3622 C CG    . HIS B 1 124 ? 7.107  -5.433  30.571  1.00 18.39 ? 115 HIS B CG    1 
ATOM   3623 N ND1   . HIS B 1 124 ? 7.287  -5.906  29.283  1.00 18.85 ? 115 HIS B ND1   1 
ATOM   3624 C CD2   . HIS B 1 124 ? 6.027  -4.612  30.517  1.00 22.04 ? 115 HIS B CD2   1 
ATOM   3625 C CE1   . HIS B 1 124 ? 6.317  -5.453  28.509  1.00 22.44 ? 115 HIS B CE1   1 
ATOM   3626 N NE2   . HIS B 1 124 ? 5.544  -4.659  29.230  1.00 20.91 ? 115 HIS B NE2   1 
ATOM   3627 N N     . GLU B 1 125 ? 7.157  -8.662  30.665  1.00 20.90 ? 116 GLU B N     1 
ATOM   3628 C CA    . GLU B 1 125 ? 7.361  -9.650  29.603  1.00 19.71 ? 116 GLU B CA    1 
ATOM   3629 C C     . GLU B 1 125 ? 8.659  -9.452  28.826  1.00 24.90 ? 116 GLU B C     1 
ATOM   3630 O O     . GLU B 1 125 ? 9.353  -10.424 28.528  1.00 24.20 ? 116 GLU B O     1 
ATOM   3631 C CB    . GLU B 1 125 ? 6.181  -9.595  28.625  1.00 23.75 ? 116 GLU B CB    1 
ATOM   3632 N N     . VAL B 1 126 ? 9.011  -8.203  28.487  1.00 18.95 ? 117 VAL B N     1 
ATOM   3633 C CA    . VAL B 1 126 ? 10.178 -7.987  27.639  1.00 21.81 ? 117 VAL B CA    1 
ATOM   3634 C C     . VAL B 1 126 ? 11.475 -8.357  28.349  1.00 21.61 ? 117 VAL B C     1 
ATOM   3635 O O     . VAL B 1 126 ? 12.493 -8.593  27.682  1.00 16.95 ? 117 VAL B O     1 
ATOM   3636 C CB    . VAL B 1 126 ? 10.209 -6.533  27.116  1.00 21.58 ? 117 VAL B CB    1 
ATOM   3637 C CG1   . VAL B 1 126 ? 10.694 -5.547  28.209  1.00 22.91 ? 117 VAL B CG1   1 
ATOM   3638 C CG2   . VAL B 1 126 ? 11.126 -6.433  25.878  1.00 26.87 ? 117 VAL B CG2   1 
ATOM   3639 N N     . TYR B 1 127 ? 11.453 -8.492  29.676  1.00 20.51 ? 118 TYR B N     1 
ATOM   3640 C CA    . TYR B 1 127 ? 12.645 -8.864  30.433  1.00 17.24 ? 118 TYR B CA    1 
ATOM   3641 C C     . TYR B 1 127 ? 12.655 -10.331 30.863  1.00 19.71 ? 118 TYR B C     1 
ATOM   3642 O O     . TYR B 1 127 ? 13.629 -10.767 31.475  1.00 20.64 ? 118 TYR B O     1 
ATOM   3643 C CB    . TYR B 1 127 ? 12.792 -7.990  31.714  1.00 19.52 ? 118 TYR B CB    1 
ATOM   3644 C CG    . TYR B 1 127 ? 13.007 -6.540  31.438  1.00 17.26 ? 118 TYR B CG    1 
ATOM   3645 C CD1   . TYR B 1 127 ? 14.117 -6.109  30.689  1.00 17.59 ? 118 TYR B CD1   1 
ATOM   3646 C CD2   . TYR B 1 127 ? 12.093 -5.586  31.891  1.00 16.79 ? 118 TYR B CD2   1 
ATOM   3647 C CE1   . TYR B 1 127 ? 14.328 -4.762  30.433  1.00 17.02 ? 118 TYR B CE1   1 
ATOM   3648 C CE2   . TYR B 1 127 ? 12.279 -4.238  31.611  1.00 18.84 ? 118 TYR B CE2   1 
ATOM   3649 C CZ    . TYR B 1 127 ? 13.391 -3.835  30.863  1.00 15.36 ? 118 TYR B CZ    1 
ATOM   3650 O OH    . TYR B 1 127 ? 13.603 -2.498  30.600  1.00 19.49 ? 118 TYR B OH    1 
ATOM   3651 N N     . GLN B 1 128 ? 11.591 -11.095 30.576  1.00 18.28 ? 119 GLN B N     1 
ATOM   3652 C CA    . GLN B 1 128 ? 11.442 -12.482 31.008  1.00 22.60 ? 119 GLN B CA    1 
ATOM   3653 C C     . GLN B 1 128 ? 11.613 -13.461 29.857  1.00 25.47 ? 119 GLN B C     1 
ATOM   3654 O O     . GLN B 1 128 ? 11.124 -13.203 28.746  1.00 26.37 ? 119 GLN B O     1 
ATOM   3655 C CB    . GLN B 1 128 ? 10.066 -12.689 31.621  1.00 19.35 ? 119 GLN B CB    1 
ATOM   3656 C CG    . GLN B 1 128 ? 9.901  -11.939 32.922  1.00 19.93 ? 119 GLN B CG    1 
ATOM   3657 C CD    . GLN B 1 128 ? 10.827 -12.486 33.990  1.00 19.91 ? 119 GLN B CD    1 
ATOM   3658 O OE1   . GLN B 1 128 ? 11.129 -13.696 34.004  1.00 26.10 ? 119 GLN B OE1   1 
ATOM   3659 N NE2   . GLN B 1 128 ? 11.285 -11.612 34.895  1.00 19.38 ? 119 GLN B NE2   1 
ATOM   3660 N N     . PRO B 1 129 ? 12.279 -14.594 30.085  1.00 26.01 ? 120 PRO B N     1 
ATOM   3661 C CA    . PRO B 1 129 ? 12.379 -15.611 29.017  1.00 25.74 ? 120 PRO B CA    1 
ATOM   3662 C C     . PRO B 1 129 ? 10.991 -16.023 28.554  1.00 26.27 ? 120 PRO B C     1 
ATOM   3663 O O     . PRO B 1 129 ? 10.070 -16.209 29.362  1.00 26.85 ? 120 PRO B O     1 
ATOM   3664 C CB    . PRO B 1 129 ? 13.127 -16.776 29.679  1.00 25.98 ? 120 PRO B CB    1 
ATOM   3665 C CG    . PRO B 1 129 ? 13.726 -16.239 30.947  1.00 30.34 ? 120 PRO B CG    1 
ATOM   3666 C CD    . PRO B 1 129 ? 12.903 -15.035 31.342  1.00 21.99 ? 120 PRO B CD    1 
ATOM   3667 N N     . ALA B 1 130 ? 10.836 -16.095 27.232  1.00 29.88 ? 121 ALA B N     1 
ATOM   3668 C CA    . ALA B 1 130 ? 9.588  -16.461 26.575  1.00 27.38 ? 121 ALA B CA    1 
ATOM   3669 C C     . ALA B 1 130 ? 8.448  -15.547 26.973  1.00 30.33 ? 121 ALA B C     1 
ATOM   3670 O O     . ALA B 1 130 ? 7.288  -15.957 26.897  1.00 33.30 ? 121 ALA B O     1 
ATOM   3671 C CB    . ALA B 1 130 ? 9.219  -17.926 26.856  1.00 33.81 ? 121 ALA B CB    1 
ATOM   3672 N N     . GLY B 1 131 ? 8.779  -14.313 27.410  1.00 27.80 ? 122 GLY B N     1 
ATOM   3673 C CA    . GLY B 1 131 ? 7.812  -13.312 27.819  1.00 28.84 ? 122 GLY B CA    1 
ATOM   3674 C C     . GLY B 1 131 ? 6.868  -13.813 28.893  1.00 29.36 ? 122 GLY B C     1 
ATOM   3675 O O     . GLY B 1 131 ? 5.707  -13.395 28.951  1.00 32.55 ? 122 GLY B O     1 
ATOM   3676 N N     . ALA B 1 132 ? 7.361  -14.730 29.724  1.00 28.89 ? 123 ALA B N     1 
ATOM   3677 C CA    . ALA B 1 132 ? 6.579  -15.332 30.794  1.00 28.85 ? 123 ALA B CA    1 
ATOM   3678 C C     . ALA B 1 132 ? 6.351  -14.333 31.931  1.00 28.70 ? 123 ALA B C     1 
ATOM   3679 O O     . ALA B 1 132 ? 6.981  -13.277 31.988  1.00 31.39 ? 123 ALA B O     1 
ATOM   3680 C CB    . ALA B 1 132 ? 7.294  -16.556 31.340  1.00 31.33 ? 123 ALA B CB    1 
ATOM   3681 N N     . ALA B 1 133 ? 5.453  -14.691 32.861  1.00 24.88 ? 124 ALA B N     1 
ATOM   3682 C CA    . ALA B 1 133 ? 5.120  -13.777 33.962  1.00 25.57 ? 124 ALA B CA    1 
ATOM   3683 C C     . ALA B 1 133 ? 6.275  -13.692 34.956  1.00 24.44 ? 124 ALA B C     1 
ATOM   3684 O O     . ALA B 1 133 ? 6.950  -14.688 35.203  1.00 24.67 ? 124 ALA B O     1 
ATOM   3685 C CB    . ALA B 1 133 ? 3.854  -14.230 34.707  1.00 25.26 ? 124 ALA B CB    1 
ATOM   3686 N N     . PRO B 1 134 ? 6.514  -12.523 35.555  1.00 21.39 ? 125 PRO B N     1 
ATOM   3687 C CA    . PRO B 1 134 ? 7.452  -12.446 36.695  1.00 20.43 ? 125 PRO B CA    1 
ATOM   3688 C C     . PRO B 1 134 ? 6.903  -13.221 37.877  1.00 18.35 ? 125 PRO B C     1 
ATOM   3689 O O     . PRO B 1 134 ? 5.708  -13.497 37.944  1.00 21.26 ? 125 PRO B O     1 
ATOM   3690 C CB    . PRO B 1 134 ? 7.523  -10.953 37.025  1.00 18.90 ? 125 PRO B CB    1 
ATOM   3691 C CG    . PRO B 1 134 ? 6.524  -10.279 36.204  1.00 27.44 ? 125 PRO B CG    1 
ATOM   3692 C CD    . PRO B 1 134 ? 5.795  -11.266 35.312  1.00 24.23 ? 125 PRO B CD    1 
ATOM   3693 N N     . ILE B 1 135 ? 7.779  -13.524 38.847  1.00 22.07 ? 126 ILE B N     1 
ATOM   3694 C CA    . ILE B 1 135 ? 7.402  -14.295 40.032  1.00 17.06 ? 126 ILE B CA    1 
ATOM   3695 C C     . ILE B 1 135 ? 7.355  -13.385 41.262  1.00 18.94 ? 126 ILE B C     1 
ATOM   3696 O O     . ILE B 1 135 ? 7.998  -12.328 41.314  1.00 20.80 ? 126 ILE B O     1 
ATOM   3697 C CB    . ILE B 1 135 ? 8.349  -15.489 40.297  1.00 20.27 ? 126 ILE B CB    1 
ATOM   3698 C CG1   . ILE B 1 135 ? 9.813  -15.034 40.357  1.00 19.78 ? 126 ILE B CG1   1 
ATOM   3699 C CG2   . ILE B 1 135 ? 8.171  -16.587 39.215  1.00 19.47 ? 126 ILE B CG2   1 
ATOM   3700 C CD1   . ILE B 1 135 ? 10.569 -15.707 41.460  1.00 18.09 ? 126 ILE B CD1   1 
ATOM   3701 N N     . SER B 1 136 ? 6.594  -13.812 42.271  1.00 19.41 ? 127 SER B N     1 
ATOM   3702 C CA    . SER B 1 136 ? 6.468  -13.006 43.486  1.00 17.02 ? 127 SER B CA    1 
ATOM   3703 C C     . SER B 1 136 ? 5.942  -13.875 44.616  1.00 21.17 ? 127 SER B C     1 
ATOM   3704 O O     . SER B 1 136 ? 5.644  -15.064 44.441  1.00 19.64 ? 127 SER B O     1 
ATOM   3705 C CB    . SER B 1 136 ? 5.552  -11.791 43.255  1.00 17.45 ? 127 SER B CB    1 
ATOM   3706 O OG    . SER B 1 136 ? 5.685  -10.825 44.311  1.00 21.06 ? 127 SER B OG    1 
ATOM   3707 N N     . SER B 1 137 ? 5.857  -13.261 45.797  1.00 21.97 ? 128 SER B N     1 
ATOM   3708 C CA    . SER B 1 137 ? 5.167  -13.867 46.932  1.00 18.04 ? 128 SER B CA    1 
ATOM   3709 C C     . SER B 1 137 ? 3.681  -14.002 46.668  1.00 17.56 ? 128 SER B C     1 
ATOM   3710 O O     . SER B 1 137 ? 3.016  -14.862 47.270  1.00 20.89 ? 128 SER B O     1 
ATOM   3711 C CB    . SER B 1 137 ? 5.369  -12.986 48.166  1.00 18.18 ? 128 SER B CB    1 
ATOM   3712 O OG    . SER B 1 137 ? 4.939  -11.673 47.831  1.00 18.66 ? 128 SER B OG    1 
ATOM   3713 N N     . THR B 1 138 ? 3.172  -13.186 45.744  1.00 24.40 ? 129 THR B N     1 
ATOM   3714 C CA    . THR B 1 138 ? 1.791  -12.762 45.637  1.00 22.61 ? 129 THR B CA    1 
ATOM   3715 C C     . THR B 1 138 ? 1.391  -12.804 44.168  1.00 24.96 ? 129 THR B C     1 
ATOM   3716 O O     . THR B 1 138 ? 2.250  -12.771 43.279  1.00 20.72 ? 129 THR B O     1 
ATOM   3717 C CB    . THR B 1 138 ? 1.665  -11.311 46.154  1.00 29.64 ? 129 THR B CB    1 
ATOM   3718 O OG1   . THR B 1 138 ? 0.301  -10.929 46.175  1.00 29.96 ? 129 THR B OG1   1 
ATOM   3719 C CG2   . THR B 1 138 ? 2.497  -10.281 45.225  1.00 23.92 ? 129 THR B CG2   1 
ATOM   3720 N N     . GLU B 1 139 ? 0.083  -12.873 43.902  1.00 25.23 ? 130 GLU B N     1 
ATOM   3721 C CA    . GLU B 1 139 ? -0.391 -12.573 42.548  1.00 24.54 ? 130 GLU B CA    1 
ATOM   3722 C C     . GLU B 1 139 ? -0.711 -11.097 42.334  1.00 26.14 ? 130 GLU B C     1 
ATOM   3723 O O     . GLU B 1 139 ? -1.185 -10.736 41.255  1.00 25.69 ? 130 GLU B O     1 
ATOM   3724 C CB    . GLU B 1 139 ? -1.642 -13.385 42.211  1.00 26.90 ? 130 GLU B CB    1 
ATOM   3725 C CG    . GLU B 1 139 ? -1.405 -14.872 42.156  1.00 32.46 ? 130 GLU B CG    1 
ATOM   3726 C CD    . GLU B 1 139 ? -2.642 -15.639 41.697  1.00 46.91 ? 130 GLU B CD    1 
ATOM   3727 O OE1   . GLU B 1 139 ? -3.779 -15.261 42.075  1.00 48.26 ? 130 GLU B OE1   1 
ATOM   3728 O OE2   . GLU B 1 139 ? -2.471 -16.604 40.926  1.00 44.61 ? 130 GLU B OE2   1 
ATOM   3729 N N     . LYS B 1 140 ? -0.473 -10.236 43.313  1.00 23.62 ? 131 LYS B N     1 
ATOM   3730 C CA    . LYS B 1 140 ? -0.841 -8.828  43.154  1.00 21.70 ? 131 LYS B CA    1 
ATOM   3731 C C     . LYS B 1 140 ? 0.209  -8.090  42.328  1.00 24.62 ? 131 LYS B C     1 
ATOM   3732 O O     . LYS B 1 140 ? 1.403  -8.216  42.606  1.00 20.94 ? 131 LYS B O     1 
ATOM   3733 C CB    . LYS B 1 140 ? -1.011 -8.153  44.516  1.00 27.33 ? 131 LYS B CB    1 
ATOM   3734 C CG    . LYS B 1 140 ? -2.072 -8.845  45.336  1.00 26.89 ? 131 LYS B CG    1 
ATOM   3735 C CD    . LYS B 1 140 ? -2.214 -8.254  46.722  1.00 35.44 ? 131 LYS B CD    1 
ATOM   3736 C CE    . LYS B 1 140 ? -0.874 -7.985  47.364  1.00 31.89 ? 131 LYS B CE    1 
ATOM   3737 N NZ    . LYS B 1 140 ? -1.041 -7.563  48.779  1.00 41.58 ? 131 LYS B NZ    1 
ATOM   3738 N N     . PRO B 1 141 ? -0.194 -7.319  41.324  1.00 25.70 ? 132 PRO B N     1 
ATOM   3739 C CA    . PRO B 1 141 ? 0.769  -6.507  40.579  1.00 21.89 ? 132 PRO B CA    1 
ATOM   3740 C C     . PRO B 1 141 ? 1.068  -5.201  41.295  1.00 20.30 ? 132 PRO B C     1 
ATOM   3741 O O     . PRO B 1 141 ? 0.306  -4.728  42.140  1.00 20.68 ? 132 PRO B O     1 
ATOM   3742 C CB    . PRO B 1 141 ? 0.042  -6.243  39.255  1.00 28.55 ? 132 PRO B CB    1 
ATOM   3743 C CG    . PRO B 1 141 ? -1.407 -6.175  39.655  1.00 29.19 ? 132 PRO B CG    1 
ATOM   3744 C CD    . PRO B 1 141 ? -1.581 -7.031  40.915  1.00 26.74 ? 132 PRO B CD    1 
ATOM   3745 N N     . ILE B 1 142 ? 2.217  -4.619  40.941  1.00 20.71 ? 133 ILE B N     1 
ATOM   3746 C CA    . ILE B 1 142 ? 2.453  -3.212  41.243  1.00 19.12 ? 133 ILE B CA    1 
ATOM   3747 C C     . ILE B 1 142 ? 1.375  -2.388  40.558  1.00 20.07 ? 133 ILE B C     1 
ATOM   3748 O O     . ILE B 1 142 ? 1.040  -2.638  39.398  1.00 20.53 ? 133 ILE B O     1 
ATOM   3749 C CB    . ILE B 1 142 ? 3.863  -2.817  40.777  1.00 21.39 ? 133 ILE B CB    1 
ATOM   3750 C CG1   . ILE B 1 142 ? 4.900  -3.672  41.515  1.00 19.05 ? 133 ILE B CG1   1 
ATOM   3751 C CG2   . ILE B 1 142 ? 4.131  -1.326  40.960  1.00 21.63 ? 133 ILE B CG2   1 
ATOM   3752 C CD1   . ILE B 1 142 ? 6.242  -3.593  40.887  1.00 19.85 ? 133 ILE B CD1   1 
ATOM   3753 N N     . SER B 1 143 ? 0.808  -1.416  41.270  1.00 19.69 ? 134 SER B N     1 
ATOM   3754 C CA    . SER B 1 143 ? -0.331 -0.694  40.715  1.00 22.53 ? 134 SER B CA    1 
ATOM   3755 C C     . SER B 1 143 ? 0.129  0.275   39.624  1.00 22.28 ? 134 SER B C     1 
ATOM   3756 O O     . SER B 1 143 ? 1.325  0.480   39.406  1.00 21.11 ? 134 SER B O     1 
ATOM   3757 C CB    . SER B 1 143 ? -1.055 0.064   41.808  1.00 21.59 ? 134 SER B CB    1 
ATOM   3758 O OG    . SER B 1 143 ? -0.268 1.163   42.153  1.00 25.23 ? 134 SER B OG    1 
ATOM   3759 N N     . ASN B 1 144 ? -0.842 0.909   38.954  1.00 27.16 ? 135 ASN B N     1 
ATOM   3760 C CA    . ASN B 1 144 ? -0.495 1.750   37.806  1.00 30.67 ? 135 ASN B CA    1 
ATOM   3761 C C     . ASN B 1 144 ? 0.034  3.117   38.224  1.00 31.33 ? 135 ASN B C     1 
ATOM   3762 O O     . ASN B 1 144 ? 0.368  3.920   37.353  1.00 32.84 ? 135 ASN B O     1 
ATOM   3763 C CB    . ASN B 1 144 ? -1.695 1.935   36.856  1.00 34.16 ? 135 ASN B CB    1 
ATOM   3764 C CG    . ASN B 1 144 ? -2.900 2.598   37.522  1.00 40.29 ? 135 ASN B CG    1 
ATOM   3765 O OD1   . ASN B 1 144 ? -2.914 2.856   38.730  1.00 44.85 ? 135 ASN B OD1   1 
ATOM   3766 N ND2   . ASN B 1 144 ? -3.939 2.848   36.728  1.00 47.20 ? 135 ASN B ND2   1 
ATOM   3767 N N     . ARG B 1 145 ? 0.124  3.400   39.533  1.00 24.88 ? 136 ARG B N     1 
ATOM   3768 C CA    . ARG B 1 145 ? 0.916  4.523   40.026  1.00 26.49 ? 136 ARG B CA    1 
ATOM   3769 C C     . ARG B 1 145 ? 2.369  4.450   39.568  1.00 27.07 ? 136 ARG B C     1 
ATOM   3770 O O     . ARG B 1 145 ? 3.037  5.489   39.503  1.00 31.13 ? 136 ARG B O     1 
ATOM   3771 C CB    . ARG B 1 145 ? 0.859  4.580   41.566  1.00 27.48 ? 136 ARG B CB    1 
ATOM   3772 N N     . TRP B 1 146 ? 2.871  3.257   39.233  1.00 22.38 ? 137 TRP B N     1 
ATOM   3773 C CA    . TRP B 1 146 ? 4.266  3.054   38.846  1.00 22.94 ? 137 TRP B CA    1 
ATOM   3774 C C     . TRP B 1 146 ? 4.323  2.442   37.464  1.00 21.69 ? 137 TRP B C     1 
ATOM   3775 O O     . TRP B 1 146 ? 3.449  1.646   37.109  1.00 21.72 ? 137 TRP B O     1 
ATOM   3776 C CB    . TRP B 1 146 ? 5.001  2.116   39.812  1.00 24.37 ? 137 TRP B CB    1 
ATOM   3777 C CG    . TRP B 1 146 ? 4.811  2.475   41.223  1.00 27.70 ? 137 TRP B CG    1 
ATOM   3778 C CD1   . TRP B 1 146 ? 3.761  2.132   42.030  1.00 23.56 ? 137 TRP B CD1   1 
ATOM   3779 C CD2   . TRP B 1 146 ? 5.694  3.249   42.012  1.00 26.35 ? 137 TRP B CD2   1 
ATOM   3780 N NE1   . TRP B 1 146 ? 3.937  2.664   43.280  1.00 29.14 ? 137 TRP B NE1   1 
ATOM   3781 C CE2   . TRP B 1 146 ? 5.120  3.352   43.300  1.00 27.04 ? 137 TRP B CE2   1 
ATOM   3782 C CE3   . TRP B 1 146 ? 6.929  3.855   41.770  1.00 27.42 ? 137 TRP B CE3   1 
ATOM   3783 C CZ2   . TRP B 1 146 ? 5.737  4.036   44.335  1.00 30.54 ? 137 TRP B CZ2   1 
ATOM   3784 C CZ3   . TRP B 1 146 ? 7.537  4.538   42.802  1.00 30.38 ? 137 TRP B CZ3   1 
ATOM   3785 C CH2   . TRP B 1 146 ? 6.940  4.623   44.063  1.00 31.12 ? 137 TRP B CH2   1 
ATOM   3786 N N     . ARG B 1 147 ? 5.431  2.867   36.718  1.00 21.09 ? 138 ARG B N     1 
ATOM   3787 C CA    . ARG B 1 147 ? 5.582  2.327   35.380  1.00 19.64 ? 138 ARG B CA    1 
ATOM   3788 C C     . ARG B 1 147 ? 7.016  1.816   35.203  1.00 22.09 ? 138 ARG B C     1 
ATOM   3789 O O     . ARG B 1 147 ? 7.968  2.367   35.765  1.00 22.28 ? 138 ARG B O     1 
ATOM   3790 C CB    . ARG B 1 147 ? 5.252  3.381   34.322  1.00 26.44 ? 138 ARG B CB    1 
ATOM   3791 C CG    . ARG B 1 147 ? 3.812  3.867   34.359  1.00 32.96 ? 138 ARG B CG    1 
ATOM   3792 C CD    . ARG B 1 147 ? 2.788  2.802   33.997  1.00 35.74 ? 138 ARG B CD    1 
ATOM   3793 N NE    . ARG B 1 147 ? 1.424  3.322   34.025  1.00 36.04 ? 138 ARG B NE    1 
ATOM   3794 C CZ    . ARG B 1 147 ? 0.337  2.566   33.975  1.00 47.47 ? 138 ARG B CZ    1 
ATOM   3795 N NH1   . ARG B 1 147 ? 0.448  1.245   33.900  1.00 39.86 ? 138 ARG B NH1   1 
ATOM   3796 N NH2   . ARG B 1 147 ? -0.866 3.125   34.005  1.00 54.83 ? 138 ARG B NH2   1 
ATOM   3797 N N     . ILE B 1 148 ? 7.299  0.824   34.451  1.00 17.90 ? 139 ILE B N     1 
ATOM   3798 C CA    . ILE B 1 148 ? 8.642  0.249   34.327  1.00 16.56 ? 139 ILE B CA    1 
ATOM   3799 C C     . ILE B 1 148 ? 9.371  0.837   33.132  1.00 21.13 ? 139 ILE B C     1 
ATOM   3800 O O     . ILE B 1 148 ? 8.805  1.019   32.053  1.00 20.24 ? 139 ILE B O     1 
ATOM   3801 C CB    . ILE B 1 148 ? 8.584  -1.295  34.221  1.00 18.01 ? 139 ILE B CB    1 
ATOM   3802 C CG1   . ILE B 1 148 ? 9.985  -1.929  34.297  1.00 17.90 ? 139 ILE B CG1   1 
ATOM   3803 C CG2   . ILE B 1 148 ? 7.871  -1.779  32.937  1.00 17.20 ? 139 ILE B CG2   1 
ATOM   3804 C CD1   . ILE B 1 148 ? 9.937  -3.468  34.411  1.00 17.34 ? 139 ILE B CD1   1 
ATOM   3805 N N     . LEU B 1 149 ? 10.654 1.087   33.311  1.00 18.82 ? 140 LEU B N     1 
ATOM   3806 C CA    . LEU B 1 149 ? 11.486 1.523   32.200  1.00 17.05 ? 140 LEU B CA    1 
ATOM   3807 C C     . LEU B 1 149 ? 11.636 0.392   31.185  1.00 16.83 ? 140 LEU B C     1 
ATOM   3808 O O     . LEU B 1 149 ? 12.019 -0.726  31.541  1.00 14.62 ? 140 LEU B O     1 
ATOM   3809 C CB    . LEU B 1 149 ? 12.845 1.953   32.730  1.00 16.95 ? 140 LEU B CB    1 
ATOM   3810 C CG    . LEU B 1 149 ? 13.859 2.336   31.656  1.00 17.11 ? 140 LEU B CG    1 
ATOM   3811 C CD1   . LEU B 1 149 ? 13.312 3.562   30.895  1.00 19.24 ? 140 LEU B CD1   1 
ATOM   3812 C CD2   . LEU B 1 149 ? 15.230 2.606   32.300  1.00 19.97 ? 140 LEU B CD2   1 
ATOM   3813 N N     . MET B 1 150 ? 11.342 0.675   29.935  1.00 16.13 ? 141 MET B N     1 
ATOM   3814 C CA    . MET B 1 150 ? 11.475 -0.334  28.874  1.00 18.68 ? 141 MET B CA    1 
ATOM   3815 C C     . MET B 1 150 ? 12.834 -0.241  28.164  1.00 18.44 ? 141 MET B C     1 
ATOM   3816 O O     . MET B 1 150 ? 13.516 0.784   28.230  1.00 18.49 ? 141 MET B O     1 
ATOM   3817 C CB    . MET B 1 150 ? 10.345 -0.153  27.858  1.00 17.60 ? 141 MET B CB    1 
ATOM   3818 C CG    . MET B 1 150 ? 9.014  -0.320  28.559  1.00 19.88 ? 141 MET B CG    1 
ATOM   3819 S SD    . MET B 1 150 ? 8.554  -2.022  28.912  1.00 23.71 ? 141 MET B SD    1 
ATOM   3820 C CE    . MET B 1 150 ? 8.407  -2.695  27.270  1.00 22.01 ? 141 MET B CE    1 
ATOM   3821 N N     . PRO B 1 151 ? 13.280 -1.303  27.462  1.00 16.16 ? 142 PRO B N     1 
ATOM   3822 C CA    . PRO B 1 151 ? 14.580 -1.217  26.751  1.00 16.15 ? 142 PRO B CA    1 
ATOM   3823 C C     . PRO B 1 151 ? 14.655 -0.092  25.728  1.00 18.22 ? 142 PRO B C     1 
ATOM   3824 O O     . PRO B 1 151 ? 15.752 0.410   25.438  1.00 18.22 ? 142 PRO B O     1 
ATOM   3825 C CB    . PRO B 1 151 ? 14.715 -2.589  26.063  1.00 20.42 ? 142 PRO B CB    1 
ATOM   3826 C CG    . PRO B 1 151 ? 13.739 -3.465  26.708  1.00 21.10 ? 142 PRO B CG    1 
ATOM   3827 C CD    . PRO B 1 151 ? 12.746 -2.670  27.504  1.00 22.15 ? 142 PRO B CD    1 
ATOM   3828 N N     . ASP B 1 152 ? 13.530 0.397   25.256  1.00 17.53 ? 143 ASP B N     1 
ATOM   3829 C CA    . ASP B 1 152 ? 13.573 1.487   24.286  1.00 18.81 ? 143 ASP B CA    1 
ATOM   3830 C C     . ASP B 1 152 ? 13.441 2.860   24.938  1.00 19.25 ? 143 ASP B C     1 
ATOM   3831 O O     . ASP B 1 152 ? 13.316 3.863   24.225  1.00 19.05 ? 143 ASP B O     1 
ATOM   3832 C CB    . ASP B 1 152 ? 12.508 1.285   23.213  1.00 17.21 ? 143 ASP B CB    1 
ATOM   3833 C CG    . ASP B 1 152 ? 11.078 1.468   23.714  1.00 23.69 ? 143 ASP B CG    1 
ATOM   3834 O OD1   . ASP B 1 152 ? 10.859 1.817   24.909  1.00 24.40 ? 143 ASP B OD1   1 
ATOM   3835 O OD2   . ASP B 1 152 ? 10.148 1.257   22.883  1.00 25.82 ? 143 ASP B OD2   1 
ATOM   3836 N N     . GLY B 1 153 ? 13.472 2.938   26.273  1.00 20.16 ? 144 GLY B N     1 
ATOM   3837 C CA    . GLY B 1 153 ? 13.336 4.208   26.949  1.00 18.64 ? 144 GLY B CA    1 
ATOM   3838 C C     . GLY B 1 153 ? 11.914 4.688   27.156  1.00 20.84 ? 144 GLY B C     1 
ATOM   3839 O O     . GLY B 1 153 ? 11.715 5.709   27.828  1.00 25.38 ? 144 GLY B O     1 
ATOM   3840 N N     . THR B 1 154 ? 10.917 3.990   26.629  1.00 24.25 ? 145 THR B N     1 
ATOM   3841 C CA    . THR B 1 154 ? 9.539  4.271   27.001  1.00 20.92 ? 145 THR B CA    1 
ATOM   3842 C C     . THR B 1 154 ? 9.273  3.647   28.367  1.00 22.06 ? 145 THR B C     1 
ATOM   3843 O O     . THR B 1 154 ? 10.147 3.008   28.959  1.00 19.72 ? 145 THR B O     1 
ATOM   3844 C CB    . THR B 1 154 ? 8.565  3.723   25.955  1.00 17.20 ? 145 THR B CB    1 
ATOM   3845 O OG1   . THR B 1 154 ? 8.652  2.294   25.874  1.00 21.34 ? 145 THR B OG1   1 
ATOM   3846 C CG2   . THR B 1 154 ? 8.867  4.317   24.549  1.00 21.45 ? 145 THR B CG2   1 
ATOM   3847 N N     . HIS B 1 155 ? 8.039  3.792   28.851  1.00 19.67 ? 146 HIS B N     1 
ATOM   3848 C CA    . HIS B 1 155 ? 7.608  3.147   30.090  1.00 21.71 ? 146 HIS B CA    1 
ATOM   3849 C C     . HIS B 1 155 ? 6.454  2.215   29.790  1.00 27.75 ? 146 HIS B C     1 
ATOM   3850 O O     . HIS B 1 155 ? 5.661  2.467   28.873  1.00 27.68 ? 146 HIS B O     1 
ATOM   3851 C CB    . HIS B 1 155 ? 7.245  4.209   31.131  1.00 22.32 ? 146 HIS B CB    1 
ATOM   3852 C CG    . HIS B 1 155 ? 8.427  5.030   31.516  1.00 30.78 ? 146 HIS B CG    1 
ATOM   3853 N ND1   . HIS B 1 155 ? 9.404  4.560   32.373  1.00 33.84 ? 146 HIS B ND1   1 
ATOM   3854 C CD2   . HIS B 1 155 ? 8.857  6.238   31.077  1.00 29.83 ? 146 HIS B CD2   1 
ATOM   3855 C CE1   . HIS B 1 155 ? 10.356 5.470   32.488  1.00 34.26 ? 146 HIS B CE1   1 
ATOM   3856 N NE2   . HIS B 1 155 ? 10.051 6.492   31.705  1.00 34.89 ? 146 HIS B NE2   1 
ATOM   3857 N N     . GLY B 1 156 ? 6.405  1.099   30.526  1.00 22.72 ? 147 GLY B N     1 
ATOM   3858 C CA    . GLY B 1 156 ? 5.386  0.088   30.327  1.00 19.77 ? 147 GLY B CA    1 
ATOM   3859 C C     . GLY B 1 156 ? 4.661  -0.282  31.618  1.00 19.02 ? 147 GLY B C     1 
ATOM   3860 O O     . GLY B 1 156 ? 4.941  0.254   32.694  1.00 20.54 ? 147 GLY B O     1 
ATOM   3861 N N     . ILE B 1 157 ? 3.722  -1.207  31.480  1.00 19.59 ? 148 ILE B N     1 
ATOM   3862 C CA    . ILE B 1 157 ? 2.832  -1.587  32.582  1.00 22.81 ? 148 ILE B CA    1 
ATOM   3863 C C     . ILE B 1 157 ? 3.437  -2.767  33.320  1.00 21.84 ? 148 ILE B C     1 
ATOM   3864 O O     . ILE B 1 157 ? 3.812  -3.764  32.693  1.00 20.10 ? 148 ILE B O     1 
ATOM   3865 C CB    . ILE B 1 157 ? 1.432  -1.957  32.058  1.00 24.90 ? 148 ILE B CB    1 
ATOM   3866 C CG1   . ILE B 1 157 ? 0.894  -0.911  31.067  1.00 29.08 ? 148 ILE B CG1   1 
ATOM   3867 C CG2   . ILE B 1 157 ? 0.462  -2.246  33.219  1.00 24.30 ? 148 ILE B CG2   1 
ATOM   3868 C CD1   . ILE B 1 157 ? 0.689  0.410   31.659  1.00 29.10 ? 148 ILE B CD1   1 
ATOM   3869 N N     . TYR B 1 158 ? 3.509  -2.680  34.651  1.00 19.97 ? 149 TYR B N     1 
ATOM   3870 C CA    . TYR B 1 158 ? 3.911  -3.864  35.425  1.00 19.71 ? 149 TYR B CA    1 
ATOM   3871 C C     . TYR B 1 158 ? 2.807  -4.914  35.377  1.00 21.01 ? 149 TYR B C     1 
ATOM   3872 O O     . TYR B 1 158 ? 1.650  -4.603  35.698  1.00 20.32 ? 149 TYR B O     1 
ATOM   3873 C CB    . TYR B 1 158 ? 4.189  -3.519  36.881  1.00 20.92 ? 149 TYR B CB    1 
ATOM   3874 C CG    . TYR B 1 158 ? 5.437  -2.702  37.120  1.00 18.87 ? 149 TYR B CG    1 
ATOM   3875 C CD1   . TYR B 1 158 ? 6.699  -3.280  37.093  1.00 18.10 ? 149 TYR B CD1   1 
ATOM   3876 C CD2   . TYR B 1 158 ? 5.335  -1.336  37.396  1.00 16.83 ? 149 TYR B CD2   1 
ATOM   3877 C CE1   . TYR B 1 158 ? 7.834  -2.524  37.343  1.00 19.02 ? 149 TYR B CE1   1 
ATOM   3878 C CE2   . TYR B 1 158 ? 6.458  -0.571  37.632  1.00 19.97 ? 149 TYR B CE2   1 
ATOM   3879 C CZ    . TYR B 1 158 ? 7.696  -1.162  37.630  1.00 17.28 ? 149 TYR B CZ    1 
ATOM   3880 O OH    . TYR B 1 158 ? 8.791  -0.352  37.851  1.00 18.15 ? 149 TYR B OH    1 
ATOM   3881 N N     . PRO B 1 159 ? 3.124  -6.148  35.005  1.00 24.24 ? 150 PRO B N     1 
ATOM   3882 C CA    . PRO B 1 159 ? 2.115  -7.189  34.802  1.00 23.61 ? 150 PRO B CA    1 
ATOM   3883 C C     . PRO B 1 159 ? 1.761  -7.940  36.081  1.00 24.85 ? 150 PRO B C     1 
ATOM   3884 O O     . PRO B 1 159 ? 2.397  -7.798  37.128  1.00 21.96 ? 150 PRO B O     1 
ATOM   3885 C CB    . PRO B 1 159 ? 2.813  -8.137  33.820  1.00 26.40 ? 150 PRO B CB    1 
ATOM   3886 C CG    . PRO B 1 159 ? 4.289  -8.048  34.259  1.00 23.42 ? 150 PRO B CG    1 
ATOM   3887 C CD    . PRO B 1 159 ? 4.473  -6.586  34.593  1.00 22.01 ? 150 PRO B CD    1 
ATOM   3888 N N     . LYS B 1 160 ? 0.735  -8.774  35.961  1.00 26.57 ? 151 LYS B N     1 
ATOM   3889 C CA    . LYS B 1 160 ? 0.353  -9.665  37.055  1.00 26.70 ? 151 LYS B CA    1 
ATOM   3890 C C     . LYS B 1 160 ? 1.448  -10.703 37.282  1.00 23.17 ? 151 LYS B C     1 
ATOM   3891 O O     . LYS B 1 160 ? 1.819  -11.417 36.338  1.00 25.60 ? 151 LYS B O     1 
ATOM   3892 C CB    . LYS B 1 160 ? -0.981 -10.339 36.719  1.00 28.45 ? 151 LYS B CB    1 
ATOM   3893 C CG    . LYS B 1 160 ? -1.395 -11.430 37.693  1.00 33.27 ? 151 LYS B CG    1 
ATOM   3894 C CD    . LYS B 1 160 ? -2.912 -11.519 37.809  1.00 37.81 ? 151 LYS B CD    1 
ATOM   3895 C CE    . LYS B 1 160 ? -3.317 -12.018 39.205  1.00 41.19 ? 151 LYS B CE    1 
ATOM   3896 N NZ    . LYS B 1 160 ? -3.696 -10.902 40.167  1.00 37.20 ? 151 LYS B NZ    1 
ATOM   3897 N N     . PRO B 1 161 ? 2.002  -10.816 38.486  1.00 25.41 ? 152 PRO B N     1 
ATOM   3898 C CA    . PRO B 1 161 ? 3.009  -11.852 38.743  1.00 23.57 ? 152 PRO B CA    1 
ATOM   3899 C C     . PRO B 1 161 ? 2.370  -13.205 39.043  1.00 19.06 ? 152 PRO B C     1 
ATOM   3900 O O     . PRO B 1 161 ? 1.172  -13.336 39.304  1.00 22.70 ? 152 PRO B O     1 
ATOM   3901 C CB    . PRO B 1 161 ? 3.745  -11.325 39.977  1.00 22.51 ? 152 PRO B CB    1 
ATOM   3902 C CG    . PRO B 1 161 ? 2.647  -10.584 40.750  1.00 21.60 ? 152 PRO B CG    1 
ATOM   3903 C CD    . PRO B 1 161 ? 1.731  -9.981  39.679  1.00 21.24 ? 152 PRO B CD    1 
ATOM   3904 N N     . ARG B 1 162 ? 3.226  -14.214 39.052  1.00 21.95 ? 153 ARG B N     1 
ATOM   3905 C CA    . ARG B 1 162 ? 2.873  -15.567 39.437  1.00 22.94 ? 153 ARG B CA    1 
ATOM   3906 C C     . ARG B 1 162 ? 3.376  -15.808 40.861  1.00 22.95 ? 153 ARG B C     1 
ATOM   3907 O O     . ARG B 1 162 ? 4.570  -15.647 41.132  1.00 21.88 ? 153 ARG B O     1 
ATOM   3908 C CB    . ARG B 1 162 ? 3.514  -16.552 38.453  1.00 23.81 ? 153 ARG B CB    1 
ATOM   3909 C CG    . ARG B 1 162 ? 3.369  -17.984 38.794  1.00 28.33 ? 153 ARG B CG    1 
ATOM   3910 C CD    . ARG B 1 162 ? 3.905  -18.837 37.643  1.00 24.87 ? 153 ARG B CD    1 
ATOM   3911 N NE    . ARG B 1 162 ? 5.351  -18.759 37.402  1.00 21.47 ? 153 ARG B NE    1 
ATOM   3912 C CZ    . ARG B 1 162 ? 6.258  -19.433 38.090  1.00 22.96 ? 153 ARG B CZ    1 
ATOM   3913 N NH1   . ARG B 1 162 ? 5.924  -20.145 39.158  1.00 26.23 ? 153 ARG B NH1   1 
ATOM   3914 N NH2   . ARG B 1 162 ? 7.533  -19.394 37.701  1.00 23.78 ? 153 ARG B NH2   1 
ATOM   3915 N N     . ALA B 1 163 ? 2.462  -16.160 41.772  1.00 23.68 ? 154 ALA B N     1 
ATOM   3916 C CA    . ALA B 1 163 ? 2.817  -16.457 43.156  1.00 22.70 ? 154 ALA B CA    1 
ATOM   3917 C C     . ALA B 1 163 ? 3.456  -17.841 43.251  1.00 22.91 ? 154 ALA B C     1 
ATOM   3918 O O     . ALA B 1 163 ? 2.870  -18.837 42.816  1.00 23.76 ? 154 ALA B O     1 
ATOM   3919 C CB    . ALA B 1 163 ? 1.581  -16.389 44.052  1.00 21.27 ? 154 ALA B CB    1 
ATOM   3920 N N     . ILE B 1 164 ? 4.639  -17.918 43.830  1.00 20.77 ? 155 ILE B N     1 
ATOM   3921 C CA    . ILE B 1 164 ? 5.376  -19.179 43.780  1.00 22.36 ? 155 ILE B CA    1 
ATOM   3922 C C     . ILE B 1 164 ? 5.092  -20.024 45.016  1.00 20.19 ? 155 ILE B C     1 
ATOM   3923 O O     . ILE B 1 164 ? 4.844  -19.510 46.110  1.00 21.31 ? 155 ILE B O     1 
ATOM   3924 C CB    . ILE B 1 164 ? 6.885  -18.925 43.613  1.00 21.71 ? 155 ILE B CB    1 
ATOM   3925 C CG1   . ILE B 1 164 ? 7.429  -18.054 44.750  1.00 19.94 ? 155 ILE B CG1   1 
ATOM   3926 C CG2   . ILE B 1 164 ? 7.164  -18.315 42.255  1.00 19.84 ? 155 ILE B CG2   1 
ATOM   3927 C CD1   . ILE B 1 164 ? 8.888  -17.922 44.708  1.00 20.42 ? 155 ILE B CD1   1 
ATOM   3928 N N     . GLY B 1 165 ? 5.200  -21.347 44.849  1.00 21.05 ? 156 GLY B N     1 
ATOM   3929 C CA    . GLY B 1 165 ? 5.075  -22.276 45.956  1.00 19.91 ? 156 GLY B CA    1 
ATOM   3930 C C     . GLY B 1 165 ? 6.390  -22.485 46.670  1.00 20.96 ? 156 GLY B C     1 
ATOM   3931 O O     . GLY B 1 165 ? 7.430  -21.915 46.325  1.00 21.19 ? 156 GLY B O     1 
ATOM   3932 N N     . THR B 1 166 ? 6.356  -23.350 47.691  1.00 18.12 ? 157 THR B N     1 
ATOM   3933 C CA    . THR B 1 166 ? 7.548  -23.433 48.526  1.00 15.58 ? 157 THR B CA    1 
ATOM   3934 C C     . THR B 1 166 ? 8.681  -24.191 47.850  1.00 18.29 ? 157 THR B C     1 
ATOM   3935 O O     . THR B 1 166 ? 9.855  -23.945 48.156  1.00 17.80 ? 157 THR B O     1 
ATOM   3936 C CB    . THR B 1 166 ? 7.205  -24.047 49.893  1.00 22.57 ? 157 THR B CB    1 
ATOM   3937 O OG1   . THR B 1 166 ? 6.766  -25.415 49.736  1.00 21.26 ? 157 THR B OG1   1 
ATOM   3938 C CG2   . THR B 1 166 ? 6.109  -23.212 50.576  1.00 24.04 ? 157 THR B CG2   1 
ATOM   3939 N N     . TYR B 1 167 ? 8.378  -25.113 46.925  1.00 18.64 ? 158 TYR B N     1 
ATOM   3940 C CA    . TYR B 1 167 ? 9.458  -25.730 46.161  1.00 21.18 ? 158 TYR B CA    1 
ATOM   3941 C C     . TYR B 1 167 ? 10.191 -24.694 45.306  1.00 16.70 ? 158 TYR B C     1 
ATOM   3942 O O     . TYR B 1 167 ? 11.426 -24.643 45.290  1.00 18.73 ? 158 TYR B O     1 
ATOM   3943 C CB    . TYR B 1 167 ? 8.902  -26.849 45.279  1.00 16.65 ? 158 TYR B CB    1 
ATOM   3944 C CG    . TYR B 1 167 ? 9.966  -27.489 44.409  1.00 21.65 ? 158 TYR B CG    1 
ATOM   3945 C CD1   . TYR B 1 167 ? 10.971 -28.264 44.974  1.00 24.17 ? 158 TYR B CD1   1 
ATOM   3946 C CD2   . TYR B 1 167 ? 9.958  -27.325 43.023  1.00 18.80 ? 158 TYR B CD2   1 
ATOM   3947 C CE1   . TYR B 1 167 ? 11.941 -28.874 44.180  1.00 23.81 ? 158 TYR B CE1   1 
ATOM   3948 C CE2   . TYR B 1 167 ? 10.925 -27.929 42.230  1.00 26.19 ? 158 TYR B CE2   1 
