data_9FCN
# 
_entry.id   9FCN 
# 
_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   9FCN         pdb_00009fcn 10.2210/pdb9fcn/pdb 
WWPDB D_1292138663 ?            ?                   
# 
_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       2025-05-28 
_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                        9FCN 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-15 
_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 
# 
_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 ? 
'Kerschbaumer, B.' 2 ? 
'Macheroux, P.'    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                     'Insights into the complexity of coenzyme specificity in ene-reductases' 
_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 'Kerschaumer, B.' 1 ? 
primary 'Macheroux, P.'   2 ? 
primary 'Bijelic, A.'     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,Old yellow enzyme OYE4'        44167.883 2   1.3.1.42,1.6.99.1 ? ? ? 
2 non-polymer syn 'FLAVIN MONONUCLEOTIDE'                                         456.344   2   ?                 ? ? ? 
3 non-polymer syn '1,4,5,6-TETRAHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE' 747.437   2   ?                 ? ? ? 
4 water       nat water                                                           18.015    479 ?                 ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '12-oxophytodienoate-10,11-reductase 3,OPDA-reductase 3,LeOPR3' 
# 
_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
DRVGVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTAEADWDDAPDMPEEEEARLMRTLRNAYQGTF
ICSGGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLSRL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MASHHHHHHMASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTS
AGFPHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPK
PRAIGTYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGA
DRVGVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTAEADWDDAPDMPEEEEARLMRTLRNAYQGTF
ICSGGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLSRL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN MONONUCLEOTIDE'                                         FMN 
3 '1,4,5,6-TETRAHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE' TXP 
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 ALA n 
1 291 GLU n 
1 292 ALA n 
1 293 ASP n 
1 294 TRP n 
1 295 ASP n 
1 296 ASP n 
1 297 ALA n 
1 298 PRO n 
1 299 ASP n 
1 300 MET n 
1 301 PRO n 
1 302 GLU n 
1 303 GLU n 
1 304 GLU n 
1 305 GLU n 
1 306 ALA n 
1 307 ARG n 
1 308 LEU n 
1 309 MET n 
1 310 ARG n 
1 311 THR n 
1 312 LEU n 
1 313 ARG n 
1 314 ASN n 
1 315 ALA n 
1 316 TYR n 
1 317 GLN n 
1 318 GLY n 
1 319 THR n 
1 320 PHE n 
1 321 ILE n 
1 322 CYS n 
1 323 SER n 
1 324 GLY n 
1 325 GLY n 
1 326 TYR n 
1 327 THR n 
1 328 ARG n 
1 329 GLU n 
1 330 LEU n 
1 331 GLY n 
1 332 ILE n 
1 333 GLU n 
1 334 ALA n 
1 335 VAL n 
1 336 ALA n 
1 337 GLN n 
1 338 GLY n 
1 339 ASP n 
1 340 ALA n 
1 341 ASP n 
1 342 LEU n 
1 343 VAL n 
1 344 SER n 
1 345 TYR n 
1 346 GLY n 
1 347 ARG n 
1 348 LEU n 
1 349 PHE n 
1 350 ILE n 
1 351 SER n 
1 352 ASN n 
1 353 PRO n 
1 354 ASP n 
1 355 LEU n 
1 356 VAL n 
1 357 MET n 
1 358 ARG n 
1 359 ILE n 
1 360 LYS n 
1 361 LEU n 
1 362 ASN n 
1 363 ALA n 
1 364 PRO n 
1 365 LEU n 
1 366 ASN n 
1 367 LYS n 
1 368 TYR n 
1 369 ASN n 
1 370 ARG n 
1 371 LYS n 
1 372 THR n 
1 373 PHE n 
1 374 TYR n 
1 375 THR n 
1 376 GLN n 
1 377 ASP n 
1 378 PRO n 
1 379 VAL n 
1 380 VAL n 
1 381 GLY n 
1 382 TYR n 
1 383 THR n 
1 384 ASP n 
1 385 TYR n 
1 386 PRO n 
1 387 PHE n 
1 388 LEU n 
1 389 GLN n 
1 390 GLY n 
1 391 ASN n 
1 392 GLY n 
1 393 SER n 
1 394 ASN n 
1 395 GLY n 
1 396 PRO n 
1 397 LEU n 
1 398 SER n 
1 399 ARG n 
1 400 LEU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1   289 tomato ? OPR3 ? ? ? ? ? ? 'Solanum lycopersicum'   4081    ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 290 301 ?      ? ?    ? ? ? ? ? ? 'Achromobacter sp. JA81' 1109013 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 3 sample 'Biological sequence' 302 400 tomato ? OPR3 ? ? ? ? ? ? 'Solanum lycopersicum'   4081    ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                         ?                          'C3 H7 N O2' 
89.093  
ARG 'L-peptide linking' y ARGININE                                                        ?                          
'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                      ?                          'C4 H8 N2 O3' 
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                 ?                          'C4 H7 N O4' 
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                        ?                          
'C3 H7 N O2 S'      121.158 
FMN non-polymer         . 'FLAVIN MONONUCLEOTIDE'                                         'RIBOFLAVIN MONOPHOSPHATE' 
'C17 H21 N4 O9 P'   456.344 
GLN 'L-peptide linking' y GLUTAMINE                                                       ?                          
'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                 ?                          'C5 H9 N O4' 
147.129 
GLY 'peptide linking'   y GLYCINE                                                         ?                          'C2 H5 N O2' 
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                       ?                          
'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                                           ?                          'H2 O' 18.015 
ILE 'L-peptide linking' y ISOLEUCINE                                                      ?                          'C6 H13 N O2' 
131.173 
LEU 'L-peptide linking' y LEUCINE                                                         ?                          'C6 H13 N O2' 
131.173 
LYS 'L-peptide linking' y LYSINE                                                          ?                          
'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                                                      ?                          
'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                   ?                          'C9 H11 N O2' 
165.189 
PRO 'L-peptide linking' y PROLINE                                                         ?                          'C5 H9 N O2' 
115.130 
SER 'L-peptide linking' y SERINE                                                          ?                          'C3 H7 N O3' 
105.093 
THR 'L-peptide linking' y THREONINE                                                       ?                          'C4 H9 N O3' 
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                      ?                          
'C11 H12 N2 O2'     204.225 
TXP non-polymer         n '1,4,5,6-TETRAHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE' ?                          
'C21 H32 N7 O17 P3' 747.437 
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 ALA 290 281 281 ALA ALA A . n 
A 1 291 GLU 291 282 282 GLU GLU A . n 
A 1 292 ALA 292 283 283 ALA ALA A . n 
A 1 293 ASP 293 284 284 ASP ASP A . n 
A 1 294 TRP 294 285 285 TRP TRP A . n 
A 1 295 ASP 295 286 ?   ?   ?   A . n 
A 1 296 ASP 296 287 ?   ?   ?   A . n 
A 1 297 ALA 297 288 ?   ?   ?   A . n 
A 1 298 PRO 298 289 ?   ?   ?   A . n 
A 1 299 ASP 299 290 ?   ?   ?   A . n 
A 1 300 MET 300 291 ?   ?   ?   A . n 
A 1 301 PRO 301 292 ?   ?   ?   A . n 
A 1 302 GLU 302 293 ?   ?   ?   A . n 
A 1 303 GLU 303 294 ?   ?   ?   A . n 
A 1 304 GLU 304 295 ?   ?   ?   A . n 
A 1 305 GLU 305 296 296 GLU GLU A . n 
A 1 306 ALA 306 297 297 ALA ALA A . n 
A 1 307 ARG 307 298 298 ARG ARG A . n 
A 1 308 LEU 308 299 299 LEU LEU A . n 
A 1 309 MET 309 300 300 MET MET A . n 
A 1 310 ARG 310 301 301 ARG ARG A . n 
A 1 311 THR 311 302 302 THR THR A . n 
A 1 312 LEU 312 303 303 LEU LEU A . n 
A 1 313 ARG 313 304 304 ARG ARG A . n 
A 1 314 ASN 314 305 305 ASN ASN A . n 
A 1 315 ALA 315 306 306 ALA ALA A . n 
A 1 316 TYR 316 307 307 TYR TYR A . n 
A 1 317 GLN 317 308 308 GLN GLN A . n 
A 1 318 GLY 318 309 309 GLY GLY A . n 
A 1 319 THR 319 310 310 THR THR A . n 
A 1 320 PHE 320 311 311 PHE PHE A . n 
A 1 321 ILE 321 312 312 ILE ILE A . n 
A 1 322 CYS 322 313 313 CYS CYS A . n 
A 1 323 SER 323 314 314 SER SER A . n 
A 1 324 GLY 324 315 315 GLY GLY A . n 
A 1 325 GLY 325 316 316 GLY GLY A . n 
A 1 326 TYR 326 317 317 TYR TYR A . n 
A 1 327 THR 327 318 318 THR THR A . n 
A 1 328 ARG 328 319 319 ARG ARG A . n 
A 1 329 GLU 329 320 320 GLU GLU A . n 
A 1 330 LEU 330 321 321 LEU LEU A . n 
A 1 331 GLY 331 322 322 GLY GLY A . n 
A 1 332 ILE 332 323 323 ILE ILE A . n 
A 1 333 GLU 333 324 324 GLU GLU A . n 
A 1 334 ALA 334 325 325 ALA ALA A . n 
A 1 335 VAL 335 326 326 VAL VAL A . n 
A 1 336 ALA 336 327 327 ALA ALA A . n 
A 1 337 GLN 337 328 328 GLN GLN A . n 
A 1 338 GLY 338 329 329 GLY GLY A . n 
A 1 339 ASP 339 330 330 ASP ASP A . n 
A 1 340 ALA 340 331 331 ALA ALA A . n 
A 1 341 ASP 341 332 332 ASP ASP A . n 
A 1 342 LEU 342 333 333 LEU LEU A . n 
A 1 343 VAL 343 334 334 VAL VAL A . n 
A 1 344 SER 344 335 335 SER SER A . n 
A 1 345 TYR 345 336 336 TYR TYR A . n 
A 1 346 GLY 346 337 337 GLY GLY A . n 
A 1 347 ARG 347 338 338 ARG ARG A . n 
A 1 348 LEU 348 339 339 LEU LEU A . n 
A 1 349 PHE 349 340 340 PHE PHE A . n 
A 1 350 ILE 350 341 341 ILE ILE A . n 
A 1 351 SER 351 342 342 SER SER A . n 
A 1 352 ASN 352 343 343 ASN ASN A . n 
A 1 353 PRO 353 344 344 PRO PRO A . n 
A 1 354 ASP 354 345 345 ASP ASP A . n 
A 1 355 LEU 355 346 346 LEU LEU A . n 
A 1 356 VAL 356 347 347 VAL VAL A . n 
A 1 357 MET 357 348 348 MET MET A . n 
A 1 358 ARG 358 349 349 ARG ARG A . n 
A 1 359 ILE 359 350 350 ILE ILE A . n 
A 1 360 LYS 360 351 351 LYS LYS 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 ALA 363 354 354 ALA ALA A . n 
A 1 364 PRO 364 355 355 PRO PRO A . n 
A 1 365 LEU 365 356 356 LEU LEU A . n 
A 1 366 ASN 366 357 357 ASN ASN A . n 
A 1 367 LYS 367 358 358 LYS LYS A . n 
A 1 368 TYR 368 359 359 TYR TYR A . n 
A 1 369 ASN 369 360 360 ASN ASN A . n 
A 1 370 ARG 370 361 361 ARG ARG A . n 
A 1 371 LYS 371 362 362 LYS LYS A . n 
A 1 372 THR 372 363 363 THR THR A . n 
A 1 373 PHE 373 364 364 PHE PHE A . n 
A 1 374 TYR 374 365 365 TYR TYR A . n 
A 1 375 THR 375 366 366 THR THR A . n 
A 1 376 GLN 376 367 367 GLN GLN A . n 
A 1 377 ASP 377 368 368 ASP ASP A . n 
A 1 378 PRO 378 369 369 PRO PRO A . n 
A 1 379 VAL 379 370 370 VAL VAL A . n 
A 1 380 VAL 380 371 371 VAL VAL A . n 
A 1 381 GLY 381 372 372 GLY GLY A . n 
A 1 382 TYR 382 373 373 TYR TYR A . n 
A 1 383 THR 383 374 374 THR THR A . n 
A 1 384 ASP 384 375 375 ASP ASP A . n 
A 1 385 TYR 385 376 376 TYR TYR A . n 
A 1 386 PRO 386 377 377 PRO PRO A . n 
A 1 387 PHE 387 378 378 PHE PHE A . n 
A 1 388 LEU 388 379 379 LEU LEU A . n 
A 1 389 GLN 389 380 ?   ?   ?   A . n 
A 1 390 GLY 390 381 ?   ?   ?   A . n 
A 1 391 ASN 391 382 ?   ?   ?   A . n 
A 1 392 GLY 392 383 ?   ?   ?   A . n 
A 1 393 SER 393 384 ?   ?   ?   A . n 
A 1 394 ASN 394 385 ?   ?   ?   A . n 
A 1 395 GLY 395 386 ?   ?   ?   A . n 
A 1 396 PRO 396 387 ?   ?   ?   A . n 
A 1 397 LEU 397 388 ?   ?   ?   A . n 
A 1 398 SER 398 389 ?   ?   ?   A . n 
A 1 399 ARG 399 390 ?   ?   ?   A . n 
A 1 400 LEU 400 391 ?   ?   ?   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 ALA 290 281 281 ALA ALA B . n 
B 1 291 GLU 291 282 282 GLU GLU B . n 
B 1 292 ALA 292 283 283 ALA ALA B . n 
B 1 293 ASP 293 284 284 ASP ASP B . n 
B 1 294 TRP 294 285 285 TRP TRP B . n 
B 1 295 ASP 295 286 ?   ?   ?   B . n 
B 1 296 ASP 296 287 ?   ?   ?   B . n 
B 1 297 ALA 297 288 ?   ?   ?   B . n 
B 1 298 PRO 298 289 ?   ?   ?   B . n 
B 1 299 ASP 299 290 ?   ?   ?   B . n 
B 1 300 MET 300 291 ?   ?   ?   B . n 
B 1 301 PRO 301 292 ?   ?   ?   B . n 
B 1 302 GLU 302 293 ?   ?   ?   B . n 
B 1 303 GLU 303 294 ?   ?   ?   B . n 
B 1 304 GLU 304 295 ?   ?   ?   B . n 
B 1 305 GLU 305 296 296 GLU GLU B . n 
B 1 306 ALA 306 297 297 ALA ALA B . n 
B 1 307 ARG 307 298 298 ARG ARG B . n 
B 1 308 LEU 308 299 299 LEU LEU B . n 
B 1 309 MET 309 300 300 MET MET B . n 
B 1 310 ARG 310 301 301 ARG ARG B . n 
B 1 311 THR 311 302 302 THR THR B . n 
B 1 312 LEU 312 303 303 LEU LEU B . n 
B 1 313 ARG 313 304 304 ARG ARG B . n 
B 1 314 ASN 314 305 305 ASN ASN B . n 
B 1 315 ALA 315 306 306 ALA ALA B . n 
B 1 316 TYR 316 307 307 TYR TYR B . n 
B 1 317 GLN 317 308 308 GLN GLN B . n 
B 1 318 GLY 318 309 309 GLY GLY B . n 
B 1 319 THR 319 310 310 THR THR B . n 
B 1 320 PHE 320 311 311 PHE PHE B . n 
B 1 321 ILE 321 312 312 ILE ILE B . n 
B 1 322 CYS 322 313 313 CYS CYS B . n 
B 1 323 SER 323 314 314 SER SER B . n 
B 1 324 GLY 324 315 315 GLY GLY B . n 
B 1 325 GLY 325 316 316 GLY GLY B . n 
B 1 326 TYR 326 317 317 TYR TYR B . n 
B 1 327 THR 327 318 318 THR THR B . n 
B 1 328 ARG 328 319 319 ARG ARG B . n 
B 1 329 GLU 329 320 320 GLU GLU B . n 
B 1 330 LEU 330 321 321 LEU LEU B . n 
B 1 331 GLY 331 322 322 GLY GLY B . n 
B 1 332 ILE 332 323 323 ILE ILE B . n 
B 1 333 GLU 333 324 324 GLU GLU B . n 
B 1 334 ALA 334 325 325 ALA ALA B . n 
B 1 335 VAL 335 326 326 VAL VAL B . n 
B 1 336 ALA 336 327 327 ALA ALA B . n 
B 1 337 GLN 337 328 328 GLN GLN B . n 
B 1 338 GLY 338 329 329 GLY GLY B . n 
B 1 339 ASP 339 330 330 ASP ASP B . n 
B 1 340 ALA 340 331 331 ALA ALA B . n 
B 1 341 ASP 341 332 332 ASP ASP B . n 
B 1 342 LEU 342 333 333 LEU LEU B . n 
B 1 343 VAL 343 334 334 VAL VAL B . n 
B 1 344 SER 344 335 335 SER SER B . n 
B 1 345 TYR 345 336 336 TYR TYR B . n 
B 1 346 GLY 346 337 337 GLY GLY B . n 
B 1 347 ARG 347 338 338 ARG ARG B . n 
B 1 348 LEU 348 339 339 LEU LEU B . n 
B 1 349 PHE 349 340 340 PHE PHE B . n 
B 1 350 ILE 350 341 341 ILE ILE B . n 
B 1 351 SER 351 342 342 SER SER B . n 
B 1 352 ASN 352 343 343 ASN ASN B . n 
B 1 353 PRO 353 344 344 PRO PRO B . n 
B 1 354 ASP 354 345 345 ASP ASP B . n 
B 1 355 LEU 355 346 346 LEU LEU B . n 
B 1 356 VAL 356 347 347 VAL VAL B . n 
B 1 357 MET 357 348 348 MET MET B . n 
B 1 358 ARG 358 349 349 ARG ARG B . n 
B 1 359 ILE 359 350 350 ILE ILE B . n 
B 1 360 LYS 360 351 351 LYS LYS 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 ALA 363 354 354 ALA ALA B . n 
B 1 364 PRO 364 355 355 PRO PRO B . n 
B 1 365 LEU 365 356 356 LEU LEU B . n 
B 1 366 ASN 366 357 357 ASN ASN B . n 
B 1 367 LYS 367 358 358 LYS LYS B . n 
B 1 368 TYR 368 359 359 TYR TYR B . n 
B 1 369 ASN 369 360 360 ASN ASN B . n 
B 1 370 ARG 370 361 361 ARG ARG B . n 
B 1 371 LYS 371 362 362 LYS LYS B . n 
B 1 372 THR 372 363 363 THR THR B . n 
B 1 373 PHE 373 364 364 PHE PHE B . n 
B 1 374 TYR 374 365 365 TYR TYR B . n 
B 1 375 THR 375 366 366 THR THR B . n 
B 1 376 GLN 376 367 367 GLN GLN B . n 
B 1 377 ASP 377 368 368 ASP ASP B . n 
B 1 378 PRO 378 369 369 PRO PRO B . n 
B 1 379 VAL 379 370 370 VAL VAL B . n 
B 1 380 VAL 380 371 371 VAL VAL B . n 
B 1 381 GLY 381 372 372 GLY GLY B . n 
B 1 382 TYR 382 373 373 TYR TYR B . n 
B 1 383 THR 383 374 374 THR THR B . n 
B 1 384 ASP 384 375 375 ASP ASP B . n 
B 1 385 TYR 385 376 376 TYR TYR B . n 
B 1 386 PRO 386 377 377 PRO PRO B . n 
B 1 387 PHE 387 378 378 PHE PHE B . n 
B 1 388 LEU 388 379 379 LEU LEU B . n 
B 1 389 GLN 389 380 ?   ?   ?   B . n 
B 1 390 GLY 390 381 ?   ?   ?   B . n 
B 1 391 ASN 391 382 ?   ?   ?   B . n 
B 1 392 GLY 392 383 ?   ?   ?   B . n 
B 1 393 SER 393 384 ?   ?   ?   B . n 
B 1 394 ASN 394 385 ?   ?   ?   B . n 
B 1 395 GLY 395 386 ?   ?   ?   B . n 
B 1 396 PRO 396 387 ?   ?   ?   B . n 
B 1 397 LEU 397 388 ?   ?   ?   B . n 
B 1 398 SER 398 389 ?   ?   ?   B . n 
B 1 399 ARG 399 390 ?   ?   ?   B . n 
B 1 400 LEU 400 391 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        TXP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   TXP 
_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   401 396 FMN FMN A . 
D 3 TXP 1   402 397 TXP TXP A . 
E 2 FMN 1   401 396 FMN FMN B . 
F 3 TXP 1   402 397 TXP TXP B . 
G 4 HOH 1   501 402 HOH HOH A . 
G 4 HOH 2   502 307 HOH HOH A . 
G 4 HOH 3   503 322 HOH HOH A . 
G 4 HOH 4   504 223 HOH HOH A . 
G 4 HOH 5   505 257 HOH HOH A . 
G 4 HOH 6   506 401 HOH HOH A . 
G 4 HOH 7   507 158 HOH HOH A . 
G 4 HOH 8   508 406 HOH HOH A . 
G 4 HOH 9   509 27  HOH HOH A . 
G 4 HOH 10  510 113 HOH HOH A . 
G 4 HOH 11  511 174 HOH HOH A . 
G 4 HOH 12  512 41  HOH HOH A . 
G 4 HOH 13  513 491 HOH HOH A . 
G 4 HOH 14  514 384 HOH HOH A . 
G 4 HOH 15  515 320 HOH HOH A . 
G 4 HOH 16  516 90  HOH HOH A . 
G 4 HOH 17  517 167 HOH HOH A . 
G 4 HOH 18  518 193 HOH HOH A . 
G 4 HOH 19  519 349 HOH HOH A . 
G 4 HOH 20  520 64  HOH HOH A . 
G 4 HOH 21  521 93  HOH HOH A . 
G 4 HOH 22  522 253 HOH HOH A . 
G 4 HOH 23  523 133 HOH HOH A . 
G 4 HOH 24  524 250 HOH HOH A . 
G 4 HOH 25  525 26  HOH HOH A . 
G 4 HOH 26  526 131 HOH HOH A . 
G 4 HOH 27  527 259 HOH HOH A . 
G 4 HOH 28  528 10  HOH HOH A . 
G 4 HOH 29  529 2   HOH HOH A . 
G 4 HOH 30  530 217 HOH HOH A . 
G 4 HOH 31  531 40  HOH HOH A . 
G 4 HOH 32  532 109 HOH HOH A . 
G 4 HOH 33  533 269 HOH HOH A . 
G 4 HOH 34  534 304 HOH HOH A . 
G 4 HOH 35  535 449 HOH HOH A . 
G 4 HOH 36  536 271 HOH HOH A . 
G 4 HOH 37  537 169 HOH HOH A . 
G 4 HOH 38  538 146 HOH HOH A . 
G 4 HOH 39  539 266 HOH HOH A . 
G 4 HOH 40  540 4   HOH HOH A . 
G 4 HOH 41  541 215 HOH HOH A . 
G 4 HOH 42  542 390 HOH HOH A . 
G 4 HOH 43  543 126 HOH HOH A . 
G 4 HOH 44  544 114 HOH HOH A . 
G 4 HOH 45  545 210 HOH HOH A . 
G 4 HOH 46  546 249 HOH HOH A . 
G 4 HOH 47  547 98  HOH HOH A . 
G 4 HOH 48  548 319 HOH HOH A . 
G 4 HOH 49  549 21  HOH HOH A . 
G 4 HOH 50  550 356 HOH HOH A . 
G 4 HOH 51  551 404 HOH HOH A . 
G 4 HOH 52  552 51  HOH HOH A . 
G 4 HOH 53  553 252 HOH HOH A . 
G 4 HOH 54  554 237 HOH HOH A . 
G 4 HOH 55  555 42  HOH HOH A . 
G 4 HOH 56  556 341 HOH HOH A . 
G 4 HOH 57  557 327 HOH HOH A . 
G 4 HOH 58  558 212 HOH HOH A . 
G 4 HOH 59  559 102 HOH HOH A . 
G 4 HOH 60  560 56  HOH HOH A . 
G 4 HOH 61  561 358 HOH HOH A . 
G 4 HOH 62  562 94  HOH HOH A . 
G 4 HOH 63  563 35  HOH HOH A . 
G 4 HOH 64  564 19  HOH HOH A . 
G 4 HOH 65  565 24  HOH HOH A . 
G 4 HOH 66  566 209 HOH HOH A . 
G 4 HOH 67  567 170 HOH HOH A . 
G 4 HOH 68  568 234 HOH HOH A . 
G 4 HOH 69  569 151 HOH HOH A . 
G 4 HOH 70  570 117 HOH HOH A . 
G 4 HOH 71  571 270 HOH HOH A . 
G 4 HOH 72  572 33  HOH HOH A . 
G 4 HOH 73  573 20  HOH HOH A . 
G 4 HOH 74  574 82  HOH HOH A . 
G 4 HOH 75  575 22  HOH HOH A . 
G 4 HOH 76  576 281 HOH HOH A . 
G 4 HOH 77  577 115 HOH HOH A . 
G 4 HOH 78  578 140 HOH HOH A . 
G 4 HOH 79  579 197 HOH HOH A . 
G 4 HOH 80  580 490 HOH HOH A . 
G 4 HOH 81  581 168 HOH HOH A . 
G 4 HOH 82  582 81  HOH HOH A . 
G 4 HOH 83  583 95  HOH HOH A . 
G 4 HOH 84  584 142 HOH HOH A . 
G 4 HOH 85  585 400 HOH HOH A . 
G 4 HOH 86  586 11  HOH HOH A . 
G 4 HOH 87  587 119 HOH HOH A . 
G 4 HOH 88  588 199 HOH HOH A . 
G 4 HOH 89  589 499 HOH HOH A . 
G 4 HOH 90  590 125 HOH HOH A . 
G 4 HOH 91  591 163 HOH HOH A . 
G 4 HOH 92  592 399 HOH HOH A . 
G 4 HOH 93  593 315 HOH HOH A . 
G 4 HOH 94  594 91  HOH HOH A . 
G 4 HOH 95  595 427 HOH HOH A . 
G 4 HOH 96  596 373 HOH HOH A . 
G 4 HOH 97  597 84  HOH HOH A . 
G 4 HOH 98  598 62  HOH HOH A . 
G 4 HOH 99  599 497 HOH HOH A . 
G 4 HOH 100 600 465 HOH HOH A . 
G 4 HOH 101 601 172 HOH HOH A . 
G 4 HOH 102 602 46  HOH HOH A . 
G 4 HOH 103 603 422 HOH HOH A . 
G 4 HOH 104 604 173 HOH HOH A . 
G 4 HOH 105 605 153 HOH HOH A . 
G 4 HOH 106 606 236 HOH HOH A . 
G 4 HOH 107 607 238 HOH HOH A . 
G 4 HOH 108 608 323 HOH HOH A . 
G 4 HOH 109 609 206 HOH HOH A . 
G 4 HOH 110 610 290 HOH HOH A . 
G 4 HOH 111 611 245 HOH HOH A . 
G 4 HOH 112 612 165 HOH HOH A . 
G 4 HOH 113 613 247 HOH HOH A . 
G 4 HOH 114 614 5   HOH HOH A . 
G 4 HOH 115 615 299 HOH HOH A . 
G 4 HOH 116 616 258 HOH HOH A . 
G 4 HOH 117 617 37  HOH HOH A . 
G 4 HOH 118 618 176 HOH HOH A . 
G 4 HOH 119 619 76  HOH HOH A . 
G 4 HOH 120 620 198 HOH HOH A . 
G 4 HOH 121 621 161 HOH HOH A . 
G 4 HOH 122 622 256 HOH HOH A . 
G 4 HOH 123 623 136 HOH HOH A . 
G 4 HOH 124 624 460 HOH HOH A . 
G 4 HOH 125 625 75  HOH HOH A . 
G 4 HOH 126 626 305 HOH HOH A . 
G 4 HOH 127 627 39  HOH HOH A . 
G 4 HOH 128 628 137 HOH HOH A . 
G 4 HOH 129 629 150 HOH HOH A . 
G 4 HOH 130 630 3   HOH HOH A . 
G 4 HOH 131 631 416 HOH HOH A . 
G 4 HOH 132 632 296 HOH HOH A . 
G 4 HOH 133 633 116 HOH HOH A . 
G 4 HOH 134 634 110 HOH HOH A . 
G 4 HOH 135 635 248 HOH HOH A . 
G 4 HOH 136 636 428 HOH HOH A . 
G 4 HOH 137 637 342 HOH HOH A . 
G 4 HOH 138 638 336 HOH HOH A . 
G 4 HOH 139 639 53  HOH HOH A . 
G 4 HOH 140 640 156 HOH HOH A . 
G 4 HOH 141 641 60  HOH HOH A . 
G 4 HOH 142 642 149 HOH HOH A . 
G 4 HOH 143 643 513 HOH HOH A . 
G 4 HOH 144 644 351 HOH HOH A . 
G 4 HOH 145 645 211 HOH HOH A . 
G 4 HOH 146 646 162 HOH HOH A . 
G 4 HOH 147 647 325 HOH HOH A . 
G 4 HOH 148 648 458 HOH HOH A . 
G 4 HOH 149 649 330 HOH HOH A . 
G 4 HOH 150 650 124 HOH HOH A . 
G 4 HOH 151 651 226 HOH HOH A . 
G 4 HOH 152 652 216 HOH HOH A . 
G 4 HOH 153 653 487 HOH HOH A . 
G 4 HOH 154 654 360 HOH HOH A . 
G 4 HOH 155 655 326 HOH HOH A . 
G 4 HOH 156 656 498 HOH HOH A . 
G 4 HOH 157 657 54  HOH HOH A . 
G 4 HOH 158 658 350 HOH HOH A . 
G 4 HOH 159 659 284 HOH HOH A . 
G 4 HOH 160 660 279 HOH HOH A . 
G 4 HOH 161 661 391 HOH HOH A . 
G 4 HOH 162 662 120 HOH HOH A . 
G 4 HOH 163 663 160 HOH HOH A . 
G 4 HOH 164 664 180 HOH HOH A . 
G 4 HOH 165 665 184 HOH HOH A . 
G 4 HOH 166 666 348 HOH HOH A . 
G 4 HOH 167 667 207 HOH HOH A . 
G 4 HOH 168 668 70  HOH HOH A . 
G 4 HOH 169 669 421 HOH HOH A . 
G 4 HOH 170 670 222 HOH HOH A . 
G 4 HOH 171 671 283 HOH HOH A . 
G 4 HOH 172 672 66  HOH HOH A . 
G 4 HOH 173 673 287 HOH HOH A . 
G 4 HOH 174 674 275 HOH HOH A . 
G 4 HOH 175 675 486 HOH HOH A . 
G 4 HOH 176 676 32  HOH HOH A . 
G 4 HOH 177 677 154 HOH HOH A . 
G 4 HOH 178 678 272 HOH HOH A . 
G 4 HOH 179 679 87  HOH HOH A . 
G 4 HOH 180 680 385 HOH HOH A . 
G 4 HOH 181 681 191 HOH HOH A . 
G 4 HOH 182 682 183 HOH HOH A . 
G 4 HOH 183 683 392 HOH HOH A . 
G 4 HOH 184 684 375 HOH HOH A . 
G 4 HOH 185 685 368 HOH HOH A . 
G 4 HOH 186 686 434 HOH HOH A . 
G 4 HOH 187 687 501 HOH HOH A . 
G 4 HOH 188 688 111 HOH HOH A . 
G 4 HOH 189 689 339 HOH HOH A . 
G 4 HOH 190 690 267 HOH HOH A . 
G 4 HOH 191 691 503 HOH HOH A . 
G 4 HOH 192 692 410 HOH HOH A . 
G 4 HOH 193 693 508 HOH HOH A . 
G 4 HOH 194 694 276 HOH HOH A . 
G 4 HOH 195 695 73  HOH HOH A . 
G 4 HOH 196 696 418 HOH HOH A . 
G 4 HOH 197 697 450 HOH HOH A . 
G 4 HOH 198 698 440 HOH HOH A . 
G 4 HOH 199 699 386 HOH HOH A . 
G 4 HOH 200 700 352 HOH HOH A . 
G 4 HOH 201 701 446 HOH HOH A . 
G 4 HOH 202 702 435 HOH HOH A . 
G 4 HOH 203 703 433 HOH HOH A . 
G 4 HOH 204 704 495 HOH HOH A . 
G 4 HOH 205 705 496 HOH HOH A . 
G 4 HOH 206 706 312 HOH HOH A . 
G 4 HOH 207 707 413 HOH HOH A . 
G 4 HOH 208 708 282 HOH HOH A . 
G 4 HOH 209 709 242 HOH HOH A . 
G 4 HOH 210 710 405 HOH HOH A . 
G 4 HOH 211 711 186 HOH HOH A . 
G 4 HOH 212 712 466 HOH HOH A . 
G 4 HOH 213 713 317 HOH HOH A . 
G 4 HOH 214 714 457 HOH HOH A . 
G 4 HOH 215 715 426 HOH HOH A . 
G 4 HOH 216 716 97  HOH HOH A . 
G 4 HOH 217 717 507 HOH HOH A . 
G 4 HOH 218 718 107 HOH HOH A . 
G 4 HOH 219 719 414 HOH HOH A . 
G 4 HOH 220 720 484 HOH HOH A . 
G 4 HOH 221 721 285 HOH HOH A . 
G 4 HOH 222 722 83  HOH HOH A . 
G 4 HOH 223 723 423 HOH HOH A . 
G 4 HOH 224 724 483 HOH HOH A . 
G 4 HOH 225 725 397 HOH HOH A . 
G 4 HOH 226 726 293 HOH HOH A . 
G 4 HOH 227 727 301 HOH HOH A . 
G 4 HOH 228 728 441 HOH HOH A . 
G 4 HOH 229 729 338 HOH HOH A . 
H 4 HOH 1   501 7   HOH HOH B . 
H 4 HOH 2   502 141 HOH HOH B . 
H 4 HOH 3   503 122 HOH HOH B . 
H 4 HOH 4   504 485 HOH HOH B . 
H 4 HOH 5   505 455 HOH HOH B . 
H 4 HOH 6   506 129 HOH HOH B . 
H 4 HOH 7   507 492 HOH HOH B . 
H 4 HOH 8   508 354 HOH HOH B . 
H 4 HOH 9   509 50  HOH HOH B . 
H 4 HOH 10  510 291 HOH HOH B . 
H 4 HOH 11  511 139 HOH HOH B . 
H 4 HOH 12  512 203 HOH HOH B . 
H 4 HOH 13  513 127 HOH HOH B . 
H 4 HOH 14  514 34  HOH HOH B . 
H 4 HOH 15  515 232 HOH HOH B . 
H 4 HOH 16  516 280 HOH HOH B . 
H 4 HOH 17  517 105 HOH HOH B . 
H 4 HOH 18  518 500 HOH HOH B . 
H 4 HOH 19  519 17  HOH HOH B . 
H 4 HOH 20  520 1   HOH HOH B . 
H 4 HOH 21  521 57  HOH HOH B . 
H 4 HOH 22  522 86  HOH HOH B . 
H 4 HOH 23  523 221 HOH HOH B . 
H 4 HOH 24  524 25  HOH HOH B . 
H 4 HOH 25  525 152 HOH HOH B . 
H 4 HOH 26  526 112 HOH HOH B . 
H 4 HOH 27  527 445 HOH HOH B . 
H 4 HOH 28  528 16  HOH HOH B . 
H 4 HOH 29  529 143 HOH HOH B . 
H 4 HOH 30  530 189 HOH HOH B . 
H 4 HOH 31  531 511 HOH HOH B . 
H 4 HOH 32  532 92  HOH HOH B . 
H 4 HOH 33  533 15  HOH HOH B . 
H 4 HOH 34  534 38  HOH HOH B . 
H 4 HOH 35  535 130 HOH HOH B . 
H 4 HOH 36  536 231 HOH HOH B . 
H 4 HOH 37  537 188 HOH HOH B . 
H 4 HOH 38  538 444 HOH HOH B . 
H 4 HOH 39  539 104 HOH HOH B . 
H 4 HOH 40  540 376 HOH HOH B . 
H 4 HOH 41  541 135 HOH HOH B . 
H 4 HOH 42  542 28  HOH HOH B . 
H 4 HOH 43  543 49  HOH HOH B . 
H 4 HOH 44  544 515 HOH HOH B . 
H 4 HOH 45  545 8   HOH HOH B . 
H 4 HOH 46  546 409 HOH HOH B . 
H 4 HOH 47  547 106 HOH HOH B . 
H 4 HOH 48  548 378 HOH HOH B . 
H 4 HOH 49  549 357 HOH HOH B . 
H 4 HOH 50  550 251 HOH HOH B . 
H 4 HOH 51  551 194 HOH HOH B . 
H 4 HOH 52  552 225 HOH HOH B . 
H 4 HOH 53  553 359 HOH HOH B . 
H 4 HOH 54  554 18  HOH HOH B . 
H 4 HOH 55  555 343 HOH HOH B . 
H 4 HOH 56  556 396 HOH HOH B . 
H 4 HOH 57  557 382 HOH HOH B . 
H 4 HOH 58  558 302 HOH HOH B . 
H 4 HOH 59  559 6   HOH HOH B . 
H 4 HOH 60  560 43  HOH HOH B . 
H 4 HOH 61  561 14  HOH HOH B . 
H 4 HOH 62  562 181 HOH HOH B . 
H 4 HOH 63  563 85  HOH HOH B . 
H 4 HOH 64  564 473 HOH HOH B . 
H 4 HOH 65  565 303 HOH HOH B . 
H 4 HOH 66  566 196 HOH HOH B . 
H 4 HOH 67  567 132 HOH HOH B . 
H 4 HOH 68  568 244 HOH HOH B . 
H 4 HOH 69  569 121 HOH HOH B . 
H 4 HOH 70  570 77  HOH HOH B . 
H 4 HOH 71  571 9   HOH HOH B . 
H 4 HOH 72  572 213 HOH HOH B . 
H 4 HOH 73  573 239 HOH HOH B . 
H 4 HOH 74  574 462 HOH HOH B . 
H 4 HOH 75  575 268 HOH HOH B . 
H 4 HOH 76  576 371 HOH HOH B . 
H 4 HOH 77  577 388 HOH HOH B . 
H 4 HOH 78  578 148 HOH HOH B . 
H 4 HOH 79  579 59  HOH HOH B . 
H 4 HOH 80  580 370 HOH HOH B . 
H 4 HOH 81  581 321 HOH HOH B . 
H 4 HOH 82  582 451 HOH HOH B . 
H 4 HOH 83  583 383 HOH HOH B . 
H 4 HOH 84  584 134 HOH HOH B . 
H 4 HOH 85  585 506 HOH HOH B . 
H 4 HOH 86  586 164 HOH HOH B . 
H 4 HOH 87  587 195 HOH HOH B . 
H 4 HOH 88  588 297 HOH HOH B . 
H 4 HOH 89  589 157 HOH HOH B . 
H 4 HOH 90  590 144 HOH HOH B . 
H 4 HOH 91  591 447 HOH HOH B . 
H 4 HOH 92  592 292 HOH HOH B . 
H 4 HOH 93  593 365 HOH HOH B . 
H 4 HOH 94  594 512 HOH HOH B . 
H 4 HOH 95  595 395 HOH HOH B . 
H 4 HOH 96  596 494 HOH HOH B . 
H 4 HOH 97  597 145 HOH HOH B . 
H 4 HOH 98  598 353 HOH HOH B . 
H 4 HOH 99  599 220 HOH HOH B . 
H 4 HOH 100 600 374 HOH HOH B . 
H 4 HOH 101 601 381 HOH HOH B . 
H 4 HOH 102 602 328 HOH HOH B . 
H 4 HOH 103 603 12  HOH HOH B . 
H 4 HOH 104 604 61  HOH HOH B . 
H 4 HOH 105 605 29  HOH HOH B . 
H 4 HOH 106 606 235 HOH HOH B . 
H 4 HOH 107 607 431 HOH HOH B . 
H 4 HOH 108 608 58  HOH HOH B . 
H 4 HOH 109 609 31  HOH HOH B . 
H 4 HOH 110 610 218 HOH HOH B . 
H 4 HOH 111 611 68  HOH HOH B . 
H 4 HOH 112 612 362 HOH HOH B . 
H 4 HOH 113 613 159 HOH HOH B . 
H 4 HOH 114 614 364 HOH HOH B . 
H 4 HOH 115 615 123 HOH HOH B . 
H 4 HOH 116 616 337 HOH HOH B . 
H 4 HOH 117 617 204 HOH HOH B . 
H 4 HOH 118 618 452 HOH HOH B . 
H 4 HOH 119 619 459 HOH HOH B . 
H 4 HOH 120 620 347 HOH HOH B . 
H 4 HOH 121 621 45  HOH HOH B . 
H 4 HOH 122 622 88  HOH HOH B . 
H 4 HOH 123 623 52  HOH HOH B . 
H 4 HOH 124 624 55  HOH HOH B . 
H 4 HOH 125 625 166 HOH HOH B . 
H 4 HOH 126 626 262 HOH HOH B . 
H 4 HOH 127 627 147 HOH HOH B . 
H 4 HOH 128 628 233 HOH HOH B . 
H 4 HOH 129 629 200 HOH HOH B . 
H 4 HOH 130 630 230 HOH HOH B . 
H 4 HOH 131 631 118 HOH HOH B . 
H 4 HOH 132 632 69  HOH HOH B . 
H 4 HOH 133 633 224 HOH HOH B . 
H 4 HOH 134 634 240 HOH HOH B . 
H 4 HOH 135 635 71  HOH HOH B . 
H 4 HOH 136 636 229 HOH HOH B . 
H 4 HOH 137 637 30  HOH HOH B . 
H 4 HOH 138 638 205 HOH HOH B . 
H 4 HOH 139 639 74  HOH HOH B . 
H 4 HOH 140 640 298 HOH HOH B . 
H 4 HOH 141 641 398 HOH HOH B . 
H 4 HOH 142 642 208 HOH HOH B . 
H 4 HOH 143 643 372 HOH HOH B . 
H 4 HOH 144 644 367 HOH HOH B . 
H 4 HOH 145 645 264 HOH HOH B . 
H 4 HOH 146 646 78  HOH HOH B . 
H 4 HOH 147 647 202 HOH HOH B . 
H 4 HOH 148 648 380 HOH HOH B . 
H 4 HOH 149 649 36  HOH HOH B . 
H 4 HOH 150 650 178 HOH HOH B . 
H 4 HOH 151 651 13  HOH HOH B . 
H 4 HOH 152 652 334 HOH HOH B . 
H 4 HOH 153 653 419 HOH HOH B . 
H 4 HOH 154 654 99  HOH HOH B . 
H 4 HOH 155 655 448 HOH HOH B . 
H 4 HOH 156 656 363 HOH HOH B . 
H 4 HOH 157 657 101 HOH HOH B . 
H 4 HOH 158 658 437 HOH HOH B . 
H 4 HOH 159 659 65  HOH HOH B . 
H 4 HOH 160 660 254 HOH HOH B . 
H 4 HOH 161 661 171 HOH HOH B . 
H 4 HOH 162 662 23  HOH HOH B . 
H 4 HOH 163 663 340 HOH HOH B . 
H 4 HOH 164 664 179 HOH HOH B . 
H 4 HOH 165 665 407 HOH HOH B . 
H 4 HOH 166 666 103 HOH HOH B . 
H 4 HOH 167 667 108 HOH HOH B . 
H 4 HOH 168 668 345 HOH HOH B . 
H 4 HOH 169 669 331 HOH HOH B . 
H 4 HOH 170 670 481 HOH HOH B . 
H 4 HOH 171 671 219 HOH HOH B . 
H 4 HOH 172 672 96  HOH HOH B . 
H 4 HOH 173 673 72  HOH HOH B . 
H 4 HOH 174 674 255 HOH HOH B . 
H 4 HOH 175 675 263 HOH HOH B . 
H 4 HOH 176 676 443 HOH HOH B . 
H 4 HOH 177 677 470 HOH HOH B . 
H 4 HOH 178 678 314 HOH HOH B . 
H 4 HOH 179 679 516 HOH HOH B . 
H 4 HOH 180 680 502 HOH HOH B . 
H 4 HOH 181 681 241 HOH HOH B . 
H 4 HOH 182 682 288 HOH HOH B . 
H 4 HOH 183 683 273 HOH HOH B . 
H 4 HOH 184 684 155 HOH HOH B . 
H 4 HOH 185 685 454 HOH HOH B . 
H 4 HOH 186 686 408 HOH HOH B . 
H 4 HOH 187 687 265 HOH HOH B . 
H 4 HOH 188 688 310 HOH HOH B . 
H 4 HOH 189 689 442 HOH HOH B . 
H 4 HOH 190 690 48  HOH HOH B . 
H 4 HOH 191 691 243 HOH HOH B . 
H 4 HOH 192 692 295 HOH HOH B . 
H 4 HOH 193 693 80  HOH HOH B . 
H 4 HOH 194 694 379 HOH HOH B . 
H 4 HOH 195 695 333 HOH HOH B . 
H 4 HOH 196 696 185 HOH HOH B . 
H 4 HOH 197 697 260 HOH HOH B . 
H 4 HOH 198 698 335 HOH HOH B . 
H 4 HOH 199 699 138 HOH HOH B . 
H 4 HOH 200 700 479 HOH HOH B . 
H 4 HOH 201 701 493 HOH HOH B . 
H 4 HOH 202 702 201 HOH HOH B . 
H 4 HOH 203 703 510 HOH HOH B . 
H 4 HOH 204 704 47  HOH HOH B . 
H 4 HOH 205 705 436 HOH HOH B . 
H 4 HOH 206 706 394 HOH HOH B . 
H 4 HOH 207 707 311 HOH HOH B . 
H 4 HOH 208 708 346 HOH HOH B . 
H 4 HOH 209 709 286 HOH HOH B . 
H 4 HOH 210 710 175 HOH HOH B . 
H 4 HOH 211 711 361 HOH HOH B . 
H 4 HOH 212 712 192 HOH HOH B . 
H 4 HOH 213 713 366 HOH HOH B . 
H 4 HOH 214 714 415 HOH HOH B . 
H 4 HOH 215 715 227 HOH HOH B . 
H 4 HOH 216 716 438 HOH HOH B . 
H 4 HOH 217 717 471 HOH HOH B . 
H 4 HOH 218 718 387 HOH HOH B . 
H 4 HOH 219 719 389 HOH HOH B . 
H 4 HOH 220 720 505 HOH HOH B . 
H 4 HOH 221 721 456 HOH HOH B . 
H 4 HOH 222 722 309 HOH HOH B . 
H 4 HOH 223 723 469 HOH HOH B . 
H 4 HOH 224 724 316 HOH HOH B . 
H 4 HOH 225 725 261 HOH HOH B . 
H 4 HOH 226 726 411 HOH HOH B . 
H 4 HOH 227 727 464 HOH HOH B . 
H 4 HOH 228 728 308 HOH HOH B . 
H 4 HOH 229 729 79  HOH HOH B . 
H 4 HOH 230 730 306 HOH HOH B . 
H 4 HOH 231 731 476 HOH HOH B . 
H 4 HOH 232 732 514 HOH HOH B . 
H 4 HOH 233 733 377 HOH HOH B . 
H 4 HOH 234 734 89  HOH HOH B . 
H 4 HOH 235 735 313 HOH HOH B . 
H 4 HOH 236 736 100 HOH HOH B . 
H 4 HOH 237 737 412 HOH HOH B . 
H 4 HOH 238 738 278 HOH HOH B . 
H 4 HOH 239 739 468 HOH HOH B . 
H 4 HOH 240 740 300 HOH HOH B . 
H 4 HOH 241 741 187 HOH HOH B . 
H 4 HOH 242 742 289 HOH HOH B . 
H 4 HOH 243 743 475 HOH HOH B . 
H 4 HOH 244 744 329 HOH HOH B . 
H 4 HOH 245 745 472 HOH HOH B . 
H 4 HOH 246 746 190 HOH HOH B . 
H 4 HOH 247 747 318 HOH HOH B . 
H 4 HOH 248 748 424 HOH HOH B . 
H 4 HOH 249 749 294 HOH HOH B . 
H 4 HOH 250 750 478 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 ASN 22  ? CG    ? A ASN 31  CG    
6   1 Y 1 A ASN 22  ? OD1   ? A ASN 31  OD1   
7   1 Y 1 A ASN 22  ? ND2   ? A ASN 31  ND2   
8   1 Y 1 A LYS 83  ? CG    ? A LYS 92  CG    
9   1 Y 1 A LYS 83  ? CD    ? A LYS 92  CD    
10  1 Y 1 A LYS 83  ? CE    ? A LYS 92  CE    
11  1 Y 1 A LYS 83  ? NZ    ? A LYS 92  NZ    
12  1 Y 1 A GLU 116 ? CG    ? A GLU 125 CG    
13  1 Y 1 A GLU 116 ? CD    ? A GLU 125 CD    
14  1 Y 1 A GLU 116 ? OE1   ? A GLU 125 OE1   
15  1 Y 1 A GLU 116 ? OE2   ? A GLU 125 OE2   
16  1 Y 1 A ARG 136 ? CG    ? A ARG 145 CG    
17  1 Y 1 A ARG 136 ? CD    ? A ARG 145 CD    
18  1 Y 1 A ARG 136 ? NE    ? A ARG 145 NE    
19  1 Y 1 A ARG 136 ? CZ    ? A ARG 145 CZ    
20  1 Y 1 A ARG 136 ? NH1   ? A ARG 145 NH1   
21  1 Y 1 A ARG 136 ? NH2   ? A ARG 145 NH2   
22  1 Y 1 A ARG 169 ? CG    ? A ARG 178 CG    
23  1 Y 1 A ARG 169 ? CD    ? A ARG 178 CD    
24  1 Y 1 A ARG 169 ? NE    ? A ARG 178 NE    
25  1 Y 1 A ARG 169 ? CZ    ? A ARG 178 CZ    
26  1 Y 1 A ARG 169 ? NH1   ? A ARG 178 NH1   
27  1 Y 1 A ARG 169 ? NH2   ? A ARG 178 NH2   
28  1 Y 1 A LYS 216 ? CG    ? A LYS 225 CG    
29  1 Y 1 A LYS 216 ? CD    ? A LYS 225 CD    
30  1 Y 1 A LYS 216 ? CE    ? A LYS 225 CE    
31  1 Y 1 A LYS 216 ? NZ    ? A LYS 225 NZ    
32  1 Y 1 A HIS 269 ? CG    ? A HIS 278 CG    
33  1 Y 1 A HIS 269 ? ND1   ? A HIS 278 ND1   
34  1 Y 1 A HIS 269 ? CD2   ? A HIS 278 CD2   
35  1 Y 1 A HIS 269 ? CE1   ? A HIS 278 CE1   
36  1 Y 1 A HIS 269 ? NE2   ? A HIS 278 NE2   
37  1 Y 1 A GLU 282 ? CG    ? A GLU 291 CG    
38  1 Y 1 A GLU 282 ? CD    ? A GLU 291 CD    
39  1 Y 1 A GLU 282 ? OE1   ? A GLU 291 OE1   
40  1 Y 1 A GLU 282 ? OE2   ? A GLU 291 OE2   
41  1 Y 1 A ASP 284 ? CG    ? A ASP 293 CG    
42  1 Y 1 A ASP 284 ? OD1   ? A ASP 293 OD1   
43  1 Y 1 A ASP 284 ? OD2   ? A ASP 293 OD2   
44  1 Y 1 A GLU 296 ? CG    ? A GLU 305 CG    
45  1 Y 1 A GLU 296 ? CD    ? A GLU 305 CD    
46  1 Y 1 A GLU 296 ? OE1   ? A GLU 305 OE1   
47  1 Y 1 A GLU 296 ? OE2   ? A GLU 305 OE2   
48  1 Y 1 A GLU 320 ? CG    ? A GLU 329 CG    
49  1 Y 1 A GLU 320 ? CD    ? A GLU 329 CD    
50  1 Y 1 A GLU 320 ? OE1   ? A GLU 329 OE1   
51  1 Y 1 A GLU 320 ? OE2   ? A GLU 329 OE2   
52  1 Y 1 A LYS 362 ? CG    ? A LYS 371 CG    
53  1 Y 1 A LYS 362 ? CD    ? A LYS 371 CD    
54  1 Y 1 A LYS 362 ? CE    ? A LYS 371 CE    
55  1 Y 1 A LYS 362 ? NZ    ? A LYS 371 NZ    
56  1 Y 1 B LYS 17  ? CG    ? B LYS 26  CG    
57  1 Y 1 B LYS 17  ? CD    ? B LYS 26  CD    
58  1 Y 1 B LYS 17  ? CE    ? B LYS 26  CE    
59  1 Y 1 B LYS 17  ? NZ    ? B LYS 26  NZ    
60  1 Y 1 B LYS 83  ? CG    ? B LYS 92  CG    
61  1 Y 1 B LYS 83  ? CD    ? B LYS 92  CD    
62  1 Y 1 B LYS 83  ? CE    ? B LYS 92  CE    
63  1 Y 1 B LYS 83  ? NZ    ? B LYS 92  NZ    
64  1 Y 1 B GLU 116 ? CG    ? B GLU 125 CG    
65  1 Y 1 B GLU 116 ? CD    ? B GLU 125 CD    
66  1 Y 1 B GLU 116 ? OE1   ? B GLU 125 OE1   
67  1 Y 1 B GLU 116 ? OE2   ? B GLU 125 OE2   
68  1 Y 1 B LYS 131 ? CG    ? B LYS 140 CG    
69  1 Y 1 B LYS 131 ? CD    ? B LYS 140 CD    
70  1 Y 1 B LYS 131 ? CE    ? B LYS 140 CE    
71  1 Y 1 B LYS 131 ? NZ    ? B LYS 140 NZ    
72  1 Y 1 B ARG 136 ? CG    ? B ARG 145 CG    
73  1 Y 1 B ARG 136 ? CD    ? B ARG 145 CD    
74  1 Y 1 B ARG 136 ? NE    ? B ARG 145 NE    
75  1 Y 1 B ARG 136 ? CZ    ? B ARG 145 CZ    
76  1 Y 1 B ARG 136 ? NH1   ? B ARG 145 NH1   
77  1 Y 1 B ARG 136 ? NH2   ? B ARG 145 NH2   
78  1 Y 1 B HIS 269 ? CG    ? B HIS 278 CG    
79  1 Y 1 B HIS 269 ? ND1   ? B HIS 278 ND1   
80  1 Y 1 B HIS 269 ? CD2   ? B HIS 278 CD2   
81  1 Y 1 B HIS 269 ? CE1   ? B HIS 278 CE1   
82  1 Y 1 B HIS 269 ? NE2   ? B HIS 278 NE2   
83  1 Y 1 B ASP 284 ? CG    ? B ASP 293 CG    
84  1 Y 1 B ASP 284 ? OD1   ? B ASP 293 OD1   
85  1 Y 1 B ASP 284 ? OD2   ? B ASP 293 OD2   
86  1 Y 1 B GLU 296 ? CG    ? B GLU 305 CG    
87  1 Y 1 B GLU 296 ? CD    ? B GLU 305 CD    
88  1 Y 1 B GLU 296 ? OE1   ? B GLU 305 OE1   
89  1 Y 1 B GLU 296 ? OE2   ? B GLU 305 OE2   
90  1 Y 1 B GLU 320 ? CG    ? B GLU 329 CG    
91  1 Y 1 B GLU 320 ? CD    ? B GLU 329 CD    
92  1 Y 1 B GLU 320 ? OE1   ? B GLU 329 OE1   
93  1 Y 1 B GLU 320 ? OE2   ? B GLU 329 OE2   
94  1 N 1 B TXP 402 ? "C5'" ? F TXP 1   "C5'" 
95  1 N 1 B TXP 402 ? "C4'" ? F TXP 1   "C4'" 
96  1 N 1 B TXP 402 ? "C3'" ? F TXP 1   "C3'" 
97  1 N 1 B TXP 402 ? "O4'" ? F TXP 1   "O4'" 
98  1 N 1 B TXP 402 ? "C1'" ? F TXP 1   "C1'" 
99  1 N 1 B TXP 402 ? "C2'" ? F TXP 1   "C2'" 
100 1 N 1 B TXP 402 ? "O2'" ? F TXP 1   "O2'" 
101 1 N 1 B TXP 402 ? P2    ? F TXP 1   P2    
102 1 N 1 B TXP 402 ? OP3   ? F TXP 1   OP3   
103 1 N 1 B TXP 402 ? OP2   ? F TXP 1   OP2   
104 1 N 1 B TXP 402 ? OP1   ? F TXP 1   OP1   
105 1 N 1 B TXP 402 ? C4A   ? F TXP 1   C4A   
106 1 N 1 B TXP 402 ? N3A   ? F TXP 1   N3A   
107 1 N 1 B TXP 402 ? C2A   ? F TXP 1   C2A   
108 1 N 1 B TXP 402 ? N1A   ? F TXP 1   N1A   
109 1 N 1 B TXP 402 ? C6A   ? F TXP 1   C6A   
110 1 N 1 B TXP 402 ? N6A   ? F TXP 1   N6A   
111 1 N 1 B TXP 402 ? C5A   ? F TXP 1   C5A   
112 1 N 1 B TXP 402 ? N7A   ? F TXP 1   N7A   
113 1 N 1 B TXP 402 ? C8A   ? F TXP 1   C8A   
# 
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 ? ? ? 1.21_5207 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .         4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.601 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FCN 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.322 
_cell.length_a_esd                 ? 
_cell.length_b                     93.996 
_cell.length_b_esd                 ? 
_cell.length_c                     89.275 
_cell.length_c_esd                 ? 
_cell.volume                       410248.499 
_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                         9FCN 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_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                   9FCN 
_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          47.03 
_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              7.5 
_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 Tris-HCl, 50 mM sodium tartrate, 16-20% 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         2023-07-23 
_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                          32.09 
_reflns.entry_id                                       9FCN 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.25 
_reflns.d_resolution_low                               45.41 
_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                                     50345 
_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                           98.19 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.35 
_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                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.2212 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.25 
_reflns_shell.d_res_low                                     2.31 
_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                             3357 
_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                                  0.21 
_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                                  4.257 
_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                               30.09 
_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                                 9FCN 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.25 
_refine.ls_d_res_low                             45.41 
_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                     37710 
_refine.ls_number_reflns_R_free                  1922 
_refine.ls_number_reflns_R_work                  35788 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.19 
_refine.ls_percent_reflns_R_free                 5.10 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1863 
_refine.ls_R_factor_R_free                       0.2348 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1837 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 25.9104 
_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                            0.3418 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.25 
_refine_hist.d_res_low                        45.41 
_refine_hist.number_atoms_solvent             485 
_refine_hist.number_atoms_total               6148 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5525 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         138 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0078  ? 5800 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6281  ? 7913 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0457  ? 876  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0037  ? 1006 ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.1604 ? 2081 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.25 2.31  . . 147 2374 92.07 . . . . 0.4034 . . . . . . . . . . . 0.4332 
'X-RAY DIFFRACTION' 2.31 2.37  . . 130 2596 99.56 . . . . 0.2757 . . . . . . . . . . . 0.3866 
'X-RAY DIFFRACTION' 2.37 2.44  . . 130 2578 99.67 . . . . 0.2414 . . . . . . . . . . . 0.2764 
'X-RAY DIFFRACTION' 2.44 2.52  . . 138 2561 99.52 . . . . 0.2069 . . . . . . . . . . . 0.2489 
'X-RAY DIFFRACTION' 2.52 2.61  . . 153 2618 99.89 . . . . 0.2102 . . . . . . . . . . . 0.2758 
'X-RAY DIFFRACTION' 2.61 2.71  . . 129 2567 99.41 . . . . 0.2140 . . . . . . . . . . . 0.2711 
'X-RAY DIFFRACTION' 2.71 2.83  . . 139 2529 98.27 . . . . 0.1906 . . . . . . . . . . . 0.2557 
'X-RAY DIFFRACTION' 2.83 2.98  . . 137 2517 96.76 . . . . 0.1873 . . . . . . . . . . . 0.2467 
'X-RAY DIFFRACTION' 2.98 3.17  . . 141 2492 96.02 . . . . 0.1868 . . . . . . . . . . . 0.2769 
'X-RAY DIFFRACTION' 3.17 3.42  . . 123 2469 94.53 . . . . 0.1834 . . . . . . . . . . . 0.2515 
'X-RAY DIFFRACTION' 3.42 3.76  . . 130 2601 99.56 . . . . 0.1701 . . . . . . . . . . . 0.2324 
'X-RAY DIFFRACTION' 3.76 4.30  . . 132 2613 99.96 . . . . 0.1492 . . . . . . . . . . . 0.2003 
'X-RAY DIFFRACTION' 4.30 5.42  . . 143 2629 99.96 . . . . 0.1407 . . . . . . . . . . . 0.1636 
'X-RAY DIFFRACTION' 5.42 45.41 . . 150 2644 99.50 . . . . 0.1663 . . . . . . . . . . . 0.1741 
# 
_struct.entry_id                     9FCN 
_struct.title                        'OPR3 loop swap variant L6(AchrOYE4) 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        9FCN 
_struct_keywords.text            'Flavoenzymes, ene-reductases, old yellow enzymes, coenzymes, 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 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP OPR3_SOLLC   Q9FEW9 ? 1 
;MASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTSAGFPHVPGI
FTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRAIGTYEI
SQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGADRVGVRVSP
AIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVT
;
1   
2 UNP I3V5V6_9BURK I3V5V6 ? 1 AEADWDDAPDMP 273 
3 UNP OPR3_SOLLC   Q9FEW9 ? 1 
;EEEEARLMRTLRNAYQGTFICSGGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVG
YTDYPFLQGNGSNGPLSRL
;
298 
# 
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 9FCN A 10  ? 289 ? Q9FEW9 1   ? 280 ? 1   280 
2 2 9FCN A 290 ? 301 ? I3V5V6 273 ? 284 ? 281 292 
3 3 9FCN A 302 ? 400 ? Q9FEW9 298 ? 396 ? 293 391 
4 1 9FCN B 10  ? 289 ? Q9FEW9 1   ? 280 ? 1   280 
5 2 9FCN B 290 ? 301 ? I3V5V6 273 ? 284 ? 281 292 
6 3 9FCN B 302 ? 400 ? Q9FEW9 298 ? 396 ? 293 391 
# 
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 9FCN MET A 1 ? UNP Q9FEW9 ? ? 'initiating methionine' -8 1  
1 9FCN ALA A 2 ? UNP Q9FEW9 ? ? 'expression tag'        -7 2  
1 9FCN SER A 3 ? UNP Q9FEW9 ? ? 'expression tag'        -6 3  
1 9FCN HIS A 4 ? UNP Q9FEW9 ? ? 'expression tag'        -5 4  
1 9FCN HIS A 5 ? UNP Q9FEW9 ? ? 'expression tag'        -4 5  
1 9FCN HIS A 6 ? UNP Q9FEW9 ? ? 'expression tag'        -3 6  
1 9FCN HIS A 7 ? UNP Q9FEW9 ? ? 'expression tag'        -2 7  
1 9FCN HIS A 8 ? UNP Q9FEW9 ? ? 'expression tag'        -1 8  
1 9FCN HIS A 9 ? UNP Q9FEW9 ? ? 'expression tag'        0  9  
4 9FCN MET B 1 ? UNP Q9FEW9 ? ? 'initiating methionine' -8 10 
4 9FCN ALA B 2 ? UNP Q9FEW9 ? ? 'expression tag'        -7 11 
4 9FCN SER B 3 ? UNP Q9FEW9 ? ? 'expression tag'        -6 12 
4 9FCN HIS B 4 ? UNP Q9FEW9 ? ? 'expression tag'        -5 13 
4 9FCN HIS B 5 ? UNP Q9FEW9 ? ? 'expression tag'        -4 14 
4 9FCN HIS B 6 ? UNP Q9FEW9 ? ? 'expression tag'        -3 15 
4 9FCN HIS B 7 ? UNP Q9FEW9 ? ? 'expression tag'        -2 16 
4 9FCN HIS B 8 ? UNP Q9FEW9 ? ? 'expression tag'        -1 17 
4 9FCN HIS B 9 ? UNP Q9FEW9 ? ? 'expression tag'        0  18 
# 
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 ARG A 307 ? TYR A 316 ? ARG A 298 TYR A 307 1 ? 10 
HELX_P HELX_P11 AB2 THR A 327 ? GLN A 337 ? THR A 318 GLN A 328 1 ? 11 
HELX_P HELX_P12 AB3 GLY A 346 ? ASN A 352 ? GLY A 337 ASN A 343 1 ? 7  
HELX_P HELX_P13 AB4 ASP A 354 ? ASN A 362 ? ASP A 345 ASN A 353 1 ? 9  
HELX_P HELX_P14 AB5 ASN A 369 ? PHE A 373 ? ASN A 360 PHE A 364 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 ? ALA B 186 ? GLY B 156 ALA B 177 1 ? 22 
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 ARG B 307 ? TYR B 316 ? ARG B 298 TYR B 307 1 ? 10 
HELX_P HELX_P26 AC8 THR B 327 ? GLN B 337 ? THR B 318 GLN B 328 1 ? 11 
HELX_P HELX_P27 AC9 GLY B 346 ? ASN B 352 ? GLY B 337 ASN B 343 1 ? 7  
HELX_P HELX_P28 AD1 ASP B 354 ? ASN B 362 ? ASP B 345 ASN B 353 1 ? 9  
HELX_P HELX_P29 AD2 ASN B 369 ? PHE B 373 ? ASN B 360 PHE B 364 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 9 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 9 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? parallel      
AA2 8 9 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? parallel      
AA6 6 7 ? parallel      
AA6 7 8 ? parallel      
AA6 8 9 ? parallel      
AA7 1 2 ? parallel      
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 25  ? MET A 27  ? TYR A 16  MET A 18  
AA1 2 PHE A 30  ? LEU A 32  ? PHE A 21  LEU A 23  
AA2 1 VAL A 36  ? LEU A 38  ? VAL A 27  LEU A 29  
AA2 2 PHE A 68  ? THR A 74  ? PHE A 59  THR A 65  
AA2 3 VAL A 111 ? LEU A 116 ? VAL A 102 LEU A 107 
AA2 4 GLY A 190 ? GLY A 195 ? GLY A 181 GLY A 186 
AA2 5 VAL A 243 ? VAL A 247 ? VAL A 234 VAL A 238 
AA2 6 TYR A 285 ? THR A 289 ? TYR A 276 THR A 280 
AA2 7 PHE A 320 ? SER A 323 ? PHE A 311 SER A 314 
AA2 8 LEU A 342 ? TYR A 345 ? LEU A 333 TYR A 336 
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  ? THR B 74  ? PHE B 59  THR B 65  
AA6 3 VAL B 111 ? LEU B 116 ? VAL B 102 LEU B 107 
AA6 4 GLY B 190 ? GLY B 195 ? GLY B 181 GLY B 186 
AA6 5 VAL B 243 ? VAL B 247 ? VAL B 234 VAL B 238 
AA6 6 TYR B 285 ? THR B 289 ? TYR B 276 THR B 280 
AA6 7 PHE B 320 ? SER B 323 ? PHE B 311 SER B 314 
AA6 8 LEU B 342 ? TYR B 345 ? LEU B 333 TYR B 336 
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 MET A 27  ? N MET A 18  O PHE A 30  ? O PHE A 21  
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 GLY A 244 ? O GLY A 235 
AA2 5 6 N VAL A 245 ? N VAL A 236 O HIS A 287 ? O HIS A 278 
AA2 6 7 N LEU A 286 ? N LEU A 277 O ILE A 321 ? O ILE A 312 
AA2 7 8 N CYS A 322 ? N CYS A 313 O SER A 344 ? O SER A 335 
AA2 8 9 O VAL A 343 ? O VAL A 334 N VAL A 37  ? N VAL A 28  
AA3 1 2 N SER A 136 ? N SER A 127 O ARG A 162 ? O ARG A 153 
AA4 1 2 N ILE A 148 ? N ILE A 139 O GLY A 156 ? O GLY A 147 
AA5 1 2 N TYR B 25  ? N TYR B 16  O LEU B 32  ? O LEU B 23  
AA6 1 2 N LEU B 38  ? N LEU B 29  O PHE B 68  ? O PHE B 59  
AA6 2 3 N LEU B 69  ? N LEU B 60  O VAL B 111 ? O VAL B 102 
AA6 3 4 N LEU B 116 ? N LEU B 107 O GLU B 192 ? O GLU B 183 
AA6 4 5 N ILE B 193 ? N ILE B 184 O GLY B 244 ? O GLY B 235 
AA6 5 6 N VAL B 245 ? N VAL B 236 O HIS B 287 ? O HIS B 278 
AA6 6 7 N LEU B 286 ? N LEU B 277 O ILE B 321 ? O ILE B 312 
AA6 7 8 N CYS B 322 ? N CYS B 313 O LEU B 342 ? O LEU B 333 
AA6 8 9 O TYR B 345 ? O TYR B 336 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                   9FCN 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    63 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    501 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.14 
# 
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  ? ? -142.09 28.24  
2 1 ASP A 284 ? ? -96.63  47.01  
3 1 ASP A 345 ? ? -96.94  47.81  
4 1 VAL A 370 ? ? -126.47 -53.29 
5 1 TYR A 373 ? ? -127.99 -59.01 
6 1 ILE B 80  ? ? -144.35 28.96  
7 1 ASP B 345 ? ? -98.39  49.18  
8 1 VAL B 370 ? ? -128.73 -54.44 
9 1 TYR B 373 ? ? -124.56 -60.87 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -8  ? A MET 1   
2  1 Y 1 A ALA -7  ? A ALA 2   
3  1 Y 1 A SER -6  ? A SER 3   
4  1 Y 1 A HIS -5  ? A HIS 4   
5  1 Y 1 A HIS -4  ? A HIS 5   
6  1 Y 1 A HIS -3  ? A HIS 6   
7  1 Y 1 A HIS -2  ? A HIS 7   
8  1 Y 1 A HIS -1  ? A HIS 8   
9  1 Y 1 A HIS 0   ? A HIS 9   
10 1 Y 1 A MET 1   ? A MET 10  
11 1 Y 1 A ALA 2   ? A ALA 11  
12 1 Y 1 A SER 3   ? A SER 12  
13 1 Y 1 A SER 4   ? A SER 13  
14 1 Y 1 A ALA 5   ? A ALA 14  
15 1 Y 1 A GLN 6   ? A GLN 15  
16 1 Y 1 A ASP 7   ? A ASP 16  
17 1 Y 1 A GLY 8   ? A GLY 17  
18 1 Y 1 A ASN 9   ? A ASN 18  
19 1 Y 1 A ASP 286 ? A ASP 295 
20 1 Y 1 A ASP 287 ? A ASP 296 
21 1 Y 1 A ALA 288 ? A ALA 297 
22 1 Y 1 A PRO 289 ? A PRO 298 
23 1 Y 1 A ASP 290 ? A ASP 299 
24 1 Y 1 A MET 291 ? A MET 300 
25 1 Y 1 A PRO 292 ? A PRO 301 
26 1 Y 1 A GLU 293 ? A GLU 302 
27 1 Y 1 A GLU 294 ? A GLU 303 
28 1 Y 1 A GLU 295 ? A GLU 304 
29 1 Y 1 A GLN 380 ? A GLN 389 
30 1 Y 1 A GLY 381 ? A GLY 390 
31 1 Y 1 A ASN 382 ? A ASN 391 
32 1 Y 1 A GLY 383 ? A GLY 392 
33 1 Y 1 A SER 384 ? A SER 393 
34 1 Y 1 A ASN 385 ? A ASN 394 
35 1 Y 1 A GLY 386 ? A GLY 395 
36 1 Y 1 A PRO 387 ? A PRO 396 
37 1 Y 1 A LEU 388 ? A LEU 397 
38 1 Y 1 A SER 389 ? A SER 398 
39 1 Y 1 A ARG 390 ? A ARG 399 
40 1 Y 1 A LEU 391 ? A LEU 400 
41 1 Y 1 B MET -8  ? B MET 1   
42 1 Y 1 B ALA -7  ? B ALA 2   
43 1 Y 1 B SER -6  ? B SER 3   
44 1 Y 1 B HIS -5  ? B HIS 4   
45 1 Y 1 B HIS -4  ? B HIS 5   
46 1 Y 1 B HIS -3  ? B HIS 6   
47 1 Y 1 B HIS -2  ? B HIS 7   
48 1 Y 1 B HIS -1  ? B HIS 8   
49 1 Y 1 B HIS 0   ? B HIS 9   
50 1 Y 1 B MET 1   ? B MET 10  
51 1 Y 1 B ALA 2   ? B ALA 11  
52 1 Y 1 B SER 3   ? B SER 12  
53 1 Y 1 B SER 4   ? B SER 13  
54 1 Y 1 B ALA 5   ? B ALA 14  
55 1 Y 1 B GLN 6   ? B GLN 15  
56 1 Y 1 B ASP 7   ? B ASP 16  
57 1 Y 1 B GLY 8   ? B GLY 17  
58 1 Y 1 B ASN 9   ? B ASN 18  
59 1 Y 1 B ASP 286 ? B ASP 295 
60 1 Y 1 B ASP 287 ? B ASP 296 
61 1 Y 1 B ALA 288 ? B ALA 297 
62 1 Y 1 B PRO 289 ? B PRO 298 
63 1 Y 1 B ASP 290 ? B ASP 299 
64 1 Y 1 B MET 291 ? B MET 300 
65 1 Y 1 B PRO 292 ? B PRO 301 
66 1 Y 1 B GLU 293 ? B GLU 302 
67 1 Y 1 B GLU 294 ? B GLU 303 
68 1 Y 1 B GLU 295 ? B GLU 304 
69 1 Y 1 B GLN 380 ? B GLN 389 
70 1 Y 1 B GLY 381 ? B GLY 390 
71 1 Y 1 B ASN 382 ? B ASN 391 
72 1 Y 1 B GLY 383 ? B GLY 392 
73 1 Y 1 B SER 384 ? B SER 393 
74 1 Y 1 B ASN 385 ? B ASN 394 
75 1 Y 1 B GLY 386 ? B GLY 395 
76 1 Y 1 B PRO 387 ? B PRO 396 
77 1 Y 1 B LEU 388 ? B LEU 397 
78 1 Y 1 B SER 389 ? B SER 398 
79 1 Y 1 B ARG 390 ? B ARG 399 
80 1 Y 1 B LEU 391 ? B LEU 400 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
FMN N1     N N N 88  
FMN C2     C N N 89  
FMN O2     O N N 90  
FMN N3     N N N 91  
FMN C4     C N N 92  
FMN O4     O N N 93  
FMN C4A    C N N 94  
FMN N5     N N N 95  
FMN C5A    C Y N 96  
FMN C6     C Y N 97  
FMN C7     C Y N 98  
FMN C7M    C N N 99  
FMN C8     C Y N 100 
FMN C8M    C N N 101 
FMN C9     C Y N 102 
FMN C9A    C Y N 103 
FMN N10    N N N 104 
FMN C10    C N N 105 
FMN "C1'"  C N N 106 
FMN "C2'"  C N S 107 
FMN "O2'"  O N N 108 
FMN "C3'"  C N S 109 
FMN "O3'"  O N N 110 
FMN "C4'"  C N R 111 
FMN "O4'"  O N N 112 
FMN "C5'"  C N N 113 
FMN "O5'"  O N N 114 
FMN P      P N N 115 
FMN O1P    O N N 116 
FMN O2P    O N N 117 
FMN O3P    O N N 118 
FMN HN3    H N N 119 
FMN H6     H N N 120 
FMN HM71   H N N 121 
FMN HM72   H N N 122 
FMN HM73   H N N 123 
FMN HM81   H N N 124 
FMN HM82   H N N 125 
FMN HM83   H N N 126 
FMN H9     H N N 127 
FMN "H1'1" H N N 128 
FMN "H1'2" H N N 129 
FMN "H2'"  H N N 130 
FMN "HO2'" H N N 131 
FMN "H3'"  H N N 132 
FMN "HO3'" H N N 133 
FMN "H4'"  H N N 134 
FMN "HO4'" H N N 135 
FMN "H5'1" H N N 136 
FMN "H5'2" H N N 137 
FMN HOP2   H N N 138 
FMN HOP3   H N N 139 
GLN N      N N N 140 
GLN CA     C N S 141 
GLN C      C N N 142 
GLN O      O N N 143 
GLN CB     C N N 144 
GLN CG     C N N 145 
GLN CD     C N N 146 
GLN OE1    O N N 147 
GLN NE2    N N N 148 
GLN OXT    O N N 149 
GLN H      H N N 150 
GLN H2     H N N 151 
GLN HA     H N N 152 
GLN HB2    H N N 153 
GLN HB3    H N N 154 
GLN HG2    H N N 155 
GLN HG3    H N N 156 
GLN HE21   H N N 157 
GLN HE22   H N N 158 
GLN HXT    H N N 159 
GLU N      N N N 160 
GLU CA     C N S 161 
GLU C      C N N 162 
GLU O      O N N 163 
GLU CB     C N N 164 
GLU CG     C N N 165 
GLU CD     C N N 166 
GLU OE1    O N N 167 
GLU OE2    O N N 168 
GLU OXT    O N N 169 
GLU H      H N N 170 
GLU H2     H N N 171 
GLU HA     H N N 172 
GLU HB2    H N N 173 
GLU HB3    H N N 174 
GLU HG2    H N N 175 
GLU HG3    H N N 176 
GLU HE2    H N N 177 
GLU HXT    H N N 178 
GLY N      N N N 179 
GLY CA     C N N 180 
GLY C      C N N 181 
GLY O      O N N 182 
GLY OXT    O N N 183 
GLY H      H N N 184 
GLY H2     H N N 185 
GLY HA2    H N N 186 
GLY HA3    H N N 187 
GLY HXT    H N N 188 
HIS N      N N N 189 
HIS CA     C N S 190 
HIS C      C N N 191 
HIS O      O N N 192 
HIS CB     C N N 193 
HIS CG     C Y N 194 
HIS ND1    N Y N 195 
HIS CD2    C Y N 196 
HIS CE1    C Y N 197 
HIS NE2    N Y N 198 
HIS OXT    O N N 199 
HIS H      H N N 200 
HIS H2     H N N 201 
HIS HA     H N N 202 
HIS HB2    H N N 203 
HIS HB3    H N N 204 
HIS HD1    H N N 205 
HIS HD2    H N N 206 
HIS HE1    H N N 207 
HIS HE2    H N N 208 
HIS HXT    H N N 209 
HOH O      O N N 210 
HOH H1     H N N 211 
HOH H2     H N N 212 
ILE N      N N N 213 
ILE CA     C N S 214 
ILE C      C N N 215 
ILE O      O N N 216 
ILE CB     C N S 217 
ILE CG1    C N N 218 
ILE CG2    C N N 219 
ILE CD1    C N N 220 
ILE OXT    O N N 221 
ILE H      H N N 222 
ILE H2     H N N 223 
ILE HA     H N N 224 
ILE HB     H N N 225 
ILE HG12   H N N 226 
ILE HG13   H N N 227 
ILE HG21   H N N 228 
ILE HG22   H N N 229 
ILE HG23   H N N 230 
ILE HD11   H N N 231 
ILE HD12   H N N 232 
ILE HD13   H N N 233 
ILE HXT    H N N 234 
LEU N      N N N 235 
LEU CA     C N S 236 
LEU C      C N N 237 
LEU O      O N N 238 
LEU CB     C N N 239 
LEU CG     C N N 240 
LEU CD1    C N N 241 
LEU CD2    C N N 242 
LEU OXT    O N N 243 
LEU H      H N N 244 
LEU H2     H N N 245 
LEU HA     H N N 246 
LEU HB2    H N N 247 
LEU HB3    H N N 248 
LEU HG     H N N 249 
LEU HD11   H N N 250 
LEU HD12   H N N 251 
LEU HD13   H N N 252 
LEU HD21   H N N 253 
LEU HD22   H N N 254 
LEU HD23   H N N 255 
LEU HXT    H N N 256 
LYS N      N N N 257 
LYS CA     C N S 258 
LYS C      C N N 259 
LYS O      O N N 260 
LYS CB     C N N 261 
LYS CG     C N N 262 
LYS CD     C N N 263 
LYS CE     C N N 264 
LYS NZ     N N N 265 
LYS OXT    O N N 266 
LYS H      H N N 267 
LYS H2     H N N 268 
LYS HA     H N N 269 
LYS HB2    H N N 270 
LYS HB3    H N N 271 
LYS HG2    H N N 272 
LYS HG3    H N N 273 
LYS HD2    H N N 274 
LYS HD3    H N N 275 
LYS HE2    H N N 276 
LYS HE3    H N N 277 
LYS HZ1    H N N 278 
LYS HZ2    H N N 279 
LYS HZ3    H N N 280 
LYS HXT    H N N 281 
MET N      N N N 282 
MET CA     C N S 283 
MET C      C N N 284 
MET O      O N N 285 
MET CB     C N N 286 
MET CG     C N N 287 
MET SD     S N N 288 
MET CE     C N N 289 
MET OXT    O N N 290 
MET H      H N N 291 
MET H2     H N N 292 
MET HA     H N N 293 
MET HB2    H N N 294 
MET HB3    H N N 295 
MET HG2    H N N 296 
MET HG3    H N N 297 
MET HE1    H N N 298 
MET HE2    H N N 299 
MET HE3    H N N 300 
MET HXT    H N N 301 
PHE N      N N N 302 
PHE CA     C N S 303 
PHE C      C N N 304 
PHE O      O N N 305 
PHE CB     C N N 306 
PHE CG     C Y N 307 
PHE CD1    C Y N 308 
PHE CD2    C Y N 309 
PHE CE1    C Y N 310 
PHE CE2    C Y N 311 
PHE CZ     C Y N 312 
PHE OXT    O N N 313 
PHE H      H N N 314 
PHE H2     H N N 315 
PHE HA     H N N 316 
PHE HB2    H N N 317 
PHE HB3    H N N 318 
PHE HD1    H N N 319 
PHE HD2    H N N 320 
PHE HE1    H N N 321 
PHE HE2    H N N 322 
PHE HZ     H N N 323 
PHE HXT    H N N 324 
PRO N      N N N 325 
PRO CA     C N S 326 
PRO C      C N N 327 
PRO O      O N N 328 
PRO CB     C N N 329 
PRO CG     C N N 330 
PRO CD     C N N 331 
PRO OXT    O N N 332 
PRO H      H N N 333 
PRO HA     H N N 334 
PRO HB2    H N N 335 
PRO HB3    H N N 336 
PRO HG2    H N N 337 
PRO HG3    H N N 338 
PRO HD2    H N N 339 
PRO HD3    H N N 340 
PRO HXT    H N N 341 
SER N      N N N 342 
SER CA     C N S 343 
SER C      C N N 344 
SER O      O N N 345 
SER CB     C N N 346 
SER OG     O N N 347 
SER OXT    O N N 348 
SER H      H N N 349 
SER H2     H N N 350 
SER HA     H N N 351 
SER HB2    H N N 352 
SER HB3    H N N 353 
SER HG     H N N 354 
SER HXT    H N N 355 
THR N      N N N 356 
THR CA     C N S 357 
THR C      C N N 358 
THR O      O N N 359 
THR CB     C N R 360 
THR OG1    O N N 361 
THR CG2    C N N 362 
THR OXT    O N N 363 
THR H      H N N 364 
THR H2     H N N 365 
THR HA     H N N 366 
THR HB     H N N 367 
THR HG1    H N N 368 
THR HG21   H N N 369 
THR HG22   H N N 370 
THR HG23   H N N 371 
THR HXT    H N N 372 
TRP N      N N N 373 
TRP CA     C N S 374 
TRP C      C N N 375 
TRP O      O N N 376 
TRP CB     C N N 377 
TRP CG     C Y N 378 
TRP CD1    C Y N 379 
TRP CD2    C Y N 380 
TRP NE1    N Y N 381 
TRP CE2    C Y N 382 
TRP CE3    C Y N 383 
TRP CZ2    C Y N 384 
TRP CZ3    C Y N 385 
TRP CH2    C Y N 386 
TRP OXT    O N N 387 
TRP H      H N N 388 
TRP H2     H N N 389 
TRP HA     H N N 390 
TRP HB2    H N N 391 
TRP HB3    H N N 392 
TRP HD1    H N N 393 
TRP HE1    H N N 394 
TRP HE3    H N N 395 
TRP HZ2    H N N 396 
TRP HZ3    H N N 397 
TRP HH2    H N N 398 
TRP HXT    H N N 399 
TXP O2N    O N N 400 
TXP PN     P N R 401 
TXP O1N    O N N 402 
TXP "O5'A" O N N 403 
TXP "C5'A" C N N 404 
TXP "C4'A" C N R 405 
TXP "C3'A" C N S 406 
TXP "O3'A" O N N 407 
TXP "C2'A" C N R 408 
TXP "O2'A" O N N 409 
TXP "C1'A" C N R 410 
TXP N1N    N N N 411 
TXP C6N    C N N 412 
TXP C5N    C N N 413 
TXP C4N    C N N 414 
TXP C3N    C N S 415 
TXP C7N    C N N 416 
TXP O7N    O N N 417 
TXP N7N    N N N 418 
TXP C2N    C N N 419 
TXP "O4'A" O N N 420 
TXP O3     O N N 421 
TXP PA     P N R 422 
TXP O1A    O N N 423 
TXP O2A    O N N 424 
TXP "O5'"  O N N 425 
TXP "C5'"  C N N 426 
TXP "C4'"  C N R 427 
TXP "C3'"  C N R 428 
TXP "O3'"  O N N 429 
TXP "O4'"  O N N 430 
TXP "C1'"  C N R 431 
TXP "C2'"  C N R 432 
TXP "O2'"  O N N 433 
TXP P2     P N N 434 
TXP OP3    O N N 435 
TXP OP2    O N N 436 
TXP OP1    O N N 437 
TXP N9A    N Y N 438 
TXP C4A    C Y N 439 
TXP N3A    N Y N 440 
TXP C2A    C Y N 441 
TXP N1A    N Y N 442 
TXP C6A    C Y N 443 
TXP N6A    N N N 444 
TXP C5A    C Y N 445 
TXP N7A    N Y N 446 
TXP C8A    C Y N 447 
TXP HO2N   H N N 448 
TXP "H5'1" H N N 449 
TXP "H5'2" H N N 450 
TXP "H4'A" H N N 451 
TXP "H3'A" H N N 452 
TXP HO3A   H N N 453 
TXP "H2'A" H N N 454 
TXP "HO2'" H N N 455 
TXP "H1'A" H N N 456 
TXP H6N1   H N N 457 
TXP H6N2   H N N 458 
TXP H5N    H N N 459 
TXP H4N    H N N 460 
TXP H7N1   H N N 461 
TXP H7N2   H N N 462 
TXP H2N1   H N N 463 
TXP H2N2   H N N 464 
TXP H3N    H N N 465 
TXP HO2A   H N N 466 
TXP "H5'A" H N N 467 
TXP "H5'B" H N N 468 
TXP "H4'"  H N N 469 
TXP "H3'"  H N N 470 
TXP "HO3'" H N N 471 
TXP "H1'"  H N N 472 
TXP "H2'"  H N N 473 
TXP HOP3   H N N 474 
TXP HOP2   H N N 475 
TXP H2A    H N N 476 
TXP H6A1   H N N 477 
TXP H6A2   H N N 478 
TXP H8A    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 
ALA N      CA     sing N N 1   
ALA N      H      sing N N 2   
ALA N      H2     sing N N 3   
ALA CA     C      sing N N 4   
ALA CA     CB     sing N N 5   
ALA CA     HA     sing N N 6   
ALA C      O      doub N N 7   
ALA C      OXT    sing N N 8   
ALA CB     HB1    sing N N 9   
ALA CB     HB2    sing N N 10  
ALA CB     HB3    sing N N 11  
ALA OXT    HXT    sing N N 12  
ARG N      CA     sing N N 13  
ARG N      H      sing N N 14  
ARG N      H2     sing N N 15  
ARG CA     C      sing N N 16  
ARG CA     CB     sing N N 17  
ARG CA     HA     sing N N 18  
ARG C      O      doub N N 19  
ARG C      OXT    sing N N 20  
ARG CB     CG     sing N N 21  
ARG CB     HB2    sing N N 22  
ARG CB     HB3    sing N N 23  
ARG CG     CD     sing N N 24  
ARG CG     HG2    sing N N 25  
ARG CG     HG3    sing N N 26  
ARG CD     NE     sing N N 27  
ARG CD     HD2    sing N N 28  
ARG CD     HD3    sing N N 29  
ARG NE     CZ     sing N N 30  
ARG NE     HE     sing N N 31  
ARG CZ     NH1    sing N N 32  
ARG CZ     NH2    doub N N 33  
ARG NH1    HH11   sing N N 34  
ARG NH1    HH12   sing N N 35  
ARG NH2    HH21   sing N N 36  
ARG NH2    HH22   sing N N 37  
ARG OXT    HXT    sing N N 38  
ASN N      CA     sing N N 39  
ASN N      H      sing N N 40  
ASN N      H2     sing N N 41  
ASN CA     C      sing N N 42  
ASN CA     CB     sing N N 43  
ASN CA     HA     sing N N 44  
ASN C      O      doub N N 45  
ASN C      OXT    sing N N 46  
ASN CB     CG     sing N N 47  
ASN CB     HB2    sing N N 48  
ASN CB     HB3    sing N N 49  
ASN CG     OD1    doub N N 50  
ASN CG     ND2    sing N N 51  
ASN ND2    HD21   sing N N 52  
ASN ND2    HD22   sing N N 53  
ASN OXT    HXT    sing N N 54  
ASP N      CA     sing N N 55  
ASP N      H      sing N N 56  
ASP N      H2     sing N N 57  
ASP CA     C      sing N N 58  
ASP CA     CB     sing N N 59  
ASP CA     HA     sing N N 60  
ASP C      O      doub N N 61  
ASP C      OXT    sing N N 62  
ASP CB     CG     sing N N 63  
ASP CB     HB2    sing N N 64  
ASP CB     HB3    sing N N 65  
ASP CG     OD1    doub N N 66  
ASP CG     OD2    sing N N 67  
ASP OD2    HD2    sing N N 68  
ASP OXT    HXT    sing N N 69  
CYS N      CA     sing N N 70  
CYS N      H      sing N N 71  
CYS N      H2     sing N N 72  
CYS CA     C      sing N N 73  
CYS CA     CB     sing N N 74  
CYS CA     HA     sing N N 75  
CYS C      O      doub N N 76  
CYS C      OXT    sing N N 77  
CYS CB     SG     sing N N 78  
CYS CB     HB2    sing N N 79  
CYS CB     HB3    sing N N 80  
CYS SG     HG     sing N N 81  
CYS OXT    HXT    sing N N 82  
FMN N1     C2     sing N N 83  
FMN N1     C10    doub N N 84  
FMN C2     O2     doub N N 85  
FMN C2     N3     sing N N 86  
FMN N3     C4     sing N N 87  
FMN N3     HN3    sing N N 88  
FMN C4     O4     doub N N 89  
FMN C4     C4A    sing N N 90  
FMN C4A    N5     doub N N 91  
FMN C4A    C10    sing N N 92  
FMN N5     C5A    sing N N 93  
FMN C5A    C6     doub Y N 94  
FMN C5A    C9A    sing Y N 95  
FMN C6     C7     sing Y N 96  
FMN C6     H6     sing N N 97  
FMN C7     C7M    sing N N 98  
FMN C7     C8     doub Y N 99  
FMN C7M    HM71   sing N N 100 
FMN C7M    HM72   sing N N 101 
FMN C7M    HM73   sing N N 102 
FMN C8     C8M    sing N N 103 
FMN C8     C9     sing Y N 104 
FMN C8M    HM81   sing N N 105 
FMN C8M    HM82   sing N N 106 
FMN C8M    HM83   sing N N 107 
FMN C9     C9A    doub Y N 108 
FMN C9     H9     sing N N 109 
FMN C9A    N10    sing N N 110 
FMN N10    C10    sing N N 111 
FMN N10    "C1'"  sing N N 112 
FMN "C1'"  "C2'"  sing N N 113 
FMN "C1'"  "H1'1" sing N N 114 
FMN "C1'"  "H1'2" sing N N 115 
FMN "C2'"  "O2'"  sing N N 116 
FMN "C2'"  "C3'"  sing N N 117 
FMN "C2'"  "H2'"  sing N N 118 
FMN "O2'"  "HO2'" sing N N 119 
FMN "C3'"  "O3'"  sing N N 120 
FMN "C3'"  "C4'"  sing N N 121 
FMN "C3'"  "H3'"  sing N N 122 
FMN "O3'"  "HO3'" sing N N 123 
FMN "C4'"  "O4'"  sing N N 124 
FMN "C4'"  "C5'"  sing N N 125 
FMN "C4'"  "H4'"  sing N N 126 
FMN "O4'"  "HO4'" sing N N 127 
FMN "C5'"  "O5'"  sing N N 128 
FMN "C5'"  "H5'1" sing N N 129 
FMN "C5'"  "H5'2" sing N N 130 
FMN "O5'"  P      sing N N 131 
FMN P      O1P    doub N N 132 
FMN P      O2P    sing N N 133 
FMN P      O3P    sing N N 134 
FMN O2P    HOP2   sing N N 135 
FMN O3P    HOP3   sing N N 136 
GLN N      CA     sing N N 137 
GLN N      H      sing N N 138 
GLN N      H2     sing N N 139 
GLN CA     C      sing N N 140 
GLN CA     CB     sing N N 141 
GLN CA     HA     sing N N 142 
GLN C      O      doub N N 143 
GLN C      OXT    sing N N 144 
GLN CB     CG     sing N N 145 
GLN CB     HB2    sing N N 146 
GLN CB     HB3    sing N N 147 
GLN CG     CD     sing N N 148 
GLN CG     HG2    sing N N 149 
GLN CG     HG3    sing N N 150 
GLN CD     OE1    doub N N 151 
GLN CD     NE2    sing N N 152 
GLN NE2    HE21   sing N N 153 
GLN NE2    HE22   sing N N 154 
GLN OXT    HXT    sing N N 155 
GLU N      CA     sing N N 156 
GLU N      H      sing N N 157 
GLU N      H2     sing N N 158 
GLU CA     C      sing N N 159 
GLU CA     CB     sing N N 160 
GLU CA     HA     sing N N 161 
GLU C      O      doub N N 162 
GLU C      OXT    sing N N 163 
GLU CB     CG     sing N N 164 
GLU CB     HB2    sing N N 165 
GLU CB     HB3    sing N N 166 
GLU CG     CD     sing N N 167 
GLU CG     HG2    sing N N 168 
GLU CG     HG3    sing N N 169 
GLU CD     OE1    doub N N 170 
GLU CD     OE2    sing N N 171 
GLU OE2    HE2    sing N N 172 
GLU OXT    HXT    sing N N 173 
GLY N      CA     sing N N 174 
GLY N      H      sing N N 175 
GLY N      H2     sing N N 176 
GLY CA     C      sing N N 177 
GLY CA     HA2    sing N N 178 
GLY CA     HA3    sing N N 179 
GLY C      O      doub N N 180 
GLY C      OXT    sing N N 181 
GLY OXT    HXT    sing N N 182 
HIS N      CA     sing N N 183 
HIS N      H      sing N N 184 
HIS N      H2     sing N N 185 
HIS CA     C      sing N N 186 
HIS CA     CB     sing N N 187 
HIS CA     HA     sing N N 188 
HIS C      O      doub N N 189 
HIS C      OXT    sing N N 190 
HIS CB     CG     sing N N 191 
HIS CB     HB2    sing N N 192 
HIS CB     HB3    sing N N 193 
HIS CG     ND1    sing Y N 194 
HIS CG     CD2    doub Y N 195 
HIS ND1    CE1    doub Y N 196 
HIS ND1    HD1    sing N N 197 
HIS CD2    NE2    sing Y N 198 
HIS CD2    HD2    sing N N 199 
HIS CE1    NE2    sing Y N 200 
HIS CE1    HE1    sing N N 201 
HIS NE2    HE2    sing N N 202 
HIS OXT    HXT    sing N N 203 
HOH O      H1     sing N N 204 
HOH O      H2     sing N N 205 
ILE N      CA     sing N N 206 
ILE N      H      sing N N 207 
ILE N      H2     sing N N 208 
ILE CA     C      sing N N 209 
ILE CA     CB     sing N N 210 
ILE CA     HA     sing N N 211 
ILE C      O      doub N N 212 
ILE C      OXT    sing N N 213 
ILE CB     CG1    sing N N 214 
ILE CB     CG2    sing N N 215 
ILE CB     HB     sing N N 216 
ILE CG1    CD1    sing N N 217 
ILE CG1    HG12   sing N N 218 
ILE CG1    HG13   sing N N 219 
ILE CG2    HG21   sing N N 220 
ILE CG2    HG22   sing N N 221 
ILE CG2    HG23   sing N N 222 
ILE CD1    HD11   sing N N 223 
ILE CD1    HD12   sing N N 224 
ILE CD1    HD13   sing N N 225 
ILE OXT    HXT    sing N N 226 
LEU N      CA     sing N N 227 
LEU N      H      sing N N 228 
LEU N      H2     sing N N 229 
LEU CA     C      sing N N 230 
LEU CA     CB     sing N N 231 
LEU CA     HA     sing N N 232 
LEU C      O      doub N N 233 
LEU C      OXT    sing N N 234 
LEU CB     CG     sing N N 235 
LEU CB     HB2    sing N N 236 
LEU CB     HB3    sing N N 237 
LEU CG     CD1    sing N N 238 
LEU CG     CD2    sing N N 239 
LEU CG     HG     sing N N 240 
LEU CD1    HD11   sing N N 241 
LEU CD1    HD12   sing N N 242 
LEU CD1    HD13   sing N N 243 
LEU CD2    HD21   sing N N 244 
LEU CD2    HD22   sing N N 245 
LEU CD2    HD23   sing N N 246 
LEU OXT    HXT    sing N N 247 
LYS N      CA     sing N N 248 
LYS N      H      sing N N 249 
LYS N      H2     sing N N 250 
LYS CA     C      sing N N 251 
LYS CA     CB     sing N N 252 
LYS CA     HA     sing N N 253 
LYS C      O      doub N N 254 
LYS C      OXT    sing N N 255 
LYS CB     CG     sing N N 256 
LYS CB     HB2    sing N N 257 
LYS CB     HB3    sing N N 258 
LYS CG     CD     sing N N 259 
LYS CG     HG2    sing N N 260 
LYS CG     HG3    sing N N 261 
LYS CD     CE     sing N N 262 
LYS CD     HD2    sing N N 263 
LYS CD     HD3    sing N N 264 
LYS CE     NZ     sing N N 265 
LYS CE     HE2    sing N N 266 
LYS CE     HE3    sing N N 267 
LYS NZ     HZ1    sing N N 268 
LYS NZ     HZ2    sing N N 269 
LYS NZ     HZ3    sing N N 270 
LYS OXT    HXT    sing N N 271 
MET N      CA     sing N N 272 
MET N      H      sing N N 273 
MET N      H2     sing N N 274 
MET CA     C      sing N N 275 
MET CA     CB     sing N N 276 
MET CA     HA     sing N N 277 
MET C      O      doub N N 278 
MET C      OXT    sing N N 279 
MET CB     CG     sing N N 280 
MET CB     HB2    sing N N 281 
MET CB     HB3    sing N N 282 
MET CG     SD     sing N N 283 
MET CG     HG2    sing N N 284 
MET CG     HG3    sing N N 285 
MET SD     CE     sing N N 286 
MET CE     HE1    sing N N 287 
MET CE     HE2    sing N N 288 
MET CE     HE3    sing N N 289 
MET OXT    HXT    sing N N 290 
PHE N      CA     sing N N 291 
PHE N      H      sing N N 292 
PHE N      H2     sing N N 293 
PHE CA     C      sing N N 294 
PHE CA     CB     sing N N 295 
PHE CA     HA     sing N N 296 
PHE C      O      doub N N 297 
PHE C      OXT    sing N N 298 
PHE CB     CG     sing N N 299 
PHE CB     HB2    sing N N 300 
PHE CB     HB3    sing N N 301 
PHE CG     CD1    doub Y N 302 
PHE CG     CD2    sing Y N 303 
PHE CD1    CE1    sing Y N 304 
PHE CD1    HD1    sing N N 305 
PHE CD2    CE2    doub Y N 306 
PHE CD2    HD2    sing N N 307 
PHE CE1    CZ     doub Y N 308 
PHE CE1    HE1    sing N N 309 
PHE CE2    CZ     sing Y N 310 
PHE CE2    HE2    sing N N 311 
PHE CZ     HZ     sing N N 312 
PHE OXT    HXT    sing N N 313 
PRO N      CA     sing N N 314 
PRO N      CD     sing N N 315 
PRO N      H      sing N N 316 
PRO CA     C      sing N N 317 
PRO CA     CB     sing N N 318 
PRO CA     HA     sing N N 319 
PRO C      O      doub N N 320 
PRO C      OXT    sing N N 321 
PRO CB     CG     sing N N 322 
PRO CB     HB2    sing N N 323 
PRO CB     HB3    sing N N 324 
PRO CG     CD     sing N N 325 
PRO CG     HG2    sing N N 326 
PRO CG     HG3    sing N N 327 
PRO CD     HD2    sing N N 328 
PRO CD     HD3    sing N N 329 
PRO OXT    HXT    sing N N 330 
SER N      CA     sing N N 331 
SER N      H      sing N N 332 
SER N      H2     sing N N 333 
SER CA     C      sing N N 334 
SER CA     CB     sing N N 335 
SER CA     HA     sing N N 336 
SER C      O      doub N N 337 
SER C      OXT    sing N N 338 
SER CB     OG     sing N N 339 
SER CB     HB2    sing N N 340 
SER CB     HB3    sing N N 341 
SER OG     HG     sing N N 342 
SER OXT    HXT    sing N N 343 
THR N      CA     sing N N 344 
THR N      H      sing N N 345 
THR N      H2     sing N N 346 
THR CA     C      sing N N 347 
THR CA     CB     sing N N 348 
THR CA     HA     sing N N 349 
THR C      O      doub N N 350 
THR C      OXT    sing N N 351 
THR CB     OG1    sing N N 352 
THR CB     CG2    sing N N 353 
THR CB     HB     sing N N 354 
THR OG1    HG1    sing N N 355 
THR CG2    HG21   sing N N 356 
THR CG2    HG22   sing N N 357 
THR CG2    HG23   sing N N 358 
THR OXT    HXT    sing N N 359 
TRP N      CA     sing N N 360 
TRP N      H      sing N N 361 
TRP N      H2     sing N N 362 
TRP CA     C      sing N N 363 
TRP CA     CB     sing N N 364 
TRP CA     HA     sing N N 365 
TRP C      O      doub N N 366 
TRP C      OXT    sing N N 367 
TRP CB     CG     sing N N 368 
TRP CB     HB2    sing N N 369 
TRP CB     HB3    sing N N 370 
TRP CG     CD1    doub Y N 371 
TRP CG     CD2    sing Y N 372 
TRP CD1    NE1    sing Y N 373 
TRP CD1    HD1    sing N N 374 
TRP CD2    CE2    doub Y N 375 
TRP CD2    CE3    sing Y N 376 
TRP NE1    CE2    sing Y N 377 
TRP NE1    HE1    sing N N 378 
TRP CE2    CZ2    sing Y N 379 
TRP CE3    CZ3    doub Y N 380 
TRP CE3    HE3    sing N N 381 
TRP CZ2    CH2    doub Y N 382 
TRP CZ2    HZ2    sing N N 383 
TRP CZ3    CH2    sing Y N 384 
TRP CZ3    HZ3    sing N N 385 
TRP CH2    HH2    sing N N 386 
TRP OXT    HXT    sing N N 387 
TXP O2N    PN     sing N N 388 
TXP O2N    HO2N   sing N N 389 
TXP PN     O1N    doub N N 390 
TXP PN     O3     sing N N 391 
TXP PN     "O5'A" sing N N 392 
TXP "O5'A" "C5'A" sing N N 393 
TXP "C5'A" "C4'A" sing N N 394 
TXP "C5'A" "H5'1" sing N N 395 
TXP "C5'A" "H5'2" sing N N 396 
TXP "C4'A" "C3'A" sing N N 397 
TXP "C4'A" "O4'A" sing N N 398 
TXP "C4'A" "H4'A" sing N N 399 
TXP "C3'A" "O3'A" sing N N 400 
TXP "C3'A" "C2'A" sing N N 401 
TXP "C3'A" "H3'A" sing N N 402 
TXP "O3'A" HO3A   sing N N 403 
TXP "C2'A" "C1'A" sing N N 404 
TXP "C2'A" "O2'A" sing N N 405 
TXP "C2'A" "H2'A" sing N N 406 
TXP "O2'A" "HO2'" sing N N 407 
TXP "C1'A" "O4'A" sing N N 408 
TXP "C1'A" N1N    sing N N 409 
TXP "C1'A" "H1'A" sing N N 410 
TXP N1N    C2N    sing N N 411 
TXP N1N    C6N    sing N N 412 
TXP C6N    C5N    sing N N 413 
TXP C6N    H6N1   sing N N 414 
TXP C6N    H6N2   sing N N 415 
TXP C5N    C4N    doub N N 416 
TXP C5N    H5N    sing N N 417 
TXP C4N    C3N    sing N N 418 
TXP C4N    H4N    sing N N 419 
TXP C3N    C2N    sing N N 420 
TXP C3N    H3N    sing N N 421 
TXP C3N    C7N    sing N N 422 
TXP C7N    N7N    sing N N 423 
TXP C7N    O7N    doub N N 424 
TXP N7N    H7N1   sing N N 425 
TXP N7N    H7N2   sing N N 426 
TXP C2N    H2N1   sing N N 427 
TXP C2N    H2N2   sing N N 428 
TXP O3     PA     sing N N 429 
TXP PA     "O5'"  sing N N 430 
TXP PA     O1A    doub N N 431 
TXP PA     O2A    sing N N 432 
TXP O2A    HO2A   sing N N 433 
TXP "O5'"  "C5'"  sing N N 434 
TXP "C5'"  "C4'"  sing N N 435 
TXP "C5'"  "H5'A" sing N N 436 
TXP "C5'"  "H5'B" sing N N 437 
TXP "C4'"  "O4'"  sing N N 438 
TXP "C4'"  "C3'"  sing N N 439 
TXP "C4'"  "H4'"  sing N N 440 
TXP "C3'"  "C2'"  sing N N 441 
TXP "C3'"  "O3'"  sing N N 442 
TXP "C3'"  "H3'"  sing N N 443 
TXP "O3'"  "HO3'" sing N N 444 
TXP "O4'"  "C1'"  sing N N 445 
TXP "C1'"  N9A    sing N N 446 
TXP "C1'"  "C2'"  sing N N 447 
TXP "C1'"  "H1'"  sing N N 448 
TXP "C2'"  "O2'"  sing N N 449 
TXP "C2'"  "H2'"  sing N N 450 
TXP "O2'"  P2     sing N N 451 
TXP P2     OP1    doub N N 452 
TXP P2     OP2    sing N N 453 
TXP P2     OP3    sing N N 454 
TXP OP3    HOP3   sing N N 455 
TXP OP2    HOP2   sing N N 456 
TXP N9A    C4A    sing Y N 457 
TXP N9A    C8A    sing Y N 458 
TXP C4A    N3A    doub Y N 459 
TXP C4A    C5A    sing Y N 460 
TXP N3A    C2A    sing Y N 461 
TXP C2A    N1A    doub Y N 462 
TXP C2A    H2A    sing N N 463 
TXP N1A    C6A    sing Y N 464 
TXP C6A    N6A    sing N N 465 
TXP C6A    C5A    doub Y N 466 
TXP N6A    H6A1   sing N N 467 
TXP N6A    H6A2   sing N N 468 
TXP C5A    N7A    sing Y N 469 
TXP N7A    C8A    doub Y N 470 
TXP C8A    H8A    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          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9FCN 
_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]   0.020275 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002706 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010639 
_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]   0.011301 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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  ? 0.31400  -19.16500 10.50600  1.000 35.52636  ? 10  ASN A N      1 
ATOM   2    C CA     . ASN A 1 19  ? 1.56200  -18.57600 10.03700  1.000 36.96139  ? 10  ASN A CA     1 
ATOM   3    C C      . ASN A 1 19  ? 1.60700  -17.08800 10.36600  1.000 39.18375  ? 10  ASN A C      1 
ATOM   4    O O      . ASN A 1 19  ? 0.86400  -16.29600 9.78600   1.000 39.38676  ? 10  ASN A O      1 
ATOM   5    C CB     . ASN A 1 19  ? 1.72700  -18.79300 8.53100   1.000 36.80235  ? 10  ASN A CB     1 
ATOM   6    C CG     . ASN A 1 19  ? 3.15600  -18.58000 8.06000   1.000 39.80353  ? 10  ASN A CG     1 
ATOM   7    O OD1    . ASN A 1 19  ? 3.92200  -17.83200 8.67000   1.000 36.95795  ? 10  ASN A OD1    1 
ATOM   8    N ND2    . ASN A 1 19  ? 3.52200  -19.24100 6.96700   1.000 34.12868  ? 10  ASN A ND2    1 
ATOM   9    N N      . PRO A 1 20  ? 2.48400  -16.70600 11.30000  1.000 36.04651  ? 11  PRO A N      1 
ATOM   10   C CA     . PRO A 1 20  ? 2.57600  -15.28700 11.67700  1.000 35.63217  ? 11  PRO A CA     1 
ATOM   11   C C      . PRO A 1 20  ? 3.16100  -14.40100 10.59000  1.000 31.94118  ? 11  PRO A C      1 
ATOM   12   O O      . PRO A 1 20  ? 2.95200  -13.18200 10.63400  1.000 31.16394  ? 11  PRO A O      1 
ATOM   13   C CB     . PRO A 1 20  ? 3.47400  -15.31200 12.92200  1.000 30.83414  ? 11  PRO A CB     1 
ATOM   14   C CG     . PRO A 1 20  ? 4.29600  -16.54600 12.76100  1.000 36.04244  ? 11  PRO A CG     1 
ATOM   15   C CD     . PRO A 1 20  ? 3.41000  -17.55000 12.07300  1.000 34.86513  ? 11  PRO A CD     1 
ATOM   16   N N      . LEU A 1 21  ? 3.88000  -14.96400 9.61600   1.000 35.78553  ? 12  LEU A N      1 
ATOM   17   C CA     . LEU A 1 21  ? 4.41700  -14.15300 8.52900   1.000 31.92854  ? 12  LEU A CA     1 
ATOM   18   C C      . LEU A 1 21  ? 3.32400  -13.56300 7.64800   1.000 34.45315  ? 12  LEU A C      1 
ATOM   19   O O      . LEU A 1 21  ? 3.59300  -12.61700 6.90000   1.000 36.60162  ? 12  LEU A O      1 
ATOM   20   C CB     . LEU A 1 21  ? 5.37500  -14.98000 7.66900   1.000 31.76794  ? 12  LEU A CB     1 
ATOM   21   C CG     . LEU A 1 21  ? 6.77800  -15.21800 8.23000   1.000 34.30704  ? 12  LEU A CG     1 
ATOM   22   C CD1    . LEU A 1 21  ? 7.58500  -16.10100 7.29200   1.000 25.80353  ? 12  LEU A CD1    1 
ATOM   23   C CD2    . LEU A 1 21  ? 7.48600  -13.89300 8.46100   1.000 29.93841  ? 12  LEU A CD2    1 
ATOM   24   N N      . PHE A 1 22  ? 2.10300  -14.09200 7.71800   1.000 33.37061  ? 13  PHE A N      1 
ATOM   25   C CA     . PHE A 1 22  ? 1.01000  -13.63200 6.87300   1.000 34.84992  ? 13  PHE A CA     1 
ATOM   26   C C      . PHE A 1 22  ? -0.10500 -12.96500 7.67000   1.000 35.58630  ? 13  PHE A C      1 
ATOM   27   O O      . PHE A 1 22  ? -1.24100 -12.88000 7.19400   1.000 41.56690  ? 13  PHE A O      1 
ATOM   28   C CB     . PHE A 1 22  ? 0.47300  -14.79000 6.03300   1.000 31.88297  ? 13  PHE A CB     1 
ATOM   29   C CG     . PHE A 1 22  ? 1.41900  -15.22100 4.95200   1.000 32.93154  ? 13  PHE A CG     1 
ATOM   30   C CD1    . PHE A 1 22  ? 2.42600  -16.13500 5.21700   1.000 31.94163  ? 13  PHE A CD1    1 
ATOM   31   C CD2    . PHE A 1 22  ? 1.32600  -14.68200 3.68100   1.000 33.16620  ? 13  PHE A CD2    1 
ATOM   32   C CE1    . PHE A 1 22  ? 3.30800  -16.51800 4.22800   1.000 35.47490  ? 13  PHE A CE1    1 
ATOM   33   C CE2    . PHE A 1 22  ? 2.20500  -15.06200 2.68700   1.000 31.89921  ? 13  PHE A CE2    1 
ATOM   34   C CZ     . PHE A 1 22  ? 3.19900  -15.97800 2.96200   1.000 33.40146  ? 13  PHE A CZ     1 
ATOM   35   N N      . SER A 1 23  ? 0.19700  -12.49300 8.87100   1.000 37.37657  ? 14  SER A N      1 
ATOM   36   C CA     . SER A 1 23  ? -0.71600 -11.56900 9.52100   1.000 34.81544  ? 14  SER A CA     1 
ATOM   37   C C      . SER A 1 23  ? -0.42200 -10.15000 9.03900   1.000 35.06612  ? 14  SER A C      1 
ATOM   38   O O      . SER A 1 23  ? 0.73600  -9.81000  8.78500   1.000 32.57869  ? 14  SER A O      1 
ATOM   39   C CB     . SER A 1 23  ? -0.57800 -11.64600 11.04100  1.000 33.24881  ? 14  SER A CB     1 
ATOM   40   O OG     . SER A 1 23  ? 0.70400  -11.21600 11.46500  1.000 38.05304  ? 14  SER A OG     1 
ATOM   41   N N      . PRO A 1 24  ? -1.44200 -9.31000  8.88700   1.000 32.24253  ? 15  PRO A N      1 
ATOM   42   C CA     . PRO A 1 24  ? -1.20800 -7.96100  8.36400   1.000 31.49686  ? 15  PRO A CA     1 
ATOM   43   C C      . PRO A 1 24  ? -0.39600 -7.11400  9.33200   1.000 30.68819  ? 15  PRO A C      1 
ATOM   44   O O      . PRO A 1 24  ? -0.33600 -7.36900  10.53700  1.000 31.08422  ? 15  PRO A O      1 
ATOM   45   C CB     . PRO A 1 24  ? -2.62300 -7.39700  8.18200   1.000 27.23706  ? 15  PRO A CB     1 
ATOM   46   C CG     . PRO A 1 24  ? -3.46100 -8.17800  9.13900   1.000 39.71642  ? 15  PRO A CG     1 
ATOM   47   C CD     . PRO A 1 24  ? -2.86800 -9.55800  9.16200   1.000 33.07562  ? 15  PRO A CD     1 
ATOM   48   N N      . TYR A 1 25  ? 0.25000  -6.09200  8.77500   1.000 27.27910  ? 16  TYR A N      1 
ATOM   49   C CA     . TYR A 1 25  ? 1.05500  -5.17200  9.56400   1.000 27.35501  ? 16  TYR A CA     1 
ATOM   50   C C      . TYR A 1 25  ? 0.98700  -3.78800  8.94000   1.000 28.48327  ? 16  TYR A C      1 
ATOM   51   O O      . TYR A 1 25  ? 1.07000  -3.64700  7.71800   1.000 30.64415  ? 16  TYR A O      1 
ATOM   52   C CB     . TYR A 1 25  ? 2.51500  -5.63000  9.66300   1.000 24.75483  ? 16  TYR A CB     1 
ATOM   53   C CG     . TYR A 1 25  ? 3.34900  -4.73900  10.55400  1.000 32.96605  ? 16  TYR A CG     1 
ATOM   54   C CD1    . TYR A 1 25  ? 3.31400  -4.88300  11.93500  1.000 28.19752  ? 16  TYR A CD1    1 
ATOM   55   C CD2    . TYR A 1 25  ? 4.15800  -3.74500  10.01800  1.000 27.74369  ? 16  TYR A CD2    1 
ATOM   56   C CE1    . TYR A 1 25  ? 4.06600  -4.06800  12.75700  1.000 26.88379  ? 16  TYR A CE1    1 
ATOM   57   C CE2    . TYR A 1 25  ? 4.91300  -2.92400  10.83300  1.000 29.90374  ? 16  TYR A CE2    1 
ATOM   58   C CZ     . TYR A 1 25  ? 4.86300  -3.09100  12.20300  1.000 29.15380  ? 16  TYR A CZ     1 
ATOM   59   O OH     . TYR A 1 25  ? 5.61400  -2.27900  13.02100  1.000 31.80841  ? 16  TYR A OH     1 
ATOM   60   N N      . LYS A 1 26  ? 0.84600  -2.77200  9.78800   1.000 26.96613  ? 17  LYS A N      1 
ATOM   61   C CA     . LYS A 1 26  ? 0.74100  -1.38600  9.34800   1.000 31.83231  ? 17  LYS A CA     1 
ATOM   62   C C      . LYS A 1 26  ? 2.11700  -0.73800  9.44400   1.000 32.24395  ? 17  LYS A C      1 
ATOM   63   O O      . LYS A 1 26  ? 2.59700  -0.44100  10.54200  1.000 29.06837  ? 17  LYS A O      1 
ATOM   64   C CB     . LYS A 1 26  ? -0.28600 -0.62600  10.18500  1.000 29.97948  ? 17  LYS A CB     1 
ATOM   65   N N      . MET A 1 27  ? 2.75100  -0.52300  8.29400   1.000 33.71458  ? 18  MET A N      1 
ATOM   66   C CA     . MET A 1 27  ? 4.04400  0.15300   8.22600   1.000 32.56074  ? 18  MET A CA     1 
ATOM   67   C C      . MET A 1 27  ? 3.78000  1.59300   7.80300   1.000 36.06147  ? 18  MET A C      1 
ATOM   68   O O      . MET A 1 27  ? 3.69700  1.90600   6.61500   1.000 34.11893  ? 18  MET A O      1 
ATOM   69   C CB     . MET A 1 27  ? 4.98500  -0.55500  7.26100   1.000 31.65151  ? 18  MET A CB     1 
ATOM   70   C CG     . MET A 1 27  ? 6.38500  0.02900   7.24200   1.000 29.76821  ? 18  MET A CG     1 
ATOM   71   S SD     . MET A 1 27  ? 7.36500  -0.59300  5.86900   1.000 38.60572  ? 18  MET A SD     1 
ATOM   72   C CE     . MET A 1 27  ? 6.51800  0.16600   4.48400   1.000 32.12632  ? 18  MET A CE     1 
ATOM   73   N N      . GLY A 1 28  ? 3.65200  2.47500   8.78700   1.000 39.83005  ? 19  GLY A N      1 
ATOM   74   C CA     . GLY A 1 28  ? 3.28800  3.84900   8.48300   1.000 42.44861  ? 19  GLY A CA     1 
ATOM   75   C C      . GLY A 1 28  ? 1.86200  3.90400   7.97500   1.000 37.20107  ? 19  GLY A C      1 
ATOM   76   O O      . GLY A 1 28  ? 0.92900  3.41800   8.62400   1.000 37.40764  ? 19  GLY A O      1 
ATOM   77   N N      . LYS A 1 29  ? 1.68200  4.49200   6.79500   1.000 37.31040  ? 20  LYS A N      1 
ATOM   78   C CA     . LYS A 1 29  ? 0.37700  4.56900   6.15600   1.000 35.41131  ? 20  LYS A CA     1 
ATOM   79   C C      . LYS A 1 29  ? 0.16800  3.47200   5.12000   1.000 34.70541  ? 20  LYS A C      1 
ATOM   80   O O      . LYS A 1 29  ? -0.81100 3.52000   4.37000   1.000 42.35332  ? 20  LYS A O      1 
ATOM   81   C CB     . LYS A 1 29  ? 0.18300  5.94600   5.52000   1.000 36.69875  ? 20  LYS A CB     1 
ATOM   82   C CG     . LYS A 1 29  ? 1.38900  6.45900   4.75200   1.000 41.21780  ? 20  LYS A CG     1 
ATOM   83   C CD     . LYS A 1 29  ? 1.19100  7.90900   4.34100   1.000 52.73727  ? 20  LYS A CD     1 
ATOM   84   C CE     . LYS A 1 29  ? 0.89900  8.78800   5.54900   1.000 49.87954  ? 20  LYS A CE     1 
ATOM   85   N NZ     . LYS A 1 29  ? 0.68700  10.21300  5.16800   1.000 44.08948  ? 20  LYS A NZ     1 
ATOM   86   N N      . PHE A 1 30  ? 1.06000  2.48500   5.06500   1.000 32.14056  ? 21  PHE A N      1 
ATOM   87   C CA     . PHE A 1 30  ? 0.94600  1.35400   4.15000   1.000 33.13417  ? 21  PHE A CA     1 
ATOM   88   C C      . PHE A 1 30  ? 0.58200  0.12200   4.96800   1.000 34.78504  ? 21  PHE A C      1 
ATOM   89   O O      . PHE A 1 30  ? 1.38600  -0.35100  5.77900   1.000 41.31930  ? 21  PHE A O      1 
ATOM   90   C CB     . PHE A 1 30  ? 2.24700  1.13800   3.37900   1.000 39.20237  ? 21  PHE A CB     1 
ATOM   91   C CG     . PHE A 1 30  ? 2.88300  2.40900   2.89200   1.000 30.43701  ? 21  PHE A CG     1 
ATOM   92   C CD1    . PHE A 1 30  ? 2.41100  3.04400   1.75500   1.000 35.38827  ? 21  PHE A CD1    1 
ATOM   93   C CD2    . PHE A 1 30  ? 3.95700  2.96400   3.56800   1.000 35.25570  ? 21  PHE A CD2    1 
ATOM   94   C CE1    . PHE A 1 30  ? 2.99600  4.21300   1.30400   1.000 32.03233  ? 21  PHE A CE1    1 
ATOM   95   C CE2    . PHE A 1 30  ? 4.54700  4.13300   3.12300   1.000 40.14705  ? 21  PHE A CE2    1 
ATOM   96   C CZ     . PHE A 1 30  ? 4.06500  4.75800   1.98800   1.000 36.29402  ? 21  PHE A CZ     1 
ATOM   97   N N      . ASN A 1 31  ? -0.62700 -0.39600  4.75800   1.000 35.02150  ? 22  ASN A N      1 
ATOM   98   C CA     . ASN A 1 31  ? -1.12000 -1.55000  5.51000   1.000 34.09363  ? 22  ASN A CA     1 
ATOM   99   C C      . ASN A 1 31  ? -0.73600 -2.81500  4.75300   1.000 32.46302  ? 22  ASN A C      1 
ATOM   100  O O      . ASN A 1 31  ? -1.44300 -3.26600  3.85200   1.000 41.43239  ? 22  ASN A O      1 
ATOM   101  C CB     . ASN A 1 31  ? -2.62600 -1.45200  5.72000   1.000 30.08343  ? 22  ASN A CB     1 
ATOM   102  N N      . LEU A 1 32  ? 0.39900  -3.39800  5.13100   1.000 28.18561  ? 23  LEU A N      1 
ATOM   103  C CA     . LEU A 1 32  ? 0.88900  -4.59100  4.45300   1.000 27.68120  ? 23  LEU A CA     1 
ATOM   104  C C      . LEU A 1 32  ? 0.05800  -5.80800  4.83900   1.000 29.13228  ? 23  LEU A C      1 
ATOM   105  O O      . LEU A 1 32  ? -0.39200 -5.93800  5.98100   1.000 28.59113  ? 23  LEU A O      1 
ATOM   106  C CB     . LEU A 1 32  ? 2.35800  -4.83200  4.79800   1.000 27.14005  ? 23  LEU A CB     1 
ATOM   107  C CG     . LEU A 1 32  ? 3.30500  -3.64600  4.60700   1.000 27.52513  ? 23  LEU A CG     1 
ATOM   108  C CD1    . LEU A 1 32  ? 4.71500  -4.01500  5.04000   1.000 21.88004  ? 23  LEU A CD1    1 
ATOM   109  C CD2    . LEU A 1 32  ? 3.28800  -3.17200  3.16000   1.000 27.58277  ? 23  LEU A CD2    1 
ATOM   110  N N      . SER A 1 33  ? -0.14200 -6.70700  3.87700   1.000 23.80291  ? 24  SER A N      1 
ATOM   111  C CA     . SER A 1 33  ? -0.91500 -7.91900  4.11100   1.000 26.99336  ? 24  SER A CA     1 
ATOM   112  C C      . SER A 1 33  ? -0.05500 -9.10500  4.52700   1.000 30.41539  ? 24  SER A C      1 
ATOM   113  O O      . SER A 1 33  ? -0.60300 -10.13200 4.94100   1.000 28.74472  ? 24  SER A O      1 
ATOM   114  C CB     . SER A 1 33  ? -1.72100 -8.28100  2.85900   1.000 25.08355  ? 24  SER A CB     1 
ATOM   115  O OG     . SER A 1 33  ? -0.87300 -8.45500  1.73900   1.000 39.10268  ? 24  SER A OG     1 
ATOM   116  N N      . HIS A 1 34  ? 1.26700  -8.99400  4.42400   1.000 25.86382  ? 25  HIS A N      1 
ATOM   117  C CA     . HIS A 1 34  ? 2.16800  -10.02300 4.91900   1.000 23.99644  ? 25  HIS A CA     1 
ATOM   118  C C      . HIS A 1 34  ? 3.50400  -9.37000  5.24000   1.000 29.90591  ? 25  HIS A C      1 
ATOM   119  O O      . HIS A 1 34  ? 3.73500  -8.19700  4.93800   1.000 26.26189  ? 25  HIS A O      1 
ATOM   120  C CB     . HIS A 1 34  ? 2.32700  -11.17100 3.91500   1.000 22.42378  ? 25  HIS A CB     1 
ATOM   121  C CG     . HIS A 1 34  ? 2.92800  -10.75700 2.61000   1.000 26.61599  ? 25  HIS A CG     1 
ATOM   122  N ND1    . HIS A 1 34  ? 4.28100  -10.54700 2.44500   1.000 29.48380  ? 25  HIS A ND1    1 
ATOM   123  C CD2    . HIS A 1 34  ? 2.36100  -10.51400 1.40500   1.000 24.22561  ? 25  HIS A CD2    1 
ATOM   124  C CE1    . HIS A 1 34  ? 4.52100  -10.19300 1.19500   1.000 26.67741  ? 25  HIS A CE1    1 
ATOM   125  N NE2    . HIS A 1 34  ? 3.37300  -10.16600 0.54300   1.000 26.55057  ? 25  HIS A NE2    1 
ATOM   126  N N      . ARG A 1 35  ? 4.39400  -10.14800 5.85200   1.000 24.47144  ? 26  ARG A N      1 
ATOM   127  C CA     . ARG A 1 35  ? 5.62700  -9.61600  6.41400   1.000 25.96750  ? 26  ARG A CA     1 
ATOM   128  C C      . ARG A 1 35  ? 6.87800  -10.08300 5.67900   1.000 28.25573  ? 26  ARG A C      1 
ATOM   129  O O      . ARG A 1 35  ? 7.99100  -9.83300  6.15400   1.000 30.30881  ? 26  ARG A O      1 
ATOM   130  C CB     . ARG A 1 35  ? 5.71000  -9.97800  7.89600   1.000 23.76756  ? 26  ARG A CB     1 
ATOM   131  C CG     . ARG A 1 35  ? 4.57000  -9.38400  8.70200   1.000 27.52342  ? 26  ARG A CG     1 
ATOM   132  C CD     . ARG A 1 35  ? 4.22500  -10.24100 9.89600   1.000 37.38655  ? 26  ARG A CD     1 
ATOM   133  N NE     . ARG A 1 35  ? 3.11500  -9.68100  10.65500  1.000 39.34236  ? 26  ARG A NE     1 
ATOM   134  C CZ     . ARG A 1 35  ? 3.25400  -8.85900  11.68500  1.000 32.09318  ? 26  ARG A CZ     1 
ATOM   135  N NH1    . ARG A 1 35  ? 4.44800  -8.47100  12.10300  1.000 30.74709  ? 26  ARG A NH1    1 
ATOM   136  N NH2    . ARG A 1 35  ? 2.16900  -8.41700  12.31400  1.000 28.19041  ? 26  ARG A NH2    1 
ATOM   137  N N      . VAL A 1 36  ? 6.73000  -10.73900 4.53300   1.000 28.42628  ? 27  VAL A N      1 
ATOM   138  C CA     . VAL A 1 36  ? 7.88100  -11.13900 3.72900   1.000 22.03963  ? 27  VAL A CA     1 
ATOM   139  C C      . VAL A 1 36  ? 8.30300  -9.95200  2.87200   1.000 27.39922  ? 27  VAL A C      1 
ATOM   140  O O      . VAL A 1 36  ? 7.51300  -9.43900  2.07200   1.000 27.34488  ? 27  VAL A O      1 
ATOM   141  C CB     . VAL A 1 36  ? 7.55500  -12.36300 2.86200   1.000 25.69474  ? 27  VAL A CB     1 
ATOM   142  C CG1    . VAL A 1 36  ? 8.74600  -12.72300 1.98800   1.000 24.58503  ? 27  VAL A CG1    1 
ATOM   143  C CG2    . VAL A 1 36  ? 7.15400  -13.54200 3.73800   1.000 19.99379  ? 27  VAL A CG2    1 
ATOM   144  N N      . VAL A 1 37  ? 9.54900  -9.51400  3.03400   1.000 21.81366  ? 28  VAL A N      1 
ATOM   145  C CA     . VAL A 1 37  ? 10.05700 -8.31200  2.38400   1.000 21.83245  ? 28  VAL A CA     1 
ATOM   146  C C      . VAL A 1 37  ? 11.16800 -8.69700  1.41600   1.000 25.35209  ? 28  VAL A C      1 
ATOM   147  O O      . VAL A 1 37  ? 11.99200 -9.56900  1.71500   1.000 20.90960  ? 28  VAL A O      1 
ATOM   148  C CB     . VAL A 1 37  ? 10.56400 -7.28600  3.41900   1.000 22.87455  ? 28  VAL A CB     1 
ATOM   149  C CG1    . VAL A 1 37  ? 11.09800 -6.03800  2.72900   1.000 20.46751  ? 28  VAL A CG1    1 
ATOM   150  C CG2    . VAL A 1 37  ? 9.45400  -6.92600  4.39600   1.000 23.61591  ? 28  VAL A CG2    1 
ATOM   151  N N      . LEU A 1 38  ? 11.18300 -8.05100  0.25200   1.000 25.00347  ? 29  LEU A N      1 
ATOM   152  C CA     . LEU A 1 38  ? 12.28300 -8.19700  -0.69700  1.000 25.26552  ? 29  LEU A CA     1 
ATOM   153  C C      . LEU A 1 38  ? 13.43900 -7.31700  -0.23900  1.000 21.04368  ? 29  LEU A C      1 
ATOM   154  O O      . LEU A 1 38  ? 13.32500 -6.08700  -0.22200  1.000 22.64527  ? 29  LEU A O      1 
ATOM   155  C CB     . LEU A 1 38  ? 11.83600 -7.82500  -2.10800  1.000 23.73570  ? 29  LEU A CB     1 
ATOM   156  C CG     . LEU A 1 38  ? 12.94000 -7.68800  -3.16300  1.000 29.49357  ? 29  LEU A CG     1 
ATOM   157  C CD1    . LEU A 1 38  ? 13.69900 -8.99500  -3.34100  1.000 23.98971  ? 29  LEU A CD1    1 
ATOM   158  C CD2    . LEU A 1 38  ? 12.37000 -7.21400  -4.49400  1.000 22.89952  ? 29  LEU A CD2    1 
ATOM   159  N N      . ALA A 1 39  ? 14.55000 -7.94100  0.13800   1.000 19.94502  ? 30  ALA A N      1 
ATOM   160  C CA     . ALA A 1 39  ? 15.71400 -7.18200  0.55800   1.000 24.84782  ? 30  ALA A CA     1 
ATOM   161  C C      . ALA A 1 39  ? 16.34900 -6.48100  -0.64300  1.000 21.53171  ? 30  ALA A C      1 
ATOM   162  O O      . ALA A 1 39  ? 16.29500 -6.98700  -1.76700  1.000 19.23213  ? 30  ALA A O      1 
ATOM   163  C CB     . ALA A 1 39  ? 16.73700 -8.09500  1.22900   1.000 22.11082  ? 30  ALA A CB     1 
ATOM   164  N N      . PRO A 1 40  ? 16.94500 -5.30800  -0.43300  1.000 24.16051  ? 31  PRO A N      1 
ATOM   165  C CA     . PRO A 1 40  ? 17.62500 -4.61700  -1.53700  1.000 21.63014  ? 31  PRO A CA     1 
ATOM   166  C C      . PRO A 1 40  ? 18.79200 -5.44500  -2.05200  1.000 25.45193  ? 31  PRO A C      1 
ATOM   167  O O      . PRO A 1 40  ? 19.59800 -5.95900  -1.27500  1.000 18.49401  ? 31  PRO A O      1 
ATOM   168  C CB     . PRO A 1 40  ? 18.09900 -3.30800  -0.89800  1.000 21.81327  ? 31  PRO A CB     1 
ATOM   169  C CG     . PRO A 1 40  ? 18.17800 -3.61000  0.56600   1.000 26.70244  ? 31  PRO A CG     1 
ATOM   170  C CD     . PRO A 1 40  ? 17.06600 -4.57300  0.83800   1.000 16.57499  ? 31  PRO A CD     1 
ATOM   171  N N      . MET A 1 41  ? 18.87700 -5.57700  -3.37500  1.000 25.07206  ? 32  MET A N      1 
ATOM   172  C CA     . MET A 1 41  ? 19.90900 -6.41800  -3.97400  1.000 26.55444  ? 32  MET A CA     1 
ATOM   173  C C      . MET A 1 41  ? 20.35700 -5.84000  -5.30700  1.000 26.35582  ? 32  MET A C      1 
ATOM   174  O O      . MET A 1 41  ? 19.57000 -5.77100  -6.25600  1.000 21.09285  ? 32  MET A O      1 
ATOM   175  C CB     . MET A 1 41  ? 19.41200 -7.85000  -4.15000  1.000 28.78227  ? 32  MET A CB     1 
ATOM   176  C CG     . MET A 1 41  ? 19.57706 -8.69766  -2.90410  1.000 28.17441  ? 32  MET A CG     1 
ATOM   177  S SD     . MET A 1 41  ? 19.06362 -10.38192 -3.21296  1.000 37.69572  ? 32  MET A SD     1 
ATOM   178  C CE     . MET A 1 41  ? 17.44329 -10.09791 -3.92120  1.000 24.13010  ? 32  MET A CE     1 
ATOM   179  N N      . THR A 1 42  ? 21.62600 -5.44300  -5.36400  1.000 23.62618  ? 33  THR A N      1 
ATOM   180  C CA     . THR A 1 42  ? 22.25100 -5.00200  -6.60100  1.000 27.00915  ? 33  THR A CA     1 
ATOM   181  C C      . THR A 1 42  ? 22.34600 -6.16000  -7.58700  1.000 26.29945  ? 33  THR A C      1 
ATOM   182  O O      . THR A 1 42  ? 22.84900 -7.23600  -7.24900  1.000 24.82597  ? 33  THR A O      1 
ATOM   183  C CB     . THR A 1 42  ? 23.64500 -4.44800  -6.30500  1.000 27.60599  ? 33  THR A CB     1 
ATOM   184  O OG1    . THR A 1 42  ? 23.53700 -3.32100  -5.42500  1.000 27.67772  ? 33  THR A OG1    1 
ATOM   185  C CG2    . THR A 1 42  ? 24.35000 -4.03300  -7.58700  1.000 24.37839  ? 33  THR A CG2    1 
ATOM   186  N N      . ARG A 1 43  ? 21.86300 -5.93700  -8.81100  1.000 27.43994  ? 34  ARG A N      1 
ATOM   187  C CA     . ARG A 1 43  ? 21.90500 -6.94600  -9.85800  1.000 23.70949  ? 34  ARG A CA     1 
ATOM   188  C C      . ARG A 1 43  ? 22.62900 -6.49000  -11.11700 1.000 27.48361  ? 34  ARG A C      1 
ATOM   189  O O      . ARG A 1 43  ? 22.93200 -7.33300  -11.97100 1.000 24.91254  ? 34  ARG A O      1 
ATOM   190  C CB     . ARG A 1 43  ? 20.48300 -7.39200  -10.23400 1.000 22.15188  ? 34  ARG A CB     1 
ATOM   191  C CG     . ARG A 1 43  ? 19.65500 -7.89400  -9.06200  1.000 23.24487  ? 34  ARG A CG     1 
ATOM   192  C CD     . ARG A 1 43  ? 20.35100 -9.03200  -8.32900  1.000 25.34429  ? 34  ARG A CD     1 
ATOM   193  N NE     . ARG A 1 43  ? 20.75300 -10.10300 -9.23200  1.000 26.33629  ? 34  ARG A NE     1 
ATOM   194  C CZ     . ARG A 1 43  ? 19.94200 -11.05300 -9.67800  1.000 28.45383  ? 34  ARG A CZ     1 
ATOM   195  N NH1    . ARG A 1 43  ? 18.66800 -11.09500 -9.32500  1.000 21.99450  ? 34  ARG A NH1    1 
ATOM   196  N NH2    . ARG A 1 43  ? 20.42100 -11.97900 -10.50400 1.000 24.36769  ? 34  ARG A NH2    1 
ATOM   197  N N      . CYS A 1 44  ? 22.90000 -5.19000  -11.26100 1.000 24.63104  ? 35  CYS A N      1 
ATOM   198  C CA     . CYS A 1 44  ? 23.71000 -4.64500  -12.35400 1.000 26.63333  ? 35  CYS A CA     1 
ATOM   199  C C      . CYS A 1 44  ? 23.06200 -4.86900  -13.72200 1.000 26.36353  ? 35  CYS A C      1 
ATOM   200  O O      . CYS A 1 44  ? 23.74300 -5.18400  -14.69800 1.000 27.70429  ? 35  CYS A O      1 
ATOM   201  C CB     . CYS A 1 44  ? 25.12900 -5.21900  -12.32800 1.000 27.27791  ? 35  CYS A CB     1 
ATOM   202  S SG     . CYS A 1 44  ? 25.95800 -5.07000  -10.72600 1.000 25.25802  ? 35  CYS A SG     1 
ATOM   203  N N      . ARG A 1 45  ? 21.74100 -4.69300  -13.79900 1.000 25.58622  ? 36  ARG A N      1 
ATOM   204  C CA     . ARG A 1 45  ? 21.02200 -4.76100  -15.06600 1.000 25.71628  ? 36  ARG A CA     1 
ATOM   205  C C      . ARG A 1 45  ? 20.58900 -3.40000  -15.59200 1.000 27.43139  ? 36  ARG A C      1 
ATOM   206  O O      . ARG A 1 45  ? 20.14000 -3.31600  -16.74100 1.000 25.22240  ? 36  ARG A O      1 
ATOM   207  C CB     . ARG A 1 45  ? 19.78200 -5.66000  -14.94000 1.000 25.53543  ? 36  ARG A CB     1 
ATOM   208  C CG     . ARG A 1 45  ? 19.98800 -7.09900  -15.38800 1.000 24.48786  ? 36  ARG A CG     1 
ATOM   209  C CD     . ARG A 1 45  ? 20.82200 -7.88500  -14.39200 1.000 25.31744  ? 36  ARG A CD     1 
ATOM   210  N NE     . ARG A 1 45  ? 20.93100 -9.29000  -14.76700 1.000 24.01041  ? 36  ARG A NE     1 
ATOM   211  C CZ     . ARG A 1 45  ? 21.53600 -10.21800 -14.03700 1.000 27.37165  ? 36  ARG A CZ     1 
ATOM   212  N NH1    . ARG A 1 45  ? 22.10900 -9.92300  -12.88000 1.000 26.22415  ? 36  ARG A NH1    1 
ATOM   213  N NH2    . ARG A 1 45  ? 21.56600 -11.47300 -14.47700 1.000 19.94849  ? 36  ARG A NH2    1 
ATOM   214  N N      . ALA A 1 46  ? 20.69300 -2.34000  -14.78900 1.000 25.93339  ? 37  ALA A N      1 
ATOM   215  C CA     . ALA A 1 46  ? 20.32500 -0.99200  -15.22200 1.000 26.45861  ? 37  ALA A CA     1 
ATOM   216  C C      . ALA A 1 46  ? 21.48400 -0.41700  -16.02900 1.000 22.11133  ? 37  ALA A C      1 
ATOM   217  O O      . ALA A 1 46  ? 22.31900 0.34500   -15.53400 1.000 24.28413  ? 37  ALA A O      1 
ATOM   218  C CB     . ALA A 1 46  ? 19.97800 -0.11400  -14.02600 1.000 26.27419  ? 37  ALA A CB     1 
ATOM   219  N N      . LEU A 1 47  ? 21.52400 -0.79700  -17.30400 1.000 25.95451  ? 38  LEU A N      1 
ATOM   220  C CA     . LEU A 1 47  ? 22.64500 -0.44700  -18.16700 1.000 24.98214  ? 38  LEU A CA     1 
ATOM   221  C C      . LEU A 1 47  ? 22.82000 1.06300   -18.25100 1.000 23.73196  ? 38  LEU A C      1 
ATOM   222  O O      . LEU A 1 47  ? 21.85000 1.80500   -18.42700 1.000 26.36299  ? 38  LEU A O      1 
ATOM   223  C CB     . LEU A 1 47  ? 22.43300 -1.03400  -19.56100 1.000 26.06820  ? 38  LEU A CB     1 
ATOM   224  C CG     . LEU A 1 47  ? 22.11900 -2.53000  -19.63000 1.000 26.93420  ? 38  LEU A CG     1 
ATOM   225  C CD1    . LEU A 1 47  ? 21.97700 -2.97000  -21.08000 1.000 23.82593  ? 38  LEU A CD1    1 
ATOM   226  C CD2    . LEU A 1 47  ? 23.18800 -3.34800  -18.91400 1.000 22.82737  ? 38  LEU A CD2    1 
ATOM   227  N N      . ASN A 1 48  ? 24.07000 1.51000   -18.11100 1.000 25.89156  ? 39  ASN A N      1 
ATOM   228  C CA     . ASN A 1 48  ? 24.43000 2.92700   -18.18900 1.000 31.25400  ? 39  ASN A CA     1 
ATOM   229  C C      . ASN A 1 48  ? 23.71500 3.75300   -17.12100 1.000 26.70277  ? 39  ASN A C      1 
ATOM   230  O O      . ASN A 1 48  ? 23.37000 4.91700   -17.34600 1.000 27.78384  ? 39  ASN A O      1 
ATOM   231  C CB     . ASN A 1 48  ? 24.15900 3.48800   -19.58900 1.000 29.38306  ? 39  ASN A CB     1 
ATOM   232  C CG     . ASN A 1 48  ? 25.27300 4.39200   -20.07600 1.000 40.95724  ? 39  ASN A CG     1 
ATOM   233  O OD1    . ASN A 1 48  ? 25.86100 5.14200   -19.29900 1.000 47.92785  ? 39  ASN A OD1    1 
ATOM   234  N ND2    . ASN A 1 48  ? 25.57400 4.31900   -21.36900 1.000 45.63894  ? 39  ASN A ND2    1 
ATOM   235  N N      . ASN A 1 49  ? 23.50100 3.14200   -15.95400 1.000 25.91809  ? 40  ASN A N      1 
ATOM   236  C CA     . ASN A 1 49  ? 22.80600 3.71100   -14.80200 1.000 24.74215  ? 40  ASN A CA     1 
ATOM   237  C C      . ASN A 1 49  ? 21.36500 4.09900   -15.10300 1.000 24.99478  ? 40  ASN A C      1 
ATOM   238  O O      . ASN A 1 49  ? 20.75700 4.84200   -14.32300 1.000 27.84135  ? 40  ASN A O      1 
ATOM   239  C CB     . ASN A 1 49  ? 23.55600 4.92200   -14.22700 1.000 22.09193  ? 40  ASN A CB     1 
ATOM   240  C CG     . ASN A 1 49  ? 25.01600 4.62600   -13.94400 1.000 21.96914  ? 40  ASN A CG     1 
ATOM   241  O OD1    . ASN A 1 49  ? 25.89800 5.38600   -14.34100 1.000 24.65180  ? 40  ASN A OD1    1 
ATOM   242  N ND2    . ASN A 1 49  ? 25.28000 3.51500   -13.26600 1.000 24.43438  ? 40  ASN A ND2    1 
ATOM   243  N N      . ILE A 1 50  ? 20.79700 3.60700   -16.19600 1.000 26.46055  ? 41  ILE A N      1 
ATOM   244  C CA     . ILE A 1 50  ? 19.42600 3.92300   -16.58400 1.000 31.07642  ? 41  ILE A CA     1 
ATOM   245  C C      . ILE A 1 50  ? 18.55300 2.71100   -16.26900 1.000 29.01253  ? 41  ILE A C      1 
ATOM   246  O O      . ILE A 1 50  ? 18.83400 1.61600   -16.77900 1.000 28.65701  ? 41  ILE A O      1 
ATOM   247  C CB     . ILE A 1 50  ? 19.33600 4.29600   -18.06900 1.000 29.44897  ? 41  ILE A CB     1 
ATOM   248  C CG1    . ILE A 1 50  ? 19.97444 5.66509   -18.31307 1.000 31.29599  ? 41  ILE A CG1    1 
ATOM   249  C CG2    . ILE A 1 50  ? 17.88368 4.26712   -18.54157 1.000 25.98603  ? 41  ILE A CG2    1 
ATOM   250  C CD1    . ILE A 1 50  ? 20.18291 5.99023   -19.77798 1.000 31.88063  ? 41  ILE A CD1    1 
ATOM   251  N N      . PRO A 1 51  ? 17.51600 2.85200   -15.44500 1.000 32.21893  ? 42  PRO A N      1 
ATOM   252  C CA     . PRO A 1 51  ? 16.63700 1.70700   -15.15500 1.000 29.58562  ? 42  PRO A CA     1 
ATOM   253  C C      . PRO A 1 51  ? 15.99000 1.17400   -16.42400 1.000 29.10587  ? 42  PRO A C      1 
ATOM   254  O O      . PRO A 1 51  ? 15.21600 1.86700   -17.08900 1.000 37.40869  ? 42  PRO A O      1 
ATOM   255  C CB     . PRO A 1 51  ? 15.60000 2.29600   -14.19100 1.000 26.01664  ? 42  PRO A CB     1 
ATOM   256  C CG     . PRO A 1 51  ? 16.27100 3.47900   -13.58200 1.000 23.27137  ? 42  PRO A CG     1 
ATOM   257  C CD     . PRO A 1 51  ? 17.14000 4.04600   -14.66900 1.000 25.75751  ? 42  PRO A CD     1 
ATOM   258  N N      . GLN A 1 52  ? 16.31300 -0.07200  -16.75600 1.000 30.91806  ? 43  GLN A N      1 
ATOM   259  C CA     . GLN A 1 52  ? 15.82000 -0.70600  -17.96700 1.000 27.70870  ? 43  GLN A CA     1 
ATOM   260  C C      . GLN A 1 52  ? 14.45600 -1.34900  -17.72300 1.000 32.80572  ? 43  GLN A C      1 
ATOM   261  O O      . GLN A 1 52  ? 13.97900 -1.45700  -16.59100 1.000 30.43692  ? 43  GLN A O      1 
ATOM   262  C CB     . GLN A 1 52  ? 16.81900 -1.75200  -18.46700 1.000 28.18060  ? 43  GLN A CB     1 
ATOM   263  C CG     . GLN A 1 52  ? 18.24200 -1.23500  -18.63900 1.000 30.17719  ? 43  GLN A CG     1 
ATOM   264  C CD     . GLN A 1 52  ? 18.36600 -0.20700  -19.74800 1.000 32.11296  ? 43  GLN A CD     1 
ATOM   265  O OE1    . GLN A 1 52  ? 17.54100 -0.15700  -20.66100 1.000 38.31132  ? 43  GLN A OE1    1 
ATOM   266  N NE2    . GLN A 1 52  ? 19.40000 0.62300   -19.67300 1.000 30.11591  ? 43  GLN A NE2    1 
ATOM   267  N N      . ALA A 1 53  ? 13.82600 -1.78500  -18.81700 1.000 28.19395  ? 44  ALA A N      1 
ATOM   268  C CA     . ALA A 1 53  ? 12.55400 -2.49100  -18.71700 1.000 28.63264  ? 44  ALA A CA     1 
ATOM   269  C C      . ALA A 1 53  ? 12.70000 -3.84700  -18.04100 1.000 28.59117  ? 44  ALA A C      1 
ATOM   270  O O      . ALA A 1 53  ? 11.72000 -4.36000  -17.48900 1.000 27.99401  ? 44  ALA A O      1 
ATOM   271  C CB     . ALA A 1 53  ? 11.93800 -2.66600  -20.10500 1.000 29.02456  ? 44  ALA A CB     1 
ATOM   272  N N      . ALA A 1 54  ? 13.89600 -4.43900  -18.07900 1.000 28.96839  ? 45  ALA A N      1 
ATOM   273  C CA     . ALA A 1 54  ? 14.11100 -5.71500  -17.40600 1.000 25.19748  ? 45  ALA A CA     1 
ATOM   274  C C      . ALA A 1 54  ? 13.92100 -5.59200  -15.90100 1.000 24.88747  ? 45  ALA A C      1 
ATOM   275  O O      . ALA A 1 54  ? 13.48200 -6.54900  -15.25200 1.000 25.56244  ? 45  ALA A O      1 
ATOM   276  C CB     . ALA A 1 54  ? 15.50800 -6.24600  -17.72300 1.000 21.61324  ? 45  ALA A CB     1 
ATOM   277  N N      . LEU A 1 55  ? 14.24700 -4.43000  -15.32900 1.000 21.65633  ? 46  LEU A N      1 
ATOM   278  C CA     . LEU A 1 55  ? 14.00400 -4.21500  -13.90500 1.000 25.30684  ? 46  LEU A CA     1 
ATOM   279  C C      . LEU A 1 55  ? 12.51500 -4.27500  -13.58900 1.000 24.38745  ? 46  LEU A C      1 
ATOM   280  O O      . LEU A 1 55  ? 12.10600 -4.89900  -12.60200 1.000 24.35938  ? 46  LEU A O      1 
ATOM   281  C CB     . LEU A 1 55  ? 14.59200 -2.87500  -13.46100 1.000 22.51723  ? 46  LEU A CB     1 
ATOM   282  C CG     . LEU A 1 55  ? 16.07800 -2.80200  -13.09200 1.000 26.75380  ? 46  LEU A CG     1 
ATOM   283  C CD1    . LEU A 1 55  ? 16.97700 -3.04400  -14.29700 1.000 25.68377  ? 46  LEU A CD1    1 
ATOM   284  C CD2    . LEU A 1 55  ? 16.39400 -1.46000  -12.44700 1.000 25.83987  ? 46  LEU A CD2    1 
ATOM   285  N N      . GLY A 1 56  ? 11.68800 -3.63300  -14.41800 1.000 27.04653  ? 47  GLY A N      1 
ATOM   286  C CA     . GLY A 1 56  ? 10.25000 -3.71100  -14.21800 1.000 26.44184  ? 47  GLY A CA     1 
ATOM   287  C C      . GLY A 1 56  ? 9.73700  -5.13700  -14.25100 1.000 28.11489  ? 47  GLY A C      1 
ATOM   288  O O      . GLY A 1 56  ? 8.93100  -5.53600  -13.40900 1.000 34.59961  ? 47  GLY A O      1 
ATOM   289  N N      . GLU A 1 57  ? 10.20500 -5.92700  -15.22100 1.000 28.24877  ? 48  GLU A N      1 
ATOM   290  C CA     . GLU A 1 57  ? 9.85200  -7.34200  -15.26400 1.000 28.68931  ? 48  GLU A CA     1 
ATOM   291  C C      . GLU A 1 57  ? 10.35100 -8.07300  -14.02300 1.000 29.11799  ? 48  GLU A C      1 
ATOM   292  O O      . GLU A 1 57  ? 9.65500  -8.93900  -13.47900 1.000 29.58145  ? 48  GLU A O      1 
ATOM   293  C CB     . GLU A 1 57  ? 10.42600 -7.97900  -16.53200 1.000 32.40485  ? 48  GLU A CB     1 
ATOM   294  C CG     . GLU A 1 57  ? 10.48050 -9.49900  -16.51198 1.000 34.81647  ? 48  GLU A CG     1 
ATOM   295  C CD     . GLU A 1 57  ? 9.27036  -10.14305 -17.15776 1.000 49.39374  ? 48  GLU A CD     1 
ATOM   296  O OE1    . GLU A 1 57  ? 8.18379  -9.52694  -17.14234 1.000 53.92010  ? 48  GLU A OE1    1 
ATOM   297  O OE2    . GLU A 1 57  ? 9.40815  -11.26687 -17.68606 1.000 50.77814  ? 48  GLU A OE2    1 
ATOM   298  N N      . TYR A 1 58  ? 11.55100 -7.72600  -13.55700 1.000 25.79545  ? 49  TYR A N      1 
ATOM   299  C CA     . TYR A 1 58  ? 12.13500 -8.39600  -12.39900 1.000 23.83978  ? 49  TYR A CA     1 
ATOM   300  C C      . TYR A 1 58  ? 11.33300 -8.11700  -11.13200 1.000 27.79253  ? 49  TYR A C      1 
ATOM   301  O O      . TYR A 1 58  ? 10.97800 -9.04200  -10.39300 1.000 23.85664  ? 49  TYR A O      1 
ATOM   302  C CB     . TYR A 1 58  ? 13.59000 -7.95400  -12.24000 1.000 22.15769  ? 49  TYR A CB     1 
ATOM   303  C CG     . TYR A 1 58  ? 14.24851 -8.34884  -10.93897 1.000 27.18964  ? 49  TYR A CG     1 
ATOM   304  C CD1    . TYR A 1 58  ? 14.87662 -9.57948  -10.79839 1.000 25.95894  ? 49  TYR A CD1    1 
ATOM   305  C CD2    . TYR A 1 58  ? 14.26536 -7.47843  -9.85777  1.000 25.86081  ? 49  TYR A CD2    1 
ATOM   306  C CE1    . TYR A 1 58  ? 15.49007 -9.93575  -9.61315  1.000 22.58715  ? 49  TYR A CE1    1 
ATOM   307  C CE2    . TYR A 1 58  ? 14.87312 -7.82510  -8.67134  1.000 25.34908  ? 49  TYR A CE2    1 
ATOM   308  C CZ     . TYR A 1 58  ? 15.48452 -9.05319  -8.55303  1.000 26.26481  ? 49  TYR A CZ     1 
ATOM   309  O OH     . TYR A 1 58  ? 16.09114 -9.39794  -7.36656  1.000 30.70109  ? 49  TYR A OH     1 
ATOM   310  N N      . TYR A 1 59  ? 11.03200 -6.84400  -10.86600 1.000 25.21712  ? 50  TYR A N      1 
ATOM   311  C CA     . TYR A 1 59  ? 10.27900 -6.51100  -9.66100  1.000 26.58239  ? 50  TYR A CA     1 
ATOM   312  C C      . TYR A 1 59  ? 8.82100  -6.94100  -9.76600  1.000 28.31983  ? 50  TYR A C      1 
ATOM   313  O O      . TYR A 1 59  ? 8.18900  -7.22500  -8.74200  1.000 23.53736  ? 50  TYR A O      1 
ATOM   314  C CB     . TYR A 1 59  ? 10.37600 -5.01300  -9.37100  1.000 19.91287  ? 50  TYR A CB     1 
ATOM   315  C CG     . TYR A 1 59  ? 11.74900 -4.58000  -8.90600  1.000 22.51888  ? 50  TYR A CG     1 
ATOM   316  C CD1    . TYR A 1 59  ? 12.25100 -4.99900  -7.68100  1.000 22.40851  ? 50  TYR A CD1    1 
ATOM   317  C CD2    . TYR A 1 59  ? 12.54200 -3.75200  -9.68900  1.000 23.18486  ? 50  TYR A CD2    1 
ATOM   318  C CE1    . TYR A 1 59  ? 13.50400 -4.61100  -7.25100  1.000 25.09214  ? 50  TYR A CE1    1 
ATOM   319  C CE2    . TYR A 1 59  ? 13.79700 -3.35600  -9.26600  1.000 24.35456  ? 50  TYR A CE2    1 
ATOM   320  C CZ     . TYR A 1 59  ? 14.27200 -3.78900  -8.04600  1.000 25.66774  ? 50  TYR A CZ     1 
ATOM   321  O OH     . TYR A 1 59  ? 15.52100 -3.40000  -7.61900  1.000 28.72450  ? 50  TYR A OH     1 
ATOM   322  N N      . GLU A 1 60  ? 8.27200  -7.00500  -10.98300 1.000 27.02186  ? 51  GLU A N      1 
ATOM   323  C CA     . GLU A 1 60  ? 6.88500  -7.43600  -11.13900 1.000 30.41338  ? 51  GLU A CA     1 
ATOM   324  C C      . GLU A 1 60  ? 6.72100  -8.90900  -10.79300 1.000 27.08074  ? 51  GLU A C      1 
ATOM   325  O O      . GLU A 1 60  ? 5.71600  -9.30100  -10.18900 1.000 36.32834  ? 51  GLU A O      1 
ATOM   326  C CB     . GLU A 1 60  ? 6.40400  -7.17200  -12.56500 1.000 27.95681  ? 51  GLU A CB     1 
ATOM   327  C CG     . GLU A 1 60  ? 4.92500  -7.45200  -12.78700 1.000 34.01913  ? 51  GLU A CG     1 
ATOM   328  C CD     . GLU A 1 60  ? 4.51700  -7.30500  -14.24100 1.000 46.30631  ? 51  GLU A CD     1 
ATOM   329  O OE1    . GLU A 1 60  ? 5.37200  -7.53000  -15.12400 1.000 48.95043  ? 51  GLU A OE1    1 
ATOM   330  O OE2    . GLU A 1 60  ? 3.34500  -6.96000  -14.50200 1.000 47.32818  ? 51  GLU A OE2    1 
ATOM   331  N N      . GLN A 1 61  ? 7.69700  -9.74200  -11.17000 1.000 24.76887  ? 52  GLN A N      1 
ATOM   332  C CA     . GLN A 1 61  ? 7.62800  -11.16300 -10.84500 1.000 27.96108  ? 52  GLN A CA     1 
ATOM   333  C C      . GLN A 1 61  ? 7.57600  -11.39500 -9.34300  1.000 24.21564  ? 52  GLN A C      1 
ATOM   334  O O      . GLN A 1 61  ? 7.00900  -12.39400 -8.88800  1.000 28.25585  ? 52  GLN A O      1 
ATOM   335  C CB     . GLN A 1 61  ? 8.82700  -11.90400 -11.43800 1.000 28.16259  ? 52  GLN A CB     1 
ATOM   336  C CG     . GLN A 1 61  ? 8.82600  -12.03700 -12.94900 1.000 26.72604  ? 52  GLN A CG     1 
ATOM   337  C CD     . GLN A 1 61  ? 10.06600 -12.74900 -13.45800 1.000 31.97182  ? 52  GLN A CD     1 
ATOM   338  O OE1    . GLN A 1 61  ? 11.07400 -12.84300 -12.75400 1.000 28.43474  ? 52  GLN A OE1    1 
ATOM   339  N NE2    . GLN A 1 61  ? 9.99600  -13.26300 -14.67900 1.000 31.13337  ? 52  GLN A NE2    1 
ATOM   340  N N      . ARG A 1 62  ? 8.15700  -10.48900 -8.55900  1.000 24.78833  ? 53  ARG A N      1 
ATOM   341  C CA     . ARG A 1 62  ? 8.27400  -10.66000 -7.11900  1.000 28.80805  ? 53  ARG A CA     1 
ATOM   342  C C      . ARG A 1 62  ? 7.27500  -9.82700  -6.32800  1.000 30.19242  ? 53  ARG A C      1 
ATOM   343  O O      . ARG A 1 62  ? 7.17300  -10.00600 -5.11000  1.000 29.04332  ? 53  ARG A O      1 
ATOM   344  C CB     . ARG A 1 62  ? 9.70400  -10.32700 -6.67300  1.000 25.22489  ? 53  ARG A CB     1 
ATOM   345  C CG     . ARG A 1 62  ? 10.70600 -11.39200 -7.08800  1.000 28.21151  ? 53  ARG A CG     1 
ATOM   346  C CD     . ARG A 1 62  ? 12.04800 -10.82700 -7.52400  1.000 25.12821  ? 53  ARG A CD     1 
ATOM   347  N NE     . ARG A 1 62  ? 12.90500 -11.89100 -8.03300  1.000 25.47704  ? 53  ARG A NE     1 
ATOM   348  C CZ     . ARG A 1 62  ? 12.84700 -12.37200 -9.26800  1.000 25.99849  ? 53  ARG A CZ     1 
ATOM   349  N NH1    . ARG A 1 62  ? 12.01700 -11.87000 -10.16700 1.000 27.88479  ? 53  ARG A NH1    1 
ATOM   350  N NH2    . ARG A 1 62  ? 13.63600 -13.38800 -9.60700  1.000 21.62317  ? 53  ARG A NH2    1 
ATOM   351  N N      . ALA A 1 63  ? 6.53500  -8.93900  -6.98300  1.000 29.78575  ? 54  ALA A N      1 
ATOM   352  C CA     . ALA A 1 63  ? 5.54900  -8.12100  -6.29400  1.000 27.58486  ? 54  ALA A CA     1 
ATOM   353  C C      . ALA A 1 63  ? 4.30300  -8.93800  -5.97500  1.000 30.93682  ? 54  ALA A C      1 
ATOM   354  O O      . ALA A 1 63  ? 3.83800  -9.73900  -6.79100  1.000 30.02954  ? 54  ALA A O      1 
ATOM   355  C CB     . ALA A 1 63  ? 5.17500  -6.90600  -7.14300  1.000 24.63929  ? 54  ALA A CB     1 
ATOM   356  N N      . THR A 1 64  ? 3.77000  -8.73400  -4.77300  1.000 28.61353  ? 55  THR A N      1 
ATOM   357  C CA     . THR A 1 64  ? 2.52600  -9.35400  -4.34400  1.000 31.62420  ? 55  THR A CA     1 
ATOM   358  C C      . THR A 1 64  ? 1.59800  -8.28200  -3.79200  1.000 31.43600  ? 55  THR A C      1 
ATOM   359  O O      . THR A 1 64  ? 2.03400  -7.20000  -3.39200  1.000 29.25841  ? 55  THR A O      1 
ATOM   360  C CB     . THR A 1 64  ? 2.75700  -10.43600 -3.27800  1.000 28.62725  ? 55  THR A CB     1 
ATOM   361  O OG1    . THR A 1 64  ? 3.49500  -9.87800  -2.18300  1.000 26.65663  ? 55  THR A OG1    1 
ATOM   362  C CG2    . THR A 1 64  ? 3.52400  -11.61400 -3.86200  1.000 27.00727  ? 55  THR A CG2    1 
ATOM   363  N N      . ALA A 1 65  ? 0.30500  -8.59800  -3.77700  1.000 28.46218  ? 56  ALA A N      1 
ATOM   364  C CA     . ALA A 1 65  ? -0.68900 -7.66900  -3.25800  1.000 29.39042  ? 56  ALA A CA     1 
ATOM   365  C C      . ALA A 1 65  ? -0.47300 -7.44900  -1.76700  1.000 26.68545  ? 56  ALA A C      1 
ATOM   366  O O      . ALA A 1 65  ? -0.59600 -8.38100  -0.97000  1.000 25.88794  ? 56  ALA A O      1 
ATOM   367  C CB     . ALA A 1 65  ? -2.09600 -8.19800  -3.53100  1.000 27.94264  ? 56  ALA A CB     1 
ATOM   368  N N      . GLY A 1 66  ? -0.14400 -6.21400  -1.39600  1.000 27.59065  ? 57  GLY A N      1 
ATOM   369  C CA     . GLY A 1 66  ? 0.16000  -5.90600  -0.01500  1.000 29.60968  ? 57  GLY A CA     1 
ATOM   370  C C      . GLY A 1 66  ? 1.55000  -6.28700  0.43300   1.000 27.99275  ? 57  GLY A C      1 
ATOM   371  O O      . GLY A 1 66  ? 1.79700  -6.37300  1.63900   1.000 25.67666  ? 57  GLY A O      1 
ATOM   372  N N      . GLY A 1 67  ? 2.46900  -6.52200  -0.50000  1.000 23.20043  ? 58  GLY A N      1 
ATOM   373  C CA     . GLY A 1 67  ? 3.83500  -6.88000  -0.17300  1.000 22.42125  ? 58  GLY A CA     1 
ATOM   374  C C      . GLY A 1 67  ? 4.77100  -5.69000  -0.28100  1.000 24.32605  ? 58  GLY A C      1 
ATOM   375  O O      . GLY A 1 67  ? 4.54900  -4.77600  -1.07100  1.000 27.49280  ? 58  GLY A O      1 
ATOM   376  N N      . PHE A 1 68  ? 5.82800  -5.71400  0.52500   1.000 21.69951  ? 59  PHE A N      1 
ATOM   377  C CA     . PHE A 1 68  ? 6.79900  -4.62800  0.58100   1.000 22.03290  ? 59  PHE A CA     1 
ATOM   378  C C      . PHE A 1 68  ? 8.06800  -5.02900  -0.16200  1.000 26.19019  ? 59  PHE A C      1 
ATOM   379  O O      . PHE A 1 68  ? 8.66900  -6.06600  0.13800   1.000 27.65031  ? 59  PHE A O      1 
ATOM   380  C CB     . PHE A 1 68  ? 7.12400  -4.26800  2.03300   1.000 24.44264  ? 59  PHE A CB     1 
ATOM   381  C CG     . PHE A 1 68  ? 8.07600  -3.11100  2.17700   1.000 26.19210  ? 59  PHE A CG     1 
ATOM   382  C CD1    . PHE A 1 68  ? 8.08800  -2.08100  1.24900   1.000 26.86290  ? 59  PHE A CD1    1 
ATOM   383  C CD2    . PHE A 1 68  ? 8.96600  -3.06000  3.23700   1.000 25.08074  ? 59  PHE A CD2    1 
ATOM   384  C CE1    . PHE A 1 68  ? 8.96500  -1.02100  1.38000   1.000 27.83537  ? 59  PHE A CE1    1 
ATOM   385  C CE2    . PHE A 1 68  ? 9.84600  -2.00400  3.37300   1.000 25.72833  ? 59  PHE A CE2    1 
ATOM   386  C CZ     . PHE A 1 68  ? 9.84500  -0.98200  2.44400   1.000 25.80121  ? 59  PHE A CZ     1 
ATOM   387  N N      . LEU A 1 69  ? 8.47300  -4.20200  -1.12400  1.000 25.47422  ? 60  LEU A N      1 
ATOM   388  C CA     . LEU A 1 69  ? 9.67800  -4.42500  -1.91200  1.000 23.65463  ? 60  LEU A CA     1 
ATOM   389  C C      . LEU A 1 69  ? 10.65100 -3.27100  -1.70900  1.000 26.56075  ? 60  LEU A C      1 
ATOM   390  O O      . LEU A 1 69  ? 10.24200 -2.10800  -1.63800  1.000 21.29356  ? 60  LEU A O      1 
ATOM   391  C CB     . LEU A 1 69  ? 9.35200  -4.55800  -3.40400  1.000 24.19410  ? 60  LEU A CB     1 
ATOM   392  C CG     . LEU A 1 69  ? 8.23500  -5.52000  -3.80500  1.000 29.22585  ? 60  LEU A CG     1 
ATOM   393  C CD1    . LEU A 1 69  ? 8.05400  -5.51300  -5.31600  1.000 27.69821  ? 60  LEU A CD1    1 