ATOM   3949 C CZ    . TYR B 1 167 ? 11.915 -28.693 42.811  1.00 28.16 ? 158 TYR B CZ    1 
ATOM   3950 O OH    . TYR B 1 167 ? 12.885 -29.307 42.023  1.00 27.14 ? 158 TYR B OH    1 
ATOM   3951 N N     . GLU B 1 168 ? 9.452  -23.818 44.636  1.00 20.49 ? 159 GLU B N     1 
ATOM   3952 C CA    . GLU B 1 168 ? 10.127 -22.802 43.836  1.00 22.17 ? 159 GLU B CA    1 
ATOM   3953 C C     . GLU B 1 168 ? 10.865 -21.799 44.712  1.00 17.94 ? 159 GLU B C     1 
ATOM   3954 O O     . GLU B 1 168 ? 11.909 -21.278 44.303  1.00 17.50 ? 159 GLU B O     1 
ATOM   3955 C CB    . GLU B 1 168 ? 9.129  -22.090 42.926  1.00 20.32 ? 159 GLU B CB    1 
ATOM   3956 C CG    . GLU B 1 168 ? 9.811  -21.195 41.847  1.00 18.90 ? 159 GLU B CG    1 
ATOM   3957 C CD    . GLU B 1 168 ? 8.883  -20.884 40.676  1.00 24.08 ? 159 GLU B CD    1 
ATOM   3958 O OE1   . GLU B 1 168 ? 7.748  -21.420 40.639  1.00 22.01 ? 159 GLU B OE1   1 
ATOM   3959 O OE2   . GLU B 1 168 ? 9.282  -20.102 39.776  1.00 25.97 ? 159 GLU B OE2   1 
ATOM   3960 N N     . ILE B 1 169 ? 10.367 -21.525 45.924  1.00 16.28 ? 160 ILE B N     1 
ATOM   3961 C CA    . ILE B 1 169 ? 11.127 -20.684 46.837  1.00 16.73 ? 160 ILE B CA    1 
ATOM   3962 C C     . ILE B 1 169 ? 12.484 -21.306 47.107  1.00 18.45 ? 160 ILE B C     1 
ATOM   3963 O O     . ILE B 1 169 ? 13.520 -20.631 47.035  1.00 16.36 ? 160 ILE B O     1 
ATOM   3964 C CB    . ILE B 1 169 ? 10.345 -20.451 48.140  1.00 18.36 ? 160 ILE B CB    1 
ATOM   3965 C CG1   . ILE B 1 169 ? 9.157  -19.528 47.875  1.00 18.68 ? 160 ILE B CG1   1 
ATOM   3966 C CG2   . ILE B 1 169 ? 11.282 -19.909 49.207  1.00 21.15 ? 160 ILE B CG2   1 
ATOM   3967 C CD1   . ILE B 1 169 ? 8.213  -19.506 49.078  1.00 19.81 ? 160 ILE B CD1   1 
ATOM   3968 N N     . SER B 1 170 ? 12.510 -22.617 47.413  1.00 19.37 ? 161 SER B N     1 
ATOM   3969 C CA    . SER B 1 170 ? 13.798 -23.254 47.645  1.00 17.18 ? 161 SER B CA    1 
ATOM   3970 C C     . SER B 1 170 ? 14.688 -23.208 46.394  1.00 16.88 ? 161 SER B C     1 
ATOM   3971 O O     . SER B 1 170 ? 15.921 -23.150 46.520  1.00 17.54 ? 161 SER B O     1 
ATOM   3972 C CB    . SER B 1 170 ? 13.599 -24.697 48.157  1.00 18.99 ? 161 SER B CB    1 
ATOM   3973 O OG    . SER B 1 170 ? 13.244 -25.569 47.085  1.00 25.30 ? 161 SER B OG    1 
ATOM   3974 N N     . GLN B 1 171 ? 14.093 -23.212 45.192  1.00 18.52 ? 162 GLN B N     1 
ATOM   3975 C CA    . GLN B 1 171 ? 14.885 -23.096 43.961  1.00 17.00 ? 162 GLN B CA    1 
ATOM   3976 C C     . GLN B 1 171 ? 15.508 -21.707 43.831  1.00 20.28 ? 162 GLN B C     1 
ATOM   3977 O O     . GLN B 1 171 ? 16.657 -21.565 43.387  1.00 18.34 ? 162 GLN B O     1 
ATOM   3978 C CB    . GLN B 1 171 ? 14.014 -23.382 42.731  1.00 19.62 ? 162 GLN B CB    1 
ATOM   3979 C CG    . GLN B 1 171 ? 13.503 -24.809 42.615  1.00 21.73 ? 162 GLN B CG    1 
ATOM   3980 C CD    . GLN B 1 171 ? 12.761 -25.014 41.311  1.00 23.24 ? 162 GLN B CD    1 
ATOM   3981 O OE1   . GLN B 1 171 ? 11.705 -24.411 41.078  1.00 25.39 ? 162 GLN B OE1   1 
ATOM   3982 N NE2   . GLN B 1 171 ? 13.332 -25.849 40.430  1.00 25.51 ? 162 GLN B NE2   1 
ATOM   3983 N N     . VAL B 1 172 ? 14.765 -20.673 44.229  1.00 17.09 ? 163 VAL B N     1 
ATOM   3984 C CA    . VAL B 1 172 ? 15.299 -19.315 44.149  1.00 16.97 ? 163 VAL B CA    1 
ATOM   3985 C C     . VAL B 1 172 ? 16.424 -19.137 45.162  1.00 14.58 ? 163 VAL B C     1 
ATOM   3986 O O     . VAL B 1 172 ? 17.476 -18.545 44.864  1.00 15.75 ? 163 VAL B O     1 
ATOM   3987 C CB    . VAL B 1 172 ? 14.162 -18.295 44.356  1.00 19.15 ? 163 VAL B CB    1 
ATOM   3988 C CG1   . VAL B 1 172 ? 14.731 -16.863 44.415  1.00 17.78 ? 163 VAL B CG1   1 
ATOM   3989 C CG2   . VAL B 1 172 ? 13.130 -18.404 43.205  1.00 16.85 ? 163 VAL B CG2   1 
ATOM   3990 N N     . VAL B 1 173 ? 16.219 -19.655 46.381  1.00 16.62 ? 164 VAL B N     1 
ATOM   3991 C CA    . VAL B 1 173 ? 17.278 -19.680 47.377  1.00 18.26 ? 164 VAL B CA    1 
ATOM   3992 C C     . VAL B 1 173 ? 18.526 -20.331 46.797  1.00 16.76 ? 164 VAL B C     1 
ATOM   3993 O O     . VAL B 1 173 ? 19.646 -19.835 46.974  1.00 18.07 ? 164 VAL B O     1 
ATOM   3994 C CB    . VAL B 1 173 ? 16.782 -20.415 48.653  1.00 16.87 ? 164 VAL B CB    1 
ATOM   3995 C CG1   . VAL B 1 173 ? 17.934 -20.676 49.628  1.00 20.24 ? 164 VAL B CG1   1 
ATOM   3996 C CG2   . VAL B 1 173 ? 15.630 -19.627 49.382  1.00 18.17 ? 164 VAL B CG2   1 
ATOM   3997 N N     . GLU B 1 174 ? 18.362 -21.455 46.090  1.00 18.81 ? 165 GLU B N     1 
ATOM   3998 C CA    . GLU B 1 174 ? 19.511 -22.102 45.455  1.00 17.45 ? 165 GLU B CA    1 
ATOM   3999 C C     . GLU B 1 174 ? 20.138 -21.216 44.364  1.00 16.25 ? 165 GLU B C     1 
ATOM   4000 O O     . GLU B 1 174 ? 21.365 -21.232 44.172  1.00 17.71 ? 165 GLU B O     1 
ATOM   4001 C CB    . GLU B 1 174 ? 19.103 -23.472 44.880  1.00 19.81 ? 165 GLU B CB    1 
ATOM   4002 C CG    . GLU B 1 174 ? 20.226 -24.097 44.029  1.00 24.15 ? 165 GLU B CG    1 
ATOM   4003 C CD    . GLU B 1 174 ? 21.426 -24.580 44.875  1.00 29.14 ? 165 GLU B CD    1 
ATOM   4004 O OE1   . GLU B 1 174 ? 21.350 -24.586 46.137  1.00 31.71 ? 165 GLU B OE1   1 
ATOM   4005 O OE2   . GLU B 1 174 ? 22.450 -24.967 44.277  1.00 33.15 ? 165 GLU B OE2   1 
ATOM   4006 N N     . ASP B 1 175 ? 19.323 -20.417 43.673  1.00 15.87 ? 166 ASP B N     1 
ATOM   4007 C CA    . ASP B 1 175 ? 19.878 -19.467 42.709  1.00 19.94 ? 166 ASP B CA    1 
ATOM   4008 C C     . ASP B 1 175 ? 20.759 -18.428 43.399  1.00 17.63 ? 166 ASP B C     1 
ATOM   4009 O O     . ASP B 1 175 ? 21.833 -18.084 42.892  1.00 18.19 ? 166 ASP B O     1 
ATOM   4010 C CB    . ASP B 1 175 ? 18.768 -18.780 41.923  1.00 21.03 ? 166 ASP B CB    1 
ATOM   4011 C CG    . ASP B 1 175 ? 18.145 -19.680 40.850  1.00 24.51 ? 166 ASP B CG    1 
ATOM   4012 O OD1   . ASP B 1 175 ? 18.807 -20.647 40.381  1.00 25.38 ? 166 ASP B OD1   1 
ATOM   4013 O OD2   . ASP B 1 175 ? 16.990 -19.399 40.467  1.00 24.11 ? 166 ASP B OD2   1 
ATOM   4014 N N     . TYR B 1 176 ? 20.322 -17.922 44.564  1.00 16.08 ? 167 TYR B N     1 
ATOM   4015 C CA    . TYR B 1 176 ? 21.189 -17.054 45.357  1.00 16.66 ? 167 TYR B CA    1 
ATOM   4016 C C     . TYR B 1 176 ? 22.478 -17.766 45.735  1.00 17.41 ? 167 TYR B C     1 
ATOM   4017 O O     . TYR B 1 176 ? 23.574 -17.202 45.611  1.00 17.80 ? 167 TYR B O     1 
ATOM   4018 C CB    . TYR B 1 176 ? 20.449 -16.605 46.616  1.00 17.15 ? 167 TYR B CB    1 
ATOM   4019 C CG    . TYR B 1 176 ? 19.518 -15.451 46.393  1.00 17.38 ? 167 TYR B CG    1 
ATOM   4020 C CD1   . TYR B 1 176 ? 20.004 -14.156 46.304  1.00 19.29 ? 167 TYR B CD1   1 
ATOM   4021 C CD2   . TYR B 1 176 ? 18.132 -15.655 46.357  1.00 15.60 ? 167 TYR B CD2   1 
ATOM   4022 C CE1   . TYR B 1 176 ? 19.136 -13.086 46.120  1.00 15.61 ? 167 TYR B CE1   1 
ATOM   4023 C CE2   . TYR B 1 176 ? 17.269 -14.612 46.198  1.00 16.90 ? 167 TYR B CE2   1 
ATOM   4024 C CZ    . TYR B 1 176 ? 17.798 -13.318 46.070  1.00 14.36 ? 167 TYR B CZ    1 
ATOM   4025 O OH    . TYR B 1 176 ? 16.948 -12.270 45.949  1.00 17.19 ? 167 TYR B OH    1 
ATOM   4026 N N     . ARG B 1 177 ? 22.357 -19.017 46.209  1.00 18.89 ? 168 ARG B N     1 
ATOM   4027 C CA    . ARG B 1 177 ? 23.528 -19.777 46.654  1.00 17.54 ? 168 ARG B CA    1 
ATOM   4028 C C     . ARG B 1 177 ? 24.546 -19.962 45.534  1.00 16.38 ? 168 ARG B C     1 
ATOM   4029 O O     . ARG B 1 177 ? 25.760 -19.756 45.743  1.00 16.08 ? 168 ARG B O     1 
ATOM   4030 C CB    . ARG B 1 177 ? 23.084 -21.133 47.218  1.00 18.26 ? 168 ARG B CB    1 
ATOM   4031 C CG    . ARG B 1 177 ? 24.149 -21.779 48.106  1.00 22.98 ? 168 ARG B CG    1 
ATOM   4032 C CD    . ARG B 1 177 ? 23.730 -23.198 48.506  1.00 30.96 ? 168 ARG B CD    1 
ATOM   4033 N NE    . ARG B 1 177 ? 23.801 -24.055 47.339  1.00 31.74 ? 168 ARG B NE    1 
ATOM   4034 C CZ    . ARG B 1 177 ? 24.905 -24.651 46.908  1.00 40.66 ? 168 ARG B CZ    1 
ATOM   4035 N NH1   . ARG B 1 177 ? 26.037 -24.600 47.597  1.00 36.10 ? 168 ARG B NH1   1 
ATOM   4036 N NH2   . ARG B 1 177 ? 24.871 -25.319 45.756  1.00 36.86 ? 168 ARG B NH2   1 
ATOM   4037 N N     . ARG B 1 178 ? 24.069 -20.319 44.328  1.00 16.62 ? 169 ARG B N     1 
ATOM   4038 C CA    . ARG B 1 178 ? 24.963 -20.567 43.199  1.00 18.89 ? 169 ARG B CA    1 
ATOM   4039 C C     . ARG B 1 178 ? 25.622 -19.275 42.738  1.00 20.59 ? 169 ARG B C     1 
ATOM   4040 O O     . ARG B 1 178 ? 26.815 -19.259 42.379  1.00 17.24 ? 169 ARG B O     1 
ATOM   4041 C CB    . ARG B 1 178 ? 24.203 -21.212 42.025  1.00 17.16 ? 169 ARG B CB    1 
ATOM   4042 N N     . SER B 1 179 ? 24.856 -18.177 42.745  1.00 19.05 ? 170 SER B N     1 
ATOM   4043 C CA    . SER B 1 179 ? 25.426 -16.887 42.368  1.00 19.46 ? 170 SER B CA    1 
ATOM   4044 C C     . SER B 1 179 ? 26.464 -16.441 43.379  1.00 17.65 ? 170 SER B C     1 
ATOM   4045 O O     . SER B 1 179 ? 27.497 -15.884 43.001  1.00 19.08 ? 170 SER B O     1 
ATOM   4046 C CB    . SER B 1 179 ? 24.324 -15.823 42.222  1.00 19.71 ? 170 SER B CB    1 
ATOM   4047 O OG    . SER B 1 179 ? 23.415 -16.196 41.207  1.00 20.52 ? 170 SER B OG    1 
ATOM   4048 N N     . ALA B 1 180 ? 26.225 -16.699 44.676  1.00 15.75 ? 171 ALA B N     1 
ATOM   4049 C CA    . ALA B 1 180 ? 27.225 -16.385 45.691  1.00 18.50 ? 171 ALA B CA    1 
ATOM   4050 C C     . ALA B 1 180 ? 28.539 -17.104 45.410  1.00 18.30 ? 171 ALA B C     1 
ATOM   4051 O O     . ALA B 1 180 ? 29.620 -16.513 45.497  1.00 17.38 ? 171 ALA B O     1 
ATOM   4052 C CB    . ALA B 1 180 ? 26.699 -16.790 47.065  1.00 15.65 ? 171 ALA B CB    1 
ATOM   4053 N N     . LEU B 1 181 ? 28.455 -18.402 45.113  1.00 19.06 ? 172 LEU B N     1 
ATOM   4054 C CA    . LEU B 1 181 ? 29.640 -19.174 44.747  1.00 20.72 ? 172 LEU B CA    1 
ATOM   4055 C C     . LEU B 1 181 ? 30.290 -18.619 43.490  1.00 16.61 ? 172 LEU B C     1 
ATOM   4056 O O     . LEU B 1 181 ? 31.518 -18.534 43.393  1.00 19.34 ? 172 LEU B O     1 
ATOM   4057 C CB    . LEU B 1 181 ? 29.252 -20.645 44.550  1.00 17.72 ? 172 LEU B CB    1 
ATOM   4058 C CG    . LEU B 1 181 ? 28.966 -21.318 45.906  1.00 19.40 ? 172 LEU B CG    1 
ATOM   4059 C CD1   . LEU B 1 181 ? 28.267 -22.667 45.676  1.00 23.54 ? 172 LEU B CD1   1 
ATOM   4060 C CD2   . LEU B 1 181 ? 30.255 -21.455 46.717  1.00 22.63 ? 172 LEU B CD2   1 
ATOM   4061 N N     . ASN B 1 182 ? 29.481 -18.258 42.502  1.00 18.18 ? 173 ASN B N     1 
ATOM   4062 C CA    . ASN B 1 182 ? 30.038 -17.696 41.276  1.00 17.78 ? 173 ASN B CA    1 
ATOM   4063 C C     . ASN B 1 182 ? 30.788 -16.397 41.559  1.00 17.07 ? 173 ASN B C     1 
ATOM   4064 O O     . ASN B 1 182 ? 31.881 -16.160 41.011  1.00 21.20 ? 173 ASN B O     1 
ATOM   4065 C CB    . ASN B 1 182 ? 28.910 -17.495 40.270  1.00 18.14 ? 173 ASN B CB    1 
ATOM   4066 C CG    . ASN B 1 182 ? 28.588 -18.739 39.525  1.00 28.06 ? 173 ASN B CG    1 
ATOM   4067 O OD1   . ASN B 1 182 ? 29.192 -19.787 39.753  1.00 22.26 ? 173 ASN B OD1   1 
ATOM   4068 N ND2   . ASN B 1 182 ? 27.616 -18.652 38.636  1.00 28.92 ? 173 ASN B ND2   1 
ATOM   4069 N N     . ALA B 1 183 ? 30.222 -15.535 42.424  1.00 16.89 ? 174 ALA B N     1 
ATOM   4070 C CA    . ALA B 1 183 ? 30.919 -14.297 42.788  1.00 16.97 ? 174 ALA B CA    1 
ATOM   4071 C C     . ALA B 1 183 ? 32.294 -14.590 43.386  1.00 17.94 ? 174 ALA B C     1 
ATOM   4072 O O     . ALA B 1 183 ? 33.284 -13.931 43.041  1.00 19.69 ? 174 ALA B O     1 
ATOM   4073 C CB    . ALA B 1 183 ? 30.072 -13.464 43.763  1.00 15.87 ? 174 ALA B CB    1 
ATOM   4074 N N     . ILE B 1 184 ? 32.389 -15.590 44.267  1.00 19.91 ? 175 ILE B N     1 
ATOM   4075 C CA    . ILE B 1 184 ? 33.690 -15.901 44.855  1.00 19.48 ? 175 ILE B CA    1 
ATOM   4076 C C     . ILE B 1 184 ? 34.641 -16.399 43.770  1.00 21.08 ? 175 ILE B C     1 
ATOM   4077 O O     . ILE B 1 184 ? 35.812 -15.997 43.714  1.00 21.14 ? 175 ILE B O     1 
ATOM   4078 C CB    . ILE B 1 184 ? 33.539 -16.920 46.000  1.00 19.21 ? 175 ILE B CB    1 
ATOM   4079 C CG1   . ILE B 1 184 ? 32.715 -16.355 47.169  1.00 23.05 ? 175 ILE B CG1   1 
ATOM   4080 C CG2   . ILE B 1 184 ? 34.901 -17.380 46.505  1.00 22.26 ? 175 ILE B CG2   1 
ATOM   4081 C CD1   . ILE B 1 184 ? 33.299 -15.142 47.779  1.00 24.09 ? 175 ILE B CD1   1 
ATOM   4082 N N     . GLU B 1 185 ? 34.132 -17.233 42.857  1.00 22.57 ? 176 GLU B N     1 
ATOM   4083 C CA    . GLU B 1 185 ? 34.935 -17.676 41.721  1.00 23.96 ? 176 GLU B CA    1 
ATOM   4084 C C     . GLU B 1 185 ? 35.478 -16.504 40.896  1.00 23.94 ? 176 GLU B C     1 
ATOM   4085 O O     . GLU B 1 185 ? 36.621 -16.549 40.411  1.00 29.23 ? 176 GLU B O     1 
ATOM   4086 C CB    . GLU B 1 185 ? 34.101 -18.603 40.849  1.00 24.21 ? 176 GLU B CB    1 
ATOM   4087 C CG    . GLU B 1 185 ? 34.922 -19.341 39.782  1.00 26.28 ? 176 GLU B CG    1 
ATOM   4088 C CD    . GLU B 1 185 ? 34.046 -20.264 38.946  1.00 41.20 ? 176 GLU B CD    1 
ATOM   4089 O OE1   . GLU B 1 185 ? 33.094 -20.849 39.516  1.00 38.67 ? 176 GLU B OE1   1 
ATOM   4090 O OE2   . GLU B 1 185 ? 34.302 -20.397 37.727  1.00 45.86 ? 176 GLU B OE2   1 
ATOM   4091 N N     . ALA B 1 186 ? 34.662 -15.477 40.665  1.00 21.54 ? 177 ALA B N     1 
ATOM   4092 C CA    . ALA B 1 186 ? 35.111 -14.300 39.926  1.00 20.81 ? 177 ALA B CA    1 
ATOM   4093 C C     . ALA B 1 186 ? 36.104 -13.440 40.705  1.00 21.08 ? 177 ALA B C     1 
ATOM   4094 O O     . ALA B 1 186 ? 36.705 -12.529 40.120  1.00 24.58 ? 177 ALA B O     1 
ATOM   4095 C CB    . ALA B 1 186 ? 33.899 -13.469 39.530  1.00 17.23 ? 177 ALA B CB    1 
ATOM   4096 N N     . GLY B 1 187 ? 36.302 -13.706 41.996  1.00 20.19 ? 178 GLY B N     1 
ATOM   4097 C CA    . GLY B 1 187 ? 37.247 -12.972 42.800  1.00 22.96 ? 178 GLY B CA    1 
ATOM   4098 C C     . GLY B 1 187 ? 36.642 -11.906 43.700  1.00 16.50 ? 178 GLY B C     1 
ATOM   4099 O O     . GLY B 1 187 ? 37.388 -11.235 44.416  1.00 19.37 ? 178 GLY B O     1 
ATOM   4100 N N     . PHE B 1 188 ? 35.326 -11.729 43.677  1.00 16.33 ? 179 PHE B N     1 
ATOM   4101 C CA    . PHE B 1 188 ? 34.690 -10.795 44.595  1.00 16.03 ? 179 PHE B CA    1 
ATOM   4102 C C     . PHE B 1 188 ? 35.080 -11.132 46.027  1.00 22.39 ? 179 PHE B C     1 
ATOM   4103 O O     . PHE B 1 188 ? 35.256 -12.299 46.383  1.00 21.27 ? 179 PHE B O     1 
ATOM   4104 C CB    . PHE B 1 188 ? 33.165 -10.855 44.461  1.00 13.31 ? 179 PHE B CB    1 
ATOM   4105 C CG    . PHE B 1 188 ? 32.656 -10.065 43.297  1.00 17.92 ? 179 PHE B CG    1 
ATOM   4106 C CD1   . PHE B 1 188 ? 32.626 -8.662  43.358  1.00 18.33 ? 179 PHE B CD1   1 
ATOM   4107 C CD2   . PHE B 1 188 ? 32.268 -10.711 42.143  1.00 17.74 ? 179 PHE B CD2   1 
ATOM   4108 C CE1   . PHE B 1 188 ? 32.183 -7.906  42.264  1.00 19.41 ? 179 PHE B CE1   1 
ATOM   4109 C CE2   . PHE B 1 188 ? 31.823 -9.977  41.020  1.00 16.62 ? 179 PHE B CE2   1 
ATOM   4110 C CZ    . PHE B 1 188 ? 31.785 -8.570  41.091  1.00 19.20 ? 179 PHE B CZ    1 
ATOM   4111 N N     . ASP B 1 189 ? 35.240 -10.089 46.832  1.00 19.21 ? 180 ASP B N     1 
ATOM   4112 C CA    . ASP B 1 189 ? 35.506 -10.265 48.250  1.00 17.32 ? 180 ASP B CA    1 
ATOM   4113 C C     . ASP B 1 189 ? 34.284 -10.807 48.985  1.00 21.21 ? 180 ASP B C     1 
ATOM   4114 O O     . ASP B 1 189 ? 34.425 -11.543 49.958  1.00 20.91 ? 180 ASP B O     1 
ATOM   4115 C CB    . ASP B 1 189 ? 35.975 -8.926  48.809  1.00 16.06 ? 180 ASP B CB    1 
ATOM   4116 C CG    . ASP B 1 189 ? 37.256 -8.501  48.184  1.00 21.38 ? 180 ASP B CG    1 
ATOM   4117 O OD1   . ASP B 1 189 ? 38.240 -9.237  48.446  1.00 22.60 ? 180 ASP B OD1   1 
ATOM   4118 O OD2   . ASP B 1 189 ? 37.270 -7.536  47.353  1.00 21.25 ? 180 ASP B OD2   1 
ATOM   4119 N N     . GLY B 1 190 ? 33.092 -10.504 48.499  1.00 19.36 ? 181 GLY B N     1 
ATOM   4120 C CA    . GLY B 1 190 ? 31.875 -10.948 49.133  1.00 16.53 ? 181 GLY B CA    1 
ATOM   4121 C C     . GLY B 1 190 ? 30.680 -10.591 48.278  1.00 15.90 ? 181 GLY B C     1 
ATOM   4122 O O     . GLY B 1 190 ? 30.818 -10.079 47.165  1.00 15.01 ? 181 GLY B O     1 
ATOM   4123 N N     . ILE B 1 191 ? 29.498 -10.825 48.832  1.00 15.29 ? 182 ILE B N     1 
ATOM   4124 C CA    . ILE B 1 191 ? 28.245 -10.449 48.192  1.00 14.87 ? 182 ILE B CA    1 
ATOM   4125 C C     . ILE B 1 191 ? 27.364 -9.664  49.159  1.00 17.72 ? 182 ILE B C     1 
ATOM   4126 O O     . ILE B 1 191 ? 27.439 -9.801  50.392  1.00 15.24 ? 182 ILE B O     1 
ATOM   4127 C CB    . ILE B 1 191 ? 27.467 -11.673 47.667  1.00 16.44 ? 182 ILE B CB    1 
ATOM   4128 C CG1   . ILE B 1 191 ? 27.033 -12.570 48.833  1.00 14.64 ? 182 ILE B CG1   1 
ATOM   4129 C CG2   . ILE B 1 191 ? 28.303 -12.505 46.736  1.00 14.61 ? 182 ILE B CG2   1 
ATOM   4130 C CD1   . ILE B 1 191 ? 25.629 -12.345 49.266  1.00 16.75 ? 182 ILE B CD1   1 
ATOM   4131 N N     . GLU B 1 192 ? 26.454 -8.890  48.579  1.00 14.28 ? 183 GLU B N     1 
ATOM   4132 C CA    . GLU B 1 192 ? 25.374 -8.259  49.327  1.00 12.49 ? 183 GLU B CA    1 
ATOM   4133 C C     . GLU B 1 192 ? 24.036 -8.811  48.862  1.00 13.82 ? 183 GLU B C     1 
ATOM   4134 O O     . GLU B 1 192 ? 23.754 -8.869  47.663  1.00 17.47 ? 183 GLU B O     1 
ATOM   4135 C CB    . GLU B 1 192 ? 25.381 -6.738  49.149  1.00 14.39 ? 183 GLU B CB    1 
ATOM   4136 C CG    . GLU B 1 192 ? 24.263 -6.046  49.925  1.00 12.65 ? 183 GLU B CG    1 
ATOM   4137 C CD    . GLU B 1 192 ? 24.351 -4.517  49.820  1.00 16.26 ? 183 GLU B CD    1 
ATOM   4138 O OE1   . GLU B 1 192 ? 25.080 -3.892  50.606  1.00 17.97 ? 183 GLU B OE1   1 
ATOM   4139 O OE2   . GLU B 1 192 ? 23.707 -3.917  48.930  1.00 18.27 ? 183 GLU B OE2   1 
ATOM   4140 N N     . ILE B 1 193 ? 23.186 -9.156  49.807  1.00 15.21 ? 184 ILE B N     1 
ATOM   4141 C CA    . ILE B 1 193 ? 21.836 -9.585  49.473  1.00 11.46 ? 184 ILE B CA    1 
ATOM   4142 C C     . ILE B 1 193 ? 20.963 -8.338  49.301  1.00 16.62 ? 184 ILE B C     1 
ATOM   4143 O O     . ILE B 1 193 ? 20.807 -7.556  50.241  1.00 17.07 ? 184 ILE B O     1 
ATOM   4144 C CB    . ILE B 1 193 ? 21.277 -10.514 50.549  1.00 13.32 ? 184 ILE B CB    1 
ATOM   4145 C CG1   . ILE B 1 193 ? 22.051 -11.847 50.616  1.00 14.27 ? 184 ILE B CG1   1 
ATOM   4146 C CG2   . ILE B 1 193 ? 19.787 -10.762 50.257  1.00 14.80 ? 184 ILE B CG2   1 
ATOM   4147 C CD1   . ILE B 1 193 ? 22.040 -12.601 49.231  1.00 16.80 ? 184 ILE B CD1   1 
ATOM   4148 N N     . HIS B 1 194 ? 20.377 -8.153  48.102  1.00 15.13 ? 185 HIS B N     1 
ATOM   4149 C CA    . HIS B 1 194 ? 19.507 -7.001  47.851  1.00 15.76 ? 185 HIS B CA    1 
ATOM   4150 C C     . HIS B 1 194 ? 18.127 -7.342  48.424  1.00 15.95 ? 185 HIS B C     1 
ATOM   4151 O O     . HIS B 1 194 ? 17.319 -8.031  47.779  1.00 16.25 ? 185 HIS B O     1 
ATOM   4152 C CB    . HIS B 1 194 ? 19.372 -6.677  46.355  1.00 13.88 ? 185 HIS B CB    1 
ATOM   4153 C CG    . HIS B 1 194 ? 18.734 -5.332  46.062  1.00 16.60 ? 185 HIS B CG    1 
ATOM   4154 N ND1   . HIS B 1 194 ? 17.720 -4.798  46.838  1.00 15.32 ? 185 HIS B ND1   1 
ATOM   4155 C CD2   . HIS B 1 194 ? 18.799 -4.544  44.952  1.00 13.79 ? 185 HIS B CD2   1 
ATOM   4156 C CE1   . HIS B 1 194 ? 17.314 -3.655  46.304  1.00 15.75 ? 185 HIS B CE1   1 
ATOM   4157 N NE2   . HIS B 1 194 ? 17.918 -3.509  45.133  1.00 15.80 ? 185 HIS B NE2   1 
ATOM   4158 N N     . GLY B 1 195 ? 17.821 -6.825  49.605  1.00 14.17 ? 186 GLY B N     1 
ATOM   4159 C CA    . GLY B 1 195 ? 16.511 -7.079  50.167  1.00 13.94 ? 186 GLY B CA    1 
ATOM   4160 C C     . GLY B 1 195 ? 15.698 -5.804  50.295  1.00 16.26 ? 186 GLY B C     1 
ATOM   4161 O O     . GLY B 1 195 ? 14.845 -5.686  51.182  1.00 18.24 ? 186 GLY B O     1 
ATOM   4162 N N     . ALA B 1 196 ? 15.941 -4.849  49.406  1.00 13.16 ? 187 ALA B N     1 
ATOM   4163 C CA    . ALA B 1 196 ? 15.375 -3.515  49.585  1.00 14.26 ? 187 ALA B CA    1 
ATOM   4164 C C     . ALA B 1 196 ? 14.419 -3.168  48.430  1.00 19.56 ? 187 ALA B C     1 
ATOM   4165 O O     . ALA B 1 196 ? 14.219 -3.952  47.506  1.00 14.61 ? 187 ALA B O     1 
ATOM   4166 C CB    . ALA B 1 196 ? 16.500 -2.496  49.671  1.00 15.47 ? 187 ALA B CB    1 
ATOM   4167 N N     . HIS B 1 197 ? 13.822 -1.969  48.520  1.00 15.08 ? 188 HIS B N     1 
ATOM   4168 C CA    . HIS B 1 197 ? 13.202 -1.267  47.385  1.00 15.40 ? 188 HIS B CA    1 
ATOM   4169 C C     . HIS B 1 197 ? 12.070 -2.020  46.703  1.00 17.53 ? 188 HIS B C     1 
ATOM   4170 O O     . HIS B 1 197 ? 11.838 -1.814  45.510  1.00 17.65 ? 188 HIS B O     1 
ATOM   4171 C CB    . HIS B 1 197 ? 14.277 -0.902  46.338  1.00 14.62 ? 188 HIS B CB    1 
ATOM   4172 C CG    . HIS B 1 197 ? 15.376 -0.038  46.871  1.00 18.45 ? 188 HIS B CG    1 
ATOM   4173 N ND1   . HIS B 1 197 ? 16.708 -0.254  46.583  1.00 17.50 ? 188 HIS B ND1   1 
ATOM   4174 C CD2   . HIS B 1 197 ? 15.343 1.051   47.679  1.00 18.32 ? 188 HIS B CD2   1 
ATOM   4175 C CE1   . HIS B 1 197 ? 17.445 0.656   47.198  1.00 19.16 ? 188 HIS B CE1   1 
ATOM   4176 N NE2   . HIS B 1 197 ? 16.637 1.468   47.856  1.00 17.88 ? 188 HIS B NE2   1 
ATOM   4177 N N     . GLY B 1 198 ? 11.352 -2.903  47.406  1.00 17.29 ? 189 GLY B N     1 
ATOM   4178 C CA    . GLY B 1 198 ? 10.166 -3.522  46.793  1.00 16.65 ? 189 GLY B CA    1 
ATOM   4179 C C     . GLY B 1 198 ? 10.455 -4.620  45.792  1.00 17.57 ? 189 GLY B C     1 
ATOM   4180 O O     . GLY B 1 198 ? 9.549  -5.025  45.035  1.00 14.93 ? 189 GLY B O     1 
ATOM   4181 N N     . TYR B 1 199 ? 11.686 -5.093  45.738  1.00 12.64 ? 190 TYR B N     1 
ATOM   4182 C CA    . TYR B 1 199 ? 12.030 -6.233  44.901  1.00 13.48 ? 190 TYR B CA    1 
ATOM   4183 C C     . TYR B 1 199 ? 11.646 -7.546  45.600  1.00 14.73 ? 190 TYR B C     1 
ATOM   4184 O O     . TYR B 1 199 ? 10.824 -7.531  46.528  1.00 16.67 ? 190 TYR B O     1 
ATOM   4185 C CB    . TYR B 1 199 ? 13.504 -6.101  44.520  1.00 13.54 ? 190 TYR B CB    1 
ATOM   4186 C CG    . TYR B 1 199 ? 13.688 -4.888  43.611  1.00 16.00 ? 190 TYR B CG    1 
ATOM   4187 C CD1   . TYR B 1 199 ? 12.941 -4.755  42.445  1.00 15.66 ? 190 TYR B CD1   1 
ATOM   4188 C CD2   . TYR B 1 199 ? 14.556 -3.838  43.951  1.00 15.19 ? 190 TYR B CD2   1 
ATOM   4189 C CE1   . TYR B 1 199 ? 13.099 -3.605  41.615  1.00 16.15 ? 190 TYR B CE1   1 
ATOM   4190 C CE2   . TYR B 1 199 ? 14.718 -2.721  43.126  1.00 16.97 ? 190 TYR B CE2   1 
ATOM   4191 C CZ    . TYR B 1 199 ? 13.993 -2.608  41.960  1.00 18.54 ? 190 TYR B CZ    1 
ATOM   4192 O OH    . TYR B 1 199 ? 14.184 -1.474  41.146  1.00 18.74 ? 190 TYR B OH    1 
ATOM   4193 N N     . LEU B 1 200 ? 12.175 -8.681  45.126  1.00 14.89 ? 191 LEU B N     1 
ATOM   4194 C CA    . LEU B 1 200 ? 11.554 -9.963  45.459  1.00 14.29 ? 191 LEU B CA    1 
ATOM   4195 C C     . LEU B 1 200 ? 11.573 -10.198 46.960  1.00 13.79 ? 191 LEU B C     1 
ATOM   4196 O O     . LEU B 1 200 ? 10.557 -10.548 47.560  1.00 15.45 ? 191 LEU B O     1 
ATOM   4197 C CB    . LEU B 1 200 ? 12.270 -11.098 44.732  1.00 15.61 ? 191 LEU B CB    1 
ATOM   4198 C CG    . LEU B 1 200 ? 11.782 -12.504 45.145  1.00 17.63 ? 191 LEU B CG    1 
ATOM   4199 C CD1   . LEU B 1 200 ? 10.309 -12.686 44.769  1.00 18.78 ? 191 LEU B CD1   1 
ATOM   4200 C CD2   . LEU B 1 200 ? 12.634 -13.531 44.456  1.00 16.99 ? 191 LEU B CD2   1 
ATOM   4201 N N     . ILE B 1 201 ? 12.721 -9.974  47.594  1.00 13.49 ? 192 ILE B N     1 
ATOM   4202 C CA    . ILE B 1 201 ? 12.776 -10.216 49.029  1.00 15.25 ? 192 ILE B CA    1 
ATOM   4203 C C     . ILE B 1 201 ? 11.817 -9.287  49.766  1.00 16.77 ? 192 ILE B C     1 
ATOM   4204 O O     . ILE B 1 201 ? 11.064 -9.718  50.633  1.00 15.76 ? 192 ILE B O     1 
ATOM   4205 C CB    . ILE B 1 201 ? 14.224 -10.086 49.518  1.00 12.93 ? 192 ILE B CB    1 
ATOM   4206 C CG1   . ILE B 1 201 ? 15.030 -11.282 48.956  1.00 15.86 ? 192 ILE B CG1   1 
ATOM   4207 C CG2   . ILE B 1 201 ? 14.219 -10.001 51.058  1.00 18.31 ? 192 ILE B CG2   1 
ATOM   4208 C CD1   . ILE B 1 201 ? 16.516 -11.258 49.247  1.00 14.42 ? 192 ILE B CD1   1 
ATOM   4209 N N     . ASP B 1 202 ? 11.772 -8.010  49.378  1.00 14.12 ? 193 ASP B N     1 
ATOM   4210 C CA    . ASP B 1 202 ? 10.835 -7.076  50.006  1.00 17.17 ? 193 ASP B CA    1 
ATOM   4211 C C     . ASP B 1 202 ? 9.368  -7.472  49.771  1.00 16.30 ? 193 ASP B C     1 
ATOM   4212 O O     . ASP B 1 202 ? 8.497  -7.177  50.609  1.00 17.20 ? 193 ASP B O     1 
ATOM   4213 C CB    . ASP B 1 202 ? 11.127 -5.673  49.474  1.00 20.46 ? 193 ASP B CB    1 
ATOM   4214 C CG    . ASP B 1 202 ? 10.996 -4.603  50.537  1.00 22.36 ? 193 ASP B CG    1 
ATOM   4215 O OD1   . ASP B 1 202 ? 11.188 -4.882  51.744  1.00 17.74 ? 193 ASP B OD1   1 
ATOM   4216 O OD2   . ASP B 1 202 ? 10.729 -3.451  50.157  1.00 24.70 ? 193 ASP B OD2   1 
ATOM   4217 N N     . GLN B 1 203 ? 9.066  -8.143  48.653  1.00 14.49 ? 194 GLN B N     1 
ATOM   4218 C CA    . GLN B 1 203 ? 7.701  -8.620  48.417  1.00 14.58 ? 194 GLN B CA    1 
ATOM   4219 C C     . GLN B 1 203 ? 7.298  -9.737  49.374  1.00 18.08 ? 194 GLN B C     1 
ATOM   4220 O O     . GLN B 1 203 ? 6.099  -9.962  49.577  1.00 18.70 ? 194 GLN B O     1 
ATOM   4221 C CB    . GLN B 1 203 ? 7.543  -9.094  46.948  1.00 16.63 ? 194 GLN B CB    1 
ATOM   4222 C CG    . GLN B 1 203 ? 7.679  -7.946  45.913  1.00 16.17 ? 194 GLN B CG    1 
ATOM   4223 C CD    . GLN B 1 203 ? 8.304  -8.385  44.583  1.00 15.80 ? 194 GLN B CD    1 
ATOM   4224 O OE1   . GLN B 1 203 ? 8.028  -9.490  44.094  1.00 18.09 ? 194 GLN B OE1   1 
ATOM   4225 N NE2   . GLN B 1 203 ? 9.127  -7.515  43.982  1.00 13.98 ? 194 GLN B NE2   1 
ATOM   4226 N N     . PHE B 1 204 ? 8.264  -10.448 49.957  1.00 16.29 ? 195 PHE B N     1 
ATOM   4227 C CA    . PHE B 1 204 ? 7.959  -11.369 51.043  1.00 15.73 ? 195 PHE B CA    1 
ATOM   4228 C C     . PHE B 1 204 ? 7.936  -10.645 52.383  1.00 16.38 ? 195 PHE B C     1 
ATOM   4229 O O     . PHE B 1 204 ? 7.098  -10.970 53.225  1.00 19.70 ? 195 PHE B O     1 
ATOM   4230 C CB    . PHE B 1 204 ? 8.971  -12.514 51.078  1.00 17.87 ? 195 PHE B CB    1 
ATOM   4231 C CG    . PHE B 1 204 ? 8.662  -13.603 50.082  1.00 18.19 ? 195 PHE B CG    1 
ATOM   4232 C CD1   . PHE B 1 204 ? 9.087  -13.488 48.763  1.00 17.51 ? 195 PHE B CD1   1 
ATOM   4233 C CD2   . PHE B 1 204 ? 7.865  -14.689 50.449  1.00 17.27 ? 195 PHE B CD2   1 
ATOM   4234 C CE1   . PHE B 1 204 ? 8.795  -14.473 47.836  1.00 17.98 ? 195 PHE B CE1   1 
ATOM   4235 C CE2   . PHE B 1 204 ? 7.573  -15.685 49.566  1.00 20.71 ? 195 PHE B CE2   1 
ATOM   4236 C CZ    . PHE B 1 204 ? 8.035  -15.578 48.218  1.00 22.59 ? 195 PHE B CZ    1 
ATOM   4237 N N     . LEU B 1 205 ? 8.783  -9.622  52.562  1.00 17.39 ? 196 LEU B N     1 
ATOM   4238 C CA    . LEU B 1 205 ? 8.895  -8.986  53.886  1.00 15.41 ? 196 LEU B CA    1 
ATOM   4239 C C     . LEU B 1 205 ? 7.686  -8.110  54.205  1.00 21.45 ? 196 LEU B C     1 
ATOM   4240 O O     . LEU B 1 205 ? 7.196  -8.122  55.335  1.00 20.51 ? 196 LEU B O     1 
ATOM   4241 C CB    . LEU B 1 205 ? 10.163 -8.138  53.959  1.00 13.02 ? 196 LEU B CB    1 
ATOM   4242 C CG    . LEU B 1 205 ? 11.526 -8.740  54.187  1.00 14.05 ? 196 LEU B CG    1 
ATOM   4243 C CD1   . LEU B 1 205 ? 12.602 -7.667  54.021  1.00 16.89 ? 196 LEU B CD1   1 
ATOM   4244 C CD2   . LEU B 1 205 ? 11.607 -9.438  55.577  1.00 18.50 ? 196 LEU B CD2   1 
ATOM   4245 N N     . LYS B 1 206 ? 7.219  -7.312  53.247  1.00 18.64 ? 197 LYS B N     1 
ATOM   4246 C CA    . LYS B 1 206 ? 6.303  -6.218  53.560  1.00 21.28 ? 197 LYS B CA    1 
ATOM   4247 C C     . LYS B 1 206 ? 4.857  -6.721  53.608  1.00 23.20 ? 197 LYS B C     1 
ATOM   4248 O O     . LYS B 1 206 ? 4.390  -7.399  52.686  1.00 21.84 ? 197 LYS B O     1 
ATOM   4249 C CB    . LYS B 1 206 ? 6.459  -5.091  52.536  1.00 19.22 ? 197 LYS B CB    1 
ATOM   4250 C CG    . LYS B 1 206 ? 7.863  -4.488  52.481  1.00 22.09 ? 197 LYS B CG    1 
ATOM   4251 C CD    . LYS B 1 206 ? 8.001  -3.215  53.319  1.00 25.61 ? 197 LYS B CD    1 
ATOM   4252 C CE    . LYS B 1 206 ? 9.445  -2.666  53.364  1.00 22.94 ? 197 LYS B CE    1 
ATOM   4253 N NZ    . LYS B 1 206 ? 9.737  -1.683  52.228  1.00 26.33 ? 197 LYS B NZ    1 
ATOM   4254 N N     . ASP B 1 207 ? 4.143  -6.397  54.685  1.00 21.35 ? 198 ASP B N     1 
ATOM   4255 C CA    . ASP B 1 207 ? 2.782  -6.914  54.774  1.00 23.68 ? 198 ASP B CA    1 
ATOM   4256 C C     . ASP B 1 207 ? 1.814  -6.182  53.845  1.00 21.66 ? 198 ASP B C     1 
ATOM   4257 O O     . ASP B 1 207 ? 0.692  -6.659  53.675  1.00 26.90 ? 198 ASP B O     1 
ATOM   4258 C CB    . ASP B 1 207 ? 2.267  -6.914  56.231  1.00 29.66 ? 198 ASP B CB    1 
ATOM   4259 C CG    . ASP B 1 207 ? 2.208  -5.538  56.871  1.00 27.84 ? 198 ASP B CG    1 
ATOM   4260 O OD1   . ASP B 1 207 ? 2.497  -4.513  56.232  1.00 24.11 ? 198 ASP B OD1   1 
ATOM   4261 O OD2   . ASP B 1 207 ? 1.882  -5.485  58.088  1.00 33.94 ? 198 ASP B OD2   1 
ATOM   4262 N N     . GLY B 1 208 ? 2.211  -5.048  53.257  1.00 23.36 ? 199 GLY B N     1 
ATOM   4263 C CA    . GLY B 1 208 ? 1.428  -4.461  52.179  1.00 26.29 ? 199 GLY B CA    1 
ATOM   4264 C C     . GLY B 1 208 ? 1.347  -5.343  50.945  1.00 27.26 ? 199 GLY B C     1 
ATOM   4265 O O     . GLY B 1 208 ? 0.400  -5.216  50.159  1.00 31.25 ? 199 GLY B O     1 
ATOM   4266 N N     . ILE B 1 209 ? 2.313  -6.236  50.757  1.00 21.88 ? 200 ILE B N     1 
ATOM   4267 C CA    . ILE B 1 209 ? 2.410  -7.076  49.563  1.00 20.88 ? 200 ILE B CA    1 
ATOM   4268 C C     . ILE B 1 209 ? 2.086  -8.525  49.881  1.00 29.17 ? 200 ILE B C     1 
ATOM   4269 O O     . ILE B 1 209 ? 1.304  -9.167  49.178  1.00 33.95 ? 200 ILE B O     1 
ATOM   4270 C CB    . ILE B 1 209 ? 3.809  -6.966  48.918  1.00 21.92 ? 200 ILE B CB    1 
ATOM   4271 C CG1   . ILE B 1 209 ? 4.084  -5.545  48.405  1.00 23.75 ? 200 ILE B CG1   1 
ATOM   4272 C CG2   . ILE B 1 209 ? 3.981  -8.047  47.813  1.00 24.20 ? 200 ILE B CG2   1 
ATOM   4273 C CD1   . ILE B 1 209 ? 5.530  -5.283  47.930  1.00 17.33 ? 200 ILE B CD1   1 
ATOM   4274 N N     . ASN B 1 210 ? 2.673  -9.055  50.953  1.00 23.21 ? 201 ASN B N     1 