ATOM   394  C CD2    . LEU A 1 69  ? 8.52200  -6.92400  -3.30300  1.000 26.30458  ? 60  LEU A CD2    1 
ATOM   395  N N      . ILE A 1 70  ? 11.93900 -3.59500  -1.62300  1.000 21.80734  ? 61  ILE A N      1 
ATOM   396  C CA     . ILE A 1 70  ? 13.00400 -2.60100  -1.54000  1.000 22.47624  ? 61  ILE A CA     1 
ATOM   397  C C      . ILE A 1 70  ? 13.93100 -2.80400  -2.73000  1.000 20.57533  ? 61  ILE A C      1 
ATOM   398  O O      . ILE A 1 70  ? 14.44600 -3.90900  -2.93900  1.000 22.47844  ? 61  ILE A O      1 
ATOM   399  C CB     . ILE A 1 70  ? 13.78000 -2.70300  -0.21500  1.000 24.67043  ? 61  ILE A CB     1 
ATOM   400  C CG1    . ILE A 1 70  ? 12.81200 -2.73600  0.96800   1.000 24.70392  ? 61  ILE A CG1    1 
ATOM   401  C CG2    . ILE A 1 70  ? 14.74100 -1.53400  -0.07400  1.000 19.30481  ? 61  ILE A CG2    1 
ATOM   402  C CD1    . ILE A 1 70  ? 13.49400 -2.89700  2.30500   1.000 20.58792  ? 61  ILE A CD1    1 
ATOM   403  N N      . THR A 1 71  ? 14.14700 -1.74300  -3.50300  1.000 21.63985  ? 62  THR A N      1 
ATOM   404  C CA     . THR A 1 71  ? 14.93200 -1.85900  -4.72100  1.000 25.33055  ? 62  THR A CA     1 
ATOM   405  C C      . THR A 1 71  ? 16.41700 -2.01500  -4.40500  1.000 23.73680  ? 62  THR A C      1 
ATOM   406  O O      . THR A 1 71  ? 16.87900 -1.78900  -3.28400  1.000 24.51814  ? 62  THR A O      1 
ATOM   407  C CB     . THR A 1 71  ? 14.75200 -0.63200  -5.61400  1.000 26.87915  ? 62  THR A CB     1 
ATOM   408  O OG1    . THR A 1 71  ? 15.44500 0.48100   -5.03300  1.000 20.79892  ? 62  THR A OG1    1 
ATOM   409  C CG2    . THR A 1 71  ? 13.28400 -0.28900  -5.77000  1.000 19.66411  ? 62  THR A CG2    1 
ATOM   410  N N      . GLU A 1 72  ? 17.16800 -2.39200  -5.43900  1.000 23.26186  ? 63  GLU A N      1 
ATOM   411  C CA     . GLU A 1 72  ? 18.62500 -2.38000  -5.42200  1.000 24.32394  ? 63  GLU A CA     1 
ATOM   412  C C      . GLU A 1 72  ? 19.15400 -1.00900  -5.02100  1.000 24.82790  ? 63  GLU A C      1 
ATOM   413  O O      . GLU A 1 72  ? 18.43300 -0.00900  -5.11300  1.000 20.47508  ? 63  GLU A O      1 
ATOM   414  C CB     . GLU A 1 72  ? 19.15900 -2.76400  -6.80400  1.000 24.87877  ? 63  GLU A CB     1 
ATOM   415  C CG     . GLU A 1 72  ? 18.54200 -1.94100  -7.92700  1.000 24.71712  ? 63  GLU A CG     1 
ATOM   416  C CD     . GLU A 1 72  ? 18.68600 -2.58800  -9.29300  1.000 30.65037  ? 63  GLU A CD     1 
ATOM   417  O OE1    . GLU A 1 72  ? 19.82900 -2.72600  -9.77400  1.000 29.17092  ? 63  GLU A OE1    1 
ATOM   418  O OE2    . GLU A 1 72  ? 17.65200 -2.96300  -9.88300  1.000 26.53648  ? 63  GLU A OE2    1 
ATOM   419  N N      . GLY A 1 73  ? 20.40800 -0.95400  -4.58100  1.000 23.41601  ? 64  GLY A N      1 
ATOM   420  C CA     . GLY A 1 73  ? 21.01900 0.33100   -4.29000  1.000 21.01841  ? 64  GLY A CA     1 
ATOM   421  C C      . GLY A 1 73  ? 21.01500 1.23000   -5.51400  1.000 22.86869  ? 64  GLY A C      1 
ATOM   422  O O      . GLY A 1 73  ? 21.31800 0.79800   -6.62900  1.000 17.94083  ? 64  GLY A O      1 
ATOM   423  N N      . THR A 1 74  ? 20.66100 2.49300   -5.30000  1.000 20.41034  ? 65  THR A N      1 
ATOM   424  C CA     . THR A 1 74  ? 20.46700 3.44900   -6.38100  1.000 19.41336  ? 65  THR A CA     1 
ATOM   425  C C      . THR A 1 74  ? 21.35300 4.66400   -6.14600  1.000 24.94451  ? 65  THR A C      1 
ATOM   426  O O      . THR A 1 74  ? 21.42600 5.17900   -5.02600  1.000 27.74285  ? 65  THR A O      1 
ATOM   427  C CB     . THR A 1 74  ? 18.99300 3.85700   -6.48200  1.000 24.36455  ? 65  THR A CB     1 
ATOM   428  O OG1    . THR A 1 74  ? 18.18800 2.68200   -6.65500  1.000 21.81125  ? 65  THR A OG1    1 
ATOM   429  C CG2    . THR A 1 74  ? 18.76600 4.78300   -7.66300  1.000 19.35591  ? 65  THR A CG2    1 
ATOM   430  N N      . MET A 1 75  ? 22.02900 5.11000   -7.20300  1.000 22.30634  ? 66  MET A N      1 
ATOM   431  C CA     . MET A 1 75  ? 22.96300 6.22200   -7.09100  1.000 27.77985  ? 66  MET A CA     1 
ATOM   432  C C      . MET A 1 75  ? 22.23800 7.51100   -6.72000  1.000 29.74154  ? 66  MET A C      1 
ATOM   433  O O      . MET A 1 75  ? 21.10100 7.75600   -7.13200  1.000 27.70347  ? 66  MET A O      1 
ATOM   434  C CB     . MET A 1 75  ? 23.72000 6.41400   -8.40700  1.000 23.37659  ? 66  MET A CB     1 
ATOM   435  C CG     . MET A 1 75  ? 24.66117 5.27450   -8.76656  1.000 20.09171  ? 66  MET A CG     1 
ATOM   436  S SD     . MET A 1 75  ? 25.06545 5.22904   -10.52728 1.000 31.72198  ? 66  MET A SD     1 
ATOM   437  C CE     . MET A 1 75  ? 26.06092 6.70736   -10.69999 1.000 18.00964  ? 66  MET A CE     1 
ATOM   438  N N      . ILE A 1 76  ? 22.91600 8.34500   -5.93100  1.000 27.19282  ? 67  ILE A N      1 
ATOM   439  C CA     . ILE A 1 76  ? 22.41200 9.66900   -5.58300  1.000 26.99502  ? 67  ILE A CA     1 
ATOM   440  C C      . ILE A 1 76  ? 23.18800 10.78600  -6.25800  1.000 25.98575  ? 67  ILE A C      1 
ATOM   441  O O      . ILE A 1 76  ? 22.78700 11.95600  -6.14100  1.000 32.19638  ? 67  ILE A O      1 
ATOM   442  C CB     . ILE A 1 76  ? 22.40700 9.89200   -4.05600  1.000 21.13990  ? 67  ILE A CB     1 
ATOM   443  C CG1    . ILE A 1 76  ? 23.84000 9.90800   -3.51800  1.000 22.49016  ? 67  ILE A CG1    1 
ATOM   444  C CG2    . ILE A 1 76  ? 21.57300 8.82600   -3.36500  1.000 23.58329  ? 67  ILE A CG2    1 
ATOM   445  C CD1    . ILE A 1 76  ? 23.94400 10.28600  -2.05900  1.000 25.91381  ? 67  ILE A CD1    1 
ATOM   446  N N      . SER A 1 77  ? 24.27200 10.47200  -6.95500  1.000 27.17949  ? 68  SER A N      1 
ATOM   447  C CA     . SER A 1 77  ? 25.14200 11.46700  -7.56600  1.000 28.59954  ? 68  SER A CA     1 
ATOM   448  C C      . SER A 1 77  ? 26.06100 10.74900  -8.54900  1.000 27.94710  ? 68  SER A C      1 
ATOM   449  O O      . SER A 1 77  ? 26.20500 9.52400   -8.47800  1.000 27.86824  ? 68  SER A O      1 
ATOM   450  C CB     . SER A 1 77  ? 25.96500 12.21600  -6.50500  1.000 24.29124  ? 68  SER A CB     1 
ATOM   451  O OG     . SER A 1 77  ? 26.89500 11.35000  -5.87900  1.000 26.57817  ? 68  SER A OG     1 
ATOM   452  N N      . PRO A 1 78  ? 26.68400 11.48500  -9.47600  1.000 30.04972  ? 69  PRO A N      1 
ATOM   453  C CA     . PRO A 1 78  ? 27.61000 10.84000  -10.42300 1.000 27.46074  ? 69  PRO A CA     1 
ATOM   454  C C      . PRO A 1 78  ? 28.81200 10.18000  -9.76500  1.000 28.87348  ? 69  PRO A C      1 
ATOM   455  O O      . PRO A 1 78  ? 29.49900 9.39400   -10.43000 1.000 26.39316  ? 69  PRO A O      1 
ATOM   456  C CB     . PRO A 1 78  ? 28.04700 11.99700  -11.33400 1.000 23.96264  ? 69  PRO A CB     1 
ATOM   457  C CG     . PRO A 1 78  ? 26.94800 12.99400  -11.23300 1.000 26.20983  ? 69  PRO A CG     1 
ATOM   458  C CD     . PRO A 1 78  ? 26.44300 12.89800  -9.82200  1.000 31.79268  ? 69  PRO A CD     1 
ATOM   459  N N      . THR A 1 79  ? 29.09000 10.46400  -8.49300  1.000 24.78769  ? 70  THR A N      1 
ATOM   460  C CA     . THR A 1 79  ? 30.26800 9.93400   -7.81900  1.000 30.14115  ? 70  THR A CA     1 
ATOM   461  C C      . THR A 1 79  ? 29.93600 8.83900   -6.81300  1.000 23.58916  ? 70  THR A C      1 
ATOM   462  O O      . THR A 1 79  ? 30.82500 8.40000   -6.07800  1.000 27.79791  ? 70  THR A O      1 
ATOM   463  C CB     . THR A 1 79  ? 31.02800 11.06200  -7.11700  1.000 30.05371  ? 70  THR A CB     1 
ATOM   464  O OG1    . THR A 1 79  ? 30.22800 11.58600  -6.05000  1.000 30.48299  ? 70  THR A OG1    1 
ATOM   465  C CG2    . THR A 1 79  ? 31.34900 12.17800  -8.09800  1.000 30.04212  ? 70  THR A CG2    1 
ATOM   466  N N      . SER A 1 80  ? 28.68800 8.37600   -6.76800  1.000 22.44840  ? 71  SER A N      1 
ATOM   467  C CA     . SER A 1 80  ? 28.24300 7.46100   -5.72500  1.000 24.02808  ? 71  SER A CA     1 
ATOM   468  C C      . SER A 1 80  ? 28.26400 5.99600   -6.14600  1.000 23.02967  ? 71  SER A C      1 
ATOM   469  O O      . SER A 1 80  ? 27.91000 5.13400   -5.33600  1.000 24.59422  ? 71  SER A O      1 
ATOM   470  C CB     . SER A 1 80  ? 26.83200 7.84300   -5.26000  1.000 27.17105  ? 71  SER A CB     1 
ATOM   471  O OG     . SER A 1 80  ? 25.89200 7.74100   -6.31200  1.000 31.29476  ? 71  SER A OG     1 
ATOM   472  N N      . ALA A 1 81  ? 28.67900 5.68900   -7.37200  1.000 24.32567  ? 72  ALA A N      1 
ATOM   473  C CA     . ALA A 1 81  ? 28.64400 4.32300   -7.87400  1.000 21.22237  ? 72  ALA A CA     1 
ATOM   474  C C      . ALA A 1 81  ? 29.96100 3.60000   -7.61400  1.000 23.61272  ? 72  ALA A C      1 
ATOM   475  O O      . ALA A 1 81  ? 31.04200 4.19300   -7.65500  1.000 21.81387  ? 72  ALA A O      1 
ATOM   476  C CB     . ALA A 1 81  ? 28.33800 4.30600   -9.37200  1.000 26.32228  ? 72  ALA A CB     1 
ATOM   477  N N      . GLY A 1 82  ? 29.85300 2.30100   -7.34500  1.000 25.79757  ? 73  GLY A N      1 
ATOM   478  C CA     . GLY A 1 82  ? 31.00800 1.44800   -7.14600  1.000 24.46591  ? 73  GLY A CA     1 
ATOM   479  C C      . GLY A 1 82  ? 30.80400 0.08400   -7.77400  1.000 26.09791  ? 73  GLY A C      1 
ATOM   480  O O      . GLY A 1 82  ? 31.64400 -0.81100  -7.63800  1.000 25.26705  ? 73  GLY A O      1 
ATOM   481  N N      . PHE A 1 83  ? 29.67700 -0.07900  -8.45900  1.000 25.05537  ? 74  PHE A N      1 
ATOM   482  C CA     . PHE A 1 83  ? 29.30700 -1.28100  -9.18600  1.000 21.21683  ? 74  PHE A CA     1 
ATOM   483  C C      . PHE A 1 83  ? 28.91500 -0.90500  -10.60700 1.000 25.36894  ? 74  PHE A C      1 
ATOM   484  O O      . PHE A 1 83  ? 28.48000 0.22500   -10.85400 1.000 24.72577  ? 74  PHE A O      1 
ATOM   485  C CB     . PHE A 1 83  ? 28.13600 -2.00800  -8.50600  1.000 23.19271  ? 74  PHE A CB     1 
ATOM   486  C CG     . PHE A 1 83  ? 28.55800 -3.04300  -7.50200  1.000 25.60371  ? 74  PHE A CG     1 
ATOM   487  C CD1    . PHE A 1 83  ? 28.94100 -2.67500  -6.22400  1.000 23.57644  ? 74  PHE A CD1    1 
ATOM   488  C CD2    . PHE A 1 83  ? 28.55700 -4.38800  -7.83500  1.000 24.14107  ? 74  PHE A CD2    1 
ATOM   489  C CE1    . PHE A 1 83  ? 29.32400 -3.62900  -5.29800  1.000 21.65470  ? 74  PHE A CE1    1 
ATOM   490  C CE2    . PHE A 1 83  ? 28.93700 -5.34600  -6.91300  1.000 23.59097  ? 74  PHE A CE2    1 
ATOM   491  C CZ     . PHE A 1 83  ? 29.32100 -4.96500  -5.64300  1.000 20.18925  ? 74  PHE A CZ     1 
ATOM   492  N N      . PRO A 1 84  ? 29.05800 -1.82400  -11.56100 1.000 23.07803  ? 75  PRO A N      1 
ATOM   493  C CA     . PRO A 1 84  ? 28.72000 -1.49300  -12.94900 1.000 24.15167  ? 75  PRO A CA     1 
ATOM   494  C C      . PRO A 1 84  ? 27.22100 -1.55800  -13.19500 1.000 24.41278  ? 75  PRO A C      1 
ATOM   495  O O      . PRO A 1 84  ? 26.53000 -2.45900  -12.71500 1.000 25.50658  ? 75  PRO A O      1 
ATOM   496  C CB     . PRO A 1 84  ? 29.46100 -2.56800  -13.75400 1.000 21.71989  ? 75  PRO A CB     1 
ATOM   497  C CG     . PRO A 1 84  ? 29.48400 -3.74600  -12.83700 1.000 23.99927  ? 75  PRO A CG     1 
ATOM   498  C CD     . PRO A 1 84  ? 29.59100 -3.19300  -11.43300 1.000 19.81817  ? 75  PRO A CD     1 
ATOM   499  N N      . HIS A 1 85  ? 26.72400 -0.57400  -13.94600 1.000 22.41152  ? 76  HIS A N      1 
ATOM   500  C CA     . HIS A 1 85  ? 25.33900 -0.55300  -14.42300 1.000 25.52915  ? 76  HIS A CA     1 
ATOM   501  C C      . HIS A 1 85  ? 24.33700 -0.65800  -13.27400 1.000 26.10086  ? 76  HIS A C      1 
ATOM   502  O O      . HIS A 1 85  ? 23.39300 -1.45100  -13.30800 1.000 26.21660  ? 76  HIS A O      1 
ATOM   503  C CB     . HIS A 1 85  ? 25.10800 -1.65500  -15.45800 1.000 24.34399  ? 76  HIS A CB     1 
ATOM   504  C CG     . HIS A 1 85  ? 26.08300 -1.62200  -16.59200 1.000 27.40808  ? 76  HIS A CG     1 
ATOM   505  N ND1    . HIS A 1 85  ? 26.10400 -0.60700  -17.52400 1.000 23.75587  ? 76  HIS A ND1    1 
ATOM   506  C CD2    . HIS A 1 85  ? 27.08000 -2.47000  -16.93600 1.000 26.76218  ? 76  HIS A CD2    1 
ATOM   507  C CE1    . HIS A 1 85  ? 27.06800 -0.83400  -18.39700 1.000 31.03138  ? 76  HIS A CE1    1 
ATOM   508  N NE2    . HIS A 1 85  ? 27.67600 -1.95900  -18.06300 1.000 27.76533  ? 76  HIS A NE2    1 
ATOM   509  N N      . VAL A 1 86  ? 24.54800 0.15700   -12.24600 1.000 26.66587  ? 77  VAL A N      1 
ATOM   510  C CA     . VAL A 1 86  ? 23.59300 0.27000   -11.14700 1.000 24.03017  ? 77  VAL A CA     1 
ATOM   511  C C      . VAL A 1 86  ? 22.67500 1.45000   -11.43800 1.000 27.77024  ? 77  VAL A C      1 
ATOM   512  O O      . VAL A 1 86  ? 23.13200 2.46600   -11.98100 1.000 28.35169  ? 77  VAL A O      1 
ATOM   513  C CB     . VAL A 1 86  ? 24.30300 0.43300   -9.79600  1.000 21.82105  ? 77  VAL A CB     1 
ATOM   514  C CG1    . VAL A 1 86  ? 24.93200 -0.87800  -9.38000  1.000 24.50885  ? 77  VAL A CG1    1 
ATOM   515  C CG2    . VAL A 1 86  ? 25.35400 1.53200   -9.87800  1.000 23.05974  ? 77  VAL A CG2    1 
ATOM   516  N N      . PRO A 1 87  ? 21.37700 1.35000   -11.06200 1.000 22.67720  ? 78  PRO A N      1 
ATOM   517  C CA     . PRO A 1 87  ? 20.44100 2.42700   -11.31400 1.000 23.32043  ? 78  PRO A CA     1 
ATOM   518  C C      . PRO A 1 87  ? 20.72800 3.69300   -10.54400 1.000 23.11422  ? 78  PRO A C      1 
ATOM   519  O O      . PRO A 1 87  ? 21.24000 3.62300   -9.42600  1.000 28.06256  ? 78  PRO A O      1 
ATOM   520  C CB     . PRO A 1 87  ? 19.10600 1.78300   -10.90600 1.000 22.90592  ? 78  PRO A CB     1 
ATOM   521  C CG     . PRO A 1 87  ? 19.48100 0.85600   -9.79600  1.000 26.46542  ? 78  PRO A CG     1 
ATOM   522  C CD     . PRO A 1 87  ? 20.73700 0.23500   -10.35500 1.000 19.97978  ? 78  PRO A CD     1 
ATOM   523  N N      . GLY A 1 88  ? 20.44500 4.83000   -11.16100 1.000 24.27350  ? 79  GLY A N      1 
ATOM   524  C CA     . GLY A 1 88  ? 20.57400 6.12600   -10.48800 1.000 24.29304  ? 79  GLY A CA     1 
ATOM   525  C C      . GLY A 1 88  ? 19.21800 6.78000   -10.38800 1.000 24.21340  ? 79  GLY A C      1 
ATOM   526  O O      . GLY A 1 88  ? 18.28900 6.28300   -11.02400 1.000 23.50938  ? 79  GLY A O      1 
ATOM   527  N N      . ILE A 1 89  ? 19.11000 7.82900   -9.57900  1.000 26.81052  ? 80  ILE A N      1 
ATOM   528  C CA     . ILE A 1 89  ? 17.82900 8.56800   -9.40200  1.000 27.72548  ? 80  ILE A CA     1 
ATOM   529  C C      . ILE A 1 89  ? 18.17500 10.06100  -9.28200  1.000 32.01446  ? 80  ILE A C      1 
ATOM   530  O O      . ILE A 1 89  ? 17.41000 10.80800  -8.66500  1.000 30.59359  ? 80  ILE A O      1 
ATOM   531  C CB     . ILE A 1 89  ? 17.00800 8.00600   -8.22100  1.000 33.43099  ? 80  ILE A CB     1 
ATOM   532  C CG1    . ILE A 1 89  ? 15.55500 8.50100   -8.24900  1.000 29.68876  ? 80  ILE A CG1    1 
ATOM   533  C CG2    . ILE A 1 89  ? 17.68000 8.28700   -6.87600  1.000 28.81971  ? 80  ILE A CG2    1 
ATOM   534  C CD1    . ILE A 1 89  ? 14.51600 7.40000   -8.19800  1.000 26.33944  ? 80  ILE A CD1    1 
ATOM   535  N N      . PHE A 1 90  ? 19.28200 10.47200  -9.89800  1.000 30.90640  ? 81  PHE A N      1 
ATOM   536  C CA     . PHE A 1 90  ? 19.74000 11.88200  -9.81400  1.000 32.62203  ? 81  PHE A CA     1 
ATOM   537  C C      . PHE A 1 90  ? 19.54800 12.61500  -11.15000 1.000 29.53531  ? 81  PHE A C      1 
ATOM   538  O O      . PHE A 1 90  ? 19.83000 13.81500  -11.19200 1.000 33.71530  ? 81  PHE A O      1 
ATOM   539  C CB     . PHE A 1 90  ? 21.19800 11.88000  -9.34700  1.000 31.12078  ? 81  PHE A CB     1 
ATOM   540  C CG     . PHE A 1 90  ? 22.19000 11.10200  -10.19700 1.000 31.63475  ? 81  PHE A CG     1 
ATOM   541  C CD1    . PHE A 1 90  ? 22.35900 9.73400   -10.02500 1.000 29.76672  ? 81  PHE A CD1    1 
ATOM   542  C CD2    . PHE A 1 90  ? 22.97400 11.74800  -11.14500 1.000 29.73820  ? 81  PHE A CD2    1 
ATOM   543  C CE1    . PHE A 1 90  ? 23.26700 9.03300   -10.79800 1.000 25.02914  ? 81  PHE A CE1    1 
ATOM   544  C CE2    . PHE A 1 90  ? 23.88500 11.03900  -11.90900 1.000 28.22827  ? 81  PHE A CE2    1 
ATOM   545  C CZ     . PHE A 1 90  ? 24.02800 9.68500   -11.73300 1.000 28.00226  ? 81  PHE A CZ     1 
ATOM   546  N N      . THR A 1 91  ? 19.10000 11.92100  -12.19100 1.000 26.28557  ? 82  THR A N      1 
ATOM   547  C CA     . THR A 1 91  ? 18.86300 12.55300  -13.51500 1.000 32.95599  ? 82  THR A CA     1 
ATOM   548  C C      . THR A 1 91  ? 17.38000 12.56200  -13.82700 1.000 31.83121  ? 82  THR A C      1 
ATOM   549  O O      . THR A 1 91  ? 16.66500 11.70500  -13.30000 1.000 32.46788  ? 82  THR A O      1 
ATOM   550  C CB     . THR A 1 91  ? 19.66000 11.89600  -14.64900 1.000 31.27255  ? 82  THR A CB     1 
ATOM   551  O OG1    . THR A 1 91  ? 18.93900 10.73300  -15.03600 1.000 36.14521  ? 82  THR A OG1    1 
ATOM   552  C CG2    . THR A 1 91  ? 21.08400 11.55900  -14.24500 1.000 29.83745  ? 82  THR A CG2    1 
ATOM   553  N N      . LYS A 1 92  ? 16.95400 13.48200  -14.69600 1.000 34.36617  ? 83  LYS A N      1 
ATOM   554  C CA     . LYS A 1 92  ? 15.54900 13.48200  -15.08700 1.000 36.29262  ? 83  LYS A CA     1 
ATOM   555  C C      . LYS A 1 92  ? 15.18100 12.23200  -15.87500 1.000 32.82845  ? 83  LYS A C      1 
ATOM   556  O O      . LYS A 1 92  ? 14.05500 11.73600  -15.75600 1.000 33.27866  ? 83  LYS A O      1 
ATOM   557  C CB     . LYS A 1 92  ? 15.23200 14.73600  -15.90300 1.000 41.33502  ? 83  LYS A CB     1 
ATOM   558  N N      . GLU A 1 93  ? 16.11100 11.70500  -16.67500 1.000 34.72848  ? 84  GLU A N      1 
ATOM   559  C CA     . GLU A 1 93  ? 15.81600 10.50600  -17.45200 1.000 38.87386  ? 84  GLU A CA     1 
ATOM   560  C C      . GLU A 1 93  ? 15.63300 9.29200   -16.54800 1.000 33.20866  ? 84  GLU A C      1 
ATOM   561  O O      . GLU A 1 93  ? 14.74900 8.46100   -16.78700 1.000 33.88359  ? 84  GLU A O      1 
ATOM   562  C CB     . GLU A 1 93  ? 16.92400 10.25400  -18.47400 1.000 33.37855  ? 84  GLU A CB     1 
ATOM   563  C CG     . GLU A 1 93  ? 16.71622 8.99586   -19.30239 1.000 40.20697  ? 84  GLU A CG     1 
ATOM   564  C CD     . GLU A 1 93  ? 17.76622 8.81932   -20.37975 1.000 49.77772  ? 84  GLU A CD     1 
ATOM   565  O OE1    . GLU A 1 93  ? 18.68326 9.66274   -20.46629 1.000 57.47303  ? 84  GLU A OE1    1 
ATOM   566  O OE2    . GLU A 1 93  ? 17.67176 7.83502   -21.14198 1.000 54.18462  ? 84  GLU A OE2    1 
ATOM   567  N N      . GLN A 1 94  ? 16.45700 9.17600   -15.50400 1.000 32.23107  ? 85  GLN A N      1 
ATOM   568  C CA     . GLN A 1 94  ? 16.31600 8.06900   -14.56200 1.000 31.33700  ? 85  GLN A CA     1 
ATOM   569  C C      . GLN A 1 94  ? 14.97800 8.12000   -13.83800 1.000 27.81046  ? 85  GLN A C      1 
ATOM   570  O O      . GLN A 1 94  ? 14.38900 7.07000   -13.54800 1.000 27.68735  ? 85  GLN A O      1 
ATOM   571  C CB     . GLN A 1 94  ? 17.47300 8.08500   -13.56500 1.000 28.02029  ? 85  GLN A CB     1 
ATOM   572  C CG     . GLN A 1 94  ? 18.82400 7.77400   -14.18900 1.000 27.70831  ? 85  GLN A CG     1 
ATOM   573  C CD     . GLN A 1 94  ? 19.98600 8.32000   -13.37700 1.000 32.18518  ? 85  GLN A CD     1 
ATOM   574  O OE1    . GLN A 1 94  ? 19.79100 9.03100   -12.39100 1.000 29.65890  ? 85  GLN A OE1    1 
ATOM   575  N NE2    . GLN A 1 94  ? 21.20300 7.99300   -13.79400 1.000 32.09643  ? 85  GLN A NE2    1 
ATOM   576  N N      . VAL A 1 95  ? 14.48300 9.32500   -13.54200 1.000 28.41101  ? 86  VAL A N      1 
ATOM   577  C CA     . VAL A 1 95  ? 13.17400 9.45400   -12.90700 1.000 29.80391  ? 86  VAL A CA     1 
ATOM   578  C C      . VAL A 1 95  ? 12.07900 8.92900   -13.82700 1.000 26.04520  ? 86  VAL A C      1 
ATOM   579  O O      . VAL A 1 95  ? 11.18000 8.19700   -13.39300 1.000 28.01754  ? 86  VAL A O      1 
ATOM   580  C CB     . VAL A 1 95  ? 12.91800 10.91700  -12.50000 1.000 32.56856  ? 86  VAL A CB     1 
ATOM   581  C CG1    . VAL A 1 95  ? 11.50300 11.08600  -11.96100 1.000 30.25064  ? 86  VAL A CG1    1 
ATOM   582  C CG2    . VAL A 1 95  ? 13.94100 11.37000  -11.46900 1.000 27.15602  ? 86  VAL A CG2    1 
ATOM   583  N N      . ARG A 1 96  ? 12.14400 9.27900   -15.11500 1.000 31.41096  ? 87  ARG A N      1 
ATOM   584  C CA     . ARG A 1 96  ? 11.10500 8.85500   -16.05000 1.000 34.08234  ? 87  ARG A CA     1 
ATOM   585  C C      . ARG A 1 96  ? 11.09900 7.34200   -16.22800 1.000 28.90392  ? 87  ARG A C      1 
ATOM   586  O O      . ARG A 1 96  ? 10.03100 6.72500   -16.32200 1.000 30.86524  ? 87  ARG A O      1 
ATOM   587  C CB     . ARG A 1 96  ? 11.28700 9.55100   -17.40000 1.000 35.51809  ? 87  ARG A CB     1 
ATOM   588  C CG     . ARG A 1 96  ? 11.00319 11.04488  -17.37092 1.000 36.50518  ? 87  ARG A CG     1 
ATOM   589  C CD     . ARG A 1 96  ? 10.88765 11.62328  -18.77404 1.000 50.96081  ? 87  ARG A CD     1 
ATOM   590  N NE     . ARG A 1 96  ? 12.16979 11.66261  -19.46814 1.000 49.43366  ? 87  ARG A NE     1 
ATOM   591  C CZ     . ARG A 1 96  ? 13.09929 12.58827  -19.27152 1.000 46.17080  ? 87  ARG A CZ     1 
ATOM   592  N NH1    . ARG A 1 96  ? 12.92616 13.56638  -18.39646 1.000 45.06844  ? 87  ARG A NH1    1 
ATOM   593  N NH2    . ARG A 1 96  ? 14.23049 12.52972  -19.96749 1.000 43.93954  ? 87  ARG A NH2    1 
ATOM   594  N N      . GLU A 1 97  ? 12.28100 6.72400   -16.27600 1.000 23.49843  ? 88  GLU A N      1 
ATOM   595  C CA     . GLU A 1 97  ? 12.34600 5.27600   -16.43600 1.000 24.83601  ? 88  GLU A CA     1 
ATOM   596  C C      . GLU A 1 97  ? 11.98600 4.54200   -15.15100 1.000 28.09592  ? 88  GLU A C      1 
ATOM   597  O O      . GLU A 1 97  ? 11.40400 3.45300   -15.21200 1.000 28.00871  ? 88  GLU A O      1 
ATOM   598  C CB     . GLU A 1 97  ? 13.73300 4.86400   -16.92400 1.000 27.97278  ? 88  GLU A CB     1 
ATOM   599  C CG     . GLU A 1 97  ? 14.05000 5.37500   -18.32000 1.000 32.59967  ? 88  GLU A CG     1 
ATOM   600  C CD     . GLU A 1 97  ? 12.99100 4.97900   -19.33500 1.000 38.64064  ? 88  GLU A CD     1 
ATOM   601  O OE1    . GLU A 1 97  ? 12.57600 3.80000   -19.33700 1.000 40.36123  ? 88  GLU A OE1    1 
ATOM   602  O OE2    . GLU A 1 97  ? 12.56600 5.84900   -20.12400 1.000 43.11934  ? 88  GLU A OE2    1 
ATOM   603  N N      . TRP A 1 98  ? 12.31700 5.10800   -13.98600 1.000 23.40688  ? 89  TRP A N      1 
ATOM   604  C CA     . TRP A 1 98  ? 11.83900 4.52900   -12.73300 1.000 27.57267  ? 89  TRP A CA     1 
ATOM   605  C C      . TRP A 1 98  ? 10.31900 4.56300   -12.66100 1.000 27.58686  ? 89  TRP A C      1 
ATOM   606  O O      . TRP A 1 98  ? 9.69500  3.64500   -12.11600 1.000 28.26135  ? 89  TRP A O      1 
ATOM   607  C CB     . TRP A 1 98  ? 12.43400 5.27200   -11.53500 1.000 20.03154  ? 89  TRP A CB     1 
ATOM   608  C CG     . TRP A 1 98  ? 13.71700 4.70400   -11.00800 1.000 19.95828  ? 89  TRP A CG     1 
ATOM   609  C CD1    . TRP A 1 98  ? 14.91500 5.35000   -10.90800 1.000 23.56405  ? 89  TRP A CD1    1 
ATOM   610  C CD2    . TRP A 1 98  ? 13.93200 3.38100   -10.49600 1.000 21.06367  ? 89  TRP A CD2    1 
ATOM   611  N NE1    . TRP A 1 98  ? 15.86100 4.51300   -10.36900 1.000 23.72347  ? 89  TRP A NE1    1 
ATOM   612  C CE2    . TRP A 1 98  ? 15.28400 3.29800   -10.10700 1.000 20.57214  ? 89  TRP A CE2    1 
ATOM   613  C CE3    . TRP A 1 98  ? 13.11300 2.25800   -10.33200 1.000 22.85700  ? 89  TRP A CE3    1 
ATOM   614  C CZ2    . TRP A 1 98  ? 15.83700 2.13900   -9.56400  1.000 20.58786  ? 89  TRP A CZ2    1 
ATOM   615  C CZ3    . TRP A 1 98  ? 13.66400 1.10800   -9.79100  1.000 22.61621  ? 89  TRP A CZ3    1 
ATOM   616  C CH2    . TRP A 1 98  ? 15.01300 1.05700   -9.41500  1.000 23.26317  ? 89  TRP A CH2    1 
ATOM   617  N N      . LYS A 1 99  ? 9.70800  5.62000   -13.20700 1.000 29.08157  ? 90  LYS A N      1 
ATOM   618  C CA     . LYS A 1 99  ? 8.25900  5.78100   -13.12800 1.000 30.25140  ? 90  LYS A CA     1 
ATOM   619  C C      . LYS A 1 99  ? 7.53600  4.60100   -13.76600 1.000 31.96694  ? 90  LYS A C      1 
ATOM   620  O O      . LYS A 1 99  ? 6.52000  4.12800   -13.24100 1.000 31.79355  ? 90  LYS A O      1 
ATOM   621  C CB     . LYS A 1 99  ? 7.85200  7.09500   -13.80000 1.000 33.92633  ? 90  LYS A CB     1 
ATOM   622  C CG     . LYS A 1 99  ? 6.62346  7.77226   -13.20940 1.000 36.63513  ? 90  LYS A CG     1 
ATOM   623  C CD     . LYS A 1 99  ? 5.33938  7.30736   -13.87516 1.000 50.14527  ? 90  LYS A CD     1 
ATOM   624  C CE     . LYS A 1 99  ? 4.12796  8.01581   -13.28882 1.000 47.70595  ? 90  LYS A CE     1 
ATOM   625  N NZ     . LYS A 1 99  ? 2.92341  7.14015   -13.28090 1.000 50.21032  ? 90  LYS A NZ     1 
ATOM   626  N N      . LYS A 1 100 ? 8.04900  4.11000   -14.89600 1.000 26.25353  ? 91  LYS A N      1 
ATOM   627  C CA     . LYS A 1 100 ? 7.43700  2.96100   -15.55400 1.000 28.77544  ? 91  LYS A CA     1 
ATOM   628  C C      . LYS A 1 100 ? 7.56300  1.69900   -14.71100 1.000 30.28296  ? 91  LYS A C      1 
ATOM   629  O O      . LYS A 1 100 ? 6.67800  0.83600   -14.75200 1.000 29.40843  ? 91  LYS A O      1 
ATOM   630  C CB     . LYS A 1 100 ? 8.07600  2.74900   -16.92700 1.000 27.30616  ? 91  LYS A CB     1 
ATOM   631  C CG     . LYS A 1 100 ? 8.04900  3.98100   -17.81600 1.000 29.67551  ? 91  LYS A CG     1 
ATOM   632  C CD     . LYS A 1 100 ? 8.93200  3.80300   -19.04000 1.000 33.18419  ? 91  LYS A CD     1 
ATOM   633  C CE     . LYS A 1 100 ? 8.94500  5.06000   -19.89500 1.000 35.53959  ? 91  LYS A CE     1 
ATOM   634  N NZ     . LYS A 1 100 ? 9.95400  4.97800   -20.98700 1.000 39.66716  ? 91  LYS A NZ     1 
ATOM   635  N N      . ILE A 1 101 ? 8.64700  1.57700   -13.94200 1.000 28.00250  ? 92  ILE A N      1 
ATOM   636  C CA     . ILE A 1 101 ? 8.84300  0.39500   -13.11000 1.000 27.44338  ? 92  ILE A CA     1 
ATOM   637  C C      . ILE A 1 101 ? 7.91600  0.42900   -11.90200 1.000 27.54334  ? 92  ILE A C      1 
ATOM   638  O O      . ILE A 1 101 ? 7.34100  -0.59500  -11.51400 1.000 32.80269  ? 92  ILE A O      1 
ATOM   639  C CB     . ILE A 1 101 ? 10.32000 0.28600   -12.69100 1.000 30.97054  ? 92  ILE A CB     1 
ATOM   640  C CG1    . ILE A 1 101 ? 11.20600 0.14500   -13.93000 1.000 28.14138  ? 92  ILE A CG1    1 
ATOM   641  C CG2    . ILE A 1 101 ? 10.52600 -0.88000  -11.73100 1.000 22.39275  ? 92  ILE A CG2    1 
ATOM   642  C CD1    . ILE A 1 101 ? 12.68300 0.20500   -13.63500 1.000 26.20293  ? 92  ILE A CD1    1 
ATOM   643  N N      . VAL A 1 102 ? 7.75000  1.60300   -11.29100 1.000 26.14271  ? 93  VAL A N      1 
ATOM   644  C CA     . VAL A 1 102 ? 6.90000  1.70800   -10.11000 1.000 29.83871  ? 93  VAL A CA     1 
ATOM   645  C C      . VAL A 1 102 ? 5.43400  1.50700   -10.48200 1.000 36.21991  ? 93  VAL A C      1 
ATOM   646  O O      . VAL A 1 102 ? 4.66500  0.90900   -9.72100  1.000 32.22549  ? 93  VAL A O      1 
ATOM   647  C CB     . VAL A 1 102 ? 7.13200  3.05700   -9.40600  1.000 29.98971  ? 93  VAL A CB     1 
ATOM   648  C CG1    . VAL A 1 102 ? 6.23000  3.18700   -8.19400  1.000 29.90727  ? 93  VAL A CG1    1 
ATOM   649  C CG2    . VAL A 1 102 ? 8.59300  3.19700   -9.00000  1.000 24.58479  ? 93  VAL A CG2    1 
ATOM   650  N N      . ASP A 1 103 ? 5.02400  1.99700   -11.65600 1.000 29.70400  ? 94  ASP A N      1 
ATOM   651  C CA     . ASP A 1 103 ? 3.64400  1.79900   -12.09300 1.000 31.12745  ? 94  ASP A CA     1 
ATOM   652  C C      . ASP A 1 103 ? 3.33400  0.32000   -12.27900 1.000 31.28703  ? 94  ASP A C      1 
ATOM   653  O O      . ASP A 1 103 ? 2.24600  -0.14500  -11.91900 1.000 31.52472  ? 94  ASP A O      1 
ATOM   654  C CB     . ASP A 1 103 ? 3.38400  2.56500   -13.39000 1.000 34.76703  ? 94  ASP A CB     1 
ATOM   655  C CG     . ASP A 1 103 ? 3.32800  4.06600   -13.18400 1.000 38.62707  ? 94  ASP A CG     1 
ATOM   656  O OD1    . ASP A 1 103 ? 3.37400  4.51500   -12.01900 1.000 39.21940  ? 94  ASP A OD1    1 
ATOM   657  O OD2    . ASP A 1 103 ? 3.23600  4.79800   -14.19200 1.000 47.21109  ? 94  ASP A OD2    1 
ATOM   658  N N      . VAL A 1 104 ? 4.28000  -0.43300  -12.84100 1.000 31.96827  ? 95  VAL A N      1 
ATOM   659  C CA     . VAL A 1 104 ? 4.08900  -1.86900  -13.01100 1.000 30.48838  ? 95  VAL A CA     1 
ATOM   660  C C      . VAL A 1 104 ? 4.00400  -2.56200  -11.65500 1.000 30.01707  ? 95  VAL A C      1 
ATOM   661  O O      . VAL A 1 104 ? 3.17400  -3.45600  -11.45000 1.000 31.85682  ? 95  VAL A O      1 
ATOM   662  C CB     . VAL A 1 104 ? 5.21600  -2.44300  -13.89000 1.000 33.77811  ? 95  VAL A CB     1 
ATOM   663  C CG1    . VAL A 1 104 ? 5.47920  -3.89497  -13.55524 1.000 37.84880  ? 95  VAL A CG1    1 
ATOM   664  C CG2    . VAL A 1 104 ? 4.86100  -2.29678  -15.36274 1.000 32.08187  ? 95  VAL A CG2    1 
ATOM   665  N N      . VAL A 1 105 ? 4.84200  -2.14800  -10.70200 1.000 28.02996  ? 96  VAL A N      1 
ATOM   666  C CA     . VAL A 1 105 ? 4.80700  -2.74700  -9.37100  1.000 34.69789  ? 96  VAL A CA     1 
ATOM   667  C C      . VAL A 1 105 ? 3.52300  -2.36700  -8.64100  1.000 32.45742  ? 96  VAL A C      1 
ATOM   668  O O      . VAL A 1 105 ? 2.88600  -3.21100  -7.99900  1.000 29.65961  ? 96  VAL A O      1 
ATOM   669  C CB     . VAL A 1 105 ? 6.05800  -2.33900  -8.57000  1.000 27.04631  ? 96  VAL A CB     1 
ATOM   670  C CG1    . VAL A 1 105 ? 5.94700  -2.81500  -7.13100  1.000 28.79157  ? 96  VAL A CG1    1 
ATOM   671  C CG2    . VAL A 1 105 ? 7.30800  -2.90400  -9.22300  1.000 29.04111  ? 96  VAL A CG2    1 
ATOM   672  N N      . HIS A 1 106 ? 3.12100  -1.09500  -8.72700  1.000 35.28190  ? 97  HIS A N      1 
ATOM   673  C CA     . HIS A 1 106 ? 1.90000  -0.66000  -8.05500  1.000 30.58757  ? 97  HIS A CA     1 
ATOM   674  C C      . HIS A 1 106 ? 0.65800  -1.29800  -8.66500  1.000 31.05489  ? 97  HIS A C      1 
ATOM   675  O O      . HIS A 1 106 ? -0.34400 -1.48900  -7.96600  1.000 38.25384  ? 97  HIS A O      1 
ATOM   676  C CB     . HIS A 1 106 ? 1.79000  0.86400   -8.09400  1.000 26.21715  ? 97  HIS A CB     1 
ATOM   677  C CG     . HIS A 1 106 ? 2.58300  1.55300   -7.02800  1.000 28.85880  ? 97  HIS A CG     1 
ATOM   678  N ND1    . HIS A 1 106 ? 2.87300  2.90000   -7.06700  1.000 29.37865  ? 97  HIS A ND1    1 
ATOM   679  C CD2    . HIS A 1 106 ? 3.14000  1.08200   -5.88700  1.000 32.68880  ? 97  HIS A CD2    1 
ATOM   680  C CE1    . HIS A 1 106 ? 3.57700  3.22900   -5.99900  1.000 26.68550  ? 97  HIS A CE1    1 
ATOM   681  N NE2    . HIS A 1 106 ? 3.75300  2.14300   -5.26700  1.000 31.37075  ? 97  HIS A NE2    1 
ATOM   682  N N      . ALA A 1 107 ? 0.70100  -1.63800  -9.95500  1.000 28.80911  ? 98  ALA A N      1 
ATOM   683  C CA     . ALA A 1 107 ? -0.41900 -2.34300  -10.56800 1.000 32.12467  ? 98  ALA A CA     1 
ATOM   684  C C      . ALA A 1 107 ? -0.62100 -3.72500  -9.96200  1.000 31.62157  ? 98  ALA A C      1 
ATOM   685  O O      . ALA A 1 107 ? -1.71200 -4.29200  -10.08600 1.000 30.76853  ? 98  ALA A O      1 
ATOM   686  C CB     . ALA A 1 107 ? -0.21000 -2.45600  -12.07900 1.000 30.53023  ? 98  ALA A CB     1 
ATOM   687  N N      . LYS A 1 108 ? 0.40300  -4.27800  -9.31500  1.000 31.74996  ? 99  LYS A N      1 
ATOM   688  C CA     . LYS A 1 108 ? 0.29300  -5.53400  -8.58800  1.000 33.20273  ? 99  LYS A CA     1 
ATOM   689  C C      . LYS A 1 108 ? -0.14700 -5.34000  -7.14400  1.000 29.13592  ? 99  LYS A C      1 
ATOM   690  O O      . LYS A 1 108 ? -0.34300 -6.33100  -6.43200  1.000 33.53607  ? 99  LYS A O      1 
ATOM   691  C CB     . LYS A 1 108 ? 1.63100  -6.28200  -8.62200  1.000 32.23515  ? 99  LYS A CB     1 
ATOM   692  C CG     . LYS A 1 108 ? 2.07300  -6.70100  -10.01400 1.000 40.35029  ? 99  LYS A CG     1 
ATOM   693  C CD     . LYS A 1 108 ? 1.23700  -7.85800  -10.53600 1.000 34.19825  ? 99  LYS A CD     1 
ATOM   694  C CE     . LYS A 1 108 ? 1.56900  -9.14700  -9.80000  1.000 41.04326  ? 99  LYS A CE     1 
ATOM   695  N NZ     . LYS A 1 108 ? 3.00100  -9.52400  -9.97400  1.000 37.90783  ? 99  LYS A NZ     1 
ATOM   696  N N      . GLY A 1 109 ? -0.30300 -4.09600  -6.69600  1.000 26.19800  ? 100 GLY A N      1 
ATOM   697  C CA     . GLY A 1 109 ? -0.73700 -3.84000  -5.33700  1.000 25.20306  ? 100 GLY A CA     1 
ATOM   698  C C      . GLY A 1 109 ? 0.35100  -3.95600  -4.29700  1.000 30.68691  ? 100 GLY A C      1 
ATOM   699  O O      . GLY A 1 109 ? 0.06300  -4.29900  -3.14600  1.000 32.14054  ? 100 GLY A O      1 
ATOM   700  N N      . ALA A 1 110 ? 1.59600  -3.67700  -4.66500  1.000 32.84595  ? 101 ALA A N      1 
ATOM   701  C CA     . ALA A 1 110 ? 2.73000  -3.79700  -3.76500  1.000 29.71410  ? 101 ALA A CA     1 
ATOM   702  C C      . ALA A 1 110 ? 3.26000  -2.42100  -3.38300  1.000 29.40355  ? 101 ALA A C      1 
ATOM   703  O O      . ALA A 1 110 ? 3.04500  -1.42600  -4.08100  1.000 31.89013  ? 101 ALA A O      1 
ATOM   704  C CB     . ALA A 1 110 ? 3.85000  -4.62800  -4.40000  1.000 31.47276  ? 101 ALA A CB     1 
ATOM   705  N N      . VAL A 1 111 ? 3.95500  -2.38100  -2.25200  1.000 27.28095  ? 102 VAL A N      1 
ATOM   706  C CA     . VAL A 1 111 ? 4.64800  -1.19000  -1.77700  1.000 30.74316  ? 102 VAL A CA     1 
ATOM   707  C C      . VAL A 1 111 ? 6.12500  -1.34400  -2.10600  1.000 27.55738  ? 102 VAL A C      1 
ATOM   708  O O      . VAL A 1 111 ? 6.70400  -2.42000  -1.90800  1.000 27.90265  ? 102 VAL A O      1 
ATOM   709  C CB     . VAL A 1 111 ? 4.43100  -0.99000  -0.26500  1.000 29.57273  ? 102 VAL A CB     1 
ATOM   710  C CG1    . VAL A 1 111 ? 5.11000  0.28400   0.21100   1.000 28.19851  ? 102 VAL A CG1    1 
ATOM   711  C CG2    . VAL A 1 111 ? 2.94400  -0.96700  0.05900   1.000 30.70555  ? 102 VAL A CG2    1 
ATOM   712  N N      . ILE A 1 112 ? 6.74100  -0.27800  -2.61200  1.000 23.98654  ? 103 ILE A N      1 
ATOM   713  C CA     . ILE A 1 112 ? 8.13100  -0.33700  -3.05300  1.000 22.18633  ? 103 ILE A CA     1 
ATOM   714  C C      . ILE A 1 112 ? 8.87500  0.90200   -2.56800  1.000 28.19306  ? 103 ILE A C      1 
ATOM   715  O O      . ILE A 1 112 ? 8.38900  2.02900   -2.71900  1.000 28.25877  ? 103 ILE A O      1 
ATOM   716  C CB     . ILE A 1 112 ? 8.23500  -0.49000  -4.58600  1.000 24.96936  ? 103 ILE A CB     1 
ATOM   717  C CG1    . ILE A 1 112 ? 9.69800  -0.59000  -5.02400  1.000 20.88980  ? 103 ILE A CG1    1 
ATOM   718  C CG2    . ILE A 1 112 ? 7.50700  0.64100   -5.31300  1.000 24.95269  ? 103 ILE A CG2    1 
ATOM   719  C CD1    . ILE A 1 112 ? 9.87100  -1.07400  -6.45300  1.000 19.70290  ? 103 ILE A CD1    1 
ATOM   720  N N      . PHE A 1 113 ? 10.04600 0.68800   -1.96800  1.000 24.57488  ? 104 PHE A N      1 
ATOM   721  C CA     . PHE A 1 113 ? 10.95600 1.75000   -1.56300  1.000 22.61252  ? 104 PHE A CA     1 
ATOM   722  C C      . PHE A 1 113 ? 12.22600 1.69000   -2.40300  1.000 22.28193  ? 104 PHE A C      1 
ATOM   723  O O      . PHE A 1 113 ? 12.68100 0.61100   -2.79300  1.000 22.37246  ? 104 PHE A O      1 
ATOM   724  C CB     . PHE A 1 113 ? 11.33800 1.64000   -0.08000  1.000 26.58904  ? 104 PHE A CB     1 
ATOM   725  C CG     . PHE A 1 113 ? 10.32500 2.22300   0.87000   1.000 24.82971  ? 104 PHE A CG     1 
ATOM   726  C CD1    . PHE A 1 113 ? 9.00300  2.38600   0.49600   1.000 27.94197  ? 104 PHE A CD1    1 
ATOM   727  C CD2    . PHE A 1 113 ? 10.70700 2.61300   2.14500   1.000 28.26966  ? 104 PHE A CD2    1 
ATOM   728  C CE1    . PHE A 1 113 ? 8.07800  2.92000   1.37800   1.000 28.47222  ? 104 PHE A CE1    1 
ATOM   729  C CE2    . PHE A 1 113 ? 9.78900  3.15000   3.03000   1.000 29.23272  ? 104 PHE A CE2    1 
ATOM   730  C CZ     . PHE A 1 113 ? 8.47200  3.30400   2.64500   1.000 27.11027  ? 104 PHE A CZ     1 
ATOM   731  N N      . CYS A 1 114 ? 12.80700 2.85800   -2.66300  1.000 22.62423  ? 105 CYS A N      1 
ATOM   732  C CA     . CYS A 1 114 ? 14.06000 2.96600   -3.40000  1.000 23.72468  ? 105 CYS A CA     1 
ATOM   733  C C      . CYS A 1 114 ? 15.20100 3.20000   -2.41700  1.000 24.46081  ? 105 CYS A C      1 
ATOM   734  O O      . CYS A 1 114 ? 15.17500 4.17000   -1.65200  1.000 24.47685  ? 105 CYS A O      1 
ATOM   735  C CB     . CYS A 1 114 ? 13.99700 4.09700   -4.42500  1.000 24.01512  ? 105 CYS A CB     1 
ATOM   736  S SG     . CYS A 1 114 ? 15.55300 4.37900   -5.30300  1.000 28.27934  ? 105 CYS A SG     1 
ATOM   737  N N      . GLN A 1 115 ? 16.19900 2.32000   -2.43900  1.000 22.52645  ? 106 GLN A N      1 
ATOM   738  C CA     . GLN A 1 115 ? 17.33800 2.45000   -1.53900  1.000 25.07285  ? 106 GLN A CA     1 
ATOM   739  C C      . GLN A 1 115 ? 18.35100 3.42100   -2.13200  1.000 24.39076  ? 106 GLN A C      1 
ATOM   740  O O      . GLN A 1 115 ? 18.87900 3.18600   -3.22400  1.000 22.32341  ? 106 GLN A O      1 
ATOM   741  C CB     . GLN A 1 115 ? 17.98900 1.09200   -1.28100  1.000 19.78373  ? 106 GLN A CB     1 
ATOM   742  C CG     . GLN A 1 115 ? 19.10800 1.15300   -0.24900  1.000 24.79727  ? 106 GLN A CG     1 
ATOM   743  C CD     . GLN A 1 115 ? 19.92100 -0.12700  -0.17300  1.000 24.61507  ? 106 GLN A CD     1 
ATOM   744  O OE1    . GLN A 1 115 ? 20.49100 -0.57400  -1.16700  1.000 22.93833  ? 106 GLN A OE1    1 
ATOM   745  N NE2    . GLN A 1 115 ? 19.97900 -0.72100  1.01300   1.000 19.43511  ? 106 GLN A NE2    1 
ATOM   746  N N      . LEU A 1 116 ? 18.61800 4.50900   -1.41400  1.000 23.88481  ? 107 LEU A N      1 
ATOM   747  C CA     . LEU A 1 116 ? 19.62100 5.48000   -1.83000  1.000 19.96111  ? 107 LEU A CA     1 
ATOM   748  C C      . LEU A 1 116 ? 20.99000 5.01100   -1.35100  1.000 25.44374  ? 107 LEU A C      1 
ATOM   749  O O      . LEU A 1 116 ? 21.19100 4.79600   -0.15100  1.000 24.05659  ? 107 LEU A O      1 
ATOM   750  C CB     . LEU A 1 116 ? 19.28500 6.86000   -1.27100  1.000 19.74210  ? 107 LEU A CB     1 
ATOM   751  C CG     . LEU A 1 116 ? 17.85300 7.33000   -1.54300  1.000 24.21304  ? 107 LEU A CG     1 
ATOM   752  C CD1    . LEU A 1 116 ? 17.61800 8.72300   -0.98000  1.000 19.00440  ? 107 LEU A CD1    1 
ATOM   753  C CD2    . LEU A 1 116 ? 17.54500 7.29000   -3.03500  1.000 21.63235  ? 107 LEU A CD2    1 
ATOM   754  N N      . TRP A 1 117 ? 21.93000 4.86200   -2.28200  1.000 22.51829  ? 108 TRP A N      1 
ATOM   755  C CA     . TRP A 1 117 ? 23.18200 4.15900   -2.02400  1.000 18.54819  ? 108 TRP A CA     1 
ATOM   756  C C      . TRP A 1 117 ? 24.35800 4.99100   -2.51000  1.000 26.31458  ? 108 TRP A C      1 
ATOM   757  O O      . TRP A 1 117 ? 24.43800 5.32500   -3.69700  1.000 25.01430  ? 108 TRP A O      1 
ATOM   758  C CB     . TRP A 1 117 ? 23.17200 2.79100   -2.71200  1.000 26.04650  ? 108 TRP A CB     1 
ATOM   759  C CG     . TRP A 1 117 ? 24.42000 1.97900   -2.53300  1.000 25.30436  ? 108 TRP A CG     1 
ATOM   760  C CD1    . TRP A 1 117 ? 25.30100 2.03400   -1.49100  1.000 21.64941  ? 108 TRP A CD1    1 
ATOM   761  C CD2    . TRP A 1 117 ? 24.92600 0.98800   -3.43500  1.000 20.40964  ? 108 TRP A CD2    1 
ATOM   762  N NE1    . TRP A 1 117 ? 26.32100 1.13300   -1.68700  1.000 19.03962  ? 108 TRP A NE1    1 
ATOM   763  C CE2    . TRP A 1 117 ? 26.11400 0.48000   -2.87400  1.000 22.88218  ? 108 TRP A CE2    1 
ATOM   764  C CE3    . TRP A 1 117 ? 24.48800 0.48100   -4.66300  1.000 23.10818  ? 108 TRP A CE3    1 
ATOM   765  C CZ2    . TRP A 1 117 ? 26.87000 -0.50900  -3.50000  1.000 25.66769  ? 108 TRP A CZ2    1 
ATOM   766  C CZ3    . TRP A 1 117 ? 25.23800 -0.50200  -5.28000  1.000 28.52915  ? 108 TRP A CZ3    1 
ATOM   767  C CH2    . TRP A 1 117 ? 26.41500 -0.98600  -4.69900  1.000 26.73434  ? 108 TRP A CH2    1 
ATOM   768  N N      . HIS A 1 118 ? 25.27100 5.31400   -1.59600  1.000 23.68851  ? 109 HIS A N      1 
ATOM   769  C CA     . HIS A 1 118 ? 26.55000 5.93200   -1.92700  1.000 25.73406  ? 109 HIS A CA     1 
ATOM   770  C C      . HIS A 1 118 ? 27.65300 5.00300   -1.44200  1.000 24.65275  ? 109 HIS A C      1 
ATOM   771  O O      . HIS A 1 118 ? 27.69500 4.65100   -0.25800  1.000 26.28750  ? 109 HIS A O      1 
ATOM   772  C CB     . HIS A 1 118 ? 26.68400 7.31800   -1.29000  1.000 27.28050  ? 109 HIS A CB     1 
ATOM   773  C CG     . HIS A 1 118 ? 27.77800 8.15200   -1.88500  1.000 25.17426  ? 109 HIS A CG     1 
ATOM   774  N ND1    . HIS A 1 118 ? 29.07900 7.71000   -1.99100  1.000 26.89138  ? 109 HIS A ND1    1 
ATOM   775  C CD2    . HIS A 1 118 ? 27.76400 9.40500   -2.39900  1.000 29.55774  ? 109 HIS A CD2    1 
ATOM   776  C CE1    . HIS A 1 118 ? 29.81800 8.65100   -2.55000  1.000 23.85033  ? 109 HIS A CE1    1 
ATOM   777  N NE2    . HIS A 1 118 ? 29.04500 9.69000   -2.80700  1.000 26.31976  ? 109 HIS A NE2    1 
ATOM   778  N N      . VAL A 1 119 ? 28.54200 4.60700   -2.35600  1.000 24.08303  ? 110 VAL A N      1 
ATOM   779  C CA     . VAL A 1 119 ? 29.54800 3.60000   -2.03000  1.000 23.38382  ? 110 VAL A CA     1 
ATOM   780  C C      . VAL A 1 119 ? 30.73300 4.17200   -1.26400  1.000 25.42548  ? 110 VAL A C      1 
ATOM   781  O O      . VAL A 1 119 ? 31.46000 3.41400   -0.61000  1.000 22.93045  ? 110 VAL A O      1 
ATOM   782  C CB     . VAL A 1 119 ? 30.05600 2.90100   -3.30200  1.000 22.84542  ? 110 VAL A CB     1 
ATOM   783  C CG1    . VAL A 1 119 ? 28.90800 2.23400   -4.03100  1.000 24.53554  ? 110 VAL A CG1    1 
ATOM   784  C CG2    . VAL A 1 119 ? 30.76100 3.89900   -4.21300  1.000 23.57550  ? 110 VAL A CG2    1 
ATOM   785  N N      . GLY A 1 120 ? 30.95500 5.47900   -1.32700  1.000 27.48710  ? 111 GLY A N      1 
ATOM   786  C CA     . GLY A 1 120 ? 32.10600 6.04900   -0.64800  1.000 23.19855  ? 111 GLY A CA     1 
ATOM   787  C C      . GLY A 1 120 ? 33.39700 5.56400   -1.27800  1.000 26.26194  ? 111 GLY A C      1 
ATOM   788  O O      . GLY A 1 120 ? 33.57900 5.61900   -2.50000  1.000 24.21140  ? 111 GLY A O      1 
ATOM   789  N N      . ARG A 1 121 ? 34.31000 5.07400   -0.43800  1.000 23.70462  ? 112 ARG A N      1 
ATOM   790  C CA     . ARG A 1 121 ? 35.61700 4.62900   -0.90300  1.000 26.90081  ? 112 ARG A CA     1 
ATOM   791  C C      . ARG A 1 121 ? 35.57600 3.28600   -1.62100  1.000 27.81528  ? 112 ARG A C      1 
ATOM   792  O O      . ARG A 1 121 ? 36.60300 2.86500   -2.16500  1.000 26.85026  ? 112 ARG A O      1 
ATOM   793  C CB     . ARG A 1 121 ? 36.59200 4.54300   0.27400   1.000 24.88761  ? 112 ARG A CB     1 
ATOM   794  C CG     . ARG A 1 121 ? 36.28700 3.42500   1.25300   1.000 23.58501  ? 112 ARG A CG     1 
ATOM   795  C CD     . ARG A 1 121 ? 37.33100 3.36300   2.35300   1.000 28.02937  ? 112 ARG A CD     1 
ATOM   796  N NE     . ARG A 1 121 ? 37.12500 2.21900   3.23400   1.000 25.67425  ? 112 ARG A NE     1 
ATOM   797  C CZ     . ARG A 1 121 ? 37.99300 1.81700   4.15000   1.000 23.19300  ? 112 ARG A CZ     1 
ATOM   798  N NH1    . ARG A 1 121 ? 39.13900 2.45000   4.34200   1.000 22.94344  ? 112 ARG A NH1    1 
ATOM   799  N NH2    . ARG A 1 121 ? 37.70900 0.74800   4.88800   1.000 27.18794  ? 112 ARG A NH2    1 
ATOM   800  N N      . ALA A 1 122 ? 34.43000 2.60800   -1.63500  1.000 27.26274  ? 113 ALA A N      1 
ATOM   801  C CA     . ALA A 1 122 ? 34.29800 1.31600   -2.30900  1.000 23.97143  ? 113 ALA A CA     1 
ATOM   802  C C      . ALA A 1 122 ? 33.97000 1.51800   -3.78900  1.000 30.59137  ? 113 ALA A C      1 
ATOM   803  O O      . ALA A 1 122 ? 32.95300 1.05900   -4.31000  1.000 29.64216  ? 113 ALA A O      1 
ATOM   804  C CB     . ALA A 1 122 ? 33.23900 0.46500   -1.61800  1.000 23.34192  ? 113 ALA A CB     1 
ATOM   805  N N      . SER A 1 123 ? 34.86700 2.22400   -4.47000  1.000 29.13871  ? 114 SER A N      1 
ATOM   806  C CA     . SER A 1 123 ? 34.67900 2.54400   -5.87500  1.000 25.28410  ? 114 SER A CA     1 
ATOM   807  C C      . SER A 1 123 ? 36.01100 2.36000   -6.59200  1.000 28.32070  ? 114 SER A C      1 
ATOM   808  O O      . SER A 1 123 ? 36.95700 1.77300   -6.05700  1.000 24.91290  ? 114 SER A O      1 
ATOM   809  C CB     . SER A 1 123 ? 34.11700 3.96300   -6.03600  1.000 29.28936  ? 114 SER A CB     1 
ATOM   810  O OG     . SER A 1 123 ? 33.77400 4.22700   -7.38500  1.000 24.11661  ? 114 SER A OG     1 
ATOM   811  N N      . HIS A 1 124 ? 36.07600 2.86800   -7.81900  1.000 27.89912  ? 115 HIS A N      1 
ATOM   812  C CA     . HIS A 1 124 ? 37.25400 2.74100   -8.66100  1.000 24.05191  ? 115 HIS A CA     1 
ATOM   813  C C      . HIS A 1 124 ? 37.23200 3.88900   -9.65800  1.000 26.01541  ? 115 HIS A C      1 
ATOM   814  O O      . HIS A 1 124 ? 36.18000 4.47700   -9.92500  1.000 28.61562  ? 115 HIS A O      1 
ATOM   815  C CB     . HIS A 1 124 ? 37.28400 1.38300   -9.37500  1.000 25.95886  ? 115 HIS A CB     1 
ATOM   816  C CG     . HIS A 1 124 ? 38.57500 1.08500   -10.07300 1.000 29.41046  ? 115 HIS A CG     1 
ATOM   817  N ND1    . HIS A 1 124 ? 38.86900 1.56000   -11.33400 1.000 31.65680  ? 115 HIS A ND1    1 
ATOM   818  C CD2    . HIS A 1 124 ? 39.64200 0.34300   -9.69400  1.000 29.28021  ? 115 HIS A CD2    1 
ATOM   819  C CE1    . HIS A 1 124 ? 40.06600 1.13400   -11.69500 1.000 26.29854  ? 115 HIS A CE1    1 
ATOM   820  N NE2    . HIS A 1 124 ? 40.55600 0.39100   -10.71900 1.000 29.09094  ? 115 HIS A NE2    1 
ATOM   821  N N      . GLU A 1 125 ? 38.41100 4.20700   -10.19800 1.000 26.52566  ? 116 GLU A N      1 
ATOM   822  C CA     . GLU A 1 125 ? 38.51000 5.28900   -11.17300 1.000 27.51849  ? 116 GLU A CA     1 
ATOM   823  C C      . GLU A 1 125 ? 37.59800 5.05700   -12.37300 1.000 25.70090  ? 116 GLU A C      1 
ATOM   824  O O      . GLU A 1 125 ? 37.09600 6.01900   -12.96500 1.000 29.13857  ? 116 GLU A O      1 
ATOM   825  C CB     . GLU A 1 125 ? 39.95900 5.44900   -11.63100 1.000 22.94910  ? 116 GLU A CB     1 
ATOM   826  N N      . VAL A 1 126 ? 37.36300 3.79400   -12.74100 1.000 25.19273  ? 117 VAL A N      1 
ATOM   827  C CA     . VAL A 1 126 ? 36.51400 3.49500   -13.88800 1.000 25.02541  ? 117 VAL A CA     1 
ATOM   828  C C      . VAL A 1 126 ? 35.04800 3.80000   -13.60100 1.000 30.08832  ? 117 VAL A C      1 
ATOM   829  O O      . VAL A 1 126 ? 34.25300 3.95800   -14.53700 1.000 26.76992  ? 117 VAL A O      1 
ATOM   830  C CB     . VAL A 1 126 ? 36.70500 2.02500   -14.31500 1.000 26.21361  ? 117 VAL A CB     1 
ATOM   831  C CG1    . VAL A 1 126 ? 36.00800 1.08300   -13.33900 1.000 22.72016  ? 117 VAL A CG1    1 
ATOM   832  C CG2    . VAL A 1 126 ? 36.21700 1.80500   -15.74300 1.000 22.57234  ? 117 VAL A CG2    1 
ATOM   833  N N      . TYR A 1 127 ? 34.66600 3.89900   -12.32800 1.000 25.96911  ? 118 TYR A N      1 
ATOM   834  C CA     . TYR A 1 127 ? 33.29900 4.22100   -11.94400 1.000 26.37329  ? 118 TYR A CA     1 
ATOM   835  C C      . TYR A 1 127 ? 33.09600 5.70100   -11.64800 1.000 25.18218  ? 118 TYR A C      1 
ATOM   836  O O      . TYR A 1 127 ? 31.94800 6.14400   -11.54100 1.000 25.04554  ? 118 TYR A O      1 
ATOM   837  C CB     . TYR A 1 127 ? 32.88700 3.39200   -10.71800 1.000 25.31379  ? 118 TYR A CB     1 
ATOM   838  C CG     . TYR A 1 127 ? 32.80400 1.90500   -10.99100 1.000 27.16338  ? 118 TYR A CG     1 
ATOM   839  C CD1    . TYR A 1 127 ? 32.10700 1.42200   -12.09100 1.000 23.39952  ? 118 TYR A CD1    1 
ATOM   840  C CD2    . TYR A 1 127 ? 33.43600 0.98700   -10.16100 1.000 24.61633  ? 118 TYR A CD2    1 
ATOM   841  C CE1    . TYR A 1 127 ? 32.02900 0.06800   -12.34900 1.000 22.15105  ? 118 TYR A CE1    1 
ATOM   842  C CE2    . TYR A 1 127 ? 33.36500 -0.37300  -10.41400 1.000 20.02936  ? 118 TYR A CE2    1 
ATOM   843  C CZ     . TYR A 1 127 ? 32.65900 -0.82400  -11.51000 1.000 23.09334  ? 118 TYR A CZ     1 
ATOM   844  O OH     . TYR A 1 127 ? 32.58100 -2.17300  -11.77400 1.000 25.14107  ? 118 TYR A OH     1 
ATOM   845  N N      . GLN A 1 128 ? 34.16900 6.46900   -11.52700 1.000 25.63125  ? 119 GLN A N      1 
ATOM   846  C CA     . GLN A 1 128 ? 34.12700 7.87300   -11.16200 1.000 27.88767  ? 119 GLN A CA     1 
ATOM   847  C C      . GLN A 1 128 ? 34.25600 8.76200   -12.39400 1.000 31.32904  ? 119 GLN A C      1 
ATOM   848  O O      . GLN A 1 128 ? 34.93800 8.40500   -13.35900 1.000 28.45259  ? 119 GLN A O      1 
ATOM   849  C CB     . GLN A 1 128 ? 35.25300 8.20200   -10.17800 1.000 29.43981  ? 119 GLN A CB     1 
ATOM   850  C CG     . GLN A 1 128 ? 35.10300 7.51600   -8.83200  1.000 28.46370  ? 119 GLN A CG     1 
ATOM   851  C CD     . GLN A 1 128 ? 33.84400 7.94600   -8.11000  1.000 27.34376  ? 119 GLN A CD     1 
ATOM   852  O OE1    . GLN A 1 128 ? 33.47100 9.11900   -8.14000  1.000 29.42051  ? 119 GLN A OE1    1 
ATOM   853  N NE2    . GLN A 1 128 ? 33.17300 6.99800   -7.46700  1.000 27.61519  ? 119 GLN A NE2    1 
ATOM   854  N N      . PRO A 1 129 ? 33.59800 9.92100   -12.38500 1.000 32.53993  ? 120 PRO A N      1 
ATOM   855  C CA     . PRO A 1 129 ? 33.73300 10.85500  -13.51100 1.000 33.22224  ? 120 PRO A CA     1 
ATOM   856  C C      . PRO A 1 129 ? 35.16700 11.34800  -13.64300 1.000 40.40154  ? 120 PRO A C      1 
ATOM   857  O O      . PRO A 1 129 ? 35.80900 11.71300  -12.65500 1.000 33.89465  ? 120 PRO A O      1 
ATOM   858  C CB     . PRO A 1 129 ? 32.77200 11.99400  -13.14600 1.000 38.72190  ? 120 PRO A CB     1 
ATOM   859  C CG     . PRO A 1 129 ? 31.81800 11.39500  -12.15500 1.000 32.81155  ? 120 PRO A CG     1 
ATOM   860  C CD     . PRO A 1 129 ? 32.61400 10.38400  -11.39100 1.000 29.43529  ? 120 PRO A CD     1 
ATOM   861  N N      . ALA A 1 130 ? 35.66600 11.34400  -14.88100 1.000 32.33396  ? 121 ALA A N      1 
ATOM   862  C CA     . ALA A 1 130 ? 37.02400 11.76900  -15.21800 1.000 35.22373  ? 121 ALA A CA     1 
ATOM   863  C C      . ALA A 1 130 ? 38.09000 10.96000  -14.48400 1.000 31.71764  ? 121 ALA A C      1 
ATOM   864  O O      . ALA A 1 130 ? 39.21700 11.43200  -14.30600 1.000 33.85538  ? 121 ALA A O      1 
ATOM   865  C CB     . ALA A 1 130 ? 37.22400 13.26600  -14.95100 1.000 36.35661  ? 121 ALA A CB     1 
ATOM   866  N N      . GLY A 1 131 ? 37.75700 9.74300   -14.05800 1.000 35.57253  ? 122 GLY A N      1 
ATOM   867  C CA     . GLY A 1 131 ? 38.70900 8.91600   -13.34000 1.000 31.33296  ? 122 GLY A CA     1 
ATOM   868  C C      . GLY A 1 131 ? 39.15800 9.47500   -12.01000 1.000 33.07185  ? 122 GLY A C      1 
ATOM   869  O O      . GLY A 1 131 ? 40.22700 9.10200   -11.52100 1.000 35.15945  ? 122 GLY A O      1 
ATOM   870  N N      . ALA A 1 132 ? 38.37100 10.36100  -11.40600 1.000 29.74057  ? 123 ALA A N      1 
ATOM   871  C CA     . ALA A 1 132 ? 38.76000 10.96300  -10.14100 1.000 37.61912  ? 123 ALA A CA     1 
ATOM   872  C C      . ALA A 1 132 ? 38.73200 9.92900   -9.01800  1.000 33.97887  ? 123 ALA A C      1 
ATOM   873  O O      . ALA A 1 132 ? 38.15800 8.84400   -9.14400  1.000 30.22744  ? 123 ALA A O      1 
ATOM   874  C CB     . ALA A 1 132 ? 37.84300 12.13600  -9.79600  1.000 31.55943  ? 123 ALA A CB     1 
ATOM   875  N N      . ALA A 1 133 ? 39.37200 10.27900  -7.90700  1.000 33.45730  ? 124 ALA A N      1 
ATOM   876  C CA     . ALA A 1 133 ? 39.39200 9.39200   -6.75800  1.000 34.37387  ? 124 ALA A CA     1 
ATOM   877  C C      . ALA A 1 133 ? 38.03000 9.39500   -6.06300  1.000 30.80184  ? 124 ALA A C      1 
ATOM   878  O O      . ALA A 1 133 ? 37.32600 10.40800  -6.06300  1.000 27.87004  ? 124 ALA A O      1 
ATOM   879  C CB     . ALA A 1 133 ? 40.47900 9.81300   -5.77400  1.000 33.09960  ? 124 ALA A CB     1 
ATOM   880  N N      . PRO A 1 134 ? 37.63200 8.27000   -5.47500  1.000 29.51151  ? 125 PRO A N      1 
ATOM   881  C CA     . PRO A 1 134 ? 36.39100 8.24400   -4.69500  1.000 27.84763  ? 125 PRO A CA     1 
ATOM   882  C C      . PRO A 1 134 ? 36.51300 9.10000   -3.44300  1.000 30.59064  ? 125 PRO A C      1 
ATOM   883  O O      . PRO A 1 134 ? 37.60600 9.46800   -3.00700  1.000 27.64266  ? 125 PRO A O      1 
ATOM   884  C CB     . PRO A 1 134 ? 36.22000 6.76200   -4.33800  1.000 25.83202  ? 125 PRO A CB     1 
ATOM   885  C CG     . PRO A 1 134 ? 37.11000 6.02100   -5.28900  1.000 33.47283  ? 125 PRO A CG     1 
ATOM   886  C CD     . PRO A 1 134 ? 38.25600 6.94000   -5.56500  1.000 29.26131  ? 125 PRO A CD     1 
ATOM   887  N N      . ILE A 1 135 ? 35.35900 9.41800   -2.86500  1.000 24.13962  ? 126 ILE A N      1 
ATOM   888  C CA     . ILE A 1 135 ? 35.29800 10.22900  -1.65800  1.000 27.00994  ? 126 ILE A CA     1 
ATOM   889  C C      . ILE A 1 135 ? 34.98700 9.32600   -0.47400  1.000 24.60762  ? 126 ILE A C      1 
ATOM   890  O O      . ILE A 1 135 ? 34.39200 8.25600   -0.61100  1.000 27.72406  ? 126 ILE A O      1 
ATOM   891  C CB     . ILE A 1 135 ? 34.25400 11.35900  -1.77700  1.000 22.74662  ? 126 ILE A CB     1 
ATOM   892  C CG1    . ILE A 1 135 ? 32.83900 10.77400  -1.81900  1.000 21.74671  ? 126 ILE A CG1    1 
ATOM   893  C CG2    . ILE A 1 135 ? 34.52700 12.20700  -3.00700  1.000 28.11841  ? 126 ILE A CG2    1 
ATOM   894  C CD1    . ILE A 1 135 ? 31.76100 11.75500  -1.42400  1.000 30.79281  ? 126 ILE A CD1    1 
ATOM   895  N N      . SER A 1 136 ? 35.38800 9.76500   0.71100   1.000 27.42426  ? 127 SER A N      1 
ATOM   896  C CA     . SER A 1 136 ? 35.15700 9.00700   1.93700   1.000 22.36834  ? 127 SER A CA     1 
ATOM   897  C C      . SER A 1 136 ? 35.39700 9.93300   3.12200   1.000 24.52752  ? 127 SER A C      1 
ATOM   898  O O      . SER A 1 136 ? 35.75800 11.10200  2.96200   1.000 24.81139  ? 127 SER A O      1 
ATOM   899  C CB     . SER A 1 136 ? 36.05900 7.77100   2.01200   1.000 22.34306  ? 127 SER A CB     1 
ATOM   900  O OG     . SER A 1 136 ? 35.74500 6.97800   3.14300   1.000 25.56667  ? 127 SER A OG     1 
ATOM   901  N N      . SER A 1 137 ? 35.18200 9.39300   4.32300   1.000 21.26962  ? 128 SER A N      1 
ATOM   902  C CA     . SER A 1 137 ? 35.53000 10.11400  5.53900   1.000 27.05073  ? 128 SER A CA     1 
ATOM   903  C C      . SER A 1 137 ? 37.03300 10.14400  5.77400   1.000 29.18486  ? 128 SER A C      1 
ATOM   904  O O      . SER A 1 137 ? 37.51300 10.99100  6.53400   1.000 27.27869  ? 128 SER A O      1 
ATOM   905  C CB     . SER A 1 137 ? 34.84000 9.47500   6.74200   1.000 25.04169  ? 128 SER A CB     1 
ATOM   906  O OG     . SER A 1 137 ? 35.25300 8.12800   6.89600   1.000 24.46708  ? 128 SER A OG     1 
ATOM   907  N N      . THR A 1 138 ? 37.78100 9.24700   5.13900   1.000 26.15675  ? 129 THR A N      1 
ATOM   908  C CA     . THR A 1 138 ? 39.19900 9.07300   5.40100   1.000 27.41418  ? 129 THR A CA     1 
ATOM   909  C C      . THR A 1 138 ? 39.96100 8.98600   4.08700   1.000 30.25320  ? 129 THR A C      1 
ATOM   910  O O      . THR A 1 138 ? 39.37700 8.91200   3.00300   1.000 31.34269  ? 129 THR A O      1 
ATOM   911  C CB     . THR A 1 138 ? 39.45700 7.81100   6.23700   1.000 30.69369  ? 129 THR A CB     1 
ATOM   912  O OG1    . THR A 1 138 ? 40.86600 7.64700   6.44300   1.000 34.86774  ? 129 THR A OG1    1 
ATOM   913  C CG2    . THR A 1 138 ? 38.90700 6.58200   5.53000   1.000 26.88051  ? 129 THR A CG2    1 
ATOM   914  N N      . GLU A 1 139 ? 41.28800 9.00300   4.19800   1.000 32.48748  ? 130 GLU A N      1 
ATOM   915  C CA     . GLU A 1 139 ? 42.16600 8.71900   3.07300   1.000 31.68665  ? 130 GLU A CA     1 
ATOM   916  C C      . GLU A 1 139 ? 42.60300 7.26300   3.02100   1.000 31.18712  ? 130 GLU A C      1 
ATOM   917  O O      . GLU A 1 139 ? 43.23000 6.85700   2.03800   1.000 24.88081  ? 130 GLU A O      1 
ATOM   918  C CB     . GLU A 1 139 ? 43.41000 9.61400   3.12100   1.000 35.91480  ? 130 GLU A CB     1 
ATOM   919  C CG     . GLU A 1 139 ? 43.14900 11.07800  2.83000   1.000 41.62786  ? 130 GLU A CG     1 
ATOM   920  C CD     . GLU A 1 139 ? 44.43300 11.86700  2.64700   1.000 54.05965  ? 130 GLU A CD     1 
ATOM   921  O OE1    . GLU A 1 139 ? 45.52200 11.25900  2.72900   1.000 52.21963  ? 130 GLU A OE1    1 
ATOM   922  O OE2    . GLU A 1 139 ? 44.35400 13.09200  2.42000   1.000 50.20731  ? 130 GLU A OE2    1 
ATOM   923  N N      . LYS A 1 140 ? 42.29900 6.47900   4.04700   1.000 30.41138  ? 131 LYS A N      1 
ATOM   924  C CA     . LYS A 1 140 ? 42.71500 5.08400   4.06100   1.000 31.72746  ? 131 LYS A CA     1 
ATOM   925  C C      . LYS A 1 140 ? 41.90200 4.29200   3.04500   1.000 33.68827  ? 131 LYS A C      1 
ATOM   926  O O      . LYS A 1 140 ? 40.66700 4.34100   3.07300   1.000 29.14625  ? 131 LYS A O      1 
ATOM   927  C CB     . LYS A 1 140 ? 42.54300 4.47900   5.45100   1.000 29.16995  ? 131 LYS A CB     1 
ATOM   928  C CG     . LYS A 1 140 ? 43.39700 5.12300   6.52600   1.000 36.05392  ? 131 LYS A CG     1 
ATOM   929  C CD     . LYS A 1 140 ? 43.21700 4.41200   7.85800   1.000 37.92119  ? 131 LYS A CD     1 
ATOM   930  C CE     . LYS A 1 140 ? 41.75500 4.38500   8.27300   1.000 33.92057  ? 131 LYS A CE     1 
ATOM   931  N NZ     . LYS A 1 140 ? 41.55900 3.70100   9.58100   1.000 43.48062  ? 131 LYS A NZ     1 
ATOM   932  N N      . PRO A 1 141 ? 42.54300 3.56500   2.13900   1.000 32.52290  ? 132 PRO A N      1 
ATOM   933  C CA     . PRO A 1 141 ? 41.79800 2.71600   1.20900   1.000 28.05515  ? 132 PRO A CA     1 
ATOM   934  C C      . PRO A 1 141 ? 41.39500 1.40100   1.85700   1.000 25.31465  ? 132 PRO A C      1 
ATOM   935  O O      . PRO A 1 141 ? 41.90700 1.00400   2.90600   1.000 27.77816  ? 132 PRO A O      1 
ATOM   936  C CB     . PRO A 1 141 ? 42.79900 2.48500   0.07100   1.000 30.97483  ? 132 PRO A CB     1 
ATOM   937  C CG     . PRO A 1 141 ? 44.12700 2.52500   0.75500   1.000 27.97189  ? 132 PRO A CG     1 
ATOM   938  C CD     . PRO A 1 141 ? 43.99400 3.53000   1.88000   1.000 29.03927  ? 132 PRO A CD     1 
ATOM   939  N N      . ILE A 1 142 ? 40.44300 0.72700   1.20900   1.000 26.88683  ? 133 ILE A N      1 
ATOM   940  C CA     . ILE A 1 142 ? 40.13200 -0.64400  1.58200   1.000 27.18238  ? 133 ILE A CA     1 
ATOM   941  C C      . ILE A 1 142 ? 41.36900 -1.50200  1.35700   1.000 30.32553  ? 133 ILE A C      1 
ATOM   942  O O      . ILE A 1 142 ? 42.05400 -1.38000  0.33300   1.000 30.94249  ? 133 ILE A O      1 
ATOM   943  C CB     . ILE A 1 142 ? 38.93100 -1.15700  0.76900   1.000 29.63248  ? 133 ILE A CB     1 
ATOM   944  C CG1    . ILE A 1 142 ? 37.73700 -0.21200  0.92900   1.000 27.58067  ? 133 ILE A CG1    1 
ATOM   945  C CG2    . ILE A 1 142 ? 38.55300 -2.56500  1.19400   1.000 27.49298  ? 133 ILE A CG2    1 
ATOM   946  C CD1    . ILE A 1 142 ? 36.56600 -0.54900  0.02700   1.000 27.98272  ? 133 ILE A CD1    1 
ATOM   947  N N      . SER A 1 143 ? 41.67400 -2.36500  2.32500   1.000 28.00398  ? 134 SER A N      1 
ATOM   948  C CA     . SER A 1 143 ? 42.88500 -3.17300  2.25200   1.000 32.25778  ? 134 SER A CA     1 
ATOM   949  C C      . SER A 1 143 ? 42.85500 -4.09700  1.03600   1.000 30.60720  ? 134 SER A C      1 
ATOM   950  O O      . SER A 1 143 ? 41.81300 -4.32600  0.41600   1.000 28.73212  ? 134 SER A O      1 
ATOM   951  C CB     . SER A 1 143 ? 43.06200 -3.99800  3.52600   1.000 26.65885  ? 134 SER A CB     1 
ATOM   952  O OG     . SER A 1 143 ? 42.05900 -4.99400  3.62400   1.000 33.96704  ? 134 SER A OG     1 
ATOM   953  N N      . ASN A 1 144 ? 44.02800 -4.64000  0.70300   1.000 29.54748  ? 135 ASN A N      1 
ATOM   954  C CA     . ASN A 1 144 ? 44.17800 -5.48500  -0.47900  1.000 31.77231  ? 135 ASN A CA     1 
ATOM   955  C C      . ASN A 1 144 ? 43.48900 -6.83800  -0.34400  1.000 32.44322  ? 135 ASN A C      1 
ATOM   956  O O      . ASN A 1 144 ? 43.42300 -7.57800  -1.33200  1.000 36.12029  ? 135 ASN A O      1 
ATOM   957  C CB     . ASN A 1 144 ? 45.66500 -5.68400  -0.79100  1.000 28.49086  ? 135 ASN A CB     1 
ATOM   958  C CG     . ASN A 1 144 ? 46.31800 -4.43100  -1.36500  1.000 35.75012  ? 135 ASN A CG     1 
ATOM   959  O OD1    . ASN A 1 144 ? 47.13500 -3.78400  -0.70700  1.000 34.43390  ? 135 ASN A OD1    1 
ATOM   960  N ND2    . ASN A 1 144 ? 45.96100 -4.08800  -2.59900  1.000 29.54158  ? 135 ASN A ND2    1 
ATOM   961  N N      . ARG A 1 145 ? 42.97300 -7.17600  0.84100   1.000 31.28994  ? 136 ARG A N      1 
ATOM   962  C CA     . ARG A 1 145 ? 42.21100 -8.40900  1.01800   1.000 30.05921  ? 136 ARG A CA     1 
ATOM   963  C C      . ARG A 1 145 ? 40.89200 -8.39800  0.25600   1.000 32.56916  ? 136 ARG A C      1 
ATOM   964  O O      . ARG A 1 145 ? 40.38200 -9.46800  -0.09100  1.000 30.00292  ? 136 ARG A O      1 
ATOM   965  C CB     . ARG A 1 145 ? 41.94900 -8.65500  2.50300   1.000 27.74690  ? 136 ARG A CB     1 
ATOM   966  N N      . TRP A 1 146 ? 40.33500 -7.22400  -0.01700  1.000 35.58468  ? 137 TRP A N      1 
ATOM   967  C CA     . TRP A 1 146 ? 39.09900 -7.09400  -0.77500  1.000 33.28158  ? 137 TRP A CA     1 
ATOM   968  C C      . TRP A 1 146 ? 39.40600 -6.56000  -2.16800  1.000 28.36481  ? 137 TRP A C      1 
ATOM   969  O O      . TRP A 1 146 ? 40.27500 -5.69900  -2.33400  1.000 24.61622  ? 137 TRP A O      1 
ATOM   970  C CB     . TRP A 1 146 ? 38.11100 -6.15900  -0.07000  1.000 29.59216  ? 137 TRP A CB     1 
ATOM   971  C CG     . TRP A 1 146 ? 38.01997 -6.39685  1.40069   1.000 33.47907  ? 137 TRP A CG     1 
ATOM   972  C CD1    . TRP A 1 146 ? 38.78722 -5.82234  2.37052   1.000 34.83165  ? 137 TRP A CD1    1 
ATOM   973  C CD2    . TRP A 1 146 ? 37.11055 -7.27325  2.07715   1.000 34.91617  ? 137 TRP A CD2    1 
ATOM   974  N NE1    . TRP A 1 146 ? 38.41620 -6.28654  3.60691   1.000 37.87274  ? 137 TRP A NE1    1 
ATOM   975  C CE2    . TRP A 1 146 ? 37.38788 -7.17852  3.45512   1.000 38.90089  ? 137 TRP A CE2    1 
ATOM   976  C CE3    . TRP A 1 146 ? 36.08972 -8.12854  1.65114   1.000 40.40987  ? 137 TRP A CE3    1 
ATOM   977  C CZ2    . TRP A 1 146 ? 36.68149 -7.90616  4.40970   1.000 42.16759  ? 137 TRP A CZ2    1 
ATOM   978  C CZ3    . TRP A 1 146 ? 35.39032 -8.85121  2.60165   1.000 38.50297  ? 137 TRP A CZ3    1 
ATOM   979  C CH2    . TRP A 1 146 ? 35.68963 -8.73461  3.96439   1.000 42.99565  ? 137 TRP A CH2    1 
ATOM   980  N N      . ARG A 1 147 ? 38.65869 -7.04634  -3.15582  1.000 27.62208  ? 138 ARG A N      1 
ATOM   981  C CA     . ARG A 1 147 ? 38.81280 -6.64154  -4.54239  1.000 31.02092  ? 138 ARG A CA     1 
ATOM   982  C C      . ARG A 1 147 ? 37.46602 -6.19895  -5.10069  1.000 26.91745  ? 138 ARG A C      1 
ATOM   983  O O      . ARG A 1 147 ? 36.41484 -6.71925  -4.71353  1.000 26.55770  ? 138 ARG A O      1 
ATOM   984  C CB     . ARG A 1 147 ? 39.38919 -7.78461  -5.38155  1.000 33.56037  ? 138 ARG A CB     1 
ATOM   985  C CG     . ARG A 1 147 ? 38.89627 -9.15828  -4.94604  1.000 52.85561  ? 138 ARG A CG     1 
ATOM   986  C CD     . ARG A 1 147 ? 39.15114 -10.22589 -5.98929  1.000 57.53686  ? 138 ARG A CD     1 
ATOM   987  N NE     . ARG A 1 147 ? 38.22473 -11.33870 -5.83389  1.000 64.37535  ? 138 ARG A NE     1 
ATOM   988  C CZ     . ARG A 1 147 ? 38.14242 -12.37073 -6.66140  1.000 69.43572  ? 138 ARG A CZ     1 
ATOM   989  N NH1    . ARG A 1 147 ? 38.93197 -12.47456 -7.71957  1.000 63.27538  ? 138 ARG A NH1    1 
ATOM   990  N NH2    . ARG A 1 147 ? 37.24676 -13.32187 -6.42043  1.000 72.21997  ? 138 ARG A NH2    1 
ATOM   991  N N      . ILE A 1 148 ? 37.50900 -5.23500  -6.02000  1.000 30.21808  ? 139 ILE A N      1 
ATOM   992  C CA     . ILE A 1 148 ? 36.30000 -4.63200  -6.57300  1.000 26.76181  ? 139 ILE A CA     1 
ATOM   993  C C      . ILE A 1 148 ? 36.00300 -5.25100  -7.93100  1.000 27.92946  ? 139 ILE A C      1 
ATOM   994  O O      . ILE A 1 148 ? 36.91400 -5.49400  -8.73300  1.000 32.75465  ? 139 ILE A O      1 
ATOM   995  C CB     . ILE A 1 148 ? 36.43600 -3.09800  -6.67300  1.000 25.19753  ? 139 ILE A CB     1 
ATOM   996  C CG1    . ILE A 1 148 ? 35.13900 -2.46600  -7.18600  1.000 23.36163  ? 139 ILE A CG1    1 
ATOM   997  C CG2    . ILE A 1 148 ? 37.62000 -2.70500  -7.54900  1.000 26.54571  ? 139 ILE A CG2    1 
ATOM   998  C CD1    . ILE A 1 148 ? 35.15300 -0.95200  -7.17400  1.000 20.24427  ? 139 ILE A CD1    1 
ATOM   999  N N      . LEU A 1 149 ? 34.72500 -5.52000  -8.18700  1.000 23.55888  ? 140 LEU A N      1 
ATOM   1000 C CA     . LEU A 1 149 ? 34.30900 -6.03300  -9.48500  1.000 25.54408  ? 140 LEU A CA     1 
ATOM   1001 C C      . LEU A 1 149 ? 34.43300 -4.94500  -10.54600 1.000 23.35893  ? 140 LEU A C      1 
ATOM   1002 O O      . LEU A 1 149 ? 33.95100 -3.82400  -10.36000 1.000 24.00174  ? 140 LEU A O      1 
ATOM   1003 C CB     . LEU A 1 149 ? 32.87200 -6.54500  -9.41200  1.000 23.48231  ? 140 LEU A CB     1 
ATOM   1004 C CG     . LEU A 1 149 ? 32.23400 -7.00700  -10.72200 1.000 23.78258  ? 140 LEU A CG     1 
ATOM   1005 C CD1    . LEU A 1 149 ? 32.95600 -8.22600  -11.27700 1.000 24.50247  ? 140 LEU A CD1    1 
ATOM   1006 C CD2    . LEU A 1 149 ? 30.75800 -7.29800  -10.51600 1.000 24.34492  ? 140 LEU A CD2    1 
ATOM   1007 N N      . MET A 1 150 ? 35.08300 -5.27400  -11.65600 1.000 25.61918  ? 141 MET A N      1 
ATOM   1008 C CA     . MET A 1 150 ? 35.29300 -4.33300  -12.74500 1.000 26.84669  ? 141 MET A CA     1 
ATOM   1009 C C      . MET A 1 150 ? 34.21300 -4.48900  -13.80600 1.000 24.72118  ? 141 MET A C      1 
ATOM   1010 O O      . MET A 1 150 ? 33.52800 -5.51400  -13.86600 1.000 23.04514  ? 141 MET A O      1 
ATOM   1011 C CB     . MET A 1 150 ? 36.67600 -4.54700  -13.37200 1.000 26.84291  ? 141 MET A CB     1 
ATOM   1012 C CG     . MET A 1 150 ? 37.83303 -4.27091  -12.42346 1.000 23.61002  ? 141 MET A CG     1 
ATOM   1013 S SD     . MET A 1 150 ? 37.74868 -2.63423  -11.66764 1.000 31.89324  ? 141 MET A SD     1 
ATOM   1014 C CE     . MET A 1 150 ? 38.43058 -1.61580  -12.97198 1.000 22.50972  ? 141 MET A CE     1 
ATOM   1015 N N      . PRO A 1 151 ? 34.01300 -3.46900  -14.64600 1.000 22.53276  ? 142 PRO A N      1 
ATOM   1016 C CA     . PRO A 1 151 ? 32.99400 -3.58300  -15.70400 1.000 27.82540  ? 142 PRO A CA     1 
ATOM   1017 C C      . PRO A 1 151 ? 33.17400 -4.78800  -16.61400 1.000 29.98734  ? 142 PRO A C      1 
ATOM   1018 O O      . PRO A 1 151 ? 32.17800 -5.31100  -17.13000 1.000 30.85618  ? 142 PRO A O      1 
ATOM   1019 C CB     . PRO A 1 151 ? 33.14800 -2.27200  -16.49000 1.000 29.96719  ? 142 PRO A CB     1 
ATOM   1020 C CG     . PRO A 1 151 ? 33.90200 -1.33700  -15.60500 1.000 24.52136  ? 142 PRO A CG     1 
ATOM   1021 C CD     . PRO A 1 151 ? 34.43400 -2.07600  -14.41600 1.000 25.75755  ? 142 PRO A CD     1 
ATOM   1022 N N      . ASP A 1 152 ? 34.40500 -5.25000  -16.83000 1.000 27.07395  ? 143 ASP A N      1 
ATOM   1023 C CA     . ASP A 1 152 ? 34.66200 -6.35300  -17.74700 1.000 29.28480  ? 143 ASP A CA     1 
ATOM   1024 C C      . ASP A 1 152 ? 34.60100 -7.72100  -17.07500 1.000 30.08834  ? 143 ASP A C      1 
ATOM   1025 O O      . ASP A 1 152 ? 34.97600 -8.71900  -17.69800 1.000 27.96820  ? 143 ASP A O      1 
ATOM   1026 C CB     . ASP A 1 152 ? 36.02200 -6.17100  -18.43400 1.000 28.06837  ? 143 ASP A CB     1 
ATOM   1027 C CG     . ASP A 1 152 ? 37.18900 -6.16800  -17.45500 1.000 34.17232  ? 143 ASP A CG     1 
ATOM   1028 O OD1    . ASP A 1 152 ? 36.96500 -6.29100  -16.23100 1.000 35.00848  ? 143 ASP A OD1    1 
ATOM   1029 O OD2    . ASP A 1 152 ? 38.34100 -6.03800  -17.91900 1.000 33.47071  ? 143 ASP A OD2    1 
ATOM   1030 N N      . GLY A 1 153 ? 34.14300 -7.79100  -15.82600 1.000 29.81163  ? 144 GLY A N      1 
ATOM   1031 C CA     . GLY A 1 153 ? 34.02800 -9.05000  -15.12500 1.000 29.81872  ? 144 GLY A CA     1 
ATOM   1032 C C      . GLY A 1 153 ? 35.24600 -9.45700  -14.32400 1.000 30.70562  ? 144 GLY A C      1 
ATOM   1033 O O      . GLY A 1 153 ? 35.16000 -10.41100 -13.53900 1.000 39.30353  ? 144 GLY A O      1 
ATOM   1034 N N      . THR A 1 154 ? 36.37400 -8.77400  -14.49300 1.000 30.91794  ? 145 THR A N      1 
ATOM   1035 C CA     . THR A 1 154 ? 37.56000 -9.04800  -13.69300 1.000 31.21197  ? 145 THR A CA     1 
ATOM   1036 C C      . THR A 1 154 ? 37.44200 -8.31200  -12.35900 1.000 34.48757  ? 145 THR A C      1 
ATOM   1037 O O      . THR A 1 154 ? 36.41600 -7.70400  -12.04400 1.000 32.75790  ? 145 THR A O      1 
ATOM   1038 C CB     . THR A 1 154 ? 38.82400 -8.64800  -14.45200 1.000 34.10789  ? 145 THR A CB     1 
ATOM   1039 O OG1    . THR A 1 154 ? 38.82400 -7.23200  -14.67500 1.000 34.79230  ? 145 THR A OG1    1 
ATOM   1040 C CG2    . THR A 1 154 ? 38.89200 -9.36700  -15.79200 1.000 29.51698  ? 145 THR A CG2    1 
ATOM   1041 N N      . HIS A 1 155 ? 38.50100 -8.35800  -11.55500 1.000 33.03213  ? 146 HIS A N      1 
ATOM   1042 C CA     . HIS A 1 155 ? 38.53500 -7.68600  -10.26600 1.000 33.16056  ? 146 HIS A CA     1 
ATOM   1043 C C      . HIS A 1 155 ? 39.73400 -6.75200  -10.20000 1.000 33.18268  ? 146 HIS A C      1 
ATOM   1044 O O      . HIS A 1 155 ? 40.80000 -7.05000  -10.74900 1.000 33.36012  ? 146 HIS A O      1 
ATOM   1045 C CB     . HIS A 1 155 ? 38.58100 -8.69600  -9.11400  1.000 37.50610  ? 146 HIS A CB     1 
ATOM   1046 C CG     . HIS A 1 155 ? 37.31700 -9.48300  -8.95900  1.000 40.39451  ? 146 HIS A CG     1 
ATOM   1047 N ND1    . HIS A 1 155 ? 37.00500 -10.55700 -9.76400  1.000 42.51733  ? 146 HIS A ND1    1 
ATOM   1048 C CD2    . HIS A 1 155 ? 36.27900 -9.34200  -8.10100  1.000 38.37343  ? 146 HIS A CD2    1 
ATOM   1049 C CE1    . HIS A 1 155 ? 35.83300 -11.04900 -9.40400  1.000 42.68571  ? 146 HIS A CE1    1 
ATOM   1050 N NE2    . HIS A 1 155 ? 35.37100 -10.33000 -8.39700  1.000 38.94739  ? 146 HIS A NE2    1 
ATOM   1051 N N      . GLY A 1 156 ? 39.55100 -5.62000  -9.52500  1.000 26.61559  ? 147 GLY A N      1 
ATOM   1052 C CA     . GLY A 1 156 ? 40.57600 -4.59700  -9.46900  1.000 28.91605  ? 147 GLY A CA     1 
ATOM   1053 C C      . GLY A 1 156 ? 40.94800 -4.17700  -8.06300  1.000 32.72468  ? 147 GLY A C      1 
ATOM   1054 O O      . GLY A 1 156 ? 40.59800 -4.85100  -7.09100  1.000 28.26867  ? 147 GLY A O      1 
ATOM   1055 N N      . ILE A 1 157 ? 41.65200 -3.05400  -7.94500  1.000 33.36070  ? 148 ILE A N      1 
ATOM   1056 C CA     . ILE A 1 157 ? 42.19300 -2.57800  -6.67700  1.000 26.46330  ? 148 ILE A CA     1 
ATOM   1057 C C      . ILE A 1 157 ? 41.40800 -1.35100  -6.23900  1.000 29.08524  ? 148 ILE A C      1 
ATOM   1058 O O      . ILE A 1 157 ? 41.20300 -0.42300  -7.03000  1.000 31.73337  ? 148 ILE A O      1 
ATOM   1059 C CB     . ILE A 1 157 ? 43.69000 -2.24300  -6.79500  1.000 31.97103  ? 148 ILE A CB     1 
ATOM   1060 C CG1    . ILE A 1 157 ? 44.45100 -3.38500  -7.47500  1.000 31.34003  ? 148 ILE A CG1    1 
ATOM   1061 C CG2    . ILE A 1 157 ? 44.27800 -1.93700  -5.42100  1.000 32.91354  ? 148 ILE A CG2    1 
ATOM   1062 C CD1    . ILE A 1 157 ? 44.37000 -4.70000  -6.73800  1.000 35.49069  ? 148 ILE A CD1    1 
ATOM   1063 N N      . TYR A 1 158 ? 40.98000 -1.34300  -4.98200  1.000 24.67656  ? 149 TYR A N      1 
ATOM   1064 C CA     . TYR A 1 158 ? 40.39300 -0.14300  -4.39800  1.000 25.49716  ? 149 TYR A CA     1 
ATOM   1065 C C      . TYR A 1 158 ? 41.47100 0.92100   -4.23400  1.000 28.88390  ? 149 TYR A C      1 
ATOM   1066 O O      . TYR A 1 158 ? 42.49300 0.65900   -3.58500  1.000 28.15805  ? 149 TYR A O      1 
ATOM   1067 C CB     . TYR A 1 158 ? 39.75200 -0.45000  -3.04800  1.000 24.53299  ? 149 TYR A CB     1 
ATOM   1068 C CG     . TYR A 1 158 ? 38.50900 -1.31100  -3.11200  1.000 24.74907  ? 149 TYR A CG     1 
ATOM   1069 C CD1    . TYR A 1 158 ? 37.28900 -0.78000  -3.51500  1.000 23.17102  ? 149 TYR A CD1    1 
ATOM   1070 C CD2    . TYR A 1 158 ? 38.55000 -2.65000  -2.74600  1.000 23.69814  ? 149 TYR A CD2    1 
ATOM   1071 C CE1    . TYR A 1 158 ? 36.14900 -1.56300  -3.56400  1.000 22.04333  ? 149 TYR A CE1    1 
ATOM   1072 C CE2    . TYR A 1 158 ? 37.41700 -3.44000  -2.79200  1.000 19.94768  ? 149 TYR A CE2    1 
ATOM   1073 C CZ     . TYR A 1 158 ? 36.22000 -2.89200  -3.20100  1.000 23.18222  ? 149 TYR A CZ     1 
ATOM   1074 O OH     . TYR A 1 158 ? 35.08900 -3.67500  -3.24900  1.000 24.18148  ? 149 TYR A OH     1 
ATOM   1075 N N      . PRO A 1 159 ? 41.29800 2.11300   -4.79400  1.000 27.96669  ? 150 PRO A N      1 
ATOM   1076 C CA     . PRO A 1 159 ? 42.30400 3.16800   -4.66000  1.000 28.27763  ? 150 PRO A CA     1 
ATOM   1077 C C      . PRO A 1 159 ? 42.13000 3.95200   -3.36300  1.000 30.90025  ? 150 PRO A C      1 
ATOM   1078 O O      . PRO A 1 159 ? 41.16800 3.76900   -2.61500  1.000 27.75793  ? 150 PRO A O      1 
ATOM   1079 C CB     . PRO A 1 159 ? 42.02100 4.05600   -5.87500  1.000 30.45884  ? 150 PRO A CB     1 
ATOM   1080 C CG     . PRO A 1 159 ? 40.53700 3.93100   -6.05600  1.000 27.46439  ? 150 PRO A CG     1 
ATOM   1081 C CD     . PRO A 1 159 ? 40.18400 2.51700   -5.67000  1.000 24.13248  ? 150 PRO A CD     1 
ATOM   1082 N N      . LYS A 1 160 ? 43.08500 4.84300   -3.11700  1.000 27.54806  ? 151 LYS A N      1 
ATOM   1083 C CA     . LYS A 1 160 ? 42.99200 5.73500   -1.96700  1.000 28.68564  ? 151 LYS A CA     1 
ATOM   1084 C C      . LYS A 1 160 ? 41.86400 6.73800   -2.17900  1.000 30.69325  ? 151 LYS A C      1 
ATOM   1085 O O      . LYS A 1 160 ? 41.83800 7.42600   -3.20600  1.000 31.21343  ? 151 LYS A O      1 
ATOM   1086 C CB     . LYS A 1 160 ? 44.30700 6.47700   -1.74100  1.000 34.95899  ? 151 LYS A CB     1 
ATOM   1087 C CG     . LYS A 1 160 ? 45.38200 5.65800   -1.04900  1.000 39.64019  ? 151 LYS A CG     1 
ATOM   1088 C CD     . LYS A 1 160 ? 46.58600 6.52100   -0.69900  1.000 38.59092  ? 151 LYS A CD     1 
ATOM   1089 C CE     . LYS A 1 160 ? 46.21300 7.63700   0.27100   1.000 45.86039  ? 151 LYS A CE     1 
ATOM   1090 N NZ     . LYS A 1 160 ? 45.79600 7.11900   1.60700   1.000 39.02026  ? 151 LYS A NZ     1 
ATOM   1091 N N      . PRO A 1 161 ? 40.92500 6.85200   -1.24800  1.000 31.82876  ? 152 PRO A N      1 
ATOM   1092 C CA     . PRO A 1 161 ? 39.85000 7.83600   -1.38900  1.000 30.37457  ? 152 PRO A CA     1 
ATOM   1093 C C      . PRO A 1 161 ? 40.31700 9.23100   -0.99200  1.000 33.19342  ? 152 PRO A C      1 
ATOM   1094 O O      . PRO A 1 161 ? 41.42800 9.43700   -0.50200  1.000 30.96905  ? 152 PRO A O      1 
ATOM   1095 C CB     . PRO A 1 161 ? 38.77800 7.32000   -0.42700  1.000 25.01152  ? 152 PRO A CB     1 
ATOM   1096 C CG     . PRO A 1 161 ? 39.56200 6.63500   0.64400   1.000 26.51399  ? 152 PRO A CG     1 
ATOM   1097 C CD     . PRO A 1 161 ? 40.76100 6.02100   -0.04200  1.000 27.66867  ? 152 PRO A CD     1 
ATOM   1098 N N      . ARG A 1 162 ? 39.43100 10.19700  -1.21400  1.000 30.70127  ? 153 ARG A N      1 
ATOM   1099 C CA     . ARG A 1 162 ? 39.65900 11.58900  -0.84900  1.000 31.18248  ? 153 ARG A CA     1 
ATOM   1100 C C      . ARG A 1 162 ? 38.79500 11.92400  0.36100   1.000 31.70226  ? 153 ARG A C      1 
ATOM   1101 O O      . ARG A 1 162 ? 37.56700 11.79800  0.30300   1.000 28.28273  ? 153 ARG A O      1 
ATOM   1102 C CB     . ARG A 1 162 ? 39.34200 12.51600  -2.02200  1.000 29.53813  ? 153 ARG A CB     1 
ATOM   1103 C CG     . ARG A 1 162 ? 39.52300 13.99000  -1.71700  1.000 30.66288  ? 153 ARG A CG     1 
ATOM   1104 C CD     . ARG A 1 162 ? 39.37900 14.83700  -2.97100  1.000 42.01026  ? 153 ARG A CD     1 
ATOM   1105 N NE     . ARG A 1 162 ? 38.08100 14.66300  -3.61400  1.000 35.58736  ? 153 ARG A NE     1 
ATOM   1106 C CZ     . ARG A 1 162 ? 36.99500 15.36000  -3.31000  1.000 32.28001  ? 153 ARG A CZ     1 
ATOM   1107 N NH1    . ARG A 1 162 ? 37.00700 16.27900  -2.35800  1.000 32.70851  ? 153 ARG A NH1    1 
ATOM   1108 N NH2    . ARG A 1 162 ? 35.86800 15.13100  -3.97900  1.000 31.97895  ? 153 ARG A NH2    1 
ATOM   1109 N N      . ALA A 1 163 ? 39.43600 12.34100  1.45300   1.000 29.29440  ? 154 ALA A N      1 
ATOM   1110 C CA     . ALA A 1 163 ? 38.72100 12.71500  2.66800   1.000 29.93053  ? 154 ALA A CA     1 
ATOM   1111 C C      . ALA A 1 163 ? 38.06500 14.07500  2.46900   1.000 32.39834  ? 154 ALA A C      1 
ATOM   1112 O O      . ALA A 1 163 ? 38.75500 15.08700  2.31500   1.000 36.35112  ? 154 ALA A O      1 
ATOM   1113 C CB     . ALA A 1 163 ? 39.66900 12.73500  3.86300   1.000 27.88892  ? 154 ALA A CB     1 
ATOM   1114 N N      . ILE A 1 164 ? 36.73600 14.10200  2.47900   1.000 26.13942  ? 155 ILE A N      1 
ATOM   1115 C CA     . ILE A 1 164 ? 35.99600 15.32300  2.18700   1.000 28.45420  ? 155 ILE A CA     1 
ATOM   1116 C C      . ILE A 1 164 ? 35.89200 16.18500  3.43700   1.000 32.05498  ? 155 ILE A C      1 
ATOM   1117 O O      . ILE A 1 164 ? 35.87100 15.68900  4.57000   1.000 27.01593  ? 155 ILE A O      1 
ATOM   1118 C CB     . ILE A 1 164 ? 34.60300 14.98600  1.62200   1.000 28.43590  ? 155 ILE A CB     1 
ATOM   1119 C CG1    . ILE A 1 164 ? 33.79600 14.17000  2.63500   1.000 28.63900  ? 155 ILE A CG1    1 
ATOM   1120 C CG2    . ILE A 1 164 ? 34.73700 14.22700  0.31900   1.000 28.86510  ? 155 ILE A CG2    1 
ATOM   1121 C CD1    . ILE A 1 164 ? 32.40900 13.80000  2.15800   1.000 21.22990  ? 155 ILE A CD1    1 
ATOM   1122 N N      . GLY A 1 165 ? 35.82800 17.49800  3.22500   1.000 32.62485  ? 156 GLY A N      1 
ATOM   1123 C CA     . GLY A 1 165 ? 35.59100 18.43200  4.30200   1.000 31.12969  ? 156 GLY A CA     1 
ATOM   1124 C C      . GLY A 1 165 ? 34.12000 18.52200  4.65300   1.000 32.18375  ? 156 GLY A C      1 
ATOM   1125 O O      . GLY A 1 165 ? 33.25500 17.91100  4.02700   1.000 29.25112  ? 156 GLY A O      1 
ATOM   1126 N N      . THR A 1 166 ? 33.83600 19.31800  5.68700   1.000 28.19137  ? 157 THR A N      1 
ATOM   1127 C CA     . THR A 1 166 ? 32.46400 19.42500  6.17100   1.000 29.87712  ? 157 THR A CA     1 
ATOM   1128 C C      . THR A 1 166 ? 31.56000 20.12300  5.16100   1.000 29.69802  ? 157 THR A C      1 
ATOM   1129 O O      . THR A 1 166 ? 30.34900 19.87400  5.14400   1.000 28.14250  ? 157 THR A O      1 
ATOM   1130 C CB     . THR A 1 166 ? 32.43100 20.15800  7.51100   1.000 27.45081  ? 157 THR A CB     1 
ATOM   1131 O OG1    . THR A 1 166 ? 32.87800 21.50800  7.33400   1.000 28.37709  ? 157 THR A OG1    1 
ATOM   1132 C CG2    . THR A 1 166 ? 33.33400 19.46000  8.51700   1.000 26.91900  ? 157 THR A CG2    1 
ATOM   1133 N N      . TYR A 1 167 ? 32.11800 20.99100  4.31500   1.000 31.40043  ? 158 TYR A N      1 
ATOM   1134 C CA     . TYR A 1 167 ? 31.30300 21.63100  3.28800   1.000 29.49975  ? 158 TYR A CA     1 
ATOM   1135 C C      . TYR A 1 167 ? 30.82100 20.61400  2.26100   1.000 27.83348  ? 158 TYR A C      1 
ATOM   1136 O O      . TYR A 1 167 ? 29.64700 20.61500  1.87500   1.000 26.24514  ? 158 TYR A O      1 
ATOM   1137 C CB     . TYR A 1 167 ? 32.08400 22.75400  2.60700   1.000 31.85707  ? 158 TYR A CB     1 
ATOM   1138 C CG     . TYR A 1 167 ? 31.31800 23.40700  1.48000   1.000 30.45913  ? 158 TYR A CG     1 
ATOM   1139 C CD1    . TYR A 1 167 ? 30.21700 24.21200  1.74000   1.000 33.89293  ? 158 TYR A CD1    1 
ATOM   1140 C CD2    . TYR A 1 167 ? 31.69000 23.21500  0.15600   1.000 31.52391  ? 158 TYR A CD2    1 
ATOM   1141 C CE1    . TYR A 1 167 ? 29.50900 24.80900  0.71700   1.000 32.36014  ? 158 TYR A CE1    1 
ATOM   1142 C CE2    . TYR A 1 167 ? 30.99000 23.81000  -0.87500  1.000 32.63021  ? 158 TYR A CE2    1 
ATOM   1143 C CZ     . TYR A 1 167 ? 29.90000 24.60500  -0.59000  1.000 37.22750  ? 158 TYR A CZ     1 
ATOM   1144 O OH     . TYR A 1 167 ? 29.19900 25.19900  -1.61400  1.000 41.30730  ? 158 TYR A OH     1 
ATOM   1145 N N      . GLU A 1 168 ? 31.71700 19.73500  1.80600   1.000 28.05384  ? 159 GLU A N      1 
ATOM   1146 C CA     . GLU A 1 168 ? 31.30500 18.69500  0.87000   1.000 32.22946  ? 159 GLU A CA     1 
ATOM   1147 C C      . GLU A 1 168 ? 30.39500 17.67400  1.54200   1.000 28.11167  ? 159 GLU A C      1 
ATOM   1148 O O      . GLU A 1 168 ? 29.55800 17.05700  0.87300   1.000 30.72158  ? 159 GLU A O      1 
ATOM   1149 C CB     . GLU A 1 168 ? 32.53200 18.01200  0.26200   1.000 29.88849  ? 159 GLU A CB     1 
ATOM   1150 C CG     . GLU A 1 168 ? 32.20400 17.05300  -0.87400  1.000 32.05598  ? 159 GLU A CG     1 
ATOM   1151 C CD     . GLU A 1 168 ? 33.41900 16.67300  -1.70100  1.000 37.08270  ? 159 GLU A CD     1 
ATOM   1152 O OE1    . GLU A 1 168 ? 34.48600 17.30100  -1.52700  1.000 38.96403  ? 159 GLU A OE1    1 
ATOM   1153 O OE2    . GLU A 1 168 ? 33.30500 15.74500  -2.52900  1.000 33.93148  ? 159 GLU A OE2    1 
ATOM   1154 N N      . ILE A 1 169 ? 30.53700 17.49000  2.85800   1.000 27.84267  ? 160 ILE A N      1 
ATOM   1155 C CA     . ILE A 1 169 ? 29.62700 16.61300  3.59200   1.000 25.34727  ? 160 ILE A CA     1 
ATOM   1156 C C      . ILE A 1 169 ? 28.19400 17.11200  3.46100   1.000 25.63957  ? 160 ILE A C      1 
ATOM   1157 O O      . ILE A 1 169 ? 27.26900 16.33700  3.19400   1.000 26.33671  ? 160 ILE A O      1 
ATOM   1158 C CB     . ILE A 1 169 ? 30.05700 16.50400  5.06600   1.000 26.79980  ? 160 ILE A CB     1 
ATOM   1159 C CG1    . ILE A 1 169 ? 31.32600 15.66200  5.19500   1.000 23.50452  ? 160 ILE A CG1    1 
ATOM   1160 C CG2    . ILE A 1 169 ? 28.93600 15.91800  5.91500   1.000 27.69913  ? 160 ILE A CG2    1 
ATOM   1161 C CD1    . ILE A 1 169 ? 31.82400 15.52900  6.61800   1.000 26.80091  ? 160 ILE A CD1    1 
ATOM   1162 N N      . SER A 1 170 ? 27.99200 18.42100  3.63500   1.000 23.36176  ? 161 SER A N      1 
ATOM   1163 C CA     . SER A 1 170 ? 26.65600 18.98500  3.47600   1.000 29.95691  ? 161 SER A CA     1 
ATOM   1164 C C      . SER A 1 170 ? 26.17500 18.89100  2.03200   1.000 26.16134  ? 161 SER A C      1 
ATOM   1165 O O      . SER A 1 170 ? 24.96700 18.78700  1.78900   1.000 26.87303  ? 161 SER A O      1 
ATOM   1166 C CB     . SER A 1 170 ? 26.63500 20.43800  3.95200   1.000 25.21834  ? 161 SER A CB     1 
ATOM   1167 O OG     . SER A 1 170 ? 27.49300 21.24700  3.16700   1.000 33.93088  ? 161 SER A OG     1 
ATOM   1168 N N      . GLN A 1 171 ? 27.09600 18.92200  1.06600   1.000 27.66626  ? 162 GLN A N      1 
ATOM   1169 C CA     . GLN A 1 171 ? 26.70200 18.74400  -0.32900  1.000 27.89140  ? 162 GLN A CA     1 
ATOM   1170 C C      . GLN A 1 171 ? 26.20900 17.32500  -0.58400  1.000 26.60964  ? 162 GLN A C      1 
ATOM   1171 O O      . GLN A 1 171 ? 25.21200 17.12600  -1.28800  1.000 28.82024  ? 162 GLN A O      1 
ATOM   1172 C CB     . GLN A 1 171 ? 27.86900 19.08100  -1.25700  1.000 29.65349  ? 162 GLN A CB     1 
ATOM   1173 C CG     . GLN A 1 171 ? 28.13260 20.56887  -1.42120  1.000 32.30808  ? 162 GLN A CG     1 
ATOM   1174 C CD     . GLN A 1 171 ? 29.38968 20.84787  -2.22865  1.000 45.07765  ? 162 GLN A CD     1 
ATOM   1175 O OE1    . GLN A 1 171 ? 30.34041 20.06481  -2.21083  1.000 43.41207  ? 162 GLN A OE1    1 
ATOM   1176 N NE2    . GLN A 1 171 ? 29.39710 21.96686  -2.94484  1.000 40.86094  ? 162 GLN A NE2    1 
ATOM   1177 N N      . VAL A 1 172 ? 26.89300 16.32600  -0.02000  1.000 26.34583  ? 163 VAL A N      1 
ATOM   1178 C CA     . VAL A 1 172 ? 26.44400 14.94400  -0.16400  1.000 29.14178  ? 163 VAL A CA     1 
ATOM   1179 C C      . VAL A 1 172 ? 25.09200 14.75100  0.51400   1.000 27.18956  ? 163 VAL A C      1 
ATOM   1180 O O      . VAL A 1 172 ? 24.22900 14.01800  0.01500   1.000 24.82396  ? 163 VAL A O      1 
ATOM   1181 C CB     . VAL A 1 172 ? 27.50800 13.97700  0.39000   1.000 30.31126  ? 163 VAL A CB     1 
ATOM   1182 C CG1    . VAL A 1 172 ? 27.02200 12.53800  0.31100   1.000 30.47820  ? 163 VAL A CG1    1 
ATOM   1183 C CG2    . VAL A 1 172 ? 28.81400 14.13900  -0.37200  1.000 21.76831  ? 163 VAL A CG2    1 
ATOM   1184 N N      . VAL A 1 173 ? 24.88300 15.41300  1.65600   1.000 29.27456  ? 164 VAL A N      1 
ATOM   1185 C CA     . VAL A 1 173 ? 23.58400 15.35700  2.32400   1.000 24.42170  ? 164 VAL A CA     1 
ATOM   1186 C C      . VAL A 1 173 ? 22.49500 15.91700  1.41600   1.000 24.91900  ? 164 VAL A C      1 
ATOM   1187 O O      . VAL A 1 173 ? 21.38300 15.37900  1.34900   1.000 27.10330  ? 164 VAL A O      1 
ATOM   1188 C CB     . VAL A 1 173 ? 23.64400 16.10300  3.67100   1.000 30.58523  ? 164 VAL A CB     1 
ATOM   1189 C CG1    . VAL A 1 173 ? 22.25500 16.23800  4.27300   1.000 20.90327  ? 164 VAL A CG1    1 
ATOM   1190 C CG2    . VAL A 1 173 ? 24.56900 15.37700  4.63700   1.000 28.15226  ? 164 VAL A CG2    1 
ATOM   1191 N N      . GLU A 1 174 ? 22.80100 16.99700  0.69200   1.000 24.52028  ? 165 GLU A N      1 
ATOM   1192 C CA     . GLU A 1 174 ? 21.83500 17.54400  -0.25400  1.000 30.14665  ? 165 GLU A CA     1 
ATOM   1193 C C      . GLU A 1 174 ? 21.57800 16.58700  -1.41200  1.000 28.33511  ? 165 GLU A C      1 
ATOM   1194 O O      . GLU A 1 174 ? 20.48500 16.59600  -1.99000  1.000 24.47514  ? 165 GLU A O      1 
ATOM   1195 C CB     . GLU A 1 174 ? 22.31600 18.89700  -0.78000  1.000 32.81089  ? 165 GLU A CB     1 
ATOM   1196 C CG     . GLU A 1 174 ? 21.21389 19.75329  -1.38938  1.000 41.68162  ? 165 GLU A CG     1 
ATOM   1197 C CD     . GLU A 1 174 ? 20.29130 20.34873  -0.34034  1.000 50.21197  ? 165 GLU A CD     1 
ATOM   1198 O OE1    . GLU A 1 174 ? 19.05869 20.32634  -0.54765  1.000 53.39934  ? 165 GLU A OE1    1 
ATOM   1199 O OE2    . GLU A 1 174 ? 20.79746 20.84172  0.68922   1.000 49.08910  ? 165 GLU A OE2    1 
ATOM   1200 N N      . ASP A 1 175 ? 22.56400 15.75600  -1.76500  1.000 26.99947  ? 166 ASP A N      1 
ATOM   1201 C CA     . ASP A 1 175 ? 22.34300 14.75500  -2.80500  1.000 30.84301  ? 166 ASP A CA     1 
ATOM   1202 C C      . ASP A 1 175 ? 21.34800 13.69600  -2.34800  1.000 27.21671  ? 166 ASP A C      1 
ATOM   1203 O O      . ASP A 1 175 ? 20.51300 13.24000  -3.13800  1.000 25.13322  ? 166 ASP A O      1 
ATOM   1204 C CB     . ASP A 1 175 ? 23.66700 14.10800  -3.21100  1.000 26.23611  ? 166 ASP A CB     1 
ATOM   1205 C CG     . ASP A 1 175 ? 24.56700 15.05200  -3.98200  1.000 35.05906  ? 166 ASP A CG     1 
ATOM   1206 O OD1    . ASP A 1 175 ? 24.04300 15.87600  -4.76200  1.000 37.58091  ? 166 ASP A OD1    1 
ATOM   1207 O OD2    . ASP A 1 175 ? 25.80100 14.96900  -3.80800  1.000 37.37091  ? 166 ASP A OD2    1 
ATOM   1208 N N      . TYR A 1 176 ? 21.42800 13.28300  -1.07900  1.000 23.06060  ? 167 TYR A N      1 
ATOM   1209 C CA     . TYR A 1 176 ? 20.41900 12.38100  -0.53300  1.000 25.48356  ? 167 TYR A CA     1 
ATOM   1210 C C      . TYR A 1 176 ? 19.03700 13.02000  -0.57100  1.000 26.97351  ? 167 TYR A C      1 
ATOM   1211 O O      . TYR A 1 176 ? 18.04300 12.35300  -0.88400  1.000 25.85257  ? 167 TYR A O      1 
ATOM   1212 C CB     . TYR A 1 176 ? 20.77300 11.98900  0.90300   1.000 22.89607  ? 167 TYR A CB     1 
ATOM   1213 C CG     . TYR A 1 176 ? 21.81300 10.90000  1.03500   1.000 21.73244  ? 167 TYR A CG     1 
ATOM   1214 C CD1    . TYR A 1 176 ? 21.47600 9.56400   0.84500   1.000 19.62074  ? 167 TYR A CD1    1 
ATOM   1215 C CD2    . TYR A 1 176 ? 23.12600 11.20300  1.37500   1.000 19.08980  ? 167 TYR A CD2    1 
ATOM   1216 C CE1    . TYR A 1 176 ? 22.42200 8.56300   0.97300   1.000 18.03418  ? 167 TYR A CE1    1 
ATOM   1217 C CE2    . TYR A 1 176 ? 24.07800 10.20800  1.50900   1.000 20.87190  ? 167 TYR A CE2    1 
ATOM   1218 C CZ     . TYR A 1 176 ? 23.72000 8.89200   1.30700   1.000 21.41646  ? 167 TYR A CZ     1 
ATOM   1219 O OH     . TYR A 1 176 ? 24.66500 7.90200   1.44000   1.000 20.16863  ? 167 TYR A OH     1 
ATOM   1220 N N      . ARG A 1 177 ? 18.95800 14.31500  -0.25900  1.000 24.78862  ? 168 ARG A N      1 
ATOM   1221 C CA     . ARG A 1 177 ? 17.67000 14.99900  -0.21200  1.000 26.87412  ? 168 ARG A CA     1 
ATOM   1222 C C      . ARG A 1 177 ? 17.04200 15.09200  -1.59600  1.000 28.67116  ? 168 ARG A C      1 
ATOM   1223 O O      . ARG A 1 177 ? 15.86200 14.77100  -1.77500  1.000 30.47436  ? 168 ARG A O      1 
ATOM   1224 C CB     . ARG A 1 177 ? 17.84200 16.39200  0.39400   1.000 35.73559  ? 168 ARG A CB     1 
ATOM   1225 C CG     . ARG A 1 177 ? 16.55789 17.19677  0.46492   1.000 33.74538  ? 168 ARG A CG     1 
ATOM   1226 C CD     . ARG A 1 177 ? 16.81725 18.60887  0.96093   1.000 32.00377  ? 168 ARG A CD     1 
ATOM   1227 N NE     . ARG A 1 177 ? 15.86185 18.99662  1.99173   1.000 55.26778  ? 168 ARG A NE     1 
ATOM   1228 C CZ     . ARG A 1 177 ? 14.69401 19.57948  1.75429   1.000 53.39652  ? 168 ARG A CZ     1 
ATOM   1229 N NH1    . ARG A 1 177 ? 14.30215 19.87222  0.52338   1.000 46.55565  ? 168 ARG A NH1    1 
ATOM   1230 N NH2    . ARG A 1 177 ? 13.89571 19.87023  2.77789   1.000 35.54583  ? 168 ARG A NH2    1 
ATOM   1231 N N      . ARG A 1 178 ? 17.81800 15.53700  -2.58900  1.000 24.45650  ? 169 ARG A N      1 
ATOM   1232 C CA     . ARG A 1 178 ? 17.29100 15.65400  -3.94500  1.000 29.52344  ? 169 ARG A CA     1 
ATOM   1233 C C      . ARG A 1 178 ? 16.91000 14.29100  -4.51000  1.000 28.91008  ? 169 ARG A C      1 
ATOM   1234 O O      . ARG A 1 178 ? 15.91000 14.16500  -5.22700  1.000 27.47628  ? 169 ARG A O      1 
ATOM   1235 C CB     . ARG A 1 178 ? 18.31200 16.34300  -4.85100  1.000 27.87354  ? 169 ARG A CB     1 
ATOM   1236 N N      . SER A 1 179 ? 17.69500 13.25600  -4.19800  1.000 28.97153  ? 170 SER A N      1 
ATOM   1237 C CA     . SER A 1 179 ? 17.36400 11.91700  -4.67500  1.000 27.15763  ? 170 SER A CA     1 
ATOM   1238 C C      . SER A 1 179 ? 16.09500 11.39100  -4.01900  1.000 28.20360  ? 170 SER A C      1 
ATOM   1239 O O      . SER A 1 179 ? 15.32000 10.66900  -4.65900  1.000 27.96566  ? 170 SER A O      1 
ATOM   1240 C CB     . SER A 1 179 ? 18.53000 10.96400  -4.42200  1.000 25.77137  ? 170 SER A CB     1 
ATOM   1241 O OG     . SER A 1 179 ? 19.68200 11.37700  -5.13500  1.000 31.51052  ? 170 SER A OG     1 
ATOM   1242 N N      . ALA A 1 180 ? 15.86700 11.73900  -2.74900  1.000 27.20706  ? 171 ALA A N      1 
ATOM   1243 C CA     . ALA A 1 180 ? 14.63400 11.33600  -2.08100  1.000 26.78936  ? 171 ALA A CA     1 
ATOM   1244 C C      . ALA A 1 180 ? 13.42300 12.01100  -2.71100  1.000 26.73501  ? 171 ALA A C      1 
ATOM   1245 O O      . ALA A 1 180 ? 12.36200 11.39100  -2.85300  1.000 26.85203  ? 171 ALA A O      1 
ATOM   1246 C CB     . ALA A 1 180 ? 14.71700 11.65900  -0.59000  1.000 24.18599  ? 171 ALA A CB     1 
ATOM   1247 N N      . LEU A 1 181 ? 13.56200 13.28200  -3.09500  1.000 25.05351  ? 172 LEU A N      1 
ATOM   1248 C CA     . LEU A 1 181 ? 12.47600 13.96700  -3.78800  1.000 30.62836  ? 172 LEU A CA     1 
ATOM   1249 C C      . LEU A 1 181 ? 12.24900 13.38100  -5.17800  1.000 27.77680  ? 172 LEU A C      1 
ATOM   1250 O O      . LEU A 1 181 ? 11.10200 13.27400  -5.63000  1.000 31.83915  ? 172 LEU A O      1 
ATOM   1251 C CB     . LEU A 1 181 ? 12.77300 15.46400  -3.87400  1.000 28.72238  ? 172 LEU A CB     1 
ATOM   1252 C CG     . LEU A 1 181 ? 12.68700 16.23100  -2.55300  1.000 33.14778  ? 172 LEU A CG     1 
ATOM   1253 C CD1    . LEU A 1 181 ? 13.30400 17.61200  -2.68700  1.000 27.58643  ? 172 LEU A CD1    1 
ATOM   1254 C CD2    . LEU A 1 181 ? 11.23800 16.33500  -2.09900  1.000 29.97784  ? 172 LEU A CD2    1 
ATOM   1255 N N      . ASN A 1 182 ? 13.32500 12.99100  -5.86800  1.000 23.96688  ? 173 ASN A N      1 
ATOM   1256 C CA     . ASN A 1 182 ? 13.17500 12.38500  -7.18800  1.000 27.91495  ? 173 ASN A CA     1 
ATOM   1257 C C      . ASN A 1 182 ? 12.47900 11.03200  -7.11400  1.000 30.87753  ? 173 ASN A C      1 
ATOM   1258 O O      . ASN A 1 182 ? 11.72600 10.67400  -8.02700  1.000 29.96437  ? 173 ASN A O      1 
ATOM   1259 C CB     . ASN A 1 182 ? 14.53700 12.23500  -7.86600  1.000 25.62290  ? 173 ASN A CB     1 
ATOM   1260 C CG     . ASN A 1 182 ? 15.15700 13.56800  -8.23900  1.000 26.80225  ? 173 ASN A CG     1 
ATOM   1261 O OD1    . ASN A 1 182 ? 14.45600 14.56200  -8.43400  1.000 26.38370  ? 173 ASN A OD1    1 
ATOM   1262 N ND2    . ASN A 1 182 ? 16.47900 13.59400  -8.34700  1.000 27.07943  ? 173 ASN A ND2    1 
ATOM   1263 N N      . ALA A 1 183 ? 12.71800 10.26800  -6.04500  1.000 29.69716  ? 174 ALA A N      1 
ATOM   1264 C CA     . ALA A 1 183 ? 12.04400 8.98300   -5.89500  1.000 28.71346  ? 174 ALA A CA     1 
ATOM   1265 C C      . ALA A 1 183 ? 10.54700 9.16600   -5.67700  1.000 26.67916  ? 174 ALA A C      1 
ATOM   1266 O O      . ALA A 1 183 ? 9.74000  8.38700   -6.19500  1.000 30.10087  ? 174 ALA A O      1 
ATOM   1267 C CB     . ALA A 1 183 ? 12.66300 8.19500   -4.74200  1.000 30.95032  ? 174 ALA A CB     1 
ATOM   1268 N N      . ILE A 1 184 ? 10.15900 10.18600  -4.91000  1.000 27.27542  ? 175 ILE A N      1 
ATOM   1269 C CA     . ILE A 1 184 ? 8.74000  10.47800  -4.73900  1.000 29.26004  ? 175 ILE A CA     1 
ATOM   1270 C C      . ILE A 1 184 ? 8.13900  10.95800  -6.05400  1.000 32.80044  ? 175 ILE A C      1 
ATOM   1271 O O      . ILE A 1 184 ? 7.01600  10.58200  -6.41400  1.000 28.32564  ? 175 ILE A O      1 
ATOM   1272 C CB     . ILE A 1 184 ? 8.53900  11.50600  -3.61100  1.000 35.98467  ? 175 ILE A CB     1 
ATOM   1273 C CG1    . ILE A 1 184 ? 9.01800  10.93100  -2.27500  1.000 33.93417  ? 175 ILE A CG1    1 
ATOM   1274 C CG2    . ILE A 1 184 ? 7.08200  11.93600  -3.52800  1.000 24.11634  ? 175 ILE A CG2    1 
ATOM   1275 C CD1    . ILE A 1 184 ? 8.26400  9.69600   -1.83200  1.000 29.69054  ? 175 ILE A CD1    1 
ATOM   1276 N N      . GLU A 1 185 ? 8.87900  11.78700  -6.79500  1.000 31.74539  ? 176 GLU A N      1 
ATOM   1277 C CA     . GLU A 1 185 ? 8.41200  12.22600  -8.10500  1.000 26.55024  ? 176 GLU A CA     1 
ATOM   1278 C C      . GLU A 1 185 ? 8.24800  11.05100  -9.06100  1.000 30.53047  ? 176 GLU A C      1 
ATOM   1279 O O      . GLU A 1 185 ? 7.34200  11.05700  -9.90200  1.000 30.38809  ? 176 GLU A O      1 
ATOM   1280 C CB     . GLU A 1 185 ? 9.38100  13.26000  -8.68000  1.000 26.71496  ? 176 GLU A CB     1 
ATOM   1281 C CG     . GLU A 1 185 ? 9.01900  13.75300  -10.07000 1.000 40.39973  ? 176 GLU A CG     1 
ATOM   1282 C CD     . GLU A 1 185 ? 10.04000 14.72400  -10.62700 1.000 36.32542  ? 176 GLU A CD     1 
ATOM   1283 O OE1    . GLU A 1 185 ? 10.84200 15.26500  -9.83700  1.000 48.38742  ? 176 GLU A OE1    1 
ATOM   1284 O OE2    . GLU A 1 185 ? 10.04300 14.94400  -11.85600 1.000 51.05123  ? 176 GLU A OE2    1 
ATOM   1285 N N      . ALA A 1 186 ? 9.10000  10.03100  -8.93900  1.000 26.06197  ? 177 ALA A N      1 
ATOM   1286 C CA     . ALA A 1 186 ? 8.97000  8.83300   -9.76000  1.000 27.11126  ? 177 ALA A CA     1 
ATOM   1287 C C      . ALA A 1 186 ? 7.81200  7.94400   -9.32700  1.000 29.69227  ? 177 ALA A C      1 
ATOM   1288 O O      . ALA A 1 186 ? 7.43700  7.03800   -10.08000 1.000 28.36283  ? 177 ALA A O      1 
ATOM   1289 C CB     . ALA A 1 186 ? 10.27300 8.03100   -9.73100  1.000 27.35956  ? 177 ALA A CB     1 
ATOM   1290 N N      . GLY A 1 187 ? 7.24400  8.17100   -8.14400  1.000 25.94648  ? 178 GLY A N      1 
ATOM   1291 C CA     . GLY A 1 187 ? 6.12900  7.38300   -7.65800  1.000 23.15972  ? 178 GLY A CA     1 
ATOM   1292 C C      . GLY A 1 187 ? 6.45900  6.42900   -6.53200  1.000 27.57992  ? 178 GLY A C      1 
ATOM   1293 O O      . GLY A 1 187 ? 5.56800  5.69300   -6.09100  1.000 26.19723  ? 178 GLY A O      1 
ATOM   1294 N N      . PHE A 1 188 ? 7.70100  6.41100   -6.04900  1.000 26.71105  ? 179 PHE A N      1 
ATOM   1295 C CA     . PHE A 1 188 ? 8.06400  5.50800   -4.96600  1.000 24.60709  ? 179 PHE A CA     1 
ATOM   1296 C C      . PHE A 1 188 ? 7.28300  5.84100   -3.70200  1.000 26.92134  ? 179 PHE A C      1 
ATOM   1297 O O      . PHE A 1 188 ? 7.05200  7.01000   -3.38200  1.000 31.25290  ? 179 PHE A O      1 
ATOM   1298 C CB     . PHE A 1 188 ? 9.56500  5.58200   -4.68300  1.000 22.95533  ? 179 PHE A CB     1 
ATOM   1299 C CG     . PHE A 1 188 ? 10.40500 4.78400   -5.63600  1.000 24.28129  ? 179 PHE A CG     1 
ATOM   1300 C CD1    . PHE A 1 188 ? 10.45800 3.40300   -5.54000  1.000 23.26473  ? 179 PHE A CD1    1 
ATOM   1301 C CD2    . PHE A 1 188 ? 11.15400 5.41200   -6.61800  1.000 20.63718  ? 179 PHE A CD2    1 
ATOM   1302 C CE1    . PHE A 1 188 ? 11.23100 2.66200   -6.41000  1.000 21.30652  ? 179 PHE A CE1    1 
ATOM   1303 C CE2    . PHE A 1 188 ? 11.93200 4.67600   -7.49100  1.000 24.88098  ? 179 PHE A CE2    1 
ATOM   1304 C CZ     . PHE A 1 188 ? 11.97000 3.30000   -7.38600  1.000 22.70290  ? 179 PHE A CZ     1 
ATOM   1305 N N      . ASP A 1 189 ? 6.87400  4.79700   -2.98100  1.000 29.07314  ? 180 ASP A N      1 
ATOM   1306 C CA     . ASP A 1 189 ? 6.22000  4.99600   -1.69500  1.000 24.76148  ? 180 ASP A CA     1 
ATOM   1307 C C      . ASP A 1 189 ? 7.17500  5.54900   -0.64600  1.000 28.09920  ? 180 ASP A C      1 
ATOM   1308 O O      . ASP A 1 189 ? 6.72000  6.12100   0.34900   1.000 28.41399  ? 180 ASP A O      1 
ATOM   1309 C CB     . ASP A 1 189 ? 5.61500  3.67900   -1.21300  1.000 24.52803  ? 180 ASP A CB     1 
ATOM   1310 C CG     . ASP A 1 189 ? 4.61000  3.11100   -2.19400  1.000 33.05887  ? 180 ASP A CG     1 
ATOM   1311 O OD1    . ASP A 1 189 ? 3.62800  3.81400   -2.51400  1.000 30.55904  ? 180 ASP A OD1    1 
ATOM   1312 O OD2    . ASP A 1 189 ? 4.81200  1.96800   -2.65700  1.000 28.24302  ? 180 ASP A OD2    1 
ATOM   1313 N N      . GLY A 1 190 ? 8.47700  5.39800   -0.84900  1.000 27.00764  ? 181 GLY A N      1 
ATOM   1314 C CA     . GLY A 1 190 ? 9.44000  5.91700   0.10100   1.000 23.68603  ? 181 GLY A CA     1 
ATOM   1315 C C      . GLY A 1 190 ? 10.84600 5.54700   -0.31400  1.000 27.20467  ? 181 GLY A C      1 
ATOM   1316 O O      . GLY A 1 190 ? 11.07200 4.99400   -1.39300  1.000 25.19566  ? 181 GLY A O      1 
ATOM   1317 N N      . ILE A 1 191 ? 11.79700 5.86600   0.56100   1.000 23.97487  ? 182 ILE A N      1 
ATOM   1318 C CA     . ILE A 1 191 ? 13.20200 5.56900   0.32300   1.000 24.11836  ? 182 ILE A CA     1 
ATOM   1319 C C      . ILE A 1 191 ? 13.78000 4.87600   1.54700   1.000 26.01600  ? 182 ILE A C      1 
ATOM   1320 O O      . ILE A 1 191 ? 13.28400 5.02900   2.66700   1.000 26.85483  ? 182 ILE A O      1 
ATOM   1321 C CB     . ILE A 1 191 ? 14.01800 6.83900   -0.02100  1.000 22.32737  ? 182 ILE A CB     1 
ATOM   1322 C CG1    . ILE A 1 191 ? 13.95300 7.86300   1.11600   1.000 23.34570  ? 182 ILE A CG1    1 
ATOM   1323 C CG2    . ILE A 1 191 ? 13.52700 7.45800   -1.31900  1.000 25.16484  ? 182 ILE A CG2    1 
ATOM   1324 C CD1    . ILE A 1 191 ? 15.18700 7.89700   1.99500   1.000 25.80812  ? 182 ILE A CD1    1 
ATOM   1325 N N      . GLU A 1 192 ? 14.83700 4.10000   1.32100   1.000 25.39481  ? 183 GLU A N      1 
ATOM   1326 C CA     . GLU A 1 192 ? 15.62200 3.50000   2.39000   1.000 23.72153  ? 183 GLU A CA     1 
ATOM   1327 C C      . GLU A 1 192 ? 17.04000 4.04600   2.32200   1.000 26.15139  ? 183 GLU A C      1 
ATOM   1328 O O      . GLU A 1 192 ? 17.65700 4.05200   1.25100   1.000 24.01549  ? 183 GLU A O      1 
ATOM   1329 C CB     . GLU A 1 192 ? 15.63900 1.97200   2.29300   1.000 19.59031  ? 183 GLU A CB     1 
ATOM   1330 C CG     . GLU A 1 192 ? 16.67200 1.32000   3.20300   1.000 24.74684  ? 183 GLU A CG     1 
ATOM   1331 C CD     . GLU A 1 192 ? 16.62500 -0.19500  3.16100   1.000 26.57836  ? 183 GLU A CD     1 
ATOM   1332 O OE1    . GLU A 1 192 ? 15.64000 -0.77600  3.66100   1.000 29.77059  ? 183 GLU A OE1    1 
ATOM   1333 O OE2    . GLU A 1 192 ? 17.57400 -0.80400  2.62400   1.000 29.39947  ? 183 GLU A OE2    1 
ATOM   1334 N N      . ILE A 1 193 ? 17.54700 4.50800   3.46100   1.000 22.06215  ? 184 ILE A N      1 
ATOM   1335 C CA     . ILE A 1 193 ? 18.90300 5.04000   3.54700   1.000 21.10720  ? 184 ILE A CA     1 
ATOM   1336 C C      . ILE A 1 193 ? 19.86300 3.87000   3.74300   1.000 26.94510  ? 184 ILE A C      1 
ATOM   1337 O O      . ILE A 1 193 ? 19.84900 3.20900   4.78400   1.000 25.05971  ? 184 ILE A O      1 
ATOM   1338 C CB     . ILE A 1 193 ? 19.03200 6.06200   4.68100   1.000 20.77352  ? 184 ILE A CB     1 
ATOM   1339 C CG1    . ILE A 1 193 ? 18.23300 7.32300   4.35100   1.000 19.81905  ? 184 ILE A CG1    1 
ATOM   1340 C CG2    . ILE A 1 193 ? 20.48700 6.40900   4.92100   1.000 19.45915  ? 184 ILE A CG2    1 
ATOM   1341 C CD1    . ILE A 1 193 ? 18.69900 8.02400   3.09300   1.000 23.79208  ? 184 ILE A CD1    1 
ATOM   1342 N N      . HIS A 1 194 ? 20.69700 3.60900   2.73800   1.000 19.40994  ? 185 HIS A N      1 
ATOM   1343 C CA     . HIS A 1 194 ? 21.68300 2.53100   2.80100   1.000 21.17561  ? 185 HIS A CA     1 
ATOM   1344 C C      . HIS A 1 194 ? 22.85900 3.00400   3.64400   1.000 22.54333  ? 185 HIS A C      1 
ATOM   1345 O O      . HIS A 1 194 ? 23.74200 3.71600   3.16100   1.000 23.11584  ? 185 HIS A O      1 
ATOM   1346 C CB     . HIS A 1 194 ? 22.12900 2.13200   1.39800   1.000 21.22077  ? 185 HIS A CB     1 
ATOM   1347 C CG     . HIS A 1 194 ? 22.99400 0.90800   1.35400   1.000 23.85825  ? 185 HIS A CG     1 
ATOM   1348 N ND1    . HIS A 1 194 ? 23.59400 0.37200   2.47400   1.000 24.94375  ? 185 HIS A ND1    1 
ATOM   1349 C CD2    . HIS A 1 194 ? 23.35900 0.11500   0.31800   1.000 22.35577  ? 185 HIS A CD2    1 
ATOM   1350 C CE1    . HIS A 1 194 ? 24.29200 -0.69500  2.13000   1.000 23.64973  ? 185 HIS A CE1    1 
ATOM   1351 N NE2    . HIS A 1 194 ? 24.16600 -0.87300  0.82700   1.000 23.72230  ? 185 HIS A NE2    1 
ATOM   1352 N N      . GLY A 1 195 ? 22.87700 2.60500   4.91200   1.000 21.71050  ? 186 GLY A N      1 
ATOM   1353 C CA     . GLY A 1 195 ? 23.98800 2.92800   5.78400   1.000 22.77374  ? 186 GLY A CA     1 
ATOM   1354 C C      . GLY A 1 195 ? 24.64300 1.68600   6.34800   1.000 20.66002  ? 186 GLY A C      1 
ATOM   1355 O O      . GLY A 1 195 ? 24.90800 1.60700   7.55100   1.000 26.03628  ? 186 GLY A O      1 
ATOM   1356 N N      . ALA A 1 196 ? 24.91300 0.70700   5.48600   1.000 19.11583  ? 187 ALA A N      1 
ATOM   1357 C CA     . ALA A 1 196 ? 25.42200 -0.58700  5.91300   1.000 22.29296  ? 187 ALA A CA     1 
ATOM   1358 C C      . ALA A 1 196 ? 26.52700 -1.04100  4.96800   1.000 24.03058  ? 187 ALA A C      1 
ATOM   1359 O O      . ALA A 1 196 ? 26.89900 -0.33800  4.02100   1.000 21.36813  ? 187 ALA A O      1 
ATOM   1360 C CB     . ALA A 1 196 ? 24.29300 -1.62300  5.96900   1.000 21.40713  ? 187 ALA A CB     1 
ATOM   1361 N N      . HIS A 1 197 ? 27.06800 -2.22700  5.25600   1.000 22.32565  ? 188 HIS A N      1 
ATOM   1362 C CA     . HIS A 1 197 ? 27.95200 -2.96000  4.34700   1.000 22.37562  ? 188 HIS A CA     1 
ATOM   1363 C C      . HIS A 1 197 ? 29.21400 -2.17700  3.99200   1.000 24.23779  ? 188 HIS A C      1 
ATOM   1364 O O      . HIS A 1 197 ? 29.79200 -2.37000  2.92000   1.000 26.92013  ? 188 HIS A O      1 
ATOM   1365 C CB     . HIS A 1 197 ? 27.20600 -3.37500  3.07600   1.000 26.90403  ? 188 HIS A CB     1 
ATOM   1366 C CG     . HIS A 1 197 ? 26.05900 -4.30300  3.32800   1.000 27.70553  ? 188 HIS A CG     1 
ATOM   1367 N ND1    . HIS A 1 197 ? 24.84300 -4.17400  2.69300   1.000 32.68687  ? 188 HIS A ND1    1 
ATOM   1368 C CD2    . HIS A 1 197 ? 25.94400 -5.37500  4.14700   1.000 31.70749  ? 188 HIS A CD2    1 
ATOM   1369 C CE1    . HIS A 1 197 ? 24.02700 -5.12600  3.11100   1.000 30.60068  ? 188 HIS A CE1    1 
ATOM   1370 N NE2    . HIS A 1 197 ? 24.67100 -5.86800  3.99300   1.000 32.26867  ? 188 HIS A NE2    1 
ATOM   1371 N N      . GLY A 1 198 ? 29.65500 -1.29300  4.88200   1.000 23.73631  ? 189 GLY A N      1 
ATOM   1372 C CA     . GLY A 1 198 ? 30.92800 -0.62000  4.69700   1.000 21.83889  ? 189 GLY A CA     1 
ATOM   1373 C C      . GLY A 1 198 ? 30.98100 0.38500   3.56800   1.000 25.95288  ? 189 GLY A C      1 
ATOM   1374 O O      . GLY A 1 198 ? 32.04400 0.57300   2.96900   1.000 20.59129  ? 189 GLY A O      1 
ATOM   1375 N N      . TYR A 1 199 ? 29.86700 1.03900   3.26100   1.000 23.65809  ? 190 TYR A N      1 
ATOM   1376 C CA     . TYR A 1 199 ? 29.84500 2.07700   2.24500   1.000 20.12192  ? 190 TYR A CA     1 
ATOM   1377 C C      . TYR A 1 199 ? 29.92500 3.44800   2.92500   1.000 27.00260  ? 190 TYR A C      1 
ATOM   1378 O O      . TYR A 1 199 ? 30.29800 3.54400   4.10000   1.000 25.20904  ? 190 TYR A O      1 
ATOM   1379 C CB     . TYR A 1 199 ? 28.61200 1.88000   1.35600   1.000 23.07355  ? 190 TYR A CB     1 
ATOM   1380 C CG     . TYR A 1 199 ? 28.70000 0.60300   0.54600   1.000 26.44511  ? 190 TYR A CG     1 
ATOM   1381 C CD1    . TYR A 1 199 ? 29.64300 0.46800   -0.46500  1.000 23.88308  ? 190 TYR A CD1    1 
ATOM   1382 C CD2    . TYR A 1 199 ? 27.85900 -0.47200  0.80500   1.000 23.04229  ? 190 TYR A CD2    1 
ATOM   1383 C CE1    . TYR A 1 199 ? 29.74100 -0.69700  -1.20400  1.000 23.18956  ? 190 TYR A CE1    1 
ATOM   1384 C CE2    . TYR A 1 199 ? 27.94900 -1.64200  0.07100   1.000 21.05579  ? 190 TYR A CE2    1 
ATOM   1385 C CZ     . TYR A 1 199 ? 28.89200 -1.74800  -0.93200  1.000 28.33150  ? 190 TYR A CZ     1 
ATOM   1386 O OH     . TYR A 1 199 ? 28.98900 -2.90800  -1.66600  1.000 24.45815  ? 190 TYR A OH     1 
ATOM   1387 N N      . LEU A 1 200 ? 29.56900 4.51200   2.19500   1.000 24.26858  ? 191 LEU A N      1 
ATOM   1388 C CA     . LEU A 1 200 ? 29.91300 5.87200   2.61500   1.000 25.66278  ? 191 LEU A CA     1 
ATOM   1389 C C      . LEU A 1 200 ? 29.45300 6.17000   4.03700   1.000 25.85651  ? 191 LEU A C      1 
ATOM   1390 O O      . LEU A 1 200 ? 30.23000 6.66500   4.86200   1.000 22.53895  ? 191 LEU A O      1 
ATOM   1391 C CB     . LEU A 1 200 ? 29.31600 6.89400   1.64600   1.000 25.86590  ? 191 LEU A CB     1 
ATOM   1392 C CG     . LEU A 1 200 ? 29.60800 8.34700   2.03300   1.000 21.46608  ? 191 LEU A CG     1 
ATOM   1393 C CD1    . LEU A 1 200 ? 31.10800 8.60200   2.04800   1.000 27.04744  ? 191 LEU A CD1    1 
ATOM   1394 C CD2    . LEU A 1 200 ? 28.90400 9.33300   1.11000   1.000 23.18859  ? 191 LEU A CD2    1 
ATOM   1395 N N      . ILE A 1 201 ? 28.18800 5.88300   4.34000   1.000 25.61573  ? 192 ILE A N      1 
ATOM   1396 C CA     . ILE A 1 201 ? 27.66700 6.16400   5.67300   1.000 27.38103  ? 192 ILE A CA     1 
ATOM   1397 C C      . ILE A 1 201 ? 28.35500 5.28900   6.71300   1.000 26.74136  ? 192 ILE A C      1 
ATOM   1398 O O      . ILE A 1 201 ? 28.69100 5.75100   7.81100   1.000 24.79190  ? 192 ILE A O      1 
ATOM   1399 C CB     . ILE A 1 201 ? 26.14000 5.98100   5.69100   1.000 26.33203  ? 192 ILE A CB     1 
ATOM   1400 C CG1    . ILE A 1 201 ? 25.48600 6.98900   4.74600   1.000 22.73414  ? 192 ILE A CG1    1 
ATOM   1401 C CG2    . ILE A 1 201 ? 25.59800 6.12700   7.10200   1.000 22.91512  ? 192 ILE A CG2    1 
ATOM   1402 C CD1    . ILE A 1 201 ? 23.98800 6.89200   4.69500   1.000 21.40350  ? 192 ILE A CD1    1 
ATOM   1403 N N      . ASP A 1 202 ? 28.58700 4.01800   6.38200   1.000 25.64644  ? 193 ASP A N      1 
ATOM   1404 C CA     . ASP A 1 202 ? 29.29400 3.13400   7.30100   1.000 27.40008  ? 193 ASP A CA     1 
ATOM   1405 C C      . ASP A 1 202 ? 30.73900 3.57400   7.49800   1.000 28.04353  ? 193 ASP A C      1 
ATOM   1406 O O      . ASP A 1 202 ? 31.33100 3.30300   8.54900   1.000 26.62448  ? 193 ASP A O      1 
ATOM   1407 C CB     . ASP A 1 202 ? 29.23700 1.69700   6.78700   1.000 27.15867  ? 193 ASP A CB     1 
ATOM   1408 C CG     . ASP A 1 202 ? 29.06900 0.68500   7.90100   1.000 29.80230  ? 193 ASP A CG     1 
ATOM   1409 O OD1    . ASP A 1 202 ? 28.73800 1.09400   9.03400   1.000 35.18774  ? 193 ASP A OD1    1 
ATOM   1410 O OD2    . ASP A 1 202 ? 29.26900 -0.52100  7.64300   1.000 28.53081  ? 193 ASP A OD2    1 
ATOM   1411 N N      . GLN A 1 203 ? 31.31800 4.25900   6.50700   1.000 18.64839  ? 194 GLN A N      1 
ATOM   1412 C CA     . GLN A 1 203 ? 32.68200 4.75800   6.63100   1.000 24.07294  ? 194 GLN A CA     1 
ATOM   1413 C C      . GLN A 1 203 ? 32.79400 5.88900   7.64600   1.000 23.87536  ? 194 GLN A C      1 
ATOM   1414 O O      . GLN A 1 203 ? 33.89400 6.15000   8.14500   1.000 21.02127  ? 194 GLN A O      1 
ATOM   1415 C CB     . GLN A 1 203 ? 33.19600 5.21300   5.26100   1.000 21.81298  ? 194 GLN A CB     1 
ATOM   1416 C CG     . GLN A 1 203 ? 33.38200 4.06800   4.27200   1.000 19.40762  ? 194 GLN A CG     1 
ATOM   1417 C CD     . GLN A 1 203 ? 33.33900 4.52000   2.82200   1.000 24.12329  ? 194 GLN A CD     1 
ATOM   1418 O OE1    . GLN A 1 203 ? 33.63200 5.67300   2.50800   1.000 26.12994  ? 194 GLN A OE1    1 
ATOM   1419 N NE2    . GLN A 1 203 ? 32.96500 3.60900   1.93100   1.000 20.83895  ? 194 GLN A NE2    1 
ATOM   1420 N N      . PHE A 1 204 ? 31.68800 6.56300   7.96300   1.000 23.87370  ? 195 PHE A N      1 
ATOM   1421 C CA     . PHE A 1 204 ? 31.67300 7.52800   9.05600   1.000 24.77250  ? 195 PHE A CA     1 
ATOM   1422 C C      . PHE A 1 204 ? 31.34200 6.88500   10.39700  1.000 24.32152  ? 195 PHE A C      1 
ATOM   1423 O O      . PHE A 1 204 ? 31.81500 7.35900   11.43600  1.000 29.18846  ? 195 PHE A O      1 
ATOM   1424 C CB     . PHE A 1 204 ? 30.66700 8.64700   8.76700   1.000 22.21175  ? 195 PHE A CB     1 
ATOM   1425 C CG     . PHE A 1 204 ? 31.19100 9.71800   7.84900   1.000 26.54377  ? 195 PHE A CG     1 
ATOM   1426 C CD1    . PHE A 1 204 ? 31.10100 9.57900   6.47400   1.000 24.25569  ? 195 PHE A CD1    1 
ATOM   1427 C CD2    . PHE A 1 204 ? 31.76800 10.86900  8.36400   1.000 24.21533  ? 195 PHE A CD2    1 
ATOM   1428 C CE1    . PHE A 1 204 ? 31.58000 10.56400  5.62600   1.000 24.87165  ? 195 PHE A CE1    1 
ATOM   1429 C CE2    . PHE A 1 204 ? 32.24800 11.85900  7.52300   1.000 26.55995  ? 195 PHE A CE2    1 
ATOM   1430 C CZ     . PHE A 1 204 ? 32.15400 11.70600  6.15000   1.000 21.67870  ? 195 PHE A CZ     1 
ATOM   1431 N N      . LEU A 1 205 ? 30.55400 5.80700   10.39600  1.000 22.64943  ? 196 LEU A N      1 
ATOM   1432 C CA     . LEU A 1 205 ? 30.12200 5.17900   11.64200  1.000 25.73923  ? 196 LEU A CA     1 
ATOM   1433 C C      . LEU A 1 205 ? 31.24200 4.36700   12.28700  1.000 29.24034  ? 196 LEU A C      1 
ATOM   1434 O O      . LEU A 1 205 ? 31.61000 4.60500   13.44300  1.000 32.21765  ? 196 LEU A O      1 
ATOM   1435 C CB     . LEU A 1 205 ? 28.90400 4.28700   11.38400  1.000 22.13692  ? 196 LEU A CB     1 
ATOM   1436 C CG     . LEU A 1 205 ? 27.58400 4.96100   11.00900  1.000 25.19026  ? 196 LEU A CG     1 
ATOM   1437 C CD1    . LEU A 1 205 ? 26.57500 3.91600   10.56100  1.000 19.58935  ? 196 LEU A CD1    1 
ATOM   1438 C CD2    . LEU A 1 205 ? 27.04000 5.76400   12.18100  1.000 20.33115  ? 196 LEU A CD2    1 
ATOM   1439 N N      . LYS A 1 206 ? 31.78200 3.39300   11.55400  1.000 23.35435  ? 197 LYS A N      1 
ATOM   1440 C CA     . LYS A 1 206 ? 32.76300 2.46900   12.11200  1.000 25.10541  ? 197 LYS A CA     1 
ATOM   1441 C C      . LYS A 1 206 ? 34.05500 3.19700   12.46400  1.000 27.84617  ? 197 LYS A C      1 
ATOM   1442 O O      . LYS A 1 206 ? 34.64900 3.87500   11.61900  1.000 26.40862  ? 197 LYS A O      1 
ATOM   1443 C CB     . LYS A 1 206 ? 33.05200 1.34300   11.11800  1.000 29.15259  ? 197 LYS A CB     1 
ATOM   1444 C CG     . LYS A 1 206 ? 31.82300 0.57800   10.64100  1.000 29.49291  ? 197 LYS A CG     1 
ATOM   1445 C CD     . LYS A 1 206 ? 31.20900 -0.24400  11.76000  1.000 28.44224  ? 197 LYS A CD     1 
ATOM   1446 C CE     . LYS A 1 206 ? 29.96500 -0.99200  11.29700  1.000 28.06825  ? 197 LYS A CE     1 
ATOM   1447 N NZ     . LYS A 1 206 ? 30.26300 -2.03500  10.27600  1.000 21.26406  ? 197 LYS A NZ     1 
ATOM   1448 N N      . ASP A 1 207 ? 34.50000 3.04400   13.71500  1.000 26.47997  ? 198 ASP A N      1 
ATOM   1449 C CA     . ASP A 1 207 ? 35.74000 3.68100   14.14700  1.000 31.08196  ? 198 ASP A CA     1 
ATOM   1450 C C      . ASP A 1 207 ? 36.97700 3.02300   13.55200  1.000 27.79211  ? 198 ASP A C      1 
ATOM   1451 O O      . ASP A 1 207 ? 38.06400 3.60800   13.62200  1.000 36.63049  ? 198 ASP A O      1 
ATOM   1452 C CB     . ASP A 1 207 ? 35.82600 3.69600   15.67900  1.000 30.87381  ? 198 ASP A CB     1 
ATOM   1453 C CG     . ASP A 1 207 ? 35.76800 2.30600   16.29100  1.000 32.40710  ? 198 ASP A CG     1 
ATOM   1454 O OD1    . ASP A 1 207 ? 35.68100 1.31600   15.53600  1.000 34.29861  ? 198 ASP A OD1    1 
ATOM   1455 O OD2    . ASP A 1 207 ? 35.80700 2.20300   17.53400  1.000 33.75955  ? 198 ASP A OD2    1 
ATOM   1456 N N      . GLY A 1 208 ? 36.84000 1.82900   12.97400  1.000 30.14495  ? 199 GLY A N      1 
ATOM   1457 C CA     . GLY A 1 208 ? 37.92100 1.22800   12.21400  1.000 31.87473  ? 199 GLY A CA     1 
ATOM   1458 C C      . GLY A 1 208 ? 38.21600 1.91700   10.89700  1.000 31.15521  ? 199 GLY A C      1 
ATOM   1459 O O      . GLY A 1 208 ? 39.27900 1.67600   10.31600  1.000 35.03779  ? 199 GLY A O      1 
ATOM   1460 N N      . ILE A 1 209 ? 37.30500 2.75900   10.41500  1.000 30.81837  ? 200 ILE A N      1 
ATOM   1461 C CA     . ILE A 1 209 ? 37.50000 3.52600   9.18900   1.000 29.01707  ? 200 ILE A CA     1 
ATOM   1462 C C      . ILE A 1 209 ? 37.62700 5.01600   9.48300   1.000 32.37764  ? 200 ILE A C      1 
ATOM   1463 O O      . ILE A 1 209 ? 38.55800 5.67500   9.01600   1.000 36.31710  ? 200 ILE A O      1 
ATOM   1464 C CB     . ILE A 1 209 ? 36.35900 3.26100   8.18000   1.000 28.15041  ? 200 ILE A CB     1 
ATOM   1465 C CG1    . ILE A 1 209 ? 36.28000 1.77600   7.83600   1.000 29.54188  ? 200 ILE A CG1    1 
ATOM   1466 C CG2    . ILE A 1 209 ? 36.54500 4.10300   6.92100   1.000 28.75053  ? 200 ILE A CG2    1 
ATOM   1467 C CD1    . ILE A 1 209 ? 35.11600 1.42600   6.93000   1.000 29.96856  ? 200 ILE A CD1    1 
ATOM   1468 N N      . ASN A 1 210 ? 36.69700 5.55800   10.26200  1.000 31.78439  ? 201 ASN A N      1 
ATOM   1469 C CA     . ASN A 1 210 ? 36.65700 6.98000   10.59000  1.000 30.16111  ? 201 ASN A CA     1 
ATOM   1470 C C      . ASN A 1 210 ? 37.83600 7.32000   11.49300  1.000 39.01001  ? 201 ASN A C      1 
ATOM   1471 O O      . ASN A 1 210 ? 37.81800 7.04000   12.69400  1.000 33.66808  ? 201 ASN A O      1 
ATOM   1472 C CB     . ASN A 1 210 ? 35.33200 7.32100   11.26100  1.000 28.43627  ? 201 ASN A CB     1 
ATOM   1473 C CG     . ASN A 1 210 ? 35.10900 8.81400   11.40100  1.000 32.45130  ? 201 ASN A CG     1 
ATOM   1474 O OD1    . ASN A 1 210 ? 36.05600 9.59900   11.45800  1.000 30.90007  ? 201 ASN A OD1    1 
ATOM   1475 N ND2    . ASN A 1 210 ? 33.84400 9.21400   11.46600  1.000 28.05767  ? 201 ASN A ND2    1 
ATOM   1476 N N      . ASP A 1 211 ? 38.86900 7.93300   10.91500  1.000 33.29235  ? 202 ASP A N      1 
ATOM   1477 C CA     . ASP A 1 211 ? 40.01200 8.43400   11.66700  1.000 34.46195  ? 202 ASP A CA     1 
ATOM   1478 C C      . ASP A 1 211 ? 40.04500 9.95800   11.70400  1.000 36.24740  ? 202 ASP A C      1 
ATOM   1479 O O      . ASP A 1 211 ? 41.11100 10.54900  11.90300  1.000 34.63445  ? 202 ASP A O      1 
ATOM   1480 C CB     . ASP A 1 211 ? 41.31400 7.88300   11.08200  1.000 32.19998  ? 202 ASP A CB     1 
ATOM   1481 C CG     . ASP A 1 211 ? 41.55900 8.35000   9.65800   1.000 41.04921  ? 202 ASP A CG     1 
ATOM   1482 O OD1    . ASP A 1 211 ? 40.58900 8.76400   8.99000   1.000 37.38463  ? 202 ASP A OD1    1 
ATOM   1483 O OD2    . ASP A 1 211 ? 42.72200 8.30100   9.20600   1.000 42.12496  ? 202 ASP A OD2    1 
ATOM   1484 N N      . ARG A 1 212 ? 38.89700 10.60400  11.51700  1.000 34.18924  ? 203 ARG A N      1 
ATOM   1485 C CA     . ARG A 1 212 ? 38.84200 12.05600  11.47700  1.000 35.17767  ? 203 ARG A CA     1 
ATOM   1486 C C      . ARG A 1 212 ? 39.05700 12.65000  12.86700  1.000 34.88090  ? 203 ARG A C      1 
ATOM   1487 O O      . ARG A 1 212 ? 38.82600 12.00700  13.89500  1.000 34.76624  ? 203 ARG A O      1 
ATOM   1488 C CB     . ARG A 1 212 ? 37.50000 12.52800  10.91900  1.000 30.56306  ? 203 ARG A CB     1 
ATOM   1489 C CG     . ARG A 1 212 ? 37.16100 11.97100  9.55000   1.000 27.68920  ? 203 ARG A CG     1 
ATOM   1490 C CD     . ARG A 1 212 ? 35.76100 12.37600  9.12700   1.000 24.54192  ? 203 ARG A CD     1 
ATOM   1491 N NE     . ARG A 1 212 ? 35.66100 13.80500  8.85900   1.000 24.79465  ? 203 ARG A NE     1 
ATOM   1492 C CZ     . ARG A 1 212 ? 35.71000 14.34300  7.64800   1.000 27.11126  ? 203 ARG A CZ     1 
ATOM   1493 N NH1    . ARG A 1 212 ? 35.84200 13.59500  6.56400   1.000 27.40722  ? 203 ARG A NH1    1 
ATOM   1494 N NH2    . ARG A 1 212 ? 35.62000 15.66400  7.52100   1.000 25.37981  ? 203 ARG A NH2    1 
ATOM   1495 N N      . THR A 1 213 ? 39.50600 13.90500  12.88400  1.000 36.42431  ? 204 THR A N      1 
ATOM   1496 C CA     . THR A 1 213 ? 39.68000 14.65800  14.11700  1.000 42.05189  ? 204 THR A CA     1 
ATOM   1497 C C      . THR A 1 213 ? 38.76600 15.87200  14.20400  1.000 37.70802  ? 204 THR A C      1 
ATOM   1498 O O      . THR A 1 213 ? 38.87200 16.64000  15.16800  1.000 40.32317  ? 204 THR A O      1 
ATOM   1499 C CB     . THR A 1 213 ? 41.14000 15.10700  14.27200  1.000 39.97966  ? 204 THR A CB     1 
ATOM   1500 O OG1    . THR A 1 213 ? 41.52500 15.89400  13.13700  1.000 40.11003  ? 204 THR A OG1    1 
ATOM   1501 C CG2    . THR A 1 213 ? 42.06000 13.90000  14.38300  1.000 35.29936  ? 204 THR A CG2    1 
ATOM   1502 N N      . ASP A 1 214 ? 37.87700 16.07000  13.23600  1.000 34.41513  ? 205 ASP A N      1 
ATOM   1503 C CA     . ASP A 1 214 ? 36.94000 17.18400  13.26300  1.000 36.75975  ? 205 ASP A CA     1 
ATOM   1504 C C      . ASP A 1 214 ? 35.67400 16.75000  14.00600  1.000 29.03232  ? 205 ASP A C      1 
ATOM   1505 O O      . ASP A 1 214 ? 35.67900 15.75600  14.73700  1.000 32.78472  ? 205 ASP A O      1 
ATOM   1506 C CB     . ASP A 1 214 ? 36.66300 17.66900  11.83500  1.000 32.80923  ? 205 ASP A CB     1 
ATOM   1507 C CG     . ASP A 1 214 ? 35.94300 16.63200  10.99100  1.000 34.61738  ? 205 ASP A CG     1 