ATOM   4275 C CA    . ASN B 1 210 ? 2.659  -10.487 51.218  1.00 22.14 ? 201 ASN B CA    1 
ATOM   4276 C C     . ASN B 1 210 ? 1.328  -10.839 51.887  1.00 27.13 ? 201 ASN B C     1 
ATOM   4277 O O     . ASN B 1 210 ? 1.152  -10.676 53.094  1.00 31.05 ? 201 ASN B O     1 
ATOM   4278 C CB    . ASN B 1 210 ? 3.886  -10.865 52.048  1.00 19.64 ? 201 ASN B CB    1 
ATOM   4279 C CG    . ASN B 1 210 ? 3.984  -12.360 52.314  1.00 18.50 ? 201 ASN B CG    1 
ATOM   4280 O OD1   . ASN B 1 210 ? 3.029  -13.091 52.134  1.00 23.53 ? 201 ASN B OD1   1 
ATOM   4281 N ND2   . ASN B 1 210 ? 5.138  -12.808 52.786  1.00 18.14 ? 201 ASN B ND2   1 
ATOM   4282 N N     . ASP B 1 211 ? 0.389  -11.331 51.076  1.00 31.72 ? 202 ASP B N     1 
ATOM   4283 C CA    . ASP B 1 211 ? -0.887 -11.858 51.534  1.00 31.85 ? 202 ASP B CA    1 
ATOM   4284 C C     . ASP B 1 211 ? -0.921 -13.389 51.523  1.00 36.28 ? 202 ASP B C     1 
ATOM   4285 O O     . ASP B 1 211 ? -1.982 -13.979 51.284  1.00 37.01 ? 202 ASP B O     1 
ATOM   4286 C CB    . ASP B 1 211 ? -2.035 -11.314 50.675  1.00 34.82 ? 202 ASP B CB    1 
ATOM   4287 C CG    . ASP B 1 211 ? -1.803 -11.484 49.152  1.00 40.53 ? 202 ASP B CG    1 
ATOM   4288 O OD1   . ASP B 1 211 ? -0.817 -12.132 48.703  1.00 39.25 ? 202 ASP B OD1   1 
ATOM   4289 O OD2   . ASP B 1 211 ? -2.655 -10.977 48.382  1.00 44.18 ? 202 ASP B OD2   1 
ATOM   4290 N N     . ARG B 1 212 ? 0.213  -14.049 51.755  1.00 29.68 ? 203 ARG B N     1 
ATOM   4291 C CA    . ARG B 1 212 ? 0.240  -15.510 51.707  1.00 26.55 ? 203 ARG B CA    1 
ATOM   4292 C C     . ARG B 1 212 ? -0.393 -16.116 52.952  1.00 28.00 ? 203 ARG B C     1 
ATOM   4293 O O     . ARG B 1 212 ? -0.291 -15.582 54.060  1.00 27.23 ? 203 ARG B O     1 
ATOM   4294 C CB    . ARG B 1 212 ? 1.664  -16.051 51.585  1.00 21.92 ? 203 ARG B CB    1 
ATOM   4295 C CG    . ARG B 1 212 ? 2.410  -15.643 50.292  1.00 19.36 ? 203 ARG B CG    1 
ATOM   4296 C CD    . ARG B 1 212 ? 3.842  -16.113 50.335  1.00 20.91 ? 203 ARG B CD    1 
ATOM   4297 N NE    . ARG B 1 212 ? 3.948  -17.558 50.130  1.00 21.36 ? 203 ARG B NE    1 
ATOM   4298 C CZ    . ARG B 1 212 ? 4.244  -18.105 48.958  1.00 24.16 ? 203 ARG B CZ    1 
ATOM   4299 N NH1   . ARG B 1 212 ? 4.364  -17.371 47.873  1.00 19.99 ? 203 ARG B NH1   1 
ATOM   4300 N NH2   . ARG B 1 212 ? 4.433  -19.421 48.875  1.00 20.88 ? 203 ARG B NH2   1 
ATOM   4301 N N     . THR B 1 213 ? -0.992 -17.285 52.762  1.00 31.76 ? 204 THR B N     1 
ATOM   4302 C CA    . THR B 1 213 ? -1.590 -18.039 53.851  1.00 29.25 ? 204 THR B CA    1 
ATOM   4303 C C     . THR B 1 213 ? -0.825 -19.321 54.157  1.00 34.07 ? 204 THR B C     1 
ATOM   4304 O O     . THR B 1 213 ? -1.308 -20.150 54.934  1.00 35.74 ? 204 THR B O     1 
ATOM   4305 C CB    . THR B 1 213 ? -3.038 -18.371 53.510  1.00 32.48 ? 204 THR B CB    1 
ATOM   4306 O OG1   . THR B 1 213 ? -3.070 -19.027 52.233  1.00 39.32 ? 204 THR B OG1   1 
ATOM   4307 C CG2   . THR B 1 213 ? -3.858 -17.096 53.436  1.00 33.94 ? 204 THR B CG2   1 
ATOM   4308 N N     . ASP B 1 214 ? 0.356  -19.497 53.592  1.00 28.17 ? 205 ASP B N     1 
ATOM   4309 C CA    . ASP B 1 214 ? 1.183  -20.628 53.964  1.00 26.03 ? 205 ASP B CA    1 
ATOM   4310 C C     . ASP B 1 214 ? 2.251  -20.168 54.964  1.00 25.80 ? 205 ASP B C     1 
ATOM   4311 O O     . ASP B 1 214 ? 2.093  -19.135 55.637  1.00 24.26 ? 205 ASP B O     1 
ATOM   4312 C CB    . ASP B 1 214 ? 1.761  -21.262 52.701  1.00 24.50 ? 205 ASP B CB    1 
ATOM   4313 C CG    . ASP B 1 214 ? 2.817  -20.397 52.042  1.00 25.53 ? 205 ASP B CG    1 
ATOM   4314 O OD1   . ASP B 1 214 ? 3.018  -19.214 52.449  1.00 22.03 ? 205 ASP B OD1   1 
ATOM   4315 O OD2   . ASP B 1 214 ? 3.465  -20.938 51.123  1.00 21.52 ? 205 ASP B OD2   1 
ATOM   4316 N N     . GLU B 1 215 ? 3.348  -20.922 55.069  1.00 22.27 ? 206 GLU B N     1 
ATOM   4317 C CA    . GLU B 1 215 ? 4.335  -20.652 56.110  1.00 24.72 ? 206 GLU B CA    1 
ATOM   4318 C C     . GLU B 1 215 ? 5.230  -19.456 55.807  1.00 24.45 ? 206 GLU B C     1 
ATOM   4319 O O     . GLU B 1 215 ? 6.048  -19.079 56.659  1.00 24.65 ? 206 GLU B O     1 
ATOM   4320 C CB    . GLU B 1 215 ? 5.199  -21.893 56.375  1.00 27.36 ? 206 GLU B CB    1 
ATOM   4321 C CG    . GLU B 1 215 ? 6.074  -22.315 55.241  1.00 27.84 ? 206 GLU B CG    1 
ATOM   4322 C CD    . GLU B 1 215 ? 5.457  -23.449 54.433  1.00 36.54 ? 206 GLU B CD    1 
ATOM   4323 O OE1   . GLU B 1 215 ? 4.217  -23.426 54.215  1.00 34.44 ? 206 GLU B OE1   1 
ATOM   4324 O OE2   . GLU B 1 215 ? 6.216  -24.362 54.010  1.00 39.45 ? 206 GLU B OE2   1 
ATOM   4325 N N     . TYR B 1 216 ? 5.068  -18.817 54.651  1.00 23.09 ? 207 TYR B N     1 
ATOM   4326 C CA    . TYR B 1 216 ? 5.873  -17.653 54.279  1.00 20.80 ? 207 TYR B CA    1 
ATOM   4327 C C     . TYR B 1 216 ? 5.119  -16.344 54.401  1.00 20.69 ? 207 TYR B C     1 
ATOM   4328 O O     . TYR B 1 216 ? 5.642  -15.303 53.986  1.00 22.27 ? 207 TYR B O     1 
ATOM   4329 C CB    . TYR B 1 216 ? 6.402  -17.815 52.847  1.00 20.04 ? 207 TYR B CB    1 
ATOM   4330 C CG    . TYR B 1 216 ? 7.550  -18.792 52.788  1.00 21.41 ? 207 TYR B CG    1 
ATOM   4331 C CD1   . TYR B 1 216 ? 7.311  -20.151 52.660  1.00 22.31 ? 207 TYR B CD1   1 
ATOM   4332 C CD2   . TYR B 1 216 ? 8.871  -18.356 52.898  1.00 20.51 ? 207 TYR B CD2   1 
ATOM   4333 C CE1   . TYR B 1 216 ? 8.352  -21.060 52.591  1.00 24.52 ? 207 TYR B CE1   1 
ATOM   4334 C CE2   . TYR B 1 216 ? 9.918  -19.250 52.845  1.00 22.17 ? 207 TYR B CE2   1 
ATOM   4335 C CZ    . TYR B 1 216 ? 9.643  -20.610 52.695  1.00 24.12 ? 207 TYR B CZ    1 
ATOM   4336 O OH    . TYR B 1 216 ? 10.663 -21.518 52.637  1.00 23.36 ? 207 TYR B OH    1 
ATOM   4337 N N     . GLY B 1 217 ? 3.889  -16.361 54.926  1.00 21.68 ? 208 GLY B N     1 
ATOM   4338 C CA    . GLY B 1 217 ? 3.151  -15.130 55.104  1.00 22.64 ? 208 GLY B CA    1 
ATOM   4339 C C     . GLY B 1 217 ? 2.319  -15.141 56.367  1.00 27.22 ? 208 GLY B C     1 
ATOM   4340 O O     . GLY B 1 217 ? 2.234  -16.146 57.065  1.00 24.15 ? 208 GLY B O     1 
ATOM   4341 N N     . GLY B 1 218 ? 1.691  -13.992 56.629  1.00 31.88 ? 209 GLY B N     1 
ATOM   4342 C CA    . GLY B 1 218 ? 1.002  -13.738 57.898  1.00 33.38 ? 209 GLY B CA    1 
ATOM   4343 C C     . GLY B 1 218 ? 1.908  -13.004 58.890  1.00 32.93 ? 209 GLY B C     1 
ATOM   4344 O O     . GLY B 1 218 ? 2.236  -11.804 58.682  1.00 34.00 ? 209 GLY B O     1 
ATOM   4345 N N     . SER B 1 219 ? 2.347  -13.724 59.921  1.00 31.50 ? 210 SER B N     1 
ATOM   4346 C CA    . SER B 1 219 ? 3.158  -13.156 60.984  1.00 28.02 ? 210 SER B CA    1 
ATOM   4347 C C     . SER B 1 219 ? 4.449  -12.559 60.440  1.00 30.62 ? 210 SER B C     1 
ATOM   4348 O O     . SER B 1 219 ? 4.908  -12.887 59.334  1.00 26.03 ? 210 SER B O     1 
ATOM   4349 C CB    . SER B 1 219 ? 3.509  -14.228 62.015  1.00 27.94 ? 210 SER B CB    1 
ATOM   4350 O OG    . SER B 1 219 ? 4.129  -15.343 61.387  1.00 26.68 ? 210 SER B OG    1 
ATOM   4351 N N     . LEU B 1 220 ? 5.034  -11.665 61.242  1.00 27.31 ? 211 LEU B N     1 
ATOM   4352 C CA    . LEU B 1 220 ? 6.400  -11.212 60.997  1.00 26.60 ? 211 LEU B CA    1 
ATOM   4353 C C     . LEU B 1 220 ? 7.347  -12.384 60.833  1.00 31.04 ? 211 LEU B C     1 
ATOM   4354 O O     . LEU B 1 220 ? 8.251  -12.347 59.986  1.00 25.04 ? 211 LEU B O     1 
ATOM   4355 C CB    . LEU B 1 220 ? 6.893  -10.354 62.162  1.00 29.02 ? 211 LEU B CB    1 
ATOM   4356 C CG    . LEU B 1 220 ? 6.607  -8.877  62.186  1.00 32.27 ? 211 LEU B CG    1 
ATOM   4357 C CD1   . LEU B 1 220 ? 6.881  -8.363  63.601  1.00 26.31 ? 211 LEU B CD1   1 
ATOM   4358 C CD2   . LEU B 1 220 ? 7.430  -8.160  61.105  1.00 26.83 ? 211 LEU B CD2   1 
ATOM   4359 N N     . ALA B 1 221 ? 7.184  -13.426 61.668  1.00 27.56 ? 212 ALA B N     1 
ATOM   4360 C CA    . ALA B 1 221 ? 8.077  -14.573 61.578  1.00 24.43 ? 212 ALA B CA    1 
ATOM   4361 C C     . ALA B 1 221 ? 7.998  -15.196 60.202  1.00 25.56 ? 212 ALA B C     1 
ATOM   4362 O O     . ALA B 1 221 ? 9.021  -15.515 59.591  1.00 27.92 ? 212 ALA B O     1 
ATOM   4363 C CB    . ALA B 1 221 ? 7.720  -15.633 62.630  1.00 24.36 ? 212 ALA B CB    1 
ATOM   4364 N N     . ASN B 1 222 ? 6.774  -15.418 59.720  1.00 21.46 ? 213 ASN B N     1 
ATOM   4365 C CA    . ASN B 1 222 ? 6.615  -16.058 58.424  1.00 21.85 ? 213 ASN B CA    1 
ATOM   4366 C C     . ASN B 1 222 ? 7.096  -15.140 57.316  1.00 24.69 ? 213 ASN B C     1 
ATOM   4367 O O     . ASN B 1 222 ? 7.704  -15.593 56.344  1.00 21.70 ? 213 ASN B O     1 
ATOM   4368 C CB    . ASN B 1 222 ? 5.159  -16.460 58.220  1.00 21.55 ? 213 ASN B CB    1 
ATOM   4369 C CG    . ASN B 1 222 ? 4.755  -17.609 59.126  1.00 22.12 ? 213 ASN B CG    1 
ATOM   4370 O OD1   . ASN B 1 222 ? 5.574  -18.084 59.908  1.00 23.99 ? 213 ASN B OD1   1 
ATOM   4371 N ND2   . ASN B 1 222 ? 3.512  -18.069 59.008  1.00 24.75 ? 213 ASN B ND2   1 
ATOM   4372 N N     . ARG B 1 223 ? 6.876  -13.841 57.473  1.00 20.59 ? 214 ARG B N     1 
ATOM   4373 C CA    . ARG B 1 223 ? 7.306  -12.926 56.425  1.00 20.47 ? 214 ARG B CA    1 
ATOM   4374 C C     . ARG B 1 223 ? 8.816  -12.809 56.360  1.00 19.64 ? 214 ARG B C     1 
ATOM   4375 O O     . ARG B 1 223 ? 9.360  -12.495 55.297  1.00 20.00 ? 214 ARG B O     1 
ATOM   4376 C CB    . ARG B 1 223 ? 6.614  -11.573 56.634  1.00 24.01 ? 214 ARG B CB    1 
ATOM   4377 C CG    . ARG B 1 223 ? 5.150  -11.737 56.318  1.00 21.29 ? 214 ARG B CG    1 
ATOM   4378 C CD    . ARG B 1 223 ? 4.316  -10.532 56.633  1.00 31.97 ? 214 ARG B CD    1 
ATOM   4379 N NE    . ARG B 1 223 ? 5.117  -9.337  56.823  1.00 36.14 ? 214 ARG B NE    1 
ATOM   4380 C CZ    . ARG B 1 223 ? 5.053  -8.573  57.903  1.00 30.10 ? 214 ARG B CZ    1 
ATOM   4381 N NH1   . ARG B 1 223 ? 4.341  -8.927  58.962  1.00 35.05 ? 214 ARG B NH1   1 
ATOM   4382 N NH2   . ARG B 1 223 ? 5.724  -7.428  57.927  1.00 26.78 ? 214 ARG B NH2   1 
ATOM   4383 N N     . CYS B 1 224 ? 9.507  -13.096 57.449  1.00 16.20 ? 215 CYS B N     1 
ATOM   4384 C CA    . CYS B 1 224 ? 10.953 -13.041 57.443  1.00 20.44 ? 215 CYS B CA    1 
ATOM   4385 C C     . CYS B 1 224 ? 11.602 -14.344 57.014  1.00 19.37 ? 215 CYS B C     1 
ATOM   4386 O O     . CYS B 1 224 ? 12.824 -14.373 56.880  1.00 17.76 ? 215 CYS B O     1 
ATOM   4387 C CB    . CYS B 1 224 ? 11.475 -12.655 58.831  1.00 19.44 ? 215 CYS B CB    1 
ATOM   4388 S SG    . CYS B 1 224 ? 11.106 -10.915 59.258  1.00 23.44 ? 215 CYS B SG    1 
ATOM   4389 N N     . LYS B 1 225 ? 10.824 -15.415 56.840  1.00 19.97 ? 216 LYS B N     1 
ATOM   4390 C CA    . LYS B 1 225 ? 11.394 -16.715 56.493  1.00 18.93 ? 216 LYS B CA    1 
ATOM   4391 C C     . LYS B 1 225 ? 12.206 -16.643 55.207  1.00 20.20 ? 216 LYS B C     1 
ATOM   4392 O O     . LYS B 1 225 ? 13.307 -17.200 55.126  1.00 18.86 ? 216 LYS B O     1 
ATOM   4393 C CB    . LYS B 1 225 ? 10.262 -17.726 56.341  1.00 22.00 ? 216 LYS B CB    1 
ATOM   4394 C CG    . LYS B 1 225 ? 10.665 -19.172 56.300  1.00 29.60 ? 216 LYS B CG    1 
ATOM   4395 C CD    . LYS B 1 225 ? 9.438  -20.057 56.638  1.00 29.60 ? 216 LYS B CD    1 
ATOM   4396 C CE    . LYS B 1 225 ? 9.229  -20.173 58.153  1.00 35.23 ? 216 LYS B CE    1 
ATOM   4397 N NZ    . LYS B 1 225 ? 7.794  -20.155 58.611  1.00 29.04 ? 216 LYS B NZ    1 
ATOM   4398 N N     . PHE B 1 226 ? 11.665 -15.990 54.165  1.00 16.91 ? 217 PHE B N     1 
ATOM   4399 C CA    . PHE B 1 226 ? 12.378 -15.982 52.886  1.00 18.84 ? 217 PHE B CA    1 
ATOM   4400 C C     . PHE B 1 226 ? 13.759 -15.340 53.029  1.00 16.62 ? 217 PHE B C     1 
ATOM   4401 O O     . PHE B 1 226 ? 14.768 -15.936 52.638  1.00 17.22 ? 217 PHE B O     1 
ATOM   4402 C CB    . PHE B 1 226 ? 11.550 -15.276 51.794  1.00 18.60 ? 217 PHE B CB    1 
ATOM   4403 C CG    . PHE B 1 226 ? 12.163 -15.366 50.404  1.00 20.43 ? 217 PHE B CG    1 
ATOM   4404 C CD1   . PHE B 1 226 ? 12.480 -16.585 49.838  1.00 22.26 ? 217 PHE B CD1   1 
ATOM   4405 C CD2   . PHE B 1 226 ? 12.430 -14.212 49.668  1.00 18.72 ? 217 PHE B CD2   1 
ATOM   4406 C CE1   . PHE B 1 226 ? 13.074 -16.658 48.568  1.00 22.85 ? 217 PHE B CE1   1 
ATOM   4407 C CE2   . PHE B 1 226 ? 13.009 -14.273 48.412  1.00 18.23 ? 217 PHE B CE2   1 
ATOM   4408 C CZ    . PHE B 1 226 ? 13.320 -15.498 47.846  1.00 21.24 ? 217 PHE B CZ    1 
ATOM   4409 N N     . ILE B 1 227 ? 13.840 -14.131 53.629  1.00 16.56 ? 218 ILE B N     1 
ATOM   4410 C CA    . ILE B 1 227 ? 15.155 -13.484 53.710  1.00 14.60 ? 218 ILE B CA    1 
ATOM   4411 C C     . ILE B 1 227 ? 16.085 -14.308 54.579  1.00 16.25 ? 218 ILE B C     1 
ATOM   4412 O O     . ILE B 1 227 ? 17.291 -14.393 54.304  1.00 17.52 ? 218 ILE B O     1 
ATOM   4413 C CB    . ILE B 1 227 ? 15.103 -12.000 54.191  1.00 15.11 ? 218 ILE B CB    1 
ATOM   4414 C CG1   . ILE B 1 227 ? 16.464 -11.324 53.905  1.00 16.83 ? 218 ILE B CG1   1 
ATOM   4415 C CG2   . ILE B 1 227 ? 14.700 -11.846 55.686  1.00 16.84 ? 218 ILE B CG2   1 
ATOM   4416 C CD1   . ILE B 1 227 ? 16.519 -9.818  54.214  1.00 19.42 ? 218 ILE B CD1   1 
ATOM   4417 N N     . THR B 1 228 ? 15.550 -14.941 55.618  1.00 15.97 ? 219 THR B N     1 
ATOM   4418 C CA    . THR B 1 228 ? 16.382 -15.762 56.494  1.00 20.70 ? 219 THR B CA    1 
ATOM   4419 C C     . THR B 1 228 ? 17.014 -16.914 55.728  1.00 16.06 ? 219 THR B C     1 
ATOM   4420 O O     . THR B 1 228 ? 18.217 -17.177 55.860  1.00 19.20 ? 219 THR B O     1 
ATOM   4421 C CB    . THR B 1 228 ? 15.555 -16.289 57.671  1.00 19.84 ? 219 THR B CB    1 
ATOM   4422 O OG1   . THR B 1 228 ? 15.098 -15.176 58.466  1.00 23.55 ? 219 THR B OG1   1 
ATOM   4423 C CG2   . THR B 1 228 ? 16.431 -17.187 58.522  1.00 22.14 ? 219 THR B CG2   1 
ATOM   4424 N N     . GLN B 1 229 ? 16.220 -17.605 54.912  1.00 17.75 ? 220 GLN B N     1 
ATOM   4425 C CA    . GLN B 1 229 ? 16.733 -18.755 54.158  1.00 18.62 ? 220 GLN B CA    1 
ATOM   4426 C C     . GLN B 1 229 ? 17.732 -18.339 53.084  1.00 18.67 ? 220 GLN B C     1 
ATOM   4427 O O     . GLN B 1 229 ? 18.745 -19.013 52.867  1.00 19.09 ? 220 GLN B O     1 
ATOM   4428 C CB    . GLN B 1 229 ? 15.560 -19.524 53.575  1.00 21.33 ? 220 GLN B CB    1 
ATOM   4429 C CG    . GLN B 1 229 ? 14.625 -20.084 54.664  1.00 26.47 ? 220 GLN B CG    1 
ATOM   4430 C CD    . GLN B 1 229 ? 13.381 -20.772 54.107  1.00 29.81 ? 220 GLN B CD    1 
ATOM   4431 O OE1   . GLN B 1 229 ? 13.128 -20.749 52.907  1.00 29.12 ? 220 GLN B OE1   1 
ATOM   4432 N NE2   . GLN B 1 229 ? 12.592 -21.374 54.993  1.00 38.96 ? 220 GLN B NE2   1 
ATOM   4433 N N     . VAL B 1 230 ? 17.485 -17.217 52.409  1.00 20.71 ? 221 VAL B N     1 
ATOM   4434 C CA    . VAL B 1 230 ? 18.462 -16.713 51.454  1.00 15.36 ? 221 VAL B CA    1 
ATOM   4435 C C     . VAL B 1 230 ? 19.782 -16.431 52.153  1.00 14.56 ? 221 VAL B C     1 
ATOM   4436 O O     . VAL B 1 230 ? 20.854 -16.858 51.707  1.00 16.36 ? 221 VAL B O     1 
ATOM   4437 C CB    . VAL B 1 230 ? 17.902 -15.449 50.772  1.00 16.01 ? 221 VAL B CB    1 
ATOM   4438 C CG1   . VAL B 1 230 ? 18.996 -14.734 50.014  1.00 17.79 ? 221 VAL B CG1   1 
ATOM   4439 C CG2   . VAL B 1 230 ? 16.704 -15.810 49.891  1.00 18.87 ? 221 VAL B CG2   1 
ATOM   4440 N N     . VAL B 1 231 ? 19.723 -15.685 53.265  1.00 16.77 ? 222 VAL B N     1 
ATOM   4441 C CA    . VAL B 1 231 ? 20.948 -15.333 53.971  1.00 18.05 ? 222 VAL B CA    1 
ATOM   4442 C C     . VAL B 1 231 ? 21.634 -16.588 54.521  1.00 16.40 ? 222 VAL B C     1 
ATOM   4443 O O     . VAL B 1 231 ? 22.857 -16.740 54.386  1.00 18.34 ? 222 VAL B O     1 
ATOM   4444 C CB    . VAL B 1 231 ? 20.647 -14.289 55.065  1.00 18.08 ? 222 VAL B CB    1 
ATOM   4445 C CG1   . VAL B 1 231 ? 21.897 -14.033 55.889  1.00 18.37 ? 222 VAL B CG1   1 
ATOM   4446 C CG2   . VAL B 1 231 ? 20.149 -12.955 54.370  1.00 14.94 ? 222 VAL B CG2   1 
ATOM   4447 N N     . GLN B 1 232 ? 20.866 -17.539 55.083  1.00 19.44 ? 223 GLN B N     1 
ATOM   4448 C CA    A GLN B 1 232 ? 21.514 -18.742 55.600  0.50 21.82 ? 223 GLN B CA    1 
ATOM   4449 C CA    B GLN B 1 232 ? 21.472 -18.770 55.596  0.50 21.82 ? 223 GLN B CA    1 
ATOM   4450 C C     . GLN B 1 232 ? 22.195 -19.523 54.490  1.00 21.98 ? 223 GLN B C     1 
ATOM   4451 O O     . GLN B 1 232 ? 23.301 -20.054 54.693  1.00 23.57 ? 223 GLN B O     1 
ATOM   4452 C CB    A GLN B 1 232 ? 20.525 -19.647 56.326  0.50 22.13 ? 223 GLN B CB    1 
ATOM   4453 C CB    B GLN B 1 232 ? 20.408 -19.680 56.216  0.50 22.18 ? 223 GLN B CB    1 
ATOM   4454 C CG    A GLN B 1 232 ? 21.177 -20.879 56.966  0.50 23.59 ? 223 GLN B CG    1 
ATOM   4455 C CG    B GLN B 1 232 ? 19.924 -19.312 57.630  0.50 19.56 ? 223 GLN B CG    1 
ATOM   4456 C CD    A GLN B 1 232 ? 22.302 -20.529 57.923  0.50 23.52 ? 223 GLN B CD    1 
ATOM   4457 C CD    B GLN B 1 232 ? 18.684 -20.114 58.066  0.50 23.66 ? 223 GLN B CD    1 
ATOM   4458 O OE1   A GLN B 1 232 ? 22.049 -20.064 59.031  0.50 22.27 ? 223 GLN B OE1   1 
ATOM   4459 O OE1   B GLN B 1 232 ? 17.726 -20.286 57.303  0.50 21.37 ? 223 GLN B OE1   1 
ATOM   4460 N NE2   A GLN B 1 232 ? 23.547 -20.763 57.507  0.50 22.30 ? 223 GLN B NE2   1 
ATOM   4461 N NE2   B GLN B 1 232 ? 18.711 -20.622 59.289  0.50 17.73 ? 223 GLN B NE2   1 
ATOM   4462 N N     . ALA B 1 233 ? 21.552 -19.628 53.326  1.00 18.42 ? 224 ALA B N     1 
ATOM   4463 C CA    . ALA B 1 233 ? 22.135 -20.390 52.230  1.00 20.45 ? 224 ALA B CA    1 
ATOM   4464 C C     . ALA B 1 233 ? 23.452 -19.778 51.773  1.00 21.02 ? 224 ALA B C     1 
ATOM   4465 O O     . ALA B 1 233 ? 24.445 -20.494 51.614  1.00 21.17 ? 224 ALA B O     1 
ATOM   4466 C CB    . ALA B 1 233 ? 21.127 -20.487 51.084  1.00 20.33 ? 224 ALA B CB    1 
ATOM   4467 N N     . VAL B 1 234 ? 23.497 -18.445 51.573  1.00 18.80 ? 225 VAL B N     1 
ATOM   4468 C CA    . VAL B 1 234 ? 24.745 -17.838 51.111  1.00 20.93 ? 225 VAL B CA    1 
ATOM   4469 C C     . VAL B 1 234 ? 25.818 -17.899 52.198  1.00 20.70 ? 225 VAL B C     1 
ATOM   4470 O O     . VAL B 1 234 ? 27.006 -18.099 51.894  1.00 23.04 ? 225 VAL B O     1 
ATOM   4471 C CB    . VAL B 1 234 ? 24.530 -16.399 50.578  1.00 16.53 ? 225 VAL B CB    1 
ATOM   4472 C CG1   . VAL B 1 234 ? 23.694 -16.455 49.285  1.00 16.20 ? 225 VAL B CG1   1 
ATOM   4473 C CG2   . VAL B 1 234 ? 23.898 -15.435 51.640  1.00 20.45 ? 225 VAL B CG2   1 
ATOM   4474 N N     . VAL B 1 235 ? 25.431 -17.730 53.472  1.00 17.40 ? 226 VAL B N     1 
ATOM   4475 C CA    . VAL B 1 235 ? 26.407 -17.821 54.569  1.00 18.95 ? 226 VAL B CA    1 
ATOM   4476 C C     . VAL B 1 235 ? 27.025 -19.216 54.627  1.00 20.94 ? 226 VAL B C     1 
ATOM   4477 O O     . VAL B 1 235 ? 28.250 -19.371 54.759  1.00 22.66 ? 226 VAL B O     1 
ATOM   4478 C CB    . VAL B 1 235 ? 25.756 -17.447 55.914  1.00 21.74 ? 226 VAL B CB    1 
ATOM   4479 C CG1   . VAL B 1 235 ? 26.629 -17.944 57.114  1.00 18.44 ? 226 VAL B CG1   1 
ATOM   4480 C CG2   . VAL B 1 235 ? 25.567 -15.948 56.013  1.00 19.17 ? 226 VAL B CG2   1 
ATOM   4481 N N     . SER B 1 236 ? 26.198 -20.249 54.513  1.00 21.08 ? 227 SER B N     1 
ATOM   4482 C CA    . SER B 1 236 ? 26.730 -21.611 54.466  1.00 25.10 ? 227 SER B CA    1 
ATOM   4483 C C     . SER B 1 236 ? 27.626 -21.843 53.255  1.00 26.41 ? 227 SER B C     1 
ATOM   4484 O O     . SER B 1 236 ? 28.582 -22.618 53.336  1.00 26.67 ? 227 SER B O     1 
ATOM   4485 C CB    . SER B 1 236 ? 25.582 -22.618 54.472  1.00 27.04 ? 227 SER B CB    1 
ATOM   4486 O OG    . SER B 1 236 ? 24.839 -22.466 55.680  1.00 36.25 ? 227 SER B OG    1 
ATOM   4487 N N     . ALA B 1 237 ? 27.356 -21.171 52.129  1.00 20.07 ? 228 ALA B N     1 
ATOM   4488 C CA    . ALA B 1 237 ? 28.160 -21.412 50.939  1.00 24.60 ? 228 ALA B CA    1 
ATOM   4489 C C     . ALA B 1 237 ? 29.484 -20.677 50.981  1.00 23.29 ? 228 ALA B C     1 
ATOM   4490 O O     . ALA B 1 237 ? 30.495 -21.229 50.550  1.00 23.29 ? 228 ALA B O     1 
ATOM   4491 C CB    . ALA B 1 237 ? 27.413 -21.015 49.667  1.00 21.21 ? 228 ALA B CB    1 
ATOM   4492 N N     . ILE B 1 238 ? 29.512 -19.430 51.454  1.00 20.72 ? 229 ILE B N     1 
ATOM   4493 C CA    . ILE B 1 238 ? 30.747 -18.664 51.301  1.00 20.30 ? 229 ILE B CA    1 
ATOM   4494 C C     . ILE B 1 238 ? 31.267 -18.098 52.621  1.00 17.16 ? 229 ILE B C     1 
ATOM   4495 O O     . ILE B 1 238 ? 32.360 -17.520 52.656  1.00 22.19 ? 229 ILE B O     1 
ATOM   4496 C CB    . ILE B 1 238 ? 30.577 -17.543 50.252  1.00 24.03 ? 229 ILE B CB    1 
ATOM   4497 C CG1   . ILE B 1 238 ? 29.685 -16.417 50.764  1.00 18.83 ? 229 ILE B CG1   1 
ATOM   4498 C CG2   . ILE B 1 238 ? 30.066 -18.132 48.904  1.00 21.03 ? 229 ILE B CG2   1 
ATOM   4499 C CD1   . ILE B 1 238 ? 29.836 -15.108 49.936  1.00 22.10 ? 229 ILE B CD1   1 
ATOM   4500 N N     . GLY B 1 239 ? 30.521 -18.262 53.712  1.00 19.86 ? 230 GLY B N     1 
ATOM   4501 C CA    . GLY B 1 239 ? 30.968 -17.750 55.012  1.00 21.00 ? 230 GLY B CA    1 
ATOM   4502 C C     . GLY B 1 239 ? 30.307 -16.422 55.374  1.00 21.81 ? 230 GLY B C     1 
ATOM   4503 O O     . GLY B 1 239 ? 30.162 -15.544 54.511  1.00 20.13 ? 230 GLY B O     1 
ATOM   4504 N N     . ALA B 1 240 ? 29.906 -16.265 56.642  1.00 21.12 ? 231 ALA B N     1 
ATOM   4505 C CA    . ALA B 1 240 ? 29.148 -15.084 57.068  1.00 20.00 ? 231 ALA B CA    1 
ATOM   4506 C C     . ALA B 1 240 ? 29.925 -13.799 56.820  1.00 21.84 ? 231 ALA B C     1 
ATOM   4507 O O     . ALA B 1 240 ? 29.357 -12.796 56.364  1.00 20.14 ? 231 ALA B O     1 
ATOM   4508 C CB    . ALA B 1 240 ? 28.786 -15.199 58.558  1.00 20.54 ? 231 ALA B CB    1 
ATOM   4509 N N     . ASP B 1 241 ? 31.236 -13.825 57.066  1.00 20.53 ? 232 ASP B N     1 
ATOM   4510 C CA    . ASP B 1 241 ? 32.064 -12.638 56.938  1.00 22.33 ? 232 ASP B CA    1 
ATOM   4511 C C     . ASP B 1 241 ? 32.199 -12.164 55.500  1.00 20.10 ? 232 ASP B C     1 
ATOM   4512 O O     . ASP B 1 241 ? 32.785 -11.103 55.271  1.00 22.65 ? 232 ASP B O     1 
ATOM   4513 C CB    . ASP B 1 241 ? 33.421 -12.924 57.567  1.00 25.50 ? 232 ASP B CB    1 
ATOM   4514 C CG    . ASP B 1 241 ? 34.202 -13.976 56.824  1.00 31.41 ? 232 ASP B CG    1 
ATOM   4515 O OD1   . ASP B 1 241 ? 33.614 -14.820 56.100  1.00 32.49 ? 232 ASP B OD1   1 
ATOM   4516 O OD2   . ASP B 1 241 ? 35.429 -14.007 57.023  1.00 43.03 ? 232 ASP B OD2   1 
ATOM   4517 N N     . ARG B 1 242 ? 31.673 -12.916 54.531  1.00 17.86 ? 233 ARG B N     1 
ATOM   4518 C CA    . ARG B 1 242 ? 31.663 -12.461 53.150  1.00 17.84 ? 233 ARG B CA    1 
ATOM   4519 C C     . ARG B 1 242 ? 30.259 -12.076 52.680  1.00 19.19 ? 233 ARG B C     1 
ATOM   4520 O O     . ARG B 1 242 ? 30.034 -11.965 51.475  1.00 18.44 ? 233 ARG B O     1 
ATOM   4521 C CB    . ARG B 1 242 ? 32.240 -13.547 52.237  1.00 16.43 ? 233 ARG B CB    1 
ATOM   4522 C CG    . ARG B 1 242 ? 33.753 -13.557 52.159  1.00 21.30 ? 233 ARG B CG    1 
ATOM   4523 C CD    . ARG B 1 242 ? 34.251 -14.858 51.560  1.00 24.81 ? 233 ARG B CD    1 
ATOM   4524 N NE    . ARG B 1 242 ? 35.702 -15.049 51.563  1.00 37.35 ? 233 ARG B NE    1 
ATOM   4525 C CZ    . ARG B 1 242 ? 36.630 -14.207 51.099  1.00 38.95 ? 233 ARG B CZ    1 
ATOM   4526 N NH1   . ARG B 1 242 ? 36.326 -13.025 50.568  1.00 29.79 ? 233 ARG B NH1   1 
ATOM   4527 N NH2   . ARG B 1 242 ? 37.908 -14.572 51.143  1.00 40.16 ? 233 ARG B NH2   1 
ATOM   4528 N N     . VAL B 1 243 ? 29.305 -11.880 53.597  1.00 18.26 ? 234 VAL B N     1 
ATOM   4529 C CA    . VAL B 1 243 ? 27.898 -11.687 53.244  1.00 16.87 ? 234 VAL B CA    1 
ATOM   4530 C C     . VAL B 1 243 ? 27.402 -10.410 53.902  1.00 15.86 ? 234 VAL B C     1 
ATOM   4531 O O     . VAL B 1 243 ? 27.483 -10.273 55.132  1.00 17.76 ? 234 VAL B O     1 
ATOM   4532 C CB    . VAL B 1 243 ? 27.032 -12.884 53.677  1.00 17.83 ? 234 VAL B CB    1 
ATOM   4533 C CG1   . VAL B 1 243 ? 25.535 -12.628 53.448  1.00 16.71 ? 234 VAL B CG1   1 
ATOM   4534 C CG2   . VAL B 1 243 ? 27.460 -14.157 52.932  1.00 16.96 ? 234 VAL B CG2   1 
ATOM   4535 N N     . GLY B 1 244 ? 26.902 -9.470  53.087  1.00 13.67 ? 235 GLY B N     1 
ATOM   4536 C CA    . GLY B 1 244 ? 26.223 -8.305  53.617  1.00 14.08 ? 235 GLY B CA    1 
ATOM   4537 C C     . GLY B 1 244 ? 24.754 -8.384  53.267  1.00 12.54 ? 235 GLY B C     1 
ATOM   4538 O O     . GLY B 1 244 ? 24.370 -9.137  52.368  1.00 17.44 ? 235 GLY B O     1 
ATOM   4539 N N     . VAL B 1 245 ? 23.900 -7.633  53.951  1.00 15.59 ? 236 VAL B N     1 
ATOM   4540 C CA    . VAL B 1 245 ? 22.455 -7.740  53.724  1.00 13.71 ? 236 VAL B CA    1 
ATOM   4541 C C     . VAL B 1 245 ? 21.916 -6.328  53.680  1.00 16.62 ? 236 VAL B C     1 
ATOM   4542 O O     . VAL B 1 245 ? 22.202 -5.557  54.591  1.00 14.21 ? 236 VAL B O     1 
ATOM   4543 C CB    . VAL B 1 245 ? 21.755 -8.529  54.846  1.00 12.09 ? 236 VAL B CB    1 
ATOM   4544 C CG1   . VAL B 1 245 ? 20.311 -8.610  54.576  1.00 15.25 ? 236 VAL B CG1   1 
ATOM   4545 C CG2   . VAL B 1 245 ? 22.379 -9.927  54.978  1.00 13.57 ? 236 VAL B CG2   1 
ATOM   4546 N N     . ARG B 1 246 ? 21.152 -5.979  52.642  1.00 14.22 ? 237 ARG B N     1 
ATOM   4547 C CA    . ARG B 1 246 ? 20.622 -4.625  52.491  1.00 10.79 ? 237 ARG B CA    1 
ATOM   4548 C C     . ARG B 1 246 ? 19.110 -4.656  52.603  1.00 15.97 ? 237 ARG B C     1 
ATOM   4549 O O     . ARG B 1 246 ? 18.456 -5.435  51.902  1.00 14.80 ? 237 ARG B O     1 
ATOM   4550 C CB    . ARG B 1 246 ? 21.007 -3.971  51.147  1.00 13.46 ? 237 ARG B CB    1 
ATOM   4551 C CG    . ARG B 1 246 ? 20.742 -2.468  51.182  1.00 12.96 ? 237 ARG B CG    1 
ATOM   4552 C CD    . ARG B 1 246 ? 21.214 -1.801  49.886  1.00 15.48 ? 237 ARG B CD    1 
ATOM   4553 N NE    . ARG B 1 246 ? 21.626 -0.419  50.137  1.00 15.54 ? 237 ARG B NE    1 
ATOM   4554 C CZ    . ARG B 1 246 ? 21.536 0.564   49.260  1.00 18.24 ? 237 ARG B CZ    1 
ATOM   4555 N NH1   . ARG B 1 246 ? 20.928 0.393   48.077  1.00 15.86 ? 237 ARG B NH1   1 
ATOM   4556 N NH2   . ARG B 1 246 ? 22.117 1.730   49.549  1.00 15.90 ? 237 ARG B NH2   1 
ATOM   4557 N N     . VAL B 1 247 ? 18.543 -3.778  53.449  1.00 11.51 ? 238 VAL B N     1 
ATOM   4558 C CA    . VAL B 1 247 ? 17.084 -3.661  53.542  1.00 12.81 ? 238 VAL B CA    1 
ATOM   4559 C C     . VAL B 1 247 ? 16.675 -2.183  53.612  1.00 13.06 ? 238 VAL B C     1 
ATOM   4560 O O     . VAL B 1 247 ? 17.472 -1.313  53.930  1.00 15.02 ? 238 VAL B O     1 
ATOM   4561 C CB    . VAL B 1 247 ? 16.510 -4.393  54.775  1.00 14.92 ? 238 VAL B CB    1 
ATOM   4562 C CG1   . VAL B 1 247 ? 16.625 -5.956  54.686  1.00 15.68 ? 238 VAL B CG1   1 
ATOM   4563 C CG2   . VAL B 1 247 ? 17.160 -3.835  56.061  1.00 16.97 ? 238 VAL B CG2   1 
ATOM   4564 N N     . SER B 1 248 ? 15.375 -1.940  53.413  1.00 15.05 ? 239 SER B N     1 
ATOM   4565 C CA    . SER B 1 248 ? 14.817 -0.586  53.384  1.00 16.84 ? 239 SER B CA    1 
ATOM   4566 C C     . SER B 1 248 ? 13.418 -0.624  53.981  1.00 19.70 ? 239 SER B C     1 
ATOM   4567 O O     . SER B 1 248 ? 12.410 -0.419  53.290  1.00 19.27 ? 239 SER B O     1 
ATOM   4568 C CB    . SER B 1 248 ? 14.815 -0.032  51.951  1.00 18.21 ? 239 SER B CB    1 
ATOM   4569 O OG    . SER B 1 248 ? 13.959 -0.802  51.097  1.00 16.10 ? 239 SER B OG    1 
ATOM   4570 N N     . PRO B 1 249 ? 13.314 -0.887  55.290  1.00 17.83 ? 240 PRO B N     1 
ATOM   4571 C CA    . PRO B 1 249 ? 11.970 -1.033  55.881  1.00 17.16 ? 240 PRO B CA    1 
ATOM   4572 C C     . PRO B 1 249 ? 11.094 0.201   55.694  1.00 18.00 ? 240 PRO B C     1 
ATOM   4573 O O     . PRO B 1 249 ? 9.875  0.058   55.645  1.00 20.46 ? 240 PRO B O     1 
ATOM   4574 C CB    . PRO B 1 249 ? 12.244 -1.307  57.366  1.00 19.10 ? 240 PRO B CB    1 
ATOM   4575 C CG    . PRO B 1 249 ? 13.721 -1.319  57.533  1.00 22.51 ? 240 PRO B CG    1 
ATOM   4576 C CD    . PRO B 1 249 ? 14.379 -0.789  56.306  1.00 17.95 ? 240 PRO B CD    1 
ATOM   4577 N N     . ALA B 1 250 ? 11.664 1.393   55.528  1.00 16.68 ? 241 ALA B N     1 
ATOM   4578 C CA    . ALA B 1 250 ? 10.853 2.604   55.468  1.00 25.99 ? 241 ALA B CA    1 
ATOM   4579 C C     . ALA B 1 250 ? 10.757 3.201   54.069  1.00 23.31 ? 241 ALA B C     1 
ATOM   4580 O O     . ALA B 1 250 ? 10.312 4.344   53.931  1.00 24.18 ? 241 ALA B O     1 
ATOM   4581 C CB    . ALA B 1 250 ? 11.397 3.659   56.443  1.00 29.10 ? 241 ALA B CB    1 
ATOM   4582 N N     . ILE B 1 251 ? 11.170 2.467   53.029  1.00 20.46 ? 242 ILE B N     1 
ATOM   4583 C CA    . ILE B 1 251 ? 11.126 2.958   51.657  1.00 20.85 ? 242 ILE B CA    1 
ATOM   4584 C C     . ILE B 1 251 ? 9.930  2.246   51.037  1.00 23.53 ? 242 ILE B C     1 
ATOM   4585 O O     . ILE B 1 251 ? 9.842  1.011   51.106  1.00 21.83 ? 242 ILE B O     1 
ATOM   4586 C CB    . ILE B 1 251 ? 12.432 2.604   50.933  1.00 18.92 ? 242 ILE B CB    1 
ATOM   4587 C CG1   . ILE B 1 251 ? 13.524 3.599   51.348  1.00 16.82 ? 242 ILE B CG1   1 
ATOM   4588 C CG2   . ILE B 1 251 ? 12.202 2.749   49.403  1.00 25.19 ? 242 ILE B CG2   1 
ATOM   4589 C CD1   . ILE B 1 251 ? 14.823 3.641   50.480  1.00 17.68 ? 242 ILE B CD1   1 
ATOM   4590 N N     . ASP B 1 252 ? 8.971  2.987   50.467  1.00 22.85 ? 243 ASP B N     1 
ATOM   4591 C CA    . ASP B 1 252 ? 7.742  2.350   50.005  1.00 26.10 ? 243 ASP B CA    1 
ATOM   4592 C C     . ASP B 1 252 ? 7.708  2.176   48.486  1.00 29.38 ? 243 ASP B C     1 
ATOM   4593 O O     . ASP B 1 252 ? 6.622  2.059   47.897  1.00 33.30 ? 243 ASP B O     1 
ATOM   4594 C CB    . ASP B 1 252 ? 6.508  3.114   50.477  1.00 32.57 ? 243 ASP B CB    1 
ATOM   4595 C CG    . ASP B 1 252 ? 6.333  4.435   49.776  1.00 48.40 ? 243 ASP B CG    1 
ATOM   4596 O OD1   . ASP B 1 252 ? 7.278  4.895   49.079  1.00 53.84 ? 243 ASP B OD1   1 
ATOM   4597 O OD2   . ASP B 1 252 ? 5.233  5.013   49.915  1.00 60.43 ? 243 ASP B OD2   1 
ATOM   4598 N N     . HIS B 1 253 ? 8.890  2.113   47.870  1.00 27.10 ? 244 HIS B N     1 
ATOM   4599 C CA    . HIS B 1 253 ? 9.048  2.050   46.420  1.00 26.90 ? 244 HIS B CA    1 
ATOM   4600 C C     . HIS B 1 253 ? 8.281  0.864   45.832  1.00 23.83 ? 244 HIS B C     1 
ATOM   4601 O O     . HIS B 1 253 ? 8.352  -0.254  46.357  1.00 24.39 ? 244 HIS B O     1 