ATOM   1508 O OD1    . ASP A 1 214 ? 35.97200 15.43600  11.35100  1.000 34.25839  ? 205 ASP A OD1    1 
ATOM   1509 O OD2    . ASP A 1 214 ? 35.35300 17.01500  9.95800   1.000 32.05606  ? 205 ASP A OD2    1 
ATOM   1510 N N      . GLU A 1 215 ? 34.57300 17.48000  13.82100  1.000 33.58879  ? 206 GLU A N      1 
ATOM   1511 C CA     . GLU A 1 215 ? 33.33700 17.17200  14.53000  1.000 32.77917  ? 206 GLU A CA     1 
ATOM   1512 C C      . GLU A 1 215 ? 32.62000 15.94300  13.98100  1.000 34.11559  ? 206 GLU A C      1 
ATOM   1513 O O      . GLU A 1 215 ? 31.54300 15.60800  14.48700  1.000 33.99171  ? 206 GLU A O      1 
ATOM   1514 C CB     . GLU A 1 215 ? 32.39200 18.37600  14.49100  1.000 34.70781  ? 206 GLU A CB     1 
ATOM   1515 C CG     . GLU A 1 215 ? 31.79824 18.65977  13.11937  1.000 39.71374  ? 206 GLU A CG     1 
ATOM   1516 C CD     . GLU A 1 215 ? 32.45400 19.83658  12.42160  1.000 45.92798  ? 206 GLU A CD     1 
ATOM   1517 O OE1    . GLU A 1 215 ? 33.67291 19.77034  12.15145  1.000 43.67155  ? 206 GLU A OE1    1 
ATOM   1518 O OE2    . GLU A 1 215 ? 31.74949 20.83075  12.14944  1.000 47.37495  ? 206 GLU A OE2    1 
ATOM   1519 N N      . TYR A 1 216 ? 33.17300 15.27100  12.97100  1.000 27.79490  ? 207 TYR A N      1 
ATOM   1520 C CA     . TYR A 1 216 ? 32.57600 14.06600  12.41200  1.000 26.70010  ? 207 TYR A CA     1 
ATOM   1521 C C      . TYR A 1 216 ? 33.32600 12.79600  12.78900  1.000 29.89644  ? 207 TYR A C      1 
ATOM   1522 O O      . TYR A 1 216 ? 32.94200 11.71100  12.34000  1.000 29.64193  ? 207 TYR A O      1 
ATOM   1523 C CB     . TYR A 1 216 ? 32.48300 14.17900  10.88400  1.000 27.08470  ? 207 TYR A CB     1 
ATOM   1524 C CG     . TYR A 1 216 ? 31.36600 15.08300  10.41100  1.000 26.70957  ? 207 TYR A CG     1 
ATOM   1525 C CD1    . TYR A 1 216 ? 31.55900 16.45200  10.28400  1.000 25.31878  ? 207 TYR A CD1    1 
ATOM   1526 C CD2    . TYR A 1 216 ? 30.11500 14.56600  10.09800  1.000 25.27821  ? 207 TYR A CD2    1 
ATOM   1527 C CE1    . TYR A 1 216 ? 30.53600 17.28200  9.85700   1.000 24.30248  ? 207 TYR A CE1    1 
ATOM   1528 C CE2    . TYR A 1 216 ? 29.08700 15.38700  9.67100   1.000 23.65608  ? 207 TYR A CE2    1 
ATOM   1529 C CZ     . TYR A 1 216 ? 29.30300 16.74400  9.55200   1.000 29.03873  ? 207 TYR A CZ     1 
ATOM   1530 O OH     . TYR A 1 216 ? 28.28300 17.56400  9.12700   1.000 28.86632  ? 207 TYR A OH     1 
ATOM   1531 N N      . GLY A 1 217 ? 34.37800 12.89700  13.60300  1.000 28.04541  ? 208 GLY A N      1 
ATOM   1532 C CA     . GLY A 1 217 ? 35.14200 11.73700  13.99700  1.000 30.12072  ? 208 GLY A CA     1 
ATOM   1533 C C      . GLY A 1 217 ? 35.41400 11.73400  15.48900  1.000 33.35762  ? 208 GLY A C      1 
ATOM   1534 O O      . GLY A 1 217 ? 35.29400 12.75100  16.17200  1.000 33.03857  ? 208 GLY A O      1 
ATOM   1535 N N      . GLY A 1 218 ? 35.78500 10.55600  15.98500  1.000 33.76746  ? 209 GLY A N      1 
ATOM   1536 C CA     . GLY A 1 218 ? 36.10900 10.39500  17.38800  1.000 29.48519  ? 209 GLY A CA     1 
ATOM   1537 C C      . GLY A 1 218 ? 35.02100 9.70900   18.18900  1.000 32.30211  ? 209 GLY A C      1 
ATOM   1538 O O      . GLY A 1 218 ? 34.88300 8.48300   18.14200  1.000 34.87181  ? 209 GLY A O      1 
ATOM   1539 N N      . SER A 1 219 ? 34.23900 10.49500  18.92400  1.000 24.83598  ? 210 SER A N      1 
ATOM   1540 C CA     . SER A 1 219 ? 33.21400 9.94600   19.79800  1.000 31.93847  ? 210 SER A CA     1 
ATOM   1541 C C      . SER A 1 219 ? 32.06600 9.35300   18.98200  1.000 31.16124  ? 210 SER A C      1 
ATOM   1542 O O      . SER A 1 219 ? 31.96400 9.53800   17.76500  1.000 26.05045  ? 210 SER A O      1 
ATOM   1543 C CB     . SER A 1 219 ? 32.68300 11.02600  20.73800  1.000 28.62387  ? 210 SER A CB     1 
ATOM   1544 O OG     . SER A 1 219 ? 32.05100 12.06100  20.00300  1.000 33.31146  ? 210 SER A OG     1 
ATOM   1545 N N      . LEU A 1 220 ? 31.18900 8.62800   19.68300  1.000 29.07838  ? 211 LEU A N      1 
ATOM   1546 C CA     . LEU A 1 220 ? 30.00900 8.06000   19.03700  1.000 30.67491  ? 211 LEU A CA     1 
ATOM   1547 C C      . LEU A 1 220 ? 29.11400 9.15000   18.46300  1.000 30.18147  ? 211 LEU A C      1 
ATOM   1548 O O      . LEU A 1 220 ? 28.54400 8.98600   17.37800  1.000 31.17129  ? 211 LEU A O      1 
ATOM   1549 C CB     . LEU A 1 220 ? 29.22800 7.20100   20.03100  1.000 29.15688  ? 211 LEU A CB     1 
ATOM   1550 C CG     . LEU A 1 220 ? 29.81600 5.84400   20.41200  1.000 32.68876  ? 211 LEU A CG     1 
ATOM   1551 C CD1    . LEU A 1 220 ? 29.08800 5.28600   21.62200  1.000 26.17449  ? 211 LEU A CD1    1 
ATOM   1552 C CD2    . LEU A 1 220 ? 29.72900 4.87900   19.24200  1.000 24.26230  ? 211 LEU A CD2    1 
ATOM   1553 N N      . ALA A 1 221 ? 28.97500 10.26800  19.18000  1.000 28.29114  ? 212 ALA A N      1 
ATOM   1554 C CA     . ALA A 1 221 ? 28.13900 11.36100  18.69200  1.000 28.63646  ? 212 ALA A CA     1 
ATOM   1555 C C      . ALA A 1 221 ? 28.69500 11.94800  17.40200  1.000 27.03430  ? 212 ALA A C      1 
ATOM   1556 O O      . ALA A 1 221 ? 27.94300 12.21500  16.45700  1.000 24.97911  ? 212 ALA A O      1 
ATOM   1557 C CB     . ALA A 1 221 ? 28.01100 12.44500  19.76200  1.000 28.48113  ? 212 ALA A CB     1 
ATOM   1558 N N      . ASN A 1 222 ? 30.01100 12.15700  17.34400  1.000 27.64620  ? 213 ASN A N      1 
ATOM   1559 C CA     . ASN A 1 222 ? 30.61800 12.70200  16.13500  1.000 26.25383  ? 213 ASN A CA     1 
ATOM   1560 C C      . ASN A 1 222 ? 30.54700 11.70800  14.98200  1.000 25.32451  ? 213 ASN A C      1 
ATOM   1561 O O      . ASN A 1 222 ? 30.35200 12.10100  13.82700  1.000 25.70330  ? 213 ASN A O      1 
ATOM   1562 C CB     . ASN A 1 222 ? 32.06400 13.10800  16.41600  1.000 29.68363  ? 213 ASN A CB     1 
ATOM   1563 C CG     . ASN A 1 222 ? 32.16100 14.35400  17.27400  1.000 26.90944  ? 213 ASN A CG     1 
ATOM   1564 O OD1    . ASN A 1 222 ? 31.14700 14.91100  17.69200  1.000 32.84350  ? 213 ASN A OD1    1 
ATOM   1565 N ND2    . ASN A 1 222 ? 33.38300 14.79700  17.54300  1.000 23.43762  ? 213 ASN A ND2    1 
ATOM   1566 N N      . ARG A 1 223 ? 30.69500 10.41500  15.27600  1.000 26.02061  ? 214 ARG A N      1 
ATOM   1567 C CA     . ARG A 1 223 ? 30.65000 9.39800   14.23300  1.000 26.73003  ? 214 ARG A CA     1 
ATOM   1568 C C      . ARG A 1 223 ? 29.23100 9.08600   13.77600  1.000 29.13745  ? 214 ARG A C      1 
ATOM   1569 O O      . ARG A 1 223 ? 29.05600 8.50400   12.69900  1.000 27.87023  ? 214 ARG A O      1 
ATOM   1570 C CB     . ARG A 1 223 ? 31.34800 8.12600   14.72000  1.000 27.40896  ? 214 ARG A CB     1 
ATOM   1571 C CG     . ARG A 1 223 ? 32.86000 8.17500   14.54600  1.000 31.14201  ? 214 ARG A CG     1 
ATOM   1572 C CD     . ARG A 1 223 ? 33.59600 7.16500   15.41700  1.000 35.40849  ? 214 ARG A CD     1 
ATOM   1573 N NE     . ARG A 1 223 ? 32.98400 5.84200   15.40400  1.000 36.73412  ? 214 ARG A NE     1 
ATOM   1574 C CZ     . ARG A 1 223 ? 32.53500 5.21800   16.48400  1.000 28.43199  ? 214 ARG A CZ     1 
ATOM   1575 N NH1    . ARG A 1 223 ? 32.63100 5.76100   17.68500  1.000 29.66852  ? 214 ARG A NH1    1 
ATOM   1576 N NH2    . ARG A 1 223 ? 31.98600 4.01300   16.35700  1.000 31.26074  ? 214 ARG A NH2    1 
ATOM   1577 N N      . CYS A 1 224 ? 28.22200 9.46100   14.55800  1.000 23.68763  ? 215 CYS A N      1 
ATOM   1578 C CA     . CYS A 1 224 ? 26.82700 9.31000   14.16600  1.000 25.60788  ? 215 CYS A CA     1 
ATOM   1579 C C      . CYS A 1 224 ? 26.26600 10.55600  13.49600  1.000 27.19434  ? 215 CYS A C      1 
ATOM   1580 O O      . CYS A 1 224 ? 25.12500 10.52600  13.02300  1.000 26.91733  ? 215 CYS A O      1 
ATOM   1581 C CB     . CYS A 1 224 ? 25.96400 8.96400   15.38900  1.000 26.43809  ? 215 CYS A CB     1 
ATOM   1582 S SG     . CYS A 1 224 ? 26.09500 7.25800   15.97400  1.000 31.03310  ? 215 CYS A SG     1 
ATOM   1583 N N      . LYS A 1 225 ? 27.03700 11.64500  13.44100  1.000 23.59220  ? 216 LYS A N      1 
ATOM   1584 C CA     . LYS A 1 225 ? 26.50300 12.90800  12.94100  1.000 28.87209  ? 216 LYS A CA     1 
ATOM   1585 C C      . LYS A 1 225 ? 26.12600 12.81800  11.46500  1.000 27.41742  ? 216 LYS A C      1 
ATOM   1586 O O      . LYS A 1 225 ? 25.12100 13.40000  11.04100  1.000 25.23393  ? 216 LYS A O      1 
ATOM   1587 C CB     . LYS A 1 225 ? 27.51500 14.03100  13.17000  1.000 28.78865  ? 216 LYS A CB     1 
ATOM   1588 N N      . PHE A 1 226 ? 26.91200 12.09000  10.66700  1.000 25.19223  ? 217 PHE A N      1 
ATOM   1589 C CA     . PHE A 1 226 ? 26.65100 12.03600  9.23100   1.000 21.81355  ? 217 PHE A CA     1 
ATOM   1590 C C      . PHE A 1 226 ? 25.32700 11.34100  8.93200   1.000 22.39759  ? 217 PHE A C      1 
ATOM   1591 O O      . PHE A 1 226 ? 24.49200 11.87300  8.19100   1.000 22.68074  ? 217 PHE A O      1 
ATOM   1592 C CB     . PHE A 1 226 ? 27.80200 11.33900  8.50500   1.000 22.31176  ? 217 PHE A CB     1 
ATOM   1593 C CG     . PHE A 1 226 ? 27.63700 11.29700  7.01000   1.000 24.64980  ? 217 PHE A CG     1 
ATOM   1594 C CD1    . PHE A 1 226 ? 27.67000 12.46500  6.26300   1.000 22.93061  ? 217 PHE A CD1    1 
ATOM   1595 C CD2    . PHE A 1 226 ? 27.45200 10.09300  6.35100   1.000 21.61820  ? 217 PHE A CD2    1 
ATOM   1596 C CE1    . PHE A 1 226 ? 27.51700 12.43300  4.88800   1.000 30.50367  ? 217 PHE A CE1    1 
ATOM   1597 C CE2    . PHE A 1 226 ? 27.30200 10.05400  4.97500   1.000 30.94457  ? 217 PHE A CE2    1 
ATOM   1598 C CZ     . PHE A 1 226 ? 27.33300 11.22600  4.24300   1.000 29.74677  ? 217 PHE A CZ     1 
ATOM   1599 N N      . ILE A 1 227 ? 25.11400 10.14900  9.49800   1.000 20.89585  ? 218 ILE A N      1 
ATOM   1600 C CA     . ILE A 1 227 ? 23.86500 9.43800   9.24000   1.000 21.21366  ? 218 ILE A CA     1 
ATOM   1601 C C      . ILE A 1 227 ? 22.68300 10.19500  9.83300   1.000 24.31614  ? 218 ILE A C      1 
ATOM   1602 O O      . ILE A 1 227 ? 21.57200 10.14700  9.29000   1.000 26.37659  ? 218 ILE A O      1 
ATOM   1603 C CB     . ILE A 1 227 ? 23.94000 7.99000   9.76600   1.000 25.76499  ? 218 ILE A CB     1 
ATOM   1604 C CG1    . ILE A 1 227 ? 22.72200 7.18600   9.29700   1.000 20.41222  ? 218 ILE A CG1    1 
ATOM   1605 C CG2    . ILE A 1 227 ? 24.05600 7.96200   11.28700  1.000 20.40640  ? 218 ILE A CG2    1 
ATOM   1606 C CD1    . ILE A 1 227 ? 22.76800 5.72000   9.67700   1.000 21.16148  ? 218 ILE A CD1    1 
ATOM   1607 N N      . THR A 1 228 ? 22.89600 10.91600  10.93800  1.000 21.38001  ? 219 THR A N      1 
ATOM   1608 C CA     . THR A 1 228 ? 21.82900 11.72800  11.51100  1.000 21.19836  ? 219 THR A CA     1 
ATOM   1609 C C      . THR A 1 228 ? 21.40100 12.82500  10.54400  1.000 23.34453  ? 219 THR A C      1 
ATOM   1610 O O      . THR A 1 228 ? 20.20400 13.04400  10.32200  1.000 24.44936  ? 219 THR A O      1 
ATOM   1611 C CB     . THR A 1 228 ? 22.28400 12.33200  12.84300  1.000 25.18558  ? 219 THR A CB     1 
ATOM   1612 O OG1    . THR A 1 228 ? 22.56600 11.28400  13.77800  1.000 28.52883  ? 219 THR A OG1    1 
ATOM   1613 C CG2    . THR A 1 228 ? 21.20500 13.23800  13.41700  1.000 21.56525  ? 219 THR A CG2    1 
ATOM   1614 N N      . GLN A 1 229 ? 22.37300 13.51800  9.94600   1.000 22.86468  ? 220 GLN A N      1 
ATOM   1615 C CA     . GLN A 1 229 ? 22.04900 14.60700  9.03000   1.000 25.45740  ? 220 GLN A CA     1 
ATOM   1616 C C      . GLN A 1 229 ? 21.45800 14.09300  7.72300   1.000 25.45743  ? 220 GLN A C      1 
ATOM   1617 O O      . GLN A 1 229 ? 20.60400 14.76200  7.12800   1.000 27.01380  ? 220 GLN A O      1 
ATOM   1618 C CB     . GLN A 1 229 ? 23.29600 15.45000  8.76400   1.000 22.43600  ? 220 GLN A CB     1 
ATOM   1619 C CG     . GLN A 1 229 ? 23.81600 16.16800  10.00100  1.000 28.01185  ? 220 GLN A CG     1 
ATOM   1620 C CD     . GLN A 1 229 ? 25.20700 16.73700  9.80800   1.000 32.23527  ? 220 GLN A CD     1 
ATOM   1621 O OE1    . GLN A 1 229 ? 25.82100 16.56600  8.75400   1.000 32.44075  ? 220 GLN A OE1    1 
ATOM   1622 N NE2    . GLN A 1 229 ? 25.71500 17.41600  10.83000  1.000 30.97656  ? 220 GLN A NE2    1 
ATOM   1623 N N      . VAL A 1 230 ? 21.89100 12.91700  7.26000   1.000 25.18356  ? 221 VAL A N      1 
ATOM   1624 C CA     . VAL A 1 230 ? 21.30200 12.33100  6.05700   1.000 25.05230  ? 221 VAL A CA     1 
ATOM   1625 C C      . VAL A 1 230 ? 19.83500 11.99600  6.29700   1.000 24.85016  ? 221 VAL A C      1 
ATOM   1626 O O      . VAL A 1 230 ? 18.96500 12.30900  5.47600   1.000 23.00676  ? 221 VAL A O      1 
ATOM   1627 C CB     . VAL A 1 230 ? 22.10000 11.09100  5.61500   1.000 26.38916  ? 221 VAL A CB     1 
ATOM   1628 C CG1    . VAL A 1 230 ? 21.35300 10.34000  4.52400   1.000 26.07963  ? 221 VAL A CG1    1 
ATOM   1629 C CG2    . VAL A 1 230 ? 23.48400 11.49400  5.12900   1.000 22.88225  ? 221 VAL A CG2    1 
ATOM   1630 N N      . VAL A 1 231 ? 19.54000 11.35900  7.43300   1.000 24.91818  ? 222 VAL A N      1 
ATOM   1631 C CA     . VAL A 1 231 ? 18.16000 11.00100  7.75000   1.000 25.68830  ? 222 VAL A CA     1 
ATOM   1632 C C      . VAL A 1 231 ? 17.31300 12.25000  7.95800   1.000 24.53326  ? 222 VAL A C      1 
ATOM   1633 O O      . VAL A 1 231 ? 16.18100 12.33500  7.46900   1.000 25.33465  ? 222 VAL A O      1 
ATOM   1634 C CB     . VAL A 1 231 ? 18.11900 10.07400  8.98000   1.000 23.71157  ? 222 VAL A CB     1 
ATOM   1635 C CG1    . VAL A 1 231 ? 16.68700 9.86500   9.44200   1.000 20.66947  ? 222 VAL A CG1    1 
ATOM   1636 C CG2    . VAL A 1 231 ? 18.77300 8.73700   8.66000   1.000 25.86803  ? 222 VAL A CG2    1 
ATOM   1637 N N      . GLN A 1 232 ? 17.84400 13.24100  8.68000   1.000 25.41103  ? 223 GLN A N      1 
ATOM   1638 C CA     . GLN A 1 232 ? 17.08500 14.46500  8.92600   1.000 28.35850  ? 223 GLN A CA     1 
ATOM   1639 C C      . GLN A 1 232 ? 16.74200 15.17800  7.62400   1.000 25.19442  ? 223 GLN A C      1 
ATOM   1640 O O      . GLN A 1 232 ? 15.65500 15.75100  7.49000   1.000 32.86704  ? 223 GLN A O      1 
ATOM   1641 C CB     . GLN A 1 232 ? 17.86700 15.39400  9.85600   1.000 28.19526  ? 223 GLN A CB     1 
ATOM   1642 C CG     . GLN A 1 232 ? 17.69541 15.08563  11.33432  1.000 36.56246  ? 223 GLN A CG     1 
ATOM   1643 C CD     . GLN A 1 232 ? 18.64986 15.87472  12.21167  1.000 44.61554  ? 223 GLN A CD     1 
ATOM   1644 O OE1    . GLN A 1 232 ? 19.77846 16.16550  11.81577  1.000 36.79704  ? 223 GLN A OE1    1 
ATOM   1645 N NE2    . GLN A 1 232 ? 18.19945 16.22410  13.41284  1.000 35.06784  ? 223 GLN A NE2    1 
ATOM   1646 N N      . ALA A 1 233 ? 17.65400 15.14900  6.65100   1.000 26.24120  ? 224 ALA A N      1 
ATOM   1647 C CA     . ALA A 1 233 ? 17.39900 15.81800  5.37900   1.000 27.22632  ? 224 ALA A CA     1 
ATOM   1648 C C      . ALA A 1 233 ? 16.24600 15.16000  4.63000   1.000 29.12188  ? 224 ALA A C      1 
ATOM   1649 O O      . ALA A 1 233 ? 15.34700 15.84500  4.13000   1.000 28.80337  ? 224 ALA A O      1 
ATOM   1650 C CB     . ALA A 1 233 ? 18.66600 15.82100  4.52400   1.000 21.13448  ? 224 ALA A CB     1 
ATOM   1651 N N      . VAL A 1 234 ? 16.25200 13.82800  4.54500   1.000 25.69756  ? 225 VAL A N      1 
ATOM   1652 C CA     . VAL A 1 234 ? 15.20200 13.14900  3.79300   1.000 28.43046  ? 225 VAL A CA     1 
ATOM   1653 C C      . VAL A 1 234 ? 13.89300 13.12400  4.57700   1.000 28.36778  ? 225 VAL A C      1 
ATOM   1654 O O      . VAL A 1 234 ? 12.81200 13.07800  3.98000   1.000 30.11140  ? 225 VAL A O      1 
ATOM   1655 C CB     . VAL A 1 234 ? 15.65100 11.73200  3.39000   1.000 25.70462  ? 225 VAL A CB     1 
ATOM   1656 C CG1    . VAL A 1 234 ? 16.87700 11.80200  2.48800   1.000 24.65300  ? 225 VAL A CG1    1 
ATOM   1657 C CG2    . VAL A 1 234 ? 15.93900 10.88200  4.61600   1.000 29.88017  ? 225 VAL A CG2    1 
ATOM   1658 N N      . VAL A 1 235 ? 13.95700 13.15900  5.91000   1.000 28.22650  ? 226 VAL A N      1 
ATOM   1659 C CA     . VAL A 1 235 ? 12.73600 13.26800  6.70600   1.000 32.74013  ? 226 VAL A CA     1 
ATOM   1660 C C      . VAL A 1 235 ? 12.05200 14.60200  6.44000   1.000 27.92572  ? 226 VAL A C      1 
ATOM   1661 O O      . VAL A 1 235 ? 10.83600 14.66700  6.21900   1.000 25.56628  ? 226 VAL A O      1 
ATOM   1662 C CB     . VAL A 1 235 ? 13.04700 13.08100  8.20200   1.000 29.21230  ? 226 VAL A CB     1 
ATOM   1663 C CG1    . VAL A 1 235 ? 11.91900 13.63900  9.05400   1.000 25.28031  ? 226 VAL A CG1    1 
ATOM   1664 C CG2    . VAL A 1 235 ? 13.26700 11.61000  8.51600   1.000 26.25863  ? 226 VAL A CG2    1 
ATOM   1665 N N      . SER A 1 236 ? 12.82800 15.68900  6.44500   1.000 22.86803  ? 227 SER A N      1 
ATOM   1666 C CA     . SER A 1 236 ? 12.26200 17.01000  6.20200   1.000 32.10426  ? 227 SER A CA     1 
ATOM   1667 C C      . SER A 1 236 ? 11.74300 17.16900  4.78100   1.000 28.75798  ? 227 SER A C      1 
ATOM   1668 O O      . SER A 1 236 ? 10.86700 18.00800  4.54700   1.000 31.00628  ? 227 SER A O      1 
ATOM   1669 C CB     . SER A 1 236 ? 13.30400 18.09100  6.49300   1.000 29.56441  ? 227 SER A CB     1 
ATOM   1670 O OG     . SER A 1 236 ? 13.72200 18.03700  7.84500   1.000 40.03693  ? 227 SER A OG     1 
ATOM   1671 N N      . ALA A 1 237 ? 12.25100 16.38300  3.83400   1.000 32.04583  ? 228 ALA A N      1 
ATOM   1672 C CA     . ALA A 1 237 ? 11.88000 16.54700  2.43400   1.000 29.36466  ? 228 ALA A CA     1 
ATOM   1673 C C      . ALA A 1 237 ? 10.63400 15.75500  2.05000   1.000 30.81371  ? 228 ALA A C      1 
ATOM   1674 O O      . ALA A 1 237 ? 9.78200  16.26700  1.31700   1.000 27.96098  ? 228 ALA A O      1 
ATOM   1675 C CB     . ALA A 1 237 ? 13.04900 16.14200  1.53300   1.000 31.58224  ? 228 ALA A CB     1 
ATOM   1676 N N      . ILE A 1 238 ? 10.51100 14.51400  2.51900   1.000 28.11333  ? 229 ILE A N      1 
ATOM   1677 C CA     . ILE A 1 238 ? 9.42700  13.63300  2.09800   1.000 26.44674  ? 229 ILE A CA     1 
ATOM   1678 C C      . ILE A 1 238 ? 8.60500  13.09500  3.25900   1.000 27.36314  ? 229 ILE A C      1 
ATOM   1679 O O      . ILE A 1 238 ? 7.58800  12.42700  3.01700   1.000 29.54953  ? 229 ILE A O      1 
ATOM   1680 C CB     . ILE A 1 238 ? 9.95600  12.46200  1.24100   1.000 23.52717  ? 229 ILE A CB     1 
ATOM   1681 C CG1    . ILE A 1 238 ? 10.73800 11.47300  2.10700   1.000 27.63809  ? 229 ILE A CG1    1 
ATOM   1682 C CG2    . ILE A 1 238 ? 10.83500 12.98200  0.11200   1.000 26.36296  ? 229 ILE A CG2    1 
ATOM   1683 C CD1    . ILE A 1 238 ? 11.28200 10.29700  1.33400   1.000 26.59757  ? 229 ILE A CD1    1 
ATOM   1684 N N      . GLY A 1 239 ? 8.99300  13.35600  4.50200   1.000 24.54093  ? 230 GLY A N      1 
ATOM   1685 C CA     . GLY A 1 239 ? 8.24300  12.84000  5.63100   1.000 28.62164  ? 230 GLY A CA     1 
ATOM   1686 C C      . GLY A 1 239 ? 8.87000  11.60600  6.24400   1.000 28.32207  ? 230 GLY A C      1 
ATOM   1687 O O      . GLY A 1 239 ? 9.38800  10.74300  5.52800   1.000 26.38504  ? 230 GLY A O      1 
ATOM   1688 N N      . ALA A 1 240 ? 8.81600  11.50600  7.57500   1.000 29.01613  ? 231 ALA A N      1 
ATOM   1689 C CA     . ALA A 1 240 ? 9.49700  10.41600  8.26600   1.000 25.68429  ? 231 ALA A CA     1 
ATOM   1690 C C      . ALA A 1 240 ? 8.89000  9.06000   7.92500   1.000 24.59648  ? 231 ALA A C      1 
ATOM   1691 O O      . ALA A 1 240 ? 9.61600  8.06500   7.81000   1.000 22.46518  ? 231 ALA A O      1 
ATOM   1692 C CB     . ALA A 1 240 ? 9.46600  10.64700  9.77700   1.000 27.99589  ? 231 ALA A CB     1 
ATOM   1693 N N      . ASP A 1 241 ? 7.56800  8.99500   7.75200   1.000 22.72347  ? 232 ASP A N      1 
ATOM   1694 C CA     . ASP A 1 241 ? 6.90700  7.71200   7.53300   1.000 22.75614  ? 232 ASP A CA     1 
ATOM   1695 C C      . ASP A 1 241 ? 7.21900  7.10100   6.17400   1.000 29.01917  ? 232 ASP A C      1 
ATOM   1696 O O      . ASP A 1 241 ? 6.75400  5.99000   5.89500   1.000 29.36475  ? 232 ASP A O      1 
ATOM   1697 C CB     . ASP A 1 241 ? 5.39400  7.86200   7.69600   1.000 27.78037  ? 232 ASP A CB     1 
ATOM   1698 C CG     . ASP A 1 241 ? 4.83351  9.01858   6.89649   1.000 38.32178  ? 232 ASP A CG     1 
ATOM   1699 O OD1    . ASP A 1 241 ? 4.50283  10.05905  7.50094   1.000 55.74423  ? 232 ASP A OD1    1 
ATOM   1700 O OD2    . ASP A 1 241 ? 4.72701  8.88545   5.66118   1.000 44.92616  ? 232 ASP A OD2    1 
ATOM   1701 N N      . ARG A 1 242 ? 7.98200  7.79100   5.33000   1.000 26.88811  ? 233 ARG A N      1 
ATOM   1702 C CA     . ARG A 1 242 ? 8.38900  7.27900   4.02900   1.000 26.18483  ? 233 ARG A CA     1 
ATOM   1703 C C      . ARG A 1 242 ? 9.90700  7.15100   3.94800   1.000 28.03127  ? 233 ARG A C      1 
ATOM   1704 O O      . ARG A 1 242 ? 10.48500 7.16400   2.85900   1.000 25.43642  ? 233 ARG A O      1 
ATOM   1705 C CB     . ARG A 1 242 ? 7.85500  8.17400   2.91000   1.000 27.31901  ? 233 ARG A CB     1 
ATOM   1706 C CG     . ARG A 1 242 ? 6.34712  8.37402   2.96116   1.000 27.78258  ? 233 ARG A CG     1 
ATOM   1707 C CD     . ARG A 1 242 ? 5.76643  8.80922   1.62165   1.000 31.66955  ? 233 ARG A CD     1 
ATOM   1708 N NE     . ARG A 1 242 ? 6.30225  10.08667  1.16681   1.000 36.41785  ? 233 ARG A NE     1 
ATOM   1709 C CZ     . ARG A 1 242 ? 5.63477  10.95908  0.42284   1.000 50.01531  ? 233 ARG A CZ     1 
ATOM   1710 N NH1    . ARG A 1 242 ? 4.38959  10.73063  0.03515   1.000 51.91953  ? 233 ARG A NH1    1 
ATOM   1711 N NH2    . ARG A 1 242 ? 6.23034  12.09275  0.06237   1.000 38.86487  ? 233 ARG A NH2    1 
ATOM   1712 N N      . VAL A 1 243 ? 10.56400 7.02500   5.09900   1.000 21.57482  ? 234 VAL A N      1 
ATOM   1713 C CA     . VAL A 1 243 ? 12.01800 6.93400   5.17300   1.000 22.95747  ? 234 VAL A CA     1 
ATOM   1714 C C      . VAL A 1 243 ? 12.38800 5.71400   6.00500   1.000 26.33788  ? 234 VAL A C      1 
ATOM   1715 O O      . VAL A 1 243 ? 12.02400 5.62700   7.18600   1.000 27.29878  ? 234 VAL A O      1 
ATOM   1716 C CB     . VAL A 1 243 ? 12.64900 8.20200   5.77300   1.000 25.17730  ? 234 VAL A CB     1 
ATOM   1717 C CG1    . VAL A 1 243 ? 14.12400 7.96500   6.06100   1.000 20.81613  ? 234 VAL A CG1    1 
ATOM   1718 C CG2    . VAL A 1 243 ? 12.47300 9.37700   4.82700   1.000 21.88662  ? 234 VAL A CG2    1 
ATOM   1719 N N      . GLY A 1 244 ? 13.10500 4.77600   5.39100   1.000 22.19933  ? 235 GLY A N      1 
ATOM   1720 C CA     . GLY A 1 244 ? 13.67700 3.65500   6.11100   1.000 22.28419  ? 235 GLY A CA     1 
ATOM   1721 C C      . GLY A 1 244 ? 15.17500 3.81200   6.27000   1.000 23.92625  ? 235 GLY A C      1 
ATOM   1722 O O      . GLY A 1 244 ? 15.80900 4.54600   5.50500   1.000 26.84013  ? 235 GLY A O      1 
ATOM   1723 N N      . VAL A 1 245 ? 15.75400 3.13900   7.26100   1.000 24.29093  ? 236 VAL A N      1 
ATOM   1724 C CA     . VAL A 1 245 ? 17.18400 3.21300   7.54100   1.000 21.91663  ? 236 VAL A CA     1 
ATOM   1725 C C      . VAL A 1 245 ? 17.71800 1.79700   7.70100   1.000 23.53835  ? 236 VAL A C      1 
ATOM   1726 O O      . VAL A 1 245 ? 17.17200 1.00900   8.48100   1.000 24.18967  ? 236 VAL A O      1 
ATOM   1727 C CB     . VAL A 1 245 ? 17.48200 4.04300   8.80500   1.000 20.11344  ? 236 VAL A CB     1 
ATOM   1728 C CG1    . VAL A 1 245 ? 18.98000 4.06400   9.08400   1.000 20.03668  ? 236 VAL A CG1    1 
ATOM   1729 C CG2    . VAL A 1 245 ? 16.94200 5.45700   8.65800   1.000 19.78686  ? 236 VAL A CG2    1 
ATOM   1730 N N      . ARG A 1 246 ? 18.78400 1.47800   6.97000   1.000 19.51644  ? 237 ARG A N      1 
ATOM   1731 C CA     . ARG A 1 246 ? 19.42400 0.17300   7.05100   1.000 19.61291  ? 237 ARG A CA     1 
ATOM   1732 C C      . ARG A 1 246 ? 20.84400 0.33000   7.57200   1.000 19.98389  ? 237 ARG A C      1 
ATOM   1733 O O      . ARG A 1 246 ? 21.59500 1.18500   7.09100   1.000 19.71363  ? 237 ARG A O      1 
ATOM   1734 C CB     . ARG A 1 246 ? 19.43800 -0.53800  5.69500   1.000 23.23141  ? 237 ARG A CB     1 
ATOM   1735 C CG     . ARG A 1 246 ? 19.76100 -2.01700  5.82300   1.000 22.89287  ? 237 ARG A CG     1 
ATOM   1736 C CD     . ARG A 1 246 ? 19.72700 -2.75300  4.49800   1.000 17.80670  ? 237 ARG A CD     1 
ATOM   1737 N NE     . ARG A 1 246 ? 19.34800 -4.14700  4.69500   1.000 23.83754  ? 237 ARG A NE     1 
ATOM   1738 C CZ     . ARG A 1 246 ? 19.61900 -5.13000  3.84900   1.000 24.24898  ? 237 ARG A CZ     1 
ATOM   1739 N NH1    . ARG A 1 246 ? 20.31400 -4.91900  2.74600   1.000 26.58579  ? 237 ARG A NH1    1 
ATOM   1740 N NH2    . ARG A 1 246 ? 19.18500 -6.35700  4.12100   1.000 24.27918  ? 237 ARG A NH2    1 
ATOM   1741 N N      . VAL A 1 247 ? 21.20700 -0.49400  8.55900   1.000 23.10902  ? 238 VAL A N      1 
ATOM   1742 C CA     . VAL A 1 247 ? 22.54100 -0.48600  9.14800   1.000 21.84718  ? 238 VAL A CA     1 
ATOM   1743 C C      . VAL A 1 247 ? 22.99400 -1.92300  9.36600   1.000 18.06707  ? 238 VAL A C      1 
ATOM   1744 O O      . VAL A 1 247 ? 22.19500 -2.86200  9.35900   1.000 18.93620  ? 238 VAL A O      1 
ATOM   1745 C CB     . VAL A 1 247 ? 22.59600 0.29500   10.48300  1.000 19.59749  ? 238 VAL A CB     1 
ATOM   1746 C CG1    . VAL A 1 247 ? 22.30400 1.77400   10.26100  1.000 17.92999  ? 238 VAL A CG1    1 
ATOM   1747 C CG2    . VAL A 1 247 ? 21.62700 -0.30200  11.48800  1.000 21.73159  ? 238 VAL A CG2    1 
ATOM   1748 N N      . SER A 1 248 ? 24.30000 -2.08600  9.56100   1.000 20.96740  ? 239 SER A N      1 
ATOM   1749 C CA     . SER A 1 248 ? 24.89300 -3.39600  9.83700   1.000 22.50621  ? 239 SER A CA     1 
ATOM   1750 C C      . SER A 1 248 ? 26.11600 -3.20000  10.71700  1.000 24.36680  ? 239 SER A C      1 
ATOM   1751 O O      . SER A 1 248 ? 27.26000 -3.24300  10.24700  1.000 21.44571  ? 239 SER A O      1 
ATOM   1752 C CB     . SER A 1 248 ? 25.26000 -4.12700  8.54500   1.000 24.92919  ? 239 SER A CB     1 
ATOM   1753 O OG     . SER A 1 248 ? 26.21600 -3.40000  7.79500   1.000 22.20313  ? 239 SER A OG     1 
ATOM   1754 N N      . PRO A 1 249 ? 25.91100 -2.98400  12.02000  1.000 25.49201  ? 240 PRO A N      1 
ATOM   1755 C CA     . PRO A 1 249 ? 27.04700 -2.65600  12.89800  1.000 20.83637  ? 240 PRO A CA     1 
ATOM   1756 C C      . PRO A 1 249 ? 28.05600 -3.78100  13.06500  1.000 22.96882  ? 240 PRO A C      1 
ATOM   1757 O O      . PRO A 1 249 ? 29.21300 -3.49600  13.39800  1.000 26.70310  ? 240 PRO A O      1 
ATOM   1758 C CB     . PRO A 1 249 ? 26.37200 -2.31800  14.23700  1.000 24.77589  ? 240 PRO A CB     1 
ATOM   1759 C CG     . PRO A 1 249 ? 24.93900 -2.02800  13.89400  1.000 26.25099  ? 240 PRO A CG     1 
ATOM   1760 C CD     . PRO A 1 249 ? 24.62100 -2.90300  12.72400  1.000 19.80860  ? 240 PRO A CD     1 
ATOM   1761 N N      . ALA A 1 250 ? 27.67200 -5.04100  12.84700  1.000 23.04463  ? 241 ALA A N      1 
ATOM   1762 C CA     . ALA A 1 250 ? 28.54900 -6.17600  13.11700  1.000 27.72950  ? 241 ALA A CA     1 
ATOM   1763 C C      . ALA A 1 250 ? 28.92200 -6.93900  11.84900  1.000 27.92883  ? 241 ALA A C      1 
ATOM   1764 O O      . ALA A 1 250 ? 29.12900 -8.15300  11.88900  1.000 37.52154  ? 241 ALA A O      1 
ATOM   1765 C CB     . ALA A 1 250 ? 27.90900 -7.11900  14.13500  1.000 23.70511  ? 241 ALA A CB     1 
ATOM   1766 N N      . ILE A 1 251 ? 29.01900 -6.24600  10.71800  1.000 33.88781  ? 242 ILE A N      1 
ATOM   1767 C CA     . ILE A 1 251 ? 29.47800 -6.83800  9.46500   1.000 27.94686  ? 242 ILE A CA     1 
ATOM   1768 C C      . ILE A 1 251 ? 30.75500 -6.12000  9.05300   1.000 28.99255  ? 242 ILE A C      1 
ATOM   1769 O O      . ILE A 1 251 ? 30.73800 -4.91100  8.79200   1.000 31.67268  ? 242 ILE A O      1 
ATOM   1770 C CB     . ILE A 1 251 ? 28.41300 -6.75400  8.36000   1.000 24.33607  ? 242 ILE A CB     1 
ATOM   1771 C CG1    . ILE A 1 251 ? 27.17700 -7.56500  8.75200   1.000 30.25382  ? 242 ILE A CG1    1 
ATOM   1772 C CG2    . ILE A 1 251 ? 28.97600 -7.26000  7.03800   1.000 26.47361  ? 242 ILE A CG2    1 
ATOM   1773 C CD1    . ILE A 1 251 ? 26.11400 -7.61900  7.67700   1.000 26.76530  ? 242 ILE A CD1    1 
ATOM   1774 N N      . ASP A 1 252 ? 31.86100 -6.86400  8.99600   1.000 32.93073  ? 243 ASP A N      1 
ATOM   1775 C CA     . ASP A 1 252 ? 33.17300 -6.31100  8.69100   1.000 36.49289  ? 243 ASP A CA     1 
ATOM   1776 C C      . ASP A 1 252 ? 33.45500 -6.24600  7.19300   1.000 32.75643  ? 243 ASP A C      1 
ATOM   1777 O O      . ASP A 1 252 ? 34.62500 -6.21700  6.79500   1.000 35.96160  ? 243 ASP A O      1 
ATOM   1778 C CB     . ASP A 1 252 ? 34.26400 -7.12600  9.39000   1.000 36.12790  ? 243 ASP A CB     1 
ATOM   1779 C CG     . ASP A 1 252 ? 34.03300 -7.25200  10.88300  1.000 49.02864  ? 243 ASP A CG     1 
ATOM   1780 O OD1    . ASP A 1 252 ? 32.98700 -6.77400  11.36900  1.000 50.63663  ? 243 ASP A OD1    1 
ATOM   1781 O OD2    . ASP A 1 252 ? 34.89900 -7.83400  11.57100  1.000 59.38807  ? 243 ASP A OD2    1 
ATOM   1782 N N      . HIS A 1 253 ? 32.41500 -6.22700  6.36200   1.000 35.48707  ? 244 HIS A N      1 
ATOM   1783 C CA     . HIS A 1 253 ? 32.59800 -6.17800  4.91600   1.000 36.89645  ? 244 HIS A CA     1 
ATOM   1784 C C      . HIS A 1 253 ? 33.33500 -4.90500  4.51400   1.000 32.42055  ? 244 HIS A C      1 
ATOM   1785 O O      . HIS A 1 253 ? 32.98300 -3.80700  4.95200   1.000 32.68778  ? 244 HIS A O      1 
ATOM   1786 C CB     . HIS A 1 253 ? 31.23700 -6.25700  4.22100   1.000 35.29952  ? 244 HIS A CB     1 
ATOM   1787 C CG     . HIS A 1 253 ? 31.31656 -6.34550  2.72776   1.000 47.67996  ? 244 HIS A CG     1 
ATOM   1788 N ND1    . HIS A 1 253 ? 30.74232 -5.40757  1.89628   1.000 41.18538  ? 244 HIS A ND1    1 
ATOM   1789 C CD2    . HIS A 1 253 ? 31.89173 -7.26497  1.91735   1.000 39.55481  ? 244 HIS A CD2    1 
ATOM   1790 C CE1    . HIS A 1 253 ? 30.96379 -5.74465  0.63801   1.000 43.30814  ? 244 HIS A CE1    1 
ATOM   1791 N NE2    . HIS A 1 253 ? 31.66076 -6.86642  0.62316   1.000 44.07013  ? 244 HIS A NE2    1 
ATOM   1792 N N      . LEU A 1 254 ? 34.37200 -5.06400  3.68700   1.000 34.54458  ? 245 LEU A N      1 
ATOM   1793 C CA     . LEU A 1 254 ? 35.17500 -3.94600  3.18500   1.000 32.08905  ? 245 LEU A CA     1 
ATOM   1794 C C      . LEU A 1 254 ? 35.80700 -3.15300  4.33100   1.000 38.74539  ? 245 LEU A C      1 
ATOM   1795 O O      . LEU A 1 254 ? 35.72900 -1.92300  4.38300   1.000 34.86831  ? 245 LEU A O      1 
ATOM   1796 C CB     . LEU A 1 254 ? 34.34300 -3.03200  2.28100   1.000 30.72167  ? 245 LEU A CB     1 
ATOM   1797 C CG     . LEU A 1 254 ? 33.67200 -3.68200  1.06900   1.000 39.15940  ? 245 LEU A CG     1 
ATOM   1798 C CD1    . LEU A 1 254 ? 32.79300 -2.67900  0.33200   1.000 28.65317  ? 245 LEU A CD1    1 
ATOM   1799 C CD2    . LEU A 1 254 ? 34.71000 -4.28000  0.13100   1.000 31.45678  ? 245 LEU A CD2    1 
ATOM   1800 N N      . ASP A 1 255 ? 36.43700 -3.87800  5.25900   1.000 34.26107  ? 246 ASP A N      1 
ATOM   1801 C CA     . ASP A 1 255 ? 37.16200 -3.28600  6.38700   1.000 32.77790  ? 246 ASP A CA     1 
ATOM   1802 C C      . ASP A 1 255 ? 36.26900 -2.40900  7.25900   1.000 32.81277  ? 246 ASP A C      1 
ATOM   1803 O O      . ASP A 1 255 ? 36.73200 -1.42500  7.84000   1.000 36.93537  ? 246 ASP A O      1 
ATOM   1804 C CB     . ASP A 1 255 ? 38.37600 -2.48000  5.91300   1.000 41.78345  ? 246 ASP A CB     1 
ATOM   1805 C CG     . ASP A 1 255 ? 39.51900 -3.35800  5.46500   1.000 38.97985  ? 246 ASP A CG     1 
ATOM   1806 O OD1    . ASP A 1 255 ? 39.38400 -4.59700  5.53800   1.000 43.72395  ? 246 ASP A OD1    1 
ATOM   1807 O OD2    . ASP A 1 255 ? 40.55700 -2.80600  5.04400   1.000 37.25613  ? 246 ASP A OD2    1 
ATOM   1808 N N      . ALA A 1 256 ? 34.98700 -2.75500  7.36900   1.000 33.65219  ? 247 ALA A N      1 
ATOM   1809 C CA     . ALA A 1 256 ? 34.04700 -1.97300  8.17500   1.000 32.95703  ? 247 ALA A CA     1 
ATOM   1810 C C      . ALA A 1 256 ? 33.93700 -2.58000  9.57400   1.000 34.34102  ? 247 ALA A C      1 
ATOM   1811 O O      . ALA A 1 256 ? 32.93100 -3.17700  9.96200   1.000 34.52385  ? 247 ALA A O      1 
ATOM   1812 C CB     . ALA A 1 256 ? 32.69000 -1.89800  7.48900   1.000 34.11813  ? 247 ALA A CB     1 
ATOM   1813 N N      . MET A 1 257 ? 35.00900 -2.40400  10.33900  1.000 35.23352  ? 248 MET A N      1 
ATOM   1814 C CA     . MET A 1 257 ? 35.11000 -2.92300  11.69600  1.000 32.47805  ? 248 MET A CA     1 
ATOM   1815 C C      . MET A 1 257 ? 34.85800 -1.81200  12.70700  1.000 31.44573  ? 248 MET A C      1 
ATOM   1816 O O      . MET A 1 257 ? 35.30100 -0.67500  12.51900  1.000 33.29261  ? 248 MET A O      1 
ATOM   1817 C CB     . MET A 1 257 ? 36.49300 -3.53800  11.93600  1.000 33.50385  ? 248 MET A CB     1 
ATOM   1818 C CG     . MET A 1 257 ? 36.78291 -3.89900  13.38418  1.000 46.54049  ? 248 MET A CG     1 
ATOM   1819 S SD     . MET A 1 257 ? 36.46066 -5.62966  13.77244  1.000 70.39638  ? 248 MET A SD     1 
ATOM   1820 C CE     . MET A 1 257 ? 38.13216 -6.27062  13.84744  1.000 53.50461  ? 248 MET A CE     1 
ATOM   1821 N N      . ASP A 1 258 ? 34.13900 -2.14500  13.77600  1.000 34.09221  ? 249 ASP A N      1 
ATOM   1822 C CA     . ASP A 1 258 ? 33.99100 -1.25600  14.91800  1.000 31.86295  ? 249 ASP A CA     1 
ATOM   1823 C C      . ASP A 1 258 ? 34.39300 -1.99900  16.18100  1.000 31.97235  ? 249 ASP A C      1 
ATOM   1824 O O      . ASP A 1 258 ? 34.09000 -3.18500  16.33700  1.000 31.59889  ? 249 ASP A O      1 
ATOM   1825 C CB     . ASP A 1 258 ? 32.56000 -0.72800  15.05700  1.000 27.78624  ? 249 ASP A CB     1 
ATOM   1826 C CG     . ASP A 1 258 ? 32.46800 0.44800   16.01100  1.000 35.10188  ? 249 ASP A CG     1 
ATOM   1827 O OD1    . ASP A 1 258 ? 32.78000 1.58100   15.58900  1.000 30.09868  ? 249 ASP A OD1    1 
ATOM   1828 O OD2    . ASP A 1 258 ? 32.09900 0.23700   17.18600  1.000 36.56640  ? 249 ASP A OD2    1 
ATOM   1829 N N      . SER A 1 259 ? 35.08100 -1.29300  17.08300  1.000 34.05893  ? 250 SER A N      1 
ATOM   1830 C CA     . SER A 1 259 ? 35.56900 -1.91500  18.30800  1.000 37.93745  ? 250 SER A CA     1 
ATOM   1831 C C      . SER A 1 259 ? 34.44000 -2.36000  19.22800  1.000 35.61842  ? 250 SER A C      1 
ATOM   1832 O O      . SER A 1 259 ? 34.64900 -3.25400  20.05500  1.000 36.94349  ? 250 SER A O      1 
ATOM   1833 C CB     . SER A 1 259 ? 36.49300 -0.95200  19.05300  1.000 32.93332  ? 250 SER A CB     1 
ATOM   1834 O OG     . SER A 1 259 ? 35.80500 0.23500   19.40800  1.000 40.04384  ? 250 SER A OG     1 
ATOM   1835 N N      . ASN A 1 260 ? 33.25800 -1.76200  19.10700  1.000 28.11054  ? 251 ASN A N      1 
ATOM   1836 C CA     . ASN A 1 260 ? 32.11000 -2.10600  19.94400  1.000 28.63141  ? 251 ASN A CA     1 
ATOM   1837 C C      . ASN A 1 260 ? 30.85000 -1.99900  19.09900  1.000 27.40615  ? 251 ASN A C      1 
ATOM   1838 O O      . ASN A 1 260 ? 30.10500 -1.01500  19.18200  1.000 27.21207  ? 251 ASN A O      1 
ATOM   1839 C CB     . ASN A 1 260 ? 32.03700 -1.19700  21.17400  1.000 27.38154  ? 251 ASN A CB     1 
ATOM   1840 C CG     . ASN A 1 260 ? 31.11400 -1.73900  22.24800  1.000 33.76982  ? 251 ASN A CG     1 
ATOM   1841 O OD1    . ASN A 1 260 ? 30.18000 -2.49100  21.96400  1.000 34.14259  ? 251 ASN A OD1    1 
ATOM   1842 N ND2    . ASN A 1 260 ? 31.37100 -1.35600  23.49400  1.000 34.30200  ? 251 ASN A ND2    1 
ATOM   1843 N N      . PRO A 1 261 ? 30.57600 -3.00800  18.26700  1.000 26.99416  ? 252 PRO A N      1 
ATOM   1844 C CA     . PRO A 1 261 ? 29.41400 -2.92000  17.36600  1.000 31.45024  ? 252 PRO A CA     1 
ATOM   1845 C C      . PRO A 1 261 ? 28.09300 -2.77800  18.09600  1.000 26.46822  ? 252 PRO A C      1 
ATOM   1846 O O      . PRO A 1 261 ? 27.18100 -2.11200  17.58900  1.000 29.68576  ? 252 PRO A O      1 
ATOM   1847 C CB     . PRO A 1 261 ? 29.48200 -4.23700  16.57800  1.000 31.19078  ? 252 PRO A CB     1 
ATOM   1848 C CG     . PRO A 1 261 ? 30.90300 -4.69300  16.70900  1.000 31.68605  ? 252 PRO A CG     1 
ATOM   1849 C CD     . PRO A 1 261 ? 31.33100 -4.25800  18.07500  1.000 26.66169  ? 252 PRO A CD     1 
ATOM   1850 N N      . LEU A 1 262 ? 27.96200 -3.38700  19.27500  1.000 28.18424  ? 253 LEU A N      1 
ATOM   1851 C CA     . LEU A 1 262 ? 26.72300 -3.26800  20.03200  1.000 28.77052  ? 253 LEU A CA     1 
ATOM   1852 C C      . LEU A 1 262 ? 26.49600 -1.83100  20.48800  1.000 24.32209  ? 253 LEU A C      1 
ATOM   1853 O O      . LEU A 1 262 ? 25.38300 -1.30400  20.37300  1.000 24.48751  ? 253 LEU A O      1 
ATOM   1854 C CB     . LEU A 1 262 ? 26.75300 -4.22800  21.22100  1.000 29.00153  ? 253 LEU A CB     1 
ATOM   1855 C CG     . LEU A 1 262 ? 25.61454 -4.19114  22.23809  1.000 37.70084  ? 253 LEU A CG     1 
ATOM   1856 C CD1    . LEU A 1 262 ? 24.26676 -4.17614  21.54415  1.000 34.76468  ? 253 LEU A CD1    1 
ATOM   1857 C CD2    . LEU A 1 262 ? 25.72704 -5.39663  23.15619  1.000 38.89713  ? 253 LEU A CD2    1 
ATOM   1858 N N      . SER A 1 263 ? 27.54400 -1.17600  20.98900  1.000 23.85295  ? 254 SER A N      1 
ATOM   1859 C CA     . SER A 1 263 ? 27.42100 0.22000   21.39700  1.000 23.70036  ? 254 SER A CA     1 
ATOM   1860 C C      . SER A 1 263 ? 27.11800 1.12100   20.20600  1.000 25.92562  ? 254 SER A C      1 
ATOM   1861 O O      . SER A 1 263 ? 26.32600 2.06500   20.32100  1.000 22.73073  ? 254 SER A O      1 
ATOM   1862 C CB     . SER A 1 263 ? 28.70000 0.67400   22.10300  1.000 26.59865  ? 254 SER A CB     1 
ATOM   1863 O OG     . SER A 1 263 ? 28.67300 2.06400   22.37100  1.000 32.72555  ? 254 SER A OG     1 
ATOM   1864 N N      . LEU A 1 264 ? 27.73600 0.84700   19.05400  1.000 21.85248  ? 255 LEU A N      1 
ATOM   1865 C CA     . LEU A 1 264 ? 27.49700 1.67500   17.87600  1.000 22.61657  ? 255 LEU A CA     1 
ATOM   1866 C C      . LEU A 1 264 ? 26.05500 1.55600   17.39900  1.000 17.87686  ? 255 LEU A C      1 
ATOM   1867 O O      . LEU A 1 264 ? 25.41500 2.56600   17.08300  1.000 21.34323  ? 255 LEU A O      1 
ATOM   1868 C CB     . LEU A 1 264 ? 28.46700 1.29300   16.75900  1.000 22.70739  ? 255 LEU A CB     1 
ATOM   1869 C CG     . LEU A 1 264 ? 28.27500 2.03200   15.43400  1.000 28.54890  ? 255 LEU A CG     1 
ATOM   1870 C CD1    . LEU A 1 264 ? 28.51200 3.52500   15.61000  1.000 21.46681  ? 255 LEU A CD1    1 
ATOM   1871 C CD2    . LEU A 1 264 ? 29.18700 1.45800   14.36200  1.000 27.30405  ? 255 LEU A CD2    1 
ATOM   1872 N N      . GLY A 1 265 ? 25.52600 0.33300   17.34500  1.000 17.44128  ? 256 GLY A N      1 
ATOM   1873 C CA     . GLY A 1 265 ? 24.14100 0.15400   16.94200  1.000 20.33792  ? 256 GLY A CA     1 
ATOM   1874 C C      . GLY A 1 265 ? 23.16500 0.83900   17.87900  1.000 23.80083  ? 256 GLY A C      1 
ATOM   1875 O O      . GLY A 1 265 ? 22.18500 1.44400   17.43700  1.000 22.55172  ? 256 GLY A O      1 
ATOM   1876 N N      . LEU A 1 266 ? 23.41700 0.75500   19.18700  1.000 23.02177  ? 257 LEU A N      1 
ATOM   1877 C CA     . LEU A 1 266 ? 22.55600 1.44700   20.14000  1.000 23.39067  ? 257 LEU A CA     1 
ATOM   1878 C C      . LEU A 1 266 ? 22.67300 2.95700   19.99000  1.000 22.25372  ? 257 LEU A C      1 
ATOM   1879 O O      . LEU A 1 266 ? 21.68400 3.68100   20.15600  1.000 25.10214  ? 257 LEU A O      1 
ATOM   1880 C CB     . LEU A 1 266 ? 22.89700 1.01700   21.56800  1.000 23.80204  ? 257 LEU A CB     1 
ATOM   1881 C CG     . LEU A 1 266 ? 22.52300 -0.42100  21.93200  1.000 21.97343  ? 257 LEU A CG     1 
ATOM   1882 C CD1    . LEU A 1 266 ? 23.00300 -0.76700  23.33000  1.000 25.74402  ? 257 LEU A CD1    1 
ATOM   1883 C CD2    . LEU A 1 266 ? 21.02200 -0.62100  21.81700  1.000 22.38840  ? 257 LEU A CD2    1 
ATOM   1884 N N      . ALA A 1 267 ? 23.87400 3.44900   19.67500  1.000 20.73351  ? 258 ALA A N      1 
ATOM   1885 C CA     . ALA A 1 267 ? 24.05300 4.88000   19.45500  1.000 23.65730  ? 258 ALA A CA     1 
ATOM   1886 C C      . ALA A 1 267 ? 23.23600 5.35900   18.26200  1.000 23.49009  ? 258 ALA A C      1 
ATOM   1887 O O      . ALA A 1 267 ? 22.57400 6.40000   18.33400  1.000 23.60240  ? 258 ALA A O      1 
ATOM   1888 C CB     . ALA A 1 267 ? 25.53400 5.20000   19.25500  1.000 21.65477  ? 258 ALA A CB     1 
ATOM   1889 N N      . VAL A 1 268 ? 23.26300 4.60600   17.16000  1.000 20.55439  ? 259 VAL A N      1 
ATOM   1890 C CA     . VAL A 1 268 ? 22.48100 4.97900   15.98400  1.000 23.48676  ? 259 VAL A CA     1 
ATOM   1891 C C      . VAL A 1 268 ? 20.99100 4.95600   16.30300  1.000 21.12752  ? 259 VAL A C      1 
ATOM   1892 O O      . VAL A 1 268 ? 20.24300 5.85700   15.90400  1.000 23.63780  ? 259 VAL A O      1 
ATOM   1893 C CB     . VAL A 1 268 ? 22.82600 4.05300   14.80000  1.000 27.12443  ? 259 VAL A CB     1 
ATOM   1894 C CG1    . VAL A 1 268 ? 21.91100 4.33100   13.61600  1.000 20.51940  ? 259 VAL A CG1    1 
ATOM   1895 C CG2    . VAL A 1 268 ? 24.28300 4.23000   14.40000  1.000 18.97822  ? 259 VAL A CG2    1 
ATOM   1896 N N      . VAL A 1 269 ? 20.54000 3.93500   17.03600  1.000 23.78415  ? 260 VAL A N      1 
ATOM   1897 C CA     . VAL A 1 269 ? 19.12700 3.84100   17.39700  1.000 22.42995  ? 260 VAL A CA     1 
ATOM   1898 C C      . VAL A 1 269 ? 18.70800 5.03800   18.24100  1.000 27.04714  ? 260 VAL A C      1 
ATOM   1899 O O      . VAL A 1 269 ? 17.60800 5.58200   18.07500  1.000 24.00714  ? 260 VAL A O      1 
ATOM   1900 C CB     . VAL A 1 269 ? 18.85200 2.50900   18.12000  1.000 27.63116  ? 260 VAL A CB     1 
ATOM   1901 C CG1    . VAL A 1 269 ? 17.48000 2.52800   18.77100  1.000 22.41988  ? 260 VAL A CG1    1 
ATOM   1902 C CG2    . VAL A 1 269 ? 18.96500 1.34600   17.14700  1.000 23.60156  ? 260 VAL A CG2    1 
ATOM   1903 N N      . GLU A 1 270 ? 19.58400 5.47400   19.15100  1.000 23.80256  ? 261 GLU A N      1 
ATOM   1904 C CA     . GLU A 1 270 ? 19.29100 6.64200   19.97600  1.000 26.05593  ? 261 GLU A CA     1 
ATOM   1905 C C      . GLU A 1 270 ? 19.04500 7.88000   19.12200  1.000 27.36891  ? 261 GLU A C      1 
ATOM   1906 O O      . GLU A 1 270 ? 18.11700 8.65300   19.38900  1.000 30.81293  ? 261 GLU A O      1 
ATOM   1907 C CB     . GLU A 1 270 ? 20.43900 6.88500   20.95700  1.000 25.97939  ? 261 GLU A CB     1 
ATOM   1908 C CG     . GLU A 1 270 ? 20.39100 8.22700   21.67000  1.000 31.03165  ? 261 GLU A CG     1 
ATOM   1909 C CD     . GLU A 1 270 ? 21.65200 8.50400   22.47000  1.000 36.77326  ? 261 GLU A CD     1 
ATOM   1910 O OE1    . GLU A 1 270 ? 22.32900 7.53400   22.87200  1.000 36.98420  ? 261 GLU A OE1    1 
ATOM   1911 O OE2    . GLU A 1 270 ? 21.97200 9.69100   22.68900  1.000 40.48260  ? 261 GLU A OE2    1 
ATOM   1912 N N      . ARG A 1 271 ? 19.86400 8.08700   18.08700  1.000 26.27015  ? 262 ARG A N      1 
ATOM   1913 C CA     . ARG A 1 271 ? 19.65900 9.23600   17.21100  1.000 27.59227  ? 262 ARG A CA     1 
ATOM   1914 C C      . ARG A 1 271 ? 18.38200 9.09500   16.39100  1.000 28.31625  ? 262 ARG A C      1 
ATOM   1915 O O      . ARG A 1 271 ? 17.72700 10.10000  16.09400  1.000 31.08219  ? 262 ARG A O      1 
ATOM   1916 C CB     . ARG A 1 271 ? 20.86400 9.43000   16.28700  1.000 28.96956  ? 262 ARG A CB     1 
ATOM   1917 C CG     . ARG A 1 271 ? 21.99800 10.25800  16.88500  1.000 28.18010  ? 262 ARG A CG     1 
ATOM   1918 C CD     . ARG A 1 271 ? 22.79200 9.45500   17.89500  1.000 34.92364  ? 262 ARG A CD     1 
ATOM   1919 N NE     . ARG A 1 271 ? 23.73700 10.26600  18.65300  1.000 33.42058  ? 262 ARG A NE     1 
ATOM   1920 C CZ     . ARG A 1 271 ? 24.43800 9.81900   19.68600  1.000 32.70230  ? 262 ARG A CZ     1 
ATOM   1921 N NH1    . ARG A 1 271 ? 24.33600 8.56600   20.10000  1.000 27.90716  ? 262 ARG A NH1    1 
ATOM   1922 N NH2    . ARG A 1 271 ? 25.25700 10.65000  20.32400  1.000 34.79322  ? 262 ARG A NH2    1 
ATOM   1923 N N      . LEU A 1 272 ? 18.01200 7.86700   16.01900  1.000 25.50515  ? 263 LEU A N      1 
ATOM   1924 C CA     . LEU A 1 272 ? 16.77400 7.66700   15.27200  1.000 27.83770  ? 263 LEU A CA     1 
ATOM   1925 C C      . LEU A 1 272 ? 15.55300 7.95000   16.14000  1.000 28.18923  ? 263 LEU A C      1 
ATOM   1926 O O      . LEU A 1 272 ? 14.58200 8.55800   15.67300  1.000 30.29422  ? 263 LEU A O      1 
ATOM   1927 C CB     . LEU A 1 272 ? 16.71900 6.24600   14.70800  1.000 24.31977  ? 263 LEU A CB     1 
ATOM   1928 C CG     . LEU A 1 272 ? 17.79200 5.88700   13.67500  1.000 25.40749  ? 263 LEU A CG     1 
ATOM   1929 C CD1    . LEU A 1 272 ? 17.60000 4.47000   13.15500  1.000 20.86051  ? 263 LEU A CD1    1 
ATOM   1930 C CD2    . LEU A 1 272 ? 17.79200 6.88600   12.52900  1.000 20.70127  ? 263 LEU A CD2    1 
ATOM   1931 N N      . ASN A 1 273 ? 15.58100 7.51800   17.40400  1.000 27.45044  ? 264 ASN A N      1 
ATOM   1932 C CA     . ASN A 1 273 ? 14.47900 7.82300   18.31000  1.000 26.66634  ? 264 ASN A CA     1 
ATOM   1933 C C      . ASN A 1 273 ? 14.34800 9.32500   18.52600  1.000 27.08267  ? 264 ASN A C      1 
ATOM   1934 O O      . ASN A 1 273 ? 13.23400 9.85300   18.61600  1.000 25.32152  ? 264 ASN A O      1 
ATOM   1935 C CB     . ASN A 1 273 ? 14.67500 7.10600   19.64700  1.000 21.70667  ? 264 ASN A CB     1 
ATOM   1936 C CG     . ASN A 1 273 ? 14.50400 5.60200   19.53900  1.000 26.25639  ? 264 ASN A CG     1 
ATOM   1937 O OD1    . ASN A 1 273 ? 13.80800 5.10400   18.65400  1.000 26.70691  ? 264 ASN A OD1    1 
ATOM   1938 N ND2    . ASN A 1 273 ? 15.13700 4.86900   20.44900  1.000 24.10002  ? 264 ASN A ND2    1 
ATOM   1939 N N      . LYS A 1 274 ? 15.47900 10.03100  18.60000  1.000 24.31250  ? 265 LYS A N      1 
ATOM   1940 C CA     . LYS A 1 274 ? 15.44100 11.47000  18.83600  1.000 25.93078  ? 265 LYS A CA     1 
ATOM   1941 C C      . LYS A 1 274 ? 14.91100 12.21900  17.61700  1.000 30.98121  ? 265 LYS A C      1 
ATOM   1942 O O      . LYS A 1 274 ? 14.22400 13.23700  17.75900  1.000 32.29208  ? 265 LYS A O      1 
ATOM   1943 C CB     . LYS A 1 274 ? 16.83400 11.96900  19.21700  1.000 33.63322  ? 265 LYS A CB     1 
ATOM   1944 C CG     . LYS A 1 274 ? 16.83600 13.03400  20.29800  1.000 37.66322  ? 265 LYS A CG     1 
ATOM   1945 C CD     . LYS A 1 274 ? 18.21900 13.19300  20.91200  1.000 43.31668  ? 265 LYS A CD     1 
ATOM   1946 C CE     . LYS A 1 274 ? 19.23400 13.65300  19.87900  1.000 53.14823  ? 265 LYS A CE     1 
ATOM   1947 N NZ     . LYS A 1 274 ? 18.88800 14.98900  19.32100  1.000 47.64541  ? 265 LYS A NZ     1 
ATOM   1948 N N      . ILE A 1 275 ? 15.22100 11.73600  16.41200  1.000 25.37444  ? 266 ILE A N      1 
ATOM   1949 C CA     . ILE A 1 275 ? 14.68200 12.35800  15.20500  1.000 25.77508  ? 266 ILE A CA     1 
ATOM   1950 C C      . ILE A 1 275 ? 13.17000 12.18800  15.15200  1.000 27.60968  ? 266 ILE A C      1 
ATOM   1951 O O      . ILE A 1 275 ? 12.44000 13.09800  14.73600  1.000 25.00222  ? 266 ILE A O      1 
ATOM   1952 C CB     . ILE A 1 275 ? 15.36400 11.77300  13.95300  1.000 30.27564  ? 266 ILE A CB     1 
ATOM   1953 C CG1    . ILE A 1 275 ? 16.82900 12.20500  13.89200  1.000 25.31136  ? 266 ILE A CG1    1 
ATOM   1954 C CG2    . ILE A 1 275 ? 14.62800 12.19200  12.68700  1.000 27.19711  ? 266 ILE A CG2    1 
ATOM   1955 C CD1    . ILE A 1 275 ? 17.57800 11.63400  12.71200  1.000 26.87863  ? 266 ILE A CD1    1 
ATOM   1956 N N      . GLN A 1 276 ? 12.67500 11.02600  15.58500  1.000 28.33456  ? 267 GLN A N      1 
ATOM   1957 C CA     . GLN A 1 276 ? 11.23800 10.77800  15.56900  1.000 32.42382  ? 267 GLN A CA     1 
ATOM   1958 C C      . GLN A 1 276 ? 10.49600 11.65800  16.56900  1.000 33.85218  ? 267 GLN A C      1 
ATOM   1959 O O      . GLN A 1 276 ? 9.36800  12.08300  16.29600  1.000 34.37836  ? 267 GLN A O      1 
ATOM   1960 C CB     . GLN A 1 276 ? 10.96200 9.30000   15.84400  1.000 26.44796  ? 267 GLN A CB     1 
ATOM   1961 C CG     . GLN A 1 276 ? 11.43000 8.36800   14.73600  1.000 26.04057  ? 267 GLN A CG     1 
ATOM   1962 C CD     . GLN A 1 276 ? 11.13500 6.91300   15.03900  1.000 31.31345  ? 267 GLN A CD     1 
ATOM   1963 O OE1    . GLN A 1 276 ? 11.07900 6.07600   14.13600  1.000 26.40579  ? 267 GLN A OE1    1 
ATOM   1964 N NE2    . GLN A 1 276 ? 10.94600 6.60300   16.31600  1.000 25.36205  ? 267 GLN A NE2    1 
ATOM   1965 N N      . LEU A 1 277 ? 11.10500 11.94500  17.72000  1.000 33.56664  ? 268 LEU A N      1 
ATOM   1966 C CA     . LEU A 1 277 ? 10.46200 12.81700  18.69900  1.000 36.81558  ? 268 LEU A CA     1 
ATOM   1967 C C      . LEU A 1 277 ? 10.49600 14.27700  18.26300  1.000 35.24401  ? 268 LEU A C      1 
ATOM   1968 O O      . LEU A 1 277 ? 9.55000  15.02700  18.52800  1.000 42.39500  ? 268 LEU A O      1 
ATOM   1969 C CB     . LEU A 1 277 ? 11.12000 12.65800  20.06900  1.000 31.30248  ? 268 LEU A CB     1 
ATOM   1970 C CG     . LEU A 1 277 ? 10.84596 11.34685  20.80715  1.000 42.65436  ? 268 LEU A CG     1 
ATOM   1971 C CD1    . LEU A 1 277 ? 11.16773 11.49173  22.28989  1.000 42.63304  ? 268 LEU A CD1    1 
ATOM   1972 C CD2    . LEU A 1 277 ? 9.40347  10.90666  20.60589  1.000 41.01492  ? 268 LEU A CD2    1 
ATOM   1973 N N      . HIS A 1 278 ? 11.57400 14.70000  17.60000  1.000 33.83707  ? 269 HIS A N      1 
ATOM   1974 C CA     . HIS A 1 278 ? 11.65500 16.08300  17.14200  1.000 35.63696  ? 269 HIS A CA     1 
ATOM   1975 C C      . HIS A 1 278 ? 10.66100 16.34500  16.01700  1.000 37.39302  ? 269 HIS A C      1 
ATOM   1976 O O      . HIS A 1 278 ? 9.95400  17.36000  16.02100  1.000 42.25538  ? 269 HIS A O      1 
ATOM   1977 C CB     . HIS A 1 278 ? 13.07900 16.40800  16.69000  1.000 34.11610  ? 269 HIS A CB     1 
ATOM   1978 N N      . SER A 1 279 ? 10.58700 15.43400  15.04700  1.000 34.08734  ? 270 SER A N      1 
ATOM   1979 C CA     . SER A 1 279 ? 9.65000  15.57400  13.94100  1.000 32.82444  ? 270 SER A CA     1 
ATOM   1980 C C      . SER A 1 279 ? 8.22400  15.20000  14.31900  1.000 37.50128  ? 270 SER A C      1 
ATOM   1981 O O      . SER A 1 279 ? 7.30500  15.47100  13.53900  1.000 33.51173  ? 270 SER A O      1 
ATOM   1982 C CB     . SER A 1 279 ? 10.10300 14.71800  12.75500  1.000 37.20810  ? 270 SER A CB     1 
ATOM   1983 O OG     . SER A 1 279 ? 11.34900 15.16500  12.25000  1.000 43.86798  ? 270 SER A OG     1 
ATOM   1984 N N      . GLY A 1 280 ? 8.01700  14.58800  15.48400  1.000 41.59653  ? 271 GLY A N      1 
ATOM   1985 C CA     . GLY A 1 280 ? 6.68400  14.19200  15.89100  1.000 37.24278  ? 271 GLY A CA     1 
ATOM   1986 C C      . GLY A 1 280 ? 6.06700  13.09000  15.06400  1.000 38.92335  ? 271 GLY A C      1 
ATOM   1987 O O      . GLY A 1 280 ? 4.84800  12.90900  15.10300  1.000 44.41280  ? 271 GLY A O      1 
ATOM   1988 N N      . SER A 1 281 ? 6.87400  12.34400  14.31200  1.000 37.10994  ? 272 SER A N      1 
ATOM   1989 C CA     . SER A 1 281 ? 6.37800  11.26100  13.47800  1.000 35.36806  ? 272 SER A CA     1 
ATOM   1990 C C      . SER A 1 281 ? 7.38100  10.11800  13.48400  1.000 37.43160  ? 272 SER A C      1 
ATOM   1991 O O      . SER A 1 281 ? 8.58000  10.32400  13.69000  1.000 37.38215  ? 272 SER A O      1 
ATOM   1992 C CB     . SER A 1 281 ? 6.11800  11.73000  12.04000  1.000 38.99200  ? 272 SER A CB     1 
ATOM   1993 O OG     . SER A 1 281 ? 7.25800  12.38100  11.50600  1.000 46.12742  ? 272 SER A OG     1 
ATOM   1994 N N      . LYS A 1 282 ? 6.87800  8.91000   13.25200  1.000 37.39056  ? 273 LYS A N      1 
ATOM   1995 C CA     . LYS A 1 282 ? 7.70500  7.71300   13.25700  1.000 33.81078  ? 273 LYS A CA     1 
ATOM   1996 C C      . LYS A 1 282 ? 8.32100  7.47600   11.88500  1.000 30.66287  ? 273 LYS A C      1 
ATOM   1997 O O      . LYS A 1 282 ? 7.69000  7.72800   10.85400  1.000 26.67945  ? 273 LYS A O      1 
ATOM   1998 C CB     . LYS A 1 282 ? 6.88000  6.49300   13.66900  1.000 36.86471  ? 273 LYS A CB     1 
ATOM   1999 C CG     . LYS A 1 282 ? 6.45600  6.48200   15.12700  1.000 41.69365  ? 273 LYS A CG     1 
ATOM   2000 C CD     . LYS A 1 282 ? 7.53700  5.88700   16.01500  1.000 38.32499  ? 273 LYS A CD     1 
ATOM   2001 C CE     . LYS A 1 282 ? 7.11900  5.91200   17.47600  1.000 38.33976  ? 273 LYS A CE     1 
ATOM   2002 N NZ     . LYS A 1 282 ? 5.77200  5.30900   17.67300  1.000 42.73691  ? 273 LYS A NZ     1 
ATOM   2003 N N      . LEU A 1 283 ? 9.56000  6.99100   11.88200  1.000 32.18119  ? 274 LEU A N      1 
ATOM   2004 C CA     . LEU A 1 283 ? 10.17300 6.52800   10.64800  1.000 22.84076  ? 274 LEU A CA     1 
ATOM   2005 C C      . LEU A 1 283 ? 9.41800  5.31500   10.11300  1.000 23.33684  ? 274 LEU A C      1 
ATOM   2006 O O      . LEU A 1 283 ? 8.64100  4.66900   10.82300  1.000 21.90999  ? 274 LEU A O      1 
ATOM   2007 C CB     . LEU A 1 283 ? 11.64100 6.16700   10.87600  1.000 23.13512  ? 274 LEU A CB     1 
ATOM   2008 C CG     . LEU A 1 283 ? 12.62600 7.30700   11.13500  1.000 26.60472  ? 274 LEU A CG     1 
ATOM   2009 C CD1    . LEU A 1 283 ? 13.98400 6.75000   11.53300  1.000 25.99758  ? 274 LEU A CD1    1 
ATOM   2010 C CD2    . LEU A 1 283 ? 12.74900 8.19400   9.90700   1.000 22.27844  ? 274 LEU A CD2    1 
ATOM   2011 N N      . ALA A 1 284 ? 9.65400  5.00900   8.83700   1.000 19.89122  ? 275 ALA A N      1 
ATOM   2012 C CA     . ALA A 1 284 ? 9.03100  3.83400   8.23900   1.000 22.97845  ? 275 ALA A CA     1 
ATOM   2013 C C      . ALA A 1 284 ? 9.45600  2.56400   8.96500   1.000 23.77739  ? 275 ALA A C      1 
ATOM   2014 O O      . ALA A 1 284 ? 8.61300  1.76900   9.39600   1.000 25.17519  ? 275 ALA A O      1 
ATOM   2015 C CB     . ALA A 1 284 ? 9.37600  3.75200   6.75300   1.000 22.05859  ? 275 ALA A CB     1 
ATOM   2016 N N      . TYR A 1 285 ? 10.76100 2.36800   9.12700   1.000 20.40344  ? 276 TYR A N      1 
ATOM   2017 C CA     . TYR A 1 285 ? 11.27600 1.17300   9.78300   1.000 24.75649  ? 276 TYR A CA     1 
ATOM   2018 C C      . TYR A 1 285 ? 12.76100 1.36200   10.05200  1.000 27.20830  ? 276 TYR A C      1 
ATOM   2019 O O      . TYR A 1 285 ? 13.40500 2.26600   9.51300   1.000 22.35960  ? 276 TYR A O      1 
ATOM   2020 C CB     . TYR A 1 285 ? 11.04300 -0.08200  8.93400   1.000 24.22766  ? 276 TYR A CB     1 
ATOM   2021 C CG     . TYR A 1 285 ? 11.60700 0.02000   7.53400   1.000 27.33487  ? 276 TYR A CG     1 
ATOM   2022 C CD1    . TYR A 1 285 ? 12.93600 -0.29200  7.27300   1.000 27.25761  ? 276 TYR A CD1    1 
ATOM   2023 C CD2    . TYR A 1 285 ? 10.81000 0.42800   6.47300   1.000 25.34888  ? 276 TYR A CD2    1 
ATOM   2024 C CE1    . TYR A 1 285 ? 13.45400 -0.19900  5.99700   1.000 23.48908  ? 276 TYR A CE1    1 
ATOM   2025 C CE2    . TYR A 1 285 ? 11.32000 0.52400   5.19400   1.000 27.40037  ? 276 TYR A CE2    1 
ATOM   2026 C CZ     . TYR A 1 285 ? 12.64200 0.20900   4.96200   1.000 24.04460  ? 276 TYR A CZ     1 
ATOM   2027 O OH     . TYR A 1 285 ? 13.15200 0.30300   3.68800   1.000 26.61508  ? 276 TYR A OH     1 
ATOM   2028 N N      . LEU A 1 286 ? 13.29400 0.48900   10.90100  1.000 25.60409  ? 277 LEU A N      1 
ATOM   2029 C CA     . LEU A 1 286 ? 14.73000 0.30200   11.05500  1.000 23.06768  ? 277 LEU A CA     1 
ATOM   2030 C C      . LEU A 1 286 ? 15.07600 -1.07200  10.50000  1.000 28.40144  ? 277 LEU A C      1 
ATOM   2031 O O      . LEU A 1 286 ? 14.48300 -2.07600  10.90900  1.000 24.67482  ? 277 LEU A O      1 
ATOM   2032 C CB     . LEU A 1 286 ? 15.15700 0.42000   12.51800  1.000 25.75497  ? 277 LEU A CB     1 
ATOM   2033 C CG     . LEU A 1 286 ? 16.60900 0.02900   12.80600  1.000 21.97473  ? 277 LEU A CG     1 
ATOM   2034 C CD1    . LEU A 1 286 ? 17.56900 0.92300   12.03600  1.000 21.01577  ? 277 LEU A CD1    1 
ATOM   2035 C CD2    . LEU A 1 286 ? 16.91200 0.06500   14.29900  1.000 21.45705  ? 277 LEU A CD2    1 
ATOM   2036 N N      . HIS A 1 287 ? 16.01000 -1.11200  9.55700   1.000 23.96580  ? 278 HIS A N      1 
ATOM   2037 C CA     . HIS A 1 287 ? 16.40700 -2.34600  8.89100   1.000 22.55524  ? 278 HIS A CA     1 
ATOM   2038 C C      . HIS A 1 287 ? 17.81400 -2.70300  9.34700   1.000 21.61583  ? 278 HIS A C      1 
ATOM   2039 O O      . HIS A 1 287 ? 18.74700 -1.91300  9.17000   1.000 25.15337  ? 278 HIS A O      1 
ATOM   2040 C CB     . HIS A 1 287 ? 16.34300 -2.18500  7.37100   1.000 20.42193  ? 278 HIS A CB     1 
ATOM   2041 C CG     . HIS A 1 287 ? 16.34600 -3.48000  6.62000   1.000 22.22407  ? 278 HIS A CG     1 
ATOM   2042 N ND1    . HIS A 1 287 ? 16.20900 -3.54300  5.24900   1.000 25.44605  ? 278 HIS A ND1    1 
ATOM   2043 C CD2    . HIS A 1 287 ? 16.46800 -4.76000  7.04400   1.000 21.73493  ? 278 HIS A CD2    1 
ATOM   2044 C CE1    . HIS A 1 287 ? 16.24600 -4.80500  4.86200   1.000 24.32173  ? 278 HIS A CE1    1 
ATOM   2045 N NE2    . HIS A 1 287 ? 16.40200 -5.56400  5.93200   1.000 25.37306  ? 278 HIS A NE2    1 
ATOM   2046 N N      . VAL A 1 288 ? 17.96700 -3.87800  9.94900   1.000 22.18892  ? 279 VAL A N      1 
ATOM   2047 C CA     . VAL A 1 288 ? 19.25200 -4.32400  10.47300  1.000 23.58373  ? 279 VAL A CA     1 
ATOM   2048 C C      . VAL A 1 288 ? 19.57900 -5.66800  9.84400   1.000 25.82803  ? 279 VAL A C      1 
ATOM   2049 O O      . VAL A 1 288 ? 18.82500 -6.63600  10.00400  1.000 24.74272  ? 279 VAL A O      1 
ATOM   2050 C CB     . VAL A 1 288 ? 19.24600 -4.42400  12.00600  1.000 23.95866  ? 279 VAL A CB     1 
ATOM   2051 C CG1    . VAL A 1 288 ? 20.58100 -4.96300  12.50200  1.000 20.73392  ? 279 VAL A CG1    1 
ATOM   2052 C CG2    . VAL A 1 288 ? 18.95600 -3.06500  12.62200  1.000 19.70141  ? 279 VAL A CG2    1 
ATOM   2053 N N      . THR A 1 289 ? 20.69800 -5.72700  9.13300   1.000 25.23624  ? 280 THR A N      1 
ATOM   2054 C CA     . THR A 1 289 ? 21.18700 -6.96300  8.54800   1.000 28.22184  ? 280 THR A CA     1 
ATOM   2055 C C      . THR A 1 289 ? 22.44400 -7.41000  9.28500   1.000 25.12647  ? 280 THR A C      1 
ATOM   2056 O O      . THR A 1 289 ? 23.20500 -6.58900  9.80600   1.000 26.22295  ? 280 THR A O      1 
ATOM   2057 C CB     . THR A 1 289 ? 21.46700 -6.79500  7.04700   1.000 24.76648  ? 280 THR A CB     1 
ATOM   2058 O OG1    . THR A 1 289 ? 21.84800 -8.05500  6.48300   1.000 30.90446  ? 280 THR A OG1    1 
ATOM   2059 C CG2    . THR A 1 289 ? 22.57200 -5.77700  6.80800   1.000 26.00821  ? 280 THR A CG2    1 
ATOM   2060 N N      . ALA A 1 290 ? 22.64100 -8.72500  9.34600   1.000 26.77843  ? 281 ALA A N      1 
ATOM   2061 C CA     . ALA A 1 290 ? 23.74700 -9.31000  10.08900  1.000 31.95841  ? 281 ALA A CA     1 
ATOM   2062 C C      . ALA A 1 290 ? 24.34100 -10.45500 9.28000   1.000 30.83487  ? 281 ALA A C      1 
ATOM   2063 O O      . ALA A 1 290 ? 23.87000 -10.78300 8.18600   1.000 29.99846  ? 281 ALA A O      1 
ATOM   2064 C CB     . ALA A 1 290 ? 23.29400 -9.79300  11.47100  1.000 27.66747  ? 281 ALA A CB     1 