ATOM   4602 C CB    . HIS B 1 253 ? 10.535 1.886   46.099  1.00 25.59 ? 244 HIS B CB    1 
ATOM   4603 C CG    . HIS B 1 253 ? 10.851 1.922   44.638  1.00 26.04 ? 244 HIS B CG    1 
ATOM   4604 N ND1   . HIS B 1 253 ? 11.665 0.983   44.033  1.00 21.71 ? 244 HIS B ND1   1 
ATOM   4605 C CD2   . HIS B 1 253 ? 10.618 2.875   43.702  1.00 23.77 ? 244 HIS B CD2   1 
ATOM   4606 C CE1   . HIS B 1 253 ? 11.824 1.303   42.760  1.00 22.40 ? 244 HIS B CE1   1 
ATOM   4607 N NE2   . HIS B 1 253 ? 11.204 2.449   42.533  1.00 29.72 ? 244 HIS B NE2   1 
ATOM   4608 N N     . LEU B 1 254 ? 7.550  1.108   44.736  1.00 24.98 ? 245 LEU B N     1 
ATOM   4609 C CA    . LEU B 1 254 ? 6.867  0.051   43.974  1.00 19.26 ? 245 LEU B CA    1 
ATOM   4610 C C     . LEU B 1 254 ? 5.804  -0.644  44.816  1.00 21.06 ? 245 LEU B C     1 
ATOM   4611 O O     . LEU B 1 254 ? 5.688  -1.865  44.789  1.00 17.24 ? 245 LEU B O     1 
ATOM   4612 C CB    . LEU B 1 254 ? 7.858  -0.976  43.426  1.00 15.67 ? 245 LEU B CB    1 
ATOM   4613 C CG    . LEU B 1 254 ? 8.897  -0.428  42.469  1.00 22.92 ? 245 LEU B CG    1 
ATOM   4614 C CD1   . LEU B 1 254 ? 9.881  -1.546  42.116  1.00 23.44 ? 245 LEU B CD1   1 
ATOM   4615 C CD2   . LEU B 1 254 ? 8.186  0.186   41.239  1.00 23.78 ? 245 LEU B CD2   1 
ATOM   4616 N N     . ASP B 1 255 ? 5.039  0.159   45.583  1.00 20.88 ? 246 ASP B N     1 
ATOM   4617 C CA    . ASP B 1 255 ? 3.900  -0.318  46.375  1.00 21.44 ? 246 ASP B CA    1 
ATOM   4618 C C     . ASP B 1 255 ? 4.334  -1.319  47.431  1.00 21.77 ? 246 ASP B C     1 
ATOM   4619 O O     . ASP B 1 255 ? 3.663  -2.332  47.643  1.00 24.94 ? 246 ASP B O     1 
ATOM   4620 C CB    . ASP B 1 255 ? 2.812  -0.935  45.492  1.00 23.72 ? 246 ASP B CB    1 
ATOM   4621 C CG    . ASP B 1 255 ? 2.111  0.094   44.676  1.00 27.22 ? 246 ASP B CG    1 
ATOM   4622 O OD1   . ASP B 1 255 ? 2.214  1.282   45.062  1.00 30.70 ? 246 ASP B OD1   1 
ATOM   4623 O OD2   . ASP B 1 255 ? 1.477  -0.254  43.656  1.00 30.47 ? 246 ASP B OD2   1 
ATOM   4624 N N     . ALA B 1 256 ? 5.466  -1.047  48.084  1.00 16.94 ? 247 ALA B N     1 
ATOM   4625 C CA    . ALA B 1 256 ? 6.066  -1.958  49.060  1.00 23.68 ? 247 ALA B CA    1 
ATOM   4626 C C     . ALA B 1 256 ? 6.067  -1.263  50.402  1.00 23.25 ? 247 ALA B C     1 
ATOM   4627 O O     . ALA B 1 256 ? 7.082  -0.712  50.817  1.00 26.26 ? 247 ALA B O     1 
ATOM   4628 C CB    . ALA B 1 256 ? 7.479  -2.338  48.667  1.00 25.58 ? 247 ALA B CB    1 
ATOM   4629 N N     . MET B 1 257 ? 4.948  -1.308  51.098  1.00 20.09 ? 248 MET B N     1 
ATOM   4630 C CA    . MET B 1 257 ? 4.845  -0.612  52.372  1.00 22.01 ? 248 MET B CA    1 
ATOM   4631 C C     . MET B 1 257 ? 4.540  -1.604  53.485  1.00 19.70 ? 248 MET B C     1 
ATOM   4632 O O     . MET B 1 257 ? 3.849  -2.604  53.260  1.00 20.54 ? 248 MET B O     1 
ATOM   4633 C CB    . MET B 1 257 ? 3.785  0.477   52.274  1.00 26.01 ? 248 MET B CB    1 
ATOM   4634 C CG    . MET B 1 257 ? 3.175  0.932   53.594  1.00 40.62 ? 248 MET B CG    1 
ATOM   4635 S SD    . MET B 1 257 ? 1.960  2.223   53.263  1.00 70.57 ? 248 MET B SD    1 
ATOM   4636 C CE    . MET B 1 257 ? 2.609  2.897   51.728  1.00 43.35 ? 248 MET B CE    1 
ATOM   4637 N N     . ASP B 1 258 ? 5.062  -1.341  54.692  1.00 23.04 ? 249 ASP B N     1 
ATOM   4638 C CA    . ASP B 1 258 ? 4.690  -2.150  55.844  1.00 23.03 ? 249 ASP B CA    1 
ATOM   4639 C C     . ASP B 1 258 ? 3.906  -1.287  56.830  1.00 22.44 ? 249 ASP B C     1 
ATOM   4640 O O     . ASP B 1 258 ? 4.174  -0.086  56.967  1.00 20.61 ? 249 ASP B O     1 
ATOM   4641 C CB    . ASP B 1 258 ? 5.918  -2.755  56.551  1.00 19.23 ? 249 ASP B CB    1 
ATOM   4642 C CG    . ASP B 1 258 ? 5.542  -3.916  57.501  1.00 26.78 ? 249 ASP B CG    1 
ATOM   4643 O OD1   . ASP B 1 258 ? 5.316  -5.060  56.996  1.00 23.05 ? 249 ASP B OD1   1 
ATOM   4644 O OD2   . ASP B 1 258 ? 5.399  -3.684  58.745  1.00 25.99 ? 249 ASP B OD2   1 
ATOM   4645 N N     . SER B 1 259 ? 2.928  -1.918  57.502  1.00 20.56 ? 250 SER B N     1 
ATOM   4646 C CA    . SER B 1 259 ? 2.119  -1.272  58.543  1.00 24.75 ? 250 SER B CA    1 
ATOM   4647 C C     . SER B 1 259 ? 2.942  -0.882  59.776  1.00 27.57 ? 250 SER B C     1 
ATOM   4648 O O     . SER B 1 259 ? 2.548  0.024   60.528  1.00 25.26 ? 250 SER B O     1 
ATOM   4649 C CB    . SER B 1 259 ? 0.966  -2.199  58.951  1.00 26.37 ? 250 SER B CB    1 
ATOM   4650 O OG    . SER B 1 259 ? 1.383  -3.363  59.665  1.00 24.60 ? 250 SER B OG    1 
ATOM   4651 N N     . ASN B 1 260 ? 4.077  -1.516  59.996  1.00 21.10 ? 251 ASN B N     1 
ATOM   4652 C CA    . ASN B 1 260 ? 4.936  -1.195  61.138  1.00 24.22 ? 251 ASN B CA    1 
ATOM   4653 C C     . ASN B 1 260 ? 6.384  -1.324  60.693  1.00 24.65 ? 251 ASN B C     1 
ATOM   4654 O O     . ASN B 1 260 ? 7.032  -2.344  60.959  1.00 24.21 ? 251 ASN B O     1 
ATOM   4655 C CB    . ASN B 1 260 ? 4.621  -2.120  62.320  1.00 25.33 ? 251 ASN B CB    1 
ATOM   4656 C CG    . ASN B 1 260 ? 5.227  -1.639  63.628  1.00 25.01 ? 251 ASN B CG    1 
ATOM   4657 O OD1   . ASN B 1 260 ? 6.137  -0.819  63.635  1.00 25.42 ? 251 ASN B OD1   1 
ATOM   4658 N ND2   . ASN B 1 260 ? 4.712  -2.150  64.747  1.00 30.24 ? 251 ASN B ND2   1 
ATOM   4659 N N     . PRO B 1 261 ? 6.917  -0.319  59.967  1.00 21.93 ? 252 PRO B N     1 
ATOM   4660 C CA    . PRO B 1 261 ? 8.306  -0.440  59.455  1.00 21.03 ? 252 PRO B CA    1 
ATOM   4661 C C     . PRO B 1 261 ? 9.348  -0.754  60.517  1.00 20.61 ? 252 PRO B C     1 
ATOM   4662 O O     . PRO B 1 261 ? 10.215 -1.607  60.289  1.00 20.22 ? 252 PRO B O     1 
ATOM   4663 C CB    . PRO B 1 261 ? 8.560  0.932   58.805  1.00 19.75 ? 252 PRO B CB    1 
ATOM   4664 C CG    . PRO B 1 261 ? 7.148  1.318   58.302  1.00 23.32 ? 252 PRO B CG    1 
ATOM   4665 C CD    . PRO B 1 261 ? 6.193  0.811   59.344  1.00 20.98 ? 252 PRO B CD    1 
ATOM   4666 N N     . LEU B 1 262 ? 9.310  -0.068  61.664  1.00 21.75 ? 253 LEU B N     1 
ATOM   4667 C CA    . LEU B 1 262 ? 10.320 -0.311  62.694  1.00 20.40 ? 253 LEU B CA    1 
ATOM   4668 C C     . LEU B 1 262 ? 10.250 -1.744  63.212  1.00 18.11 ? 253 LEU B C     1 
ATOM   4669 O O     . LEU B 1 262 ? 11.289 -2.368  63.474  1.00 16.30 ? 253 LEU B O     1 
ATOM   4670 C CB    . LEU B 1 262 ? 10.155 0.696   63.837  1.00 21.55 ? 253 LEU B CB    1 
ATOM   4671 C CG    . LEU B 1 262 ? 11.229 0.652   64.944  1.00 29.81 ? 253 LEU B CG    1 
ATOM   4672 C CD1   . LEU B 1 262 ? 12.679 0.813   64.402  1.00 28.64 ? 253 LEU B CD1   1 
ATOM   4673 C CD2   . LEU B 1 262 ? 10.939 1.614   66.122  1.00 23.04 ? 253 LEU B CD2   1 
ATOM   4674 N N     . SER B 1 263 ? 9.036  -2.283  63.381  1.00 16.93 ? 254 SER B N     1 
ATOM   4675 C CA    . SER B 1 263 ? 8.887  -3.663  63.825  1.00 19.73 ? 254 SER B CA    1 
ATOM   4676 C C     . SER B 1 263 ? 9.393  -4.652  62.782  1.00 18.35 ? 254 SER B C     1 
ATOM   4677 O O     . SER B 1 263 ? 10.055 -5.650  63.122  1.00 17.91 ? 254 SER B O     1 
ATOM   4678 C CB    . SER B 1 263 ? 7.419  -3.946  64.140  1.00 22.33 ? 254 SER B CB    1 
ATOM   4679 O OG    . SER B 1 263 ? 7.270  -5.281  64.571  1.00 25.97 ? 254 SER B OG    1 
ATOM   4680 N N     . LEU B 1 264 ? 9.064  -4.401  61.509  1.00 17.02 ? 255 LEU B N     1 
ATOM   4681 C CA    . LEU B 1 264 ? 9.613  -5.237  60.447  1.00 15.79 ? 255 LEU B CA    1 
ATOM   4682 C C     . LEU B 1 264 ? 11.139 -5.201  60.462  1.00 16.56 ? 255 LEU B C     1 
ATOM   4683 O O     . LEU B 1 264 ? 11.789 -6.250  60.385  1.00 17.77 ? 255 LEU B O     1 
ATOM   4684 C CB    . LEU B 1 264 ? 9.083  -4.772  59.101  1.00 18.14 ? 255 LEU B CB    1 
ATOM   4685 C CG    . LEU B 1 264 ? 9.728  -5.476  57.899  1.00 20.74 ? 255 LEU B CG    1 
ATOM   4686 C CD1   . LEU B 1 264 ? 9.471  -6.955  57.986  1.00 19.88 ? 255 LEU B CD1   1 
ATOM   4687 C CD2   . LEU B 1 264 ? 9.080  -4.888  56.680  1.00 19.63 ? 255 LEU B CD2   1 
ATOM   4688 N N     . GLY B 1 265 ? 11.722 -4.002  60.569  1.00 16.43 ? 256 GLY B N     1 
ATOM   4689 C CA    . GLY B 1 265 ? 13.174 -3.880  60.584  1.00 12.89 ? 256 GLY B CA    1 
ATOM   4690 C C     . GLY B 1 265 ? 13.802 -4.583  61.778  1.00 19.90 ? 256 GLY B C     1 
ATOM   4691 O O     . GLY B 1 265 ? 14.827 -5.256  61.650  1.00 16.59 ? 256 GLY B O     1 
ATOM   4692 N N     . LEU B 1 266 ? 13.173 -4.465  62.949  1.00 16.05 ? 257 LEU B N     1 
ATOM   4693 C CA    . LEU B 1 266 ? 13.723 -5.122  64.128  1.00 15.93 ? 257 LEU B CA    1 
ATOM   4694 C C     . LEU B 1 266 ? 13.610 -6.647  64.038  1.00 20.67 ? 257 LEU B C     1 
ATOM   4695 O O     . LEU B 1 266 ? 14.495 -7.359  64.547  1.00 16.43 ? 257 LEU B O     1 
ATOM   4696 C CB    . LEU B 1 266 ? 13.032 -4.578  65.369  1.00 14.93 ? 257 LEU B CB    1 
ATOM   4697 C CG    . LEU B 1 266 ? 13.395 -3.166  65.744  1.00 19.83 ? 257 LEU B CG    1 
ATOM   4698 C CD1   . LEU B 1 266 ? 12.530 -2.674  66.975  1.00 15.72 ? 257 LEU B CD1   1 
ATOM   4699 C CD2   . LEU B 1 266 ? 14.877 -3.182  66.109  1.00 19.15 ? 257 LEU B CD2   1 
ATOM   4700 N N     . ALA B 1 267 ? 12.530 -7.156  63.411  1.00 19.07 ? 258 ALA B N     1 
ATOM   4701 C CA    . ALA B 1 267 ? 12.388 -8.587  63.174  1.00 17.36 ? 258 ALA B CA    1 
ATOM   4702 C C     . ALA B 1 267 ? 13.459 -9.105  62.231  1.00 19.86 ? 258 ALA B C     1 
ATOM   4703 O O     . ALA B 1 267 ? 14.033 -10.171 62.469  1.00 17.09 ? 258 ALA B O     1 
ATOM   4704 C CB    . ALA B 1 267 ? 10.989 -8.925  62.638  1.00 20.46 ? 258 ALA B CB    1 
ATOM   4705 N N     . VAL B 1 268 ? 13.774 -8.354  61.165  1.00 17.92 ? 259 VAL B N     1 
ATOM   4706 C CA    . VAL B 1 268 ? 14.870 -8.802  60.311  1.00 19.60 ? 259 VAL B CA    1 
ATOM   4707 C C     . VAL B 1 268 ? 16.174 -8.826  61.093  1.00 18.64 ? 259 VAL B C     1 
ATOM   4708 O O     . VAL B 1 268 ? 16.980 -9.749  60.962  1.00 17.91 ? 259 VAL B O     1 
ATOM   4709 C CB    . VAL B 1 268 ? 14.997 -7.909  59.069  1.00 16.95 ? 259 VAL B CB    1 
ATOM   4710 C CG1   . VAL B 1 268 ? 16.282 -8.264  58.317  1.00 16.45 ? 259 VAL B CG1   1 
ATOM   4711 C CG2   . VAL B 1 268 ? 13.754 -8.008  58.203  1.00 16.21 ? 259 VAL B CG2   1 
ATOM   4712 N N     . VAL B 1 269 ? 16.406 -7.804  61.914  1.00 15.80 ? 260 VAL B N     1 
ATOM   4713 C CA    . VAL B 1 269 ? 17.663 -7.725  62.659  1.00 15.58 ? 260 VAL B CA    1 
ATOM   4714 C C     . VAL B 1 269 ? 17.788 -8.902  63.624  1.00 14.65 ? 260 VAL B C     1 
ATOM   4715 O O     . VAL B 1 269 ? 18.861 -9.504  63.768  1.00 20.76 ? 260 VAL B O     1 
ATOM   4716 C CB    . VAL B 1 269 ? 17.740 -6.377  63.383  1.00 15.76 ? 260 VAL B CB    1 
ATOM   4717 C CG1   . VAL B 1 269 ? 18.792 -6.427  64.534  1.00 18.68 ? 260 VAL B CG1   1 
ATOM   4718 C CG2   . VAL B 1 269 ? 18.063 -5.266  62.372  1.00 15.32 ? 260 VAL B CG2   1 
ATOM   4719 N N     . GLU B 1 270 ? 16.683 -9.268  64.267  1.00 16.49 ? 261 GLU B N     1 
ATOM   4720 C CA    . GLU B 1 270 ? 16.668 -10.448 65.139  1.00 22.07 ? 261 GLU B CA    1 
ATOM   4721 C C     . GLU B 1 270 ? 17.100 -11.717 64.402  1.00 21.73 ? 261 GLU B C     1 
ATOM   4722 O O     . GLU B 1 270 ? 17.882 -12.513 64.930  1.00 21.28 ? 261 GLU B O     1 
ATOM   4723 C CB    . GLU B 1 270 ? 15.271 -10.642 65.738  1.00 27.48 ? 261 GLU B CB    1 
ATOM   4724 C CG    . GLU B 1 270 ? 15.204 -11.852 66.687  1.00 29.34 ? 261 GLU B CG    1 
ATOM   4725 C CD    . GLU B 1 270 ? 13.807 -12.106 67.277  1.00 46.02 ? 261 GLU B CD    1 
ATOM   4726 O OE1   . GLU B 1 270 ? 12.952 -12.644 66.532  1.00 50.08 ? 261 GLU B OE1   1 
ATOM   4727 O OE2   . GLU B 1 270 ? 13.569 -11.809 68.484  1.00 51.89 ? 261 GLU B OE2   1 
ATOM   4728 N N     . ARG B 1 271 ? 16.557 -11.958 63.203  1.00 20.49 ? 262 ARG B N     1 
ATOM   4729 C CA    . ARG B 1 271 ? 16.952 -13.153 62.443  1.00 18.72 ? 262 ARG B CA    1 
ATOM   4730 C C     . ARG B 1 271 ? 18.439 -13.129 62.077  1.00 19.34 ? 262 ARG B C     1 
ATOM   4731 O O     . ARG B 1 271 ? 19.118 -14.166 62.137  1.00 19.53 ? 262 ARG B O     1 
ATOM   4732 C CB    . ARG B 1 271 ? 16.079 -13.327 61.193  1.00 21.48 ? 262 ARG B CB    1 
ATOM   4733 C CG    . ARG B 1 271 ? 14.776 -14.108 61.495  1.00 27.92 ? 262 ARG B CG    1 
ATOM   4734 C CD    . ARG B 1 271 ? 13.689 -13.130 61.764  1.00 31.72 ? 262 ARG B CD    1 
ATOM   4735 N NE    . ARG B 1 271 ? 12.450 -13.734 62.245  1.00 40.54 ? 262 ARG B NE    1 
ATOM   4736 C CZ    . ARG B 1 271 ? 11.755 -13.254 63.273  1.00 40.57 ? 262 ARG B CZ    1 
ATOM   4737 N NH1   . ARG B 1 271 ? 12.153 -12.162 63.935  1.00 30.13 ? 262 ARG B NH1   1 
ATOM   4738 N NH2   . ARG B 1 271 ? 10.637 -13.879 63.648  1.00 42.32 ? 262 ARG B NH2   1 
ATOM   4739 N N     . LEU B 1 272 ? 18.964 -11.968 61.683  1.00 18.42 ? 263 LEU B N     1 
ATOM   4740 C CA    . LEU B 1 272 ? 20.395 -11.856 61.375  1.00 15.38 ? 263 LEU B CA    1 
ATOM   4741 C C     . LEU B 1 272 ? 21.260 -12.136 62.606  1.00 17.02 ? 263 LEU B C     1 
ATOM   4742 O O     . LEU B 1 272 ? 22.294 -12.823 62.520  1.00 18.64 ? 263 LEU B O     1 
ATOM   4743 C CB    . LEU B 1 272 ? 20.691 -10.460 60.823  1.00 17.43 ? 263 LEU B CB    1 
ATOM   4744 C CG    . LEU B 1 272 ? 19.924 -10.096 59.539  1.00 16.26 ? 263 LEU B CG    1 
ATOM   4745 C CD1   . LEU B 1 272 ? 20.433 -8.752  59.025  1.00 17.23 ? 263 LEU B CD1   1 
ATOM   4746 C CD2   . LEU B 1 272 ? 20.060 -11.189 58.474  1.00 18.96 ? 263 LEU B CD2   1 
ATOM   4747 N N     . ASN B 1 273 ? 20.867 -11.593 63.764  1.00 18.19 ? 264 ASN B N     1 
ATOM   4748 C CA    . ASN B 1 273 ? 21.617 -11.871 64.976  1.00 19.35 ? 264 ASN B CA    1 
ATOM   4749 C C     . ASN B 1 273 ? 21.606 -13.360 65.271  1.00 19.66 ? 264 ASN B C     1 
ATOM   4750 O O     . ASN B 1 273 ? 22.622 -13.921 65.693  1.00 21.68 ? 264 ASN B O     1 
ATOM   4751 C CB    . ASN B 1 273 ? 21.031 -11.104 66.156  1.00 17.28 ? 264 ASN B CB    1 
ATOM   4752 C CG    . ASN B 1 273 ? 21.376 -9.616  66.128  1.00 16.11 ? 264 ASN B CG    1 
ATOM   4753 O OD1   . ASN B 1 273 ? 22.233 -9.152  65.364  1.00 18.77 ? 264 ASN B OD1   1 
ATOM   4754 N ND2   . ASN B 1 273 ? 20.693 -8.857  66.988  1.00 17.04 ? 264 ASN B ND2   1 
ATOM   4755 N N     . LYS B 1 274 ? 20.469 -14.017 65.043  1.00 18.38 ? 265 LYS B N     1 
ATOM   4756 C CA    . LYS B 1 274 ? 20.409 -15.447 65.338  1.00 22.48 ? 265 LYS B CA    1 
ATOM   4757 C C     . LYS B 1 274 ? 21.204 -16.259 64.319  1.00 22.04 ? 265 LYS B C     1 
ATOM   4758 O O     . LYS B 1 274 ? 21.863 -17.233 64.688  1.00 24.05 ? 265 LYS B O     1 
ATOM   4759 C CB    . LYS B 1 274 ? 18.958 -15.919 65.424  1.00 24.36 ? 265 LYS B CB    1 
ATOM   4760 C CG    . LYS B 1 274 ? 18.145 -15.216 66.473  1.00 31.26 ? 265 LYS B CG    1 
ATOM   4761 C CD    . LYS B 1 274 ? 17.383 -16.185 67.380  1.00 44.24 ? 265 LYS B CD    1 
ATOM   4762 C CE    . LYS B 1 274 ? 16.562 -15.387 68.399  1.00 39.51 ? 265 LYS B CE    1 
ATOM   4763 N NZ    . LYS B 1 274 ? 15.146 -15.837 68.528  1.00 42.32 ? 265 LYS B NZ    1 
ATOM   4764 N N     . ILE B 1 275 ? 21.197 -15.855 63.039  1.00 19.92 ? 266 ILE B N     1 
ATOM   4765 C CA    . ILE B 1 275 ? 22.059 -16.517 62.059  1.00 20.22 ? 266 ILE B CA    1 
ATOM   4766 C C     . ILE B 1 275 ? 23.524 -16.423 62.476  1.00 21.64 ? 266 ILE B C     1 
ATOM   4767 O O     . ILE B 1 275 ? 24.296 -17.382 62.314  1.00 20.75 ? 266 ILE B O     1 
ATOM   4768 C CB    . ILE B 1 275 ? 21.850 -15.912 60.657  1.00 23.06 ? 266 ILE B CB    1 
ATOM   4769 C CG1   . ILE B 1 275 ? 20.538 -16.418 60.093  1.00 20.35 ? 266 ILE B CG1   1 
ATOM   4770 C CG2   . ILE B 1 275 ? 23.040 -16.263 59.757  1.00 22.99 ? 266 ILE B CG2   1 
ATOM   4771 C CD1   . ILE B 1 275 ? 20.010 -15.617 58.902  1.00 19.98 ? 266 ILE B CD1   1 
ATOM   4772 N N     . GLN B 1 276 ? 23.927 -15.269 63.020  1.00 20.85 ? 267 GLN B N     1 
ATOM   4773 C CA    . GLN B 1 276 ? 25.305 -15.100 63.473  1.00 20.96 ? 267 GLN B CA    1 
ATOM   4774 C C     . GLN B 1 276 ? 25.611 -16.012 64.654  1.00 21.97 ? 267 GLN B C     1 
ATOM   4775 O O     . GLN B 1 276 ? 26.633 -16.707 64.653  1.00 28.12 ? 267 GLN B O     1 
ATOM   4776 C CB    . GLN B 1 276 ? 25.571 -13.632 63.826  1.00 22.60 ? 267 GLN B CB    1 
ATOM   4777 C CG    . GLN B 1 276 ? 25.499 -12.747 62.577  1.00 17.95 ? 267 GLN B CG    1 
ATOM   4778 C CD    . GLN B 1 276 ? 25.693 -11.267 62.837  1.00 20.38 ? 267 GLN B CD    1 
ATOM   4779 O OE1   . GLN B 1 276 ? 26.049 -10.522 61.916  1.00 20.65 ? 267 GLN B OE1   1 
ATOM   4780 N NE2   . GLN B 1 276 ? 25.470 -10.825 64.094  1.00 16.77 ? 267 GLN B NE2   1 
ATOM   4781 N N     . LEU B 1 277 ? 24.741 -16.010 65.670  1.00 25.42 ? 268 LEU B N     1 
ATOM   4782 C CA    . LEU B 1 277 ? 24.988 -16.834 66.855  1.00 26.45 ? 268 LEU B CA    1 
ATOM   4783 C C     . LEU B 1 277 ? 25.072 -18.301 66.471  1.00 28.76 ? 268 LEU B C     1 
ATOM   4784 O O     . LEU B 1 277 ? 26.017 -19.006 66.846  1.00 35.21 ? 268 LEU B O     1 
ATOM   4785 C CB    . LEU B 1 277 ? 23.887 -16.597 67.890  1.00 31.49 ? 268 LEU B CB    1 
ATOM   4786 C CG    . LEU B 1 277 ? 23.917 -15.163 68.420  1.00 34.00 ? 268 LEU B CG    1 
ATOM   4787 C CD1   . LEU B 1 277 ? 22.700 -14.863 69.266  1.00 26.56 ? 268 LEU B CD1   1 
ATOM   4788 C CD2   . LEU B 1 277 ? 25.206 -14.871 69.202  1.00 33.57 ? 268 LEU B CD2   1 
ATOM   4789 N N     . HIS B 1 278 ? 24.116 -18.758 65.662  1.00 26.97 ? 269 HIS B N     1 
ATOM   4790 C CA    . HIS B 1 278 ? 24.090 -20.149 65.210  1.00 35.73 ? 269 HIS B CA    1 
ATOM   4791 C C     . HIS B 1 278 ? 25.290 -20.487 64.328  1.00 37.31 ? 269 HIS B C     1 
ATOM   4792 O O     . HIS B 1 278 ? 25.886 -21.561 64.481  1.00 43.47 ? 269 HIS B O     1 
ATOM   4793 C CB    . HIS B 1 278 ? 22.762 -20.429 64.491  1.00 35.50 ? 269 HIS B CB    1 
ATOM   4794 C CG    . HIS B 1 278 ? 21.554 -20.264 65.378  1.00 44.81 ? 269 HIS B CG    1 
ATOM   4795 N ND1   . HIS B 1 278 ? 21.651 -19.964 66.725  1.00 45.96 ? 269 HIS B ND1   1 
ATOM   4796 C CD2   . HIS B 1 278 ? 20.225 -20.343 65.111  1.00 42.45 ? 269 HIS B CD2   1 
ATOM   4797 C CE1   . HIS B 1 278 ? 20.439 -19.862 67.245  1.00 43.92 ? 269 HIS B CE1   1 
ATOM   4798 N NE2   . HIS B 1 278 ? 19.556 -20.091 66.288  1.00 46.24 ? 269 HIS B NE2   1 
ATOM   4799 N N     . SER B 1 279 ? 25.652 -19.596 63.395  1.00 33.82 ? 270 SER B N     1 
ATOM   4800 C CA    . SER B 1 279 ? 26.826 -19.762 62.538  1.00 32.68 ? 270 SER B CA    1 
ATOM   4801 C C     . SER B 1 279 ? 28.145 -19.622 63.288  1.00 35.19 ? 270 SER B C     1 
ATOM   4802 O O     . SER B 1 279 ? 29.188 -19.997 62.739  1.00 38.91 ? 270 SER B O     1 
ATOM   4803 C CB    . SER B 1 279 ? 26.842 -18.719 61.412  1.00 35.24 ? 270 SER B CB    1 
ATOM   4804 O OG    . SER B 1 279 ? 26.082 -19.116 60.277  1.00 38.43 ? 270 SER B OG    1 
ATOM   4805 N N     . GLY B 1 280 ? 28.132 -19.046 64.488  1.00 31.35 ? 271 GLY B N     1 
ATOM   4806 C CA    . GLY B 1 280 ? 29.373 -18.721 65.175  1.00 34.02 ? 271 GLY B CA    1 
ATOM   4807 C C     . GLY B 1 280 ? 30.245 -17.705 64.463  1.00 36.61 ? 271 GLY B C     1 
ATOM   4808 O O     . GLY B 1 280 ? 31.464 -17.701 64.667  1.00 36.81 ? 271 GLY B O     1 
ATOM   4809 N N     . SER B 1 281 ? 29.654 -16.817 63.655  1.00 30.63 ? 272 SER B N     1 
ATOM   4810 C CA    . SER B 1 281 ? 30.406 -15.842 62.877  1.00 31.85 ? 272 SER B CA    1 
ATOM   4811 C C     . SER B 1 281 ? 29.513 -14.635 62.640  1.00 27.24 ? 272 SER B C     1 
ATOM   4812 O O     . SER B 1 281 ? 28.293 -14.762 62.629  1.00 33.43 ? 272 SER B O     1 
ATOM   4813 C CB    . SER B 1 281 ? 30.871 -16.446 61.540  1.00 32.58 ? 272 SER B CB    1 
ATOM   4814 O OG    . SER B 1 281 ? 31.453 -15.456 60.708  1.00 38.83 ? 272 SER B OG    1 
ATOM   4815 N N     . LYS B 1 282 ? 30.119 -13.471 62.455  1.00 30.29 ? 273 LYS B N     1 
ATOM   4816 C CA    . LYS B 1 282 ? 29.377 -12.260 62.120  1.00 25.45 ? 273 LYS B CA    1 
ATOM   4817 C C     . LYS B 1 282 ? 29.275 -12.086 60.601  1.00 20.50 ? 273 LYS B C     1 
ATOM   4818 O O     . LYS B 1 282 ? 30.223 -12.379 59.872  1.00 19.37 ? 273 LYS B O     1 
ATOM   4819 C CB    . LYS B 1 282 ? 30.060 -11.038 62.723  1.00 25.27 ? 273 LYS B CB    1 
ATOM   4820 C CG    . LYS B 1 282 ? 30.184 -11.081 64.214  1.00 32.31 ? 273 LYS B CG    1 
ATOM   4821 C CD    . LYS B 1 282 ? 29.025 -10.398 64.882  1.00 30.51 ? 273 LYS B CD    1 
ATOM   4822 C CE    . LYS B 1 282 ? 29.222 -10.359 66.392  1.00 35.08 ? 273 LYS B CE    1 
ATOM   4823 N NZ    . LYS B 1 282 ? 29.230 -8.938  66.893  1.00 38.02 ? 273 LYS B NZ    1 
ATOM   4824 N N     . LEU B 1 283 ? 28.128 -11.601 60.142  1.00 17.54 ? 274 LEU B N     1 
ATOM   4825 C CA    . LEU B 1 283 ? 27.981 -11.112 58.771  1.00 19.75 ? 274 LEU B CA    1 
ATOM   4826 C C     . LEU B 1 283 ? 28.981 -9.993  58.495  1.00 21.88 ? 274 LEU B C     1 
ATOM   4827 O O     . LEU B 1 283 ? 29.503 -9.356  59.409  1.00 18.28 ? 274 LEU B O     1 
ATOM   4828 C CB    . LEU B 1 283 ? 26.552 -10.599 58.543  1.00 19.51 ? 274 LEU B CB    1 
ATOM   4829 C CG    . LEU B 1 283 ? 25.438 -11.646 58.690  1.00 19.70 ? 274 LEU B CG    1 
ATOM   4830 C CD1   . LEU B 1 283 ? 24.072 -11.012 58.696  1.00 21.22 ? 274 LEU B CD1   1 
ATOM   4831 C CD2   . LEU B 1 283 ? 25.511 -12.697 57.584  1.00 18.60 ? 274 LEU B CD2   1 
ATOM   4832 N N     . ALA B 1 284 ? 29.217 -9.717  57.207  1.00 17.65 ? 275 ALA B N     1 
ATOM   4833 C CA    . ALA B 1 284 ? 30.031 -8.559  56.875  1.00 17.88 ? 275 ALA B CA    1 
ATOM   4834 C C     . ALA B 1 284 ? 29.395 -7.275  57.411  1.00 15.29 ? 275 ALA B C     1 
ATOM   4835 O O     . ALA B 1 284 ? 30.089 -6.432  57.984  1.00 17.19 ? 275 ALA B O     1 
ATOM   4836 C CB    . ALA B 1 284 ? 30.261 -8.470  55.363  1.00 20.60 ? 275 ALA B CB    1 
ATOM   4837 N N     . TYR B 1 285 ? 28.084 -7.120  57.253  1.00 16.78 ? 276 TYR B N     1 
ATOM   4838 C CA    . TYR B 1 285 ? 27.405 -5.903  57.679  1.00 15.63 ? 276 TYR B CA    1 
ATOM   4839 C C     . TYR B 1 285 ? 25.921 -6.045  57.402  1.00 12.34 ? 276 TYR B C     1 
ATOM   4840 O O     . TYR B 1 285 ? 25.494 -6.894  56.615  1.00 16.45 ? 276 TYR B O     1 
ATOM   4841 C CB    . TYR B 1 285 ? 27.911 -4.656  56.927  1.00 14.22 ? 276 TYR B CB    1 
ATOM   4842 C CG    . TYR B 1 285 ? 27.777 -4.795  55.419  1.00 14.35 ? 276 TYR B CG    1 
ATOM   4843 C CD1   . TYR B 1 285 ? 26.549 -4.539  54.776  1.00 15.78 ? 276 TYR B CD1   1 
ATOM   4844 C CD2   . TYR B 1 285 ? 28.878 -5.143  54.627  1.00 16.10 ? 276 TYR B CD2   1 
ATOM   4845 C CE1   . TYR B 1 285 ? 26.446 -4.639  53.382  1.00 13.40 ? 276 TYR B CE1   1 
ATOM   4846 C CE2   . TYR B 1 285 ? 28.761 -5.260  53.229  1.00 16.26 ? 276 TYR B CE2   1 
ATOM   4847 C CZ    . TYR B 1 285 ? 27.540 -4.997  52.637  1.00 14.20 ? 276 TYR B CZ    1 
ATOM   4848 O OH    . TYR B 1 285 ? 27.377 -5.097  51.263  1.00 15.59 ? 276 TYR B OH    1 
ATOM   4849 N N     . LEU B 1 286 ? 25.153 -5.204  58.077  1.00 14.73 ? 277 LEU B N     1 
ATOM   4850 C CA    . LEU B 1 286 ? 23.769 -4.878  57.777  1.00 16.88 ? 277 LEU B CA    1 
ATOM   4851 C C     . LEU B 1 286 ? 23.789 -3.488  57.157  1.00 19.54 ? 277 LEU B C     1 
ATOM   4852 O O     . LEU B 1 286 ? 24.410 -2.566  57.704  1.00 15.72 ? 277 LEU B O     1 
ATOM   4853 C CB    . LEU B 1 286 ? 22.897 -4.876  59.047  1.00 15.06 ? 277 LEU B CB    1 
ATOM   4854 C CG    . LEU B 1 286 ? 21.447 -4.380  58.930  1.00 16.68 ? 277 LEU B CG    1 
ATOM   4855 C CD1   . LEU B 1 286 ? 20.612 -5.256  57.968  1.00 17.87 ? 277 LEU B CD1   1 
ATOM   4856 C CD2   . LEU B 1 286 ? 20.773 -4.262  60.395  1.00 18.66 ? 277 LEU B CD2   1 
ATOM   4857 N N     . HIS B 1 287 ? 23.092 -3.334  56.047  1.00 13.62 ? 278 HIS B N     1 
ATOM   4858 C CA    . HIS B 1 287 ? 23.121 -2.112  55.237  1.00 12.75 ? 278 HIS B CA    1 
ATOM   4859 C C     . HIS B 1 287 ? 21.680 -1.610  55.135  1.00 13.42 ? 278 HIS B C     1 
ATOM   4860 O O     . HIS B 1 287 ? 20.843 -2.271  54.538  1.00 16.27 ? 278 HIS B O     1 
ATOM   4861 C CB    . HIS B 1 287 ? 23.721 -2.477  53.884  1.00 12.16 ? 278 HIS B CB    1 
ATOM   4862 C CG    . HIS B 1 287 ? 23.966 -1.326  52.951  1.00 17.63 ? 278 HIS B CG    1 
ATOM   4863 N ND1   . HIS B 1 287 ? 24.482 -1.531  51.690  1.00 15.44 ? 278 HIS B ND1   1 
ATOM   4864 C CD2   . HIS B 1 287 ? 23.801 0.014   53.084  1.00 14.51 ? 278 HIS B CD2   1 
ATOM   4865 C CE1   . HIS B 1 287 ? 24.619 -0.369  51.085  1.00 13.53 ? 278 HIS B CE1   1 
ATOM   4866 N NE2   . HIS B 1 287 ? 24.220 0.589   51.908  1.00 15.15 ? 278 HIS B NE2   1 
ATOM   4867 N N     . VAL B 1 288 ? 21.349 -0.491  55.784  1.00 13.90 ? 279 VAL B N     1 
ATOM   4868 C CA    . VAL B 1 288 ? 19.958 -0.023  55.824  1.00 15.22 ? 279 VAL B CA    1 
ATOM   4869 C C     . VAL B 1 288 ? 19.878 1.268   55.016  1.00 15.38 ? 279 VAL B C     1 
ATOM   4870 O O     . VAL B 1 288 ? 20.661 2.192   55.248  1.00 14.79 ? 279 VAL B O     1 
ATOM   4871 C CB    . VAL B 1 288 ? 19.459 0.200   57.263  1.00 15.39 ? 279 VAL B CB    1 
ATOM   4872 C CG1   . VAL B 1 288 ? 18.040 0.822   57.215  1.00 15.38 ? 279 VAL B CG1   1 
ATOM   4873 C CG2   . VAL B 1 288 ? 19.445 -1.144  58.050  1.00 19.63 ? 279 VAL B CG2   1 
ATOM   4874 N N     . THR B 1 289 ? 18.940 1.342   54.077  1.00 14.04 ? 280 THR B N     1 
ATOM   4875 C CA    . THR B 1 289 ? 18.819 2.536   53.253  1.00 14.42 ? 280 THR B CA    1 
ATOM   4876 C C     . THR B 1 289 ? 17.441 3.159   53.474  1.00 18.09 ? 280 THR B C     1 
ATOM   4877 O O     . THR B 1 289 ? 16.467 2.448   53.761  1.00 17.72 ? 280 THR B O     1 
ATOM   4878 C CB    . THR B 1 289 ? 19.113 2.219   51.767  1.00 18.50 ? 280 THR B CB    1 
ATOM   4879 O OG1   . THR B 1 289 ? 19.254 3.453   51.039  1.00 17.90 ? 280 THR B OG1   1 
ATOM   4880 C CG2   . THR B 1 289 ? 18.019 1.391   51.127  1.00 16.10 ? 280 THR B CG2   1 
ATOM   4881 N N     . GLN B 1 290 ? 17.394 4.496   53.473  1.00 17.63 ? 281 GLN B N     1 
ATOM   4882 C CA    . GLN B 1 290 ? 16.210 5.276   53.777  1.00 17.40 ? 281 GLN B CA    1 
ATOM   4883 C C     . GLN B 1 290 ? 15.891 6.222   52.643  1.00 16.57 ? 281 GLN B C     1 
ATOM   4884 O O     . GLN B 1 290 ? 16.776 6.571   51.867  1.00 15.46 ? 281 GLN B O     1 
ATOM   4885 C CB    . GLN B 1 290 ? 16.441 6.115   55.050  1.00 18.48 ? 281 GLN B CB    1 
ATOM   4886 C CG    . GLN B 1 290 ? 17.545 7.164   54.872  1.00 19.33 ? 281 GLN B CG    1 
ATOM   4887 C CD    . GLN B 1 290 ? 17.915 7.880   56.160  1.00 22.06 ? 281 GLN B CD    1 
ATOM   4888 O OE1   . GLN B 1 290 ? 17.334 7.627   57.212  1.00 20.88 ? 281 GLN B OE1   1 
ATOM   4889 N NE2   . GLN B 1 290 ? 18.893 8.776   56.080  1.00 22.00 ? 281 GLN B NE2   1 
ATOM   4890 N N     . PRO B 1 291 ? 14.674 6.748   52.575  1.00 20.11 ? 282 PRO B N     1 
ATOM   4891 C CA    . PRO B 1 291 ? 14.399 7.767   51.556  1.00 21.70 ? 282 PRO B CA    1 
ATOM   4892 C C     . PRO B 1 291 ? 15.415 8.895   51.635  1.00 25.53 ? 282 PRO B C     1 
ATOM   4893 O O     . PRO B 1 291 ? 15.815 9.329   52.727  1.00 25.03 ? 282 PRO B O     1 
ATOM   4894 C CB    . PRO B 1 291 ? 12.987 8.250   51.900  1.00 19.80 ? 282 PRO B CB    1 
ATOM   4895 C CG    . PRO B 1 291 ? 12.385 7.193   52.720  1.00 21.51 ? 282 PRO B CG    1 
ATOM   4896 C CD    . PRO B 1 291 ? 13.556 6.614   53.523  1.00 21.82 ? 282 PRO B CD    1 
ATOM   4897 N N     . GLY B 1 292 ? 15.871 9.337   50.458  1.00 22.05 ? 283 GLY B N     1 
ATOM   4898 C CA    . GLY B 1 292 ? 16.900 10.369  50.403  1.00 20.40 ? 283 GLY B CA    1 
ATOM   4899 C C     . GLY B 1 292 ? 16.403 11.726  50.883  1.00 29.08 ? 283 GLY B C     1 
ATOM   4900 O O     . GLY B 1 292 ? 17.086 12.405  51.655  1.00 29.55 ? 283 GLY B O     1 
ATOM   4901 N N     . ASP B 1 293 ? 15.218 12.142  50.425  1.00 32.62 ? 284 ASP B N     1 
ATOM   4902 C CA    . ASP B 1 293 ? 14.658 13.452  50.808  1.00 39.13 ? 284 ASP B CA    1 
ATOM   4903 C C     . ASP B 1 293 ? 13.842 13.353  52.087  1.00 41.93 ? 284 ASP B C     1 
ATOM   4904 O O     . ASP B 1 293 ? 12.851 12.625  52.126  1.00 43.15 ? 284 ASP B O     1 
ATOM   4905 C CB    . ASP B 1 293 ? 13.776 14.030  49.703  1.00 35.49 ? 284 ASP B CB    1 
ATOM   4906 N N     . GLY B 1 296 ? 10.587 16.416  55.407  1.00 42.10 ? 287 GLY B N     1 
ATOM   4907 C CA    . GLY B 1 296 ? 11.112 17.038  56.616  1.00 47.31 ? 287 GLY B CA    1 
ATOM   4908 C C     . GLY B 1 296 ? 10.988 16.254  57.922  1.00 55.05 ? 287 GLY B C     1 
ATOM   4909 O O     . GLY B 1 296 ? 11.106 16.836  59.004  1.00 54.34 ? 287 GLY B O     1 
ATOM   4910 N N     . SER B 1 297 ? 10.759 14.942  57.844  1.00 57.14 ? 288 SER B N     1 
ATOM   4911 C CA    . SER B 1 297 ? 10.698 14.103  59.048  1.00 51.50 ? 288 SER B CA    1 
ATOM   4912 C C     . SER B 1 297 ? 12.093 13.622  59.461  1.00 50.26 ? 288 SER B C     1 
ATOM   4913 O O     . SER B 1 297 ? 12.331 12.432  59.698  1.00 46.45 ? 288 SER B O     1 
ATOM   4914 C CB    . SER B 1 297 ? 9.749  12.931  58.826  1.00 42.77 ? 288 SER B CB    1 
ATOM   4915 N N     . GLU B 1 298 ? 13.020 14.581  59.575  1.00 46.31 ? 289 GLU B N     1 
ATOM   4916 C CA    . GLU B 1 298 ? 14.445 14.310  59.719  1.00 47.25 ? 289 GLU B CA    1 
ATOM   4917 C C     . GLU B 1 298 ? 14.765 13.496  60.966  1.00 51.26 ? 289 GLU B C     1 
ATOM   4918 O O     . GLU B 1 298 ? 15.194 12.338  60.861  1.00 45.65 ? 289 GLU B O     1 
ATOM   4919 C CB    . GLU B 1 298 ? 15.240 15.619  59.743  1.00 49.32 ? 289 GLU B CB    1 
ATOM   4920 N N     . GLU B 1 299 ? 14.577 14.088  62.150  1.00 43.81 ? 290 GLU B N     1 
ATOM   4921 C CA    . GLU B 1 299 ? 14.999 13.406  63.369  1.00 42.98 ? 290 GLU B CA    1 
ATOM   4922 C C     . GLU B 1 299 ? 14.230 12.105  63.609  1.00 36.50 ? 290 GLU B C     1 
ATOM   4923 O O     . GLU B 1 299 ? 14.725 11.243  64.345  1.00 41.49 ? 290 GLU B O     1 
ATOM   4924 C CB    . GLU B 1 299 ? 14.869 14.344  64.570  1.00 40.38 ? 290 GLU B CB    1 
ATOM   4925 N N     . GLU B 1 300 ? 13.046 11.928  63.006  1.00 40.64 ? 291 GLU B N     1 
ATOM   4926 C CA    . GLU B 1 300 ? 12.365 10.636  63.101  1.00 33.52 ? 291 GLU B CA    1 
ATOM   4927 C C     . GLU B 1 300 ? 13.132 9.564   62.340  1.00 38.74 ? 291 GLU B C     1 
ATOM   4928 O O     . GLU B 1 300 ? 13.422 8.489   62.883  1.00 40.23 ? 291 GLU B O     1 
ATOM   4929 C CB    . GLU B 1 300 ? 10.935 10.734  62.571  1.00 32.68 ? 291 GLU B CB    1 
ATOM   4930 N N     . GLU B 1 301 ? 13.470 9.839   61.076  1.00 40.65 ? 292 GLU B N     1 
ATOM   4931 C CA    . GLU B 1 301 ? 14.157 8.838   60.266  1.00 38.98 ? 292 GLU B CA    1 
ATOM   4932 C C     . GLU B 1 301 ? 15.522 8.521   60.853  1.00 34.87 ? 292 GLU B C     1 
ATOM   4933 O O     . GLU B 1 301 ? 15.966 7.363   60.807  1.00 30.40 ? 292 GLU B O     1 
ATOM   4934 C CB    . GLU B 1 301 ? 14.283 9.314   58.814  1.00 36.64 ? 292 GLU B CB    1 
ATOM   4935 N N     . ALA B 1 302 ? 16.187 9.538   61.428  1.00 34.21 ? 293 ALA B N     1 
ATOM   4936 C CA    . ALA B 1 302 ? 17.461 9.336   62.118  1.00 34.80 ? 293 ALA B CA    1 
ATOM   4937 C C     . ALA B 1 302 ? 17.303 8.383   63.293  1.00 34.57 ? 293 ALA B C     1 
ATOM   4938 O O     . ALA B 1 302 ? 18.208 7.577   63.592  1.00 28.39 ? 293 ALA B O     1 
ATOM   4939 C CB    . ALA B 1 302 ? 18.022 10.675  62.604  1.00 35.04 ? 293 ALA B CB    1 
ATOM   4940 N N     . ARG B 1 303 ? 16.151 8.459   63.961  1.00 33.08 ? 294 ARG B N     1 
ATOM   4941 C CA    . ARG B 1 303 ? 15.887 7.601   65.105  1.00 36.33 ? 294 ARG B CA    1 
ATOM   4942 C C     . ARG B 1 303 ? 15.582 6.183   64.657  1.00 32.80 ? 294 ARG B C     1 
ATOM   4943 O O     . ARG B 1 303 ? 16.007 5.222   65.311  1.00 29.28 ? 294 ARG B O     1 
ATOM   4944 C CB    . ARG B 1 303 ? 14.722 8.157   65.924  1.00 38.69 ? 294 ARG B CB    1 
ATOM   4945 C CG    . ARG B 1 303 ? 14.371 7.380   67.161  1.00 33.49 ? 294 ARG B CG    1 
ATOM   4946 C CD    . ARG B 1 303 ? 13.145 8.005   67.809  1.00 43.25 ? 294 ARG B CD    1 
ATOM   4947 N NE    . ARG B 1 303 ? 11.957 7.909   66.961  1.00 39.78 ? 294 ARG B NE    1 
ATOM   4948 C CZ    . ARG B 1 303 ? 10.843 8.612   67.138  1.00 36.22 ? 294 ARG B CZ    1 
ATOM   4949 N NH1   . ARG B 1 303 ? 10.709 9.463   68.147  1.00 45.77 ? 294 ARG B NH1   1 
ATOM   4950 N NH2   . ARG B 1 303 ? 9.815  8.411   66.325  1.00 42.32 ? 294 ARG B NH2   1 
ATOM   4951 N N     . LEU B 1 304 ? 14.817 6.026   63.571  1.00 28.40 ? 295 LEU B N     1 
ATOM   4952 C CA    . LEU B 1 304 ? 14.612 4.684   63.028  1.00 29.30 ? 295 LEU B CA    1 
ATOM   4953 C C     . LEU B 1 304 ? 15.950 4.053   62.646  1.00 25.23 ? 295 LEU B C     1 
ATOM   4954 O O     . LEU B 1 304 ? 16.207 2.877   62.943  1.00 25.56 ? 295 LEU B O     1 
ATOM   4955 C CB    . LEU B 1 304 ? 13.660 4.737   61.828  1.00 32.15 ? 295 LEU B CB    1 
ATOM   4956 C CG    . LEU B 1 304 ? 13.063 3.475   61.189  1.00 29.32 ? 295 LEU B CG    1 
ATOM   4957 C CD1   . LEU B 1 304 ? 12.254 3.899   59.976  1.00 42.67 ? 295 LEU B CD1   1 
ATOM   4958 C CD2   . LEU B 1 304 ? 14.063 2.452   60.723  1.00 32.55 ? 295 LEU B CD2   1 
ATOM   4959 N N     . MET B 1 305 ? 16.806 4.813   61.960  1.00 20.89 ? 296 MET B N     1 
ATOM   4960 C CA    . MET B 1 305 ? 18.156 4.336   61.655  1.00 23.15 ? 296 MET B CA    1 
ATOM   4961 C C     . MET B 1 305 ? 18.895 3.870   62.913  1.00 21.65 ? 296 MET B C     1 
ATOM   4962 O O     . MET B 1 305 ? 19.480 2.785   62.939  1.00 20.32 ? 296 MET B O     1 
ATOM   4963 C CB    . MET B 1 305 ? 18.972 5.450   60.999  1.00 25.20 ? 296 MET B CB    1 
ATOM   4964 C CG    . MET B 1 305 ? 20.019 5.074   59.946  1.00 24.03 ? 296 MET B CG    1 
ATOM   4965 S SD    . MET B 1 305 ? 19.829 3.774   58.706  1.00 22.23 ? 296 MET B SD    1 
ATOM   4966 C CE    . MET B 1 305 ? 19.263 4.737   57.266  1.00 22.48 ? 296 MET B CE    1 
ATOM   4967 N N     . ARG B 1 306 ? 18.965 4.715   63.943  1.00 24.94 ? 297 ARG B N     1 
ATOM   4968 C CA    . ARG B 1 306 ? 19.817 4.332   65.068  1.00 24.22 ? 297 ARG B CA    1 
ATOM   4969 C C     . ARG B 1 306 ? 19.192 3.195   65.865  1.00 20.58 ? 297 ARG B C     1 
ATOM   4970 O O     . ARG B 1 306 ? 19.922 2.381   66.440  1.00 22.24 ? 297 ARG B O     1 
ATOM   4971 C CB    . ARG B 1 306 ? 20.161 5.564   65.934  1.00 25.48 ? 297 ARG B CB    1 
ATOM   4972 C CG    . ARG B 1 306 ? 21.045 5.222   67.168  1.00 30.59 ? 297 ARG B CG    1 
ATOM   4973 C CD    . ARG B 1 306 ? 22.539 5.287   66.830  1.00 32.19 ? 297 ARG B CD    1 
ATOM   4974 N NE    . ARG B 1 306 ? 23.381 4.557   67.779  1.00 36.62 ? 297 ARG B NE    1 
ATOM   4975 C CZ    . ARG B 1 306 ? 24.338 5.118   68.513  1.00 38.24 ? 297 ARG B CZ    1 
ATOM   4976 N NH1   . ARG B 1 306 ? 24.624 6.410   68.412  1.00 31.29 ? 297 ARG B NH1   1 
ATOM   4977 N NH2   . ARG B 1 306 ? 25.041 4.362   69.356  1.00 44.72 ? 297 ARG B NH2   1 
ATOM   4978 N N     . THR B 1 307 ? 17.872 3.040   65.797  1.00 19.83 ? 298 THR B N     1 
ATOM   4979 C CA    . THR B 1 307 ? 17.211 1.949   66.505  1.00 20.58 ? 298 THR B CA    1 
ATOM   4980 C C     . THR B 1 307 ? 17.554 0.590   65.892  1.00 23.46 ? 298 THR B C     1 
ATOM   4981 O O     . THR B 1 307 ? 17.692 -0.414  66.617  1.00 19.18 ? 298 THR B O     1 
ATOM   4982 C CB    . THR B 1 307 ? 15.706 2.198   66.502  1.00 26.22 ? 298 THR B CB    1 
ATOM   4983 O OG1   . THR B 1 307 ? 15.432 3.437   67.197  1.00 29.98 ? 298 THR B OG1   1 
ATOM   4984 C CG2   . THR B 1 307 ? 14.969 1.069   67.131  1.00 22.64 ? 298 THR B CG2   1 
ATOM   4985 N N     . LEU B 1 308 ? 17.703 0.531   64.562  1.00 21.28 ? 299 LEU B N     1 
ATOM   4986 C CA    . LEU B 1 308 ? 18.082 -0.726  63.915  1.00 16.46 ? 299 LEU B CA    1 
ATOM   4987 C C     . LEU B 1 308 ? 19.545 -1.008  64.169  1.00 16.32 ? 299 LEU B C     1 
ATOM   4988 O O     . LEU B 1 308 ? 19.930 -2.148  64.476  1.00 19.36 ? 299 LEU B O     1 
ATOM   4989 C CB    . LEU B 1 308 ? 17.808 -0.671  62.401  1.00 19.60 ? 299 LEU B CB    1 
ATOM   4990 C CG    . LEU B 1 308 ? 16.326 -0.506  61.983  1.00 24.12 ? 299 LEU B CG    1 
ATOM   4991 C CD1   . LEU B 1 308 ? 16.143 -0.652  60.435  1.00 24.64 ? 299 LEU B CD1   1 
ATOM   4992 C CD2   . LEU B 1 308 ? 15.425 -1.530  62.683  1.00 21.44 ? 299 LEU B CD2   1 
ATOM   4993 N N     . ARG B 1 309 ? 20.370 0.038   64.068  1.00 18.03 ? 300 ARG B N     1 
ATOM   4994 C CA    . ARG B 1 309 ? 21.779 -0.067  64.405  1.00 17.30 ? 300 ARG B CA    1 
ATOM   4995 C C     . ARG B 1 309 ? 21.971 -0.621  65.814  1.00 15.24 ? 300 ARG B C     1 
ATOM   4996 O O     . ARG B 1 309 ? 22.752 -1.557  66.029  1.00 18.40 ? 300 ARG B O     1 
ATOM   4997 C CB    . ARG B 1 309 ? 22.445 1.313   64.260  1.00 17.44 ? 300 ARG B CB    1 
ATOM   4998 C CG    . ARG B 1 309 ? 23.979 1.269   64.201  1.00 18.50 ? 300 ARG B CG    1 
ATOM   4999 C CD    . ARG B 1 309 ? 24.618 1.243   65.603  1.00 18.89 ? 300 ARG B CD    1 
ATOM   5000 N NE    . ARG B 1 309 ? 25.931 1.863   65.554  1.00 20.59 ? 300 ARG B NE    1 
ATOM   5001 C CZ    . ARG B 1 309 ? 26.998 1.272   65.039  1.00 20.02 ? 300 ARG B CZ    1 
ATOM   5002 N NH1   . ARG B 1 309 ? 26.959 0.003   64.615  1.00 19.47 ? 300 ARG B NH1   1 
ATOM   5003 N NH2   . ARG B 1 309 ? 28.128 1.955   64.943  1.00 24.86 ? 300 ARG B NH2   1 
ATOM   5004 N N     . ASN B 1 310 ? 21.297 -0.016  66.795  1.00 16.58 ? 301 ASN B N     1 
ATOM   5005 C CA    . ASN B 1 310 ? 21.418 -0.439  68.193  1.00 17.26 ? 301 ASN B CA    1 
ATOM   5006 C C     . ASN B 1 310 ? 20.982 -1.878  68.404  1.00 18.46 ? 301 ASN B C     1 
ATOM   5007 O O     . ASN B 1 310 ? 21.476 -2.562  69.319  1.00 19.12 ? 301 ASN B O     1 
ATOM   5008 C CB    . ASN B 1 310 ? 20.570 0.473   69.064  1.00 18.39 ? 301 ASN B CB    1 
ATOM   5009 C CG    . ASN B 1 310 ? 21.217 1.794   69.318  1.00 20.20 ? 301 ASN B CG    1 
ATOM   5010 O OD1   . ASN B 1 310 ? 22.409 1.964   69.073  1.00 19.61 ? 301 ASN B OD1   1 
ATOM   5011 N ND2   . ASN B 1 310 ? 20.436 2.745   69.845  1.00 23.19 ? 301 ASN B ND2   1 
ATOM   5012 N N     . ALA B 1 311 ? 20.045 -2.360  67.579  1.00 17.87 ? 302 ALA B N     1 
ATOM   5013 C CA    . ALA B 1 311 ? 19.580 -3.726  67.732  1.00 16.28 ? 302 ALA B CA    1 
ATOM   5014 C C     . ALA B 1 311 ? 20.505 -4.738  67.092  1.00 16.76 ? 302 ALA B C     1 
ATOM   5015 O O     . ALA B 1 311 ? 20.402 -5.928  67.414  1.00 16.46 ? 302 ALA B O     1 
ATOM   5016 C CB    . ALA B 1 311 ? 18.177 -3.901  67.157  1.00 16.92 ? 302 ALA B CB    1 
ATOM   5017 N N     . TYR B 1 312 ? 21.367 -4.322  66.168  1.00 15.70 ? 303 TYR B N     1 
ATOM   5018 C CA    . TYR B 1 312 ? 22.078 -5.268  65.311  1.00 18.65 ? 303 TYR B CA    1 
ATOM   5019 C C     . TYR B 1 312 ? 23.477 -5.510  65.892  1.00 19.47 ? 303 TYR B C     1 
ATOM   5020 O O     . TYR B 1 312 ? 24.177 -4.558  66.242  1.00 18.68 ? 303 TYR B O     1 
ATOM   5021 C CB    . TYR B 1 312 ? 22.144 -4.763  63.860  1.00 18.31 ? 303 TYR B CB    1 
ATOM   5022 C CG    . TYR B 1 312 ? 23.075 -5.640  63.045  1.00 13.66 ? 303 TYR B CG    1 
ATOM   5023 C CD1   . TYR B 1 312 ? 22.865 -7.009  62.981  1.00 17.27 ? 303 TYR B CD1   1 
ATOM   5024 C CD2   . TYR B 1 312 ? 24.206 -5.119  62.465  1.00 16.00 ? 303 TYR B CD2   1 
ATOM   5025 C CE1   . TYR B 1 312 ? 23.746 -7.848  62.297  1.00 16.41 ? 303 TYR B CE1   1 
ATOM   5026 C CE2   . TYR B 1 312 ? 25.101 -5.949  61.750  1.00 18.69 ? 303 TYR B CE2   1 
ATOM   5027 C CZ    . TYR B 1 312 ? 24.862 -7.316  61.705  1.00 17.79 ? 303 TYR B CZ    1 
ATOM   5028 O OH    . TYR B 1 312 ? 25.731 -8.125  61.022  1.00 19.13 ? 303 TYR B OH    1 
ATOM   5029 N N     . GLN B 1 313 ? 23.844 -6.783  66.069  1.00 17.08 ? 304 GLN B N     1 
ATOM   5030 C CA    . GLN B 1 313 ? 25.158 -7.140  66.611  1.00 17.93 ? 304 GLN B CA    1 
ATOM   5031 C C     . GLN B 1 313 ? 26.178 -7.191  65.471  1.00 23.42 ? 304 GLN B C     1 
ATOM   5032 O O     . GLN B 1 313 ? 26.574 -8.260  64.991  1.00 19.71 ? 304 GLN B O     1 
ATOM   5033 C CB    . GLN B 1 313 ? 25.098 -8.467  67.368  1.00 20.33 ? 304 GLN B CB    1 
ATOM   5034 C CG    . GLN B 1 313 ? 24.159 -8.494  68.573  1.00 20.42 ? 304 GLN B CG    1 
ATOM   5035 C CD    . GLN B 1 313 ? 24.056 -9.873  69.224  1.00 23.95 ? 304 GLN B CD    1 
ATOM   5036 O OE1   . GLN B 1 313 ? 24.916 -10.731 69.049  1.00 23.44 ? 304 GLN B OE1   1 
ATOM   5037 N NE2   . GLN B 1 313 ? 22.976 -10.087 69.964  1.00 23.22 ? 304 GLN B NE2   1 
ATOM   5038 N N     . GLY B 1 314 ? 26.646 -6.018  65.050  1.00 16.95 ? 305 GLY B N     1 
ATOM   5039 C CA    . GLY B 1 314 ? 27.691 -6.017  64.035  1.00 17.30 ? 305 GLY B CA    1 
ATOM   5040 C C     . GLY B 1 314 ? 27.806 -4.669  63.338  1.00 16.81 ? 305 GLY B C     1 
ATOM   5041 O O     . GLY B 1 314 ? 27.340 -3.642  63.845  1.00 17.86 ? 305 GLY B O     1 
ATOM   5042 N N     . THR B 1 315 ? 28.455 -4.726  62.181  1.00 18.67 ? 306 THR B N     1 
ATOM   5043 C CA    . THR B 1 315 ? 28.776 -3.554  61.380  1.00 18.29 ? 306 THR B CA    1 
ATOM   5044 C C     . THR B 1 315 ? 27.517 -3.040  60.689  1.00 18.51 ? 306 THR B C     1 
ATOM   5045 O O     . THR B 1 315 ? 26.747 -3.811  60.084  1.00 15.68 ? 306 THR B O     1 
ATOM   5046 C CB    . THR B 1 315 ? 29.847 -3.919  60.350  1.00 21.84 ? 306 THR B CB    1 
ATOM   5047 O OG1   . THR B 1 315 ? 31.057 -4.290  61.025  1.00 20.71 ? 306 THR B OG1   1 
ATOM   5048 C CG2   . THR B 1 315 ? 30.110 -2.741  59.348  1.00 19.86 ? 306 THR B CG2   1 
ATOM   5049 N N     . PHE B 1 316 ? 27.328 -1.728  60.742  1.00 14.72 ? 307 PHE B N     1 
ATOM   5050 C CA    . PHE B 1 316 ? 26.138 -1.090  60.192  1.00 12.59 ? 307 PHE B CA    1 
ATOM   5051 C C     . PHE B 1 316 ? 26.559 -0.071  59.137  1.00 15.76 ? 307 PHE B C     1 
ATOM   5052 O O     . PHE B 1 316 ? 27.340 0.852   59.434  1.00 15.96 ? 307 PHE B O     1 
ATOM   5053 C CB    . PHE B 1 316 ? 25.382 -0.378  61.318  1.00 16.06 ? 307 PHE B CB    1 
ATOM   5054 C CG    . PHE B 1 316 ? 24.003 0.096   60.953  1.00 15.04 ? 307 PHE B CG    1 
ATOM   5055 C CD1   . PHE B 1 316 ? 22.918 -0.744  61.108  1.00 18.28 ? 307 PHE B CD1   1 
ATOM   5056 C CD2   . PHE B 1 316 ? 23.795 1.414   60.525  1.00 17.11 ? 307 PHE B CD2   1 
ATOM   5057 C CE1   . PHE B 1 316 ? 21.635 -0.321  60.822  1.00 20.13 ? 307 PHE B CE1   1 
ATOM   5058 C CE2   . PHE B 1 316 ? 22.509 1.854   60.221  1.00 21.49 ? 307 PHE B CE2   1 
ATOM   5059 C CZ    . PHE B 1 316 ? 21.425 0.992   60.377  1.00 18.81 ? 307 PHE B CZ    1 
ATOM   5060 N N     . ILE B 1 317 ? 25.987 -0.183  57.946  1.00 16.52 ? 308 ILE B N     1 
ATOM   5061 C CA    . ILE B 1 317 ? 26.204 0.806   56.895  1.00 14.29 ? 308 ILE B CA    1 
ATOM   5062 C C     . ILE B 1 317 ? 24.903 1.602   56.734  1.00 16.52 ? 308 ILE B C     1 
ATOM   5063 O O     . ILE B 1 317 ? 23.835 1.019   56.499  1.00 15.41 ? 308 ILE B O     1 
ATOM   5064 C CB    . ILE B 1 317 ? 26.616 0.148   55.564  1.00 14.14 ? 308 ILE B CB    1 
ATOM   5065 C CG1   . ILE B 1 317 ? 27.792 -0.821  55.700  1.00 13.85 ? 308 ILE B CG1   1 
ATOM   5066 C CG2   . ILE B 1 317 ? 26.956 1.253   54.509  1.00 13.46 ? 308 ILE B CG2   1 
ATOM   5067 C CD1   . ILE B 1 317 ? 28.120 -1.542  54.328  1.00 15.52 ? 308 ILE B CD1   1 
ATOM   5068 N N     . CYS B 1 318 ? 24.983 2.932   56.832  1.00 15.24 ? 309 CYS B N     1 
ATOM   5069 C CA    . CYS B 1 318 ? 23.793 3.751   56.657  1.00 15.97 ? 309 CYS B CA    1 
ATOM   5070 C C     . CYS B 1 318 ? 23.827 4.368   55.272  1.00 17.18 ? 309 CYS B C     1 
ATOM   5071 O O     . CYS B 1 318 ? 24.906 4.565   54.708  1.00 15.76 ? 309 CYS B O     1 
ATOM   5072 C CB    . CYS B 1 318 ? 23.670 4.858   57.720  1.00 17.42 ? 309 CYS B CB    1 
ATOM   5073 S SG    . CYS B 1 318 ? 25.028 5.985   57.753  1.00 19.86 ? 309 CYS B SG    1 
ATOM   5074 N N     . SER B 1 319 ? 22.637 4.655   54.733  1.00 16.01 ? 310 SER B N     1 
ATOM   5075 C CA    . SER B 1 319 ? 22.513 5.028   53.325  1.00 17.03 ? 310 SER B CA    1 
ATOM   5076 C C     . SER B 1 319 ? 21.242 5.836   53.072  1.00 14.28 ? 310 SER B C     1 
ATOM   5077 O O     . SER B 1 319 ? 20.203 5.565   53.657  1.00 17.29 ? 310 SER B O     1 
ATOM   5078 C CB    . SER B 1 319 ? 22.507 3.774   52.448  1.00 16.82 ? 310 SER B CB    1 
ATOM   5079 O OG    . SER B 1 319 ? 21.851 4.033   51.233  1.00 20.56 ? 310 SER B OG    1 
ATOM   5080 N N     . GLY B 1 320 ? 21.329 6.805   52.161  1.00 14.84 ? 311 GLY B N     1 
ATOM   5081 C CA    . GLY B 1 320 ? 20.131 7.480   51.697  1.00 16.01 ? 311 GLY B CA    1 
ATOM   5082 C C     . GLY B 1 320 ? 20.129 8.951   52.106  1.00 17.77 ? 311 GLY B C     1 
ATOM   5083 O O     . GLY B 1 320 ? 19.787 9.312   53.239  1.00 17.13 ? 311 GLY B O     1 
ATOM   5084 N N     . GLY B 1 321 ? 20.555 9.805   51.180  1.00 16.76 ? 312 GLY B N     1 
ATOM   5085 C CA    . GLY B 1 321 ? 20.558 11.232  51.469  1.00 20.35 ? 312 GLY B CA    1 
ATOM   5086 C C     . GLY B 1 321 ? 21.688 11.736  52.334  1.00 23.16 ? 312 GLY B C     1 
ATOM   5087 O O     . GLY B 1 321 ? 21.629 12.887  52.785  1.00 24.28 ? 312 GLY B O     1 
ATOM   5088 N N     . TYR B 1 322 ? 22.736 10.946  52.557  1.00 18.21 ? 313 TYR B N     1 
ATOM   5089 C CA    . TYR B 1 322 ? 23.839 11.426  53.364  1.00 22.59 ? 313 TYR B CA    1 
ATOM   5090 C C     . TYR B 1 322 ? 24.696 12.421  52.576  1.00 23.09 ? 313 TYR B C     1 
ATOM   5091 O O     . TYR B 1 322 ? 24.851 12.332  51.349  1.00 21.74 ? 313 TYR B O     1 
ATOM   5092 C CB    . TYR B 1 322 ? 24.674 10.257  53.895  1.00 19.09 ? 313 TYR B CB    1 
ATOM   5093 C CG    . TYR B 1 322 ? 23.959 9.567   55.056  1.00 18.12 ? 313 TYR B CG    1 
ATOM   5094 C CD1   . TYR B 1 322 ? 23.011 8.583   54.807  1.00 18.40 ? 313 TYR B CD1   1 
ATOM   5095 C CD2   . TYR B 1 322 ? 24.157 9.970   56.394  1.00 22.35 ? 313 TYR B CD2   1 
ATOM   5096 C CE1   . TYR B 1 322 ? 22.301 7.993   55.829  1.00 19.97 ? 313 TYR B CE1   1 
ATOM   5097 C CE2   . TYR B 1 322 ? 23.439 9.364   57.438  1.00 19.63 ? 313 TYR B CE2   1 
ATOM   5098 C CZ    . TYR B 1 322 ? 22.526 8.375   57.142  1.00 19.34 ? 313 TYR B CZ    1 
ATOM   5099 O OH    . TYR B 1 322 ? 21.811 7.749   58.145  1.00 18.59 ? 313 TYR B OH    1 
ATOM   5100 N N     . THR B 1 323 ? 25.190 13.417  53.297  1.00 22.84 ? 314 THR B N     1 
ATOM   5101 C CA    . THR B 1 323 ? 26.105 14.423  52.804  1.00 22.21 ? 314 THR B CA    1 
ATOM   5102 C C     . THR B 1 323 ? 27.444 14.156  53.453  1.00 24.72 ? 314 THR B C     1 
ATOM   5103 O O     . THR B 1 323 ? 27.585 13.251  54.301  1.00 21.35 ? 314 THR B O     1 
ATOM   5104 C CB    . THR B 1 323 ? 25.615 15.823  53.167  1.00 27.13 ? 314 THR B CB    1 
ATOM   5105 O OG1   . THR B 1 323 ? 25.542 15.896  54.602  1.00 22.93 ? 314 THR B OG1   1 
ATOM   5106 C CG2   . THR B 1 323 ? 24.234 16.101  52.596  1.00 27.24 ? 314 THR B CG2   1 
ATOM   5107 N N     . ARG B 1 324 ? 28.430 14.969  53.080  1.00 21.88 ? 315 ARG B N     1 
ATOM   5108 C CA    . ARG B 1 324 ? 29.706 14.904  53.770  1.00 21.05 ? 315 ARG B CA    1 
ATOM   5109 C C     . ARG B 1 324 ? 29.506 15.113  55.268  1.00 23.42 ? 315 ARG B C     1 
ATOM   5110 O O     . ARG B 1 324 ? 29.915 14.289  56.094  1.00 22.79 ? 315 ARG B O     1 
ATOM   5111 C CB    . ARG B 1 324 ? 30.651 15.966  53.221  1.00 21.71 ? 315 ARG B CB    1 
ATOM   5112 C CG    . ARG B 1 324 ? 31.919 16.123  54.083  1.00 24.47 ? 315 ARG B CG    1 
ATOM   5113 C CD    . ARG B 1 324 ? 32.974 17.001  53.392  1.00 24.28 ? 315 ARG B CD    1 
ATOM   5114 N NE    . ARG B 1 324 ? 34.287 16.915  54.026  1.00 27.25 ? 315 ARG B NE    1 
ATOM   5115 C CZ    . ARG B 1 324 ? 34.643 17.622  55.091  1.00 27.43 ? 315 ARG B CZ    1 
ATOM   5116 N NH1   . ARG B 1 324 ? 33.795 18.438  55.692  1.00 26.14 ? 315 ARG B NH1   1 
ATOM   5117 N NH2   . ARG B 1 324 ? 35.880 17.513  55.557  1.00 29.23 ? 315 ARG B NH2   1 
ATOM   5118 N N     . GLU B 1 325 ? 28.835 16.200  55.620  1.00 23.41 ? 316 GLU B N     1 
ATOM   5119 C CA    . GLU B 1 325 ? 28.661 16.571  57.020  1.00 23.94 ? 316 GLU B CA    1 
ATOM   5120 C C     . GLU B 1 325 ? 27.780 15.574  57.780  1.00 23.66 ? 316 GLU B C     1 
ATOM   5121 O O     . GLU B 1 325 ? 28.111 15.197  58.909  1.00 25.35 ? 316 GLU B O     1 
ATOM   5122 C CB    . GLU B 1 325 ? 28.160 18.014  57.043  1.00 25.87 ? 316 GLU B CB    1 
ATOM   5123 C CG    . GLU B 1 325 ? 26.863 18.219  56.266  1.00 33.98 ? 316 GLU B CG    1 
ATOM   5124 C CD    . GLU B 1 325 ? 27.066 18.761  54.803  1.00 41.05 ? 316 GLU B CD    1 
ATOM   5125 O OE1   . GLU B 1 325 ? 28.053 18.356  54.095  1.00 27.98 ? 316 GLU B OE1   1 
ATOM   5126 O OE2   . GLU B 1 325 ? 26.210 19.581  54.351  1.00 44.83 ? 316 GLU B OE2   1 
ATOM   5127 N N     . LEU B 1 326 ? 26.724 15.043  57.152  1.00 22.39 ? 317 LEU B N     1 
ATOM   5128 C CA    . LEU B 1 326 ? 25.900 14.045  57.839  1.00 20.39 ? 317 LEU B CA    1 
ATOM   5129 C C     . LEU B 1 326 ? 26.608 12.695  57.970  1.00 22.87 ? 317 LEU B C     1 
ATOM   5130 O O     . LEU B 1 326 ? 26.342 11.938  58.918  1.00 20.45 ? 317 LEU B O     1 
ATOM   5131 C CB    . LEU B 1 326 ? 24.578 13.863  57.102  1.00 22.46 ? 317 LEU B CB    1 
ATOM   5132 C CG    . LEU B 1 326 ? 23.547 14.972  57.203  1.00 20.18 ? 317 LEU B CG    1 
ATOM   5133 C CD1   . LEU B 1 326 ? 22.313 14.568  56.411  1.00 23.54 ? 317 LEU B CD1   1 
ATOM   5134 C CD2   . LEU B 1 326 ? 23.191 15.263  58.671  1.00 21.56 ? 317 LEU B CD2   1 
ATOM   5135 N N     . GLY B 1 327 ? 27.468 12.356  57.004  1.00 23.10 ? 318 GLY B N     1 
ATOM   5136 C CA    . GLY B 1 327 ? 28.276 11.152  57.120  1.00 20.74 ? 318 GLY B CA    1 
ATOM   5137 C C     . GLY B 1 327 ? 29.283 11.255  58.252  1.00 25.87 ? 318 GLY B C     1 
ATOM   5138 O O     . GLY B 1 327 ? 29.459 10.313  59.033  1.00 21.24 ? 318 GLY B O     1 
ATOM   5139 N N     . ILE B 1 328 ? 29.945 12.404  58.374  1.00 20.91 ? 319 ILE B N     1 
ATOM   5140 C CA    . ILE B 1 328 ? 30.855 12.600  59.503  1.00 21.85 ? 319 ILE B CA    1 
ATOM   5141 C C     . ILE B 1 328 ? 30.108 12.444  60.814  1.00 19.52 ? 319 ILE B C     1 
ATOM   5142 O O     . ILE B 1 328 ? 30.554 11.733  61.722  1.00 26.77 ? 319 ILE B O     1 
ATOM   5143 C CB    . ILE B 1 328 ? 31.536 13.971  59.402  1.00 23.77 ? 319 ILE B CB    1 
ATOM   5144 C CG1   . ILE B 1 328 ? 32.540 13.958  58.262  1.00 22.41 ? 319 ILE B CG1   1 
ATOM   5145 C CG2   . ILE B 1 328 ? 32.143 14.412  60.760  1.00 24.20 ? 319 ILE B CG2   1 
ATOM   5146 C CD1   . ILE B 1 328 ? 32.890 15.346  57.809  1.00 22.89 ? 319 ILE B CD1   1 
ATOM   5147 N N     . GLU B 1 329 ? 28.936 13.055  60.917  1.00 20.57 ? 320 GLU B N     1 
ATOM   5148 C CA    . GLU B 1 329 ? 28.250 13.041  62.201  1.00 25.36 ? 320 GLU B CA    1 
ATOM   5149 C C     . GLU B 1 329 ? 27.766 11.637  62.540  1.00 22.93 ? 320 GLU B C     1 
ATOM   5150 O O     . GLU B 1 329 ? 27.829 11.214  63.699  1.00 24.03 ? 320 GLU B O     1 
ATOM   5151 C CB    . GLU B 1 329 ? 27.096 14.045  62.193  1.00 28.68 ? 320 GLU B CB    1 
ATOM   5152 N N     . ALA B 1 330 ? 27.314 10.892  61.528  1.00 24.75 ? 321 ALA B N     1 
ATOM   5153 C CA    . ALA B 1 330 ? 26.886 9.516   61.758  1.00 21.75 ? 321 ALA B CA    1 
ATOM   5154 C C     . ALA B 1 330 ? 27.998 8.684   62.359  1.00 25.13 ? 321 ALA B C     1 
ATOM   5155 O O     . ALA B 1 330 ? 27.754 7.887   63.282  1.00 22.92 ? 321 ALA B O     1 
ATOM   5156 C CB    . ALA B 1 330 ? 26.412 8.882   60.444  1.00 23.30 ? 321 ALA B CB    1 
ATOM   5157 N N     . VAL B 1 331 ? 29.221 8.813   61.832  1.00 18.57 ? 322 VAL B N     1 
ATOM   5158 C CA    . VAL B 1 331 ? 30.303 7.982   62.352  1.00 20.01 ? 322 VAL B CA    1 
ATOM   5159 C C     . VAL B 1 331 ? 30.747 8.495   63.715  1.00 24.79 ? 322 VAL B C     1 
ATOM   5160 O O     . VAL B 1 331 ? 30.883 7.718   64.670  1.00 22.92 ? 322 VAL B O     1 
ATOM   5161 C CB    . VAL B 1 331 ? 31.469 7.916   61.351  1.00 23.13 ? 322 VAL B CB    1 
ATOM   5162 C CG1   . VAL B 1 331 ? 32.630 7.127   61.929  1.00 20.19 ? 322 VAL B CG1   1 
ATOM   5163 C CG2   . VAL B 1 331 ? 30.995 7.253   60.040  1.00 20.55 ? 322 VAL B CG2   1 
ATOM   5164 N N     . ALA B 1 332 ? 30.916 9.818   63.839  1.00 20.86 ? 323 ALA B N     1 
ATOM   5165 C CA    . ALA B 1 332 ? 31.416 10.375  65.094  1.00 25.68 ? 323 ALA B CA    1 
ATOM   5166 C C     . ALA B 1 332 ? 30.465 10.108  66.245  1.00 23.81 ? 323 ALA B C     1 
ATOM   5167 O O     . ALA B 1 332 ? 30.894 10.051  67.405  1.00 28.34 ? 323 ALA B O     1 
ATOM   5168 C CB    . ALA B 1 332 ? 31.649 11.881  64.946  1.00 27.67 ? 323 ALA B CB    1 
ATOM   5169 N N     . GLN B 1 333 ? 29.169 10.009  65.959  1.00 21.28 ? 324 GLN B N     1 
ATOM   5170 C CA    . GLN B 1 333 ? 28.121 9.853   66.959  1.00 28.27 ? 324 GLN B CA    1 
ATOM   5171 C C     . GLN B 1 333 ? 27.896 8.388   67.308  1.00 29.14 ? 324 GLN B C     1 
ATOM   5172 O O     . GLN B 1 333 ? 27.041 8.084   68.145  1.00 26.69 ? 324 GLN B O     1 
ATOM   5173 C CB    . GLN B 1 333 ? 26.830 10.440  66.404  1.00 31.79 ? 324 GLN B CB    1 
ATOM   5174 C CG    . GLN B 1 333 ? 25.917 11.131  67.310  1.00 43.09 ? 324 GLN B CG    1 
ATOM   5175 C CD    . GLN B 1 333 ? 25.442 12.436  66.675  1.00 46.63 ? 324 GLN B CD    1 
ATOM   5176 O OE1   . GLN B 1 333 ? 26.247 13.220  66.164  1.00 46.99 ? 324 GLN B OE1   1 
ATOM   5177 N NE2   . GLN B 1 333 ? 24.126 12.661  66.684  1.00 54.06 ? 324 GLN B NE2   1 
ATOM   5178 N N     . GLY B 1 334 ? 28.638 7.486   66.662  1.00 22.92 ? 325 GLY B N     1 
ATOM   5179 C CA    . GLY B 1 334 ? 28.414 6.057   66.755  1.00 26.59 ? 325 GLY B CA    1 
ATOM   5180 C C     . GLY B 1 334 ? 27.140 5.555   66.117  1.00 26.96 ? 325 GLY B C     1 
ATOM   5181 O O     . GLY B 1 334 ? 26.727 4.429   66.403  1.00 24.99 ? 325 GLY B O     1 
ATOM   5182 N N     . ASP B 1 335 ? 26.503 6.359   65.258  1.00 23.03 ? 326 ASP B N     1 
ATOM   5183 C CA    . ASP B 1 335 ? 25.234 5.983   64.629  1.00 23.05 ? 326 ASP B CA    1 
ATOM   5184 C C     . ASP B 1 335 ? 25.414 4.943   63.520  1.00 21.88 ? 326 ASP B C     1 
ATOM   5185 O O     . ASP B 1 335 ? 24.441 4.274   63.150  1.00 21.50 ? 326 ASP B O     1 
ATOM   5186 C CB    . ASP B 1 335 ? 24.549 7.210   64.023  1.00 25.56 ? 326 ASP B CB    1 
ATOM   5187 C CG    . ASP B 1 335 ? 24.106 8.224   65.049  1.00 31.92 ? 326 ASP B CG    1 
ATOM   5188 O OD1   . ASP B 1 335 ? 23.876 7.862   66.216  1.00 34.76 ? 326 ASP B OD1   1 
ATOM   5189 O OD2   . ASP B 1 335 ? 23.982 9.410   64.671  1.00 35.24 ? 326 ASP B OD2   1 
ATOM   5190 N N     . ALA B 1 336 ? 26.612 4.838   62.945  1.00 20.71 ? 327 ALA B N     1 
ATOM   5191 C CA    . ALA B 1 336 ? 26.879 3.929   61.831  1.00 18.14 ? 327 ALA B CA    1 
ATOM   5192 C C     . ALA B 1 336 ? 28.370 3.683   61.823  1.00 18.04 ? 327 ALA B C     1 
ATOM   5193 O O     . ALA B 1 336 ? 29.143 4.514   62.306  1.00 20.06 ? 327 ALA B O     1 
ATOM   5194 C CB    . ALA B 1 336 ? 26.458 4.518   60.479  1.00 17.60 ? 327 ALA B CB    1 
ATOM   5195 N N     . ASP B 1 337 ? 28.776 2.566   61.232  1.00 14.21 ? 328 ASP B N     1 
ATOM   5196 C CA    . ASP B 1 337 ? 30.200 2.341   61.043  1.00 15.73 ? 328 ASP B CA    1 
ATOM   5197 C C     . ASP B 1 337 ? 30.676 2.791   59.672  1.00 19.01 ? 328 ASP B C     1 
ATOM   5198 O O     . ASP B 1 337 ? 31.802 3.294   59.544  1.00 19.15 ? 328 ASP B O     1 
ATOM   5199 C CB    . ASP B 1 337 ? 30.522 0.866   61.258  1.00 18.15 ? 328 ASP B CB    1 
ATOM   5200 C CG    . ASP B 1 337 ? 29.997 0.384   62.617  1.00 19.13 ? 328 ASP B CG    1 
ATOM   5201 O OD1   . ASP B 1 337 ? 30.488 0.894   63.650  1.00 19.07 ? 328 ASP B OD1   1 
ATOM   5202 O OD2   . ASP B 1 337 ? 29.060 -0.428  62.628  1.00 19.57 ? 328 ASP B OD2   1 
ATOM   5203 N N     . LEU B 1 338 ? 29.853 2.596   58.646  1.00 17.85 ? 329 LEU B N     1 
ATOM   5204 C CA    . LEU B 1 338 ? 30.196 3.014   57.289  1.00 17.16 ? 329 LEU B CA    1 
ATOM   5205 C C     . LEU B 1 338 ? 29.036 3.805   56.708  1.00 17.54 ? 329 LEU B C     1 
ATOM   5206 O O     . LEU B 1 338 ? 27.885 3.601   57.085  1.00 15.54 ? 329 LEU B O     1 
ATOM   5207 C CB    . LEU B 1 338 ? 30.502 1.780   56.398  1.00 15.18 ? 329 LEU B CB    1 
ATOM   5208 C CG    . LEU B 1 338 ? 31.599 0.822   56.916  1.00 20.13 ? 329 LEU B CG    1 
ATOM   5209 C CD1   . LEU B 1 338 ? 31.540 -0.517  56.204  1.00 22.02 ? 329 LEU B CD1   1 
ATOM   5210 C CD2   . LEU B 1 338 ? 32.983 1.419   56.720  1.00 18.27 ? 329 LEU B CD2   1 
ATOM   5211 N N     . VAL B 1 339 ? 29.330 4.726   55.778  1.00 14.22 ? 330 VAL B N     1 
ATOM   5212 C CA    . VAL B 1 339 ? 28.286 5.518   55.136  1.00 17.10 ? 330 VAL B CA    1 
ATOM   5213 C C     . VAL B 1 339 ? 28.364 5.283   53.631  1.00 15.15 ? 330 VAL B C     1 
ATOM   5214 O O     . VAL B 1 339 ? 29.425 5.480   53.037  1.00 17.06 ? 330 VAL B O     1 
ATOM   5215 C CB    . VAL B 1 339 ? 28.460 7.018   55.445  1.00 18.00 ? 330 VAL B CB    1 
ATOM   5216 C CG1   . VAL B 1 339 ? 27.316 7.791   54.850  1.00 19.51 ? 330 VAL B CG1   1 
ATOM   5217 C CG2   . VAL B 1 339 ? 28.571 7.235   56.935  1.00 19.31 ? 330 VAL B CG2   1 
ATOM   5218 N N     . SER B 1 340 ? 27.261 4.868   53.008  1.00 12.82 ? 331 SER B N     1 
ATOM   5219 C CA    . SER B 1 340 ? 27.311 4.642   51.558  1.00 14.38 ? 331 SER B CA    1 
ATOM   5220 C C     . SER B 1 340 ? 26.712 5.828   50.814  1.00 17.36 ? 331 SER B C     1 
ATOM   5221 O O     . SER B 1 340 ? 25.744 6.454   51.277  1.00 15.84 ? 331 SER B O     1 
ATOM   5222 C CB    . SER B 1 340 ? 26.627 3.343   51.139  1.00 16.62 ? 331 SER B CB    1 
ATOM   5223 O OG    . SER B 1 340 ? 25.221 3.383   51.322  1.00 14.15 ? 331 SER B OG    1 
ATOM   5224 N N     . TYR B 1 341 ? 27.332 6.165   49.687  1.00 15.00 ? 332 TYR B N     1 
ATOM   5225 C CA    . TYR B 1 341 ? 26.883 7.264   48.846  1.00 13.22 ? 332 TYR B CA    1 
ATOM   5226 C C     . TYR B 1 341 ? 26.551 6.736   47.460  1.00 16.05 ? 332 TYR B C     1 
ATOM   5227 O O     . TYR B 1 341 ? 27.319 5.956   46.884  1.00 14.58 ? 332 TYR B O     1 
ATOM   5228 C CB    . TYR B 1 341 ? 27.946 8.346   48.743  1.00 15.23 ? 332 TYR B CB    1 
ATOM   5229 C CG    . TYR B 1 341 ? 28.241 9.040   50.060  1.00 15.75 ? 332 TYR B CG    1 
ATOM   5230 C CD1   . TYR B 1 341 ? 29.124 8.483   50.961  1.00 18.45 ? 332 TYR B CD1   1 
ATOM   5231 C CD2   . TYR B 1 341 ? 27.623 10.257  50.392  1.00 18.73 ? 332 TYR B CD2   1 
ATOM   5232 C CE1   . TYR B 1 341 ? 29.415 9.129   52.195  1.00 18.90 ? 332 TYR B CE1   1 
ATOM   5233 C CE2   . TYR B 1 341 ? 27.899 10.910  51.585  1.00 17.46 ? 332 TYR B CE2   1 
ATOM   5234 C CZ    . TYR B 1 341 ? 28.780 10.331  52.491  1.00 18.32 ? 332 TYR B CZ    1 
ATOM   5235 O OH    . TYR B 1 341 ? 29.031 10.955  53.688  1.00 19.35 ? 332 TYR B OH    1 
ATOM   5236 N N     . GLY B 1 342 ? 25.403 7.137   46.947  1.00 14.66 ? 333 GLY B N     1 
ATOM   5237 C CA    . GLY B 1 342 ? 24.979 6.680   45.642  1.00 15.87 ? 333 GLY B CA    1 
ATOM   5238 C C     . GLY B 1 342 ? 25.139 7.783   44.613  1.00 14.91 ? 333 GLY B C     1 
ATOM   5239 O O     . GLY B 1 342 ? 26.145 7.831   43.890  1.00 16.18 ? 333 GLY B O     1 
ATOM   5240 N N     . ARG B 1 343 ? 24.173 8.693   44.559  1.00 13.26 ? 334 ARG B N     1 
ATOM   5241 C CA    . ARG B 1 343 ? 24.126 9.645   43.435  1.00 16.53 ? 334 ARG B CA    1 
ATOM   5242 C C     . ARG B 1 343 ? 25.377 10.497  43.342  1.00 16.53 ? 334 ARG B C     1 
ATOM   5243 O O     . ARG B 1 343 ? 25.855 10.789  42.241  1.00 19.21 ? 334 ARG B O     1 
ATOM   5244 C CB    . ARG B 1 343 ? 22.884 10.523  43.550  1.00 15.01 ? 334 ARG B CB    1 
ATOM   5245 C CG    . ARG B 1 343 ? 21.633 9.748   43.169  1.00 16.25 ? 334 ARG B CG    1 
ATOM   5246 C CD    . ARG B 1 343 ? 20.374 10.466  43.612  1.00 22.12 ? 334 ARG B CD    1 
ATOM   5247 N NE    . ARG B 1 343 ? 20.172 10.347  45.041  1.00 18.22 ? 334 ARG B NE    1 
ATOM   5248 C CZ    . ARG B 1 343 ? 19.048 10.683  45.656  1.00 22.42 ? 334 ARG B CZ    1 
ATOM   5249 N NH1   . ARG B 1 343 ? 18.033 11.211  44.986  1.00 21.50 ? 334 ARG B NH1   1 
ATOM   5250 N NH2   . ARG B 1 343 ? 18.910 10.419  46.960  1.00 20.35 ? 334 ARG B NH2   1 
ATOM   5251 N N     . LEU B 1 344 ? 25.915 10.940  44.480  1.00 16.12 ? 335 LEU B N     1 
ATOM   5252 C CA    . LEU B 1 344 ? 27.119 11.769  44.434  1.00 16.18 ? 335 LEU B CA    1 
ATOM   5253 C C     . LEU B 1 344 ? 28.299 11.006  43.871  1.00 20.45 ? 335 LEU B C     1 
ATOM   5254 O O     . LEU B 1 344 ? 29.192 11.618  43.289  1.00 15.95 ? 335 LEU B O     1 