ATOM   2065 N N      . GLU A 1 291 ? 25.38700 -11.06500 9.83300   1.000 35.58359  ? 282 GLU A N      1 
ATOM   2066 C CA     . GLU A 1 291 ? 26.02400 -12.20400 9.18700   1.000 37.37530  ? 282 GLU A CA     1 
ATOM   2067 C C      . GLU A 1 291 ? 25.04000 -13.36000 9.06300   1.000 38.99086  ? 282 GLU A C      1 
ATOM   2068 O O      . GLU A 1 291 ? 24.37900 -13.73900 10.03500  1.000 39.76236  ? 282 GLU A O      1 
ATOM   2069 C CB     . GLU A 1 291 ? 27.25800 -12.63600 9.98100   1.000 25.75284  ? 282 GLU A CB     1 
ATOM   2070 N N      . ALA A 1 292 ? 24.94700 -13.92300 7.85600   1.000 44.83706  ? 283 ALA A N      1 
ATOM   2071 C CA     . ALA A 1 292 ? 23.98800 -14.98500 7.57800   1.000 42.71790  ? 283 ALA A CA     1 
ATOM   2072 C C      . ALA A 1 292 ? 24.32800 -16.29800 8.27100   1.000 42.16957  ? 283 ALA A C      1 
ATOM   2073 O O      . ALA A 1 292 ? 23.51300 -17.22600 8.22900   1.000 44.58474  ? 283 ALA A O      1 
ATOM   2074 C CB     . ALA A 1 292 ? 23.88500 -15.21100 6.06800   1.000 38.66872  ? 283 ALA A CB     1 
ATOM   2075 N N      . ASP A 1 293 ? 25.49200 -16.40100 8.90200   1.000 47.17885  ? 284 ASP A N      1 
ATOM   2076 C CA     . ASP A 1 293 ? 25.90900 -17.62200 9.59500   1.000 49.21110  ? 284 ASP A CA     1 
ATOM   2077 C C      . ASP A 1 293 ? 25.60700 -17.54700 11.08700  1.000 55.79760  ? 284 ASP A C      1 
ATOM   2078 O O      . ASP A 1 293 ? 26.45000 -17.86700 11.92500  1.000 65.02956  ? 284 ASP A O      1 
ATOM   2079 C CB     . ASP A 1 293 ? 27.39100 -17.88100 9.35100   1.000 54.59571  ? 284 ASP A CB     1 
ATOM   2080 N N      . TRP A 1 294 ? 24.39600 -17.12500 11.44000  1.000 51.48557  ? 285 TRP A N      1 
ATOM   2081 C CA     . TRP A 1 294 ? 24.00000 -17.03900 12.84400  1.000 54.68220  ? 285 TRP A CA     1 
ATOM   2082 C C      . TRP A 1 294 ? 23.14100 -18.23400 13.24300  1.000 53.85364  ? 285 TRP A C      1 
ATOM   2083 O O      . TRP A 1 294 ? 22.93900 -18.49600 14.42800  1.000 58.66651  ? 285 TRP A O      1 
ATOM   2084 C CB     . TRP A 1 294 ? 23.24500 -15.73400 13.11700  1.000 42.07150  ? 285 TRP A CB     1 
ATOM   2085 C CG     . TRP A 1 294 ? 21.91500 -15.64500 12.42900  1.000 43.03370  ? 285 TRP A CG     1 
ATOM   2086 C CD1    . TRP A 1 294 ? 21.67200 -15.16400 11.17600  1.000 43.41669  ? 285 TRP A CD1    1 
ATOM   2087 C CD2    . TRP A 1 294 ? 20.64400 -16.04400 12.95900  1.000 46.43472  ? 285 TRP A CD2    1 
ATOM   2088 N NE1    . TRP A 1 294 ? 20.33000 -15.24000 10.89100  1.000 40.30948  ? 285 TRP A NE1    1 
ATOM   2089 C CE2    . TRP A 1 294 ? 19.67700 -15.77700 11.96900  1.000 42.07332  ? 285 TRP A CE2    1 
ATOM   2090 C CE3    . TRP A 1 294 ? 20.23100 -16.60200 14.17300  1.000 41.25006  ? 285 TRP A CE3    1 
ATOM   2091 C CZ2    . TRP A 1 294 ? 18.32200 -16.04800 12.15500  1.000 36.39297  ? 285 TRP A CZ2    1 
ATOM   2092 C CZ3    . TRP A 1 294 ? 18.88600 -16.87100 14.35600  1.000 42.28129  ? 285 TRP A CZ3    1 
ATOM   2093 C CH2    . TRP A 1 294 ? 17.94800 -16.59400 13.35200  1.000 42.37640  ? 285 TRP A CH2    1 
ATOM   2094 N N      . GLU A 1 305 ? 23.32500 -15.23100 26.01600  1.000 45.25112  ? 296 GLU A N      1 
ATOM   2095 C CA     . GLU A 1 305 ? 23.33500 -13.86300 25.51100  1.000 49.20594  ? 296 GLU A CA     1 
ATOM   2096 C C      . GLU A 1 305 ? 22.38900 -13.71200 24.32500  1.000 45.60819  ? 296 GLU A C      1 
ATOM   2097 O O      . GLU A 1 305 ? 22.25800 -14.62100 23.50600  1.000 54.96405  ? 296 GLU A O      1 
ATOM   2098 C CB     . GLU A 1 305 ? 24.75300 -13.44900 25.11100  1.000 46.36387  ? 296 GLU A CB     1 
ATOM   2099 N N      . ALA A 1 306 ? 21.73000 -12.56100 24.23900  1.000 37.76059  ? 297 ALA A N      1 
ATOM   2100 C CA     . ALA A 1 306 ? 20.80500 -12.28100 23.15200  1.000 40.15288  ? 297 ALA A CA     1 
ATOM   2101 C C      . ALA A 1 306 ? 21.54500 -11.69700 21.95600  1.000 37.52130  ? 297 ALA A C      1 
ATOM   2102 O O      . ALA A 1 306 ? 22.58600 -11.04800 22.09800  1.000 35.26070  ? 297 ALA A O      1 
ATOM   2103 C CB     . ALA A 1 306 ? 19.70700 -11.31800 23.60800  1.000 31.93414  ? 297 ALA A CB     1 
ATOM   2104 N N      . ARG A 1 307 ? 20.99400 -11.93800 20.76900  1.000 38.68974  ? 298 ARG A N      1 
ATOM   2105 C CA     . ARG A 1 307 ? 21.59400 -11.43400 19.54400  1.000 29.71523  ? 298 ARG A CA     1 
ATOM   2106 C C      . ARG A 1 307 ? 21.56500 -9.90900  19.51300  1.000 31.40296  ? 298 ARG A C      1 
ATOM   2107 O O      . ARG A 1 307 ? 20.73200 -9.25800  20.15200  1.000 34.75304  ? 298 ARG A O      1 
ATOM   2108 C CB     . ARG A 1 307 ? 20.85800 -11.97600 18.31700  1.000 34.34420  ? 298 ARG A CB     1 
ATOM   2109 C CG     . ARG A 1 307 ? 20.93500 -13.47900 18.12900  1.000 29.98999  ? 298 ARG A CG     1 
ATOM   2110 C CD     . ARG A 1 307 ? 20.13300 -13.89400 16.90600  1.000 39.73932  ? 298 ARG A CD     1 
ATOM   2111 N NE     . ARG A 1 307 ? 20.60200 -13.22500 15.69700  1.000 39.07619  ? 298 ARG A NE     1 
ATOM   2112 C CZ     . ARG A 1 307 ? 19.87000 -13.04600 14.60500  1.000 40.63823  ? 298 ARG A CZ     1 
ATOM   2113 N NH1    . ARG A 1 307 ? 18.61400 -13.45700 14.53900  1.000 45.96876  ? 298 ARG A NH1    1 
ATOM   2114 N NH2    . ARG A 1 307 ? 20.40900 -12.43200 13.55500  1.000 35.12058  ? 298 ARG A NH2    1 
ATOM   2115 N N      . LEU A 1 308 ? 22.49900 -9.33900  18.74700  1.000 36.05414  ? 299 LEU A N      1 
ATOM   2116 C CA     . LEU A 1 308 ? 22.48500 -7.90000  18.51200  1.000 30.69843  ? 299 LEU A CA     1 
ATOM   2117 C C      . LEU A 1 308 ? 21.20200 -7.46500  17.81600  1.000 29.09984  ? 299 LEU A C      1 
ATOM   2118 O O      . LEU A 1 308 ? 20.73900 -6.33600  18.01600  1.000 31.06029  ? 299 LEU A O      1 
ATOM   2119 C CB     . LEU A 1 308 ? 23.71300 -7.49700  17.69100  1.000 29.73419  ? 299 LEU A CB     1 
ATOM   2120 C CG     . LEU A 1 308 ? 23.83600 -6.04400  17.22600  1.000 31.35991  ? 299 LEU A CG     1 
ATOM   2121 C CD1    . LEU A 1 308 ? 25.24900 -5.52900  17.44500  1.000 28.89434  ? 299 LEU A CD1    1 
ATOM   2122 C CD2    . LEU A 1 308 ? 23.44600 -5.91800  15.76100  1.000 31.41927  ? 299 LEU A CD2    1 
ATOM   2123 N N      . MET A 1 309 ? 20.60900 -8.35100  17.01200  1.000 26.58759  ? 300 MET A N      1 
ATOM   2124 C CA     . MET A 1 309 ? 19.37300 -8.01600  16.31300  1.000 31.33273  ? 300 MET A CA     1 
ATOM   2125 C C      . MET A 1 309 ? 18.24900 -7.70100  17.29300  1.000 25.69837  ? 300 MET A C      1 
ATOM   2126 O O      . MET A 1 309 ? 17.51500 -6.72200  17.11400  1.000 25.82792  ? 300 MET A O      1 
ATOM   2127 C CB     . MET A 1 309 ? 18.97200 -9.16400  15.38400  1.000 22.96166  ? 300 MET A CB     1 
ATOM   2128 C CG     . MET A 1 309 ? 17.90684 -8.80531  14.35900  1.000 25.52192  ? 300 MET A CG     1 
ATOM   2129 S SD     . MET A 1 309 ? 18.55754 -7.88032  12.95300  1.000 35.09250  ? 300 MET A SD     1 
ATOM   2130 C CE     . MET A 1 309 ? 19.24688 -9.20377  11.96094  1.000 29.72407  ? 300 MET A CE     1 
ATOM   2131 N N      . ARG A 1 310 ? 18.10000 -8.51500  18.34200  1.000 28.30806  ? 301 ARG A N      1 
ATOM   2132 C CA     . ARG A 1 310 ? 17.02100 -8.28700  19.29800  1.000 27.39695  ? 301 ARG A CA     1 
ATOM   2133 C C      . ARG A 1 310 ? 17.30000 -7.07000  20.17200  1.000 26.96339  ? 301 ARG A C      1 
ATOM   2134 O O      . ARG A 1 310 ? 16.37500 -6.32900  20.52600  1.000 29.04420  ? 301 ARG A O      1 
ATOM   2135 C CB     . ARG A 1 310 ? 16.80500 -9.53400  20.15700  1.000 33.71600  ? 301 ARG A CB     1 
ATOM   2136 C CG     . ARG A 1 310 ? 15.66800 -9.40900  21.16600  1.000 34.29362  ? 301 ARG A CG     1 
ATOM   2137 C CD     . ARG A 1 310 ? 14.37200 -8.98400  20.48700  1.000 39.38071  ? 301 ARG A CD     1 
ATOM   2138 N NE     . ARG A 1 310 ? 13.30600 -8.71600  21.44500  1.000 40.07167  ? 301 ARG A NE     1 
ATOM   2139 C CZ     . ARG A 1 310 ? 12.28900 -9.53200  21.68700  1.000 42.50932  ? 301 ARG A CZ     1 
ATOM   2140 N NH1    . ARG A 1 310 ? 12.15900 -10.68400 21.04800  1.000 38.22677  ? 301 ARG A NH1    1 
ATOM   2141 N NH2    . ARG A 1 310 ? 11.37600 -9.18200  22.58900  1.000 39.73211  ? 301 ARG A NH2    1 
ATOM   2142 N N      . THR A 1 311 ? 18.56800 -6.84400  20.52600  1.000 27.40488  ? 302 THR A N      1 
ATOM   2143 C CA     . THR A 1 311 ? 18.90900 -5.69200  21.35500  1.000 25.89323  ? 302 THR A CA     1 
ATOM   2144 C C      . THR A 1 311 ? 18.59300 -4.38200  20.64200  1.000 25.64208  ? 302 THR A C      1 
ATOM   2145 O O      . THR A 1 311 ? 18.03800 -3.45600  21.24600  1.000 25.98711  ? 302 THR A O      1 
ATOM   2146 C CB     . THR A 1 311 ? 20.38400 -5.74400  21.75100  1.000 28.54131  ? 302 THR A CB     1 
ATOM   2147 O OG1    . THR A 1 311 ? 20.61200 -6.87600  22.60000  1.000 31.27799  ? 302 THR A OG1    1 
ATOM   2148 C CG2    . THR A 1 311 ? 20.78200 -4.47800  22.49100  1.000 25.79751  ? 302 THR A CG2    1 
ATOM   2149 N N      . LEU A 1 312 ? 18.93700 -4.28500  19.35600  1.000 20.55594  ? 303 LEU A N      1 
ATOM   2150 C CA     . LEU A 1 312 ? 18.59800 -3.08000  18.60500  1.000 24.73393  ? 303 LEU A CA     1 
ATOM   2151 C C      . LEU A 1 312 ? 17.09200 -2.95700  18.41800  1.000 23.54417  ? 303 LEU A C      1 
ATOM   2152 O O      . LEU A 1 312 ? 16.54900 -1.84600  18.42600  1.000 23.10949  ? 303 LEU A O      1 
ATOM   2153 C CB     . LEU A 1 312 ? 19.30800 -3.08000  17.25200  1.000 25.53170  ? 303 LEU A CB     1 
ATOM   2154 C CG     . LEU A 1 312 ? 20.83600 -3.10700  17.28200  1.000 31.58861  ? 303 LEU A CG     1 
ATOM   2155 C CD1    . LEU A 1 312 ? 21.40100 -2.86500  15.88800  1.000 33.46449  ? 303 LEU A CD1    1 
ATOM   2156 C CD2    . LEU A 1 312 ? 21.37600 -2.08700  18.27200  1.000 22.28049  ? 303 LEU A CD2    1 
ATOM   2157 N N      . ARG A 1 313 ? 16.40300 -4.08900  18.25000  1.000 24.05416  ? 304 ARG A N      1 
ATOM   2158 C CA     . ARG A 1 313 ? 14.94800 -4.06600  18.12700  1.000 26.59349  ? 304 ARG A CA     1 
ATOM   2159 C C      . ARG A 1 313 ? 14.30100 -3.54100  19.40200  1.000 24.29391  ? 304 ARG A C      1 
ATOM   2160 O O      . ARG A 1 313 ? 13.36300 -2.73600  19.34500  1.000 24.65749  ? 304 ARG A O      1 
ATOM   2161 C CB     . ARG A 1 313 ? 14.43500 -5.46900  17.79400  1.000 25.17650  ? 304 ARG A CB     1 
ATOM   2162 C CG     . ARG A 1 313 ? 12.99200 -5.54800  17.29700  1.000 25.38029  ? 304 ARG A CG     1 
ATOM   2163 C CD     . ARG A 1 313 ? 11.97000 -5.59500  18.42900  1.000 28.69581  ? 304 ARG A CD     1 
ATOM   2164 N NE     . ARG A 1 313 ? 10.72500 -6.22500  18.00700  1.000 32.75834  ? 304 ARG A NE     1 
ATOM   2165 C CZ     . ARG A 1 313 ? 9.77000  -5.61800  17.31600  1.000 31.81456  ? 304 ARG A CZ     1 
ATOM   2166 N NH1    . ARG A 1 313 ? 9.87700  -4.35000  16.95600  1.000 32.54248  ? 304 ARG A NH1    1 
ATOM   2167 N NH2    . ARG A 1 313 ? 8.68300  -6.30400  16.97300  1.000 28.67174  ? 304 ARG A NH2    1 
ATOM   2168 N N      . ASN A 1 314 ? 14.78500 -3.99000  20.56400  1.000 25.37664  ? 305 ASN A N      1 
ATOM   2169 C CA     . ASN A 1 314 ? 14.21300 -3.53800  21.82800  1.000 24.36967  ? 305 ASN A CA     1 
ATOM   2170 C C      . ASN A 1 314 ? 14.43400 -2.04800  22.04500  1.000 23.93422  ? 305 ASN A C      1 
ATOM   2171 O O      . ASN A 1 314 ? 13.60000 -1.38200  22.66900  1.000 23.21869  ? 305 ASN A O      1 
ATOM   2172 C CB     . ASN A 1 314 ? 14.81100 -4.33200  22.99200  1.000 22.19810  ? 305 ASN A CB     1 
ATOM   2173 C CG     . ASN A 1 314 ? 14.35000 -5.77700  23.01500  1.000 29.41491  ? 305 ASN A CG     1 
ATOM   2174 O OD1    . ASN A 1 314 ? 13.26900 -6.10600  22.52800  1.000 29.07970  ? 305 ASN A OD1    1 
ATOM   2175 N ND2    . ASN A 1 314 ? 15.16900 -6.64900  23.59400  1.000 30.57748  ? 305 ASN A ND2    1 
ATOM   2176 N N      . ALA A 1 315 ? 15.54100 -1.50600  21.53500  1.000 24.75818  ? 306 ALA A N      1 
ATOM   2177 C CA     . ALA A 1 315 ? 15.86800 -0.10700  21.78100  1.000 23.10669  ? 306 ALA A CA     1 
ATOM   2178 C C      . ALA A 1 315 ? 15.15600 0.83600   20.82100  1.000 21.86991  ? 306 ALA A C      1 
ATOM   2179 O O      . ALA A 1 315 ? 14.94100 2.00400   21.16000  1.000 23.10717  ? 306 ALA A O      1 
ATOM   2180 C CB     . ALA A 1 315 ? 17.38100 0.10000   21.69000  1.000 17.60994  ? 306 ALA A CB     1 
ATOM   2181 N N      . TYR A 1 316 ? 14.78600 0.36300   19.63300  1.000 25.05822  ? 307 TYR A N      1 
ATOM   2182 C CA     . TYR A 1 316 ? 14.16700 1.21900   18.63000  1.000 23.17996  ? 307 TYR A CA     1 
ATOM   2183 C C      . TYR A 1 316 ? 12.65900 1.29100   18.82900  1.000 25.50589  ? 307 TYR A C      1 
ATOM   2184 O O      . TYR A 1 316 ? 11.99600 0.27300   19.05000  1.000 24.75874  ? 307 TYR A O      1 
ATOM   2185 C CB     . TYR A 1 316 ? 14.47600 0.72600   17.21600  1.000 22.20435  ? 307 TYR A CB     1 
ATOM   2186 C CG     . TYR A 1 316 ? 13.78900 1.55100   16.15200  1.000 26.00171  ? 307 TYR A CG     1 
ATOM   2187 C CD1    . TYR A 1 316 ? 14.08900 2.89800   15.99300  1.000 26.96836  ? 307 TYR A CD1    1 
ATOM   2188 C CD2    . TYR A 1 316 ? 12.83500 0.98900   15.31500  1.000 23.53576  ? 307 TYR A CD2    1 
ATOM   2189 C CE1    . TYR A 1 316 ? 13.46000 3.66200   15.02900  1.000 27.95271  ? 307 TYR A CE1    1 
ATOM   2190 C CE2    . TYR A 1 316 ? 12.20400 1.74500   14.34500  1.000 26.66154  ? 307 TYR A CE2    1 
ATOM   2191 C CZ     . TYR A 1 316 ? 12.51900 3.08100   14.20800  1.000 28.06775  ? 307 TYR A CZ     1 
ATOM   2192 O OH     . TYR A 1 316 ? 11.89000 3.83800   13.24500  1.000 31.03907  ? 307 TYR A OH     1 
ATOM   2193 N N      . GLN A 1 317 ? 12.12400 2.50800   18.73300  1.000 27.71417  ? 308 GLN A N      1 
ATOM   2194 C CA     . GLN A 1 317 ? 10.69300 2.77100   18.87600  1.000 28.70535  ? 308 GLN A CA     1 
ATOM   2195 C C      . GLN A 1 317 ? 10.08800 2.84600   17.47700  1.000 28.03404  ? 308 GLN A C      1 
ATOM   2196 O O      . GLN A 1 317 ? 10.02000 3.91300   16.86700  1.000 28.27634  ? 308 GLN A O      1 
ATOM   2197 C CB     . GLN A 1 317 ? 10.45700 4.06100   19.65400  1.000 25.95623  ? 308 GLN A CB     1 
ATOM   2198 C CG     . GLN A 1 317 ? 11.18500 4.12800   20.98400  1.000 29.43617  ? 308 GLN A CG     1 
ATOM   2199 C CD     . GLN A 1 317 ? 11.11100 5.50200   21.62200  1.000 27.65321  ? 308 GLN A CD     1 
ATOM   2200 O OE1    . GLN A 1 317 ? 10.41500 6.39100   21.13400  1.000 34.11869  ? 308 GLN A OE1    1 
ATOM   2201 N NE2    . GLN A 1 317 ? 11.83600 5.68200   22.71800  1.000 32.17913  ? 308 GLN A NE2    1 
ATOM   2202 N N      . GLY A 1 318 ? 9.64800  1.70700   16.96800  1.000 27.30253  ? 309 GLY A N      1 
ATOM   2203 C CA     . GLY A 1 318 ? 9.00300  1.66400   15.67300  1.000 26.75421  ? 309 GLY A CA     1 
ATOM   2204 C C      . GLY A 1 318 ? 9.17600  0.30400   15.02600  1.000 27.83519  ? 309 GLY A C      1 
ATOM   2205 O O      . GLY A 1 318 ? 9.51700  -0.67400  15.68400  1.000 28.68789  ? 309 GLY A O      1 
ATOM   2206 N N      . THR A 1 319 ? 8.93000  0.27900   13.71800  1.000 27.06526  ? 310 THR A N      1 
ATOM   2207 C CA     . THR A 1 319 ? 8.96900  -0.96200  12.95800  1.000 26.52593  ? 310 THR A CA     1 
ATOM   2208 C C      . THR A 1 319 ? 10.40600 -1.43500  12.76800  1.000 27.60964  ? 310 THR A C      1 
ATOM   2209 O O      . THR A 1 319 ? 11.31200 -0.63900  12.50900  1.000 26.98782  ? 310 THR A O      1 
ATOM   2210 C CB     . THR A 1 319 ? 8.28900  -0.76300  11.60200  1.000 30.55398  ? 310 THR A CB     1 
ATOM   2211 O OG1    . THR A 1 319 ? 6.92400  -0.37700  11.80900  1.000 32.92368  ? 310 THR A OG1    1 
ATOM   2212 C CG2    . THR A 1 319 ? 8.33000  -2.04200  10.77300  1.000 28.30142  ? 310 THR A CG2    1 
ATOM   2213 N N      . PHE A 1 320 ? 10.61200 -2.74400  12.90000  1.000 25.30831  ? 311 PHE A N      1 
ATOM   2214 C CA     . PHE A 1 320 ? 11.93300 -3.34600  12.80100  1.000 23.01495  ? 311 PHE A CA     1 
ATOM   2215 C C      . PHE A 1 320 ? 11.90900 -4.44100  11.74400  1.000 23.30444  ? 311 PHE A C      1 
ATOM   2216 O O      . PHE A 1 320 ? 10.99000 -5.26700  11.72400  1.000 20.23402  ? 311 PHE A O      1 
ATOM   2217 C CB     . PHE A 1 320 ? 12.36900 -3.91600  14.15300  1.000 21.53639  ? 311 PHE A CB     1 
ATOM   2218 C CG     . PHE A 1 320 ? 13.81600 -4.31500  14.21100  1.000 23.54137  ? 311 PHE A CG     1 
ATOM   2219 C CD1    . PHE A 1 320 ? 14.78700 -3.39400  14.56600  1.000 20.74485  ? 311 PHE A CD1    1 
ATOM   2220 C CD2    . PHE A 1 320 ? 14.20300 -5.61400  13.92500  1.000 23.50607  ? 311 PHE A CD2    1 
ATOM   2221 C CE1    . PHE A 1 320 ? 16.11700 -3.75800  14.62700  1.000 18.54632  ? 311 PHE A CE1    1 
ATOM   2222 C CE2    . PHE A 1 320 ? 15.53200 -5.98400  13.98400  1.000 22.20429  ? 311 PHE A CE2    1 
ATOM   2223 C CZ     . PHE A 1 320 ? 16.49000 -5.05500  14.33500  1.000 22.82826  ? 311 PHE A CZ     1 
ATOM   2224 N N      . ILE A 1 321 ? 12.91700 -4.44800  10.87400  1.000 22.95324  ? 312 ILE A N      1 
ATOM   2225 C CA     . ILE A 1 321 ? 13.06200 -5.45700  9.82900   1.000 20.26219  ? 312 ILE A CA     1 
ATOM   2226 C C      . ILE A 1 321 ? 14.36500 -6.20400  10.06900  1.000 20.23123  ? 312 ILE A C      1 
ATOM   2227 O O      . ILE A 1 321 ? 15.44600 -5.60500  10.03000  1.000 22.80531  ? 312 ILE A O      1 
ATOM   2228 C CB     . ILE A 1 321 ? 13.04600 -4.83800  8.42300   1.000 22.27115  ? 312 ILE A CB     1 
ATOM   2229 C CG1    . ILE A 1 321 ? 11.75300 -4.05500  8.19400   1.000 23.70300  ? 312 ILE A CG1    1 
ATOM   2230 C CG2    . ILE A 1 321 ? 13.21600 -5.92000  7.36300   1.000 23.84861  ? 312 ILE A CG2    1 
ATOM   2231 C CD1    . ILE A 1 321 ? 11.61100 -3.52000  6.78900   1.000 20.14694  ? 312 ILE A CD1    1 
ATOM   2232 N N      . CYS A 1 322 ? 14.26800 -7.50800  10.30800  1.000 19.69100  ? 313 CYS A N      1 
ATOM   2233 C CA     . CYS A 1 322 ? 15.44900 -8.33900  10.49100  1.000 25.40219  ? 313 CYS A CA     1 
ATOM   2234 C C      . CYS A 1 322 ? 15.89000 -8.91700  9.15300   1.000 25.70284  ? 313 CYS A C      1 
ATOM   2235 O O      . CYS A 1 322 ? 15.06700 -9.23400  8.28900   1.000 24.72498  ? 313 CYS A O      1 
ATOM   2236 C CB     . CYS A 1 322 ? 15.18300 -9.46900  11.48700  1.000 21.08428  ? 313 CYS A CB     1 
ATOM   2237 S SG     . CYS A 1 322 ? 13.91900 -10.65900 10.97200  1.000 28.17580  ? 313 CYS A SG     1 
ATOM   2238 N N      . SER A 1 323 ? 17.20400 -9.05200  8.98900   1.000 24.05868  ? 314 SER A N      1 
ATOM   2239 C CA     . SER A 1 323 ? 17.78400 -9.46600  7.72100   1.000 23.68391  ? 314 SER A CA     1 
ATOM   2240 C C      . SER A 1 323 ? 19.06300 -10.25300 7.96700   1.000 29.95045  ? 314 SER A C      1 
ATOM   2241 O O      . SER A 1 323 ? 19.83900 -9.92400  8.86900   1.000 25.39464  ? 314 SER A O      1 
ATOM   2242 C CB     . SER A 1 323 ? 18.08800 -8.25600  6.83000   1.000 22.55455  ? 314 SER A CB     1 
ATOM   2243 O OG     . SER A 1 323 ? 18.80300 -8.65000  5.67400   1.000 26.86062  ? 314 SER A OG     1 
ATOM   2244 N N      . GLY A 1 324 ? 19.27700 -11.28600 7.15500   1.000 22.11883  ? 315 GLY A N      1 
ATOM   2245 C CA     . GLY A 1 324 ? 20.51200 -12.04200 7.21100   1.000 25.56829  ? 315 GLY A CA     1 
ATOM   2246 C C      . GLY A 1 324 ? 20.32900 -13.52100 7.48100   1.000 31.78681  ? 315 GLY A C      1 
ATOM   2247 O O      . GLY A 1 324 ? 20.16700 -13.93400 8.63300   1.000 26.89844  ? 315 GLY A O      1 
ATOM   2248 N N      . GLY A 1 325 ? 20.35600 -14.32900 6.42300   1.000 33.87384  ? 316 GLY A N      1 
ATOM   2249 C CA     . GLY A 1 325 ? 20.28700 -15.77100 6.57600   1.000 31.82589  ? 316 GLY A CA     1 
ATOM   2250 C C      . GLY A 1 325 ? 18.98600 -16.29300 7.14000   1.000 34.20473  ? 316 GLY A C      1 
ATOM   2251 O O      . GLY A 1 325 ? 18.98300 -17.32600 7.81900   1.000 31.61864  ? 316 GLY A O      1 
ATOM   2252 N N      . TYR A 1 326 ? 17.87500 -15.61200 6.88100   1.000 26.86420  ? 317 TYR A N      1 
ATOM   2253 C CA     . TYR A 1 326 ? 16.58000 -16.05500 7.37000   1.000 27.26312  ? 317 TYR A CA     1 
ATOM   2254 C C      . TYR A 1 326 ? 15.94700 -17.03500 6.39300   1.000 28.13784  ? 317 TYR A C      1 
ATOM   2255 O O      . TYR A 1 326 ? 16.06500 -16.88700 5.17300   1.000 31.99257  ? 317 TYR A O      1 
ATOM   2256 C CB     . TYR A 1 326 ? 15.65200 -14.86300 7.60700   1.000 23.80723  ? 317 TYR A CB     1 
ATOM   2257 C CG     . TYR A 1 326 ? 15.96400 -14.12800 8.88900   1.000 26.56961  ? 317 TYR A CG     1 
ATOM   2258 C CD1    . TYR A 1 326 ? 16.89000 -13.09300 8.91100   1.000 25.79764  ? 317 TYR A CD1    1 
ATOM   2259 C CD2    . TYR A 1 326 ? 15.35100 -14.48500 10.08400  1.000 25.50773  ? 317 TYR A CD2    1 
ATOM   2260 C CE1    . TYR A 1 326 ? 17.18800 -12.42600 10.08200  1.000 25.98052  ? 317 TYR A CE1    1 
ATOM   2261 C CE2    . TYR A 1 326 ? 15.64200 -13.82300 11.26300  1.000 24.40524  ? 317 TYR A CE2    1 
ATOM   2262 C CZ     . TYR A 1 326 ? 16.56200 -12.79400 11.25500  1.000 29.04036  ? 317 TYR A CZ     1 
ATOM   2263 O OH     . TYR A 1 326 ? 16.86100 -12.12900 12.42200  1.000 32.58634  ? 317 TYR A OH     1 
ATOM   2264 N N      . THR A 1 327 ? 15.28900 -18.04700 6.94300   1.000 31.23407  ? 318 THR A N      1 
ATOM   2265 C CA     . THR A 1 327 ? 14.57200 -19.05700 6.17800   1.000 29.91127  ? 318 THR A CA     1 
ATOM   2266 C C      . THR A 1 327 ? 13.08300 -18.94800 6.49600   1.000 30.02413  ? 318 THR A C      1 
ATOM   2267 O O      . THR A 1 327 ? 12.63900 -18.02100 7.18000   1.000 30.03660  ? 318 THR A O      1 
ATOM   2268 C CB     . THR A 1 327 ? 15.11200 -20.45400 6.49200   1.000 31.49992  ? 318 THR A CB     1 
ATOM   2269 O OG1    . THR A 1 327 ? 14.89700 -20.74600 7.87900   1.000 34.83194  ? 318 THR A OG1    1 
ATOM   2270 C CG2    . THR A 1 327 ? 16.60200 -20.53100 6.18700   1.000 25.97315  ? 318 THR A CG2    1 
ATOM   2271 N N      . ARG A 1 328 ? 12.30700 -19.91300 5.99900   1.000 31.48220  ? 319 ARG A N      1 
ATOM   2272 C CA     . ARG A 1 328 ? 10.88300 -19.93800 6.31300   1.000 35.65450  ? 319 ARG A CA     1 
ATOM   2273 C C      . ARG A 1 328 ? 10.66000 -20.17300 7.80200   1.000 31.42442  ? 319 ARG A C      1 
ATOM   2274 O O      . ARG A 1 328 ? 9.85300  -19.48400 8.43800   1.000 32.83117  ? 319 ARG A O      1 
ATOM   2275 C CB     . ARG A 1 328 ? 10.17500 -21.01300 5.48800   1.000 32.47515  ? 319 ARG A CB     1 
ATOM   2276 C CG     . ARG A 1 328 ? 8.67600  -21.06500 5.73100   1.000 30.29111  ? 319 ARG A CG     1 
ATOM   2277 C CD     . ARG A 1 328 ? 8.02300  -22.22700 5.00600   1.000 32.58003  ? 319 ARG A CD     1 
ATOM   2278 N NE     . ARG A 1 328 ? 6.57700  -22.22600 5.19500   1.000 33.47708  ? 319 ARG A NE     1 
ATOM   2279 C CZ     . ARG A 1 328 ? 5.95400  -22.78900 6.22100   1.000 36.38577  ? 319 ARG A CZ     1 
ATOM   2280 N NH1    . ARG A 1 328 ? 6.62200  -23.42100 7.17200   1.000 30.97195  ? 319 ARG A NH1    1 
ATOM   2281 N NH2    . ARG A 1 328 ? 4.62800  -22.71600 6.29500   1.000 34.81373  ? 319 ARG A NH2    1 
ATOM   2282 N N      . GLU A 1 329 ? 11.37500 -21.14200 8.37800   1.000 34.42771  ? 320 GLU A N      1 
ATOM   2283 C CA     . GLU A 1 329 ? 11.21400 -21.43500 9.79900   1.000 30.98564  ? 320 GLU A CA     1 
ATOM   2284 C C      . GLU A 1 329 ? 11.76800 -20.31000 10.66400  1.000 32.52344  ? 320 GLU A C      1 
ATOM   2285 O O      . GLU A 1 329 ? 11.14500 -19.92000 11.65900  1.000 35.76865  ? 320 GLU A O      1 
ATOM   2286 C CB     . GLU A 1 329 ? 11.89400 -22.76100 10.14000  1.000 32.54620  ? 320 GLU A CB     1 
ATOM   2287 N N      . LEU A 1 330 ? 12.93800 -19.77600 10.30400  1.000 32.52817  ? 321 LEU A N      1 
ATOM   2288 C CA     . LEU A 1 330 ? 13.52300 -18.69100 11.08600  1.000 29.30011  ? 321 LEU A CA     1 
ATOM   2289 C C      . LEU A 1 330 ? 12.70500 -17.41300 10.96000  1.000 31.66819  ? 321 LEU A C      1 
ATOM   2290 O O      . LEU A 1 330 ? 12.58100 -16.65100 11.92600  1.000 29.99740  ? 321 LEU A O      1 
ATOM   2291 C CB     . LEU A 1 330 ? 14.96900 -18.45200 10.65200  1.000 29.21518  ? 321 LEU A CB     1 
ATOM   2292 C CG     . LEU A 1 330 ? 15.96700 -19.56300 10.98600  1.000 32.56209  ? 321 LEU A CG     1 
ATOM   2293 C CD1    . LEU A 1 330 ? 17.35300 -19.20400 10.47600  1.000 32.15228  ? 321 LEU A CD1    1 
ATOM   2294 C CD2    . LEU A 1 330 ? 15.99700 -19.82600 12.48500  1.000 31.47895  ? 321 LEU A CD2    1 
ATOM   2295 N N      . GLY A 1 331 ? 12.13800 -17.16000 9.77800   1.000 33.26127  ? 322 GLY A N      1 
ATOM   2296 C CA     . GLY A 1 331 ? 11.29300 -15.98900 9.61100   1.000 30.73176  ? 322 GLY A CA     1 
ATOM   2297 C C      . GLY A 1 331 ? 9.99600  -16.09200 10.38900  1.000 31.48131  ? 322 GLY A C      1 
ATOM   2298 O O      . GLY A 1 331 ? 9.52200  -15.10300 10.95600  1.000 37.11007  ? 322 GLY A O      1 
ATOM   2299 N N      . ILE A 1 332 ? 9.40300  -17.28700 10.42600  1.000 28.51639  ? 323 ILE A N      1 
ATOM   2300 C CA     . ILE A 1 332 ? 8.19700  -17.49900 11.22200  1.000 29.26121  ? 323 ILE A CA     1 
ATOM   2301 C C      . ILE A 1 332 ? 8.50200  -17.32300 12.70400  1.000 34.95431  ? 323 ILE A C      1 
ATOM   2302 O O      . ILE A 1 332 ? 7.73200  -16.69800 13.44400  1.000 30.44540  ? 323 ILE A O      1 
ATOM   2303 C CB     . ILE A 1 332 ? 7.60200  -18.88900 10.92700  1.000 32.11468  ? 323 ILE A CB     1 
ATOM   2304 C CG1    . ILE A 1 332 ? 6.90800  -18.89700 9.56300   1.000 36.66305  ? 323 ILE A CG1    1 
ATOM   2305 C CG2    . ILE A 1 332 ? 6.64200  -19.31600 12.03000  1.000 32.93223  ? 323 ILE A CG2    1 
ATOM   2306 C CD1    . ILE A 1 332 ? 6.38200  -20.25500 9.15300   1.000 35.10983  ? 323 ILE A CD1    1 
ATOM   2307 N N      . GLU A 1 333 ? 9.63800  -17.85900 13.15500  1.000 33.25896  ? 324 GLU A N      1 
ATOM   2308 C CA     . GLU A 1 333 ? 9.99100  -17.77500 14.56700  1.000 32.43205  ? 324 GLU A CA     1 
ATOM   2309 C C      . GLU A 1 333 ? 10.32600 -16.34700 14.98400  1.000 35.43167  ? 324 GLU A C      1 
ATOM   2310 O O      . GLU A 1 333 ? 10.08000 -15.96700 16.13400  1.000 37.15726  ? 324 GLU A O      1 
ATOM   2311 C CB     . GLU A 1 333 ? 11.16300 -18.71000 14.86300  1.000 37.75186  ? 324 GLU A CB     1 
ATOM   2312 C CG     . GLU A 1 333 ? 11.40000 -18.97000 16.34000  1.000 52.31948  ? 324 GLU A CG     1 
ATOM   2313 C CD     . GLU A 1 333 ? 12.62600 -19.82700 16.59000  1.000 60.83519  ? 324 GLU A CD     1 
ATOM   2314 O OE1    . GLU A 1 333 ? 13.13600 -20.43600 15.62600  1.000 61.44124  ? 324 GLU A OE1    1 
ATOM   2315 O OE2    . GLU A 1 333 ? 13.08100 -19.89000 17.75200  1.000 64.37957  ? 324 GLU A OE2    1 
ATOM   2316 N N      . ALA A 1 334 ? 10.87200 -15.54300 14.06700  1.000 30.27371  ? 325 ALA A N      1 
ATOM   2317 C CA     . ALA A 1 334 ? 11.24100 -14.17200 14.41000  1.000 31.98819  ? 325 ALA A CA     1 
ATOM   2318 C C      . ALA A 1 334 ? 10.01100 -13.31100 14.67700  1.000 32.00707  ? 325 ALA A C      1 
ATOM   2319 O O      . ALA A 1 334 ? 10.00800 -12.49600 15.60700  1.000 32.62595  ? 325 ALA A O      1 
ATOM   2320 C CB     . ALA A 1 334 ? 12.09100 -13.56100 13.29700  1.000 26.25928  ? 325 ALA A CB     1 
ATOM   2321 N N      . VAL A 1 335 ? 8.96000  -13.46800 13.87000  1.000 33.22536  ? 326 VAL A N      1 
ATOM   2322 C CA     . VAL A 1 335 ? 7.74900  -12.67900 14.07700  1.000 34.25005  ? 326 VAL A CA     1 
ATOM   2323 C C      . VAL A 1 335 ? 6.96600  -13.20700 15.27200  1.000 32.52425  ? 326 VAL A C      1 
ATOM   2324 O O      . VAL A 1 335 ? 6.37100  -12.43400 16.03300  1.000 29.11939  ? 326 VAL A O      1 
ATOM   2325 C CB     . VAL A 1 335 ? 6.89400  -12.66800 12.79700  1.000 32.36410  ? 326 VAL A CB     1 
ATOM   2326 C CG1    . VAL A 1 335 ? 5.58700  -11.92600 13.03400  1.000 34.48082  ? 326 VAL A CG1    1 
ATOM   2327 C CG2    . VAL A 1 335 ? 7.66600  -12.03400 11.65000  1.000 28.08991  ? 326 VAL A CG2    1 
ATOM   2328 N N      . ALA A 1 336 ? 6.96100  -14.52900 15.46100  1.000 33.42716  ? 327 ALA A N      1 
ATOM   2329 C CA     . ALA A 1 336 ? 6.21600  -15.12000 16.56700  1.000 30.87057  ? 327 ALA A CA     1 
ATOM   2330 C C      . ALA A 1 336 ? 6.82700  -14.74700 17.91300  1.000 35.12239  ? 327 ALA A C      1 
ATOM   2331 O O      . ALA A 1 336 ? 6.10100  -14.45800 18.87100  1.000 36.62965  ? 327 ALA A O      1 
ATOM   2332 C CB     . ALA A 1 336 ? 6.15800  -16.63700 16.40200  1.000 25.92303  ? 327 ALA A CB     1 
ATOM   2333 N N      . GLN A 1 337 ? 8.15600  -14.74800 18.00600  1.000 35.80156  ? 328 GLN A N      1 
ATOM   2334 C CA     . GLN A 1 337 ? 8.84000  -14.41000 19.24800  1.000 31.63177  ? 328 GLN A CA     1 
ATOM   2335 C C      . GLN A 1 337 ? 8.96800  -12.90900 19.47200  1.000 35.65120  ? 328 GLN A C      1 
ATOM   2336 O O      . GLN A 1 337 ? 9.51300  -12.50100 20.50300  1.000 35.72359  ? 328 GLN A O      1 
ATOM   2337 C CB     . GLN A 1 337 ? 10.23100 -15.05000 19.27400  1.000 32.19737  ? 328 GLN A CB     1 
ATOM   2338 C CG     . GLN A 1 337 ? 10.21600 -16.56700 19.35600  1.000 41.71293  ? 328 GLN A CG     1 
ATOM   2339 C CD     . GLN A 1 337 ? 11.61000 -17.16600 19.34200  1.000 52.35369  ? 328 GLN A CD     1 
ATOM   2340 O OE1    . GLN A 1 337 ? 12.54824 -16.57638 18.80200  1.000 48.05058  ? 328 GLN A OE1    1 
ATOM   2341 N NE2    . GLN A 1 337 ? 11.75326 -18.34250 19.94197  1.000 60.43382  ? 328 GLN A NE2    1 
ATOM   2342 N N      . GLY A 1 338 ? 8.48900  -12.08400 18.54300  1.000 36.10273  ? 329 GLY A N      1 
ATOM   2343 C CA     . GLY A 1 338 ? 8.58800  -10.64600 18.68300  1.000 32.54626  ? 329 GLY A CA     1 
ATOM   2344 C C      . GLY A 1 338 ? 9.93000  -10.05300 18.31900  1.000 35.71351  ? 329 GLY A C      1 
ATOM   2345 O O      . GLY A 1 338 ? 10.17800 -8.88500  18.64000  1.000 33.44097  ? 329 GLY A O      1 
ATOM   2346 N N      . ASP A 1 339 ? 10.80500 -10.81400 17.65800  1.000 36.05418  ? 330 ASP A N      1 
ATOM   2347 C CA     . ASP A 1 339 ? 12.12200 -10.29800 17.30000  1.000 38.35923  ? 330 ASP A CA     1 
ATOM   2348 C C      . ASP A 1 339 ? 12.06600 -9.29000  16.16000  1.000 32.88775  ? 330 ASP A C      1 
ATOM   2349 O O      . ASP A 1 339 ? 13.01200 -8.51300  15.99400  1.000 28.07609  ? 330 ASP A O      1 
ATOM   2350 C CB     . ASP A 1 339 ? 13.05800 -11.44800 16.92100  1.000 37.54704  ? 330 ASP A CB     1 
ATOM   2351 C CG     . ASP A 1 339 ? 13.33700 -12.38200 18.08400  1.000 41.61839  ? 330 ASP A CG     1 
ATOM   2352 O OD1    . ASP A 1 339 ? 13.29000 -11.92000 19.24300  1.000 42.96738  ? 330 ASP A OD1    1 
ATOM   2353 O OD2    . ASP A 1 339 ? 13.60500 -13.57700 17.83700  1.000 45.97144  ? 330 ASP A OD2    1 
ATOM   2354 N N      . ALA A 1 340 ? 10.99000 -9.28200  15.37600  1.000 26.21085  ? 331 ALA A N      1 
ATOM   2355 C CA     . ALA A 1 340 ? 10.88700 -8.37200  14.24500  1.000 27.13456  ? 331 ALA A CA     1 
ATOM   2356 C C      . ALA A 1 340 ? 9.43600  -8.27400  13.80600  1.000 28.26525  ? 331 ALA A C      1 
ATOM   2357 O O      . ALA A 1 340 ? 8.63200  -9.18100  14.03700  1.000 29.55041  ? 331 ALA A O      1 
ATOM   2358 C CB     . ALA A 1 340 ? 11.76300 -8.82700  13.07400  1.000 22.88732  ? 331 ALA A CB     1 
ATOM   2359 N N      . ASP A 1 341 ? 9.11600  -7.15500  13.15900  1.000 22.21336  ? 332 ASP A N      1 
ATOM   2360 C CA     . ASP A 1 341 ? 7.80800  -6.96800  12.54500  1.000 22.55545  ? 332 ASP A CA     1 
ATOM   2361 C C      . ASP A 1 341 ? 7.79200  -7.43900  11.09700  1.000 24.59654  ? 332 ASP A C      1 
ATOM   2362 O O      . ASP A 1 341 ? 6.78800  -7.99100  10.63400  1.000 25.54196  ? 332 ASP A O      1 
ATOM   2363 C CB     . ASP A 1 341 ? 7.40500  -5.49500  12.62100  1.000 24.34887  ? 332 ASP A CB     1 
ATOM   2364 C CG     . ASP A 1 341 ? 7.51400  -4.93900  14.02300  1.000 26.67691  ? 332 ASP A CG     1 
ATOM   2365 O OD1    . ASP A 1 341 ? 6.94600  -5.55400  14.95000  1.000 30.16184  ? 332 ASP A OD1    1 
ATOM   2366 O OD2    . ASP A 1 341 ? 8.18100  -3.89900  14.20100  1.000 32.84186  ? 332 ASP A OD2    1 
ATOM   2367 N N      . LEU A 1 342 ? 8.89000  -7.23200  10.37700  1.000 24.22350  ? 333 LEU A N      1 
ATOM   2368 C CA     . LEU A 1 342 ? 9.02500  -7.65700  8.99400   1.000 19.15710  ? 333 LEU A CA     1 
ATOM   2369 C C      . LEU A 1 342 ? 10.33400 -8.41700  8.83300   1.000 23.91889  ? 333 LEU A C      1 
ATOM   2370 O O      . LEU A 1 342 ? 11.30100 -8.17800  9.56200   1.000 24.53970  ? 333 LEU A O      1 
ATOM   2371 C CB     . LEU A 1 342 ? 8.98400  -6.45700  8.03800   1.000 21.19235  ? 333 LEU A CB     1 
ATOM   2372 C CG     . LEU A 1 342 ? 7.74500  -5.56200  8.13300   1.000 21.96592  ? 333 LEU A CG     1 
ATOM   2373 C CD1    . LEU A 1 342 ? 7.97600  -4.22900  7.43700   1.000 19.65820  ? 333 LEU A CD1    1 
ATOM   2374 C CD2    . LEU A 1 342 ? 6.53200  -6.26500  7.55200   1.000 22.90566  ? 333 LEU A CD2    1 
ATOM   2375 N N      . VAL A 1 343 ? 10.35400 -9.34500  7.87900   1.000 27.51075  ? 334 VAL A N      1 
ATOM   2376 C CA     . VAL A 1 343 ? 11.53100 -10.15800 7.59500   1.000 23.65569  ? 334 VAL A CA     1 
ATOM   2377 C C      . VAL A 1 343 ? 11.86100 -10.01200 6.11600   1.000 28.60384  ? 334 VAL A C      1 
ATOM   2378 O O      . VAL A 1 343 ? 11.01600 -10.29800 5.25800   1.000 28.04479  ? 334 VAL A O      1 
ATOM   2379 C CB     . VAL A 1 343 ? 11.31600 -11.63800 7.95600   1.000 25.91476  ? 334 VAL A CB     1 
ATOM   2380 C CG1    . VAL A 1 343 ? 12.59700 -12.42800 7.73700   1.000 25.89993  ? 334 VAL A CG1    1 
ATOM   2381 C CG2    . VAL A 1 343 ? 10.83400 -11.77400 9.39400   1.000 25.68906  ? 334 VAL A CG2    1 
ATOM   2382 N N      . SER A 1 344 ? 13.08000 -9.57300  5.81700   1.000 21.93543  ? 335 SER A N      1 
ATOM   2383 C CA     . SER A 1 344 ? 13.53200 -9.40700  4.44400   1.000 24.18025  ? 335 SER A CA     1 
ATOM   2384 C C      . SER A 1 344 ? 14.38300 -10.59900 4.02400   1.000 24.38424  ? 335 SER A C      1 
ATOM   2385 O O      . SER A 1 344 ? 15.19500 -11.10400 4.80300   1.000 30.25583  ? 335 SER A O      1 
ATOM   2386 C CB     . SER A 1 344 ? 14.32500 -8.10800  4.27300   1.000 22.28773  ? 335 SER A CB     1 
ATOM   2387 O OG     . SER A 1 344 ? 15.57100 -8.16500  4.94200   1.000 24.59452  ? 335 SER A OG     1 
ATOM   2388 N N      . TYR A 1 345 ? 14.18000 -11.05000 2.78900   1.000 25.64163  ? 336 TYR A N      1 
ATOM   2389 C CA     . TYR A 1 345 ? 14.91700 -12.16600 2.21600   1.000 24.40523  ? 336 TYR A CA     1 
ATOM   2390 C C      . TYR A 1 345 ? 15.70100 -11.68100 1.00500   1.000 25.65822  ? 336 TYR A C      1 
ATOM   2391 O O      . TYR A 1 345 ? 15.18800 -10.90700 0.19000   1.000 20.93154  ? 336 TYR A O      1 
ATOM   2392 C CB     . TYR A 1 345 ? 13.97600 -13.30900 1.81500   1.000 23.84956  ? 336 TYR A CB     1 
ATOM   2393 C CG     . TYR A 1 345 ? 13.29700 -13.98500 2.98700   1.000 27.53863  ? 336 TYR A CG     1 
ATOM   2394 C CD1    . TYR A 1 345 ? 12.15900 -13.43700 3.56500   1.000 28.94943  ? 336 TYR A CD1    1 
ATOM   2395 C CD2    . TYR A 1 345 ? 13.79200 -15.17200 3.51400   1.000 23.45941  ? 336 TYR A CD2    1 
ATOM   2396 C CE1    . TYR A 1 345 ? 11.53500 -14.05000 4.63700   1.000 25.99040  ? 336 TYR A CE1    1 
ATOM   2397 C CE2    . TYR A 1 345 ? 13.17200 -15.79400 4.58400   1.000 23.77216  ? 336 TYR A CE2    1 
ATOM   2398 C CZ     . TYR A 1 345 ? 12.04500 -15.22700 5.14200   1.000 27.59966  ? 336 TYR A CZ     1 
ATOM   2399 O OH     . TYR A 1 345 ? 11.42500 -15.84000 6.20700   1.000 23.67898  ? 336 TYR A OH     1 
ATOM   2400 N N      . GLY A 1 346 ? 16.94400 -12.13800 0.89200   1.000 27.53973  ? 337 GLY A N      1 
ATOM   2401 C CA     . GLY A 1 346 ? 17.87000 -11.70000 -0.13000  1.000 23.69723  ? 337 GLY A CA     1 
ATOM   2402 C C      . GLY A 1 346 ? 18.02000 -12.76100 -1.19900  1.000 26.47518  ? 337 GLY A C      1 
ATOM   2403 O O      . GLY A 1 346 ? 17.25200 -12.80100 -2.17900  1.000 23.69666  ? 337 GLY A O      1 
ATOM   2404 N N      . ARG A 1 347 ? 19.01200 -13.64200 -1.04400  1.000 25.24882  ? 338 ARG A N      1 
ATOM   2405 C CA     . ARG A 1 347 ? 19.38200 -14.56000 -2.11700  1.000 24.39769  ? 338 ARG A CA     1 
ATOM   2406 C C      . ARG A 1 347 ? 18.24800 -15.50800 -2.48800  1.000 23.43023  ? 338 ARG A C      1 
ATOM   2407 O O      . ARG A 1 347 ? 18.14300 -15.91600 -3.65000  1.000 25.88416  ? 338 ARG A O      1 
ATOM   2408 C CB     . ARG A 1 347 ? 20.62800 -15.34700 -1.71400  1.000 24.22825  ? 338 ARG A CB     1 
ATOM   2409 C CG     . ARG A 1 347 ? 21.89500 -14.50600 -1.67700  1.000 23.02712  ? 338 ARG A CG     1 
ATOM   2410 C CD     . ARG A 1 347 ? 22.94700 -15.13700 -0.78800  1.000 23.62026  ? 338 ARG A CD     1 
ATOM   2411 N NE     . ARG A 1 347 ? 22.55300 -15.09500 0.61500   1.000 31.90431  ? 338 ARG A NE     1 
ATOM   2412 C CZ     . ARG A 1 347 ? 23.21100 -15.69700 1.59600   1.000 35.84863  ? 338 ARG A CZ     1 
ATOM   2413 N NH1    . ARG A 1 347 ? 24.30000 -16.41000 1.36000   1.000 36.20104  ? 338 ARG A NH1    1 
ATOM   2414 N NH2    . ARG A 1 347 ? 22.76300 -15.58200 2.84300   1.000 36.27232  ? 338 ARG A NH2    1 
ATOM   2415 N N      . LEU A 1 348 ? 17.39200 -15.87200 -1.53000  1.000 26.71702  ? 339 LEU A N      1 
ATOM   2416 C CA     . LEU A 1 348 ? 16.27400 -16.75000 -1.86000  1.000 26.32181  ? 339 LEU A CA     1 
ATOM   2417 C C      . LEU A 1 348 ? 15.26100 -16.05700 -2.76000  1.000 23.42614  ? 339 LEU A C      1 
ATOM   2418 O O      . LEU A 1 348 ? 14.56900 -16.72200 -3.54000  1.000 24.15804  ? 339 LEU A O      1 
ATOM   2419 C CB     . LEU A 1 348 ? 15.59600 -17.25200 -0.58600  1.000 24.27939  ? 339 LEU A CB     1 
ATOM   2420 C CG     . LEU A 1 348 ? 16.37200 -18.30100 0.21100   1.000 28.94560  ? 339 LEU A CG     1 
ATOM   2421 C CD1    . LEU A 1 348 ? 15.60800 -18.69100 1.46500   1.000 23.47401  ? 339 LEU A CD1    1 
ATOM   2422 C CD2    . LEU A 1 348 ? 16.66000 -19.52200 -0.65000  1.000 26.42004  ? 339 LEU A CD2    1 
ATOM   2423 N N      . PHE A 1 349 ? 15.16000 -14.73000 -2.67200  1.000 21.52954  ? 340 PHE A N      1 
ATOM   2424 C CA     . PHE A 1 349 ? 14.24400 -13.99100 -3.52900  1.000 27.69218  ? 340 PHE A CA     1 
ATOM   2425 C C      . PHE A 1 349 ? 14.77800 -13.82200 -4.94600  1.000 23.95831  ? 340 PHE A C      1 
ATOM   2426 O O      . PHE A 1 349 ? 13.99200 -13.54400 -5.85900  1.000 24.02687  ? 340 PHE A O      1 
ATOM   2427 C CB     . PHE A 1 349 ? 13.93900 -12.62300 -2.91300  1.000 21.30816  ? 340 PHE A CB     1 
ATOM   2428 C CG     . PHE A 1 349 ? 12.47000 -12.31600 -2.81800  1.000 25.11669  ? 340 PHE A CG     1 
ATOM   2429 C CD1    . PHE A 1 349 ? 11.60600 -12.67100 -3.84000  1.000 25.07010  ? 340 PHE A CD1    1 
ATOM   2430 C CD2    . PHE A 1 349 ? 11.95200 -11.68200 -1.69900  1.000 25.55706  ? 340 PHE A CD2    1 
ATOM   2431 C CE1    . PHE A 1 349 ? 10.25300 -12.39300 -3.75400  1.000 24.62723  ? 340 PHE A CE1    1 
ATOM   2432 C CE2    . PHE A 1 349 ? 10.59900 -11.40100 -1.60700  1.000 28.80025  ? 340 PHE A CE2    1 
ATOM   2433 C CZ     . PHE A 1 349 ? 9.74900  -11.75800 -2.63600  1.000 25.33255  ? 340 PHE A CZ     1 
ATOM   2434 N N      . ILE A 1 350 ? 16.08800 -13.98400 -5.15000  1.000 22.24487  ? 341 ILE A N      1 
ATOM   2435 C CA     . ILE A 1 350 ? 16.64100 -13.95800 -6.50200  1.000 24.33384  ? 341 ILE A CA     1 
ATOM   2436 C C      . ILE A 1 350 ? 16.12200 -15.14000 -7.30900  1.000 26.20116  ? 341 ILE A C      1 
ATOM   2437 O O      . ILE A 1 350 ? 15.66100 -14.98500 -8.44500  1.000 28.28619  ? 341 ILE A O      1 
ATOM   2438 C CB     . ILE A 1 350 ? 18.18000 -13.94700 -6.45800  1.000 27.79885  ? 341 ILE A CB     1 
ATOM   2439 C CG1    . ILE A 1 350 ? 18.70600 -12.56900 -6.05700  1.000 27.27169  ? 341 ILE A CG1    1 
ATOM   2440 C CG2    . ILE A 1 350 ? 18.76100 -14.36900 -7.80500  1.000 22.15833  ? 341 ILE A CG2    1 
ATOM   2441 C CD1    . ILE A 1 350 ? 20.21600 -12.50300 -5.95400  1.000 27.67652  ? 341 ILE A CD1    1 
ATOM   2442 N N      . SER A 1 351 ? 16.18300 -16.33800 -6.73000  1.000 25.92299  ? 342 SER A N      1 
ATOM   2443 C CA     . SER A 1 351 ? 15.85200 -17.56400 -7.44100  1.000 27.80446  ? 342 SER A CA     1 
ATOM   2444 C C      . SER A 1 351 ? 14.39500 -17.97800 -7.28900  1.000 26.37265  ? 342 SER A C      1 
ATOM   2445 O O      . SER A 1 351 ? 13.96400 -18.92000 -7.96300  1.000 31.13496  ? 342 SER A O      1 
ATOM   2446 C CB     . SER A 1 351 ? 16.75500 -18.70500 -6.96500  1.000 30.54153  ? 342 SER A CB     1 
ATOM   2447 O OG     . SER A 1 351 ? 16.68300 -18.86100 -5.55800  1.000 24.02726  ? 342 SER A OG     1 
ATOM   2448 N N      . ASN A 1 352 ? 13.63100 -17.30700 -6.43000  1.000 26.83642  ? 343 ASN A N      1 
ATOM   2449 C CA     . ASN A 1 352 ? 12.22100 -17.62400 -6.21200  1.000 26.45286  ? 343 ASN A CA     1 
ATOM   2450 C C      . ASN A 1 352 ? 11.40800 -16.35200 -6.39800  1.000 25.91260  ? 343 ASN A C      1 
ATOM   2451 O O      . ASN A 1 352 ? 11.19400 -15.59200 -5.44400  1.000 27.27821  ? 343 ASN A O      1 
ATOM   2452 C CB     . ASN A 1 352 ? 11.99800 -18.22700 -4.82700  1.000 24.72788  ? 343 ASN A CB     1 
ATOM   2453 C CG     . ASN A 1 352 ? 12.82400 -19.47400 -4.59800  1.000 27.03069  ? 343 ASN A CG     1 
ATOM   2454 O OD1    . ASN A 1 352 ? 12.39500 -20.58300 -4.91500  1.000 27.07462  ? 343 ASN A OD1    1 
ATOM   2455 N ND2    . ASN A 1 352 ? 14.02200 -19.29900 -4.05100  1.000 22.39326  ? 343 ASN A ND2    1 
ATOM   2456 N N      . PRO A 1 353 ? 10.94200 -16.08200 -7.62100  1.000 26.31639  ? 344 PRO A N      1 
ATOM   2457 C CA     . PRO A 1 353 ? 10.11000 -14.88500 -7.82900  1.000 28.04066  ? 344 PRO A CA     1 
ATOM   2458 C C      . PRO A 1 353 ? 8.84600  -14.89500 -6.98900  1.000 28.66023  ? 344 PRO A C      1 
ATOM   2459 O O      . PRO A 1 353 ? 8.43500  -13.84700 -6.47600  1.000 26.37230  ? 344 PRO A O      1 
ATOM   2460 C CB     . PRO A 1 353 ? 9.80600  -14.93000 -9.33300  1.000 28.35938  ? 344 PRO A CB     1 
ATOM   2461 C CG     . PRO A 1 353 ? 9.99300  -16.36200 -9.72200  1.000 27.90750  ? 344 PRO A CG     1 
ATOM   2462 C CD     . PRO A 1 353 ? 11.10200 -16.87100 -8.85300  1.000 29.49645  ? 344 PRO A CD     1 
ATOM   2463 N N      . ASP A 1 354 ? 8.22700  -16.05600 -6.82500  1.000 22.78567  ? 345 ASP A N      1 
ATOM   2464 C CA     . ASP A 1 354 ? 7.05900  -16.20900 -5.95800  1.000 29.11141  ? 345 ASP A CA     1 
ATOM   2465 C C      . ASP A 1 354 ? 7.46400  -16.73100 -4.58600  1.000 25.96095  ? 345 ASP A C      1 
ATOM   2466 O O      . ASP A 1 354 ? 6.87300  -17.67000 -4.05700  1.000 26.56100  ? 345 ASP A O      1 
ATOM   2467 C CB     . ASP A 1 354 ? 6.03400  -17.12600 -6.61600  1.000 29.53191  ? 345 ASP A CB     1 
ATOM   2468 C CG     . ASP A 1 354 ? 6.64300  -18.42600 -7.10800  1.000 32.35203  ? 345 ASP A CG     1 
ATOM   2469 O OD1    . ASP A 1 354 ? 7.87000  -18.61200 -6.95900  1.000 31.63785  ? 345 ASP A OD1    1 
ATOM   2470 O OD2    . ASP A 1 354 ? 5.89000  -19.26400 -7.64700  1.000 34.65848  ? 345 ASP A OD2    1 
ATOM   2471 N N      . LEU A 1 355 ? 8.49500  -16.11500 -4.00000  1.000 29.58691  ? 346 LEU A N      1 
ATOM   2472 C CA     . LEU A 1 355 ? 8.99100  -16.56400 -2.70200  1.000 25.22490  ? 346 LEU A CA     1 
ATOM   2473 C C      . LEU A 1 355 ? 7.92600  -16.42100 -1.62400  1.000 25.30238  ? 346 LEU A C      1 
ATOM   2474 O O      . LEU A 1 355 ? 7.80600  -17.28100 -0.74400  1.000 26.52547  ? 346 LEU A O      1 
ATOM   2475 C CB     . LEU A 1 355 ? 10.24900 -15.78300 -2.32000  1.000 23.58023  ? 346 LEU A CB     1 
ATOM   2476 C CG     . LEU A 1 355 ? 10.85600 -16.09300 -0.95000  1.000 24.91872  ? 346 LEU A CG     1 
ATOM   2477 C CD1    . LEU A 1 355 ? 11.26800 -17.55400 -0.85500  1.000 23.99517  ? 346 LEU A CD1    1 
ATOM   2478 C CD2    . LEU A 1 355 ? 12.03900 -15.17900 -0.67000  1.000 21.43508  ? 346 LEU A CD2    1 
ATOM   2479 N N      . VAL A 1 356 ? 7.14000  -15.34100 -1.67800  1.000 28.54533  ? 347 VAL A N      1 
ATOM   2480 C CA     . VAL A 1 356 ? 6.07500  -15.14500 -0.69800  1.000 30.11528  ? 347 VAL A CA     1 
ATOM   2481 C C      . VAL A 1 356 ? 5.09600  -16.31000 -0.74000  1.000 28.68885  ? 347 VAL A C      1 
ATOM   2482 O O      . VAL A 1 356 ? 4.68800  -16.83900 0.30200   1.000 28.37544  ? 347 VAL A O      1 
ATOM   2483 C CB     . VAL A 1 356 ? 5.36300  -13.80100 -0.94300  1.000 29.66445  ? 347 VAL A CB     1 
ATOM   2484 C CG1    . VAL A 1 356 ? 4.27300  -13.58100 0.09600   1.000 27.27513  ? 347 VAL A CG1    1 
ATOM   2485 C CG2    . VAL A 1 356 ? 6.36500  -12.65600 -0.92700  1.000 27.08622  ? 347 VAL A CG2    1 
ATOM   2486 N N      . MET A 1 357 ? 4.71800  -16.73900 -1.94500  1.000 33.60315  ? 348 MET A N      1 
ATOM   2487 C CA     . MET A 1 357 ? 3.76900  -17.83800 -2.08100  1.000 32.95003  ? 348 MET A CA     1 
ATOM   2488 C C      . MET A 1 357 ? 4.38000  -19.16200 -1.63200  1.000 32.95823  ? 348 MET A C      1 
ATOM   2489 O O      . MET A 1 357 ? 3.70000  -19.98200 -1.00400  1.000 31.40005  ? 348 MET A O      1 
ATOM   2490 C CB     . MET A 1 357 ? 3.28200  -17.92600 -3.52600  1.000 30.57577  ? 348 MET A CB     1 
ATOM   2491 C CG     . MET A 1 357 ? 2.35288  -19.09592 -3.80254  1.000 39.53486  ? 348 MET A CG     1 
ATOM   2492 S SD     . MET A 1 357 ? 0.88705  -19.09466 -2.74983  1.000 68.99081  ? 348 MET A SD     1 
ATOM   2493 C CE     . MET A 1 357 ? 0.40442  -17.37063 -2.83401  1.000 43.11154  ? 348 MET A CE     1 
ATOM   2494 N N      . ARG A 1 358 ? 5.66000  -19.38800 -1.93900  1.000 28.66382  ? 349 ARG A N      1 
ATOM   2495 C CA     . ARG A 1 358 ? 6.29900  -20.63300 -1.52500  1.000 27.01347  ? 349 ARG A CA     1 
ATOM   2496 C C      . ARG A 1 358 ? 6.43800  -20.71700 -0.01000  1.000 29.36068  ? 349 ARG A C      1 
ATOM   2497 O O      . ARG A 1 358 ? 6.34600  -21.81100 0.55900   1.000 32.16578  ? 349 ARG A O      1 
ATOM   2498 C CB     . ARG A 1 358 ? 7.66500  -20.77600 -2.19600  1.000 33.36854  ? 349 ARG A CB     1 
ATOM   2499 C CG     . ARG A 1 358 ? 7.61000  -20.74300 -3.71300  1.000 26.24628  ? 349 ARG A CG     1 
ATOM   2500 C CD     . ARG A 1 358 ? 8.87200  -21.31600 -4.32300  1.000 27.65954  ? 349 ARG A CD     1 
ATOM   2501 N NE     . ARG A 1 358 ? 8.85000  -21.24000 -5.77800  1.000 29.08074  ? 349 ARG A NE     1 
ATOM   2502 C CZ     . ARG A 1 358 ? 9.62200  -21.96300 -6.57700  1.000 32.04847  ? 349 ARG A CZ     1 
ATOM   2503 N NH1    . ARG A 1 358 ? 10.47800 -22.84800 -6.09400  1.000 27.80836  ? 349 ARG A NH1    1 
ATOM   2504 N NH2    . ARG A 1 358 ? 9.52800  -21.79900 -7.89300  1.000 35.86695  ? 349 ARG A NH2    1 
ATOM   2505 N N      . ILE A 1 359 ? 6.65000  -19.58200 0.65800   1.000 28.09900  ? 350 ILE A N      1 
ATOM   2506 C CA     . ILE A 1 359 ? 6.70300  -19.58100 2.11700   1.000 31.26161  ? 350 ILE A CA     1 
ATOM   2507 C C      . ILE A 1 359 ? 5.33600  -19.92200 2.70000   1.000 34.95774  ? 350 ILE A C      1 
ATOM   2508 O O      . ILE A 1 359 ? 5.23500  -20.63600 3.70500   1.000 33.08782  ? 350 ILE A O      1 
ATOM   2509 C CB     . ILE A 1 359 ? 7.22300  -18.22400 2.62900   1.000 30.63113  ? 350 ILE A CB     1 
ATOM   2510 C CG1    . ILE A 1 359 ? 8.70500  -18.06000 2.28500   1.000 23.77610  ? 350 ILE A CG1    1 
ATOM   2511 C CG2    . ILE A 1 359 ? 7.00400  -18.08500 4.13200   1.000 27.57713  ? 350 ILE A CG2    1 
ATOM   2512 C CD1    . ILE A 1 359 ? 9.29600  -16.75000 2.75100   1.000 23.13840  ? 350 ILE A CD1    1 
ATOM   2513 N N      . LYS A 1 360 ? 4.26400  -19.43500 2.07100   1.000 31.48580  ? 351 LYS A N      1 
ATOM   2514 C CA     . LYS A 1 360 ? 2.92100  -19.71600 2.56700   1.000 36.02245  ? 351 LYS A CA     1 
ATOM   2515 C C      . LYS A 1 360 ? 2.59200  -21.19900 2.45600   1.000 34.56357  ? 351 LYS A C      1 
ATOM   2516 O O      . LYS A 1 360 ? 2.09100  -21.80800 3.40800   1.000 37.39908  ? 351 LYS A O      1 
ATOM   2517 C CB     . LYS A 1 360 ? 1.89300  -18.88100 1.80300   1.000 35.10107  ? 351 LYS A CB     1 
ATOM   2518 C CG     . LYS A 1 360 ? 0.49600  -18.92200 2.40000   1.000 36.51723  ? 351 LYS A CG     1 
ATOM   2519 C CD     . LYS A 1 360 ? -0.48300 -18.10700 1.57200   1.000 41.97261  ? 351 LYS A CD     1 
ATOM   2520 C CE     . LYS A 1 360 ? -1.87000 -18.11300 2.19500   1.000 46.58328  ? 351 LYS A CE     1 
ATOM   2521 N NZ     . LYS A 1 360 ? -1.86800 -17.50300 3.55300   1.000 42.74534  ? 351 LYS A NZ     1 
ATOM   2522 N N      . LEU A 1 361 ? 2.86800  -21.79800 1.29700   1.000 31.03277  ? 352 LEU A N      1 
ATOM   2523 C CA     . LEU A 1 361 ? 2.56300  -23.20400 1.06700   1.000 33.72406  ? 352 LEU A CA     1 
ATOM   2524 C C      . LEU A 1 361 ? 3.62400  -24.14300 1.62300   1.000 32.35460  ? 352 LEU A C      1 
ATOM   2525 O O      . LEU A 1 361 ? 3.43000  -25.36200 1.56900   1.000 36.55019  ? 352 LEU A O      1 
ATOM   2526 C CB     . LEU A 1 361 ? 2.40000  -23.46800 -0.43200  1.000 36.21225  ? 352 LEU A CB     1 
ATOM   2527 C CG     . LEU A 1 361 ? 1.51314  -22.50404 -1.22179  1.000 36.90503  ? 352 LEU A CG     1 
ATOM   2528 C CD1    . LEU A 1 361 ? 1.47662  -22.89460 -2.69415  1.000 43.71486  ? 352 LEU A CD1    1 
ATOM   2529 C CD2    . LEU A 1 361 ? 0.11233  -22.45971 -0.63748  1.000 29.29302  ? 352 LEU A CD2    1 
ATOM   2530 N N      . ASN A 1 362 ? 4.72600  -23.60900 2.15300   1.000 31.47548  ? 353 ASN A N      1 
ATOM   2531 C CA     . ASN A 1 362 ? 5.88300  -24.41600 2.54100   1.000 31.68365  ? 353 ASN A CA     1 
ATOM   2532 C C      . ASN A 1 362 ? 6.36400  -25.25800 1.36200   1.000 31.72253  ? 353 ASN A C      1 
ATOM   2533 O O      . ASN A 1 362 ? 6.69600  -26.43800 1.49900   1.000 36.28697  ? 353 ASN A O      1 
ATOM   2534 C CB     . ASN A 1 362 ? 5.57200  -25.29000 3.75900   1.000 29.47002  ? 353 ASN A CB     1 
ATOM   2535 C CG     . ASN A 1 362 ? 6.81700  -25.89300 4.37300   1.000 33.76531  ? 353 ASN A CG     1 
ATOM   2536 O OD1    . ASN A 1 362 ? 7.93400  -25.45200 4.09700   1.000 33.20630  ? 353 ASN A OD1    1 
ATOM   2537 N ND2    . ASN A 1 362 ? 6.63400  -26.90700 5.21000   1.000 33.63538  ? 353 ASN A ND2    1 
ATOM   2538 N N      . ALA A 1 363 ? 6.38800  -24.64100 0.18400   1.000 30.41539  ? 354 ALA A N      1 
ATOM   2539 C CA     . ALA A 1 363 ? 6.82900  -25.29900 -1.03100  1.000 26.32743  ? 354 ALA A CA     1 
ATOM   2540 C C      . ALA A 1 363 ? 8.35100  -25.22800 -1.14900  1.000 30.98321  ? 354 ALA A C      1 
ATOM   2541 O O      . ALA A 1 363 ? 8.97400  -24.28700 -0.65200  1.000 30.88691  ? 354 ALA A O      1 
ATOM   2542 C CB     . ALA A 1 363 ? 6.18200  -24.64800 -2.24900  1.000 27.26047  ? 354 ALA A CB     1 
ATOM   2543 N N      . PRO A 1 364 ? 8.97200  -26.21800 -1.79200  1.000 33.65611  ? 355 PRO A N      1 
ATOM   2544 C CA     . PRO A 1 364 ? 10.43500 -26.20900 -1.90900  1.000 30.26628  ? 355 PRO A CA     1 
ATOM   2545 C C      . PRO A 1 364 ? 10.92400 -25.03500 -2.74600  1.000 28.50180  ? 355 PRO A C      1 
ATOM   2546 O O      . PRO A 1 364 ? 10.23500 -24.55300 -3.64700  1.000 29.63094  ? 355 PRO A O      1 
ATOM   2547 C CB     . PRO A 1 364 ? 10.74600 -27.55100 -2.58300  1.000 35.72681  ? 355 PRO A CB     1 
ATOM   2548 C CG     . PRO A 1 364 ? 9.47800  -27.93600 -3.27400  1.000 33.19137  ? 355 PRO A CG     1 
ATOM   2549 C CD     . PRO A 1 364 ? 8.37300  -27.41300 -2.41200  1.000 32.27455  ? 355 PRO A CD     1 
ATOM   2550 N N      . LEU A 1 365 ? 12.13000 -24.57300 -2.43200  1.000 29.62448  ? 356 LEU A N      1 
ATOM   2551 C CA     . LEU A 1 365 ? 12.68800 -23.37300 -3.03600  1.000 27.88650  ? 356 LEU A CA     1 
ATOM   2552 C C      . LEU A 1 365 ? 13.72600 -23.72600 -4.09700  1.000 30.08151  ? 356 LEU A C      1 
ATOM   2553 O O      . LEU A 1 365 ? 14.31900 -24.80800 -4.08900  1.000 30.21806  ? 356 LEU A O      1 
ATOM   2554 C CB     . LEU A 1 365 ? 13.31900 -22.47900 -1.96500  1.000 28.80279  ? 356 LEU A CB     1 
ATOM   2555 C CG     . LEU A 1 365 ? 12.46600 -22.19600 -0.72500  1.000 28.01850  ? 356 LEU A CG     1 
ATOM   2556 C CD1    . LEU A 1 365 ? 13.24600 -21.37400 0.29300   1.000 25.74550  ? 356 LEU A CD1    1 
ATOM   2557 C CD2    . LEU A 1 365 ? 11.17300 -21.49200 -1.10500  1.000 25.82064  ? 356 LEU A CD2    1 
ATOM   2558 N N      . ASN A 1 366 ? 13.94000 -22.78900 -5.01700  1.000 26.28135  ? 357 ASN A N      1 
ATOM   2559 C CA     . ASN A 1 366 ? 14.93400 -22.95000 -6.06700  1.000 27.58833  ? 357 ASN A CA     1 
ATOM   2560 C C      . ASN A 1 366 ? 16.30300 -22.48900 -5.58300  1.000 27.20874  ? 357 ASN A C      1 
ATOM   2561 O O      . ASN A 1 366 ? 16.41900 -21.58800 -4.74900  1.000 27.33989  ? 357 ASN A O      1 
ATOM   2562 C CB     . ASN A 1 366 ? 14.54900 -22.15900 -7.31900  1.000 26.40154  ? 357 ASN A CB     1 
ATOM   2563 C CG     . ASN A 1 366 ? 13.20600 -22.57000 -7.88400  1.000 29.30366  ? 357 ASN A CG     1 
ATOM   2564 O OD1    . ASN A 1 366 ? 12.78300 -23.71800 -7.75200  1.000 31.69151  ? 357 ASN A OD1    1 
ATOM   2565 N ND2    . ASN A 1 366 ? 12.52700 -21.62700 -8.52600  1.000 29.84442  ? 357 ASN A ND2    1 
ATOM   2566 N N      . LYS A 1 367 ? 17.34300 -23.11500 -6.12500  1.000 27.59356  ? 358 LYS A N      1 
ATOM   2567 C CA     . LYS A 1 367 ? 18.70400 -22.67300 -5.86600  1.000 29.72411  ? 358 LYS A CA     1 
ATOM   2568 C C      . LYS A 1 367 ? 19.02100 -21.43300 -6.69200  1.000 27.77468  ? 358 LYS A C      1 
ATOM   2569 O O      . LYS A 1 367 ? 18.49200 -21.23800 -7.79000  1.000 28.92724  ? 358 LYS A O      1 
ATOM   2570 C CB     . LYS A 1 367 ? 19.70700 -23.78200 -6.19100  1.000 29.91933  ? 358 LYS A CB     1 
ATOM   2571 C CG     . LYS A 1 367 ? 19.72600 -24.18500 -7.65600  1.000 33.27265  ? 358 LYS A CG     1 
ATOM   2572 C CD     . LYS A 1 367 ? 20.90400 -25.09000 -7.98000  1.000 40.36796  ? 358 LYS A CD     1 
ATOM   2573 C CE     . LYS A 1 367 ? 20.95700 -25.39800 -9.47100  1.000 40.08160  ? 358 LYS A CE     1 
ATOM   2574 N NZ     . LYS A 1 367 ? 22.15100 -26.21100 -9.84200  1.000 44.34020  ? 358 LYS A NZ     1 
ATOM   2575 N N      . TYR A 1 368 ? 19.89000 -20.58700 -6.15000  1.000 31.49361  ? 359 TYR A N      1 
ATOM   2576 C CA     . TYR A 1 368 ? 20.33700 -19.38700 -6.84100  1.000 27.87016  ? 359 TYR A CA     1 
ATOM   2577 C C      . TYR A 1 368 ? 21.74300 -19.58800 -7.39000  1.000 31.11563  ? 359 TYR A C      1 
ATOM   2578 O O      . TYR A 1 368 ? 22.54000 -20.35800 -6.84700  1.000 28.19627  ? 359 TYR A O      1 
ATOM   2579 C CB     . TYR A 1 368 ? 20.30100 -18.17000 -5.91300  1.000 28.16703  ? 359 TYR A CB     1 
ATOM   2580 C CG     . TYR A 1 368 ? 20.88500 -18.41200 -4.53800  1.000 32.37802  ? 359 TYR A CG     1 
ATOM   2581 C CD1    . TYR A 1 368 ? 22.25500 -18.33400 -4.31800  1.000 29.17904  ? 359 TYR A CD1    1 
ATOM   2582 C CD2    . TYR A 1 368 ? 20.06300 -18.70800 -3.45800  1.000 33.51455  ? 359 TYR A CD2    1 
ATOM   2583 C CE1    . TYR A 1 368 ? 22.78900 -18.55200 -3.06200  1.000 29.12224  ? 359 TYR A CE1    1 
ATOM   2584 C CE2    . TYR A 1 368 ? 20.58900 -18.92700 -2.19900  1.000 28.17926  ? 359 TYR A CE2    1 
ATOM   2585 C CZ     . TYR A 1 368 ? 21.95200 -18.84700 -2.00700  1.000 29.26502  ? 359 TYR A CZ     1 
ATOM   2586 O OH     . TYR A 1 368 ? 22.47900 -19.06500 -0.75500  1.000 35.36626  ? 359 TYR A OH     1 
ATOM   2587 N N      . ASN A 1 369 ? 22.04000 -18.88300 -8.48100  1.000 33.76553  ? 360 ASN A N      1 
ATOM   2588 C CA     . ASN A 1 369 ? 23.31100 -19.00000 -9.18800  1.000 32.34443  ? 360 ASN A CA     1 
ATOM   2589 C C      . ASN A 1 369 ? 24.11500 -17.72600 -8.96200  1.000 31.69349  ? 360 ASN A C      1 
ATOM   2590 O O      . ASN A 1 369 ? 23.79800 -16.67500 -9.53000  1.000 32.45826  ? 360 ASN A O      1 
ATOM   2591 C CB     . ASN A 1 369 ? 23.07900 -19.25100 -10.67600 1.000 31.39150  ? 360 ASN A CB     1 
ATOM   2592 C CG     . ASN A 1 369 ? 22.28430 -20.51554 -10.93237 1.000 39.56385  ? 360 ASN A CG     1 
ATOM   2593 O OD1    . ASN A 1 369 ? 22.67815 -21.60628 -10.51645 1.000 46.55871  ? 360 ASN A OD1    1 
ATOM   2594 N ND2    . ASN A 1 369 ? 21.14850 -20.37449 -11.60862 1.000 40.43570  ? 360 ASN A ND2    1 
ATOM   2595 N N      . ARG A 1 370 ? 25.16200 -17.82800 -8.13900  1.000 26.86758  ? 361 ARG A N      1 
ATOM   2596 C CA     . ARG A 1 370 ? 25.99300 -16.66900 -7.83200  1.000 26.99227  ? 361 ARG A CA     1 
ATOM   2597 C C      . ARG A 1 370 ? 26.66100 -16.10100 -9.07900  1.000 28.70269  ? 361 ARG A C      1 
ATOM   2598 O O      . ARG A 1 370 ? 26.92400 -14.89400 -9.14500  1.000 28.99204  ? 361 ARG A O      1 
ATOM   2599 C CB     . ARG A 1 370 ? 27.04500 -17.05100 -6.78800  1.000 34.32974  ? 361 ARG A CB     1 
ATOM   2600 C CG     . ARG A 1 370 ? 28.04200 -15.95100 -6.44800  1.000 30.78072  ? 361 ARG A CG     1 
ATOM   2601 C CD     . ARG A 1 370 ? 28.82500 -16.29000 -5.18900  1.000 42.70819  ? 361 ARG A CD     1 
ATOM   2602 N NE     . ARG A 1 370 ? 27.94800 -16.44800 -4.03400  1.000 41.79945  ? 361 ARG A NE     1 
ATOM   2603 C CZ     . ARG A 1 370 ? 27.59400 -15.46100 -3.22200  1.000 46.54020  ? 361 ARG A CZ     1 
ATOM   2604 N NH1    . ARG A 1 370 ? 28.02900 -14.22500 -3.40500  1.000 45.74942  ? 361 ARG A NH1    1 
ATOM   2605 N NH2    . ARG A 1 370 ? 26.78100 -15.72000 -2.20100  1.000 33.58213  ? 361 ARG A NH2    1 
ATOM   2606 N N      . LYS A 1 371 ? 26.92500 -16.94500 -10.08100 1.000 25.97784  ? 362 LYS A N      1 
ATOM   2607 C CA     . LYS A 1 371 ? 27.64400 -16.49200 -11.26800 1.000 32.73887  ? 362 LYS A CA     1 
ATOM   2608 C C      . LYS A 1 371 ? 26.90700 -15.37100 -11.99100 1.000 27.03587  ? 362 LYS A C      1 
ATOM   2609 O O      . LYS A 1 371 ? 27.54200 -14.53300 -12.64300 1.000 28.56743  ? 362 LYS A O      1 
ATOM   2610 C CB     . LYS A 1 371 ? 27.88400 -17.66700 -12.21800 1.000 21.28510  ? 362 LYS A CB     1 
ATOM   2611 N N      . THR A 1 372 ? 25.57800 -15.32700 -11.88400 1.000 24.76797  ? 363 THR A N      1 
ATOM   2612 C CA     . THR A 1 372 ? 24.77600 -14.31800 -12.56400 1.000 24.58281  ? 363 THR A CA     1 
ATOM   2613 C C      . THR A 1 372 ? 24.17900 -13.29500 -11.60200 1.000 27.94536  ? 363 THR A C      1 
ATOM   2614 O O      . THR A 1 372 ? 23.15500 -12.68000 -11.91700 1.000 23.41456  ? 363 THR A O      1 
ATOM   2615 C CB     . THR A 1 372 ? 23.67000 -14.98200 -13.38500 1.000 27.33415  ? 363 THR A CB     1 
ATOM   2616 O OG1    . THR A 1 372 ? 22.94800 -15.90600 -12.56200 1.000 29.94862  ? 363 THR A OG1    1 
ATOM   2617 C CG2    . THR A 1 372 ? 24.26300 -15.72300 -14.57900 1.000 26.73814  ? 363 THR A CG2    1 
ATOM   2618 N N      . PHE A 1 373 ? 24.79800 -13.09700 -10.43500 1.000 27.02987  ? 364 PHE A N      1 
ATOM   2619 C CA     . PHE A 1 373 ? 24.32300 -12.06400 -9.51900  1.000 23.75258  ? 364 PHE A CA     1 
ATOM   2620 C C      . PHE A 1 373 ? 24.51800 -10.67200 -10.10700 1.000 26.57440  ? 364 PHE A C      1 
ATOM   2621 O O      . PHE A 1 373 ? 23.61300 -9.83100  -10.03600 1.000 25.43980  ? 364 PHE A O      1 