ATOM   5255 C CB    . LEU B 1 344 ? 27.476 12.287  45.823  1.00 19.86 ? 335 LEU B CB    1 
ATOM   5256 C CG    . LEU B 1 344 ? 26.581 13.459  46.206  1.00 21.87 ? 335 LEU B CG    1 
ATOM   5257 C CD1   . LEU B 1 344 ? 26.847 13.875  47.670  1.00 18.18 ? 335 LEU B CD1   1 
ATOM   5258 C CD2   . LEU B 1 344 ? 26.848 14.590  45.247  1.00 20.13 ? 335 LEU B CD2   1 
ATOM   5259 N N     . PHE B 1 345 ? 28.328 9.679   44.052  1.00 16.07 ? 336 PHE B N     1 
ATOM   5260 C CA    . PHE B 1 345 ? 29.381 8.838   43.480  1.00 18.45 ? 336 PHE B CA    1 
ATOM   5261 C C     . PHE B 1 345 ? 29.223 8.681   41.979  1.00 17.96 ? 336 PHE B C     1 
ATOM   5262 O O     . PHE B 1 345 ? 30.214 8.421   41.286  1.00 20.06 ? 336 PHE B O     1 
ATOM   5263 C CB    . PHE B 1 345 ? 29.376 7.445   44.160  1.00 16.53 ? 336 PHE B CB    1 
ATOM   5264 C CG    . PHE B 1 345 ? 30.669 7.097   44.850  1.00 14.71 ? 336 PHE B CG    1 
ATOM   5265 C CD1   . PHE B 1 345 ? 31.872 7.284   44.209  1.00 16.78 ? 336 PHE B CD1   1 
ATOM   5266 C CD2   . PHE B 1 345 ? 30.678 6.566   46.145  1.00 14.69 ? 336 PHE B CD2   1 
ATOM   5267 C CE1   . PHE B 1 345 ? 33.078 6.994   44.851  1.00 16.96 ? 336 PHE B CE1   1 
ATOM   5268 C CE2   . PHE B 1 345 ? 31.853 6.235   46.755  1.00 16.92 ? 336 PHE B CE2   1 
ATOM   5269 C CZ    . PHE B 1 345 ? 33.064 6.429   46.107  1.00 18.89 ? 336 PHE B CZ    1 
ATOM   5270 N N     . ILE B 1 346 ? 27.998 8.826   41.455  1.00 16.19 ? 337 ILE B N     1 
ATOM   5271 C CA    . ILE B 1 346 ? 27.801 8.814   39.999  1.00 16.33 ? 337 ILE B CA    1 
ATOM   5272 C C     . ILE B 1 346 ? 28.645 9.903   39.335  1.00 19.85 ? 337 ILE B C     1 
ATOM   5273 O O     . ILE B 1 346 ? 29.376 9.642   38.376  1.00 16.80 ? 337 ILE B O     1 
ATOM   5274 C CB    . ILE B 1 346 ? 26.309 8.973   39.634  1.00 16.90 ? 337 ILE B CB    1 
ATOM   5275 C CG1   . ILE B 1 346 ? 25.572 7.676   39.937  1.00 18.79 ? 337 ILE B CG1   1 
ATOM   5276 C CG2   . ILE B 1 346 ? 26.144 9.200   38.100  1.00 18.16 ? 337 ILE B CG2   1 
ATOM   5277 C CD1   . ILE B 1 346 ? 24.117 7.693   39.574  1.00 18.30 ? 337 ILE B CD1   1 
ATOM   5278 N N     . SER B 1 347 ? 28.569 11.136  39.847  1.00 18.60 ? 338 SER B N     1 
ATOM   5279 C CA    . SER B 1 347 ? 29.153 12.294  39.184  1.00 19.91 ? 338 SER B CA    1 
ATOM   5280 C C     . SER B 1 347 ? 30.519 12.697  39.737  1.00 20.74 ? 338 SER B C     1 
ATOM   5281 O O     . SER B 1 347 ? 31.173 13.577  39.159  1.00 18.08 ? 338 SER B O     1 
ATOM   5282 C CB    . SER B 1 347 ? 28.180 13.472  39.276  1.00 14.96 ? 338 SER B CB    1 
ATOM   5283 O OG    . SER B 1 347 ? 27.801 13.685  40.611  1.00 15.33 ? 338 SER B OG    1 
ATOM   5284 N N     . ASN B 1 348 ? 30.971 12.068  40.824  1.00 18.54 ? 339 ASN B N     1 
ATOM   5285 C CA    . ASN B 1 348 ? 32.236 12.394  41.482  1.00 19.52 ? 339 ASN B CA    1 
ATOM   5286 C C     . ASN B 1 348 ? 33.015 11.098  41.586  1.00 19.64 ? 339 ASN B C     1 
ATOM   5287 O O     . ASN B 1 348 ? 32.895 10.373  42.588  1.00 18.48 ? 339 ASN B O     1 
ATOM   5288 C CB    . ASN B 1 348 ? 31.998 13.030  42.856  1.00 15.67 ? 339 ASN B CB    1 
ATOM   5289 C CG    . ASN B 1 348 ? 31.280 14.373  42.732  1.00 19.89 ? 339 ASN B CG    1 
ATOM   5290 O OD1   . ASN B 1 348 ? 31.931 15.386  42.496  1.00 21.57 ? 339 ASN B OD1   1 
ATOM   5291 N ND2   . ASN B 1 348 ? 29.951 14.379  42.853  1.00 19.35 ? 339 ASN B ND2   1 
ATOM   5292 N N     . PRO B 1 349 ? 33.761 10.724  40.533  1.00 18.39 ? 340 PRO B N     1 
ATOM   5293 C CA    . PRO B 1 349 ? 34.481 9.448   40.603  1.00 20.07 ? 340 PRO B CA    1 
ATOM   5294 C C     . PRO B 1 349 ? 35.437 9.420   41.769  1.00 18.62 ? 340 PRO B C     1 
ATOM   5295 O O     . PRO B 1 349 ? 35.606 8.366   42.402  1.00 20.29 ? 340 PRO B O     1 
ATOM   5296 C CB    . PRO B 1 349 ? 35.214 9.380   39.247  1.00 21.09 ? 340 PRO B CB    1 
ATOM   5297 C CG    . PRO B 1 349 ? 35.251 10.788  38.744  1.00 21.34 ? 340 PRO B CG    1 
ATOM   5298 C CD    . PRO B 1 349 ? 33.976 11.407  39.236  1.00 21.71 ? 340 PRO B CD    1 
ATOM   5299 N N     . ASP B 1 350 ? 36.047 10.570  42.086  1.00 19.52 ? 341 ASP B N     1 
ATOM   5300 C CA    . ASP B 1 350 ? 36.901 10.725  43.268  1.00 17.45 ? 341 ASP B CA    1 
ATOM   5301 C C     . ASP B 1 350 ? 36.138 11.255  44.482  1.00 22.89 ? 341 ASP B C     1 
ATOM   5302 O O     . ASP B 1 350 ? 36.662 12.092  45.229  1.00 20.16 ? 341 ASP B O     1 
ATOM   5303 C CB    . ASP B 1 350 ? 38.108 11.628  42.980  1.00 22.05 ? 341 ASP B CB    1 
ATOM   5304 C CG    . ASP B 1 350 ? 37.751 12.927  42.193  1.00 23.55 ? 341 ASP B CG    1 
ATOM   5305 O OD1   . ASP B 1 350 ? 36.559 13.228  41.952  1.00 22.39 ? 341 ASP B OD1   1 
ATOM   5306 O OD2   . ASP B 1 350 ? 38.689 13.647  41.799  1.00 24.87 ? 341 ASP B OD2   1 
ATOM   5307 N N     . LEU B 1 351 ? 34.923 10.760  44.727  1.00 18.14 ? 342 LEU B N     1 
ATOM   5308 C CA    . LEU B 1 351 ? 34.139 11.263  45.854  1.00 18.97 ? 342 LEU B CA    1 
ATOM   5309 C C     . LEU B 1 351 ? 34.892 11.126  47.167  1.00 19.61 ? 342 LEU B C     1 
ATOM   5310 O O     . LEU B 1 351 ? 34.837 12.031  48.007  1.00 19.70 ? 342 LEU B O     1 
ATOM   5311 C CB    . LEU B 1 351 ? 32.799 10.537  45.947  1.00 21.65 ? 342 LEU B CB    1 
ATOM   5312 C CG    . LEU B 1 351 ? 31.843 11.115  47.001  1.00 18.93 ? 342 LEU B CG    1 
ATOM   5313 C CD1   . LEU B 1 351 ? 31.444 12.592  46.697  1.00 21.67 ? 342 LEU B CD1   1 
ATOM   5314 C CD2   . LEU B 1 351 ? 30.589 10.218  47.169  1.00 17.65 ? 342 LEU B CD2   1 
ATOM   5315 N N     . VAL B 1 352 ? 35.625 10.021  47.350  1.00 19.75 ? 343 VAL B N     1 
ATOM   5316 C CA    . VAL B 1 352 ? 36.381 9.851   48.595  1.00 19.69 ? 343 VAL B CA    1 
ATOM   5317 C C     . VAL B 1 352 ? 37.345 11.019  48.797  1.00 22.22 ? 343 VAL B C     1 
ATOM   5318 O O     . VAL B 1 352 ? 37.389 11.627  49.872  1.00 22.08 ? 343 VAL B O     1 
ATOM   5319 C CB    . VAL B 1 352 ? 37.133 8.507   48.610  1.00 20.24 ? 343 VAL B CB    1 
ATOM   5320 C CG1   . VAL B 1 352 ? 37.827 8.335   49.935  1.00 23.37 ? 343 VAL B CG1   1 
ATOM   5321 C CG2   . VAL B 1 352 ? 36.175 7.304   48.336  1.00 18.55 ? 343 VAL B CG2   1 
ATOM   5322 N N     . MET B 1 353 ? 38.144 11.334  47.768  1.00 21.94 ? 344 MET B N     1 
ATOM   5323 C CA    . MET B 1 353 ? 39.108 12.435  47.866  1.00 21.10 ? 344 MET B CA    1 
ATOM   5324 C C     . MET B 1 353 ? 38.419 13.774  48.071  1.00 23.51 ? 344 MET B C     1 
ATOM   5325 O O     . MET B 1 353 ? 38.893 14.608  48.859  1.00 26.13 ? 344 MET B O     1 
ATOM   5326 C CB    . MET B 1 353 ? 39.991 12.482  46.614  1.00 25.88 ? 344 MET B CB    1 
ATOM   5327 C CG    . MET B 1 353 ? 41.175 13.468  46.699  1.00 30.20 ? 344 MET B CG    1 
ATOM   5328 S SD    . MET B 1 353 ? 42.379 13.063  47.991  1.00 45.66 ? 344 MET B SD    1 
ATOM   5329 C CE    . MET B 1 353 ? 42.571 11.277  47.758  1.00 39.77 ? 344 MET B CE    1 
ATOM   5330 N N     . ARG B 1 354 ? 37.300 13.998  47.377  1.00 18.94 ? 345 ARG B N     1 
ATOM   5331 C CA    . ARG B 1 354 ? 36.575 15.251  47.554  1.00 20.83 ? 345 ARG B CA    1 
ATOM   5332 C C     . ARG B 1 354 ? 36.069 15.377  48.980  1.00 25.09 ? 345 ARG B C     1 
ATOM   5333 O O     . ARG B 1 354 ? 36.127 16.459  49.572  1.00 23.62 ? 345 ARG B O     1 
ATOM   5334 C CB    . ARG B 1 354 ? 35.430 15.354  46.543  1.00 22.31 ? 345 ARG B CB    1 
ATOM   5335 C CG    . ARG B 1 354 ? 35.918 15.256  45.110  1.00 23.70 ? 345 ARG B CG    1 
ATOM   5336 C CD    . ARG B 1 354 ? 34.863 15.761  44.125  1.00 25.86 ? 345 ARG B CD    1 
ATOM   5337 N NE    . ARG B 1 354 ? 35.245 15.509  42.745  1.00 24.27 ? 345 ARG B NE    1 
ATOM   5338 C CZ    . ARG B 1 354 ? 35.019 16.349  41.745  1.00 27.33 ? 345 ARG B CZ    1 
ATOM   5339 N NH1   . ARG B 1 354 ? 34.441 17.532  41.945  1.00 20.93 ? 345 ARG B NH1   1 
ATOM   5340 N NH2   . ARG B 1 354 ? 35.340 15.982  40.514  1.00 28.50 ? 345 ARG B NH2   1 
ATOM   5341 N N     . ILE B 1 355 ? 35.608 14.269  49.564  1.00 24.68 ? 346 ILE B N     1 
ATOM   5342 C CA    . ILE B 1 355 ? 35.148 14.296  50.945  1.00 23.01 ? 346 ILE B CA    1 
ATOM   5343 C C     . ILE B 1 355 ? 36.316 14.544  51.887  1.00 26.17 ? 346 ILE B C     1 
ATOM   5344 O O     . ILE B 1 355 ? 36.212 15.338  52.838  1.00 26.51 ? 346 ILE B O     1 
ATOM   5345 C CB    . ILE B 1 355 ? 34.390 12.995  51.268  1.00 20.47 ? 346 ILE B CB    1 
ATOM   5346 C CG1   . ILE B 1 355 ? 33.036 13.011  50.523  1.00 17.99 ? 346 ILE B CG1   1 
ATOM   5347 C CG2   . ILE B 1 355 ? 34.198 12.840  52.785  1.00 21.73 ? 346 ILE B CG2   1 
ATOM   5348 C CD1   . ILE B 1 355 ? 32.096 11.798  50.774  1.00 17.42 ? 346 ILE B CD1   1 
ATOM   5349 N N     . LYS B 1 356 ? 37.460 13.907  51.620  1.00 21.87 ? 347 LYS B N     1 
ATOM   5350 C CA    . LYS B 1 356 ? 38.661 14.147  52.426  1.00 24.87 ? 347 LYS B CA    1 
ATOM   5351 C C     . LYS B 1 356 ? 39.072 15.625  52.411  1.00 28.73 ? 347 LYS B C     1 
ATOM   5352 O O     . LYS B 1 356 ? 39.394 16.205  53.456  1.00 29.59 ? 347 LYS B O     1 
ATOM   5353 C CB    . LYS B 1 356 ? 39.794 13.258  51.909  1.00 28.22 ? 347 LYS B CB    1 
ATOM   5354 C CG    . LYS B 1 356 ? 41.147 13.366  52.592  1.00 27.10 ? 347 LYS B CG    1 
ATOM   5355 C CD    . LYS B 1 356 ? 41.179 12.574  53.858  1.00 35.09 ? 347 LYS B CD    1 
ATOM   5356 C CE    . LYS B 1 356 ? 42.594 12.542  54.441  1.00 43.95 ? 347 LYS B CE    1 
ATOM   5357 N NZ    . LYS B 1 356 ? 42.608 12.392  55.935  1.00 45.12 ? 347 LYS B NZ    1 
ATOM   5358 N N     . LEU B 1 357 ? 39.079 16.254  51.244  1.00 24.05 ? 348 LEU B N     1 
ATOM   5359 C CA    . LEU B 1 357 ? 39.512 17.648  51.166  1.00 30.54 ? 348 LEU B CA    1 
ATOM   5360 C C     . LEU B 1 357 ? 38.392 18.662  51.333  1.00 28.92 ? 348 LEU B C     1 
ATOM   5361 O O     . LEU B 1 357 ? 38.667 19.864  51.309  1.00 27.87 ? 348 LEU B O     1 
ATOM   5362 C CB    . LEU B 1 357 ? 40.259 17.926  49.857  1.00 30.95 ? 348 LEU B CB    1 
ATOM   5363 C CG    . LEU B 1 357 ? 41.100 16.817  49.247  1.00 33.22 ? 348 LEU B CG    1 
ATOM   5364 C CD1   . LEU B 1 357 ? 41.442 17.110  47.813  1.00 30.21 ? 348 LEU B CD1   1 
ATOM   5365 C CD2   . LEU B 1 357 ? 42.377 16.693  50.075  1.00 37.17 ? 348 LEU B CD2   1 
ATOM   5366 N N     . ASN B 1 358 ? 37.160 18.217  51.547  1.00 26.11 ? 349 ASN B N     1 
ATOM   5367 C CA    . ASN B 1 358 ? 35.983 19.078  51.486  1.00 27.74 ? 349 ASN B CA    1 
ATOM   5368 C C     . ASN B 1 358 ? 35.976 19.909  50.204  1.00 28.13 ? 349 ASN B C     1 
ATOM   5369 O O     . ASN B 1 358 ? 35.743 21.124  50.215  1.00 25.18 ? 349 ASN B O     1 
ATOM   5370 C CB    . ASN B 1 358 ? 35.869 19.977  52.717  1.00 25.07 ? 349 ASN B CB    1 
ATOM   5371 C CG    . ASN B 1 358 ? 34.488 20.512  52.873  1.00 26.51 ? 349 ASN B CG    1 
ATOM   5372 O OD1   . ASN B 1 358 ? 33.581 20.051  52.197  1.00 31.22 ? 349 ASN B OD1   1 
ATOM   5373 N ND2   . ASN B 1 358 ? 34.305 21.495  53.741  1.00 33.21 ? 349 ASN B ND2   1 
ATOM   5374 N N     . ALA B 1 359 ? 36.236 19.236  49.095  1.00 24.47 ? 350 ALA B N     1 
ATOM   5375 C CA    . ALA B 1 359 ? 36.219 19.870  47.791  1.00 24.36 ? 350 ALA B CA    1 
ATOM   5376 C C     . ALA B 1 359 ? 34.802 19.897  47.240  1.00 24.78 ? 350 ALA B C     1 
ATOM   5377 O O     . ALA B 1 359 ? 33.994 19.019  47.536  1.00 24.24 ? 350 ALA B O     1 
ATOM   5378 C CB    . ALA B 1 359 ? 37.128 19.129  46.803  1.00 26.90 ? 350 ALA B CB    1 
ATOM   5379 N N     . PRO B 1 360 ? 34.478 20.879  46.416  1.00 20.90 ? 351 PRO B N     1 
ATOM   5380 C CA    . PRO B 1 360 ? 33.119 20.946  45.874  1.00 21.62 ? 351 PRO B CA    1 
ATOM   5381 C C     . PRO B 1 360 ? 32.835 19.757  44.973  1.00 20.80 ? 351 PRO B C     1 
ATOM   5382 O O     . PRO B 1 360 ? 33.722 19.257  44.279  1.00 22.08 ? 351 PRO B O     1 
ATOM   5383 C CB    . PRO B 1 360 ? 33.103 22.261  45.086  1.00 23.27 ? 351 PRO B CB    1 
ATOM   5384 C CG    . PRO B 1 360 ? 34.533 22.706  44.997  1.00 31.77 ? 351 PRO B CG    1 
ATOM   5385 C CD    . PRO B 1 360 ? 35.279 22.081  46.113  1.00 29.73 ? 351 PRO B CD    1 
ATOM   5386 N N     . LEU B 1 361 ? 31.570 19.340  44.965  1.00 21.03 ? 352 LEU B N     1 
ATOM   5387 C CA    . LEU B 1 361 ? 31.087 18.165  44.240  1.00 21.06 ? 352 LEU B CA    1 
ATOM   5388 C C     . LEU B 1 361 ? 30.470 18.546  42.906  1.00 20.39 ? 352 LEU B C     1 
ATOM   5389 O O     . LEU B 1 361 ? 29.885 19.629  42.771  1.00 22.68 ? 352 LEU B O     1 
ATOM   5390 C CB    . LEU B 1 361 ? 30.029 17.431  45.076  1.00 19.75 ? 352 LEU B CB    1 
ATOM   5391 C CG    . LEU B 1 361 ? 30.490 17.176  46.515  1.00 21.86 ? 352 LEU B CG    1 
ATOM   5392 C CD1   . LEU B 1 361 ? 29.452 16.354  47.271  1.00 24.90 ? 352 LEU B CD1   1 
ATOM   5393 C CD2   . LEU B 1 361 ? 31.823 16.454  46.509  1.00 24.32 ? 352 LEU B CD2   1 
ATOM   5394 N N     . ASN B 1 362 ? 30.580 17.635  41.927  1.00 18.71 ? 353 ASN B N     1 
ATOM   5395 C CA    . ASN B 1 362 ? 29.968 17.816  40.600  1.00 21.80 ? 353 ASN B CA    1 
ATOM   5396 C C     . ASN B 1 362 ? 28.526 17.342  40.599  1.00 20.82 ? 353 ASN B C     1 
ATOM   5397 O O     . ASN B 1 362 ? 28.197 16.311  41.211  1.00 20.99 ? 353 ASN B O     1 
ATOM   5398 C CB    . ASN B 1 362 ? 30.689 17.025  39.497  1.00 24.78 ? 353 ASN B CB    1 
ATOM   5399 C CG    . ASN B 1 362 ? 32.132 17.403  39.316  1.00 28.84 ? 353 ASN B CG    1 
ATOM   5400 O OD1   . ASN B 1 362 ? 32.566 18.524  39.607  1.00 28.17 ? 353 ASN B OD1   1 
ATOM   5401 N ND2   . ASN B 1 362 ? 32.908 16.439  38.810  1.00 35.81 ? 353 ASN B ND2   1 
ATOM   5402 N N     . LYS B 1 363 ? 27.679 18.055  39.851  1.00 19.65 ? 354 LYS B N     1 
ATOM   5403 C CA    . LYS B 1 363 ? 26.295 17.646  39.664  1.00 20.76 ? 354 LYS B CA    1 
ATOM   5404 C C     . LYS B 1 363 ? 26.197 16.373  38.807  1.00 19.69 ? 354 LYS B C     1 
ATOM   5405 O O     . LYS B 1 363 ? 27.062 16.080  37.976  1.00 18.98 ? 354 LYS B O     1 
ATOM   5406 C CB    . LYS B 1 363 ? 25.487 18.774  39.016  1.00 25.09 ? 354 LYS B CB    1 
ATOM   5407 C CG    . LYS B 1 363 ? 25.990 19.216  37.638  1.00 22.31 ? 354 LYS B CG    1 
ATOM   5408 C CD    . LYS B 1 363 ? 24.833 19.657  36.706  1.00 33.13 ? 354 LYS B CD    1 
ATOM   5409 C CE    . LYS B 1 363 ? 24.004 20.856  37.229  1.00 38.04 ? 354 LYS B CE    1 
ATOM   5410 N NZ    . LYS B 1 363 ? 24.735 22.135  37.672  1.00 30.81 ? 354 LYS B NZ    1 
ATOM   5411 N N     . TYR B 1 364 ? 25.128 15.602  39.019  1.00 21.42 ? 355 TYR B N     1 
ATOM   5412 C CA    . TYR B 1 364 ? 24.886 14.440  38.175  1.00 21.25 ? 355 TYR B CA    1 
ATOM   5413 C C     . TYR B 1 364 ? 23.719 14.697  37.239  1.00 22.69 ? 355 TYR B C     1 
ATOM   5414 O O     . TYR B 1 364 ? 22.886 15.570  37.472  1.00 22.15 ? 355 TYR B O     1 
ATOM   5415 C CB    . TYR B 1 364 ? 24.594 13.178  39.001  1.00 18.48 ? 355 TYR B CB    1 
ATOM   5416 C CG    . TYR B 1 364 ? 23.618 13.419  40.097  1.00 18.09 ? 355 TYR B CG    1 
ATOM   5417 C CD1   . TYR B 1 364 ? 22.258 13.393  39.857  1.00 20.86 ? 355 TYR B CD1   1 
ATOM   5418 C CD2   . TYR B 1 364 ? 24.044 13.682  41.393  1.00 21.26 ? 355 TYR B CD2   1 
ATOM   5419 C CE1   . TYR B 1 364 ? 21.345 13.626  40.881  1.00 22.75 ? 355 TYR B CE1   1 
ATOM   5420 C CE2   . TYR B 1 364 ? 23.143 13.911  42.395  1.00 23.69 ? 355 TYR B CE2   1 
ATOM   5421 C CZ    . TYR B 1 364 ? 21.801 13.874  42.136  1.00 22.93 ? 355 TYR B CZ    1 
ATOM   5422 O OH    . TYR B 1 364 ? 20.925 14.097  43.161  1.00 28.71 ? 355 TYR B OH    1 
ATOM   5423 N N     . ASN B 1 365 ? 23.670 13.900  36.177  1.00 21.65 ? 356 ASN B N     1 
ATOM   5424 C CA    . ASN B 1 365 ? 22.658 14.007  35.138  1.00 22.66 ? 356 ASN B CA    1 
ATOM   5425 C C     . ASN B 1 365 ? 21.775 12.772  35.184  1.00 20.88 ? 356 ASN B C     1 
ATOM   5426 O O     . ASN B 1 365 ? 22.189 11.714  34.716  1.00 18.98 ? 356 ASN B O     1 
ATOM   5427 C CB    . ASN B 1 365 ? 23.318 14.125  33.779  1.00 21.05 ? 356 ASN B CB    1 
ATOM   5428 C CG    . ASN B 1 365 ? 22.311 14.246  32.662  1.00 30.64 ? 356 ASN B CG    1 
ATOM   5429 O OD1   . ASN B 1 365 ? 21.101 14.263  32.899  1.00 36.66 ? 356 ASN B OD1   1 
ATOM   5430 N ND2   . ASN B 1 365 ? 22.798 14.268  31.429  1.00 38.70 ? 356 ASN B ND2   1 
ATOM   5431 N N     . ARG B 1 366 ? 20.539 12.940  35.671  1.00 18.16 ? 357 ARG B N     1 
ATOM   5432 C CA    . ARG B 1 366 ? 19.619 11.828  35.807  1.00 17.53 ? 357 ARG B CA    1 
ATOM   5433 C C     . ARG B 1 366 ? 19.322 11.193  34.464  1.00 20.71 ? 357 ARG B C     1 
ATOM   5434 O O     . ARG B 1 366 ? 19.072 9.982   34.400  1.00 18.71 ? 357 ARG B O     1 
ATOM   5435 C CB    . ARG B 1 366 ? 18.327 12.282  36.489  1.00 24.58 ? 357 ARG B CB    1 
ATOM   5436 N N     . LYS B 1 367 ? 19.422 11.983  33.374  1.00 17.14 ? 358 LYS B N     1 
ATOM   5437 C CA    . LYS B 1 367 ? 19.062 11.496  32.054  1.00 20.05 ? 358 LYS B CA    1 
ATOM   5438 C C     . LYS B 1 367 ? 19.929 10.315  31.630  1.00 18.28 ? 358 LYS B C     1 
ATOM   5439 O O     . LYS B 1 367 ? 19.472 9.467   30.853  1.00 20.51 ? 358 LYS B O     1 
ATOM   5440 C CB    . LYS B 1 367 ? 19.170 12.648  31.036  1.00 18.45 ? 358 LYS B CB    1 
ATOM   5441 N N     . THR B 1 368 ? 21.174 10.232  32.106  1.00 15.95 ? 359 THR B N     1 
ATOM   5442 C CA    . THR B 1 368 ? 22.052 9.130   31.711  1.00 19.64 ? 359 THR B CA    1 
ATOM   5443 C C     . THR B 1 368 ? 22.301 8.135   32.851  1.00 18.44 ? 359 THR B C     1 
ATOM   5444 O O     . THR B 1 368 ? 23.285 7.390   32.822  1.00 19.40 ? 359 THR B O     1 
ATOM   5445 C CB    . THR B 1 368 ? 23.368 9.675   31.166  1.00 19.01 ? 359 THR B CB    1 
ATOM   5446 O OG1   . THR B 1 368 ? 23.871 10.683  32.063  1.00 22.87 ? 359 THR B OG1   1 
ATOM   5447 C CG2   . THR B 1 368 ? 23.164 10.283  29.723  1.00 20.60 ? 359 THR B CG2   1 
ATOM   5448 N N     . PHE B 1 369 ? 21.436 8.116   33.859  1.00 17.93 ? 360 PHE B N     1 
ATOM   5449 C CA    . PHE B 1 369 ? 21.529 7.083   34.896  1.00 15.23 ? 360 PHE B CA    1 
ATOM   5450 C C     . PHE B 1 369 ? 21.468 5.661   34.293  1.00 18.13 ? 360 PHE B C     1 
ATOM   5451 O O     . PHE B 1 369 ? 22.258 4.785   34.669  1.00 16.77 ? 360 PHE B O     1 
ATOM   5452 C CB    . PHE B 1 369 ? 20.395 7.273   35.897  1.00 17.41 ? 360 PHE B CB    1 
ATOM   5453 C CG    . PHE B 1 369 ? 20.659 8.283   36.978  1.00 16.58 ? 360 PHE B CG    1 
ATOM   5454 C CD1   . PHE B 1 369 ? 21.848 9.014   37.049  1.00 18.13 ? 360 PHE B CD1   1 
ATOM   5455 C CD2   . PHE B 1 369 ? 19.700 8.460   37.947  1.00 18.64 ? 360 PHE B CD2   1 
ATOM   5456 C CE1   . PHE B 1 369 ? 22.045 9.931   38.105  1.00 20.41 ? 360 PHE B CE1   1 
ATOM   5457 C CE2   . PHE B 1 369 ? 19.893 9.366   38.995  1.00 17.15 ? 360 PHE B CE2   1 
ATOM   5458 C CZ    . PHE B 1 369 ? 21.047 10.092  39.064  1.00 16.18 ? 360 PHE B CZ    1 
ATOM   5459 N N     . TYR B 1 370 ? 20.540 5.412   33.356  1.00 18.18 ? 361 TYR B N     1 
ATOM   5460 C CA    . TYR B 1 370 ? 20.234 4.056   32.895  1.00 15.35 ? 361 TYR B CA    1 
ATOM   5461 C C     . TYR B 1 370 ? 20.358 3.910   31.377  1.00 18.28 ? 361 TYR B C     1 
ATOM   5462 O O     . TYR B 1 370 ? 19.762 2.993   30.799  1.00 22.68 ? 361 TYR B O     1 
ATOM   5463 C CB    . TYR B 1 370 ? 18.816 3.655   33.278  1.00 16.19 ? 361 TYR B CB    1 
ATOM   5464 C CG    . TYR B 1 370 ? 18.461 3.811   34.722  1.00 17.34 ? 361 TYR B CG    1 
ATOM   5465 C CD1   . TYR B 1 370 ? 19.146 3.089   35.700  1.00 13.82 ? 361 TYR B CD1   1 
ATOM   5466 C CD2   . TYR B 1 370 ? 17.430 4.672   35.119  1.00 17.64 ? 361 TYR B CD2   1 
ATOM   5467 C CE1   . TYR B 1 370 ? 18.825 3.212   37.046  1.00 19.32 ? 361 TYR B CE1   1 
ATOM   5468 C CE2   . TYR B 1 370 ? 17.095 4.796   36.490  1.00 22.32 ? 361 TYR B CE2   1 
ATOM   5469 C CZ    . TYR B 1 370 ? 17.801 4.047   37.437  1.00 19.76 ? 361 TYR B CZ    1 
ATOM   5470 O OH    . TYR B 1 370 ? 17.488 4.162   38.781  1.00 18.02 ? 361 TYR B OH    1 
ATOM   5471 N N     . THR B 1 371 ? 21.065 4.810   30.722  1.00 20.34 ? 362 THR B N     1 
ATOM   5472 C CA    . THR B 1 371 ? 21.323 4.679   29.301  1.00 22.98 ? 362 THR B CA    1 
ATOM   5473 C C     . THR B 1 371 ? 22.443 3.672   29.071  1.00 23.69 ? 362 THR B C     1 
ATOM   5474 O O     . THR B 1 371 ? 23.042 3.158   30.022  1.00 19.53 ? 362 THR B O     1 
ATOM   5475 C CB    . THR B 1 371 ? 21.654 6.055   28.743  1.00 19.38 ? 362 THR B CB    1 
ATOM   5476 O OG1   . THR B 1 371 ? 22.578 6.696   29.643  1.00 19.30 ? 362 THR B OG1   1 
ATOM   5477 C CG2   . THR B 1 371 ? 20.361 6.866   28.672  1.00 21.42 ? 362 THR B CG2   1 
ATOM   5478 N N     . GLN B 1 372 ? 22.737 3.365   27.787  1.00 18.89 ? 363 GLN B N     1 
ATOM   5479 C CA    . GLN B 1 372 ? 23.648 2.277   27.468  1.00 21.35 ? 363 GLN B CA    1 
ATOM   5480 C C     . GLN B 1 372 ? 25.033 2.731   27.029  1.00 20.19 ? 363 GLN B C     1 
ATOM   5481 O O     . GLN B 1 372 ? 25.898 1.879   26.814  1.00 19.80 ? 363 GLN B O     1 
ATOM   5482 C CB    . GLN B 1 372 ? 23.045 1.381   26.367  1.00 18.39 ? 363 GLN B CB    1 
ATOM   5483 C CG    . GLN B 1 372 ? 22.091 0.358   26.883  1.00 19.79 ? 363 GLN B CG    1 
ATOM   5484 C CD    . GLN B 1 372 ? 20.934 1.024   27.600  1.00 26.04 ? 363 GLN B CD    1 
ATOM   5485 O OE1   . GLN B 1 372 ? 20.009 1.557   26.970  1.00 25.28 ? 363 GLN B OE1   1 
ATOM   5486 N NE2   . GLN B 1 372 ? 20.998 1.033   28.925  1.00 23.27 ? 363 GLN B NE2   1 
ATOM   5487 N N     . ASP B 1 373 ? 25.269 4.023   26.858  1.00 21.37 ? 364 ASP B N     1 
ATOM   5488 C CA    . ASP B 1 373 ? 26.550 4.473   26.319  1.00 23.58 ? 364 ASP B CA    1 
ATOM   5489 C C     . ASP B 1 373 ? 27.670 4.118   27.275  1.00 24.61 ? 364 ASP B C     1 
ATOM   5490 O O     . ASP B 1 373 ? 27.562 4.418   28.466  1.00 23.22 ? 364 ASP B O     1 
ATOM   5491 C CB    . ASP B 1 373 ? 26.546 5.984   26.101  1.00 24.15 ? 364 ASP B CB    1 
ATOM   5492 C CG    . ASP B 1 373 ? 27.720 6.483   25.250  1.00 29.78 ? 364 ASP B CG    1 
ATOM   5493 O OD1   . ASP B 1 373 ? 28.889 6.556   25.717  1.00 23.42 ? 364 ASP B OD1   1 
ATOM   5494 O OD2   . ASP B 1 373 ? 27.437 6.840   24.082  1.00 31.03 ? 364 ASP B OD2   1 
ATOM   5495 N N     . PRO B 1 374 ? 28.785 3.549   26.798  1.00 22.70 ? 365 PRO B N     1 
ATOM   5496 C CA    . PRO B 1 374 ? 29.851 3.134   27.728  1.00 21.94 ? 365 PRO B CA    1 
ATOM   5497 C C     . PRO B 1 374 ? 30.675 4.267   28.311  1.00 24.75 ? 365 PRO B C     1 
ATOM   5498 O O     . PRO B 1 374 ? 31.533 3.994   29.169  1.00 24.73 ? 365 PRO B O     1 
ATOM   5499 C CB    . PRO B 1 374 ? 30.727 2.207   26.879  1.00 24.85 ? 365 PRO B CB    1 
ATOM   5500 C CG    . PRO B 1 374 ? 30.467 2.643   25.459  1.00 25.75 ? 365 PRO B CG    1 
ATOM   5501 C CD    . PRO B 1 374 ? 29.032 3.077   25.421  1.00 28.50 ? 365 PRO B CD    1 
ATOM   5502 N N     . VAL B 1 375 ? 30.474 5.513   27.863  1.00 26.12 ? 366 VAL B N     1 
ATOM   5503 C CA    . VAL B 1 375 ? 31.280 6.655   28.284  1.00 21.12 ? 366 VAL B CA    1 
ATOM   5504 C C     . VAL B 1 375 ? 30.344 7.729   28.806  1.00 24.06 ? 366 VAL B C     1 
ATOM   5505 O O     . VAL B 1 375 ? 30.539 8.252   29.904  1.00 20.85 ? 366 VAL B O     1 
ATOM   5506 C CB    . VAL B 1 375 ? 32.138 7.228   27.132  1.00 24.98 ? 366 VAL B CB    1 
ATOM   5507 C CG1   . VAL B 1 375 ? 32.844 8.507   27.587  1.00 23.27 ? 366 VAL B CG1   1 
ATOM   5508 C CG2   . VAL B 1 375 ? 33.144 6.195   26.638  1.00 21.75 ? 366 VAL B CG2   1 
ATOM   5509 N N     . VAL B 1 376 ? 29.336 8.084   28.010  1.00 23.04 ? 367 VAL B N     1 
ATOM   5510 C CA    . VAL B 1 376 ? 28.591 9.311   28.269  1.00 24.62 ? 367 VAL B CA    1 
ATOM   5511 C C     . VAL B 1 376 ? 27.706 9.134   29.489  1.00 19.63 ? 367 VAL B C     1 
ATOM   5512 O O     . VAL B 1 376 ? 26.839 8.258   29.512  1.00 20.35 ? 367 VAL B O     1 
ATOM   5513 C CB    . VAL B 1 376 ? 27.763 9.716   27.048  1.00 26.25 ? 367 VAL B CB    1 
ATOM   5514 C CG1   . VAL B 1 376 ? 26.828 10.826  27.444  1.00 26.17 ? 367 VAL B CG1   1 
ATOM   5515 C CG2   . VAL B 1 376 ? 28.703 10.154  25.881  1.00 28.30 ? 367 VAL B CG2   1 
ATOM   5516 N N     . GLY B 1 377 ? 27.908 10.000  30.486  1.00 20.61 ? 368 GLY B N     1 
ATOM   5517 C CA    . GLY B 1 377 ? 27.201 9.976   31.737  1.00 21.03 ? 368 GLY B CA    1 
ATOM   5518 C C     . GLY B 1 377 ? 27.579 8.779   32.572  1.00 21.89 ? 368 GLY B C     1 
ATOM   5519 O O     . GLY B 1 377 ? 26.838 8.412   33.487  1.00 17.52 ? 368 GLY B O     1 
ATOM   5520 N N     . TYR B 1 378 ? 28.696 8.134   32.229  1.00 22.29 ? 369 TYR B N     1 
ATOM   5521 C CA    . TYR B 1 378 ? 29.162 6.942   32.931  1.00 19.51 ? 369 TYR B CA    1 
ATOM   5522 C C     . TYR B 1 378 ? 30.585 7.148   33.427  1.00 19.72 ? 369 TYR B C     1 
ATOM   5523 O O     . TYR B 1 378 ? 30.803 7.242   34.630  1.00 22.06 ? 369 TYR B O     1 
ATOM   5524 C CB    . TYR B 1 378 ? 29.067 5.725   32.009  1.00 17.28 ? 369 TYR B CB    1 
ATOM   5525 C CG    . TYR B 1 378 ? 29.123 4.398   32.737  1.00 20.20 ? 369 TYR B CG    1 
ATOM   5526 C CD1   . TYR B 1 378 ? 28.427 4.194   33.923  1.00 21.12 ? 369 TYR B CD1   1 
ATOM   5527 C CD2   . TYR B 1 378 ? 29.892 3.353   32.226  1.00 19.65 ? 369 TYR B CD2   1 
ATOM   5528 C CE1   . TYR B 1 378 ? 28.496 2.939   34.597  1.00 16.87 ? 369 TYR B CE1   1 
ATOM   5529 C CE2   . TYR B 1 378 ? 29.966 2.157   32.858  1.00 19.67 ? 369 TYR B CE2   1 
ATOM   5530 C CZ    . TYR B 1 378 ? 29.276 1.935   34.031  1.00 18.90 ? 369 TYR B CZ    1 
ATOM   5531 O OH    . TYR B 1 378 ? 29.400 0.683   34.613  1.00 21.23 ? 369 TYR B OH    1 
ATOM   5532 N N     . THR B 1 379 ? 31.570 7.204   32.535  1.00 19.83 ? 370 THR B N     1 
ATOM   5533 C CA    . THR B 1 379 ? 32.959 7.411   32.916  1.00 19.61 ? 370 THR B CA    1 
ATOM   5534 C C     . THR B 1 379 ? 33.519 8.780   32.521  1.00 24.38 ? 370 THR B C     1 
ATOM   5535 O O     . THR B 1 379 ? 34.713 9.032   32.732  1.00 21.72 ? 370 THR B O     1 
ATOM   5536 C CB    . THR B 1 379 ? 33.826 6.308   32.290  1.00 23.84 ? 370 THR B CB    1 
ATOM   5537 O OG1   . THR B 1 379 ? 33.782 6.453   30.865  1.00 22.38 ? 370 THR B OG1   1 
ATOM   5538 C CG2   . THR B 1 379 ? 33.376 4.894   32.693  1.00 22.78 ? 370 THR B CG2   1 
ATOM   5539 N N     . ASP B 1 380 ? 32.708 9.674   31.974  1.00 20.09 ? 371 ASP B N     1 
ATOM   5540 C CA    . ASP B 1 380 ? 33.239 10.963  31.578  1.00 20.21 ? 371 ASP B CA    1 
ATOM   5541 C C     . ASP B 1 380 ? 32.933 12.056  32.578  1.00 27.02 ? 371 ASP B C     1 
ATOM   5542 O O     . ASP B 1 380 ? 33.194 13.225  32.296  1.00 24.73 ? 371 ASP B O     1 
ATOM   5543 C CB    . ASP B 1 380 ? 32.750 11.343  30.175  1.00 19.52 ? 371 ASP B CB    1 
ATOM   5544 C CG    . ASP B 1 380 ? 31.233 11.517  30.064  1.00 25.98 ? 371 ASP B CG    1 
ATOM   5545 O OD1   . ASP B 1 380 ? 30.473 11.338  31.059  1.00 23.18 ? 371 ASP B OD1   1 
ATOM   5546 O OD2   . ASP B 1 380 ? 30.811 11.872  28.910  1.00 26.75 ? 371 ASP B OD2   1 
ATOM   5547 N N     . TYR B 1 381 ? 32.439 11.710  33.766  1.00 23.97 ? 372 TYR B N     1 
ATOM   5548 C CA    . TYR B 1 381 ? 32.434 12.694  34.832  1.00 20.75 ? 372 TYR B CA    1 
ATOM   5549 C C     . TYR B 1 381 ? 33.872 12.961  35.245  1.00 23.46 ? 372 TYR B C     1 
ATOM   5550 O O     . TYR B 1 381 ? 34.593 12.016  35.606  1.00 25.17 ? 372 TYR B O     1 
ATOM   5551 C CB    . TYR B 1 381 ? 31.620 12.215  36.038  1.00 19.34 ? 372 TYR B CB    1 
ATOM   5552 C CG    . TYR B 1 381 ? 30.126 12.221  35.830  1.00 19.73 ? 372 TYR B CG    1 
ATOM   5553 C CD1   . TYR B 1 381 ? 29.401 13.402  35.918  1.00 21.52 ? 372 TYR B CD1   1 
ATOM   5554 C CD2   . TYR B 1 381 ? 29.429 11.031  35.578  1.00 18.61 ? 372 TYR B CD2   1 
ATOM   5555 C CE1   . TYR B 1 381 ? 28.018 13.423  35.757  1.00 22.54 ? 372 TYR B CE1   1 
ATOM   5556 C CE2   . TYR B 1 381 ? 28.026 11.044  35.404  1.00 20.78 ? 372 TYR B CE2   1 
ATOM   5557 C CZ    . TYR B 1 381 ? 27.336 12.267  35.504  1.00 18.29 ? 372 TYR B CZ    1 
ATOM   5558 O OH    . TYR B 1 381 ? 25.953 12.323  35.363  1.00 18.73 ? 372 TYR B OH    1 
ATOM   5559 N N     . PRO B 1 382 ? 34.323 14.210  35.237  1.00 29.92 ? 373 PRO B N     1 
ATOM   5560 C CA    . PRO B 1 382 ? 35.745 14.492  35.442  1.00 28.28 ? 373 PRO B CA    1 
ATOM   5561 C C     . PRO B 1 382 ? 36.172 14.368  36.898  1.00 29.89 ? 373 PRO B C     1 
ATOM   5562 O O     . PRO B 1 382 ? 35.383 14.525  37.836  1.00 29.57 ? 373 PRO B O     1 
ATOM   5563 C CB    . PRO B 1 382 ? 35.884 15.946  34.974  1.00 32.14 ? 373 PRO B CB    1 
ATOM   5564 C CG    . PRO B 1 382 ? 34.519 16.541  35.193  1.00 35.56 ? 373 PRO B CG    1 
ATOM   5565 C CD    . PRO B 1 382 ? 33.546 15.424  34.912  1.00 34.23 ? 373 PRO B CD    1 
ATOM   5566 N N     . PHE B 1 383 ? 37.469 14.123  37.064  1.00 31.37 ? 374 PHE B N     1 
ATOM   5567 C CA    . PHE B 1 383 ? 38.109 14.185  38.365  1.00 28.11 ? 374 PHE B CA    1 
ATOM   5568 C C     . PHE B 1 383 ? 38.315 15.638  38.787  1.00 28.85 ? 374 PHE B C     1 
ATOM   5569 O O     . PHE B 1 383 ? 38.152 16.584  38.008  1.00 31.50 ? 374 PHE B O     1 
ATOM   5570 C CB    . PHE B 1 383 ? 39.440 13.421  38.350  1.00 25.30 ? 374 PHE B CB    1 
ATOM   5571 C CG    . PHE B 1 383 ? 39.270 11.921  38.247  1.00 27.27 ? 374 PHE B CG    1 
ATOM   5572 C CD1   . PHE B 1 383 ? 38.881 11.338  37.054  1.00 27.78 ? 374 PHE B CD1   1 
ATOM   5573 C CD2   . PHE B 1 383 ? 39.471 11.109  39.357  1.00 26.29 ? 374 PHE B CD2   1 
ATOM   5574 C CE1   . PHE B 1 383 ? 38.710 9.954   36.956  1.00 26.23 ? 374 PHE B CE1   1 
ATOM   5575 C CE2   . PHE B 1 383 ? 39.293 9.737   39.262  1.00 22.04 ? 374 PHE B CE2   1 
ATOM   5576 C CZ    . PHE B 1 383 ? 38.920 9.168   38.076  1.00 28.44 ? 374 PHE B CZ    1 
ATOM   5577 N N     . LEU B 1 384 ? 38.650 15.807  40.056  1.00 27.36 ? 375 LEU B N     1 
ATOM   5578 C CA    . LEU B 1 384 ? 38.782 17.125  40.661  1.00 28.72 ? 375 LEU B CA    1 
ATOM   5579 C C     . LEU B 1 384 ? 39.842 17.965  39.942  1.00 36.35 ? 375 LEU B C     1 
ATOM   5580 O O     . LEU B 1 384 ? 40.817 17.423  39.411  1.00 35.60 ? 375 LEU B O     1 
ATOM   5581 C CB    . LEU B 1 384 ? 39.139 16.965  42.138  1.00 30.32 ? 375 LEU B CB    1 
ATOM   5582 C CG    . LEU B 1 384 ? 39.340 18.226  42.950  1.00 39.07 ? 375 LEU B CG    1 
ATOM   5583 C CD1   . LEU B 1 384 ? 38.274 19.257  42.624  1.00 37.45 ? 375 LEU B CD1   1 
ATOM   5584 C CD2   . LEU B 1 384 ? 39.320 17.838  44.393  1.00 34.10 ? 375 LEU B CD2   1 
HETATM 5585 N N1    . FMN C 2 .   ? 22.366 -4.451  0.193   1.00 9.71  ? 401 FMN A N1    1 
HETATM 5586 C C2    . FMN C 2 .   ? 22.156 -3.095  0.194   1.00 10.62 ? 401 FMN A C2    1 
HETATM 5587 O O2    . FMN C 2 .   ? 21.905 -2.470  1.254   1.00 12.16 ? 401 FMN A O2    1 
HETATM 5588 N N3    . FMN C 2 .   ? 22.242 -2.420  -1.011  1.00 13.20 ? 401 FMN A N3    1 
HETATM 5589 C C4    . FMN C 2 .   ? 22.525 -3.068  -2.188  1.00 12.17 ? 401 FMN A C4    1 
HETATM 5590 O O4    . FMN C 2 .   ? 22.599 -2.442  -3.252  1.00 13.32 ? 401 FMN A O4    1 
HETATM 5591 C C4A   . FMN C 2 .   ? 22.753 -4.439  -2.190  1.00 10.61 ? 401 FMN A C4A   1 
HETATM 5592 N N5    . FMN C 2 .   ? 23.085 -5.120  -3.364  1.00 12.14 ? 401 FMN A N5    1 
HETATM 5593 C C5A   . FMN C 2 .   ? 23.187 -6.500  -3.331  1.00 11.43 ? 401 FMN A C5A   1 
HETATM 5594 C C6    . FMN C 2 .   ? 23.460 -7.231  -4.500  1.00 12.41 ? 401 FMN A C6    1 
HETATM 5595 C C7    . FMN C 2 .   ? 23.591 -8.614  -4.445  1.00 15.59 ? 401 FMN A C7    1 
HETATM 5596 C C7M   . FMN C 2 .   ? 23.860 -9.390  -5.710  1.00 17.52 ? 401 FMN A C7M   1 
HETATM 5597 C C8    . FMN C 2 .   ? 23.454 -9.283  -3.245  1.00 13.32 ? 401 FMN A C8    1 
HETATM 5598 C C8M   . FMN C 2 .   ? 23.601 -10.788 -3.134  1.00 15.34 ? 401 FMN A C8M   1 
HETATM 5599 C C9    . FMN C 2 .   ? 23.220 -8.561  -2.077  1.00 14.17 ? 401 FMN A C9    1 
HETATM 5600 C C9A   . FMN C 2 .   ? 23.048 -7.202  -2.106  1.00 10.46 ? 401 FMN A C9A   1 
HETATM 5601 N N10   . FMN C 2 .   ? 22.835 -6.511  -0.932  1.00 12.05 ? 401 FMN A N10   1 
HETATM 5602 C C10   . FMN C 2 .   ? 22.640 -5.132  -0.982  1.00 13.34 ? 401 FMN A C10   1 
HETATM 5603 C "C1'" . FMN C 2 .   ? 22.641 -7.264  0.350   1.00 9.12  ? 401 FMN A "C1'" 1 
HETATM 5604 C "C2'" . FMN C 2 .   ? 21.201 -7.776  0.399   1.00 10.36 ? 401 FMN A "C2'" 1 
HETATM 5605 O "O2'" . FMN C 2 .   ? 20.302 -6.681  0.520   1.00 14.65 ? 401 FMN A "O2'" 1 
HETATM 5606 C "C3'" . FMN C 2 .   ? 20.870 -8.691  1.587   1.00 12.82 ? 401 FMN A "C3'" 1 
HETATM 5607 O "O3'" . FMN C 2 .   ? 21.028 -7.915  2.753   1.00 12.03 ? 401 FMN A "O3'" 1 
HETATM 5608 C "C4'" . FMN C 2 .   ? 21.767 -9.925  1.622   1.00 12.12 ? 401 FMN A "C4'" 1 
HETATM 5609 O "O4'" . FMN C 2 .   ? 21.699 -10.607 0.370   1.00 13.79 ? 401 FMN A "O4'" 1 
HETATM 5610 C "C5'" . FMN C 2 .   ? 21.451 -10.900 2.780   1.00 13.85 ? 401 FMN A "C5'" 1 
HETATM 5611 O "O5'" . FMN C 2 .   ? 20.111 -11.328 2.707   1.00 12.88 ? 401 FMN A "O5'" 1 
HETATM 5612 P P     . FMN C 2 .   ? 19.734 -12.749 2.053   1.00 14.18 ? 401 FMN A P     1 
HETATM 5613 O O1P   . FMN C 2 .   ? 18.229 -12.825 2.115   1.00 13.74 ? 401 FMN A O1P   1 
HETATM 5614 O O2P   . FMN C 2 .   ? 20.397 -13.792 2.920   1.00 17.63 ? 401 FMN A O2P   1 
HETATM 5615 O O3P   . FMN C 2 .   ? 20.241 -12.820 0.639   1.00 14.07 ? 401 FMN A O3P   1 
HETATM 5616 N NBU   . 5J8 D 3 .   ? 26.747 -5.587  -4.017  0.82 17.03 ? 402 5J8 A NBU   1 
HETATM 5617 C CBT   . 5J8 D 3 .   ? 26.776 -5.148  -2.643  0.82 18.59 ? 402 5J8 A CBT   1 
HETATM 5618 O OBV   . 5J8 D 3 .   ? 26.799 -3.994  -2.344  0.82 20.93 ? 402 5J8 A OBV   1 
HETATM 5619 C CBR   . 5J8 D 3 .   ? 26.779 -6.155  -1.526  0.82 21.95 ? 402 5J8 A CBR   1 
HETATM 5620 C CBQ   . 5J8 D 3 .   ? 26.827 -7.660  -1.935  0.82 19.64 ? 402 5J8 A CBQ   1 
HETATM 5621 C CBS   . 5J8 D 3 .   ? 27.353 -5.767  -0.336  0.82 21.19 ? 402 5J8 A CBS   1 
HETATM 5622 C CBN   . 5J8 D 3 .   ? 27.961 -6.954  0.547   0.82 19.30 ? 402 5J8 A CBN   1 
HETATM 5623 C CBO   . 5J8 D 3 .   ? 27.196 -8.070  0.583   0.82 15.61 ? 402 5J8 A CBO   1 
HETATM 5624 N NBP   . 5J8 D 3 .   ? 26.774 -8.596  -0.906  0.82 23.04 ? 402 5J8 A NBP   1 
HETATM 5625 C CBM   . 5J8 D 3 .   ? 26.316 -9.922  -1.140  0.82 18.65 ? 402 5J8 A CBM   1 
HETATM 5626 O OBG   . 5J8 D 3 .   ? 25.151 -10.180 -0.088  0.82 18.40 ? 402 5J8 A OBG   1 
HETATM 5627 C CBF   . 5J8 D 3 .   ? 27.198 -10.851 -0.832  0.82 22.99 ? 402 5J8 A CBF   1 
HETATM 5628 O OBI   . 5J8 D 3 .   ? 28.173 -11.056 -1.950  0.82 20.57 ? 402 5J8 A OBI   1 
HETATM 5629 C CBE   . 5J8 D 3 .   ? 26.303 -12.091 -0.648  0.82 15.67 ? 402 5J8 A CBE   1 
HETATM 5630 O OBJ   . 5J8 D 3 .   ? 25.900 -12.549 -1.858  0.82 19.22 ? 402 5J8 A OBJ   1 
HETATM 5631 C CBH   . 5J8 D 3 .   ? 25.084 -11.490 0.122   0.82 18.32 ? 402 5J8 A CBH   1 
HETATM 5632 C CBK   . 5J8 D 3 .   ? 25.192 -11.712 1.627   0.82 17.48 ? 402 5J8 A CBK   1 
HETATM 5633 O OBL   . 5J8 D 3 .   ? 26.446 -11.255 2.126   0.82 25.10 ? 402 5J8 A OBL   1 
HETATM 5634 P PAA   . 5J8 D 3 .   ? 27.159 -12.115 3.372   0.82 26.56 ? 402 5J8 A PAA   1 
HETATM 5635 O OAC   . 5J8 D 3 .   ? 28.553 -11.592 3.577   0.82 24.94 ? 402 5J8 A OAC   1 
HETATM 5636 O OAB   . 5J8 D 3 .   ? 26.244 -12.055 4.580   0.82 25.33 ? 402 5J8 A OAB   1 
HETATM 5637 O OAD   . 5J8 D 3 .   ? 27.262 -13.600 2.722   0.82 28.20 ? 402 5J8 A OAD   1 
HETATM 5638 P PAE   . 5J8 D 3 .   ? 26.995 -15.055 3.376   0.82 30.75 ? 402 5J8 A PAE   1 
HETATM 5639 O OAG   . 5J8 D 3 .   ? 27.886 -15.964 2.548   0.82 29.02 ? 402 5J8 A OAG   1 
HETATM 5640 O OAF   . 5J8 D 3 .   ? 25.534 -15.490 3.279   0.82 27.39 ? 402 5J8 A OAF   1 
HETATM 5641 O "O5'" . 5J8 D 3 .   ? 27.473 -15.090 4.955   0.82 27.42 ? 402 5J8 A "O5'" 1 
HETATM 5642 N N1    . FMN E 2 .   ? 20.199 0.257   45.288  1.00 12.04 ? 401 FMN B N1    1 
HETATM 5643 C C2    . FMN E 2 .   ? 20.399 -1.083  45.324  1.00 14.20 ? 401 FMN B C2    1 
HETATM 5644 O O2    . FMN E 2 .   ? 20.335 -1.696  46.404  1.00 15.22 ? 401 FMN B O2    1 
HETATM 5645 N N3    . FMN E 2 .   ? 20.685 -1.742  44.134  1.00 13.95 ? 401 FMN B N3    1 
HETATM 5646 C C4    . FMN E 2 .   ? 20.747 -1.065  42.937  1.00 13.62 ? 401 FMN B C4    1 
HETATM 5647 O O4    . FMN E 2 .   ? 20.985 -1.690  41.896  1.00 16.11 ? 401 FMN B O4    1 
HETATM 5648 C C4A   . FMN E 2 .   ? 20.550 0.302   42.917  1.00 12.99 ? 401 FMN B C4A   1 
HETATM 5649 N N5    . FMN E 2 .   ? 20.582 0.990   41.706  1.00 12.64 ? 401 FMN B N5    1 
HETATM 5650 C C5A   . FMN E 2 .   ? 20.493 2.362   41.714  1.00 14.04 ? 401 FMN B C5A   1 
HETATM 5651 C C6    . FMN E 2 .   ? 20.588 3.036   40.484  1.00 13.03 ? 401 FMN B C6    1 
HETATM 5652 C C7    . FMN E 2 .   ? 20.445 4.427   40.426  1.00 15.24 ? 401 FMN B C7    1 
HETATM 5653 C C7M   . FMN E 2 .   ? 20.594 5.125   39.081  1.00 15.34 ? 401 FMN B C7M   1 
HETATM 5654 C C8    . FMN E 2 .   ? 20.209 5.131   41.604  1.00 15.30 ? 401 FMN B C8    1 
HETATM 5655 C C8M   . FMN E 2 .   ? 20.043 6.629   41.641  1.00 17.07 ? 401 FMN B C8M   1 
HETATM 5656 C C9    . FMN E 2 .   ? 20.084 4.441   42.823  1.00 13.59 ? 401 FMN B C9    1 
HETATM 5657 C C9A   . FMN E 2 .   ? 20.231 3.066   42.887  1.00 9.19  ? 401 FMN B C9A   1 
HETATM 5658 N N10   . FMN E 2 .   ? 20.106 2.377   44.105  1.00 15.93 ? 401 FMN B N10   1 
HETATM 5659 C C10   . FMN E 2 .   ? 20.300 0.990   44.111  1.00 14.28 ? 401 FMN B C10   1 
HETATM 5660 C "C1'" . FMN E 2 .   ? 19.877 3.144   45.391  1.00 11.22 ? 401 FMN B "C1'" 1 
HETATM 5661 C "C2'" . FMN E 2 .   ? 21.258 3.597   45.882  1.00 13.30 ? 401 FMN B "C2'" 1 
HETATM 5662 O "O2'" . FMN E 2 .   ? 22.093 2.480   46.246  1.00 14.45 ? 401 FMN B "O2'" 1 
HETATM 5663 C "C3'" . FMN E 2 .   ? 21.209 4.534   47.102  1.00 12.75 ? 401 FMN B "C3'" 1 
HETATM 5664 O "O3'" . FMN E 2 .   ? 20.712 3.754   48.178  1.00 14.65 ? 401 FMN B "O3'" 1 
HETATM 5665 C "C4'" . FMN E 2 .   ? 20.310 5.731   46.820  1.00 15.30 ? 401 FMN B "C4'" 1 
HETATM 5666 O "O4'" . FMN E 2 .   ? 20.776 6.409   45.637  1.00 17.14 ? 401 FMN B "O4'" 1 
HETATM 5667 C "C5'" . FMN E 2 .   ? 20.270 6.764   47.965  1.00 12.57 ? 401 FMN B "C5'" 1 
HETATM 5668 O "O5'" . FMN E 2 .   ? 21.590 7.133   48.316  1.00 13.84 ? 401 FMN B "O5'" 1 
HETATM 5669 P P     . FMN E 2 .   ? 22.149 8.579   47.854  1.00 17.30 ? 401 FMN B P     1 
HETATM 5670 O O1P   . FMN E 2 .   ? 23.564 8.637   48.329  1.00 16.67 ? 401 FMN B O1P   1 
HETATM 5671 O O2P   . FMN E 2 .   ? 21.246 9.594   48.477  1.00 17.53 ? 401 FMN B O2P   1 
HETATM 5672 O O3P   . FMN E 2 .   ? 21.947 8.601   46.383  1.00 16.29 ? 401 FMN B O3P   1 
HETATM 5673 N NBU   . 5J8 F 3 .   ? 17.389 1.468   40.044  0.85 16.53 ? 402 5J8 B NBU   1 
HETATM 5674 C CBT   . 5J8 F 3 .   ? 16.807 0.945   41.257  0.85 22.57 ? 402 5J8 B CBT   1 
HETATM 5675 O OBV   . 5J8 F 3 .   ? 16.609 -0.215  41.404  0.85 27.07 ? 402 5J8 B OBV   1 
HETATM 5676 C CBR   . 5J8 F 3 .   ? 16.478 1.909   42.371  0.85 23.82 ? 402 5J8 B CBR   1 
HETATM 5677 C CBQ   . 5J8 F 3 .   ? 16.602 3.422   42.004  0.85 17.88 ? 402 5J8 B CBQ   1 
HETATM 5678 C CBS   . 5J8 F 3 .   ? 15.459 1.539   43.225  0.85 20.95 ? 402 5J8 B CBS   1 
HETATM 5679 C CBN   . 5J8 F 3 .   ? 14.724 2.754   43.952  0.85 24.82 ? 402 5J8 B CBN   1 
HETATM 5680 C CBO   . 5J8 F 3 .   ? 15.507 3.816   44.260  0.85 20.63 ? 402 5J8 B CBO   1 
HETATM 5681 N NBP   . 5J8 F 3 .   ? 16.337 4.389   42.988  0.85 25.16 ? 402 5J8 B NBP   1 
HETATM 5682 C CBM   . 5J8 F 3 .   ? 16.804 5.749   42.902  0.85 21.50 ? 402 5J8 B CBM   1 
HETATM 5683 O OBG   . 5J8 F 3 .   ? 17.632 6.030   44.238  0.85 22.80 ? 402 5J8 B OBG   1 
HETATM 5684 C CBF   . 5J8 F 3 .   ? 15.886 6.686   42.890  0.85 21.46 ? 402 5J8 B CBF   1 
HETATM 5685 O OBI   . 5J8 F 3 .   ? 15.348 6.809   41.498  0.85 21.11 ? 402 5J8 B OBI   1 
HETATM 5686 C CBE   . 5J8 F 3 .   ? 16.697 7.922   43.357  0.85 19.19 ? 402 5J8 B CBE   1 
HETATM 5687 O OBJ   . 5J8 F 3 .   ? 17.451 8.434   42.342  0.85 20.60 ? 402 5J8 B OBJ   1 
HETATM 5688 C CBH   . 5J8 F 3 .   ? 17.642 7.332   44.439  0.85 19.48 ? 402 5J8 B CBH   1 
HETATM 5689 C CBK   . 5J8 F 3 .   ? 17.032 7.582   45.825  0.85 20.65 ? 402 5J8 B CBK   1 
HETATM 5690 O OBL   . 5J8 F 3 .   ? 15.687 7.107   45.826  0.85 24.96 ? 402 5J8 B OBL   1 
HETATM 5691 P PAA   . 5J8 F 3 .   ? 14.665 7.886   46.885  0.85 28.67 ? 402 5J8 B PAA   1 
HETATM 5692 O OAC   . 5J8 F 3 .   ? 13.256 7.355   46.842  0.85 26.56 ? 402 5J8 B OAC   1 
HETATM 5693 O OAB   . 5J8 F 3 .   ? 15.308 7.742   48.238  0.85 26.48 ? 402 5J8 B OAB   1 
HETATM 5694 O OAD   . 5J8 F 3 .   ? 14.718 9.377   46.230  0.85 27.70 ? 402 5J8 B OAD   1 
HETATM 5695 P PAE   . 5J8 F 3 .   ? 14.732 10.821  46.991  0.85 30.92 ? 402 5J8 B PAE   1 
HETATM 5696 O OAG   . 5J8 F 3 .   ? 13.902 10.832  48.258  0.85 30.98 ? 402 5J8 B OAG   1 
HETATM 5697 O OAF   . 5J8 F 3 .   ? 14.080 11.719  45.936  0.85 25.20 ? 402 5J8 B OAF   1 
HETATM 5698 O "O5'" . 5J8 F 3 .   ? 16.261 11.344  47.338  0.85 31.36 ? 402 5J8 B "O5'" 1 
HETATM 5699 O O     . HOH G 4 .   ? 47.361 9.272   3.952   1.00 40.33 ? 501 HOH A O     1 
HETATM 5700 O O     . HOH G 4 .   ? 11.195 9.140   -21.339 1.00 42.61 ? 502 HOH A O     1 
HETATM 5701 O O     . HOH G 4 .   ? 19.822 -19.029 6.654   1.00 40.74 ? 503 HOH A O     1 
HETATM 5702 O O     . HOH G 4 .   ? 10.979 -5.227  22.908  1.00 36.88 ? 504 HOH A O     1 
HETATM 5703 O O     . HOH G 4 .   ? 16.864 -16.368 -20.986 1.00 26.89 ? 505 HOH A O     1 
HETATM 5704 O O     . HOH G 4 .   ? 42.522 7.516   -7.136  1.00 35.73 ? 506 HOH A O     1 
HETATM 5705 O O     . HOH G 4 .   ? 30.239 -11.588 -0.767  1.00 38.23 ? 507 HOH A O     1 
HETATM 5706 O O     . HOH G 4 .   ? 30.694 12.532  -3.327  1.00 17.20 ? 508 HOH A O     1 
HETATM 5707 O O     . HOH G 4 .   ? 41.058 -0.328  8.851   1.00 34.77 ? 509 HOH A O     1 
HETATM 5708 O O     . HOH G 4 .   ? 39.109 4.947   15.061  1.00 35.46 ? 510 HOH A O     1 
HETATM 5709 O O     . HOH G 4 .   ? 6.148  11.830  8.975   1.00 31.07 ? 511 HOH A O     1 
HETATM 5710 O O     . HOH G 4 .   ? 6.681  -21.782 -14.382 1.00 35.50 ? 512 HOH A O     1 
HETATM 5711 O O     . HOH G 4 .   ? -0.680 -7.021  -7.696  1.00 27.58 ? 513 HOH A O     1 
HETATM 5712 O O     . HOH G 4 .   ? 37.433 13.639  17.913  1.00 31.63 ? 514 HOH A O     1 
HETATM 5713 O O     . HOH G 4 .   ? 42.656 9.323   -9.131  1.00 31.39 ? 515 HOH A O     1 
HETATM 5714 O O     . HOH G 4 .   ? 32.306 14.868  -2.822  1.00 35.47 ? 516 HOH A O     1 
HETATM 5715 O O     . HOH G 4 .   ? 3.316  -17.668 -8.727  1.00 29.94 ? 517 HOH A O     1 
HETATM 5716 O O     . HOH G 4 .   ? 32.871 -3.362  -3.974  1.00 19.00 ? 518 HOH A O     1 
HETATM 5717 O O     . HOH G 4 .   ? 14.081 -7.524  -19.281 1.00 31.53 ? 519 HOH A O     1 
HETATM 5718 O O     . HOH G 4 .   ? 2.154  -3.127  -13.734 1.00 23.28 ? 520 HOH A O     1 
HETATM 5719 O O     . HOH G 4 .   ? 30.830 -4.642  -2.422  1.00 24.08 ? 521 HOH A O     1 
HETATM 5720 O O     . HOH G 4 .   ? 23.234 -27.429 -7.826  1.00 32.52 ? 522 HOH A O     1 
HETATM 5721 O O     . HOH G 4 .   ? 42.852 13.222  2.080   1.00 29.17 ? 523 HOH A O     1 
HETATM 5722 O O     . HOH G 4 .   ? 32.714 1.426   19.314  1.00 25.81 ? 524 HOH A O     1 
HETATM 5723 O O     . HOH G 4 .   ? 1.282  1.574   -3.595  1.00 31.05 ? 525 HOH A O     1 
HETATM 5724 O O     . HOH G 4 .   ? 17.890 -9.657  3.472   1.00 19.68 ? 526 HOH A O     1 
HETATM 5725 O O     . HOH G 4 .   ? 15.315 3.821   -19.733 1.00 31.13 ? 527 HOH A O     1 
HETATM 5726 O O     . HOH G 4 .   ? 43.448 -1.708  -1.712  1.00 20.95 ? 528 HOH A O     1 
HETATM 5727 O O     . HOH G 4 .   ? 10.017 -24.579 3.243   1.00 32.15 ? 529 HOH A O     1 
HETATM 5728 O O     . HOH G 4 .   ? 47.461 -1.932  -2.334  1.00 36.99 ? 530 HOH A O     1 
HETATM 5729 O O     . HOH G 4 .   ? 36.580 -5.609  19.996  1.00 36.75 ? 531 HOH A O     1 
HETATM 5730 O O     . HOH G 4 .   ? 34.230 21.967  10.907  1.00 29.02 ? 532 HOH A O     1 
HETATM 5731 O O     . HOH G 4 .   ? 3.199  6.090   -9.096  1.00 29.48 ? 533 HOH A O     1 
HETATM 5732 O O     . HOH G 4 .   ? 38.149 8.151   15.065  1.00 35.85 ? 534 HOH A O     1 
HETATM 5733 O O     . HOH G 4 .   ? 22.779 -10.194 14.098  1.00 16.97 ? 535 HOH A O     1 
HETATM 5734 O O     . HOH G 4 .   ? 17.385 -5.652  -6.970  1.00 17.51 ? 536 HOH A O     1 
HETATM 5735 O O     . HOH G 4 .   ? 29.042 6.908   -13.626 1.00 24.68 ? 537 HOH A O     1 
HETATM 5736 O O     . HOH G 4 .   ? 29.268 -3.432  7.282   1.00 23.69 ? 538 HOH A O     1 
HETATM 5737 O O     . HOH G 4 .   ? 23.383 -11.674 -17.528 1.00 22.90 ? 539 HOH A O     1 
HETATM 5738 O O     . HOH G 4 .   ? 17.632 -4.369  -10.036 1.00 18.34 ? 540 HOH A O     1 
HETATM 5739 O O     . HOH G 4 .   ? 20.120 -16.327 2.301   1.00 23.61 ? 541 HOH A O     1 
HETATM 5740 O O     . HOH G 4 .   ? 15.533 -22.297 8.541   1.00 26.60 ? 542 HOH A O     1 
HETATM 5741 O O     . HOH G 4 .   ? 7.618  -9.788  -17.409 1.00 44.52 ? 543 HOH A O     1 
HETATM 5742 O O     . HOH G 4 .   ? 35.514 11.201  -6.022  1.00 27.98 ? 544 HOH A O     1 
HETATM 5743 O O     . HOH G 4 .   ? 37.619 19.052  10.241  1.00 23.61 ? 545 HOH A O     1 
HETATM 5744 O O     . HOH G 4 .   ? 29.092 -9.233  -3.910  1.00 25.61 ? 546 HOH A O     1 
HETATM 5745 O O     . HOH G 4 .   ? 31.409 22.008  11.848  1.00 39.78 ? 547 HOH A O     1 
HETATM 5746 O O     . HOH G 4 .   ? 38.868 13.138  -5.494  1.00 23.68 ? 548 HOH A O     1 
HETATM 5747 O O     . HOH G 4 .   ? 24.267 5.734   1.217   1.00 15.70 ? 549 HOH A O     1 
HETATM 5748 O O     . HOH G 4 .   ? 17.708 -16.810 2.428   1.00 26.44 ? 550 HOH A O     1 
HETATM 5749 O O     . HOH G 4 .   ? 14.205 -25.739 -3.254  1.00 19.38 ? 551 HOH A O     1 
HETATM 5750 O O     . HOH G 4 .   ? 24.197 -10.346 4.759   1.00 21.65 ? 552 HOH A O     1 
HETATM 5751 O O     . HOH G 4 .   ? 29.631 -7.860  -13.986 1.00 27.88 ? 553 HOH A O     1 
HETATM 5752 O O     . HOH G 4 .   ? 25.317 -3.099  -0.301  1.00 14.99 ? 554 HOH A O     1 
HETATM 5753 O O     . HOH G 4 .   ? 17.970 -3.391  23.879  1.00 21.01 ? 555 HOH A O     1 
HETATM 5754 O O     . HOH G 4 .   ? 28.235 12.826  -3.292  1.00 18.88 ? 556 HOH A O     1 
HETATM 5755 O O     . HOH G 4 .   ? 35.219 0.403   3.532   1.00 18.64 ? 557 HOH A O     1 
HETATM 5756 O O     . HOH G 4 .   ? 15.887 0.461   -21.623 1.00 32.16 ? 558 HOH A O     1 
HETATM 5757 O O     . HOH G 4 .   ? 4.382  -1.296  15.037  1.00 37.08 ? 559 HOH A O     1 
HETATM 5758 O O     . HOH G 4 .   ? 16.801 -13.131 14.370  1.00 33.27 ? 560 HOH A O     1 
HETATM 5759 O O     . HOH G 4 .   ? 34.628 -7.950  -6.114  1.00 31.56 ? 561 HOH A O     1 
HETATM 5760 O O     . HOH G 4 .   ? 34.130 20.592  -2.026  1.00 35.94 ? 562 HOH A O     1 
HETATM 5761 O O     . HOH G 4 .   ? 6.650  2.376   10.488  1.00 20.89 ? 563 HOH A O     1 
HETATM 5762 O O     . HOH G 4 .   ? 30.999 7.603   -8.931  1.00 18.67 ? 564 HOH A O     1 
HETATM 5763 O O     . HOH G 4 .   ? 25.016 -6.479  11.642  1.00 21.76 ? 565 HOH A O     1 
HETATM 5764 O O     . HOH G 4 .   ? 6.601  -9.045  15.408  1.00 23.53 ? 566 HOH A O     1 
HETATM 5765 O O     . HOH G 4 .   ? 23.970 19.979  4.204   1.00 20.16 ? 567 HOH A O     1 
HETATM 5766 O O     . HOH G 4 .   ? 32.195 -2.999  -8.452  1.00 13.71 ? 568 HOH A O     1 
HETATM 5767 O O     . HOH G 4 .   ? 22.181 -15.694 9.548   1.00 35.07 ? 569 HOH A O     1 
HETATM 5768 O O     . HOH G 4 .   ? 12.797 14.622  -14.381 1.00 33.66 ? 570 HOH A O     1 
HETATM 5769 O O     . HOH G 4 .   ? 18.766 -7.760  24.590  1.00 28.81 ? 571 HOH A O     1 
HETATM 5770 O O     . HOH G 4 .   ? 22.274 -1.955  -9.861  1.00 15.14 ? 572 HOH A O     1 
HETATM 5771 O O     . HOH G 4 .   ? 16.755 -21.421 -10.947 1.00 22.37 ? 573 HOH A O     1 
HETATM 5772 O O     . HOH G 4 .   ? 22.787 -0.765  -7.464  1.00 14.27 ? 574 HOH A O     1 
HETATM 5773 O O     . HOH G 4 .   ? 33.490 -11.497 -13.250 1.00 26.09 ? 575 HOH A O     1 
HETATM 5774 O O     . HOH G 4 .   ? 29.329 -5.427  -19.557 1.00 24.52 ? 576 HOH A O     1 
HETATM 5775 O O     . HOH G 4 .   ? 23.456 -7.937  4.143   1.00 15.44 ? 577 HOH A O     1 
HETATM 5776 O O     . HOH G 4 .   ? 22.842 -4.981  -21.662 1.00 21.66 ? 578 HOH A O     1 
HETATM 5777 O O     . HOH G 4 .   ? 36.144 5.526   -16.586 1.00 38.45 ? 579 HOH A O     1 
HETATM 5778 O O     . HOH G 4 .   ? 44.474 -0.729  4.015   1.00 32.07 ? 580 HOH A O     1 
HETATM 5779 O O     . HOH G 4 .   ? 16.946 -11.902 -10.954 1.00 15.74 ? 581 HOH A O     1 
HETATM 5780 O O     . HOH G 4 .   ? 26.278 4.324   -5.681  1.00 18.48 ? 582 HOH A O     1 
HETATM 5781 O O     . HOH G 4 .   ? 30.312 10.758  11.891  1.00 17.70 ? 583 HOH A O     1 
HETATM 5782 O O     . HOH G 4 .   ? 4.761  -10.998 -7.941  1.00 24.13 ? 584 HOH A O     1 
HETATM 5783 O O     . HOH G 4 .   ? 20.277 16.521  -8.257  1.00 36.84 ? 585 HOH A O     1 
HETATM 5784 O O     . HOH G 4 .   ? 19.203 -17.871 -18.248 1.00 35.95 ? 586 HOH A O     1 
HETATM 5785 O O     . HOH G 4 .   ? 19.798 -3.127  -12.319 1.00 14.97 ? 587 HOH A O     1 
HETATM 5786 O O     . HOH G 4 .   ? 42.167 -3.829  -3.381  1.00 18.36 ? 588 HOH A O     1 
HETATM 5787 O O     . HOH G 4 .   ? 1.767  4.011   -3.146  1.00 33.88 ? 589 HOH A O     1 
HETATM 5788 O O     . HOH G 4 .   ? 15.183 -11.794 13.942  1.00 35.00 ? 590 HOH A O     1 
HETATM 5789 O O     . HOH G 4 .   ? 37.309 18.054  1.565   1.00 20.40 ? 591 HOH A O     1 
HETATM 5790 O O     . HOH G 4 .   ? 17.318 -12.504 4.698   1.00 16.45 ? 592 HOH A O     1 
HETATM 5791 O O     . HOH G 4 .   ? 21.431 -14.199 -11.291 1.00 18.87 ? 593 HOH A O     1 
HETATM 5792 O O     . HOH G 4 .   ? 11.642 -1.847  24.379  1.00 27.23 ? 594 HOH A O     1 
HETATM 5793 O O     . HOH G 4 .   ? 17.186 -14.899 0.614   1.00 15.99 ? 595 HOH A O     1 
HETATM 5794 O O     . HOH G 4 .   ? 11.957 -2.020  17.032  1.00 15.59 ? 596 HOH A O     1 
HETATM 5795 O O     . HOH G 4 .   ? 32.068 13.320  22.059  1.00 29.66 ? 597 HOH A O     1 
HETATM 5796 O O     . HOH G 4 .   ? 39.656 2.261   -0.872  1.00 16.75 ? 598 HOH A O     1 
HETATM 5797 O O     . HOH G 4 .   ? 3.512  7.716   -1.714  1.00 30.88 ? 599 HOH A O     1 
HETATM 5798 O O     . HOH G 4 .   ? 43.862 7.519   -5.187  1.00 32.01 ? 600 HOH A O     1 
HETATM 5799 O O     . HOH G 4 .   ? 6.030  -6.600  2.475   1.00 17.78 ? 601 HOH A O     1 
HETATM 5800 O O     . HOH G 4 .   ? 9.776  3.063   12.594  1.00 17.43 ? 602 HOH A O     1 
HETATM 5801 O O     . HOH G 4 .   ? 12.228 -22.520 5.999   1.00 21.72 ? 603 HOH A O     1 
HETATM 5802 O O     . HOH G 4 .   ? 28.748 3.280   -12.457 1.00 16.79 ? 604 HOH A O     1 
HETATM 5803 O O     . HOH G 4 .   ? 33.572 8.036   -3.581  1.00 18.02 ? 605 HOH A O     1 
HETATM 5804 O O     . HOH G 4 .   ? 0.495  -2.801  12.114  1.00 30.18 ? 606 HOH A O     1 
HETATM 5805 O O     . HOH G 4 .   ? 6.250  -8.090  -3.189  1.00 19.89 ? 607 HOH A O     1 
HETATM 5806 O O     . HOH G 4 .   ? 20.109 2.806   22.366  1.00 30.54 ? 608 HOH A O     1 
HETATM 5807 O O     . HOH G 4 .   ? 30.040 14.709  -6.946  1.00 32.75 ? 609 HOH A O     1 
HETATM 5808 O O     . HOH G 4 .   ? 30.683 5.377   -12.449 1.00 19.72 ? 610 HOH A O     1 
HETATM 5809 O O     . HOH G 4 .   ? 39.560 16.412  0.853   1.00 29.13 ? 611 HOH A O     1 
HETATM 5810 O O     . HOH G 4 .   ? 27.885 8.277   10.690  1.00 16.75 ? 612 HOH A O     1 
HETATM 5811 O O     . HOH G 4 .   ? 7.128  13.877  1.094   1.00 29.04 ? 613 HOH A O     1 
HETATM 5812 O O     . HOH G 4 .   ? -1.895 -14.696 8.778   1.00 36.25 ? 614 HOH A O     1 
HETATM 5813 O O     . HOH G 4 .   ? 31.914 25.938  -2.591  1.00 23.42 ? 615 HOH A O     1 
HETATM 5814 O O     . HOH G 4 .   ? 12.078 16.189  -16.379 1.00 39.49 ? 616 HOH A O     1 
HETATM 5815 O O     . HOH G 4 .   ? 10.500 -15.406 -15.804 1.00 24.87 ? 617 HOH A O     1 
HETATM 5816 O O     . HOH G 4 .   ? 19.962 -13.502 14.193  1.00 33.45 ? 618 HOH A O     1 
HETATM 5817 O O     . HOH G 4 .   ? 28.785 2.417   -15.004 1.00 19.02 ? 619 HOH A O     1 
HETATM 5818 O O     . HOH G 4 .   ? 10.037 16.271  -4.625  1.00 23.79 ? 620 HOH A O     1 
HETATM 5819 O O     . HOH G 4 .   ? 37.646 7.547   -15.033 1.00 31.60 ? 621 HOH A O     1 
HETATM 5820 O O     . HOH G 4 .   ? 25.293 -19.613 -7.842  1.00 27.86 ? 622 HOH A O     1 
HETATM 5821 O O     . HOH G 4 .   ? 35.365 -6.441  -2.611  1.00 23.38 ? 623 HOH A O     1 
HETATM 5822 O O     . HOH G 4 .   ? 32.130 -0.929  -4.756  1.00 15.38 ? 624 HOH A O     1 
HETATM 5823 O O     . HOH G 4 .   ? 20.728 -18.185 0.177   1.00 31.66 ? 625 HOH A O     1 
HETATM 5824 O O     . HOH G 4 .   ? 12.959 -21.059 3.129   1.00 25.43 ? 626 HOH A O     1 
HETATM 5825 O O     . HOH G 4 .   ? 40.157 0.117   6.641   1.00 30.30 ? 627 HOH A O     1 
HETATM 5826 O O     . HOH G 4 .   ? 37.293 -9.340  -3.082  1.00 29.27 ? 628 HOH A O     1 
HETATM 5827 O O     . HOH G 4 .   ? 16.196 -4.838  -4.703  1.00 13.48 ? 629 HOH A O     1 
HETATM 5828 O O     . HOH G 4 .   ? 8.078  -27.246 -0.183  1.00 36.85 ? 630 HOH A O     1 
HETATM 5829 O O     . HOH G 4 .   ? 37.280 5.809   17.584  1.00 33.38 ? 631 HOH A O     1 
HETATM 5830 O O     . HOH G 4 .   ? 29.549 -10.913 12.830  1.00 37.39 ? 632 HOH A O     1 
HETATM 5831 O O     . HOH G 4 .   ? 26.339 -0.121  9.526   1.00 16.89 ? 633 HOH A O     1 
HETATM 5832 O O     . HOH G 4 .   ? 28.336 16.407  -5.478  1.00 37.43 ? 634 HOH A O     1 
HETATM 5833 O O     . HOH G 4 .   ? 11.390 7.895   19.068  1.00 22.06 ? 635 HOH A O     1 
HETATM 5834 O O     . HOH G 4 .   ? 31.857 -4.648  12.922  1.00 28.15 ? 636 HOH A O     1 
HETATM 5835 O O     . HOH G 4 .   ? 21.302 17.653  8.466   1.00 27.58 ? 637 HOH A O     1 
HETATM 5836 O O     . HOH G 4 .   ? 31.007 -10.176 8.248   1.00 30.07 ? 638 HOH A O     1 
HETATM 5837 O O     . HOH G 4 .   ? 12.792 -13.547 -12.996 1.00 20.39 ? 639 HOH A O     1 
HETATM 5838 O O     . HOH G 4 .   ? 7.717  -7.642  -1.177  1.00 17.99 ? 640 HOH A O     1 
HETATM 5839 O O     . HOH G 4 .   ? 27.523 2.641   4.491   1.00 16.76 ? 641 HOH A O     1 
HETATM 5840 O O     . HOH G 4 .   ? 4.975  -7.178  14.370  1.00 19.38 ? 642 HOH A O     1 
HETATM 5841 O O     . HOH G 4 .   ? 0.522  3.394   -11.689 1.00 33.68 ? 643 HOH A O     1 
HETATM 5842 O O     . HOH G 4 .   ? 37.201 20.214  7.792   1.00 20.39 ? 644 HOH A O     1 
HETATM 5843 O O     . HOH G 4 .   ? 22.725 -15.895 22.688  1.00 44.27 ? 645 HOH A O     1 
HETATM 5844 O O     . HOH G 4 .   ? 24.409 -13.521 11.468  1.00 33.10 ? 646 HOH A O     1 
HETATM 5845 O O     . HOH G 4 .   ? 29.419 -15.012 8.999   1.00 41.19 ? 647 HOH A O     1 
HETATM 5846 O O     . HOH G 4 .   ? 43.290 1.551   -8.103  1.00 27.68 ? 648 HOH A O     1 
HETATM 5847 O O     . HOH G 4 .   ? 8.904  14.241  9.788   1.00 20.25 ? 649 HOH A O     1 
HETATM 5848 O O     . HOH G 4 .   ? 8.987  -22.401 0.770   1.00 30.41 ? 650 HOH A O     1 
HETATM 5849 O O     . HOH G 4 .   ? 6.788  -11.872 -5.081  1.00 18.36 ? 651 HOH A O     1 
HETATM 5850 O O     . HOH G 4 .   ? 27.881 -11.410 -11.624 1.00 18.38 ? 652 HOH A O     1 
HETATM 5851 O O     . HOH G 4 .   ? 32.822 -4.793  -6.553  1.00 16.17 ? 653 HOH A O     1 
HETATM 5852 O O     . HOH G 4 .   ? 20.256 -3.847  -19.064 1.00 21.76 ? 654 HOH A O     1 
HETATM 5853 O O     . HOH G 4 .   ? 7.745  -1.392  17.296  1.00 30.29 ? 655 HOH A O     1 
HETATM 5854 O O     . HOH G 4 .   ? -4.064 -11.672 5.757   1.00 46.80 ? 656 HOH A O     1 
HETATM 5855 O O     . HOH G 4 .   ? 5.281  3.163   -16.829 1.00 32.51 ? 657 HOH A O     1 
HETATM 5856 O O     . HOH G 4 .   ? 21.441 19.528  3.431   1.00 32.32 ? 658 HOH A O     1 
HETATM 5857 O O     . HOH G 4 .   ? -2.481 -12.997 2.857   1.00 41.95 ? 659 HOH A O     1 
HETATM 5858 O O     . HOH G 4 .   ? 30.009 -1.823  26.083  1.00 25.26 ? 660 HOH A O     1 
HETATM 5859 O O     . HOH G 4 .   ? 44.122 8.475   7.411   1.00 32.18 ? 661 HOH A O     1 
HETATM 5860 O O     . HOH G 4 .   ? 26.941 4.687   2.531   1.00 15.14 ? 662 HOH A O     1 
HETATM 5861 O O     . HOH G 4 .   ? 9.635  -25.002 -7.548  1.00 28.52 ? 663 HOH A O     1 
HETATM 5862 O O     . HOH G 4 .   ? 15.981 -2.570  -20.766 1.00 25.13 ? 664 HOH A O     1 
HETATM 5863 O O     . HOH G 4 .   ? -0.553 -9.545  -5.438  1.00 30.61 ? 665 HOH A O     1 
HETATM 5864 O O     . HOH G 4 .   ? 32.845 6.778   22.658  1.00 26.30 ? 666 HOH A O     1 
HETATM 5865 O O     . HOH G 4 .   ? 23.337 8.838   -15.843 1.00 24.68 ? 667 HOH A O     1 
HETATM 5866 O O     . HOH G 4 .   ? 29.049 -12.597 -9.073  1.00 28.04 ? 668 HOH A O     1 
HETATM 5867 O O     . HOH G 4 .   ? 27.757 2.025   -6.658  1.00 16.29 ? 669 HOH A O     1 
HETATM 5868 O O     . HOH G 4 .   ? 12.325 3.032   -17.232 1.00 30.72 ? 670 HOH A O     1 
HETATM 5869 O O     . HOH G 4 .   ? 14.145 -14.016 14.987  1.00 29.52 ? 671 HOH A O     1 
HETATM 5870 O O     . HOH G 4 .   ? 4.663  -13.516 -5.054  1.00 18.02 ? 672 HOH A O     1 
HETATM 5871 O O     . HOH G 4 .   ? 25.878 9.070   -14.907 1.00 29.29 ? 673 HOH A O     1 
HETATM 5872 O O     . HOH G 4 .   ? 29.566 9.616   -12.753 1.00 25.77 ? 674 HOH A O     1 
HETATM 5873 O O     . HOH G 4 .   ? 35.809 18.967  -2.805  1.00 34.75 ? 675 HOH A O     1 
HETATM 5874 O O     . HOH G 4 .   ? 25.839 2.808   22.896  1.00 25.86 ? 676 HOH A O     1 
HETATM 5875 O O     . HOH G 4 .   ? 14.182 -16.265 13.601  1.00 26.41 ? 677 HOH A O     1 
HETATM 5876 O O     . HOH G 4 .   ? 32.159 4.228   -14.805 1.00 25.84 ? 678 HOH A O     1 
HETATM 5877 O O     . HOH G 4 .   ? 30.342 -3.239  -18.501 1.00 18.27 ? 679 HOH A O     1 
HETATM 5878 O O     . HOH G 4 .   ? 25.976 19.244  -2.812  1.00 34.49 ? 680 HOH A O     1 
HETATM 5879 O O     . HOH G 4 .   ? 45.601 5.084   -4.930  1.00 26.81 ? 681 HOH A O     1 
HETATM 5880 O O     . HOH G 4 .   ? 20.963 -21.313 -5.183  1.00 31.58 ? 682 HOH A O     1 
HETATM 5881 O O     . HOH G 4 .   ? -2.213 -3.149  6.507   1.00 33.14 ? 683 HOH A O     1 
HETATM 5882 O O     . HOH G 4 .   ? 30.076 9.608   22.651  1.00 28.85 ? 684 HOH A O     1 
HETATM 5883 O O     . HOH G 4 .   ? 34.867 4.746   20.668  1.00 37.67 ? 685 HOH A O     1 
HETATM 5884 O O     . HOH G 4 .   ? 25.320 10.181  23.794  1.00 36.48 ? 686 HOH A O     1 
HETATM 5885 O O     . HOH G 4 .   ? 9.726  -22.413 -10.981 1.00 28.62 ? 687 HOH A O     1 
HETATM 5886 O O     . HOH G 4 .   ? 16.938 -5.802  24.964  1.00 18.26 ? 688 HOH A O     1 
HETATM 5887 O O     . HOH G 4 .   ? 43.256 -1.783  -10.312 1.00 31.31 ? 689 HOH A O     1 
HETATM 5888 O O     . HOH G 4 .   ? 6.881  -8.448  -15.369 1.00 34.69 ? 690 HOH A O     1 
HETATM 5889 O O     . HOH G 4 .   ? 32.025 -22.300 -15.949 1.00 50.47 ? 691 HOH A O     1 
HETATM 5890 O O     . HOH G 4 .   ? 6.106  8.601   19.237  1.00 46.44 ? 692 HOH A O     1 
HETATM 5891 O O     . HOH G 4 .   ? 19.030 15.197  -17.153 1.00 30.68 ? 693 HOH A O     1 
HETATM 5892 O O     . HOH G 4 .   ? 33.379 0.320   23.595  1.00 28.30 ? 694 HOH A O     1 
HETATM 5893 O O     . HOH G 4 .   ? 2.088  -6.337  14.520  1.00 35.18 ? 695 HOH A O     1 
HETATM 5894 O O     . HOH G 4 .   ? 8.967  -7.047  23.434  1.00 40.11 ? 696 HOH A O     1 
HETATM 5895 O O     . HOH G 4 .   ? 19.256 15.532  17.035  1.00 44.63 ? 697 HOH A O     1 
HETATM 5896 O O     . HOH G 4 .   ? 40.974 -10.325 -12.205 1.00 33.54 ? 698 HOH A O     1 
HETATM 5897 O O     . HOH G 4 .   ? 16.761 -12.140 17.098  1.00 35.82 ? 699 HOH A O     1 
HETATM 5898 O O     . HOH G 4 .   ? 10.794 17.022  10.725  1.00 42.85 ? 700 HOH A O     1 
HETATM 5899 O O     . HOH G 4 .   ? 45.719 4.460   -7.779  1.00 40.91 ? 701 HOH A O     1 
HETATM 5900 O O     . HOH G 4 .   ? 9.092  18.428  12.171  1.00 41.39 ? 702 HOH A O     1 
HETATM 5901 O O     . HOH G 4 .   ? 32.020 22.918  -4.700  1.00 46.18 ? 703 HOH A O     1 
HETATM 5902 O O     . HOH G 4 .   ? 7.067  -12.276 -16.485 1.00 38.70 ? 704 HOH A O     1 
HETATM 5903 O O     . HOH G 4 .   ? 36.635 21.089  11.793  1.00 29.68 ? 705 HOH A O     1 
HETATM 5904 O O     . HOH G 4 .   ? 29.176 -6.657  20.136  1.00 36.49 ? 706 HOH A O     1 
HETATM 5905 O O     . HOH G 4 .   ? 29.629 16.686  -2.665  1.00 35.27 ? 707 HOH A O     1 
HETATM 5906 O O     . HOH G 4 .   ? 28.161 6.453   -18.326 1.00 41.70 ? 708 HOH A O     1 
HETATM 5907 O O     . HOH G 4 .   ? 35.294 13.886  -5.721  1.00 33.18 ? 709 HOH A O     1 