ATOM   2622 C CB     . PHE A 1 373 ? 25.04100 -12.16800 -8.17300  1.000 25.50364  ? 364 PHE A CB     1 
ATOM   2623 C CG     . PHE A 1 373 ? 24.48000 -13.21900 -7.25700  1.000 26.23300  ? 364 PHE A CG     1 
ATOM   2624 C CD1    . PHE A 1 373 ? 23.39800 -13.99100 -7.64200  1.000 26.57259  ? 364 PHE A CD1    1 
ATOM   2625 C CD2    . PHE A 1 373 ? 25.03100 -13.42400 -6.00100  1.000 27.58607  ? 364 PHE A CD2    1 
ATOM   2626 C CE1    . PHE A 1 373 ? 22.88100 -14.95500 -6.79700  1.000 26.32909  ? 364 PHE A CE1    1 
ATOM   2627 C CE2    . PHE A 1 373 ? 24.51800 -14.38500 -5.14900  1.000 24.96305  ? 364 PHE A CE2    1 
ATOM   2628 C CZ     . PHE A 1 373 ? 23.44200 -15.15200 -5.54800  1.000 31.16328  ? 364 PHE A CZ     1 
ATOM   2629 N N      . TYR A 1 374 ? 25.69000 -10.41100 -10.69200 1.000 23.64885  ? 365 TYR A N      1 
ATOM   2630 C CA     . TYR A 1 374 ? 26.05500 -9.07800  -11.15900 1.000 21.89779  ? 365 TYR A CA     1 
ATOM   2631 C C      . TYR A 1 374 ? 26.31200 -9.03300  -12.66200 1.000 26.69089  ? 365 TYR A C      1 
ATOM   2632 O O      . TYR A 1 374 ? 27.00700 -8.13000  -13.13800 1.000 26.24263  ? 365 TYR A O      1 
ATOM   2633 C CB     . TYR A 1 374 ? 27.28500 -8.57000  -10.40400 1.000 25.34957  ? 365 TYR A CB     1 
ATOM   2634 C CG     . TYR A 1 374 ? 27.17300 -8.67500  -8.90100  1.000 27.25435  ? 365 TYR A CG     1 
ATOM   2635 C CD1    . TYR A 1 374 ? 26.26500 -7.89500  -8.19700  1.000 22.80524  ? 365 TYR A CD1    1 
ATOM   2636 C CD2    . TYR A 1 374 ? 27.98300 -9.54800  -8.18500  1.000 29.11325  ? 365 TYR A CD2    1 
ATOM   2637 C CE1    . TYR A 1 374 ? 26.16200 -7.98600  -6.82300  1.000 27.99599  ? 365 TYR A CE1    1 
ATOM   2638 C CE2    . TYR A 1 374 ? 27.88800 -9.64500  -6.80800  1.000 27.63975  ? 365 TYR A CE2    1 
ATOM   2639 C CZ     . TYR A 1 374 ? 26.97600 -8.86000  -6.13300  1.000 29.50762  ? 365 TYR A CZ     1 
ATOM   2640 O OH     . TYR A 1 374 ? 26.87500 -8.95100  -4.76500  1.000 27.75176  ? 365 TYR A OH     1 
ATOM   2641 N N      . THR A 1 375 ? 25.77700 -9.98500  -13.41900 1.000 25.31294  ? 366 THR A N      1 
ATOM   2642 C CA     . THR A 1 375 ? 25.90400 -9.93900  -14.86600 1.000 25.34267  ? 366 THR A CA     1 
ATOM   2643 C C      . THR A 1 375 ? 24.86200 -8.98800  -15.45700 1.000 30.58545  ? 366 THR A C      1 
ATOM   2644 O O      . THR A 1 375 ? 23.99100 -8.46500  -14.75800 1.000 24.54391  ? 366 THR A O      1 
ATOM   2645 C CB     . THR A 1 375 ? 25.77100 -11.33800 -15.46300 1.000 26.23261  ? 366 THR A CB     1 
ATOM   2646 O OG1    . THR A 1 375 ? 24.63100 -11.99600 -14.89500 1.000 29.08643  ? 366 THR A OG1    1 
ATOM   2647 C CG2    . THR A 1 375 ? 27.02200 -12.15700 -15.17500 1.000 28.68345  ? 366 THR A CG2    1 
ATOM   2648 N N      . GLN A 1 376 ? 24.96000 -8.75800  -16.76700 1.000 24.89916  ? 367 GLN A N      1 
ATOM   2649 C CA     . GLN A 1 376 ? 24.16600 -7.72300  -17.41800 1.000 29.00489  ? 367 GLN A CA     1 
ATOM   2650 C C      . GLN A 1 376 ? 23.00800 -8.25100  -18.25100 1.000 25.68513  ? 367 GLN A C      1 
ATOM   2651 O O      . GLN A 1 376 ? 22.21700 -7.44300  -18.74800 1.000 27.47061  ? 367 GLN A O      1 
ATOM   2652 C CB     . GLN A 1 376 ? 25.05900 -6.84400  -18.30900 1.000 28.63960  ? 367 GLN A CB     1 
ATOM   2653 C CG     . GLN A 1 376 ? 25.82200 -5.76700  -17.55600 1.000 21.97549  ? 367 GLN A CG     1 
ATOM   2654 C CD     . GLN A 1 376 ? 26.71400 -6.33900  -16.47600 1.000 28.72454  ? 367 GLN A CD     1 
ATOM   2655 O OE1    . GLN A 1 376 ? 27.60700 -7.14100  -16.75300 1.000 27.96113  ? 367 GLN A OE1    1 
ATOM   2656 N NE2    . GLN A 1 376 ? 26.46600 -5.94400  -15.23300 1.000 25.82902  ? 367 GLN A NE2    1 
ATOM   2657 N N      . ASP A 1 377 ? 22.88100 -9.56100  -18.41700 1.000 22.78599  ? 368 ASP A N      1 
ATOM   2658 C CA     . ASP A 1 377 ? 21.83600 -10.09300 -19.28400 1.000 30.29586  ? 368 ASP A CA     1 
ATOM   2659 C C      . ASP A 1 377 ? 20.46500 -9.78400  -18.69200 1.000 28.26679  ? 368 ASP A C      1 
ATOM   2660 O O      . ASP A 1 377 ? 20.23600 -10.03700 -17.50300 1.000 28.95529  ? 368 ASP A O      1 
ATOM   2661 C CB     . ASP A 1 377 ? 22.01100 -11.59900 -19.47700 1.000 30.55982  ? 368 ASP A CB     1 
ATOM   2662 C CG     . ASP A 1 377 ? 21.18200 -12.14200 -20.63000 1.000 30.27510  ? 368 ASP A CG     1 
ATOM   2663 O OD1    . ASP A 1 377 ? 19.93600 -12.07100 -20.56400 1.000 28.12705  ? 368 ASP A OD1    1 
ATOM   2664 O OD2    . ASP A 1 377 ? 21.78000 -12.63100 -21.61200 1.000 34.82762  ? 368 ASP A OD2    1 
ATOM   2665 N N      . PRO A 1 378 ? 19.53400 -9.23200  -19.47700 1.000 29.87051  ? 369 PRO A N      1 
ATOM   2666 C CA     . PRO A 1 378 ? 18.21800 -8.87800  -18.92300 1.000 28.76310  ? 369 PRO A CA     1 
ATOM   2667 C C      . PRO A 1 378 ? 17.33300 -10.07400 -18.61100 1.000 27.39493  ? 369 PRO A C      1 
ATOM   2668 O O      . PRO A 1 378 ? 16.25300 -9.87900  -18.03900 1.000 29.63842  ? 369 PRO A O      1 
ATOM   2669 C CB     . PRO A 1 378 ? 17.60000 -8.00800  -20.02400 1.000 28.02109  ? 369 PRO A CB     1 
ATOM   2670 C CG     . PRO A 1 378 ? 18.26000 -8.47300  -21.27900 1.000 30.88103  ? 369 PRO A CG     1 
ATOM   2671 C CD     . PRO A 1 378 ? 19.66900 -8.83400  -20.88900 1.000 26.93614  ? 369 PRO A CD     1 
ATOM   2672 N N      . VAL A 1 379 ? 17.74200 -11.29200 -18.96200 1.000 26.91520  ? 370 VAL A N      1 
ATOM   2673 C CA     . VAL A 1 379 ? 16.91800 -12.47000 -18.71600 1.000 27.42212  ? 370 VAL A CA     1 
ATOM   2674 C C      . VAL A 1 379 ? 17.71200 -13.51900 -17.94700 1.000 29.19004  ? 370 VAL A C      1 
ATOM   2675 O O      . VAL A 1 379 ? 17.27200 -13.99700 -16.89500 1.000 27.51422  ? 370 VAL A O      1 
ATOM   2676 C CB     . VAL A 1 379 ? 16.37300 -13.05300 -20.03300 1.000 26.81670  ? 370 VAL A CB     1 
ATOM   2677 C CG1    . VAL A 1 379 ? 15.67600 -14.37800 -19.78000 1.000 22.04908  ? 370 VAL A CG1    1 
ATOM   2678 C CG2    . VAL A 1 379 ? 15.42200 -12.06700 -20.69900 1.000 26.97266  ? 370 VAL A CG2    1 
ATOM   2679 N N      . VAL A 1 380 ? 18.88800 -13.87800 -18.46700 1.000 27.81084  ? 371 VAL A N      1 
ATOM   2680 C CA     . VAL A 1 380 ? 19.67000 -14.97300 -17.90000 1.000 29.55755  ? 371 VAL A CA     1 
ATOM   2681 C C      . VAL A 1 380 ? 20.03600 -14.64800 -16.45900 1.000 27.40645  ? 371 VAL A C      1 
ATOM   2682 O O      . VAL A 1 380 ? 20.68100 -13.63100 -16.17800 1.000 28.29075  ? 371 VAL A O      1 
ATOM   2683 C CB     . VAL A 1 380 ? 20.91700 -15.23800 -18.74900 1.000 28.36529  ? 371 VAL A CB     1 
ATOM   2684 C CG1    . VAL A 1 380 ? 21.78300 -16.30700 -18.10200 1.000 24.30693  ? 371 VAL A CG1    1 
ATOM   2685 C CG2    . VAL A 1 380 ? 20.51700 -15.65300 -20.15900 1.000 28.72955  ? 371 VAL A CG2    1 
ATOM   2686 N N      . GLY A 1 381 ? 19.61900 -15.51500 -15.53700 1.000 24.10859  ? 372 GLY A N      1 
ATOM   2687 C CA     . GLY A 1 381 ? 19.90400 -15.31400 -14.13000 1.000 24.09875  ? 372 GLY A CA     1 
ATOM   2688 C C      . GLY A 1 381 ? 19.21900 -14.12100 -13.50700 1.000 25.99879  ? 372 GLY A C      1 
ATOM   2689 O O      . GLY A 1 381 ? 19.62200 -13.68300 -12.42600 1.000 26.26475  ? 372 GLY A O      1 
ATOM   2690 N N      . TYR A 1 382 ? 18.18600 -13.58400 -14.15400 1.000 27.03674  ? 373 TYR A N      1 
ATOM   2691 C CA     . TYR A 1 382 ? 17.52000 -12.38500 -13.66400 1.000 24.55484  ? 373 TYR A CA     1 
ATOM   2692 C C      . TYR A 1 382 ? 16.01600 -12.61100 -13.56700 1.000 30.27281  ? 373 TYR A C      1 
ATOM   2693 O O      . TYR A 1 382 ? 15.43300 -12.49700 -12.48300 1.000 26.38574  ? 373 TYR A O      1 
ATOM   2694 C CB     . TYR A 1 382 ? 17.83800 -11.19500 -14.57700 1.000 24.57187  ? 373 TYR A CB     1 
ATOM   2695 C CG     . TYR A 1 382 ? 17.51000 -9.84100  -13.98300 1.000 26.96586  ? 373 TYR A CG     1 
ATOM   2696 C CD1    . TYR A 1 382 ? 17.90700 -9.51100  -12.69400 1.000 25.45242  ? 373 TYR A CD1    1 
ATOM   2697 C CD2    . TYR A 1 382 ? 16.82000 -8.88500  -14.72100 1.000 25.53248  ? 373 TYR A CD2    1 
ATOM   2698 C CE1    . TYR A 1 382 ? 17.61500 -8.27300  -12.14900 1.000 23.74497  ? 373 TYR A CE1    1 
ATOM   2699 C CE2    . TYR A 1 382 ? 16.52600 -7.64200  -14.18600 1.000 22.11464  ? 373 TYR A CE2    1 
ATOM   2700 C CZ     . TYR A 1 382 ? 16.92600 -7.34200  -12.89900 1.000 29.46156  ? 373 TYR A CZ     1 
ATOM   2701 O OH     . TYR A 1 382 ? 16.63600 -6.10900  -12.35800 1.000 27.23054  ? 373 TYR A OH     1 
ATOM   2702 N N      . THR A 1 383 ? 15.38100 -12.94300 -14.69200 1.000 27.51014  ? 374 THR A N      1 
ATOM   2703 C CA     . THR A 1 383 ? 13.94000 -13.16400 -14.73400 1.000 25.89649  ? 374 THR A CA     1 
ATOM   2704 C C      . THR A 1 383 ? 13.56600 -14.55800 -15.22300 1.000 23.09624  ? 374 THR A C      1 
ATOM   2705 O O      . THR A 1 383 ? 12.37500 -14.83700 -15.40400 1.000 28.55879  ? 374 THR A O      1 
ATOM   2706 C CB     . THR A 1 383 ? 13.26000 -12.11500 -15.62100 1.000 24.81815  ? 374 THR A CB     1 
ATOM   2707 O OG1    . THR A 1 383 ? 13.73400 -12.24300 -16.96700 1.000 28.29421  ? 374 THR A OG1    1 
ATOM   2708 C CG2    . THR A 1 383 ? 13.55700 -10.71100 -15.11500 1.000 26.56671  ? 374 THR A CG2    1 
ATOM   2709 N N      . ASP A 1 384 ? 14.53900 -15.44100 -15.44600 1.000 22.42784  ? 375 ASP A N      1 
ATOM   2710 C CA     . ASP A 1 384 ? 14.25400 -16.77700 -15.95100 1.000 25.80479  ? 375 ASP A CA     1 
ATOM   2711 C C      . ASP A 1 384 ? 14.23400 -17.83400 -14.85300 1.000 28.02410  ? 375 ASP A C      1 
ATOM   2712 O O      . ASP A 1 384 ? 14.20200 -19.03000 -15.16000 1.000 29.06983  ? 375 ASP A O      1 
ATOM   2713 C CB     . ASP A 1 384 ? 15.25600 -17.16100 -17.04600 1.000 27.18968  ? 375 ASP A CB     1 
ATOM   2714 C CG     . ASP A 1 384 ? 16.69600 -17.11500 -16.57400 1.000 32.49790  ? 375 ASP A CG     1 
ATOM   2715 O OD1    . ASP A 1 384 ? 16.94900 -16.67100 -15.43500 1.000 25.89605  ? 375 ASP A OD1    1 
ATOM   2716 O OD2    . ASP A 1 384 ? 17.58000 -17.52800 -17.35500 1.000 37.11409  ? 375 ASP A OD2    1 
ATOM   2717 N N      . TYR A 1 385 ? 14.25400 -17.42700 -13.59000 1.000 25.39870  ? 376 TYR A N      1 
ATOM   2718 C CA     . TYR A 1 385 ? 14.01500 -18.37500 -12.51000 1.000 29.11675  ? 376 TYR A CA     1 
ATOM   2719 C C      . TYR A 1 385 ? 12.54200 -18.77100 -12.51200 1.000 29.03223  ? 376 TYR A C      1 
ATOM   2720 O O      . TYR A 1 385 ? 11.67000 -17.89400 -12.49100 1.000 28.55598  ? 376 TYR A O      1 
ATOM   2721 C CB     . TYR A 1 385 ? 14.40300 -17.77700 -11.16200 1.000 27.52770  ? 376 TYR A CB     1 
ATOM   2722 C CG     . TYR A 1 385 ? 15.89400 -17.71200 -10.91200 1.000 27.37534  ? 376 TYR A CG     1 
ATOM   2723 C CD1    . TYR A 1 385 ? 16.61400 -18.85400 -10.58700 1.000 22.44747  ? 376 TYR A CD1    1 
ATOM   2724 C CD2    . TYR A 1 385 ? 16.57800 -16.50600 -10.98200 1.000 24.75105  ? 376 TYR A CD2    1 
ATOM   2725 C CE1    . TYR A 1 385 ? 17.97400 -18.79800 -10.34700 1.000 25.35431  ? 376 TYR A CE1    1 
ATOM   2726 C CE2    . TYR A 1 385 ? 17.93700 -16.43900 -10.74400 1.000 26.36786  ? 376 TYR A CE2    1 
ATOM   2727 C CZ     . TYR A 1 385 ? 18.63000 -17.58800 -10.42600 1.000 25.78035  ? 376 TYR A CZ     1 
ATOM   2728 O OH     . TYR A 1 385 ? 19.98300 -17.52400 -10.18700 1.000 24.59841  ? 376 TYR A OH     1 
ATOM   2729 N N      . PRO A 1 386 ? 12.22400 -20.06300 -12.53000 1.000 29.96850  ? 377 PRO A N      1 
ATOM   2730 C CA     . PRO A 1 386 ? 10.83700 -20.47700 -12.76900 1.000 27.06558  ? 377 PRO A CA     1 
ATOM   2731 C C      . PRO A 1 386 ? 9.94000  -20.24300 -11.56500 1.000 36.69117  ? 377 PRO A C      1 
ATOM   2732 O O      . PRO A 1 386 ? 10.38000 -20.25600 -10.41200 1.000 32.45805  ? 377 PRO A O      1 
ATOM   2733 C CB     . PRO A 1 386 ? 10.96700 -21.97200 -13.07600 1.000 27.25343  ? 377 PRO A CB     1 
ATOM   2734 C CG     . PRO A 1 386 ? 12.18400 -22.39100 -12.31500 1.000 33.20543  ? 377 PRO A CG     1 
ATOM   2735 C CD     . PRO A 1 386 ? 13.12700 -21.21400 -12.35700 1.000 28.20263  ? 377 PRO A CD     1 
ATOM   2736 N N      . PHE A 1 387 ? 8.65900  -20.02900 -11.85400 1.000 38.12828  ? 378 PHE A N      1 
ATOM   2737 C CA     . PHE A 1 387 ? 7.63800  -19.92600 -10.82600 1.000 32.29207  ? 378 PHE A CA     1 
ATOM   2738 C C      . PHE A 1 387 ? 7.24400  -21.31800 -10.33800 1.000 35.47898  ? 378 PHE A C      1 
ATOM   2739 O O      . PHE A 1 387 ? 7.80600  -22.33800 -10.75000 1.000 38.64333  ? 378 PHE A O      1 
ATOM   2740 C CB     . PHE A 1 387 ? 6.41700  -19.17700 -11.35400 1.000 31.81043  ? 378 PHE A CB     1 
ATOM   2741 C CG     . PHE A 1 387 ? 6.59700  -17.68900 -11.42500 1.000 34.75460  ? 378 PHE A CG     1 
ATOM   2742 C CD1    . PHE A 1 387 ? 7.27500  -17.10800 -12.48500 1.000 28.90453  ? 378 PHE A CD1    1 
ATOM   2743 C CD2    . PHE A 1 387 ? 6.07700  -16.86900 -10.43600 1.000 28.68602  ? 378 PHE A CD2    1 
ATOM   2744 C CE1    . PHE A 1 387 ? 7.43800  -15.73700 -12.55300 1.000 32.75121  ? 378 PHE A CE1    1 
ATOM   2745 C CE2    . PHE A 1 387 ? 6.23500  -15.49700 -10.49800 1.000 30.36712  ? 378 PHE A CE2    1 
ATOM   2746 C CZ     . PHE A 1 387 ? 6.91700  -14.93000 -11.55800 1.000 32.02684  ? 378 PHE A CZ     1 
ATOM   2747 N N      . LEU A 1 388 ? 6.25200  -21.36100 -9.45800  1.000 36.54897  ? 379 LEU A N      1 
ATOM   2748 C CA     . LEU A 1 388 ? 5.77500  -22.61700 -8.89800  1.000 38.46339  ? 379 LEU A CA     1 
ATOM   2749 C C      . LEU A 1 388 ? 4.75200  -23.26800 -9.82400  1.000 31.18467  ? 379 LEU A C      1 
ATOM   2750 O O      . LEU A 1 388 ? 5.04500  -24.25900 -10.49200 1.000 35.88076  ? 379 LEU A O      1 
ATOM   2751 C CB     . LEU A 1 388 ? 5.16800  -22.37900 -7.51600  1.000 37.24628  ? 379 LEU A CB     1 
ATOM   2752 C CG     . LEU A 1 388 ? 5.34289  -23.47413 -6.46682  1.000 35.91336  ? 379 LEU A CG     1 
ATOM   2753 C CD1    . LEU A 1 388 ? 6.80006  -23.89639 -6.37442  1.000 31.73538  ? 379 LEU A CD1    1 
ATOM   2754 C CD2    . LEU A 1 388 ? 4.84010  -22.97601 -5.12165  1.000 34.32008  ? 379 LEU A CD2    1 
ATOM   2755 N N      . ASN B 1 19  ? 51.32900 14.58900  -27.70800 1.000 37.76131  ? 10  ASN B N      1 
ATOM   2756 C CA     . ASN B 1 19  ? 50.25300 14.00100  -28.49800 1.000 37.09697  ? 10  ASN B CA     1 
ATOM   2757 C C      . ASN B 1 19  ? 50.15100 12.50200  -28.23100 1.000 37.36896  ? 10  ASN B C      1 
ATOM   2758 O O      . ASN B 1 19  ? 50.98600 11.72600  -28.69600 1.000 36.75666  ? 10  ASN B O      1 
ATOM   2759 C CB     . ASN B 1 19  ? 50.47700 14.26000  -29.99000 1.000 34.92894  ? 10  ASN B CB     1 
ATOM   2760 C CG     . ASN B 1 19  ? 49.22500 14.02800  -30.82100 1.000 43.33294  ? 10  ASN B CG     1 
ATOM   2761 O OD1    . ASN B 1 19  ? 48.29500 13.34400  -30.39200 1.000 39.82300  ? 10  ASN B OD1    1 
ATOM   2762 N ND2    . ASN B 1 19  ? 49.19900 14.59900  -32.02000 1.000 39.72990  ? 10  ASN B ND2    1 
ATOM   2763 N N      . PRO B 1 20  ? 49.12100 12.09500  -27.48400 1.000 32.85184  ? 11  PRO B N      1 
ATOM   2764 C CA     . PRO B 1 20  ? 48.96500 10.66600  -27.17000 1.000 35.25827  ? 11  PRO B CA     1 
ATOM   2765 C C      . PRO B 1 20  ? 48.63900 9.80400   -28.37800 1.000 36.05668  ? 11  PRO B C      1 
ATOM   2766 O O      . PRO B 1 20  ? 48.80700 8.58100   -28.30400 1.000 34.41912  ? 11  PRO B O      1 
ATOM   2767 C CB     . PRO B 1 20  ? 47.81900 10.65300  -26.14900 1.000 35.96993  ? 11  PRO B CB     1 
ATOM   2768 C CG     . PRO B 1 20  ? 47.04500 11.89500  -26.44100 1.000 40.20821  ? 11  PRO B CG     1 
ATOM   2769 C CD     . PRO B 1 20  ? 48.05800 12.91700  -26.88000 1.000 37.55330  ? 11  PRO B CD     1 
ATOM   2770 N N      . LEU B 1 21  ? 48.18400 10.39400  -29.48700 1.000 36.14474  ? 12  LEU B N      1 
ATOM   2771 C CA     . LEU B 1 21  ? 47.91700 9.60500   -30.68500 1.000 35.64198  ? 12  LEU B CA     1 
ATOM   2772 C C      . LEU B 1 21  ? 49.18600 9.02400   -31.29200 1.000 37.80764  ? 12  LEU B C      1 
ATOM   2773 O O      . LEU B 1 21  ? 49.09900 8.11500   -32.12500 1.000 39.81646  ? 12  LEU B O      1 
ATOM   2774 C CB     . LEU B 1 21  ? 47.19100 10.45200  -31.73100 1.000 34.64431  ? 12  LEU B CB     1 
ATOM   2775 C CG     . LEU B 1 21  ? 45.72100 10.78300  -31.47100 1.000 36.99897  ? 12  LEU B CG     1 
ATOM   2776 C CD1    . LEU B 1 21  ? 45.15700 11.61400  -32.61200 1.000 36.10786  ? 12  LEU B CD1    1 
ATOM   2777 C CD2    . LEU B 1 21  ? 44.91000 9.51300   -31.28600 1.000 28.48369  ? 12  LEU B CD2    1 
ATOM   2778 N N      . PHE B 1 22  ? 50.35800 9.52000   -30.89900 1.000 31.72927  ? 13  PHE B N      1 
ATOM   2779 C CA     . PHE B 1 22  ? 51.62200 9.06400   -31.46300 1.000 33.84929  ? 13  PHE B CA     1 
ATOM   2780 C C      . PHE B 1 22  ? 52.52000 8.43700   -30.40200 1.000 37.21285  ? 13  PHE B C      1 
ATOM   2781 O O      . PHE B 1 22  ? 53.74600 8.44700   -30.52500 1.000 37.46327  ? 13  PHE B O      1 
ATOM   2782 C CB     . PHE B 1 22  ? 52.32600 10.21200  -32.18400 1.000 35.35910  ? 13  PHE B CB     1 
ATOM   2783 C CG     . PHE B 1 22  ? 51.57400 10.70200  -33.38500 1.000 37.54789  ? 13  PHE B CG     1 
ATOM   2784 C CD1    . PHE B 1 22  ? 51.79500 10.14000  -34.63200 1.000 36.07113  ? 13  PHE B CD1    1 
ATOM   2785 C CD2    . PHE B 1 22  ? 50.62000 11.69800  -33.26300 1.000 35.02875  ? 13  PHE B CD2    1 
ATOM   2786 C CE1    . PHE B 1 22  ? 51.09200 10.57700  -35.73900 1.000 38.45659  ? 13  PHE B CE1    1 
ATOM   2787 C CE2    . PHE B 1 22  ? 49.91400 12.13900  -34.36600 1.000 38.83437  ? 13  PHE B CE2    1 
ATOM   2788 C CZ     . PHE B 1 22  ? 50.15000 11.57600  -35.60500 1.000 34.41398  ? 13  PHE B CZ     1 
ATOM   2789 N N      . SER B 1 23  ? 51.91500 7.89100   -29.35200 1.000 40.32540  ? 14  SER B N      1 
ATOM   2790 C CA     . SER B 1 23  ? 52.66100 7.00400   -28.47200 1.000 38.76775  ? 14  SER B CA     1 
ATOM   2791 C C      . SER B 1 23  ? 52.51800 5.56600   -28.96200 1.000 32.91427  ? 14  SER B C      1 
ATOM   2792 O O      . SER B 1 23  ? 51.45100 5.18400   -29.45200 1.000 32.97708  ? 14  SER B O      1 
ATOM   2793 C CB     . SER B 1 23  ? 52.15500 7.10800   -27.03700 1.000 34.12359  ? 14  SER B CB     1 
ATOM   2794 O OG     . SER B 1 23  ? 50.82200 6.64000   -26.93300 1.000 41.22497  ? 14  SER B OG     1 
ATOM   2795 N N      . PRO B 1 24  ? 53.56700 4.75300   -28.85400 1.000 33.92129  ? 15  PRO B N      1 
ATOM   2796 C CA     . PRO B 1 24  ? 53.49400 3.39000   -29.39200 1.000 31.95311  ? 15  PRO B CA     1 
ATOM   2797 C C      . PRO B 1 24  ? 52.44800 2.55600   -28.66900 1.000 33.50899  ? 15  PRO B C      1 
ATOM   2798 O O      . PRO B 1 24  ? 52.11000 2.80500   -27.50900 1.000 36.80027  ? 15  PRO B O      1 
ATOM   2799 C CB     . PRO B 1 24  ? 54.90700 2.84100   -29.16300 1.000 26.99640  ? 15  PRO B CB     1 
ATOM   2800 C CG     . PRO B 1 24  ? 55.44400 3.65200   -28.03100 1.000 36.68302  ? 15  PRO B CG     1 
ATOM   2801 C CD     . PRO B 1 24  ? 54.86200 5.02500   -28.20800 1.000 32.52381  ? 15  PRO B CD     1 
ATOM   2802 N N      . TYR B 1 25  ? 51.92700 1.55800   -29.37900 1.000 30.68563  ? 16  TYR B N      1 
ATOM   2803 C CA     . TYR B 1 25  ? 50.94800 0.63600   -28.82700 1.000 27.77048  ? 16  TYR B CA     1 
ATOM   2804 C C      . TYR B 1 25  ? 51.19400 -0.75200  -29.39400 1.000 28.86526  ? 16  TYR B C      1 
ATOM   2805 O O      . TYR B 1 25  ? 51.50700 -0.90100  -30.57800 1.000 32.51888  ? 16  TYR B O      1 
ATOM   2806 C CB     . TYR B 1 25  ? 49.51100 1.07700   -29.13300 1.000 30.47944  ? 16  TYR B CB     1 
ATOM   2807 C CG     . TYR B 1 25  ? 48.47100 0.19300   -28.48600 1.000 30.65056  ? 16  TYR B CG     1 
ATOM   2808 C CD1    . TYR B 1 25  ? 48.12200 0.36400   -27.15300 1.000 29.59729  ? 16  TYR B CD1    1 
ATOM   2809 C CD2    . TYR B 1 25  ? 47.84700 -0.82000  -29.20200 1.000 28.93761  ? 16  TYR B CD2    1 
ATOM   2810 C CE1    . TYR B 1 25  ? 47.17600 -0.44500  -26.55200 1.000 29.15563  ? 16  TYR B CE1    1 
ATOM   2811 C CE2    . TYR B 1 25  ? 46.90000 -1.63400  -28.61000 1.000 32.88779  ? 16  TYR B CE2    1 
ATOM   2812 C CZ     . TYR B 1 25  ? 46.56800 -1.44100  -27.28600 1.000 26.31689  ? 16  TYR B CZ     1 
ATOM   2813 O OH     . TYR B 1 25  ? 45.62600 -2.24900  -26.69200 1.000 30.19744  ? 16  TYR B OH     1 
ATOM   2814 N N      . LYS B 1 26  ? 51.04400 -1.76300  -28.54400 1.000 30.33275  ? 17  LYS B N      1 
ATOM   2815 C CA     . LYS B 1 26  ? 51.29500 -3.15300  -28.91600 1.000 37.23956  ? 17  LYS B CA     1 
ATOM   2816 C C      . LYS B 1 26  ? 49.95200 -3.84300  -29.13000 1.000 37.49473  ? 17  LYS B C      1 
ATOM   2817 O O      . LYS B 1 26  ? 49.25600 -4.18400  -28.17000 1.000 33.47989  ? 17  LYS B O      1 
ATOM   2818 C CB     . LYS B 1 26  ? 52.12200 -3.85800  -27.84600 1.000 31.54538  ? 17  LYS B CB     1 
ATOM   2819 N N      . MET B 1 27  ? 49.58900 -4.04500  -30.39600 1.000 34.57559  ? 18  MET B N      1 
ATOM   2820 C CA     . MET B 1 27  ? 48.36700 -4.77100  -30.74400 1.000 36.49651  ? 18  MET B CA     1 
ATOM   2821 C C      . MET B 1 27  ? 48.68800 -6.26200  -30.84300 1.000 38.70949  ? 18  MET B C      1 
ATOM   2822 O O      . MET B 1 27  ? 48.70400 -6.87000  -31.91500 1.000 38.19037  ? 18  MET B O      1 
ATOM   2823 C CB     . MET B 1 27  ? 47.77300 -4.23000  -32.03900 1.000 38.83725  ? 18  MET B CB     1 
ATOM   2824 C CG     . MET B 1 27  ? 46.43102 -4.84490  -32.40548 1.000 38.59552  ? 18  MET B CG     1 
ATOM   2825 S SD     . MET B 1 27  ? 45.59066 -3.96917  -33.73850 1.000 41.49213  ? 18  MET B SD     1 
ATOM   2826 C CE     . MET B 1 27  ? 46.36453 -4.70031  -35.17902 1.000 32.69906  ? 18  MET B CE     1 
ATOM   2827 N N      . GLY B 1 28  ? 48.95100 -6.84900  -29.67800 1.000 39.78304  ? 19  GLY B N      1 
ATOM   2828 C CA     . GLY B 1 28  ? 49.39700 -8.22500  -29.61200 1.000 38.80933  ? 19  GLY B CA     1 
ATOM   2829 C C      . GLY B 1 28  ? 50.83900 -8.36600  -30.05100 1.000 41.03363  ? 19  GLY B C      1 
ATOM   2830 O O      . GLY B 1 28  ? 51.75500 -7.92700  -29.34700 1.000 39.70509  ? 19  GLY B O      1 
ATOM   2831 N N      . LYS B 1 29  ? 51.05500 -8.96500  -31.21900 1.000 35.64938  ? 20  LYS B N      1 
ATOM   2832 C CA     . LYS B 1 29  ? 52.39100 -9.13400  -31.77300 1.000 38.24958  ? 20  LYS B CA     1 
ATOM   2833 C C      . LYS B 1 29  ? 52.74900 -8.06400  -32.79400 1.000 36.03306  ? 20  LYS B C      1 
ATOM   2834 O O      . LYS B 1 29  ? 53.84900 -8.10500  -33.35300 1.000 37.88435  ? 20  LYS B O      1 
ATOM   2835 C CB     . LYS B 1 29  ? 52.52700 -10.52200 -32.40700 1.000 34.63302  ? 20  LYS B CB     1 
ATOM   2836 C CG     . LYS B 1 29  ? 51.58300 -10.77000 -33.57000 1.000 42.39151  ? 20  LYS B CG     1 
ATOM   2837 C CD     . LYS B 1 29  ? 51.62800 -12.22500 -34.00400 1.000 51.43269  ? 20  LYS B CD     1 
ATOM   2838 C CE     . LYS B 1 29  ? 50.70200 -12.48000 -35.18100 1.000 50.97781  ? 20  LYS B CE     1 
ATOM   2839 N NZ     . LYS B 1 29  ? 50.61100 -13.93200 -35.50500 1.000 49.38881  ? 20  LYS B NZ     1 
ATOM   2840 N N      . PHE B 1 30  ? 51.85600 -7.11100  -33.05100 1.000 33.64741  ? 21  PHE B N      1 
ATOM   2841 C CA     . PHE B 1 30  ? 52.11000 -6.02000  -33.98600 1.000 31.33333  ? 21  PHE B CA     1 
ATOM   2842 C C      . PHE B 1 30  ? 52.39300 -4.75600  -33.18300 1.000 35.40081  ? 21  PHE B C      1 
ATOM   2843 O O      . PHE B 1 30  ? 51.51300 -4.24800  -32.48100 1.000 37.35130  ? 21  PHE B O      1 
ATOM   2844 C CB     . PHE B 1 30  ? 50.92300 -5.81600  -34.92400 1.000 31.47560  ? 21  PHE B CB     1 
ATOM   2845 C CG     . PHE B 1 30  ? 50.44800 -7.07700  -35.58800 1.000 31.60300  ? 21  PHE B CG     1 
ATOM   2846 C CD1    . PHE B 1 30  ? 51.14800 -7.62100  -36.65200 1.000 32.14589  ? 21  PHE B CD1    1 
ATOM   2847 C CD2    . PHE B 1 30  ? 49.29700 -7.71100  -35.15300 1.000 29.98560  ? 21  PHE B CD2    1 
ATOM   2848 C CE1    . PHE B 1 30  ? 50.71200 -8.78000  -37.26600 1.000 30.44385  ? 21  PHE B CE1    1 
ATOM   2849 C CE2    . PHE B 1 30  ? 48.85400 -8.87000  -35.76300 1.000 36.11891  ? 21  PHE B CE2    1 
ATOM   2850 C CZ     . PHE B 1 30  ? 49.56300 -9.40500  -36.82200 1.000 34.70560  ? 21  PHE B CZ     1 
ATOM   2851 N N      . ASN B 1 31  ? 53.61900 -4.25100  -33.28300 1.000 34.86702  ? 22  ASN B N      1 
ATOM   2852 C CA     . ASN B 1 31  ? 54.02200 -3.03500  -32.58500 1.000 32.08452  ? 22  ASN B CA     1 
ATOM   2853 C C      . ASN B 1 31  ? 53.67300 -1.83700  -33.46000 1.000 32.93416  ? 22  ASN B C      1 
ATOM   2854 O O      . ASN B 1 31  ? 54.26100 -1.65000  -34.53000 1.000 34.71840  ? 22  ASN B O      1 
ATOM   2855 C CB     . ASN B 1 31  ? 55.51300 -3.06600  -32.26500 1.000 31.77857  ? 22  ASN B CB     1 
ATOM   2856 C CG     . ASN B 1 31  ? 55.87395 -4.16047  -31.28364 1.000 40.06313  ? 22  ASN B CG     1 
ATOM   2857 O OD1    . ASN B 1 31  ? 55.07741 -4.52266  -30.41837 1.000 42.88174  ? 22  ASN B OD1    1 
ATOM   2858 N ND2    . ASN B 1 31  ? 57.08344 -4.69504  -31.41338 1.000 49.21286  ? 22  ASN B ND2    1 
ATOM   2859 N N      . LEU B 1 32  ? 52.71600 -1.03000  -33.01500 1.000 26.60508  ? 23  LEU B N      1 
ATOM   2860 C CA     . LEU B 1 32  ? 52.29700 0.13500   -33.77700 1.000 27.63756  ? 23  LEU B CA     1 
ATOM   2861 C C      . LEU B 1 32  ? 53.02500 1.37100   -33.27400 1.000 31.01691  ? 23  LEU B C      1 
ATOM   2862 O O      . LEU B 1 32  ? 53.22200 1.54300   -32.06800 1.000 30.36662  ? 23  LEU B O      1 
ATOM   2863 C CB     . LEU B 1 32  ? 50.78600 0.34000   -33.68000 1.000 23.30558  ? 23  LEU B CB     1 
ATOM   2864 C CG     . LEU B 1 32  ? 49.92600 -0.81000  -34.20500 1.000 26.53517  ? 23  LEU B CG     1 
ATOM   2865 C CD1    . LEU B 1 32  ? 48.45400 -0.50200  -33.99600 1.000 23.55636  ? 23  LEU B CD1    1 
ATOM   2866 C CD2    . LEU B 1 32  ? 50.21900 -1.09600  -35.67400 1.000 26.25749  ? 23  LEU B CD2    1 
ATOM   2867 N N      . SER B 1 33  ? 53.43900 2.22400   -34.20900 1.000 26.24885  ? 24  SER B N      1 
ATOM   2868 C CA     . SER B 1 33  ? 54.14700 3.43700   -33.83400 1.000 28.87939  ? 24  SER B CA     1 
ATOM   2869 C C      . SER B 1 33  ? 53.20000 4.57800   -33.49500 1.000 30.50073  ? 24  SER B C      1 
ATOM   2870 O O      . SER B 1 33  ? 53.62400 5.55400   -32.86800 1.000 31.16342  ? 24  SER B O      1 
ATOM   2871 C CB     . SER B 1 33  ? 55.09700 3.86300   -34.95600 1.000 24.73097  ? 24  SER B CB     1 
ATOM   2872 O OG     . SER B 1 33  ? 54.38800 4.17200   -36.14000 1.000 33.87973  ? 24  SER B OG     1 
ATOM   2873 N N      . HIS B 1 34  ? 51.93300 4.47300   -33.88500 1.000 27.55209  ? 25  HIS B N      1 
ATOM   2874 C CA     . HIS B 1 34  ? 50.94100 5.49900   -33.59700 1.000 24.64007  ? 25  HIS B CA     1 
ATOM   2875 C C      . HIS B 1 34  ? 49.56900 4.83600   -33.61000 1.000 26.87035  ? 25  HIS B C      1 
ATOM   2876 O O      . HIS B 1 34  ? 49.43600 3.65300   -33.93100 1.000 26.37520  ? 25  HIS B O      1 
ATOM   2877 C CB     . HIS B 1 34  ? 51.04500 6.65900   -34.59400 1.000 26.24643  ? 25  HIS B CB     1 
ATOM   2878 C CG     . HIS B 1 34  ? 50.85300 6.25000   -36.02200 1.000 28.17506  ? 25  HIS B CG     1 
ATOM   2879 N ND1    . HIS B 1 34  ? 49.60700 6.04300   -36.57200 1.000 27.03473  ? 25  HIS B ND1    1 
ATOM   2880 C CD2    . HIS B 1 34  ? 51.74500 6.01000   -37.01100 1.000 26.67429  ? 25  HIS B CD2    1 
ATOM   2881 C CE1    . HIS B 1 34  ? 49.73900 5.69400   -37.83900 1.000 27.90153  ? 25  HIS B CE1    1 
ATOM   2882 N NE2    . HIS B 1 34  ? 51.02600 5.66700   -38.13000 1.000 30.22384  ? 25  HIS B NE2    1 
ATOM   2883 N N      . ARG B 1 35  ? 48.54400 5.60600   -33.25200 1.000 27.73678  ? 26  ARG B N      1 
ATOM   2884 C CA     . ARG B 1 35  ? 47.20400 5.06300   -33.06500 1.000 27.15611  ? 26  ARG B CA     1 
ATOM   2885 C C      . ARG B 1 35  ? 46.20700 5.55200   -34.10900 1.000 29.19540  ? 26  ARG B C      1 
ATOM   2886 O O      . ARG B 1 35  ? 44.99800 5.34300   -33.94500 1.000 29.05024  ? 26  ARG B O      1 
ATOM   2887 C CB     . ARG B 1 35  ? 46.70900 5.38200   -31.65300 1.000 30.45632  ? 26  ARG B CB     1 
ATOM   2888 C CG     . ARG B 1 35  ? 47.51400 4.66400   -30.58200 1.000 33.84196  ? 26  ARG B CG     1 
ATOM   2889 C CD     . ARG B 1 35  ? 47.94400 5.59400   -29.46800 1.000 34.95719  ? 26  ARG B CD     1 
ATOM   2890 N NE     . ARG B 1 35  ? 48.80400 4.91200   -28.50800 1.000 34.42624  ? 26  ARG B NE     1 
ATOM   2891 C CZ     . ARG B 1 35  ? 48.36200 4.21400   -27.47200 1.000 35.09609  ? 26  ARG B CZ     1 
ATOM   2892 N NH1    . ARG B 1 35  ? 47.06800 4.07100   -27.23500 1.000 31.97519  ? 26  ARG B NH1    1 
ATOM   2893 N NH2    . ARG B 1 35  ? 49.24000 3.64400   -26.65100 1.000 32.80553  ? 26  ARG B NH2    1 
ATOM   2894 N N      . VAL B 1 36  ? 46.67800 6.18900   -35.17600 1.000 25.11796  ? 27  VAL B N      1 
ATOM   2895 C CA     . VAL B 1 36  ? 45.81500 6.57200   -36.28800 1.000 20.95591  ? 27  VAL B CA     1 
ATOM   2896 C C      . VAL B 1 36  ? 45.64100 5.36200   -37.19700 1.000 22.21457  ? 27  VAL B C      1 
ATOM   2897 O O      . VAL B 1 36  ? 46.62000 4.81500   -37.71400 1.000 24.23257  ? 27  VAL B O      1 
ATOM   2898 C CB     . VAL B 1 36  ? 46.39800 7.76600   -37.05700 1.000 24.96399  ? 27  VAL B CB     1 
ATOM   2899 C CG1    . VAL B 1 36  ? 45.49600 8.13400   -38.22500 1.000 24.58584  ? 27  VAL B CG1    1 
ATOM   2900 C CG2    . VAL B 1 36  ? 46.58600 8.95500   -36.12900 1.000 21.91150  ? 27  VAL B CG2    1 
ATOM   2901 N N      . VAL B 1 37  ? 44.39400 4.94000   -37.38900 1.000 18.30524  ? 28  VAL B N      1 
ATOM   2902 C CA     . VAL B 1 37  ? 44.07100 3.73400   -38.14200 1.000 20.63976  ? 28  VAL B CA     1 
ATOM   2903 C C      . VAL B 1 37  ? 43.25600 4.11900   -39.36900 1.000 24.22372  ? 28  VAL B C      1 
ATOM   2904 O O      . VAL B 1 37  ? 42.39800 5.00500   -39.30300 1.000 21.57824  ? 28  VAL B O      1 
ATOM   2905 C CB     . VAL B 1 37  ? 43.30200 2.71800   -37.26900 1.000 23.86262  ? 28  VAL B CB     1 
ATOM   2906 C CG1    . VAL B 1 37  ? 43.00300 1.44600   -38.05100 1.000 22.49527  ? 28  VAL B CG1    1 
ATOM   2907 C CG2    . VAL B 1 37  ? 44.08800 2.40100   -36.00600 1.000 22.69949  ? 28  VAL B CG2    1 
ATOM   2908 N N      . LEU B 1 38  ? 43.53400 3.45800   -40.49100 1.000 23.96508  ? 29  LEU B N      1 
ATOM   2909 C CA     . LEU B 1 38  ? 42.73300 3.62200   -41.70000 1.000 25.62176  ? 29  LEU B CA     1 
ATOM   2910 C C      . LEU B 1 38  ? 41.48400 2.75700   -41.58200 1.000 21.17027  ? 29  LEU B C      1 
ATOM   2911 O O      . LEU B 1 38  ? 41.57300 1.52500   -41.54700 1.000 21.96744  ? 29  LEU B O      1 
ATOM   2912 C CB     . LEU B 1 38  ? 43.54100 3.24600   -42.93900 1.000 23.92560  ? 29  LEU B CB     1 
ATOM   2913 C CG     . LEU B 1 38  ? 42.73500 3.13400   -44.23600 1.000 23.32726  ? 29  LEU B CG     1 
ATOM   2914 C CD1    . LEU B 1 38  ? 42.05500 4.45200   -44.56700 1.000 23.42309  ? 29  LEU B CD1    1 
ATOM   2915 C CD2    . LEU B 1 38  ? 43.61200 2.67800   -45.39100 1.000 26.85230  ? 29  LEU B CD2    1 
ATOM   2916 N N      . ALA B 1 39  ? 40.32000 3.39700   -41.52500 1.000 23.85730  ? 30  ALA B N      1 
ATOM   2917 C CA     . ALA B 1 39  ? 39.07200 2.66100   -41.41600 1.000 25.95086  ? 30  ALA B CA     1 
ATOM   2918 C C      . ALA B 1 39  ? 38.76800 1.93500   -42.72700 1.000 25.13477  ? 30  ALA B C      1 
ATOM   2919 O O      . ALA B 1 39  ? 39.14700 2.39900   -43.80500 1.000 23.11843  ? 30  ALA B O      1 
ATOM   2920 C CB     . ALA B 1 39  ? 37.92200 3.60300   -41.06300 1.000 20.11314  ? 30  ALA B CB     1 
ATOM   2921 N N      . PRO B 1 40  ? 38.09700 0.78500   -42.65800 1.000 27.13082  ? 31  PRO B N      1 
ATOM   2922 C CA     . PRO B 1 40  ? 37.72000 0.07800   -43.88800 1.000 24.84421  ? 31  PRO B CA     1 
ATOM   2923 C C      . PRO B 1 40  ? 36.75200 0.91300   -44.71200 1.000 25.81568  ? 31  PRO B C      1 
ATOM   2924 O O      . PRO B 1 40  ? 35.76500 1.43600   -44.19300 1.000 21.74321  ? 31  PRO B O      1 
ATOM   2925 C CB     . PRO B 1 40  ? 37.06200 -1.20600  -43.37000 1.000 24.13874  ? 31  PRO B CB     1 
ATOM   2926 C CG     . PRO B 1 40  ? 36.60500 -0.86400  -41.98500 1.000 24.14359  ? 31  PRO B CG     1 
ATOM   2927 C CD     . PRO B 1 40  ? 37.63500 0.08100   -41.44900 1.000 20.30358  ? 31  PRO B CD     1 
ATOM   2928 N N      . MET B 1 41  ? 37.04200 1.04300   -46.00500 1.000 18.08757  ? 32  MET B N      1 
ATOM   2929 C CA     . MET B 1 41  ? 36.21700 1.88400   -46.86400 1.000 25.14322  ? 32  MET B CA     1 
ATOM   2930 C C      . MET B 1 41  ? 36.12500 1.29400   -48.26200 1.000 25.16732  ? 32  MET B C      1 
ATOM   2931 O O      . MET B 1 41  ? 37.13000 1.20900   -48.97400 1.000 19.34234  ? 32  MET B O      1 
ATOM   2932 C CB     . MET B 1 41  ? 36.75900 3.30800   -46.91600 1.000 26.17148  ? 32  MET B CB     1 
ATOM   2933 C CG     . MET B 1 41  ? 36.11147 4.22479   -45.89836 1.000 26.40876  ? 32  MET B CG     1 
ATOM   2934 S SD     . MET B 1 41  ? 36.90678 5.82881   -45.90220 1.000 37.38657  ? 32  MET B SD     1 
ATOM   2935 C CE     . MET B 1 41  ? 38.62564 5.33085   -45.92123 1.000 26.98747  ? 32  MET B CE     1 
ATOM   2936 N N      . THR B 1 42  ? 34.91200 0.90300   -48.64300 1.000 19.45398  ? 33  THR B N      1 
ATOM   2937 C CA     . THR B 1 42  ? 34.63800 0.45300   -49.99900 1.000 23.86170  ? 33  THR B CA     1 
ATOM   2938 C C      . THR B 1 42  ? 34.81300 1.60800   -50.97700 1.000 25.85091  ? 33  THR B C      1 
ATOM   2939 O O      . THR B 1 42  ? 34.23800 2.68500   -50.79300 1.000 25.00184  ? 33  THR B O      1 
ATOM   2940 C CB     . THR B 1 42  ? 33.21600 -0.10000  -50.08700 1.000 25.80813  ? 33  THR B CB     1 
ATOM   2941 O OG1    . THR B 1 42  ? 33.06700 -1.19500  -49.17200 1.000 26.18789  ? 33  THR B OG1    1 
ATOM   2942 C CG2    . THR B 1 42  ? 32.91200 -0.57000  -51.49900 1.000 21.19087  ? 33  THR B CG2    1 
ATOM   2943 N N      . ARG B 1 43  ? 35.61600 1.38300   -52.01800 1.000 26.29327  ? 34  ARG B N      1 
ATOM   2944 C CA     . ARG B 1 43  ? 35.85500 2.39100   -53.03900 1.000 18.06504  ? 34  ARG B CA     1 
ATOM   2945 C C      . ARG B 1 43  ? 35.48500 1.93800   -54.44200 1.000 24.31560  ? 34  ARG B C      1 
ATOM   2946 O O      . ARG B 1 43  ? 35.41900 2.78100   -55.34400 1.000 23.46071  ? 34  ARG B O      1 
ATOM   2947 C CB     . ARG B 1 43  ? 37.32800 2.82900   -53.02800 1.000 22.31800  ? 34  ARG B CB     1 
ATOM   2948 C CG     . ARG B 1 43  ? 37.82600 3.31000   -51.67400 1.000 23.91054  ? 34  ARG B CG     1 
ATOM   2949 C CD     . ARG B 1 43  ? 36.96500 4.43900   -51.12300 1.000 24.87128  ? 34  ARG B CD     1 
ATOM   2950 N NE     . ARG B 1 43  ? 36.81200 5.53200   -52.07600 1.000 21.44480  ? 34  ARG B NE     1 
ATOM   2951 C CZ     . ARG B 1 43  ? 37.72200 6.47200   -52.29300 1.000 22.91993  ? 34  ARG B CZ     1 
ATOM   2952 N NH1    . ARG B 1 43  ? 38.87300 6.48400   -51.64000 1.000 19.91044  ? 34  ARG B NH1    1 
ATOM   2953 N NH2    . ARG B 1 43  ? 37.47500 7.41800   -53.19400 1.000 25.73560  ? 34  ARG B NH2    1 
ATOM   2954 N N      . CYS B 1 44  ? 35.26200 0.63900   -54.65400 1.000 22.45838  ? 35  CYS B N      1 
ATOM   2955 C CA     . CYS B 1 44  ? 34.73100 0.11400   -55.91200 1.000 26.31031  ? 35  CYS B CA     1 
ATOM   2956 C C      . CYS B 1 44  ? 35.70600 0.31300   -57.07400 1.000 27.06885  ? 35  CYS B C      1 
ATOM   2957 O O      . CYS B 1 44  ? 35.29500 0.57600   -58.20500 1.000 27.95283  ? 35  CYS B O      1 
ATOM   2958 C CB     . CYS B 1 44  ? 33.36800 0.73200   -56.23200 1.000 27.81978  ? 35  CYS B CB     1 
ATOM   2959 S SG     . CYS B 1 44  ? 32.15900 0.55100   -54.90300 1.000 21.63760  ? 35  CYS B SG     1 
ATOM   2960 N N      . ARG B 1 45  ? 37.00500 0.18100   -56.79800 1.000 25.28932  ? 36  ARG B N      1 
ATOM   2961 C CA     . ARG B 1 45  ? 38.02300 0.23800   -57.83800 1.000 23.56048  ? 36  ARG B CA     1 
ATOM   2962 C C      . ARG B 1 45  ? 38.57900 -1.13000  -58.21200 1.000 26.76200  ? 36  ARG B C      1 
ATOM   2963 O O      . ARG B 1 45  ? 39.31500 -1.23000  -59.19900 1.000 22.42961  ? 36  ARG B O      1 
ATOM   2964 C CB     . ARG B 1 45  ? 39.18200 1.15000   -57.41300 1.000 26.92694  ? 36  ARG B CB     1 
ATOM   2965 C CG     . ARG B 1 45  ? 39.07300 2.58700   -57.91100 1.000 23.69290  ? 36  ARG B CG     1 
ATOM   2966 C CD     . ARG B 1 45  ? 38.01000 3.36100   -57.15400 1.000 25.06068  ? 36  ARG B CD     1 
ATOM   2967 N NE     . ARG B 1 45  ? 37.97300 4.76700   -57.54000 1.000 26.14924  ? 36  ARG B NE     1 
ATOM   2968 C CZ     . ARG B 1 45  ? 37.19500 5.67900   -56.97200 1.000 26.61969  ? 36  ARG B CZ     1 
ATOM   2969 N NH1    . ARG B 1 45  ? 36.36600 5.36500   -55.98900 1.000 28.21977  ? 36  ARG B NH1    1 
ATOM   2970 N NH2    . ARG B 1 45  ? 37.25000 6.93700   -57.39900 1.000 20.92371  ? 36  ARG B NH2    1 
ATOM   2971 N N      . ALA B 1 46  ? 38.25200 -2.17800  -57.45600 1.000 22.91530  ? 37  ALA B N      1 
ATOM   2972 C CA     . ALA B 1 46  ? 38.71200 -3.53400  -57.76000 1.000 30.55481  ? 37  ALA B CA     1 
ATOM   2973 C C      . ALA B 1 46  ? 37.82000 -4.11100  -58.85600 1.000 24.76515  ? 37  ALA B C      1 
ATOM   2974 O O      . ALA B 1 46  ? 36.86500 -4.85200  -58.60600 1.000 26.51784  ? 37  ALA B O      1 
ATOM   2975 C CB     . ALA B 1 46  ? 38.70400 -4.39900  -56.50700 1.000 23.63762  ? 37  ALA B CB     1 
ATOM   2976 N N      . LEU B 1 47  ? 38.15600 -3.76300  -60.09900 1.000 22.59109  ? 38  LEU B N      1 
ATOM   2977 C CA     . LEU B 1 47  ? 37.31300 -4.09100  -61.24300 1.000 24.97657  ? 38  LEU B CA     1 
ATOM   2978 C C      . LEU B 1 47  ? 37.14000 -5.59900  -61.38600 1.000 22.31689  ? 38  LEU B C      1 
ATOM   2979 O O      . LEU B 1 47  ? 38.11300 -6.35600  -61.32800 1.000 25.51376  ? 38  LEU B O      1 
ATOM   2980 C CB     . LEU B 1 47  ? 37.91600 -3.50400  -62.51900 1.000 22.73353  ? 38  LEU B CB     1 
ATOM   2981 C CG     . LEU B 1 47  ? 38.17900 -1.99800  -62.50600 1.000 27.63219  ? 38  LEU B CG     1 
ATOM   2982 C CD1    . LEU B 1 47  ? 38.72400 -1.53200  -63.84800 1.000 24.71363  ? 38  LEU B CD1    1 
ATOM   2983 C CD2    . LEU B 1 47  ? 36.91500 -1.23200  -62.13800 1.000 19.50880  ? 38  LEU B CD2    1 
ATOM   2984 N N      . ASN B 1 48  ? 35.88700 -6.02400  -61.57600 1.000 23.63451  ? 39  ASN B N      1 
ATOM   2985 C CA     . ASN B 1 48  ? 35.52200 -7.44000  -61.69200 1.000 27.19625  ? 39  ASN B CA     1 
ATOM   2986 C C      . ASN B 1 48  ? 35.96400 -8.23700  -60.46800 1.000 25.94369  ? 39  ASN B C      1 
ATOM   2987 O O      . ASN B 1 48  ? 36.39100 -9.38900  -60.57600 1.000 26.07684  ? 39  ASN B O      1 
ATOM   2988 C CB     . ASN B 1 48  ? 36.08000 -8.05800  -62.97500 1.000 27.55286  ? 39  ASN B CB     1 
ATOM   2989 C CG     . ASN B 1 48  ? 35.15100 -7.87453  -64.15490 1.000 35.10979  ? 39  ASN B CG     1 
ATOM   2990 O OD1    . ASN B 1 48  ? 34.41859 -6.88732  -64.23147 1.000 43.44013  ? 39  ASN B OD1    1 
ATOM   2991 N ND2    . ASN B 1 48  ? 35.17221 -8.82573  -65.08146 1.000 44.93360  ? 39  ASN B ND2    1 
ATOM   2992 N N      . ASN B 1 49  ? 35.85100 -7.61500  -59.29500 1.000 25.85950  ? 40  ASN B N      1 
ATOM   2993 C CA     . ASN B 1 49  ? 36.18900 -8.22000  -58.00700 1.000 25.21200  ? 40  ASN B CA     1 
ATOM   2994 C C      . ASN B 1 49  ? 37.65100 -8.64400  -57.92300 1.000 25.31711  ? 40  ASN B C      1 
ATOM   2995 O O      . ASN B 1 49  ? 38.01600 -9.44600  -57.05800 1.000 30.73144  ? 40  ASN B O      1 
ATOM   2996 C CB     . ASN B 1 49  ? 35.27600 -9.41300  -57.69200 1.000 20.10383  ? 40  ASN B CB     1 
ATOM   2997 C CG     . ASN B 1 49  ? 33.80200 -9.06300  -57.78800 1.000 26.60723  ? 40  ASN B CG     1 
ATOM   2998 O OD1    . ASN B 1 49  ? 33.02200 -9.78600  -58.40800 1.000 24.50118  ? 40  ASN B OD1    1 
ATOM   2999 N ND2    . ASN B 1 49  ? 33.41200 -7.95100  -57.17400 1.000 22.78630  ? 40  ASN B ND2    1 
ATOM   3000 N N      . ILE B 1 50  ? 38.50200 -8.11900  -58.79200 1.000 21.93087  ? 41  ILE B N      1 
ATOM   3001 C CA     . ILE B 1 50  ? 39.92600 -8.44100  -58.80700 1.000 29.48088  ? 41  ILE B CA     1 
ATOM   3002 C C      . ILE B 1 50  ? 40.68900 -7.22300  -58.29700 1.000 28.61871  ? 41  ILE B C      1 
ATOM   3003 O O      . ILE B 1 50  ? 40.54200 -6.13000  -58.85900 1.000 28.89972  ? 41  ILE B O      1 
ATOM   3004 C CB     . ILE B 1 50  ? 40.40400 -8.84400  -60.21000 1.000 29.58434  ? 41  ILE B CB     1 
ATOM   3005 C CG1    . ILE B 1 50  ? 39.68100 -10.11200 -60.67200 1.000 30.61525  ? 41  ILE B CG1    1 
ATOM   3006 C CG2    . ILE B 1 50  ? 41.91300 -9.04600  -60.22100 1.000 28.23206  ? 41  ILE B CG2    1 
ATOM   3007 C CD1    . ILE B 1 50  ? 40.03200 -10.53900 -62.08100 1.000 34.10866  ? 41  ILE B CD1    1 
ATOM   3008 N N      . PRO B 1 51  ? 41.49700 -7.35600  -57.24500 1.000 29.38942  ? 42  PRO B N      1 
ATOM   3009 C CA     . PRO B 1 51  ? 42.28100 -6.21000  -56.75600 1.000 30.69220  ? 42  PRO B CA     1 
ATOM   3010 C C      . PRO B 1 51  ? 43.19900 -5.66500  -57.83900 1.000 31.23558  ? 42  PRO B C      1 
ATOM   3011 O O      . PRO B 1 51  ? 44.05000 -6.37700  -58.37700 1.000 34.28174  ? 42  PRO B O      1 
ATOM   3012 C CB     . PRO B 1 51  ? 43.07200 -6.80300  -55.58300 1.000 25.40771  ? 42  PRO B CB     1 
ATOM   3013 C CG     . PRO B 1 51  ? 42.25600 -7.96800  -55.13000 1.000 25.35613  ? 42  PRO B CG     1 
ATOM   3014 C CD     . PRO B 1 51  ? 41.64900 -8.54000  -56.38200 1.000 31.47875  ? 42  PRO B CD     1 
ATOM   3015 N N      . GLN B 1 52  ? 43.01600 -4.38900  -58.16100 1.000 31.78306  ? 43  GLN B N      1 
ATOM   3016 C CA     . GLN B 1 52  ? 43.77100 -3.73900  -59.21800 1.000 27.00469  ? 43  GLN B CA     1 
ATOM   3017 C C      . GLN B 1 52  ? 45.03200 -3.08700  -58.65900 1.000 31.83405  ? 43  GLN B C      1 
ATOM   3018 O O      . GLN B 1 52  ? 45.22100 -2.96500  -57.44700 1.000 28.58798  ? 43  GLN B O      1 
ATOM   3019 C CB     . GLN B 1 52  ? 42.90500 -2.69700  -59.92700 1.000 26.35961  ? 43  GLN B CB     1 
ATOM   3020 C CG     . GLN B 1 52  ? 41.62300 -3.25500  -60.51600 1.000 29.99648  ? 43  GLN B CG     1 
ATOM   3021 C CD     . GLN B 1 52  ? 41.87800 -4.21400  -61.66100 1.000 32.50055  ? 43  GLN B CD     1 
ATOM   3022 O OE1    . GLN B 1 52  ? 42.79400 -4.01600  -62.45900 1.000 36.30318  ? 43  GLN B OE1    1 
ATOM   3023 N NE2    . GLN B 1 52  ? 41.06900 -5.26300  -61.74500 1.000 31.15395  ? 43  GLN B NE2    1 
ATOM   3024 N N      . ALA B 1 53  ? 45.90800 -2.66000  -59.57300 1.000 34.10908  ? 44  ALA B N      1 
ATOM   3025 C CA     . ALA B 1 53  ? 47.12100 -1.96400  -59.16000 1.000 25.42932  ? 44  ALA B CA     1 
ATOM   3026 C C      . ALA B 1 53  ? 46.80500 -0.61800  -58.52200 1.000 32.60005  ? 44  ALA B C      1 
ATOM   3027 O O      . ALA B 1 53  ? 47.60000 -0.11300  -57.72100 1.000 32.29886  ? 44  ALA B O      1 
ATOM   3028 C CB     . ALA B 1 53  ? 48.05600 -1.78100  -60.35600 1.000 24.15077  ? 44  ALA B CB     1 
ATOM   3029 N N      . ALA B 1 54  ? 45.65600 -0.02700  -58.86200 1.000 31.32491  ? 45  ALA B N      1 
ATOM   3030 C CA     . ALA B 1 54  ? 45.25000 1.23000   -58.24500 1.000 27.68534  ? 45  ALA B CA     1 
ATOM   3031 C C      . ALA B 1 54  ? 45.07700 1.08800   -56.73900 1.000 25.21850  ? 45  ALA B C      1 
ATOM   3032 O O      . ALA B 1 54  ? 45.36000 2.03100   -55.99100 1.000 27.93472  ? 45  ALA B O      1 
ATOM   3033 C CB     . ALA B 1 54  ? 43.95200 1.73200   -58.87600 1.000 26.57475  ? 45  ALA B CB     1 
ATOM   3034 N N      . LEU B 1 55  ? 44.60100 -0.07000  -56.27800 1.000 24.33350  ? 46  LEU B N      1 
ATOM   3035 C CA     . LEU B 1 55  ? 44.50000 -0.30100  -54.84100 1.000 26.53443  ? 46  LEU B CA     1 
ATOM   3036 C C      . LEU B 1 55  ? 45.87700 -0.28600  -54.19000 1.000 26.38291  ? 46  LEU B C      1 
ATOM   3037 O O      . LEU B 1 55  ? 46.05000 0.27000   -53.09900 1.000 26.06596  ? 46  LEU B O      1 
ATOM   3038 C CB     . LEU B 1 55  ? 43.78700 -1.62800  -54.56600 1.000 20.06449  ? 46  LEU B CB     1 
ATOM   3039 C CG     . LEU B 1 55  ? 42.25500 -1.68500  -54.59800 1.000 24.16060  ? 46  LEU B CG     1 
ATOM   3040 C CD1    . LEU B 1 55  ? 41.69100 -1.42500  -55.99100 1.000 23.93566  ? 46  LEU B CD1    1 
ATOM   3041 C CD2    . LEU B 1 55  ? 41.76800 -3.02800  -54.07000 1.000 25.54313  ? 46  LEU B CD2    1 
ATOM   3042 N N      . GLY B 1 56  ? 46.87300 -0.87600  -54.85600 1.000 29.66276  ? 47  GLY B N      1 
ATOM   3043 C CA     . GLY B 1 56  ? 48.21900 -0.88700  -54.30500 1.000 24.19052  ? 47  GLY B CA     1 
ATOM   3044 C C      . GLY B 1 56  ? 48.76600 0.50800   -54.07500 1.000 29.24472  ? 47  GLY B C      1 
ATOM   3045 O O      . GLY B 1 56  ? 49.32500 0.80400   -53.01700 1.000 34.80614  ? 47  GLY B O      1 
ATOM   3046 N N      . GLU B 1 57  ? 48.60700 1.38900   -55.06700 1.000 23.53960  ? 48  GLU B N      1 
ATOM   3047 C CA     . GLU B 1 57  ? 49.04900 2.77000   -54.90600 1.000 26.88341  ? 48  GLU B CA     1 
ATOM   3048 C C      . GLU B 1 57  ? 48.19300 3.51300   -53.88900 1.000 32.11449  ? 48  GLU B C      1 
ATOM   3049 O O      . GLU B 1 57  ? 48.70400 4.36700   -53.15400 1.000 28.86940  ? 48  GLU B O      1 
ATOM   3050 C CB     . GLU B 1 57  ? 49.02400 3.49700   -56.24800 1.000 30.47139  ? 48  GLU B CB     1 
ATOM   3051 C CG     . GLU B 1 57  ? 49.70185 4.85944   -56.21338 1.000 39.78758  ? 48  GLU B CG     1 
ATOM   3052 C CD     . GLU B 1 57  ? 49.44873 5.67277   -57.46734 1.000 47.87456  ? 48  GLU B CD     1 
ATOM   3053 O OE1    . GLU B 1 57  ? 49.88828 6.84258   -57.51771 1.000 48.03982  ? 48  GLU B OE1    1 
ATOM   3054 O OE2    . GLU B 1 57  ? 48.82068 5.13960   -58.40725 1.000 50.55237  ? 48  GLU B OE2    1 
ATOM   3055 N N      . TYR B 1 58  ? 46.89600 3.20400   -53.83600 1.000 25.58849  ? 49  TYR B N      1 
ATOM   3056 C CA     . TYR B 1 58  ? 46.00100 3.87100   -52.89500 1.000 24.05381  ? 49  TYR B CA     1 
ATOM   3057 C C      . TYR B 1 58  ? 46.39600 3.57300   -51.45300 1.000 29.13991  ? 49  TYR B C      1 
ATOM   3058 O O      . TYR B 1 58  ? 46.51400 4.48600   -50.62600 1.000 26.61354  ? 49  TYR B O      1 
ATOM   3059 C CB     . TYR B 1 58  ? 44.56100 3.44000   -53.16900 1.000 26.48202  ? 49  TYR B CB     1 
ATOM   3060 C CG     . TYR B 1 58  ? 43.54500 3.84300   -52.12300 1.000 24.33549  ? 49  TYR B CG     1 
ATOM   3061 C CD1    . TYR B 1 58  ? 42.98800 5.11600   -52.11800 1.000 24.28807  ? 49  TYR B CD1    1 
ATOM   3062 C CD2    . TYR B 1 58  ? 43.11700 2.93700   -51.16100 1.000 27.45291  ? 49  TYR B CD2    1 
ATOM   3063 C CE1    . TYR B 1 58  ? 42.04500 5.48000   -51.17100 1.000 24.22354  ? 49  TYR B CE1    1 
ATOM   3064 C CE2    . TYR B 1 58  ? 42.17800 3.29100   -50.21100 1.000 24.84906  ? 49  TYR B CE2    1 
ATOM   3065 C CZ     . TYR B 1 58  ? 41.64500 4.56200   -50.22000 1.000 27.69139  ? 49  TYR B CZ     1 
ATOM   3066 O OH     . TYR B 1 58  ? 40.70900 4.91200   -49.27400 1.000 27.82785  ? 49  TYR B OH     1 
ATOM   3067 N N      . TYR B 1 59  ? 46.61400 2.29600   -51.13300 1.000 25.65478  ? 50  TYR B N      1 
ATOM   3068 C CA     . TYR B 1 59  ? 47.02300 1.94600   -49.77800 1.000 27.19456  ? 50  TYR B CA     1 
ATOM   3069 C C      . TYR B 1 59  ? 48.46800 2.34400   -49.50400 1.000 27.76700  ? 50  TYR B C      1 
ATOM   3070 O O      . TYR B 1 59  ? 48.83400 2.57300   -48.34500 1.000 22.65674  ? 50  TYR B O      1 
ATOM   3071 C CB     . TYR B 1 59  ? 46.82100 0.45000   -49.53200 1.000 22.97162  ? 50  TYR B CB     1 
ATOM   3072 C CG     . TYR B 1 59  ? 45.36800 0.04000   -49.44500 1.000 25.41089  ? 50  TYR B CG     1 
ATOM   3073 C CD1    . TYR B 1 59  ? 44.59100 0.39000   -48.34700 1.000 23.94213  ? 50  TYR B CD1    1 
ATOM   3074 C CD2    . TYR B 1 59  ? 44.77300 -0.69900  -50.45800 1.000 25.14398  ? 50  TYR B CD2    1 
ATOM   3075 C CE1    . TYR B 1 59  ? 43.26200 0.01900   -48.26200 1.000 20.46216  ? 50  TYR B CE1    1 
ATOM   3076 C CE2    . TYR B 1 59  ? 43.44500 -1.07600  -50.38300 1.000 27.39508  ? 50  TYR B CE2    1 
ATOM   3077 C CZ     . TYR B 1 59  ? 42.69400 -0.71500  -49.28300 1.000 26.89267  ? 50  TYR B CZ     1 
ATOM   3078 O OH     . TYR B 1 59  ? 41.37300 -1.08900  -49.20800 1.000 25.72565  ? 50  TYR B OH     1 
ATOM   3079 N N      . GLU B 1 60  ? 49.29700 2.43900   -50.54800 1.000 26.24643  ? 51  GLU B N      1 
ATOM   3080 C CA     . GLU B 1 60  ? 50.68000 2.86700   -50.35700 1.000 28.46275  ? 51  GLU B CA     1 
ATOM   3081 C C      . GLU B 1 60  ? 50.75300 4.33500   -49.95800 1.000 28.02429  ? 51  GLU B C      1 
ATOM   3082 O O      . GLU B 1 60  ? 51.58200 4.71600   -49.12300 1.000 32.46781  ? 51  GLU B O      1 
ATOM   3083 C CB     . GLU B 1 60  ? 51.49000 2.61600   -51.62900 1.000 27.92451  ? 51  GLU B CB     1 
ATOM   3084 C CG     . GLU B 1 60  ? 52.89600 3.19300   -51.59900 1.000 36.42037  ? 51  GLU B CG     1 
ATOM   3085 C CD     . GLU B 1 60  ? 53.67400 2.90300   -52.86800 1.000 49.60831  ? 51  GLU B CD     1 
ATOM   3086 O OE1    . GLU B 1 60  ? 53.14200 3.17200   -53.96700 1.000 50.13037  ? 51  GLU B OE1    1 
ATOM   3087 O OE2    . GLU B 1 60  ? 54.81500 2.40300   -52.76800 1.000 41.69708  ? 51  GLU B OE2    1 
ATOM   3088 N N      . GLN B 1 61  ? 49.89400 5.17400   -50.54500 1.000 26.70757  ? 52  GLN B N      1 
ATOM   3089 C CA     . GLN B 1 61  ? 49.88000 6.59000   -50.19000 1.000 30.21144  ? 52  GLN B CA     1 
ATOM   3090 C C      . GLN B 1 61  ? 49.55100 6.79700   -48.71900 1.000 24.13356  ? 52  GLN B C      1 
ATOM   3091 O O      . GLN B 1 61  ? 50.04700 7.74400   -48.09900 1.000 27.08383  ? 52  GLN B O      1 
ATOM   3092 C CB     . GLN B 1 61  ? 48.87200 7.34400   -51.05800 1.000 27.13341  ? 52  GLN B CB     1 
ATOM   3093 C CG     . GLN B 1 61  ? 49.25200 7.46000   -52.52200 1.000 24.05954  ? 52  GLN B CG     1 
ATOM   3094 C CD     . GLN B 1 61  ? 48.21200 8.21500   -53.32800 1.000 29.41587  ? 52  GLN B CD     1 
ATOM   3095 O OE1    . GLN B 1 61  ? 47.09400 8.44300   -52.86400 1.000 23.20980  ? 52  GLN B OE1    1 
ATOM   3096 N NE2    . GLN B 1 61  ? 48.57600 8.61100   -54.54100 1.000 29.86809  ? 52  GLN B NE2    1 
ATOM   3097 N N      . ARG B 1 62  ? 48.72400 5.92600   -48.14500 1.000 24.93723  ? 53  ARG B N      1 
ATOM   3098 C CA     . ARG B 1 62  ? 48.26000 6.07900   -46.77400 1.000 30.54359  ? 53  ARG B CA     1 
ATOM   3099 C C      . ARG B 1 62  ? 49.02700 5.22100   -45.77800 1.000 27.98775  ? 53  ARG B C      1 
ATOM   3100 O O      . ARG B 1 62  ? 48.85500 5.40500   -44.56800 1.000 28.06111  ? 53  ARG B O      1 
ATOM   3101 C CB     . ARG B 1 62  ? 46.76300 5.75700   -46.69600 1.000 28.73276  ? 53  ARG B CB     1 
ATOM   3102 C CG     . ARG B 1 62  ? 45.90400 6.81600   -47.36000 1.000 26.79354  ? 53  ARG B CG     1 
ATOM   3103 C CD     . ARG B 1 62  ? 44.69500 6.23400   -48.06700 1.000 26.94940  ? 53  ARG B CD     1 
ATOM   3104 N NE     . ARG B 1 62  ? 43.99900 7.26800   -48.82300 1.000 25.82963  ? 53  ARG B NE     1 
ATOM   3105 C CZ     . ARG B 1 62  ? 44.38800 7.71300   -50.01000 1.000 25.39443  ? 53  ARG B CZ     1 
ATOM   3106 N NH1    . ARG B 1 62  ? 45.44700 7.20900   -50.62300 1.000 25.11044  ? 53  ARG B NH1    1 
ATOM   3107 N NH2    . ARG B 1 62  ? 43.70400 8.69400   -50.59200 1.000 27.44071  ? 53  ARG B NH2    1 
ATOM   3108 N N      . ALA B 1 63  ? 49.87100 4.30800   -46.24900 1.000 29.87433  ? 54  ALA B N      1 
ATOM   3109 C CA     . ALA B 1 63  ? 50.65900 3.48000   -45.34800 1.000 28.49891  ? 54  ALA B CA     1 
ATOM   3110 C C      . ALA B 1 63  ? 51.76200 4.30100   -44.69100 1.000 30.14573  ? 54  ALA B C      1 
ATOM   3111 O O      . ALA B 1 63  ? 52.36300 5.17900   -45.31600 1.000 31.00484  ? 54  ALA B O      1 
ATOM   3112 C CB     . ALA B 1 63  ? 51.26300 2.29700   -46.10300 1.000 25.51877  ? 54  ALA B CB     1 
ATOM   3113 N N      . THR B 1 64  ? 52.01800 4.01500   -43.41500 1.000 27.86514  ? 55  THR B N      1 
ATOM   3114 C CA     . THR B 1 64  ? 53.09000 4.65400   -42.66600 1.000 28.19582  ? 55  THR B CA     1 
ATOM   3115 C C      . THR B 1 64  ? 53.84400 3.59300   -41.87600 1.000 31.71588  ? 55  THR B C      1 
ATOM   3116 O O      . THR B 1 64  ? 53.33500 2.49800   -41.62500 1.000 29.26940  ? 55  THR B O      1 
ATOM   3117 C CB     . THR B 1 64  ? 52.56200 5.73700   -41.71200 1.000 27.16087  ? 55  THR B CB     1 
ATOM   3118 O OG1    . THR B 1 64  ? 51.54000 5.18300   -40.87400 1.000 25.00498  ? 55  THR B OG1    1 
ATOM   3119 C CG2    . THR B 1 64  ? 51.99600 6.91800   -42.49000 1.000 25.92917  ? 55  THR B CG2    1 
ATOM   3120 N N      . ALA B 1 65  ? 55.06800 3.93500   -41.47800 1.000 28.90960  ? 56  ALA B N      1 
ATOM   3121 C CA     . ALA B 1 65  ? 55.90900 3.02200   -40.70900 1.000 25.99265  ? 56  ALA B CA     1 
ATOM   3122 C C      . ALA B 1 65  ? 55.28400 2.78300   -39.34000 1.000 30.23497  ? 56  ALA B C      1 
ATOM   3123 O O      . ALA B 1 65  ? 55.20800 3.69800   -38.51400 1.000 28.41652  ? 56  ALA B O      1 
ATOM   3124 C CB     . ALA B 1 65  ? 57.31800 3.59000   -40.57500 1.000 30.64356  ? 56  ALA B CB     1 
ATOM   3125 N N      . GLY B 1 66  ? 54.84000 1.55400   -39.09400 1.000 28.45907  ? 57  GLY B N      1 
ATOM   3126 C CA     . GLY B 1 66  ? 54.16900 1.23300   -37.85400 1.000 26.51836  ? 57  GLY B CA     1 
ATOM   3127 C C      . GLY B 1 66  ? 52.71100 1.62600   -37.79700 1.000 27.51504  ? 57  GLY B C      1 
ATOM   3128 O O      . GLY B 1 66  ? 52.12700 1.62000   -36.70600 1.000 27.73890  ? 57  GLY B O      1 
ATOM   3129 N N      . GLY B 1 67  ? 52.10400 1.97300   -38.93200 1.000 26.16569  ? 58  GLY B N      1 
ATOM   3130 C CA     . GLY B 1 67  ? 50.70200 2.32800   -38.96100 1.000 26.02314  ? 58  GLY B CA     1 
ATOM   3131 C C      . GLY B 1 67  ? 49.82000 1.14600   -39.32100 1.000 25.05759  ? 58  GLY B C      1 
ATOM   3132 O O      . GLY B 1 67  ? 50.20600 0.26700   -40.08700 1.000 28.55904  ? 58  GLY B O      1 
ATOM   3133 N N      . PHE B 1 68  ? 48.61800 1.13600   -38.75300 1.000 26.65779  ? 59  PHE B N      1 
ATOM   3134 C CA     . PHE B 1 68  ? 47.65900 0.05900   -38.96100 1.000 28.59088  ? 59  PHE B CA     1 
ATOM   3135 C C      . PHE B 1 68  ? 46.66000 0.46500   -40.03800 1.000 28.00295  ? 59  PHE B C      1 
ATOM   3136 O O      . PHE B 1 68  ? 46.06500 1.54500   -39.96300 1.000 25.63938  ? 59  PHE B O      1 
ATOM   3137 C CB     . PHE B 1 68  ? 46.92900 -0.27600  -37.65800 1.000 23.41583  ? 59  PHE B CB     1 
ATOM   3138 C CG     . PHE B 1 68  ? 46.01300 -1.46400  -37.76100 1.000 30.79663  ? 59  PHE B CG     1 
ATOM   3139 C CD1    . PHE B 1 68  ? 46.26400 -2.47800  -38.67200 1.000 25.59733  ? 59  PHE B CD1    1 
ATOM   3140 C CD2    . PHE B 1 68  ? 44.89200 -1.55900  -36.95100 1.000 26.91345  ? 59  PHE B CD2    1 
ATOM   3141 C CE1    . PHE B 1 68  ? 45.42000 -3.56500  -38.77000 1.000 25.14752  ? 59  PHE B CE1    1 
ATOM   3142 C CE2    . PHE B 1 68  ? 44.04500 -2.64500  -37.04500 1.000 25.80733  ? 59  PHE B CE2    1 
ATOM   3143 C CZ     . PHE B 1 68  ? 44.30900 -3.64900  -37.95500 1.000 29.02501  ? 59  PHE B CZ     1 
ATOM   3144 N N      . LEU B 1 69  ? 46.48100 -0.40100  -41.03300 1.000 27.41765  ? 60  LEU B N      1 
ATOM   3145 C CA     . LEU B 1 69  ? 45.55300 -0.17100  -42.13000 1.000 24.96313  ? 60  LEU B CA     1 
ATOM   3146 C C      . LEU B 1 69  ? 44.52800 -1.29500  -42.18200 1.000 23.48762  ? 60  LEU B C      1 
ATOM   3147 O O      . LEU B 1 69  ? 44.85500 -2.45800  -41.93400 1.000 23.06049  ? 60  LEU B O      1 
ATOM   3148 C CB     . LEU B 1 69  ? 46.28700 -0.08700  -43.47300 1.000 23.86727  ? 60  LEU B CB     1 
ATOM   3149 C CG     . LEU B 1 69  ? 47.46300 0.88300   -43.58900 1.000 28.32792  ? 60  LEU B CG     1 
ATOM   3150 C CD1    . LEU B 1 69  ? 47.98700 0.91300   -45.02000 1.000 22.92426  ? 60  LEU B CD1    1 
ATOM   3151 C CD2    . LEU B 1 69  ? 47.06600 2.27500   -43.12900 1.000 29.78553  ? 60  LEU B CD2    1 
ATOM   3152 N N      . ILE B 1 70  ? 43.28800 -0.94400  -42.51200 1.000 25.38221  ? 61  ILE B N      1 
ATOM   3153 C CA     . ILE B 1 70  ? 42.21400 -1.91000  -42.71000 1.000 23.08087  ? 61  ILE B CA     1 
ATOM   3154 C C      . ILE B 1 70  ? 41.64800 -1.70400  -44.10700 1.000 22.74322  ? 61  ILE B C      1 
ATOM   3155 O O      . ILE B 1 70  ? 41.25300 -0.58700  -44.46300 1.000 21.55440  ? 61  ILE B O      1 
ATOM   3156 C CB     . ILE B 1 70  ? 41.11200 -1.76900  -41.64300 1.000 28.43755  ? 61  ILE B CB     1 
ATOM   3157 C CG1    . ILE B 1 70  ? 41.70800 -1.88100  -40.23900 1.000 21.23164  ? 61  ILE B CG1    1 
ATOM   3158 C CG2    . ILE B 1 70  ? 40.04200 -2.82800  -41.84400 1.000 24.15030  ? 61  ILE B CG2    1 
ATOM   3159 C CD1    . ILE B 1 70  ? 40.70200 -1.66200  -39.13300 1.000 18.85516  ? 61  ILE B CD1    1 
ATOM   3160 N N      . THR B 1 71  ? 41.61000 -2.77600  -44.89400 1.000 21.58157  ? 62  THR B N      1 
ATOM   3161 C CA     . THR B 1 71  ? 41.18400 -2.66700  -46.27900 1.000 24.29390  ? 62  THR B CA     1 
ATOM   3162 C C      . THR B 1 71  ? 39.67300 -2.48500  -46.37400 1.000 25.30520  ? 62  THR B C      1 
ATOM   3163 O O      . THR B 1 71  ? 38.92600 -2.65500  -45.40700 1.000 27.02157  ? 62  THR B O      1 
ATOM   3164 C CB     . THR B 1 71  ? 41.58100 -3.91000  -47.07500 1.000 23.96367  ? 62  THR B CB     1 
ATOM   3165 O OG1    . THR B 1 71  ? 40.77500 -5.01900  -46.65700 1.000 19.95076  ? 62  THR B OG1    1 
ATOM   3166 C CG2    . THR B 1 71  ? 43.04000 -4.24300  -46.85700 1.000 23.68246  ? 62  THR B CG2    1 
ATOM   3167 N N      . GLU B 1 72  ? 39.23200 -2.13700  -47.58000 1.000 22.89775  ? 63  GLU B N      1 
ATOM   3168 C CA     . GLU B 1 72  ? 37.82600 -2.16700  -47.95600 1.000 24.29976  ? 63  GLU B CA     1 
ATOM   3169 C C      . GLU B 1 72  ? 37.22700 -3.54100  -47.68500 1.000 21.83386  ? 63  GLU B C      1 
ATOM   3170 O O      . GLU B 1 72  ? 37.95100 -4.54200  -47.63500 1.000 19.36581  ? 63  GLU B O      1 
ATOM   3171 C CB     . GLU B 1 72  ? 37.68400 -1.81000  -49.43600 1.000 20.91337  ? 63  GLU B CB     1 
ATOM   3172 C CG     . GLU B 1 72  ? 38.64600 -2.59200  -50.31900 1.000 23.48736  ? 63  GLU B CG     1 
ATOM   3173 C CD     . GLU B 1 72  ? 38.98200 -1.88100  -51.61600 1.000 29.27134  ? 63  GLU B CD     1 
ATOM   3174 O OE1    . GLU B 1 72  ? 38.09300 -1.76600  -52.48400 1.000 22.73356  ? 63  GLU B OE1    1 
ATOM   3175 O OE2    . GLU B 1 72  ? 40.13900 -1.43400  -51.76500 1.000 26.26027  ? 63  GLU B OE2    1 
ATOM   3176 N N      . GLY B 1 73  ? 35.91000 -3.59900  -47.50900 1.000 22.65443  ? 64  GLY B N      1 
ATOM   3177 C CA     . GLY B 1 73  ? 35.23200 -4.87200  -47.36700 1.000 20.07714  ? 64  GLY B CA     1 
ATOM   3178 C C      . GLY B 1 73  ? 35.50100 -5.78600  -48.54500 1.000 24.94898  ? 64  GLY B C      1 