HETATM 5908 O O     . HOH G 4 .   ? 14.167 2.046   -21.395 1.00 36.27 ? 710 HOH A O     1 
HETATM 5909 O O     . HOH G 4 .   ? -3.242 -17.880 8.898   1.00 48.46 ? 711 HOH A O     1 
HETATM 5910 O O     . HOH G 4 .   ? 19.642 17.166  -14.583 1.00 31.64 ? 712 HOH A O     1 
HETATM 5911 O O     . HOH G 4 .   ? 40.702 14.710  10.803  1.00 33.46 ? 713 HOH A O     1 
HETATM 5912 O O     . HOH G 4 .   ? 21.237 13.990  -17.760 1.00 39.45 ? 714 HOH A O     1 
HETATM 5913 O O     . HOH G 4 .   ? 26.305 -0.006  12.132  1.00 29.85 ? 715 HOH A O     1 
HETATM 5914 O O     . HOH G 4 .   ? 35.616 9.923   -16.777 1.00 40.65 ? 716 HOH A O     1 
HETATM 5915 O O     . HOH G 4 .   ? 9.444  -26.738 5.080   1.00 43.33 ? 717 HOH A O     1 
HETATM 5916 O O     . HOH G 4 .   ? 21.009 17.055  16.946  1.00 42.90 ? 718 HOH A O     1 
HETATM 5917 O O     . HOH G 4 .   ? 5.150  1.449   14.389  1.00 38.51 ? 719 HOH A O     1 
HETATM 5918 O O     . HOH G 4 .   ? 14.774 20.223  3.745   1.00 30.78 ? 720 HOH A O     1 
HETATM 5919 O O     . HOH G 4 .   ? 20.914 19.067  15.610  1.00 47.69 ? 721 HOH A O     1 
HETATM 5920 O O     . HOH G 4 .   ? 8.401  -19.087 22.709  1.00 43.32 ? 722 HOH A O     1 
HETATM 5921 O O     . HOH G 4 .   ? -3.897 -13.401 8.412   1.00 45.82 ? 723 HOH A O     1 
HETATM 5922 O O     . HOH G 4 .   ? 37.325 7.665   21.367  1.00 43.60 ? 724 HOH A O     1 
HETATM 5923 O O     . HOH G 4 .   ? -1.212 3.053   -9.766  1.00 36.62 ? 725 HOH A O     1 
HETATM 5924 O O     . HOH G 4 .   ? 7.698  2.311   19.609  1.00 36.62 ? 726 HOH A O     1 
HETATM 5925 O O     . HOH G 4 .   ? 5.136  -20.149 -15.076 1.00 41.83 ? 727 HOH A O     1 
HETATM 5926 O O     . HOH G 4 .   ? 15.879 10.607  24.292  1.00 45.01 ? 728 HOH A O     1 
HETATM 5927 O O     . HOH G 4 .   ? 46.245 -0.524  -0.878  1.00 43.50 ? 729 HOH A O     1 
HETATM 5928 O O     . HOH G 4 .   ? 28.340 4.211   -16.903 1.00 32.70 ? 730 HOH A O     1 
HETATM 5929 O O     . HOH G 4 .   ? 25.942 19.489  -7.168  1.00 41.02 ? 731 HOH A O     1 
HETATM 5930 O O     . HOH G 4 .   ? 32.247 1.912   21.962  1.00 35.77 ? 732 HOH A O     1 
HETATM 5931 O O     . HOH G 4 .   ? 2.169  1.206   -15.527 1.00 35.63 ? 733 HOH A O     1 
HETATM 5932 O O     . HOH G 4 .   ? 23.421 23.191  -1.604  1.00 42.65 ? 734 HOH A O     1 
HETATM 5933 O O     . HOH G 4 .   ? 33.039 15.469  -5.164  1.00 36.61 ? 735 HOH A O     1 
HETATM 5934 O O     . HOH G 4 .   ? 7.470  17.281  3.682   1.00 39.26 ? 736 HOH A O     1 
HETATM 5935 O O     . HOH G 4 .   ? 14.750 13.052  23.528  1.00 48.96 ? 737 HOH A O     1 
HETATM 5936 O O     . HOH G 4 .   ? 19.558 19.123  7.461   1.00 33.07 ? 738 HOH A O     1 
HETATM 5937 O O     . HOH G 4 .   ? 0.510  -5.294  -16.988 1.00 40.74 ? 739 HOH A O     1 
HETATM 5938 O O     . HOH G 4 .   ? 8.560  -24.278 -9.908  1.00 32.97 ? 740 HOH A O     1 
HETATM 5939 O O     . HOH G 4 .   ? 5.240  -9.725  -14.027 1.00 36.96 ? 741 HOH A O     1 
HETATM 5940 O O     . HOH G 4 .   ? 5.977  -23.807 -14.516 1.00 45.59 ? 742 HOH A O     1 
HETATM 5941 O O     . HOH G 4 .   ? 3.206  -2.311  -17.987 1.00 33.42 ? 743 HOH A O     1 
HETATM 5942 O O     . HOH G 4 .   ? -2.705 -2.878  9.223   1.00 39.87 ? 744 HOH A O     1 
HETATM 5943 O O     . HOH G 4 .   ? 24.017 4.676   -25.413 1.00 33.02 ? 745 HOH A O     1 
HETATM 5944 O O     . HOH G 4 .   ? 26.848 -14.561 11.934  1.00 40.59 ? 746 HOH A O     1 
HETATM 5945 O O     . HOH G 4 .   ? 39.020 7.076   19.761  1.00 40.71 ? 747 HOH A O     1 
HETATM 5946 O O     . HOH G 4 .   ? 42.017 16.335  0.543   1.00 40.18 ? 748 HOH A O     1 
HETATM 5947 O O     . HOH G 4 .   ? 23.447 -15.319 12.087  1.00 43.97 ? 749 HOH A O     1 
HETATM 5948 O O     . HOH G 4 .   ? 31.137 -7.033  22.183  1.00 45.52 ? 750 HOH A O     1 
HETATM 5949 O O     . HOH G 4 .   ? 24.279 -17.925 23.475  1.00 44.84 ? 751 HOH A O     1 
HETATM 5950 O O     . HOH G 4 .   ? 4.429  7.499   11.198  1.00 37.11 ? 752 HOH A O     1 
HETATM 5951 O O     . HOH G 4 .   ? 7.127  16.855  6.015   1.00 43.13 ? 753 HOH A O     1 
HETATM 5952 O O     . HOH G 4 .   ? 29.949 24.230  -5.511  1.00 49.79 ? 754 HOH A O     1 
HETATM 5953 O O     . HOH G 4 .   ? 30.782 11.842  23.885  1.00 30.10 ? 755 HOH A O     1 
HETATM 5954 O O     . HOH G 4 .   ? 10.611 1.612   -17.948 1.00 36.08 ? 756 HOH A O     1 
HETATM 5955 O O     . HOH G 4 .   ? -0.299 0.800   -1.145  1.00 41.65 ? 757 HOH A O     1 
HETATM 5956 O O     . HOH G 4 .   ? 4.591  -27.126 -3.346  1.00 40.83 ? 758 HOH A O     1 
HETATM 5957 O O     . HOH G 4 .   ? 42.691 -3.457  -12.477 1.00 35.20 ? 759 HOH A O     1 
HETATM 5958 O O     . HOH G 4 .   ? 29.056 15.299  21.322  1.00 39.91 ? 760 HOH A O     1 
HETATM 5959 O O     . HOH G 4 .   ? 30.862 -7.329  -3.597  1.00 25.23 ? 761 HOH A O     1 
HETATM 5960 O O     . HOH G 4 .   ? 11.249 -22.503 1.874   1.00 24.76 ? 762 HOH A O     1 
HETATM 5961 O O     . HOH G 4 .   ? 16.655 -16.025 13.561  1.00 31.76 ? 763 HOH A O     1 
HETATM 5962 O O     . HOH G 4 .   ? 7.950  -15.262 -16.801 1.00 42.69 ? 764 HOH A O     1 
HETATM 5963 O O     . HOH G 4 .   ? 31.907 -7.446  -6.089  1.00 25.68 ? 765 HOH A O     1 
HETATM 5964 O O     . HOH G 4 .   ? 1.334  -1.080  -15.657 1.00 36.79 ? 766 HOH A O     1 
HETATM 5965 O O     . HOH G 4 .   ? 30.247 -10.167 -12.633 1.00 25.37 ? 767 HOH A O     1 
HETATM 5966 O O     . HOH G 4 .   ? 5.431  -26.253 -6.376  1.00 42.41 ? 768 HOH A O     1 
HETATM 5967 O O     . HOH G 4 .   ? 19.445 19.387  17.319  1.00 50.62 ? 769 HOH A O     1 
HETATM 5968 O O     . HOH G 4 .   ? 10.757 -23.619 -13.105 1.00 43.87 ? 770 HOH A O     1 
HETATM 5969 O O     . HOH G 4 .   ? 2.527  -14.958 -8.811  1.00 34.98 ? 771 HOH A O     1 
HETATM 5970 O O     . HOH G 4 .   ? 23.905 19.214  7.539   1.00 36.13 ? 772 HOH A O     1 
HETATM 5971 O O     . HOH G 4 .   ? 40.101 19.511  11.185  1.00 34.25 ? 773 HOH A O     1 
HETATM 5972 O O     . HOH G 4 .   ? 27.462 10.719  -13.622 1.00 30.57 ? 774 HOH A O     1 
HETATM 5973 O O     . HOH G 4 .   ? -5.108 -2.481  -12.929 1.00 39.98 ? 775 HOH A O     1 
HETATM 5974 O O     . HOH G 4 .   ? 31.358 1.520   -15.355 1.00 22.20 ? 776 HOH A O     1 
HETATM 5975 O O     . HOH G 4 .   ? 16.307 -5.871  27.578  1.00 22.82 ? 777 HOH A O     1 
HETATM 5976 O O     . HOH G 4 .   ? 34.260 24.078  -2.603  1.00 28.40 ? 778 HOH A O     1 
HETATM 5977 O O     . HOH G 4 .   ? 32.883 4.100   22.879  1.00 32.46 ? 779 HOH A O     1 
HETATM 5978 O O     . HOH G 4 .   ? 14.529 -23.053 11.395  1.00 36.72 ? 780 HOH A O     1 
HETATM 5979 O O     . HOH G 4 .   ? -0.515 5.236   -2.107  1.00 37.84 ? 781 HOH A O     1 
HETATM 5980 O O     . HOH G 4 .   ? 3.043  -13.012 -7.301  1.00 34.42 ? 782 HOH A O     1 
HETATM 5981 O O     . HOH G 4 .   ? 8.365  -22.808 -16.395 1.00 41.31 ? 783 HOH A O     1 
HETATM 5982 O O     . HOH G 4 .   ? 11.906 -10.942 -22.695 1.00 46.41 ? 784 HOH A O     1 
HETATM 5983 O O     . HOH G 4 .   ? 37.482 15.794  -16.965 1.00 40.65 ? 785 HOH A O     1 
HETATM 5984 O O     . HOH G 4 .   ? 20.507 15.637  20.910  1.00 46.93 ? 786 HOH A O     1 
HETATM 5985 O O     . HOH G 4 .   ? 34.345 10.834  24.894  1.00 38.66 ? 787 HOH A O     1 
HETATM 5986 O O     . HOH G 4 .   ? 8.622  17.028  -2.447  1.00 29.46 ? 788 HOH A O     1 
HETATM 5987 O O     . HOH G 4 .   ? 10.285 -12.960 -22.347 1.00 48.37 ? 789 HOH A O     1 
HETATM 5988 O O     . HOH G 4 .   ? 20.464 -17.671 -22.188 1.00 40.45 ? 790 HOH A O     1 
HETATM 5989 O O     . HOH G 4 .   ? 44.371 15.177  -0.918  1.00 45.55 ? 791 HOH A O     1 
HETATM 5990 O O     . HOH G 4 .   ? 2.652  -16.840 -12.844 1.00 45.54 ? 792 HOH A O     1 
HETATM 5991 O O     . HOH G 4 .   ? 40.196 15.302  -17.455 1.00 46.42 ? 793 HOH A O     1 
HETATM 5992 O O     . HOH G 4 .   ? 28.045 13.228  24.082  1.00 40.86 ? 794 HOH A O     1 
HETATM 5993 O O     . HOH G 4 .   ? 5.360  -1.658  -19.328 1.00 42.92 ? 795 HOH A O     1 
HETATM 5994 O O     . HOH H 4 .   ? 31.941 12.056  26.828  1.00 26.00 ? 501 HOH B O     1 
HETATM 5995 O O     . HOH H 4 .   ? 27.494 8.646   22.534  1.00 37.58 ? 502 HOH B O     1 
HETATM 5996 O O     . HOH H 4 .   ? 10.749 -0.511  49.504  1.00 32.41 ? 503 HOH B O     1 
HETATM 5997 O O     . HOH H 4 .   ? -4.372 -8.980  38.890  1.00 40.11 ? 504 HOH B O     1 
HETATM 5998 O O     . HOH H 4 .   ? 20.511 7.941   62.953  1.00 32.46 ? 505 HOH B O     1 
HETATM 5999 O O     . HOH H 4 .   ? 29.250 13.735  28.786  1.00 36.53 ? 506 HOH B O     1 
HETATM 6000 O O     . HOH H 4 .   ? 34.782 -15.227 28.597  1.00 38.00 ? 507 HOH B O     1 
HETATM 6001 O O     . HOH H 4 .   ? 16.215 3.663   69.527  1.00 28.15 ? 508 HOH B O     1 
HETATM 6002 O O     . HOH H 4 .   ? 17.144 6.270   49.056  1.00 21.98 ? 509 HOH B O     1 
HETATM 6003 O O     . HOH H 4 .   ? 18.052 -11.089 29.984  1.00 27.97 ? 510 HOH B O     1 
HETATM 6004 O O     . HOH H 4 .   ? 25.421 4.064   71.809  1.00 46.62 ? 511 HOH B O     1 
HETATM 6005 O O     . HOH H 4 .   ? 43.614 -0.793  38.232  1.00 26.14 ? 512 HOH B O     1 
HETATM 6006 O O     . HOH H 4 .   ? 5.564  -26.285 51.792  1.00 32.02 ? 513 HOH B O     1 
HETATM 6007 O O     . HOH H 4 .   ? 41.476 13.154  58.080  1.00 41.29 ? 514 HOH B O     1 
HETATM 6008 O O     . HOH H 4 .   ? 26.478 9.107   70.434  1.00 40.40 ? 515 HOH B O     1 
HETATM 6009 O O     . HOH H 4 .   ? 35.972 7.391   29.893  1.00 35.12 ? 516 HOH B O     1 
HETATM 6010 O O     . HOH H 4 .   ? 38.769 -11.714 48.934  1.00 33.87 ? 517 HOH B O     1 
HETATM 6011 O O     . HOH H 4 .   ? 1.117  -11.624 33.855  1.00 28.37 ? 518 HOH B O     1 
HETATM 6012 O O     . HOH H 4 .   ? 24.440 -23.082 51.484  1.00 32.26 ? 519 HOH B O     1 
HETATM 6013 O O     . HOH H 4 .   ? 11.313 -0.899  38.102  1.00 20.96 ? 520 HOH B O     1 
HETATM 6014 O O     . HOH H 4 .   ? 28.826 7.624   36.267  1.00 16.56 ? 521 HOH B O     1 
HETATM 6015 O O     . HOH H 4 .   ? 20.574 15.259  52.741  1.00 41.70 ? 522 HOH B O     1 
HETATM 6016 O O     . HOH H 4 .   ? 23.432 5.397   49.688  1.00 18.66 ? 523 HOH B O     1 
HETATM 6017 O O     . HOH H 4 .   ? 15.586 -16.834 40.195  1.00 23.57 ? 524 HOH B O     1 
HETATM 6018 O O     . HOH H 4 .   ? 11.740 -9.937  25.583  1.00 31.89 ? 525 HOH B O     1 
HETATM 6019 O O     . HOH H 4 .   ? 13.241 -16.645 39.456  1.00 18.76 ? 526 HOH B O     1 
HETATM 6020 O O     . HOH H 4 .   ? 2.294  -2.285  49.862  1.00 34.47 ? 527 HOH B O     1 
HETATM 6021 O O     . HOH H 4 .   ? 25.062 -3.557  68.485  1.00 31.22 ? 528 HOH B O     1 
HETATM 6022 O O     . HOH H 4 .   ? 14.034 2.505   55.483  1.00 30.58 ? 529 HOH B O     1 
HETATM 6023 O O     . HOH H 4 .   ? 21.226 8.894   60.444  1.00 32.51 ? 530 HOH B O     1 
HETATM 6024 O O     . HOH H 4 .   ? 0.008  -17.449 40.616  1.00 34.16 ? 531 HOH B O     1 
HETATM 6025 O O     . HOH H 4 .   ? 3.788  -17.446 62.947  1.00 28.93 ? 532 HOH B O     1 
HETATM 6026 O O     . HOH H 4 .   ? 5.628  -22.140 42.039  1.00 21.91 ? 533 HOH B O     1 
HETATM 6027 O O     . HOH H 4 .   ? 33.174 -4.844  26.537  1.00 34.00 ? 534 HOH B O     1 
HETATM 6028 O O     . HOH H 4 .   ? 2.549  -5.596  31.265  1.00 25.98 ? 535 HOH B O     1 
HETATM 6029 O O     . HOH H 4 .   ? 18.019 -9.865  45.705  1.00 16.71 ? 536 HOH B O     1 
HETATM 6030 O O     . HOH H 4 .   ? 20.665 -19.317 38.837  1.00 32.79 ? 537 HOH B O     1 
HETATM 6031 O O     . HOH H 4 .   ? 0.550  -2.298  36.814  1.00 20.45 ? 538 HOH B O     1 
HETATM 6032 O O     . HOH H 4 .   ? 15.567 6.053   58.534  1.00 19.92 ? 539 HOH B O     1 
HETATM 6033 O O     . HOH H 4 .   ? 23.997 12.662  48.858  1.00 31.59 ? 540 HOH B O     1 
HETATM 6034 O O     . HOH H 4 .   ? 23.379 -2.268  35.829  1.00 19.01 ? 541 HOH B O     1 
HETATM 6035 O O     . HOH H 4 .   ? 16.985 -0.714  69.160  1.00 19.79 ? 542 HOH B O     1 
HETATM 6036 O O     . HOH H 4 .   ? 27.303 3.076   68.796  1.00 36.35 ? 543 HOH B O     1 
HETATM 6037 O O     . HOH H 4 .   ? 26.414 -1.119  34.147  1.00 20.67 ? 544 HOH B O     1 
HETATM 6038 O O     . HOH H 4 .   ? 32.960 -16.148 58.625  1.00 32.40 ? 545 HOH B O     1 
HETATM 6039 O O     . HOH H 4 .   ? 11.718 -19.067 39.472  1.00 33.13 ? 546 HOH B O     1 
HETATM 6040 O O     . HOH H 4 .   ? 28.479 -7.404  60.916  1.00 19.56 ? 547 HOH B O     1 
HETATM 6041 O O     . HOH H 4 .   ? 9.444  5.890   50.292  1.00 29.65 ? 548 HOH B O     1 
HETATM 6042 O O     . HOH H 4 .   ? 12.710 0.538   40.178  1.00 23.12 ? 549 HOH B O     1 
HETATM 6043 O O     . HOH H 4 .   ? 19.647 1.494   24.318  1.00 25.18 ? 550 HOH B O     1 
HETATM 6044 O O     . HOH H 4 .   ? 13.508 -1.176  34.024  1.00 18.20 ? 551 HOH B O     1 
HETATM 6045 O O     . HOH H 4 .   ? 28.927 17.033  36.300  1.00 23.19 ? 552 HOH B O     1 
HETATM 6046 O O     . HOH H 4 .   ? 27.198 1.472   39.916  1.00 20.55 ? 553 HOH B O     1 
HETATM 6047 O O     . HOH H 4 .   ? 14.810 -11.735 33.907  1.00 20.45 ? 554 HOH B O     1 
HETATM 6048 O O     . HOH H 4 .   ? 32.077 -6.565  59.792  1.00 21.65 ? 555 HOH B O     1 
HETATM 6049 O O     . HOH H 4 .   ? 23.028 -2.396  71.512  1.00 25.71 ? 556 HOH B O     1 
HETATM 6050 O O     . HOH H 4 .   ? 6.700  5.132   37.429  1.00 28.80 ? 557 HOH B O     1 
HETATM 6051 O O     . HOH H 4 .   ? 22.079 -3.396  37.882  1.00 16.86 ? 558 HOH B O     1 
HETATM 6052 O O     . HOH H 4 .   ? 13.455 -4.054  52.945  1.00 17.28 ? 559 HOH B O     1 
HETATM 6053 O O     . HOH H 4 .   ? 26.511 0.974   24.348  1.00 28.12 ? 560 HOH B O     1 
HETATM 6054 O O     . HOH H 4 .   ? 24.585 7.587   28.076  1.00 25.01 ? 561 HOH B O     1 
HETATM 6055 O O     . HOH H 4 .   ? 33.393 9.393   35.731  1.00 25.27 ? 562 HOH B O     1 
HETATM 6056 O O     . HOH H 4 .   ? 33.705 -9.552  57.287  1.00 33.61 ? 563 HOH B O     1 
HETATM 6057 O O     . HOH H 4 .   ? 9.615  -15.521 35.306  1.00 32.87 ? 564 HOH B O     1 
HETATM 6058 O O     . HOH H 4 .   ? 24.875 -12.025 66.672  1.00 24.73 ? 565 HOH B O     1 
HETATM 6059 O O     . HOH H 4 .   ? 30.588 4.898   64.565  1.00 22.01 ? 566 HOH B O     1 
HETATM 6060 O O     . HOH H 4 .   ? 22.794 -24.137 56.285  1.00 43.84 ? 567 HOH B O     1 
HETATM 6061 O O     . HOH H 4 .   ? 8.473  2.261   38.493  1.00 21.96 ? 568 HOH B O     1 
HETATM 6062 O O     . HOH H 4 .   ? 11.955 -30.097 39.599  1.00 28.95 ? 569 HOH B O     1 
HETATM 6063 O O     . HOH H 4 .   ? 27.833 0.277   36.870  1.00 22.97 ? 570 HOH B O     1 
HETATM 6064 O O     . HOH H 4 .   ? 26.069 -15.306 29.733  1.00 32.57 ? 571 HOH B O     1 
HETATM 6065 O O     . HOH H 4 .   ? 10.444 -12.208 38.362  1.00 19.66 ? 572 HOH B O     1 
HETATM 6066 O O     . HOH H 4 .   ? 27.581 0.605   42.597  1.00 18.31 ? 573 HOH B O     1 
HETATM 6067 O O     . HOH H 4 .   ? 24.711 9.967   34.556  1.00 20.31 ? 574 HOH B O     1 
HETATM 6068 O O     . HOH H 4 .   ? 0.167  -2.912  44.176  1.00 29.89 ? 575 HOH B O     1 
HETATM 6069 O O     . HOH H 4 .   ? 11.707 -12.425 53.555  1.00 17.64 ? 576 HOH B O     1 
HETATM 6070 O O     . HOH H 4 .   ? 41.678 -10.026 42.027  1.00 32.01 ? 577 HOH B O     1 
HETATM 6071 O O     . HOH H 4 .   ? 5.570  6.074   47.300  1.00 44.52 ? 578 HOH B O     1 
HETATM 6072 O O     . HOH H 4 .   ? 25.066 10.631  47.211  1.00 18.28 ? 579 HOH B O     1 
HETATM 6073 O O     . HOH H 4 .   ? 16.313 -20.330 37.977  1.00 32.76 ? 580 HOH B O     1 
HETATM 6074 O O     . HOH H 4 .   ? 29.069 21.603  44.496  1.00 20.00 ? 581 HOH B O     1 
HETATM 6075 O O     . HOH H 4 .   ? 3.741  2.606   56.595  1.00 38.58 ? 582 HOH B O     1 
HETATM 6076 O O     . HOH H 4 .   ? 27.982 -0.430  27.658  1.00 20.92 ? 583 HOH B O     1 
HETATM 6077 O O     . HOH H 4 .   ? 35.007 2.344   52.368  1.00 21.44 ? 584 HOH B O     1 
HETATM 6078 O O     . HOH H 4 .   ? 34.563 3.380   48.503  1.00 18.36 ? 585 HOH B O     1 
HETATM 6079 O O     . HOH H 4 .   ? 36.816 -14.515 45.889  1.00 26.63 ? 586 HOH B O     1 
HETATM 6080 O O     . HOH H 4 .   ? 32.424 2.814   64.054  1.00 24.71 ? 587 HOH B O     1 
HETATM 6081 O O     . HOH H 4 .   ? 17.476 -1.052  43.884  1.00 18.98 ? 588 HOH B O     1 
HETATM 6082 O O     . HOH H 4 .   ? 24.160 12.022  60.605  1.00 29.07 ? 589 HOH B O     1 
HETATM 6083 O O     . HOH H 4 .   ? 36.625 3.774   46.940  1.00 20.64 ? 590 HOH B O     1 
HETATM 6084 O O     . HOH H 4 .   ? 24.098 18.137  55.387  1.00 30.58 ? 591 HOH B O     1 
HETATM 6085 O O     . HOH H 4 .   ? 32.787 17.988  49.795  1.00 28.31 ? 592 HOH B O     1 
HETATM 6086 O O     . HOH H 4 .   ? 28.597 -2.605  66.074  1.00 28.77 ? 593 HOH B O     1 
HETATM 6087 O O     . HOH H 4 .   ? -0.410 -9.377  33.514  1.00 33.01 ? 594 HOH B O     1 
HETATM 6088 O O     . HOH H 4 .   ? 17.240 -24.214 48.710  1.00 23.69 ? 595 HOH B O     1 
HETATM 6089 O O     . HOH H 4 .   ? 24.657 -20.789 37.860  1.00 31.68 ? 596 HOH B O     1 
HETATM 6090 O O     . HOH H 4 .   ? 3.970  -6.415  38.944  1.00 20.34 ? 597 HOH B O     1 
HETATM 6091 O O     . HOH H 4 .   ? 6.856  -4.418  44.464  1.00 19.67 ? 598 HOH B O     1 
HETATM 6092 O O     . HOH H 4 .   ? 28.254 16.901  51.086  1.00 25.59 ? 599 HOH B O     1 
HETATM 6093 O O     . HOH H 4 .   ? 2.553  -23.397 50.185  1.00 31.57 ? 600 HOH B O     1 
HETATM 6094 O O     . HOH H 4 .   ? 17.874 3.835   48.647  1.00 18.35 ? 601 HOH B O     1 
HETATM 6095 O O     . HOH H 4 .   ? 0.933  -2.423  55.257  1.00 35.63 ? 602 HOH B O     1 
HETATM 6096 O O     . HOH H 4 .   ? 25.003 -2.177  64.501  1.00 16.47 ? 603 HOH B O     1 
HETATM 6097 O O     . HOH H 4 .   ? 17.361 3.714   29.570  1.00 30.26 ? 604 HOH B O     1 
HETATM 6098 O O     . HOH H 4 .   ? 18.184 -8.426  38.486  1.00 21.19 ? 605 HOH B O     1 
HETATM 6099 O O     . HOH H 4 .   ? 29.336 17.022  60.648  1.00 33.28 ? 606 HOH B O     1 
HETATM 6100 O O     . HOH H 4 .   ? 43.614 -2.691  50.586  1.00 36.70 ? 607 HOH B O     1 
HETATM 6101 O O     . HOH H 4 .   ? 12.341 -3.204  37.564  1.00 17.98 ? 608 HOH B O     1 
HETATM 6102 O O     . HOH H 4 .   ? 33.186 -20.522 44.481  1.00 26.06 ? 609 HOH B O     1 
HETATM 6103 O O     . HOH H 4 .   ? 37.539 -1.458  63.336  1.00 29.82 ? 610 HOH B O     1 
HETATM 6104 O O     . HOH H 4 .   ? 2.160  -0.435  35.719  1.00 22.57 ? 611 HOH B O     1 
HETATM 6105 O O     . HOH H 4 .   ? 6.268  -17.402 34.880  1.00 29.21 ? 612 HOH B O     1 
HETATM 6106 O O     . HOH H 4 .   ? 18.507 9.394   59.072  1.00 30.57 ? 613 HOH B O     1 
HETATM 6107 O O     . HOH H 4 .   ? 23.516 8.375   51.140  1.00 17.32 ? 614 HOH B O     1 
HETATM 6108 O O     . HOH H 4 .   ? 18.571 -21.754 53.523  1.00 24.09 ? 615 HOH B O     1 
HETATM 6109 O O     . HOH H 4 .   ? 17.722 -7.570  31.347  1.00 19.94 ? 616 HOH B O     1 
HETATM 6110 O O     . HOH H 4 .   ? 10.534 -11.935 26.290  1.00 32.41 ? 617 HOH B O     1 
HETATM 6111 O O     . HOH H 4 .   ? 8.987  -14.950 53.909  1.00 18.79 ? 618 HOH B O     1 
HETATM 6112 O O     . HOH H 4 .   ? 23.310 9.842   61.938  1.00 29.54 ? 619 HOH B O     1 
HETATM 6113 O O     . HOH H 4 .   ? 18.550 7.237   32.369  1.00 22.29 ? 620 HOH B O     1 
HETATM 6114 O O     . HOH H 4 .   ? 15.095 -8.818  46.178  1.00 17.78 ? 621 HOH B O     1 
HETATM 6115 O O     . HOH H 4 .   ? 13.825 -6.764  47.798  1.00 17.79 ? 622 HOH B O     1 
HETATM 6116 O O     . HOH H 4 .   ? 3.749  -24.462 48.030  1.00 23.51 ? 623 HOH B O     1 
HETATM 6117 O O     . HOH H 4 .   ? 32.201 -10.318 59.827  1.00 32.96 ? 624 HOH B O     1 
HETATM 6118 O O     . HOH H 4 .   ? 15.332 -8.441  28.013  1.00 23.72 ? 625 HOH B O     1 
HETATM 6119 O O     . HOH H 4 .   ? 30.710 -20.376 28.548  1.00 40.25 ? 626 HOH B O     1 
HETATM 6120 O O     . HOH H 4 .   ? 7.275  0.526   54.522  1.00 24.42 ? 627 HOH B O     1 
HETATM 6121 O O     . HOH H 4 .   ? 32.242 -17.115 25.894  1.00 42.16 ? 628 HOH B O     1 
HETATM 6122 O O     . HOH H 4 .   ? 25.519 12.818  31.073  1.00 33.43 ? 629 HOH B O     1 
HETATM 6123 O O     . HOH H 4 .   ? 12.232 0.750   35.698  1.00 17.09 ? 630 HOH B O     1 
HETATM 6124 O O     . HOH H 4 .   ? 20.137 -23.807 48.634  1.00 34.10 ? 631 HOH B O     1 
HETATM 6125 O O     . HOH H 4 .   ? 18.259 -0.980  25.114  1.00 18.80 ? 632 HOH B O     1 
HETATM 6126 O O     . HOH H 4 .   ? 4.853  -2.452  67.622  1.00 21.98 ? 633 HOH B O     1 
HETATM 6127 O O     . HOH H 4 .   ? 16.112 -9.473  30.728  1.00 24.06 ? 634 HOH B O     1 
HETATM 6128 O O     . HOH H 4 .   ? 36.694 7.564   44.969  1.00 21.06 ? 635 HOH B O     1 
HETATM 6129 O O     . HOH H 4 .   ? 4.349  -7.950  30.470  1.00 25.29 ? 636 HOH B O     1 
HETATM 6130 O O     . HOH H 4 .   ? -3.882 -7.955  49.268  1.00 49.07 ? 637 HOH B O     1 
HETATM 6131 O O     . HOH H 4 .   ? 32.630 -1.681  27.250  1.00 22.17 ? 638 HOH B O     1 
HETATM 6132 O O     . HOH H 4 .   ? 30.032 -18.596 58.390  1.00 29.29 ? 639 HOH B O     1 
HETATM 6133 O O     . HOH H 4 .   ? 38.503 9.275   45.718  1.00 21.86 ? 640 HOH B O     1 
HETATM 6134 O O     . HOH H 4 .   ? 24.271 -13.044 29.630  1.00 28.50 ? 641 HOH B O     1 
HETATM 6135 O O     . HOH H 4 .   ? 5.926  -13.786 64.294  1.00 32.32 ? 642 HOH B O     1 
HETATM 6136 O O     . HOH H 4 .   ? 21.127 -13.340 29.750  1.00 32.79 ? 643 HOH B O     1 
HETATM 6137 O O     . HOH H 4 .   ? 17.053 -13.780 30.628  1.00 29.14 ? 644 HOH B O     1 
HETATM 6138 O O     . HOH H 4 .   ? 17.364 -16.523 62.027  1.00 28.43 ? 645 HOH B O     1 
HETATM 6139 O O     . HOH H 4 .   ? 17.121 -6.165  37.096  1.00 18.45 ? 646 HOH B O     1 
HETATM 6140 O O     . HOH H 4 .   ? 18.600 -6.761  28.880  1.00 20.37 ? 647 HOH B O     1 
HETATM 6141 O O     . HOH H 4 .   ? 27.301 -20.747 36.565  1.00 37.22 ? 648 HOH B O     1 
HETATM 6142 O O     . HOH H 4 .   ? 23.108 17.116  40.577  1.00 28.83 ? 649 HOH B O     1 
HETATM 6143 O O     . HOH H 4 .   ? 7.903  2.473   62.340  1.00 33.33 ? 650 HOH B O     1 
HETATM 6144 O O     . HOH H 4 .   ? 16.487 8.494   34.598  1.00 27.27 ? 651 HOH B O     1 
HETATM 6145 O O     . HOH H 4 .   ? 15.478 -27.840 41.761  1.00 42.19 ? 652 HOH B O     1 
HETATM 6146 O O     . HOH H 4 .   ? 3.539  -2.398  28.742  1.00 27.12 ? 653 HOH B O     1 
HETATM 6147 O O     . HOH H 4 .   ? 17.731 1.629   70.483  1.00 16.19 ? 654 HOH B O     1 
HETATM 6148 O O     . HOH H 4 .   ? 44.671 -7.500  40.837  1.00 38.29 ? 655 HOH B O     1 
HETATM 6149 O O     . HOH H 4 .   ? 26.260 -24.675 50.585  1.00 36.63 ? 656 HOH B O     1 
HETATM 6150 O O     . HOH H 4 .   ? 35.590 18.186  38.484  1.00 34.19 ? 657 HOH B O     1 
HETATM 6151 O O     . HOH H 4 .   ? 2.955  -11.068 63.346  1.00 30.39 ? 658 HOH B O     1 
HETATM 6152 O O     . HOH H 4 .   ? 6.667  6.254   27.681  1.00 32.06 ? 659 HOH B O     1 
HETATM 6153 O O     . HOH H 4 .   ? 28.398 -19.477 30.022  1.00 33.14 ? 660 HOH B O     1 
HETATM 6154 O O     . HOH H 4 .   ? 3.972  -17.360 33.333  1.00 43.24 ? 661 HOH B O     1 
HETATM 6155 O O     . HOH H 4 .   ? 27.747 -8.078  24.867  1.00 37.41 ? 662 HOH B O     1 
HETATM 6156 O O     . HOH H 4 .   ? 27.689 -4.203  67.348  1.00 35.39 ? 663 HOH B O     1 
HETATM 6157 O O     . HOH H 4 .   ? -1.219 -5.791  35.525  1.00 42.07 ? 664 HOH B O     1 
HETATM 6158 O O     . HOH H 4 .   ? 1.838  -9.204  60.816  1.00 41.30 ? 665 HOH B O     1 
HETATM 6159 O O     . HOH H 4 .   ? 10.390 10.633  51.897  1.00 42.96 ? 666 HOH B O     1 
HETATM 6160 O O     . HOH H 4 .   ? 18.865 14.958  50.930  1.00 42.70 ? 667 HOH B O     1 
HETATM 6161 O O     . HOH H 4 .   ? 40.555 16.655  60.787  1.00 48.02 ? 668 HOH B O     1 
HETATM 6162 O O     . HOH H 4 .   ? 34.903 2.084   65.065  1.00 35.98 ? 669 HOH B O     1 
HETATM 6163 O O     . HOH H 4 .   ? 19.368 12.746  55.105  1.00 35.82 ? 670 HOH B O     1 
HETATM 6164 O O     . HOH H 4 .   ? 10.753 -13.198 69.340  1.00 29.63 ? 671 HOH B O     1 
HETATM 6165 O O     . HOH H 4 .   ? 22.894 -19.119 39.700  1.00 34.20 ? 672 HOH B O     1 
HETATM 6166 O O     . HOH H 4 .   ? 10.542 3.618   39.513  1.00 34.99 ? 673 HOH B O     1 
HETATM 6167 O O     . HOH H 4 .   ? 39.881 8.139   34.425  1.00 38.70 ? 674 HOH B O     1 
HETATM 6168 O O     . HOH H 4 .   ? 42.581 9.629   60.722  1.00 46.40 ? 675 HOH B O     1 
HETATM 6169 O O     . HOH H 4 .   ? 35.990 5.223   28.600  1.00 39.69 ? 676 HOH B O     1 
HETATM 6170 O O     . HOH H 4 .   ? 19.713 -8.396  27.100  1.00 31.42 ? 677 HOH B O     1 
HETATM 6171 O O     . HOH H 4 .   ? 32.466 -8.498  61.343  1.00 37.32 ? 678 HOH B O     1 
HETATM 6172 O O     . HOH H 4 .   ? 26.945 -21.622 32.211  1.00 37.02 ? 679 HOH B O     1 
HETATM 6173 O O     . HOH H 4 .   ? 43.741 -6.176  47.105  1.00 41.19 ? 680 HOH B O     1 
HETATM 6174 O O     . HOH H 4 .   ? 38.174 -3.255  32.426  1.00 37.26 ? 681 HOH B O     1 
HETATM 6175 O O     . HOH H 4 .   ? 45.340 -7.261  43.164  1.00 33.19 ? 682 HOH B O     1 
HETATM 6176 O O     . HOH H 4 .   ? 36.293 19.971  40.093  1.00 41.01 ? 683 HOH B O     1 
HETATM 6177 O O     . HOH H 4 .   ? 21.585 -23.495 66.111  1.00 43.81 ? 684 HOH B O     1 
HETATM 6178 O O     . HOH H 4 .   ? 15.581 -28.290 47.190  1.00 41.10 ? 685 HOH B O     1 
HETATM 6179 O O     . HOH H 4 .   ? 12.038 -8.270  67.049  1.00 35.04 ? 686 HOH B O     1 
HETATM 6180 O O     . HOH H 4 .   ? 17.351 -23.935 59.902  1.00 49.56 ? 687 HOH B O     1 
HETATM 6181 O O     . HOH H 4 .   ? 13.538 -19.946 58.204  1.00 40.73 ? 688 HOH B O     1 
HETATM 6182 O O     . HOH H 4 .   ? 27.245 -12.643 66.864  1.00 33.73 ? 689 HOH B O     1 
HETATM 6183 O O     . HOH H 4 .   ? 1.249  -1.202  65.780  1.00 33.95 ? 690 HOH B O     1 
HETATM 6184 O O     . HOH H 4 .   ? 4.936  2.695   64.219  1.00 38.86 ? 691 HOH B O     1 
HETATM 6185 O O     . HOH H 4 .   ? 16.920 12.898  57.509  1.00 43.99 ? 692 HOH B O     1 
HETATM 6186 O O     . HOH H 4 .   ? 5.744  3.076   55.408  1.00 40.38 ? 693 HOH B O     1 
HETATM 6187 O O     . HOH H 4 .   ? 4.843  -15.890 65.196  1.00 29.35 ? 694 HOH B O     1 
HETATM 6188 O O     . HOH H 4 .   ? 4.581  -2.933  25.795  1.00 37.59 ? 695 HOH B O     1 
HETATM 6189 O O     . HOH H 4 .   ? 43.800 -8.523  45.883  1.00 44.19 ? 696 HOH B O     1 
HETATM 6190 O O     . HOH H 4 .   ? 15.667 11.242  56.800  1.00 44.14 ? 697 HOH B O     1 
HETATM 6191 O O     . HOH H 4 .   ? 32.411 -19.001 58.176  1.00 45.38 ? 698 HOH B O     1 
HETATM 6192 O O     . HOH H 4 .   ? 40.928 -5.689  32.097  1.00 42.41 ? 699 HOH B O     1 
HETATM 6193 O O     . HOH H 4 .   ? 30.448 18.463  50.178  1.00 27.23 ? 700 HOH B O     1 
HETATM 6194 O O     . HOH H 4 .   ? -2.126 -2.037  36.484  1.00 33.25 ? 701 HOH B O     1 
HETATM 6195 O O     . HOH H 4 .   ? 13.175 3.296   39.093  1.00 30.08 ? 702 HOH B O     1 
HETATM 6196 O O     . HOH H 4 .   ? 39.341 20.467  37.134  1.00 51.17 ? 703 HOH B O     1 
HETATM 6197 O O     . HOH H 4 .   ? 4.173  -6.599  25.911  1.00 47.75 ? 704 HOH B O     1 
HETATM 6198 O O     . HOH H 4 .   ? -0.293 -17.972 37.746  1.00 40.57 ? 705 HOH B O     1 
HETATM 6199 O O     . HOH H 4 .   ? 18.526 17.399  43.578  1.00 44.14 ? 706 HOH B O     1 
HETATM 6200 O O     . HOH H 4 .   ? 22.107 18.159  54.755  1.00 42.89 ? 707 HOH B O     1 
HETATM 6201 O O     . HOH H 4 .   ? 16.617 7.505   28.627  1.00 35.92 ? 708 HOH B O     1 
HETATM 6202 O O     . HOH H 4 .   ? 40.813 6.172   36.972  1.00 37.26 ? 709 HOH B O     1 
HETATM 6203 O O     . HOH H 4 .   ? 19.730 -24.557 60.335  1.00 41.86 ? 710 HOH B O     1 
HETATM 6204 O O     . HOH H 4 .   ? 16.726 5.891   30.710  1.00 28.37 ? 711 HOH B O     1 
HETATM 6205 O O     . HOH H 4 .   ? 18.654 -19.621 70.369  1.00 52.25 ? 712 HOH B O     1 
HETATM 6206 O O     . HOH H 4 .   ? 12.792 3.141   36.296  1.00 23.61 ? 713 HOH B O     1 
HETATM 6207 O O     . HOH H 4 .   ? 24.479 18.758  58.104  1.00 34.25 ? 714 HOH B O     1 
HETATM 6208 O O     . HOH H 4 .   ? 21.289 -24.338 58.087  1.00 46.61 ? 715 HOH B O     1 
HETATM 6209 O O     . HOH H 4 .   ? 41.872 10.831  42.644  1.00 38.59 ? 716 HOH B O     1 
HETATM 6210 O O     . HOH H 4 .   ? 42.539 0.712   31.241  1.00 55.65 ? 717 HOH B O     1 
HETATM 6211 O O     . HOH H 4 .   ? 23.188 -24.734 59.390  1.00 48.19 ? 718 HOH B O     1 
HETATM 6212 O O     . HOH H 4 .   ? 23.860 13.167  27.260  1.00 40.34 ? 719 HOH B O     1 
HETATM 6213 O O     . HOH H 4 .   ? 9.729  -28.259 39.013  1.00 26.84 ? 720 HOH B O     1 
HETATM 6214 O O     . HOH H 4 .   ? 38.659 18.277  33.871  1.00 49.39 ? 721 HOH B O     1 
HETATM 6215 O O     . HOH H 4 .   ? 28.835 -12.913 69.639  1.00 36.54 ? 722 HOH B O     1 
HETATM 6216 O O     . HOH H 4 .   ? 28.324 14.545  26.193  1.00 41.10 ? 723 HOH B O     1 
HETATM 6217 O O     . HOH H 4 .   ? 24.116 14.500  62.043  1.00 37.99 ? 724 HOH B O     1 
HETATM 6218 O O     . HOH H 4 .   ? 15.676 8.497   37.152  1.00 38.32 ? 725 HOH B O     1 
HETATM 6219 O O     . HOH H 4 .   ? 14.778 -18.313 61.922  1.00 40.89 ? 726 HOH B O     1 
HETATM 6220 O O     . HOH H 4 .   ? 13.366 5.355   34.863  1.00 31.72 ? 727 HOH B O     1 
HETATM 6221 O O     . HOH H 4 .   ? 35.409 25.682  51.604  1.00 47.34 ? 728 HOH B O     1 
HETATM 6222 O O     . HOH H 4 .   ? 16.676 -20.875 34.479  1.00 36.69 ? 729 HOH B O     1 
HETATM 6223 O O     . HOH H 4 .   ? 40.668 9.043   43.810  1.00 32.95 ? 730 HOH B O     1 
HETATM 6224 O O     . HOH H 4 .   ? 41.969 0.210   64.447  1.00 47.26 ? 731 HOH B O     1 
HETATM 6225 O O     . HOH H 4 .   ? 42.635 2.969   30.808  1.00 52.70 ? 732 HOH B O     1 
HETATM 6226 O O     . HOH H 4 .   ? 40.037 11.165  33.669  1.00 42.83 ? 733 HOH B O     1 
HETATM 6227 O O     . HOH H 4 .   ? 20.212 17.477  54.221  1.00 45.04 ? 734 HOH B O     1 
HETATM 6228 O O     . HOH H 4 .   ? 0.230  -8.675  30.947  1.00 40.57 ? 735 HOH B O     1 
HETATM 6229 O O     . HOH H 4 .   ? 42.341 7.919   49.543  1.00 41.91 ? 736 HOH B O     1 
HETATM 6230 O O     . HOH H 4 .   ? 42.210 13.430  35.006  1.00 49.48 ? 737 HOH B O     1 
HETATM 6231 O O     . HOH H 4 .   ? 41.913 -2.538  31.971  1.00 39.68 ? 738 HOH B O     1 
HETATM 6232 O O     . HOH H 4 .   ? 42.525 9.878   40.309  1.00 41.51 ? 739 HOH B O     1 
HETATM 6233 O O     . HOH H 4 .   ? 35.098 3.600   24.810  1.00 36.81 ? 740 HOH B O     1 
# 