ATOM   3179 O O      . GLY B 1 73  ? 35.42200 -5.35900  -49.70100 1.000 19.08092  ? 64  GLY B O      1 
ATOM   3180 N N      . THR B 1 74  ? 35.82500 -7.04400  -48.26600 1.000 20.18641  ? 65  THR B N      1 
ATOM   3181 C CA     . THR B 1 74  ? 36.27100 -7.98300  -49.28300 1.000 18.76668  ? 65  THR B CA     1 
ATOM   3182 C C      . THR B 1 74  ? 35.35000 -9.19600  -49.30700 1.000 23.60508  ? 65  THR B C      1 
ATOM   3183 O O      . THR B 1 74  ? 34.97700 -9.72500  -48.25500 1.000 22.83706  ? 65  THR B O      1 
ATOM   3184 C CB     . THR B 1 74  ? 37.72500 -8.41000  -49.02400 1.000 23.81566  ? 65  THR B CB     1 
ATOM   3185 O OG1    . THR B 1 74  ? 38.56700 -7.24900  -48.99800 1.000 18.91625  ? 65  THR B OG1    1 
ATOM   3186 C CG2    . THR B 1 74  ? 38.21600 -9.34700  -50.10600 1.000 19.54707  ? 65  THR B CG2    1 
ATOM   3187 N N      . MET B 1 75  ? 34.98500 -9.62600  -50.51500 1.000 19.85757  ? 66  MET B N      1 
ATOM   3188 C CA     . MET B 1 75  ? 34.05800 -10.74000 -50.67800 1.000 25.29923  ? 66  MET B CA     1 
ATOM   3189 C C      . MET B 1 75  ? 34.65200 -12.03200 -50.12800 1.000 27.32882  ? 66  MET B C      1 
ATOM   3190 O O      . MET B 1 75  ? 35.84600 -12.30400 -50.27800 1.000 27.48689  ? 66  MET B O      1 
ATOM   3191 C CB     . MET B 1 75  ? 33.70200 -10.92400 -52.15600 1.000 24.47832  ? 66  MET B CB     1 
ATOM   3192 C CG     . MET B 1 75  ? 32.83731 -9.82275  -52.75102 1.000 21.74858  ? 66  MET B CG     1 
ATOM   3193 S SD     . MET B 1 75  ? 32.73676 -9.92001  -54.55421 1.000 27.08434  ? 66  MET B SD     1 
ATOM   3194 C CE     . MET B 1 75  ? 31.94066 -11.50591 -54.78356 1.000 20.93779  ? 66  MET B CE     1 
ATOM   3195 N N      . ILE B 1 76  ? 33.80100 -12.83500 -49.48900 1.000 22.58920  ? 67  ILE B N      1 
ATOM   3196 C CA     . ILE B 1 76  ? 34.18700 -14.15700 -49.00500 1.000 24.56031  ? 67  ILE B CA     1 
ATOM   3197 C C      . ILE B 1 76  ? 33.62100 -15.28000 -49.85800 1.000 26.99351  ? 67  ILE B C      1 
ATOM   3198 O O      . ILE B 1 76  ? 33.95900 -16.45000 -49.61400 1.000 30.90708  ? 67  ILE B O      1 
ATOM   3199 C CB     . ILE B 1 76  ? 33.77100 -14.36800 -47.53400 1.000 21.00698  ? 67  ILE B CB     1 
ATOM   3200 C CG1    . ILE B 1 76  ? 32.24600 -14.36600 -47.41200 1.000 21.92172  ? 67  ILE B CG1    1 
ATOM   3201 C CG2    . ILE B 1 76  ? 34.39200 -13.30600 -46.64300 1.000 24.25266  ? 67  ILE B CG2    1 
ATOM   3202 C CD1    . ILE B 1 76  ? 31.73500 -14.80800 -46.05900 1.000 24.60530  ? 67  ILE B CD1    1 
ATOM   3203 N N      . SER B 1 77  ? 32.77700 -14.97400 -50.83500 1.000 27.85015  ? 68  SER B N      1 
ATOM   3204 C CA     . SER B 1 77  ? 32.10700 -15.97100 -51.65800 1.000 26.87384  ? 68  SER B CA     1 
ATOM   3205 C C      . SER B 1 77  ? 31.47100 -15.25200 -52.84800 1.000 27.66803  ? 68  SER B C      1 
ATOM   3206 O O      . SER B 1 77  ? 31.33800 -14.02500 -52.82600 1.000 29.11601  ? 68  SER B O      1 
ATOM   3207 C CB     . SER B 1 77  ? 31.04100 -16.73600 -50.85400 1.000 26.04803  ? 68  SER B CB     1 
ATOM   3208 O OG     . SER B 1 77  ? 29.93500 -15.90500 -50.54300 1.000 26.21742  ? 68  SER B OG     1 
ATOM   3209 N N      . PRO B 1 78  ? 31.08200 -15.99000 -53.89400 1.000 33.57259  ? 69  PRO B N      1 
ATOM   3210 C CA     . PRO B 1 78  ? 30.44100 -15.33700 -55.05000 1.000 28.48155  ? 69  PRO B CA     1 
ATOM   3211 C C      . PRO B 1 78  ? 29.12200 -14.64800 -54.72600 1.000 27.10244  ? 69  PRO B C      1 
ATOM   3212 O O      . PRO B 1 78  ? 28.63600 -13.87100 -55.55900 1.000 28.85376  ? 69  PRO B O      1 
ATOM   3213 C CB     . PRO B 1 78  ? 30.22900 -16.49200 -56.03800 1.000 24.91396  ? 69  PRO B CB     1 
ATOM   3214 C CG     . PRO B 1 78  ? 31.25000 -17.50500 -55.66000 1.000 31.92446  ? 69  PRO B CG     1 
ATOM   3215 C CD     . PRO B 1 78  ? 31.38100 -17.40800 -54.16600 1.000 31.24182  ? 69  PRO B CD     1 
ATOM   3216 N N      . THR B 1 79  ? 28.53400 -14.89400 -53.55600 1.000 25.07119  ? 70  THR B N      1 
ATOM   3217 C CA     . THR B 1 79  ? 27.22200 -14.36100 -53.21200 1.000 28.33858  ? 70  THR B CA     1 
ATOM   3218 C C      . THR B 1 79  ? 27.27800 -13.27700 -52.14200 1.000 26.39531  ? 70  THR B C      1 
ATOM   3219 O O      . THR B 1 79  ? 26.22700 -12.87400 -51.63100 1.000 28.70552  ? 70  THR B O      1 
ATOM   3220 C CB     . THR B 1 79  ? 26.29900 -15.49300 -52.75000 1.000 31.76971  ? 70  THR B CB     1 
ATOM   3221 O OG1    . THR B 1 79  ? 26.84600 -16.10800 -51.57700 1.000 28.99764  ? 70  THR B OG1    1 
ATOM   3222 C CG2    . THR B 1 79  ? 26.15300 -16.54300 -53.84100 1.000 31.36924  ? 70  THR B CG2    1 
ATOM   3223 N N      . SER B 1 80  ? 28.46600 -12.78600 -51.79700 1.000 25.07013  ? 71  SER B N      1 
ATOM   3224 C CA     . SER B 1 80  ? 28.62700 -11.85700 -50.68500 1.000 27.41364  ? 71  SER B CA     1 
ATOM   3225 C C      . SER B 1 80  ? 28.70200 -10.39700 -51.11300 1.000 28.05680  ? 71  SER B C      1 
ATOM   3226 O O      . SER B 1 80  ? 28.86500 -9.52600  -50.25400 1.000 28.90051  ? 71  SER B O      1 
ATOM   3227 C CB     . SER B 1 80  ? 29.88100 -12.21700 -49.87700 1.000 26.32516  ? 71  SER B CB     1 
ATOM   3228 O OG     . SER B 1 80  ? 31.04300 -12.18500 -50.68600 1.000 32.17032  ? 71  SER B OG     1 
ATOM   3229 N N      . ALA B 1 81  ? 28.57600 -10.10400 -52.40500 1.000 19.69842  ? 72  ALA B N      1 
ATOM   3230 C CA     . ALA B 1 81  ? 28.74100 -8.74500  -52.90300 1.000 19.68680  ? 72  ALA B CA     1 
ATOM   3231 C C      . ALA B 1 81  ? 27.40900 -8.00500  -52.94500 1.000 25.16223  ? 72  ALA B C      1 
ATOM   3232 O O      . ALA B 1 81  ? 26.36200 -8.59300  -53.23100 1.000 19.62779  ? 72  ALA B O      1 
ATOM   3233 C CB     . ALA B 1 81  ? 29.37100 -8.75500  -54.29600 1.000 26.81634  ? 72  ALA B CB     1 
ATOM   3234 N N      . GLY B 1 82  ? 27.46200 -6.70700  -52.65800 1.000 28.78553  ? 73  GLY B N      1 
ATOM   3235 C CA     . GLY B 1 82  ? 26.30300 -5.84100  -52.75300 1.000 24.78963  ? 73  GLY B CA     1 
ATOM   3236 C C      . GLY B 1 82  ? 26.66300 -4.49500  -53.35100 1.000 27.38477  ? 73  GLY B C      1 
ATOM   3237 O O      . GLY B 1 82  ? 25.82400 -3.59400  -53.44200 1.000 26.21398  ? 73  GLY B O      1 
ATOM   3238 N N      . PHE B 1 83  ? 27.91800 -4.35600  -53.75400 1.000 21.21840  ? 74  PHE B N      1 
ATOM   3239 C CA     . PHE B 1 83  ? 28.46700 -3.16200  -54.37400 1.000 19.87921  ? 74  PHE B CA     1 
ATOM   3240 C C      . PHE B 1 83  ? 29.20800 -3.56100  -55.63900 1.000 24.13980  ? 74  PHE B C      1 
ATOM   3241 O O      . PHE B 1 83  ? 29.63600 -4.71200  -55.77900 1.000 24.13710  ? 74  PHE B O      1 
ATOM   3242 C CB     . PHE B 1 83  ? 29.42400 -2.42900  -53.42000 1.000 22.56839  ? 74  PHE B CB     1 
ATOM   3243 C CG     . PHE B 1 83  ? 28.74800 -1.44400  -52.51000 1.000 23.98534  ? 74  PHE B CG     1 
ATOM   3244 C CD1    . PHE B 1 83  ? 28.05800 -1.87400  -51.39000 1.000 19.11248  ? 74  PHE B CD1    1 
ATOM   3245 C CD2    . PHE B 1 83  ? 28.82000 -0.08400  -52.76600 1.000 22.66665  ? 74  PHE B CD2    1 
ATOM   3246 C CE1    . PHE B 1 83  ? 27.44200 -0.96700  -50.54700 1.000 23.43997  ? 74  PHE B CE1    1 
ATOM   3247 C CE2    . PHE B 1 83  ? 28.20800 0.82900   -51.92600 1.000 26.54557  ? 74  PHE B CE2    1 
ATOM   3248 C CZ     . PHE B 1 83  ? 27.51800 0.38500   -50.81500 1.000 24.12407  ? 74  PHE B CZ     1 
ATOM   3249 N N      . PRO B 1 84  ? 29.37700 -2.63600  -56.58300 1.000 21.98027  ? 75  PRO B N      1 
ATOM   3250 C CA     . PRO B 1 84  ? 30.09100 -2.97400  -57.81900 1.000 24.86315  ? 75  PRO B CA     1 
ATOM   3251 C C      . PRO B 1 84  ? 31.60000 -2.93600  -57.63500 1.000 23.75587  ? 75  PRO B C      1 
ATOM   3252 O O      . PRO B 1 84  ? 32.14300 -2.05600  -56.96300 1.000 26.68696  ? 75  PRO B O      1 
ATOM   3253 C CB     . PRO B 1 84  ? 29.62700 -1.88900  -58.79700 1.000 19.99685  ? 75  PRO B CB     1 
ATOM   3254 C CG     . PRO B 1 84  ? 29.36500 -0.71200  -57.92300 1.000 22.00914  ? 75  PRO B CG     1 
ATOM   3255 C CD     . PRO B 1 84  ? 28.83600 -1.26400  -56.61900 1.000 19.69424  ? 75  PRO B CD     1 
ATOM   3256 N N      . HIS B 1 85  ? 32.27100 -3.91600  -58.24100 1.000 23.64902  ? 76  HIS B N      1 
ATOM   3257 C CA     . HIS B 1 85  ? 33.73300 -3.94600  -58.33900 1.000 25.75655  ? 76  HIS B CA     1 
ATOM   3258 C C      . HIS B 1 85  ? 34.39900 -3.85500  -56.96600 1.000 25.73641  ? 76  HIS B C      1 
ATOM   3259 O O      . HIS B 1 85  ? 35.34200 -3.09100  -56.75400 1.000 25.60260  ? 76  HIS B O      1 
ATOM   3260 C CB     . HIS B 1 85  ? 34.23400 -2.84000  -59.27000 1.000 22.73285  ? 76  HIS B CB     1 
ATOM   3261 C CG     . HIS B 1 85  ? 33.56900 -2.83900  -60.61100 1.000 26.09923  ? 76  HIS B CG     1 
ATOM   3262 N ND1    . HIS B 1 85  ? 33.79600 -3.81700  -61.55400 1.000 23.07839  ? 76  HIS B ND1    1 
ATOM   3263 C CD2    . HIS B 1 85  ? 32.67200 -1.98600  -61.16100 1.000 23.17780  ? 76  HIS B CD2    1 
ATOM   3264 C CE1    . HIS B 1 85  ? 33.07200 -3.56400  -62.63100 1.000 27.20136  ? 76  HIS B CE1    1 
ATOM   3265 N NE2    . HIS B 1 85  ? 32.38200 -2.45800  -62.41800 1.000 27.62205  ? 76  HIS B NE2    1 
ATOM   3266 N N      . VAL B 1 86  ? 33.89700 -4.65000  -56.02700 1.000 26.79027  ? 77  VAL B N      1 
ATOM   3267 C CA     . VAL B 1 86  ? 34.51300 -4.76700  -54.70800 1.000 24.88109  ? 77  VAL B CA     1 
ATOM   3268 C C      . VAL B 1 86  ? 35.45900 -5.96000  -54.73900 1.000 25.32106  ? 77  VAL B C      1 
ATOM   3269 O O      . VAL B 1 86  ? 35.13800 -6.98300  -55.36000 1.000 27.06345  ? 77  VAL B O      1 
ATOM   3270 C CB     . VAL B 1 86  ? 33.45600 -4.91000  -53.60200 1.000 26.33876  ? 77  VAL B CB     1 
ATOM   3271 C CG1    . VAL B 1 86  ? 32.71500 -3.60600  -53.43000 1.000 23.74121  ? 77  VAL B CG1    1 
ATOM   3272 C CG2    . VAL B 1 86  ? 32.48400 -6.03600  -53.92900 1.000 21.39555  ? 77  VAL B CG2    1 
ATOM   3273 N N      . PRO B 1 87  ? 36.62500 -5.86700  -54.05800 1.000 23.25441  ? 78  PRO B N      1 
ATOM   3274 C CA     . PRO B 1 87  ? 37.59200 -6.94400  -54.10800 1.000 24.23946  ? 78  PRO B CA     1 
ATOM   3275 C C      . PRO B 1 87  ? 37.14100 -8.23300  -53.46100 1.000 21.62405  ? 78  PRO B C      1 
ATOM   3276 O O      . PRO B 1 87  ? 36.36800 -8.20200  -52.50400 1.000 22.89094  ? 78  PRO B O      1 
ATOM   3277 C CB     . PRO B 1 87  ? 38.79400 -6.31400  -53.38400 1.000 22.02479  ? 78  PRO B CB     1 
ATOM   3278 C CG     . PRO B 1 87  ? 38.16700 -5.42200  -52.36200 1.000 25.19460  ? 78  PRO B CG     1 
ATOM   3279 C CD     . PRO B 1 87  ? 37.06600 -4.78400  -53.17600 1.000 24.40478  ? 78  PRO B CD     1 
ATOM   3280 N N      . GLY B 1 88  ? 37.60600 -9.34800  -54.00600 1.000 26.66924  ? 79  GLY B N      1 
ATOM   3281 C CA     . GLY B 1 88  ? 37.33500 -10.65900 -53.40500 1.000 24.75289  ? 79  GLY B CA     1 
ATOM   3282 C C      . GLY B 1 88  ? 38.61500 -11.27600 -52.88400 1.000 26.33111  ? 79  GLY B C      1 
ATOM   3283 O O      . GLY B 1 88  ? 39.68500 -10.74700 -53.21000 1.000 24.44443  ? 79  GLY B O      1 
ATOM   3284 N N      . ILE B 1 89  ? 38.50400 -12.32400 -52.06500 1.000 28.66157  ? 80  ILE B N      1 
ATOM   3285 C CA     . ILE B 1 89  ? 39.68500 -13.06500 -51.52900 1.000 27.58780  ? 80  ILE B CA     1 
ATOM   3286 C C      . ILE B 1 89  ? 39.28500 -14.55100 -51.44800 1.000 28.24692  ? 80  ILE B C      1 
ATOM   3287 O O      . ILE B 1 89  ? 39.82900 -15.27900 -50.62600 1.000 27.59108  ? 80  ILE B O      1 
ATOM   3288 C CB     . ILE B 1 89  ? 40.18800 -12.46600 -50.20100 1.000 27.56374  ? 80  ILE B CB     1 
ATOM   3289 C CG1    . ILE B 1 89  ? 41.60700 -12.93900 -49.86800 1.000 25.52224  ? 80  ILE B CG1    1 
ATOM   3290 C CG2    . ILE B 1 89  ? 39.21000 -12.73500 -49.05600 1.000 27.57837  ? 80  ILE B CG2    1 
ATOM   3291 C CD1    . ILE B 1 89  ? 42.53900 -11.83600 -49.40600 1.000 24.31831  ? 80  ILE B CD1    1 
ATOM   3292 N N      . PHE B 1 90  ? 38.38000 -14.97700 -52.32600 1.000 29.14564  ? 81  PHE B N      1 
ATOM   3293 C CA     . PHE B 1 90  ? 37.89400 -16.38100 -52.32300 1.000 30.92679  ? 81  PHE B CA     1 
ATOM   3294 C C      . PHE B 1 90  ? 38.43900 -17.14800 -53.53700 1.000 28.83706  ? 81  PHE B C      1 
ATOM   3295 O O      . PHE B 1 90  ? 38.24500 -18.36100 -53.60600 1.000 32.87596  ? 81  PHE B O      1 
ATOM   3296 C CB     . PHE B 1 90  ? 36.36900 -16.32600 -52.20400 1.000 28.00398  ? 81  PHE B CB     1 
ATOM   3297 C CG     . PHE B 1 90  ? 35.62000 -15.64300 -53.33900 1.000 29.67201  ? 81  PHE B CG     1 
ATOM   3298 C CD1    . PHE B 1 90  ? 35.36000 -14.27900 -53.30300 1.000 25.62500  ? 81  PHE B CD1    1 
ATOM   3299 C CD2    . PHE B 1 90  ? 35.15200 -16.37200 -54.42400 1.000 28.68165  ? 81  PHE B CD2    1 
ATOM   3300 C CE1    . PHE B 1 90  ? 34.67300 -13.66400 -54.33300 1.000 24.46224  ? 81  PHE B CE1    1 
ATOM   3301 C CE2    . PHE B 1 90  ? 34.46000 -15.75000 -55.44900 1.000 31.56222  ? 81  PHE B CE2    1 
ATOM   3302 C CZ     . PHE B 1 90  ? 34.22500 -14.39900 -55.40100 1.000 32.68931  ? 81  PHE B CZ     1 
ATOM   3303 N N      . THR B 1 91  ? 39.11200 -16.46000 -54.45000 1.000 27.81985  ? 82  THR B N      1 
ATOM   3304 C CA     . THR B 1 91  ? 39.71900 -17.11600 -55.63000 1.000 30.40917  ? 82  THR B CA     1 
ATOM   3305 C C      . THR B 1 91  ? 41.22500 -17.00500 -55.56000 1.000 30.59165  ? 82  THR B C      1 
ATOM   3306 O O      . THR B 1 91  ? 41.71900 -16.10700 -54.87500 1.000 35.68270  ? 82  THR B O      1 
ATOM   3307 C CB     . THR B 1 91  ? 39.18900 -16.53500 -56.94300 1.000 30.23928  ? 82  THR B CB     1 
ATOM   3308 O OG1    . THR B 1 91  ? 39.96579 -15.37784 -57.22552 1.000 31.12349  ? 82  THR B OG1    1 
ATOM   3309 C CG2    . THR B 1 91  ? 37.71196 -16.19000 -56.87909 1.000 33.26393  ? 82  THR B CG2    1 
ATOM   3310 N N      . LYS B 1 92  ? 41.92200 -17.87300 -56.27700 1.000 29.83277  ? 83  LYS B N      1 
ATOM   3311 C CA     . LYS B 1 92  ? 43.40100 -17.86800 -56.29800 1.000 33.46886  ? 83  LYS B CA     1 
ATOM   3312 C C      . LYS B 1 92  ? 43.92700 -16.66600 -57.08700 1.000 34.62075  ? 83  LYS B C      1 
ATOM   3313 O O      . LYS B 1 92  ? 45.00300 -16.16600 -56.73900 1.000 36.24847  ? 83  LYS B O      1 
ATOM   3314 C CB     . LYS B 1 92  ? 43.88100 -19.17900 -56.92200 1.000 35.95897  ? 83  LYS B CB     1 
ATOM   3315 N N      . GLU B 1 93  ? 43.20500 -16.24400 -58.11800 1.000 32.32752  ? 84  GLU B N      1 
ATOM   3316 C CA     . GLU B 1 93  ? 43.61700 -15.03600 -58.87000 1.000 35.56953  ? 84  GLU B CA     1 
ATOM   3317 C C      . GLU B 1 93  ? 43.49200 -13.81500 -57.94400 1.000 32.19673  ? 84  GLU B C      1 
ATOM   3318 O O      . GLU B 1 93  ? 44.38300 -12.95900 -57.97400 1.000 35.79876  ? 84  GLU B O      1 
ATOM   3319 C CB     . GLU B 1 93  ? 42.82600 -14.89600 -60.16900 1.000 32.58717  ? 84  GLU B CB     1 
ATOM   3320 C CG     . GLU B 1 93  ? 43.04700 -13.56000 -60.87000 1.000 38.55049  ? 84  GLU B CG     1 
ATOM   3321 C CD     . GLU B 1 93  ? 42.29000 -13.34300 -62.16800 1.000 49.22127  ? 84  GLU B CD     1 
ATOM   3322 O OE1    . GLU B 1 93  ? 41.27600 -14.02500 -62.41200 1.000 56.63058  ? 84  GLU B OE1    1 
ATOM   3323 O OE2    . GLU B 1 93  ? 42.72700 -12.47400 -62.94400 1.000 52.46839  ? 84  GLU B OE2    1 
ATOM   3324 N N      . GLN B 1 94  ? 42.43600 -13.76400 -57.13500 1.000 32.30573  ? 85  GLN B N      1 
ATOM   3325 C CA     . GLN B 1 94  ? 42.32600 -12.64300 -56.20800 1.000 35.18117  ? 85  GLN B CA     1 
ATOM   3326 C C      . GLN B 1 94  ? 43.43700 -12.66800 -55.16700 1.000 28.41825  ? 85  GLN B C      1 
ATOM   3327 O O      . GLN B 1 94  ? 43.92000 -11.60800 -54.75100 1.000 23.54990  ? 85  GLN B O      1 
ATOM   3328 C CB     . GLN B 1 94  ? 40.95700 -12.65600 -55.52900 1.000 30.15978  ? 85  GLN B CB     1 
ATOM   3329 C CG     . GLN B 1 94  ? 39.79500 -12.37300 -56.47000 1.000 29.71998  ? 85  GLN B CG     1 
ATOM   3330 C CD     . GLN B 1 94  ? 38.47000 -12.87700 -55.92800 1.000 30.63569  ? 85  GLN B CD     1 
ATOM   3331 O OE1    . GLN B 1 94  ? 38.42000 -13.53000 -54.88500 1.000 27.87164  ? 85  GLN B OE1    1 
ATOM   3332 N NE2    . GLN B 1 94  ? 37.38900 -12.58000 -56.63900 1.000 27.48536  ? 85  GLN B NE2    1 
ATOM   3333 N N      . VAL B 1 95  ? 43.85600 -13.86100 -54.74100 1.000 27.31814  ? 86  VAL B N      1 
ATOM   3334 C CA     . VAL B 1 95  ? 44.95600 -13.96800 -53.78800 1.000 27.67469  ? 86  VAL B CA     1 
ATOM   3335 C C      . VAL B 1 95  ? 46.25000 -13.45300 -54.40600 1.000 29.45388  ? 86  VAL B C      1 
ATOM   3336 O O      . VAL B 1 95  ? 47.00300 -12.70800 -53.76600 1.000 27.69738  ? 86  VAL B O      1 
ATOM   3337 C CB     . VAL B 1 95  ? 45.09600 -15.42100 -53.29700 1.000 30.31355  ? 86  VAL B CB     1 
ATOM   3338 C CG1    . VAL B 1 95  ? 46.38700 -15.60000 -52.51400 1.000 25.82843  ? 86  VAL B CG1    1 
ATOM   3339 C CG2    . VAL B 1 95  ? 43.89700 -15.80700 -52.44400 1.000 27.20477  ? 86  VAL B CG2    1 
ATOM   3340 N N      . ARG B 1 96  ? 46.52200 -13.82400 -55.66100 1.000 29.10557  ? 87  ARG B N      1 
ATOM   3341 C CA     . ARG B 1 96  ? 47.76700 -13.40800 -56.30400 1.000 33.37882  ? 87  ARG B CA     1 
ATOM   3342 C C      . ARG B 1 96  ? 47.85200 -11.89200 -56.42500 1.000 29.86165  ? 87  ARG B C      1 
ATOM   3343 O O      . ARG B 1 96  ? 48.92300 -11.30600 -56.22400 1.000 27.90286  ? 87  ARG B O      1 
ATOM   3344 C CB     . ARG B 1 96  ? 47.90000 -14.06800 -57.67900 1.000 37.44918  ? 87  ARG B CB     1 
ATOM   3345 C CG     . ARG B 1 96  ? 48.17500 -15.56500 -57.62200 1.000 42.47315  ? 87  ARG B CG     1 
ATOM   3346 C CD     . ARG B 1 96  ? 48.57400 -16.13100 -58.98200 1.000 50.73826  ? 87  ARG B CD     1 
ATOM   3347 N NE     . ARG B 1 96  ? 47.44100 -16.68700 -59.71400 1.000 49.83875  ? 87  ARG B NE     1 
ATOM   3348 C CZ     . ARG B 1 96  ? 46.81300 -16.07400 -60.70900 1.000 53.79828  ? 87  ARG B CZ     1 
ATOM   3349 N NH1    . ARG B 1 96  ? 47.18200 -14.87300 -61.12600 1.000 44.88952  ? 87  ARG B NH1    1 
ATOM   3350 N NH2    . ARG B 1 96  ? 45.79000 -16.68400 -61.30300 1.000 41.73499  ? 87  ARG B NH2    1 
ATOM   3351 N N      . GLU B 1 97  ? 46.73400 -11.23700 -56.74100 1.000 23.35187  ? 88  GLU B N      1 
ATOM   3352 C CA     . GLU B 1 97  ? 46.73800 -9.78500  -56.88200 1.000 26.50547  ? 88  GLU B CA     1 
ATOM   3353 C C      . GLU B 1 97  ? 46.80600 -9.08500  -55.53000 1.000 27.49908  ? 88  GLU B C      1 
ATOM   3354 O O      . GLU B 1 97  ? 47.42800 -8.02200  -55.41300 1.000 27.07721  ? 88  GLU B O      1 
ATOM   3355 C CB     . GLU B 1 97  ? 45.50700 -9.32900  -57.66500 1.000 29.77378  ? 88  GLU B CB     1 
ATOM   3356 C CG     . GLU B 1 97  ? 45.40500 -9.94800  -59.04700 1.000 34.88128  ? 88  GLU B CG     1 
ATOM   3357 C CD     . GLU B 1 97  ? 46.67200 -9.76400  -59.85900 1.000 39.50500  ? 88  GLU B CD     1 
ATOM   3358 O OE1    . GLU B 1 97  ? 47.22200 -8.64200  -59.86600 1.000 38.17220  ? 88  GLU B OE1    1 
ATOM   3359 O OE2    . GLU B 1 97  ? 47.12500 -10.74700 -60.48200 1.000 43.52874  ? 88  GLU B OE2    1 
ATOM   3360 N N      . TRP B 1 98  ? 46.17000 -9.65300  -54.50200 1.000 22.20442  ? 89  TRP B N      1 
ATOM   3361 C CA     . TRP B 1 98  ? 46.28800 -9.08000  -53.16300 1.000 24.64975  ? 89  TRP B CA     1 
ATOM   3362 C C      . TRP B 1 98  ? 47.73500 -9.08300  -52.68600 1.000 24.59164  ? 89  TRP B C      1 
ATOM   3363 O O      . TRP B 1 98  ? 48.16700 -8.16200  -51.98300 1.000 26.42742  ? 89  TRP B O      1 
ATOM   3364 C CB     . TRP B 1 98  ? 45.41700 -9.85200  -52.17000 1.000 21.45112  ? 89  TRP B CB     1 
ATOM   3365 C CG     . TRP B 1 98  ? 44.01400 -9.34600  -52.01900 1.000 22.22168  ? 89  TRP B CG     1 
ATOM   3366 C CD1    . TRP B 1 98  ? 42.86600 -10.04600 -52.24400 1.000 23.16900  ? 89  TRP B CD1    1 
ATOM   3367 C CD2    . TRP B 1 98  ? 43.60900 -8.03700  -51.59700 1.000 21.12316  ? 89  TRP B CD2    1 
ATOM   3368 N NE1    . TRP B 1 98  ? 41.77100 -9.25600  -51.99300 1.000 21.05685  ? 89  TRP B NE1    1 
ATOM   3369 C CE2    . TRP B 1 98  ? 42.20000 -8.01700  -51.59500 1.000 20.60378  ? 89  TRP B CE2    1 
ATOM   3370 C CE3    . TRP B 1 98  ? 44.29900 -6.87900  -51.22700 1.000 23.08240  ? 89  TRP B CE3    1 
ATOM   3371 C CZ2    . TRP B 1 98  ? 41.46800 -6.88700  -51.23500 1.000 19.62776  ? 89  TRP B CZ2    1 
ATOM   3372 C CZ3    . TRP B 1 98  ? 43.57100 -5.75600  -50.86700 1.000 21.35612  ? 89  TRP B CZ3    1 
ATOM   3373 C CH2    . TRP B 1 98  ? 42.17000 -5.76900  -50.87500 1.000 24.03292  ? 89  TRP B CH2    1 
ATOM   3374 N N      . LYS B 1 99  ? 48.49700 -10.11200 -53.06200 1.000 25.15085  ? 90  LYS B N      1 
ATOM   3375 C CA     . LYS B 1 99  ? 49.87100 -10.24400 -52.58900 1.000 30.77564  ? 90  LYS B CA     1 
ATOM   3376 C C      . LYS B 1 99  ? 50.73000 -9.06700  -53.03800 1.000 29.74085  ? 90  LYS B C      1 
ATOM   3377 O O      . LYS B 1 99  ? 51.53700 -8.54700  -52.25900 1.000 30.99477  ? 90  LYS B O      1 
ATOM   3378 C CB     . LYS B 1 99  ? 50.45800 -11.56800 -53.08300 1.000 32.41197  ? 90  LYS B CB     1 
ATOM   3379 C CG     . LYS B 1 99  ? 51.68300 -12.03300 -52.31800 1.000 44.10362  ? 90  LYS B CG     1 
ATOM   3380 C CD     . LYS B 1 99  ? 52.02400 -13.47300 -52.66800 1.000 45.90572  ? 90  LYS B CD     1 
ATOM   3381 C CE     . LYS B 1 99  ? 50.83400 -14.39200 -52.42600 1.000 46.89099  ? 90  LYS B CE     1 
ATOM   3382 N NZ     . LYS B 1 99  ? 51.13000 -15.81400 -52.75800 1.000 53.50368  ? 90  LYS B NZ     1 
ATOM   3383 N N      . LYS B 1 100 ? 50.56900 -8.63200  -54.29000 1.000 28.85641  ? 91  LYS B N      1 
ATOM   3384 C CA     . LYS B 1 100 ? 51.31500 -7.47300  -54.77000 1.000 31.58320  ? 91  LYS B CA     1 
ATOM   3385 C C      . LYS B 1 100 ? 50.93800 -6.21200  -54.00600 1.000 34.32490  ? 91  LYS B C      1 
ATOM   3386 O O      . LYS B 1 100 ? 51.78600 -5.34000  -53.78500 1.000 33.72589  ? 91  LYS B O      1 
ATOM   3387 C CB     . LYS B 1 100 ? 51.07000 -7.27600  -56.26600 1.000 34.01350  ? 91  LYS B CB     1 
ATOM   3388 C CG     . LYS B 1 100 ? 51.26000 -8.53400  -57.09900 1.000 30.43512  ? 91  LYS B CG     1 
ATOM   3389 C CD     . LYS B 1 100 ? 50.76600 -8.33000  -58.52300 1.000 34.03660  ? 91  LYS B CD     1 
ATOM   3390 C CE     . LYS B 1 100 ? 50.82100 -9.62700  -59.31600 1.000 41.77817  ? 91  LYS B CE     1 
ATOM   3391 N NZ     . LYS B 1 100 ? 50.25800 -9.46700  -60.68600 1.000 45.90390  ? 91  LYS B NZ     1 
ATOM   3392 N N      . ILE B 1 101 ? 49.67400 -6.10100  -53.59300 1.000 27.27699  ? 92  ILE B N      1 
ATOM   3393 C CA     . ILE B 1 101 ? 49.23200 -4.93700  -52.83300 1.000 30.32747  ? 92  ILE B CA     1 
ATOM   3394 C C      . ILE B 1 101 ? 49.78700 -4.97900  -51.41500 1.000 27.29802  ? 92  ILE B C      1 
ATOM   3395 O O      . ILE B 1 101 ? 50.24300 -3.96000  -50.88200 1.000 25.91141  ? 92  ILE B O      1 
ATOM   3396 C CB     . ILE B 1 101 ? 47.69500 -4.85900  -52.84300 1.000 30.60775  ? 92  ILE B CB     1 
ATOM   3397 C CG1    . ILE B 1 101 ? 47.19300 -4.65400  -54.27400 1.000 29.23147  ? 92  ILE B CG1    1 
ATOM   3398 C CG2    . ILE B 1 101 ? 47.20100 -3.75200  -51.92200 1.000 27.31273  ? 92  ILE B CG2    1 
ATOM   3399 C CD1    . ILE B 1 101 ? 45.69500 -4.67600  -54.40200 1.000 27.32893  ? 92  ILE B CD1    1 
ATOM   3400 N N      . VAL B 1 102 ? 49.76600 -6.15500  -50.78400 1.000 24.70724  ? 93  VAL B N      1 
ATOM   3401 C CA     . VAL B 1 102 ? 50.26700 -6.27500  -49.41900 1.000 29.04193  ? 93  VAL B CA     1 
ATOM   3402 C C      . VAL B 1 102 ? 51.78100 -6.08900  -49.38200 1.000 34.27637  ? 93  VAL B C      1 
ATOM   3403 O O      . VAL B 1 102 ? 52.32300 -5.49500  -48.44100 1.000 30.84209  ? 93  VAL B O      1 
ATOM   3404 C CB     . VAL B 1 102 ? 49.84000 -7.62500  -48.81300 1.000 26.41323  ? 93  VAL B CB     1 
ATOM   3405 C CG1    . VAL B 1 102 ? 50.45300 -7.81300  -47.43800 1.000 28.88555  ? 93  VAL B CG1    1 
ATOM   3406 C CG2    . VAL B 1 102 ? 48.32200 -7.71100  -48.73100 1.000 23.79419  ? 93  VAL B CG2    1 
ATOM   3407 N N      . ASP B 1 103 ? 52.48800 -6.58400  -50.40300 1.000 28.04874  ? 94  ASP B N      1 
ATOM   3408 C CA     . ASP B 1 103 ? 53.94000 -6.41900  -50.44600 1.000 33.24411  ? 94  ASP B CA     1 
ATOM   3409 C C      . ASP B 1 103 ? 54.32900 -4.94800  -50.51200 1.000 29.28226  ? 94  ASP B C      1 
ATOM   3410 O O      . ASP B 1 103 ? 55.30200 -4.52500  -49.87700 1.000 30.94195  ? 94  ASP B O      1 
ATOM   3411 C CB     . ASP B 1 103 ? 54.52500 -7.17800  -51.63700 1.000 34.13239  ? 94  ASP B CB     1 
ATOM   3412 C CG     . ASP B 1 103 ? 54.49700 -8.68300  -51.44600 1.000 34.25197  ? 94  ASP B CG     1 
ATOM   3413 O OD1    . ASP B 1 103 ? 54.14300 -9.14200  -50.33900 1.000 40.09110  ? 94  ASP B OD1    1 
ATOM   3414 O OD2    . ASP B 1 103 ? 54.83100 -9.40800  -52.40700 1.000 39.87861  ? 94  ASP B OD2    1 
ATOM   3415 N N      . VAL B 1 104 ? 53.57900 -4.15200  -51.27700 1.000 29.43000  ? 95  VAL B N      1 
ATOM   3416 C CA     . VAL B 1 104 ? 53.85600 -2.72200  -51.36100 1.000 26.79915  ? 95  VAL B CA     1 
ATOM   3417 C C      . VAL B 1 104 ? 53.55200 -2.03800  -50.03200 1.000 28.73916  ? 95  VAL B C      1 
ATOM   3418 O O      . VAL B 1 104 ? 54.29400 -1.15300  -49.58900 1.000 30.44247  ? 95  VAL B O      1 
ATOM   3419 C CB     . VAL B 1 104 ? 53.06200 -2.09900  -52.52400 1.000 29.50150  ? 95  VAL B CB     1 
ATOM   3420 C CG1    . VAL B 1 104 ? 52.88836 -0.60537  -52.32071 1.000 40.11129  ? 95  VAL B CG1    1 
ATOM   3421 C CG2    . VAL B 1 104 ? 53.76362 -2.37468  -53.84654 1.000 34.67992  ? 95  VAL B CG2    1 
ATOM   3422 N N      . VAL B 1 105 ? 52.46800 -2.44600  -49.36900 1.000 28.13731  ? 96  VAL B N      1 
ATOM   3423 C CA     . VAL B 1 105 ? 52.12000 -1.86100  -48.07700 1.000 29.93925  ? 96  VAL B CA     1 
ATOM   3424 C C      . VAL B 1 105 ? 53.15200 -2.23600  -47.02100 1.000 27.56918  ? 96  VAL B C      1 
ATOM   3425 O O      . VAL B 1 105 ? 53.59200 -1.38800  -46.23400 1.000 28.24549  ? 96  VAL B O      1 
ATOM   3426 C CB     . VAL B 1 105 ? 50.70200 -2.29300  -47.66200 1.000 28.84127  ? 96  VAL B CB     1 
ATOM   3427 C CG1    . VAL B 1 105 ? 50.42100 -1.88900  -46.22300 1.000 27.74608  ? 96  VAL B CG1    1 
ATOM   3428 C CG2    . VAL B 1 105 ? 49.67100 -1.69000  -48.60200 1.000 24.26805  ? 96  VAL B CG2    1 
ATOM   3429 N N      . HIS B 1 106 ? 53.55400 -3.50900  -46.98300 1.000 26.61727  ? 97  HIS B N      1 
ATOM   3430 C CA     . HIS B 1 106 ? 54.55900 -3.93800  -46.01600 1.000 30.03721  ? 97  HIS B CA     1 
ATOM   3431 C C      . HIS B 1 106 ? 55.91200 -3.28900  -46.28000 1.000 30.14217  ? 97  HIS B C      1 
ATOM   3432 O O      . HIS B 1 106 ? 56.70300 -3.11000  -45.34600 1.000 34.11973  ? 97  HIS B O      1 
ATOM   3433 C CB     . HIS B 1 106 ? 54.68700 -5.46100  -46.03100 1.000 28.21724  ? 97  HIS B CB     1 
ATOM   3434 C CG     . HIS B 1 106 ? 53.64100 -6.16300  -45.22200 1.000 33.30723  ? 97  HIS B CG     1 
ATOM   3435 N ND1    . HIS B 1 106 ? 53.30700 -7.48500  -45.42200 1.000 33.51824  ? 97  HIS B ND1    1 
ATOM   3436 C CD2    . HIS B 1 106 ? 52.86100 -5.72800  -44.20400 1.000 31.43727  ? 97  HIS B CD2    1 
ATOM   3437 C CE1    . HIS B 1 106 ? 52.36500 -7.83300  -44.56400 1.000 33.70742  ? 97  HIS B CE1    1 
ATOM   3438 N NE2    . HIS B 1 106 ? 52.07600 -6.78500  -43.81400 1.000 33.98092  ? 97  HIS B NE2    1 
ATOM   3439 N N      . ALA B 1 107 ? 56.19400 -2.92500  -47.53300 1.000 27.04154  ? 98  ALA B N      1 
ATOM   3440 C CA     . ALA B 1 107 ? 57.45300 -2.26300  -47.85100 1.000 26.84917  ? 98  ALA B CA     1 
ATOM   3441 C C      . ALA B 1 107 ? 57.55400 -0.87900  -47.22300 1.000 29.47538  ? 98  ALA B C      1 
ATOM   3442 O O      . ALA B 1 107 ? 58.66600 -0.37100  -47.05200 1.000 26.93232  ? 98  ALA B O      1 
ATOM   3443 C CB     . ALA B 1 107 ? 57.63200 -2.16500  -49.36700 1.000 28.18285  ? 98  ALA B CB     1 
ATOM   3444 N N      . LYS B 1 108 ? 56.42700 -0.25900  -46.87900 1.000 28.30719  ? 99  LYS B N      1 
ATOM   3445 C CA     . LYS B 1 108 ? 56.43700 1.01200   -46.16800 1.000 30.27310  ? 99  LYS B CA     1 
ATOM   3446 C C      . LYS B 1 108 ? 56.37600 0.84600   -44.65500 1.000 28.62264  ? 99  LYS B C      1 
ATOM   3447 O O      . LYS B 1 108 ? 56.30900 1.85100   -43.93900 1.000 28.73679  ? 99  LYS B O      1 
ATOM   3448 C CB     . LYS B 1 108 ? 55.27600 1.89600   -46.63700 1.000 30.62407  ? 99  LYS B CB     1 
ATOM   3449 C CG     . LYS B 1 108 ? 55.28104 2.18093   -48.13027 1.000 40.23557  ? 99  LYS B CG     1 
ATOM   3450 C CD     . LYS B 1 108 ? 54.57960 3.49297   -48.43899 1.000 40.29349  ? 99  LYS B CD     1 
ATOM   3451 C CE     . LYS B 1 108 ? 55.57704 4.61845   -48.66033 1.000 45.53098  ? 99  LYS B CE     1 
ATOM   3452 N NZ     . LYS B 1 108 ? 55.41548 5.26474   -49.99174 1.000 57.03302  ? 99  LYS B NZ     1 
ATOM   3453 N N      . GLY B 1 109 ? 56.39700 -0.38600  -44.15300 1.000 32.28050  ? 100 GLY B N      1 
ATOM   3454 C CA     . GLY B 1 109 ? 56.42400 -0.61000  -42.72100 1.000 29.69441  ? 100 GLY B CA     1 
ATOM   3455 C C      . GLY B 1 109 ? 55.08400 -0.51800  -42.02800 1.000 27.89833  ? 100 GLY B C      1 
ATOM   3456 O O      . GLY B 1 109 ? 55.03100 -0.17200  -40.84400 1.000 38.92983  ? 100 GLY B O      1 
ATOM   3457 N N      . ALA B 1 110 ? 53.99700 -0.82500  -42.72700 1.000 29.41599  ? 101 ALA B N      1 
ATOM   3458 C CA     . ALA B 1 110 ? 52.65800 -0.74200  -42.16700 1.000 26.68528  ? 101 ALA B CA     1 
ATOM   3459 C C      . ALA B 1 110 ? 52.08800 -2.13300  -41.92500 1.000 26.22715  ? 101 ALA B C      1 
ATOM   3460 O O      . ALA B 1 110 ? 52.51600 -3.12200  -42.52600 1.000 28.01010  ? 101 ALA B O      1 
ATOM   3461 C CB     . ALA B 1 110 ? 51.72400 0.04900   -43.09000 1.000 27.98929  ? 101 ALA B CB     1 
ATOM   3462 N N      . VAL B 1 111 ? 51.11100 -2.19200  -41.02500 1.000 24.90223  ? 102 VAL B N      1 
ATOM   3463 C CA     . VAL B 1 111 ? 50.34500 -3.40100  -40.74600 1.000 24.43294  ? 102 VAL B CA     1 
ATOM   3464 C C      . VAL B 1 111 ? 48.98400 -3.25500  -41.40900 1.000 25.79238  ? 102 VAL B C      1 
ATOM   3465 O O      . VAL B 1 111 ? 48.35200 -2.19500  -41.31900 1.000 28.22161  ? 102 VAL B O      1 
ATOM   3466 C CB     . VAL B 1 111 ? 50.20800 -3.63200  -39.22800 1.000 32.12155  ? 102 VAL B CB     1 
ATOM   3467 C CG1    . VAL B 1 111 ? 49.34800 -4.85400  -38.94000 1.000 24.40883  ? 102 VAL B CG1    1 
ATOM   3468 C CG2    . VAL B 1 111 ? 51.58400 -3.77400  -38.58500 1.000 23.38784  ? 102 VAL B CG2    1 
ATOM   3469 N N      . ILE B 1 112 ? 48.52800 -4.30900  -42.08400 1.000 24.52558  ? 103 ILE B N      1 
ATOM   3470 C CA     . ILE B 1 112 ? 47.30100 -4.24000  -42.87100 1.000 25.37162  ? 103 ILE B CA     1 
ATOM   3471 C C      . ILE B 1 112 ? 46.45900 -5.48600  -42.61700 1.000 24.96579  ? 103 ILE B C      1 
ATOM   3472 O O      . ILE B 1 112 ? 46.96600 -6.61200  -42.66900 1.000 22.05786  ? 103 ILE B O      1 
ATOM   3473 C CB     . ILE B 1 112 ? 47.60100 -4.06400  -44.37600 1.000 22.63154  ? 103 ILE B CB     1 
ATOM   3474 C CG1    . ILE B 1 112 ? 46.30500 -3.98000  -45.18600 1.000 22.11820  ? 103 ILE B CG1    1 
ATOM   3475 C CG2    . ILE B 1 112 ? 48.50900 -5.17400  -44.89800 1.000 26.11112  ? 103 ILE B CG2    1 
ATOM   3476 C CD1    . ILE B 1 112 ? 46.52300 -3.56200  -46.63100 1.000 21.16521  ? 103 ILE B CD1    1 
ATOM   3477 N N      . PHE B 1 113 ? 45.17700 -5.27800  -42.32500 1.000 22.67655  ? 104 PHE B N      1 
ATOM   3478 C CA     . PHE B 1 113 ? 44.19900 -6.34600  -42.17800 1.000 23.24398  ? 104 PHE B CA     1 
ATOM   3479 C C      . PHE B 1 113 ? 43.18200 -6.27600  -43.31000 1.000 25.14227  ? 104 PHE B C      1 
ATOM   3480 O O      . PHE B 1 113 ? 42.83900 -5.19300  -43.79300 1.000 24.42912  ? 104 PHE B O      1 
ATOM   3481 C CB     . PHE B 1 113 ? 43.45500 -6.26000  -40.83900 1.000 26.06104  ? 104 PHE B CB     1 
ATOM   3482 C CG     . PHE B 1 113 ? 44.20600 -6.84300  -39.67300 1.000 21.87698  ? 104 PHE B CG     1 
ATOM   3483 C CD1    . PHE B 1 113 ? 45.58800 -6.92000  -39.67700 1.000 29.31532  ? 104 PHE B CD1    1 
ATOM   3484 C CD2    . PHE B 1 113 ? 43.51700 -7.31700  -38.56800 1.000 27.58886  ? 104 PHE B CD2    1 
ATOM   3485 C CE1    . PHE B 1 113 ? 46.26900 -7.45400  -38.59700 1.000 27.50583  ? 104 PHE B CE1    1 
ATOM   3486 C CE2    . PHE B 1 113 ? 44.19100 -7.85400  -37.48800 1.000 29.45775  ? 104 PHE B CE2    1 
ATOM   3487 C CZ     . PHE B 1 113 ? 45.56900 -7.92400  -37.50300 1.000 28.16932  ? 104 PHE B CZ     1 
ATOM   3488 N N      . CYS B 1 114 ? 42.68500 -7.43900  -43.71500 1.000 22.35022  ? 105 CYS B N      1 
ATOM   3489 C CA     . CYS B 1 114 ? 41.67000 -7.53700  -44.75500 1.000 23.03264  ? 105 CYS B CA     1 
ATOM   3490 C C      . CYS B 1 114 ? 40.30800 -7.76100  -44.10900 1.000 23.04417  ? 105 CYS B C      1 
ATOM   3491 O O      . CYS B 1 114 ? 40.12000 -8.73300  -43.37000 1.000 20.91113  ? 105 CYS B O      1 
ATOM   3492 C CB     . CYS B 1 114 ? 41.99500 -8.66800  -45.72900 1.000 21.25712  ? 105 CYS B CB     1 
ATOM   3493 S SG     . CYS B 1 114 ? 40.71000 -8.94600  -46.96700 1.000 25.13062  ? 105 CYS B SG     1 
ATOM   3494 N N      . GLN B 1 115 ? 39.36100 -6.87000  -44.38900 1.000 24.39193  ? 106 GLN B N      1 
ATOM   3495 C CA     . GLN B 1 115 ? 38.02600 -6.98800  -43.81600 1.000 25.32311  ? 106 GLN B CA     1 
ATOM   3496 C C      . GLN B 1 115 ? 37.19700 -7.96000  -44.64700 1.000 26.84646  ? 106 GLN B C      1 
ATOM   3497 O O      . GLN B 1 115 ? 37.00300 -7.75200  -45.85000 1.000 22.36118  ? 106 GLN B O      1 
ATOM   3498 C CB     . GLN B 1 115 ? 37.33800 -5.62700  -43.74200 1.000 23.33542  ? 106 GLN B CB     1 
ATOM   3499 C CG     . GLN B 1 115 ? 36.02900 -5.66100  -42.95600 1.000 24.75361  ? 106 GLN B CG     1 
ATOM   3500 C CD     . GLN B 1 115 ? 35.20200 -4.39800  -43.11400 1.000 23.18907  ? 106 GLN B CD     1 
ATOM   3501 O OE1    . GLN B 1 115 ? 34.96900 -3.92900  -44.22700 1.000 23.75198  ? 106 GLN B OE1    1 
ATOM   3502 N NE2    . GLN B 1 115 ? 34.75300 -3.84200  -41.99500 1.000 22.11535  ? 106 GLN B NE2    1 
ATOM   3503 N N      . LEU B 1 116 ? 36.71000 -9.02000  -44.00400 1.000 27.21606  ? 107 LEU B N      1 
ATOM   3504 C CA     . LEU B 1 116 ? 35.86000 -10.00900 -44.65400 1.000 21.51261  ? 107 LEU B CA     1 
ATOM   3505 C C      . LEU B 1 116 ? 34.41100 -9.54600  -44.55700 1.000 21.29051  ? 107 LEU B C      1 
ATOM   3506 O O      . LEU B 1 116 ? 33.88600 -9.36600  -43.45300 1.000 25.43026  ? 107 LEU B O      1 
ATOM   3507 C CB     . LEU B 1 116 ? 36.04500 -11.38100 -44.00900 1.000 20.64396  ? 107 LEU B CB     1 
ATOM   3508 C CG     . LEU B 1 116 ? 37.49400 -11.86400 -43.90800 1.000 24.42531  ? 107 LEU B CG     1 
ATOM   3509 C CD1    . LEU B 1 116 ? 37.55000 -13.30400 -43.42600 1.000 19.35886  ? 107 LEU B CD1    1 
ATOM   3510 C CD2    . LEU B 1 116 ? 38.21500 -11.70900 -45.24300 1.000 21.58522  ? 107 LEU B CD2    1 
ATOM   3511 N N      . TRP B 1 117 ? 33.76600 -9.36600  -45.70800 1.000 21.02040  ? 108 TRP B N      1 
ATOM   3512 C CA     . TRP B 1 117 ? 32.50100 -8.64600  -45.79400 1.000 21.13018  ? 108 TRP B CA     1 
ATOM   3513 C C      . TRP B 1 117 ? 31.49200 -9.45400  -46.59600 1.000 25.83404  ? 108 TRP B C      1 
ATOM   3514 O O      . TRP B 1 117 ? 31.71200 -9.72900  -47.78100 1.000 24.67990  ? 108 TRP B O      1 
ATOM   3515 C CB     . TRP B 1 117 ? 32.72100 -7.27200  -46.43600 1.000 22.12976  ? 108 TRP B CB     1 
ATOM   3516 C CG     . TRP B 1 117 ? 31.48300 -6.44800  -46.61900 1.000 24.55344  ? 108 TRP B CG     1 
ATOM   3517 C CD1    . TRP B 1 117 ? 30.35300 -6.47100  -45.85400 1.000 18.30131  ? 108 TRP B CD1    1 
ATOM   3518 C CD2    . TRP B 1 117 ? 31.25400 -5.47500  -47.64400 1.000 21.53508  ? 108 TRP B CD2    1 
ATOM   3519 N NE1    . TRP B 1 117 ? 29.43700 -5.56800  -46.33800 1.000 21.73185  ? 108 TRP B NE1    1 
ATOM   3520 C CE2    . TRP B 1 117 ? 29.96700 -4.94400  -47.43700 1.000 22.46680  ? 108 TRP B CE2    1 
ATOM   3521 C CE3    . TRP B 1 117 ? 32.01600 -5.00000  -48.71800 1.000 23.35534  ? 108 TRP B CE3    1 
ATOM   3522 C CZ2    . TRP B 1 117 ? 29.42200 -3.96400  -48.26500 1.000 25.66596  ? 108 TRP B CZ2    1 
ATOM   3523 C CZ3    . TRP B 1 117 ? 31.47600 -4.02400  -49.53600 1.000 23.71944  ? 108 TRP B CZ3    1 
ATOM   3524 C CH2    . TRP B 1 117 ? 30.19200 -3.51700  -49.30500 1.000 28.89705  ? 108 TRP B CH2    1 
ATOM   3525 N N      . HIS B 1 118 ? 30.38600 -9.82200  -45.95300 1.000 22.46731  ? 109 HIS B N      1 
ATOM   3526 C CA     . HIS B 1 118 ? 29.24000 -10.43000 -46.61900 1.000 23.95926  ? 109 HIS B CA     1 
ATOM   3527 C C      . HIS B 1 118 ? 28.04500 -9.50700  -46.42700 1.000 24.21830  ? 109 HIS B C      1 
ATOM   3528 O O      . HIS B 1 118 ? 27.70200 -9.16100  -45.29100 1.000 26.35403  ? 109 HIS B O      1 
ATOM   3529 C CB     . HIS B 1 118 ? 28.94800 -11.82700 -46.06300 1.000 23.75620  ? 109 HIS B CB     1 
ATOM   3530 C CG     . HIS B 1 118 ? 28.04200 -12.64700 -46.93000 1.000 23.69940  ? 109 HIS B CG     1 
ATOM   3531 N ND1    . HIS B 1 118 ? 26.79600 -12.21400 -47.32700 1.000 25.91785  ? 109 HIS B ND1    1 
ATOM   3532 C CD2    . HIS B 1 118 ? 28.19900 -13.88000 -47.46800 1.000 27.77800  ? 109 HIS B CD2    1 
ATOM   3533 C CE1    . HIS B 1 118 ? 26.22700 -13.14000 -48.07800 1.000 25.74430  ? 109 HIS B CE1    1 
ATOM   3534 N NE2    . HIS B 1 118 ? 27.05800 -14.16100 -48.17900 1.000 26.79586  ? 109 HIS B NE2    1 
ATOM   3535 N N      . VAL B 1 119 ? 27.41500 -9.10700  -47.53300 1.000 22.80403  ? 110 VAL B N      1 
ATOM   3536 C CA     . VAL B 1 119 ? 26.36100 -8.09900  -47.46700 1.000 22.50287  ? 110 VAL B CA     1 
ATOM   3537 C C      . VAL B 1 119 ? 25.01600 -8.67100  -47.04100 1.000 22.36370  ? 110 VAL B C      1 
ATOM   3538 O O      . VAL B 1 119 ? 24.13900 -7.91000  -46.61300 1.000 24.55911  ? 110 VAL B O      1 
ATOM   3539 C CB     . VAL B 1 119 ? 26.19600 -7.38600  -48.81800 1.000 24.96525  ? 110 VAL B CB     1 
ATOM   3540 C CG1    . VAL B 1 119 ? 27.48100 -6.68300  -49.20100 1.000 23.55869  ? 110 VAL B CG1    1 
ATOM   3541 C CG2    . VAL B 1 119 ? 25.77900 -8.37900  -49.89600 1.000 22.00351  ? 110 VAL B CG2    1 
ATOM   3542 N N      . GLY B 1 120 ? 24.82100 -9.97800  -47.15100 1.000 22.24682  ? 111 GLY B N      1 
ATOM   3543 C CA     . GLY B 1 120 ? 23.53100 -10.54500 -46.79700 1.000 23.30598  ? 111 GLY B CA     1 
ATOM   3544 C C      . GLY B 1 120 ? 22.44800 -10.05400 -47.73800 1.000 25.48341  ? 111 GLY B C      1 
ATOM   3545 O O      . GLY B 1 120 ? 22.58400 -10.11300 -48.96500 1.000 20.43737  ? 111 GLY B O      1 
ATOM   3546 N N      . ARG B 1 121 ? 21.35100 -9.55700  -47.16000 1.000 25.78283  ? 112 ARG B N      1 
ATOM   3547 C CA     . ARG B 1 121 ? 20.22700 -9.09100  -47.96300 1.000 30.10389  ? 112 ARG B CA     1 
ATOM   3548 C C      . ARG B 1 121 ? 20.49400 -7.75400  -48.64100 1.000 26.91671  ? 112 ARG B C      1 
ATOM   3549 O O      . ARG B 1 121 ? 19.67600 -7.32000  -49.45800 1.000 23.33469  ? 112 ARG B O      1 
ATOM   3550 C CB     . ARG B 1 121 ? 18.96800 -8.98600  -47.10000 1.000 26.10770  ? 112 ARG B CB     1 
ATOM   3551 C CG     . ARG B 1 121 ? 19.00600 -7.88200  -46.05600 1.000 28.21715  ? 112 ARG B CG     1 
ATOM   3552 C CD     . ARG B 1 121 ? 17.69200 -7.81000  -45.29500 1.000 24.38507  ? 112 ARG B CD     1 
ATOM   3553 N NE     . ARG B 1 121 ? 17.65800 -6.69700  -44.35400 1.000 24.46342  ? 112 ARG B NE     1 
ATOM   3554 C CZ     . ARG B 1 121 ? 16.57000 -6.29100  -43.71400 1.000 21.78101  ? 112 ARG B CZ     1 
ATOM   3555 N NH1    . ARG B 1 121 ? 15.40300 -6.88900  -43.88500 1.000 21.02896  ? 112 ARG B NH1    1 
ATOM   3556 N NH2    . ARG B 1 121 ? 16.65400 -5.25400  -42.88500 1.000 25.72015  ? 112 ARG B NH2    1 
ATOM   3557 N N      . ALA B 1 122 ? 21.61100 -7.09800  -48.33200 1.000 24.86696  ? 113 ALA B N      1 
ATOM   3558 C CA     . ALA B 1 122 ? 21.94400 -5.82400  -48.95500 1.000 21.51707  ? 113 ALA B CA     1 
ATOM   3559 C C      . ALA B 1 122 ? 22.59000 -6.03700  -50.31700 1.000 28.41176  ? 113 ALA B C      1 
ATOM   3560 O O      . ALA B 1 122 ? 23.66700 -5.50500  -50.59400 1.000 25.90687  ? 113 ALA B O      1 
ATOM   3561 C CB     . ALA B 1 122 ? 22.87100 -5.01400  -48.04900 1.000 24.44016  ? 113 ALA B CB     1 
ATOM   3562 N N      . SER B 1 123 ? 21.94200 -6.81500  -51.17600 1.000 27.07184  ? 114 SER B N      1 
ATOM   3563 C CA     . SER B 1 123 ? 22.46700 -7.07400  -52.51100 1.000 27.38304  ? 114 SER B CA     1 
ATOM   3564 C C      . SER B 1 123 ? 21.39600 -6.89900  -53.57700 1.000 25.79679  ? 114 SER B C      1 
ATOM   3565 O O      . SER B 1 123 ? 20.34300 -6.30700  -53.32400 1.000 27.82201  ? 114 SER B O      1 
ATOM   3566 C CB     . SER B 1 123 ? 23.06200 -8.47200  -52.60500 1.000 27.17075  ? 114 SER B CB     1 
ATOM   3567 O OG     . SER B 1 123 ? 23.76200 -8.63800  -53.82600 1.000 16.79311  ? 114 SER B OG     1 
ATOM   3568 N N      . HIS B 1 124 ? 21.67200 -7.39200  -54.78100 1.000 25.29179  ? 115 HIS B N      1 
ATOM   3569 C CA     . HIS B 1 124 ? 20.75100 -7.26500  -55.90000 1.000 25.05600  ? 115 HIS B CA     1 
ATOM   3570 C C      . HIS B 1 124 ? 21.02000 -8.41300  -56.86100 1.000 25.20051  ? 115 HIS B C      1 
ATOM   3571 O O      . HIS B 1 124 ? 22.09500 -9.01800  -56.84300 1.000 25.58013  ? 115 HIS B O      1 
ATOM   3572 C CB     . HIS B 1 124 ? 20.90900 -5.90800  -56.59300 1.000 24.85582  ? 115 HIS B CB     1 
ATOM   3573 C CG     . HIS B 1 124 ? 19.84400 -5.60700  -57.59800 1.000 31.27618  ? 115 HIS B CG     1 
ATOM   3574 N ND1    . HIS B 1 124 ? 19.90400 -6.05500  -58.89900 1.000 30.16783  ? 115 HIS B ND1    1 
ATOM   3575 C CD2    . HIS B 1 124 ? 18.70500 -4.88200  -57.50000 1.000 27.64199  ? 115 HIS B CD2    1 
ATOM   3576 C CE1    . HIS B 1 124 ? 18.84200 -5.62800  -59.55800 1.000 27.15119  ? 115 HIS B CE1    1 
ATOM   3577 N NE2    . HIS B 1 124 ? 18.09900 -4.91300  -58.73200 1.000 28.84786  ? 115 HIS B NE2    1 
ATOM   3578 N N      . GLU B 1 125 ? 20.01600 -8.71700  -57.68900 1.000 25.60641  ? 116 GLU B N      1 
ATOM   3579 C CA     . GLU B 1 125 ? 20.15600 -9.78700  -58.67200 1.000 28.20407  ? 116 GLU B CA     1 
ATOM   3580 C C      . GLU B 1 125 ? 21.35100 -9.55800  -59.58500 1.000 25.17259  ? 116 GLU B C      1 
ATOM   3581 O O      . GLU B 1 125 ? 22.00500 -10.52100 -59.99900 1.000 28.67136  ? 116 GLU B O      1 
ATOM   3582 C CB     . GLU B 1 125 ? 18.87500 -9.91100  -59.49900 1.000 27.29132  ? 116 GLU B CB     1 
ATOM   3583 N N      . VAL B 1 126 ? 21.65600 -8.29800  -59.90500 1.000 24.72877  ? 117 VAL B N      1 
ATOM   3584 C CA     . VAL B 1 126 ? 22.78900 -8.00200  -60.77400 1.000 28.27055  ? 117 VAL B CA     1 
ATOM   3585 C C      . VAL B 1 126 ? 24.11500 -8.33200  -60.09800 1.000 26.89399  ? 117 VAL B C      1 
ATOM   3586 O O      . VAL B 1 126 ? 25.12500 -8.53500  -60.78300 1.000 23.99652  ? 117 VAL B O      1 
ATOM   3587 C CB     . VAL B 1 126 ? 22.74300 -6.52600  -61.22100 1.000 24.45389  ? 117 VAL B CB     1 
ATOM   3588 C CG1    . VAL B 1 126 ? 23.10300 -5.60000  -60.06400 1.000 22.51765  ? 117 VAL B CG1    1 
ATOM   3589 C CG2    . VAL B 1 126 ? 23.65400 -6.29300  -62.41900 1.000 21.19827  ? 117 VAL B CG2    1 
ATOM   3590 N N      . TYR B 1 127 ? 24.13700 -8.40700  -58.76800 1.000 23.20506  ? 118 TYR B N      1 
ATOM   3591 C CA     . TYR B 1 127 ? 25.34200 -8.73700  -58.02200 1.000 24.25823  ? 118 TYR B CA     1 
ATOM   3592 C C      . TYR B 1 127 ? 25.43200 -10.21100 -57.65100 1.000 26.29356  ? 118 TYR B C      1 
ATOM   3593 O O      . TYR B 1 127 ? 26.47600 -10.64300 -57.15000 1.000 24.99305  ? 118 TYR B O      1 
ATOM   3594 C CB     . TYR B 1 127 ? 25.42100 -7.88700  -56.74600 1.000 22.87220  ? 118 TYR B CB     1 
ATOM   3595 C CG     . TYR B 1 127 ? 25.58800 -6.40800  -57.00800 1.000 23.16535  ? 118 TYR B CG     1 
ATOM   3596 C CD1    . TYR B 1 127 ? 26.53400 -5.94800  -57.91600 1.000 25.84149  ? 118 TYR B CD1    1 
ATOM   3597 C CD2    . TYR B 1 127 ? 24.79200 -5.47200  -56.36100 1.000 23.00768  ? 118 TYR B CD2    1 
ATOM   3598 C CE1    . TYR B 1 127 ? 26.69000 -4.59900  -58.16400 1.000 23.55433  ? 118 TYR B CE1    1 
ATOM   3599 C CE2    . TYR B 1 127 ? 24.94000 -4.11800  -56.60300 1.000 25.68440  ? 118 TYR B CE2    1 
ATOM   3600 C CZ     . TYR B 1 127 ? 25.89100 -3.68800  -57.50700 1.000 26.29649  ? 118 TYR B CZ     1 
ATOM   3601 O OH     . TYR B 1 127 ? 26.04500 -2.34300  -57.75600 1.000 22.61889  ? 118 TYR B OH     1 
ATOM   3602 N N      . GLN B 1 128 ? 24.37100 -10.99300 -57.88700 1.000 23.33157  ? 119 GLN B N      1 
ATOM   3603 C CA     . GLN B 1 128 ? 24.36800 -12.38500 -57.47300 1.000 26.44626  ? 119 GLN B CA     1 
ATOM   3604 C C      . GLN B 1 128 ? 24.56700 -13.30900 -58.66800 1.000 31.13832  ? 119 GLN B C      1 
ATOM   3605 O O      . GLN B 1 128 ? 24.15400 -12.98800 -59.78700 1.000 29.92141  ? 119 GLN B O      1 
ATOM   3606 C CB     . GLN B 1 128 ? 23.05200 -12.73400 -56.77200 1.000 28.12844  ? 119 GLN B CB     1 
ATOM   3607 C CG     . GLN B 1 128 ? 22.82500 -11.98400 -55.46700 1.000 28.90674  ? 119 GLN B CG     1 
ATOM   3608 C CD     . GLN B 1 128 ? 23.84200 -12.34700 -54.40100 1.000 24.82219  ? 119 GLN B CD     1 
ATOM   3609 O OE1    . GLN B 1 128 ? 24.10800 -13.52400 -54.15700 1.000 27.66036  ? 119 GLN B OE1    1 
ATOM   3610 N NE2    . GLN B 1 128 ? 24.42300 -11.33700 -53.76600 1.000 27.01601  ? 119 GLN B NE2    1 
ATOM   3611 N N      . PRO B 1 129 ? 25.21100 -14.45600 -58.45800 1.000 31.24857  ? 120 PRO B N      1 
ATOM   3612 C CA     . PRO B 1 129 ? 25.38800 -15.41600 -59.55600 1.000 37.55113  ? 120 PRO B CA     1 
ATOM   3613 C C      . PRO B 1 129 ? 24.04500 -15.90800 -60.07700 1.000 40.98564  ? 120 PRO B C      1 
ATOM   3614 O O      . PRO B 1 129 ? 23.14900 -16.25400 -59.30300 1.000 35.14496  ? 120 PRO B O      1 
ATOM   3615 C CB     . PRO B 1 129 ? 26.19600 -16.54800 -58.91000 1.000 34.73038  ? 120 PRO B CB     1 
ATOM   3616 C CG     . PRO B 1 129 ? 26.87800 -15.91000 -57.74300 1.000 30.15520  ? 120 PRO B CG     1 
ATOM   3617 C CD     . PRO B 1 129 ? 25.91700 -14.87700 -57.23600 1.000 34.91170  ? 120 PRO B CD     1 
ATOM   3618 N N      . ALA B 1 130 ? 23.91300 -15.92300 -61.40400 1.000 37.53953  ? 121 ALA B N      1 
ATOM   3619 C CA     . ALA B 1 130 ? 22.70400 -16.36300 -62.10000 1.000 41.27986  ? 121 ALA B CA     1 
ATOM   3620 C C      . ALA B 1 130 ? 21.47400 -15.54700 -61.71200 1.000 40.27565  ? 121 ALA B C      1 
ATOM   3621 O O      . ALA B 1 130 ? 20.34200 -16.01600 -61.86800 1.000 40.16633  ? 121 ALA B O      1 
ATOM   3622 C CB     . ALA B 1 130 ? 22.44000 -17.85600 -61.87000 1.000 34.44807  ? 121 ALA B CB     1 
ATOM   3623 N N      . GLY B 1 131 ? 21.67200 -14.32900 -61.21100 1.000 42.33986  ? 122 GLY B N      1 
ATOM   3624 C CA     . GLY B 1 131 ? 20.55400 -13.49500 -60.81300 1.000 37.86854  ? 122 GLY B CA     1 
ATOM   3625 C C      . GLY B 1 131 ? 19.74100 -14.03600 -59.66000 1.000 37.53925  ? 122 GLY B C      1 
ATOM   3626 O O      . GLY B 1 131 ? 18.58600 -13.63800 -59.48600 1.000 36.99303  ? 122 GLY B O      1 
ATOM   3627 N N      . ALA B 1 132 ? 20.31100 -14.93700 -58.86200 1.000 31.68827  ? 123 ALA B N      1 
ATOM   3628 C CA     . ALA B 1 132 ? 19.58100 -15.52500 -57.75200 1.000 32.61580  ? 123 ALA B CA     1 
ATOM   3629 C C      . ALA B 1 132 ? 19.36200 -14.49100 -56.64700 1.000 34.89097  ? 123 ALA B C      1 
ATOM   3630 O O      . ALA B 1 132 ? 19.97800 -13.42200 -56.62000 1.000 32.12461  ? 123 ALA B O      1 
ATOM   3631 C CB     . ALA B 1 132 ? 20.32700 -16.74000 -57.20400 1.000 29.74273  ? 123 ALA B CB     1 
ATOM   3632 N N      . ALA B 1 133 ? 18.46500 -14.82400 -55.72700 1.000 30.20716  ? 124 ALA B N      1 
ATOM   3633 C CA     . ALA B 1 133 ? 18.17200 -13.91600 -54.62800 1.000 31.69004  ? 124 ALA B CA     1 
ATOM   3634 C C      . ALA B 1 133 ? 19.29700 -13.95500 -53.59500 1.000 31.43897  ? 124 ALA B C      1 
ATOM   3635 O O      . ALA B 1 133 ? 19.89100 -15.01100 -53.36400 1.000 29.44962  ? 124 ALA B O      1 
ATOM   3636 C CB     . ALA B 1 133 ? 16.84600 -14.28400 -53.96500 1.000 26.48499  ? 124 ALA B CB     1 
ATOM   3637 N N      . PRO B 1 134 ? 19.61600 -12.82400 -52.97200 1.000 27.73386  ? 125 PRO B N      1 
ATOM   3638 C CA     . PRO B 1 134 ? 20.62500 -12.82800 -51.90900 1.000 27.75062  ? 125 PRO B CA     1 
ATOM   3639 C C      . PRO B 1 134 ? 20.13300 -13.58200 -50.68300 1.000 26.50791  ? 125 PRO B C      1 
ATOM   3640 O O      . PRO B 1 134 ? 18.93600 -13.80100 -50.48600 1.000 27.73538  ? 125 PRO B O      1 
ATOM   3641 C CB     . PRO B 1 134 ? 20.83200 -11.34000 -51.60400 1.000 26.35780  ? 125 PRO B CB     1 
ATOM   3642 C CG     . PRO B 1 134 ? 19.56900 -10.68300 -52.05800 1.000 29.01061  ? 125 PRO B CG     1 
ATOM   3643 C CD     . PRO B 1 134 ? 19.09900 -11.47200 -53.24600 1.000 26.16567  ? 125 PRO B CD     1 
ATOM   3644 N N      . ILE B 1 135 ? 21.08800 -13.98800 -49.85300 1.000 21.77455  ? 126 ILE B N      1 
ATOM   3645 C CA     . ILE B 1 135 ? 20.79900 -14.77000 -48.66100 1.000 25.72472  ? 126 ILE B CA     1 
ATOM   3646 C C      . ILE B 1 135 ? 20.78100 -13.84700 -47.45200 1.000 27.48594  ? 126 ILE B C      1 
ATOM   3647 O O      . ILE B 1 135 ? 21.40300 -12.78300 -47.43700 1.000 28.74072  ? 126 ILE B O      1 
ATOM   3648 C CB     . ILE B 1 135 ? 21.81900 -15.91200 -48.46600 1.000 21.19562  ? 126 ILE B CB     1 
ATOM   3649 C CG1    . ILE B 1 135 ? 23.20000 -15.34400 -48.13300 1.000 21.10968  ? 126 ILE B CG1    1 
ATOM   3650 C CG2    . ILE B 1 135 ? 21.87900 -16.78200 -49.70500 1.000 23.85151  ? 126 ILE B CG2    1 
ATOM   3651 C CD1    . ILE B 1 135 ? 24.14500 -16.36000 -47.53500 1.000 25.91841  ? 126 ILE B CD1    1 
ATOM   3652 N N      . SER B 1 136 ? 20.06500 -14.26500 -46.41500 1.000 29.29831  ? 127 SER B N      1 
ATOM   3653 C CA     . SER B 1 136 ? 19.96300 -13.49200 -45.18100 1.000 25.59597  ? 127 SER B CA     1 
ATOM   3654 C C      . SER B 1 136 ? 19.38500 -14.39300 -44.09800 1.000 30.30875  ? 127 SER B C      1 
ATOM   3655 O O      . SER B 1 136 ? 19.04700 -15.55500 -44.34100 1.000 27.83151  ? 127 SER B O      1 
ATOM   3656 C CB     . SER B 1 136 ? 19.10100 -12.24000 -45.36700 1.000 28.73561  ? 127 SER B CB     1 
ATOM   3657 O OG     . SER B 1 136 ? 19.00600 -11.51100 -44.15500 1.000 26.03146  ? 127 SER B OG     1 
ATOM   3658 N N      . SER B 1 137 ? 19.27900 -13.83800 -42.88900 1.000 25.45822  ? 128 SER B N      1 
ATOM   3659 C CA     . SER B 1 137 ? 18.61200 -14.53700 -41.79900 1.000 28.41292  ? 128 SER B CA     1 
ATOM   3660 C C      . SER B 1 137 ? 17.10100 -14.56000 -41.97200 1.000 25.88962  ? 128 SER B C      1 
ATOM   3661 O O      . SER B 1 137 ? 16.44000 -15.44900 -41.42700 1.000 28.18100  ? 128 SER B O      1 
ATOM   3662 C CB     . SER B 1 137 ? 18.96400 -13.87800 -40.46500 1.000 26.02876  ? 128 SER B CB     1 
ATOM   3663 O OG     . SER B 1 137 ? 18.54200 -12.52400 -40.45200 1.000 25.45791  ? 128 SER B OG     1 
ATOM   3664 N N      . THR B 1 138 ? 16.54600 -13.61000 -42.72000 1.000 24.42157  ? 129 THR B N      1 
ATOM   3665 C CA     . THR B 1 138 ? 15.11000 -13.44500 -42.88000 1.000 24.56286  ? 129 THR B CA     1 
ATOM   3666 C C      . THR B 1 138 ? 14.75900 -13.45600 -44.36200 1.000 28.31630  ? 129 THR B C      1 
ATOM   3667 O O      . THR B 1 138 ? 15.63200 -13.51300 -45.23200 1.000 26.75008  ? 129 THR B O      1 
ATOM   3668 C CB     . THR B 1 138 ? 14.63100 -12.14000 -42.23100 1.000 28.93583  ? 129 THR B CB     1 
ATOM   3669 O OG1    . THR B 1 138 ? 13.23500 -11.95600 -42.49700 1.000 27.87501  ? 129 THR B OG1    1 
ATOM   3670 C CG2    . THR B 1 138 ? 15.40900 -10.95400 -42.78800 1.000 27.00923  ? 129 THR B CG2    1 
ATOM   3671 N N      . GLU B 1 139 ? 13.45900 -13.40400 -44.64500 1.000 28.55043  ? 130 GLU B N      1 
ATOM   3672 C CA     . GLU B 1 139 ? 12.96100 -13.21100 -45.99900 1.000 32.17551  ? 130 GLU B CA     1 
ATOM   3673 C C      . GLU B 1 139 ? 12.45100 -11.79800 -46.23400 1.000 28.75256  ? 130 GLU B C      1 
ATOM   3674 O O      . GLU B 1 139 ? 12.07200 -11.46900 -47.36200 1.000 32.09721  ? 130 GLU B O      1 
ATOM   3675 C CB     . GLU B 1 139 ? 11.84800 -14.21700 -46.30900 1.000 34.59185  ? 130 GLU B CB     1 
ATOM   3676 C CG     . GLU B 1 139 ? 12.32000 -15.65800 -46.37200 1.000 44.78510  ? 130 GLU B CG     1 
ATOM   3677 C CD     . GLU B 1 139 ? 11.27100 -16.59000 -46.94300 1.000 55.18496  ? 130 GLU B CD     1 
ATOM   3678 O OE1    . GLU B 1 139 ? 10.07600 -16.22800 -46.92200 1.000 55.30635  ? 130 GLU B OE1    1 
ATOM   3679 O OE2    . GLU B 1 139 ? 11.64400 -17.68400 -47.41800 1.000 56.53743  ? 130 GLU B OE2    1 
ATOM   3680 N N      . LYS B 1 140 ? 12.43100 -10.96000 -45.19900 1.000 28.03528  ? 131 LYS B N      1 
ATOM   3681 C CA     . LYS B 1 140 ? 11.97800 -9.58300  -45.33300 1.000 28.80069  ? 131 LYS B CA     1 
ATOM   3682 C C      . LYS B 1 140 ? 13.05200 -8.74100  -46.01800 1.000 32.10188  ? 131 LYS B C      1 
ATOM   3683 O O      . LYS B 1 140 ? 14.23900 -8.86600  -45.69900 1.000 29.18544  ? 131 LYS B O      1 
ATOM   3684 C CB     . LYS B 1 140 ? 11.64800 -8.98900  -43.96400 1.000 26.73829  ? 131 LYS B CB     1 
ATOM   3685 N N      . PRO B 1 141 ? 12.67000 -7.88100  -46.95500 1.000 31.87160  ? 132 PRO B N      1 
ATOM   3686 C CA     . PRO B 1 141 ? 13.64800 -7.03300  -47.63300 1.000 27.37441  ? 132 PRO B CA     1 
ATOM   3687 C C      . PRO B 1 141 ? 13.87000 -5.71800  -46.89900 1.000 26.36079  ? 132 PRO B C      1 
ATOM   3688 O O      . PRO B 1 141 ? 13.07700 -5.29700  -46.05400 1.000 31.33601  ? 132 PRO B O      1 
ATOM   3689 C CB     . PRO B 1 141 ? 13.00200 -6.79100  -49.00500 1.000 25.20291  ? 132 PRO B CB     1 
ATOM   3690 C CG     . PRO B 1 141 ? 11.50900 -6.98500  -48.77900 1.000 27.83590  ? 132 PRO B CG     1 
ATOM   3691 C CD     . PRO B 1 141 ? 11.29800 -7.60800  -47.41600 1.000 31.55006  ? 132 PRO B CD     1 
ATOM   3692 N N      . ILE B 1 142 ? 14.99100 -5.07700  -47.23600 1.000 28.49961  ? 133 ILE B N      1 
ATOM   3693 C CA     . ILE B 1 142 ? 15.25500 -3.73500  -46.73600 1.000 29.27872  ? 133 ILE B CA     1 
ATOM   3694 C C      . ILE B 1 142 ? 14.15200 -2.80300  -47.21600 1.000 28.99866  ? 133 ILE B C      1 
ATOM   3695 O O      . ILE B 1 142 ? 13.71900 -2.86500  -48.37400 1.000 28.06145  ? 133 ILE B O      1 
ATOM   3696 C CB     . ILE B 1 142 ? 16.64400 -3.26300  -47.19700 1.000 27.07314  ? 133 ILE B CB     1 
ATOM   3697 C CG1    . ILE B 1 142 ? 17.72200 -4.22800  -46.69600 1.000 26.52753  ? 133 ILE B CG1    1 
ATOM   3698 C CG2    . ILE B 1 142 ? 16.92600 -1.85000  -46.70800 1.000 25.46668  ? 133 ILE B CG2    1 
ATOM   3699 C CD1    . ILE B 1 142 ? 19.10000 -3.95800  -47.26200 1.000 28.58754  ? 133 ILE B CD1    1 
ATOM   3700 N N      . SER B 1 143 ? 13.68400 -1.93800  -46.31700 1.000 28.87964  ? 134 SER B N      1 
ATOM   3701 C CA     . SER B 1 143 ? 12.52800 -1.10000  -46.59900 1.000 30.57739  ? 134 SER B CA     1 
ATOM   3702 C C      . SER B 1 143 ? 12.80700 -0.15100  -47.76500 1.000 32.34711  ? 134 SER B C      1 
ATOM   3703 O O      . SER B 1 143 ? 13.94400 0.03400   -48.20700 1.000 27.77616  ? 134 SER B O      1 
ATOM   3704 C CB     . SER B 1 143 ? 12.12700 -0.30500  -45.35700 1.000 33.17547  ? 134 SER B CB     1 
ATOM   3705 O OG     . SER B 1 143 ? 13.19500 0.50800   -44.90200 1.000 39.32289  ? 134 SER B OG     1 
ATOM   3706 N N      . ASN B 1 144 ? 11.73000 0.46600   -48.25500 1.000 35.44439  ? 135 ASN B N      1 
ATOM   3707 C CA     . ASN B 1 144 ? 11.78300 1.32300   -49.43300 1.000 35.12416  ? 135 ASN B CA     1 
ATOM   3708 C C      . ASN B 1 144 ? 12.54900 2.61900   -49.19500 1.000 34.32489  ? 135 ASN B C      1 
ATOM   3709 O O      . ASN B 1 144 ? 12.86400 3.31700   -50.16500 1.000 35.49672  ? 135 ASN B O      1 
ATOM   3710 C CB     . ASN B 1 144 ? 10.35900 1.63200   -49.90000 1.000 36.77294  ? 135 ASN B CB     1 
ATOM   3711 C CG     . ASN B 1 144 ? 10.31700 2.23400   -51.28800 1.000 42.13924  ? 135 ASN B CG     1 
ATOM   3712 O OD1    . ASN B 1 144 ? 10.09500 3.43400   -51.45100 1.000 47.65587  ? 135 ASN B OD1    1 
ATOM   3713 N ND2    . ASN B 1 144 ? 10.53500 1.40200   -52.30000 1.000 41.74149  ? 135 ASN B ND2    1 
ATOM   3714 N N      . ARG B 1 145 ? 12.85900 2.95600   -47.94100 1.000 35.20045  ? 136 ARG B N      1 
ATOM   3715 C CA     . ARG B 1 145 ? 13.61200 4.17200   -47.65900 1.000 31.37494  ? 136 ARG B CA     1 
ATOM   3716 C C      . ARG B 1 145 ? 15.06500 4.07500   -48.10600 1.000 32.85518  ? 136 ARG B C      1 
ATOM   3717 O O      . ARG B 1 145 ? 15.71800 5.10900   -48.27900 1.000 33.81673  ? 136 ARG B O      1 
ATOM   3718 C CB     . ARG B 1 145 ? 13.55000 4.49400   -46.16500 1.000 33.61471  ? 136 ARG B CB     1 
ATOM   3719 N N      . TRP B 1 146 ? 15.58400 2.86600   -48.29600 1.000 33.34152  ? 137 TRP B N      1 
ATOM   3720 C CA     . TRP B 1 146 ? 16.96100 2.65400   -48.71800 1.000 33.25962  ? 137 TRP B CA     1 
ATOM   3721 C C      . TRP B 1 146 ? 16.99000 2.13400   -50.14900 1.000 30.81503  ? 137 TRP B C      1 
ATOM   3722 O O      . TRP B 1 146 ? 16.13100 1.34300   -50.55000 1.000 28.39356  ? 137 TRP B O      1 
ATOM   3723 C CB     . TRP B 1 146 ? 17.67300 1.66700   -47.78900 1.000 28.33568  ? 137 TRP B CB     1 
ATOM   3724 C CG     . TRP B 1 146 ? 17.51800 1.99100   -46.33300 1.000 32.88608  ? 137 TRP B CG     1 
ATOM   3725 C CD1    . TRP B 1 146 ? 16.52100 1.56800   -45.50300 1.000 32.05839  ? 137 TRP B CD1    1 
ATOM   3726 C CD2    . TRP B 1 146 ? 18.38700 2.80300   -45.53500 1.000 34.26247  ? 137 TRP B CD2    1 
ATOM   3727 N NE1    . TRP B 1 146 ? 16.71400 2.06700   -44.23800 1.000 35.53555  ? 137 TRP B NE1    1 
ATOM   3728 C CE2    . TRP B 1 146 ? 17.85300 2.82900   -44.23100 1.000 41.34777  ? 137 TRP B CE2    1 
ATOM   3729 C CE3    . TRP B 1 146 ? 19.56500 3.51000   -45.79500 1.000 39.69038  ? 137 TRP B CE3    1 
ATOM   3730 C CZ2    . TRP B 1 146 ? 18.45600 3.53400   -43.19000 1.000 36.61088  ? 137 TRP B CZ2    1 
ATOM   3731 C CZ3    . TRP B 1 146 ? 20.16200 4.21000   -44.76000 1.000 35.29687  ? 137 TRP B CZ3    1 
ATOM   3732 C CH2    . TRP B 1 146 ? 19.60600 4.21700   -43.47500 1.000 34.95427  ? 137 TRP B CH2    1 
ATOM   3733 N N      . ARG B 1 147 ? 17.98200 2.58500   -50.91600 1.000 29.12766  ? 138 ARG B N      1 
ATOM   3734 C CA     . ARG B 1 147 ? 18.17100 2.15800   -52.29600 1.000 26.84681  ? 138 ARG B CA     1 
ATOM   3735 C C      . ARG B 1 147 ? 19.60700 1.69700   -52.48900 1.000 25.66474  ? 138 ARG B C      1 
ATOM   3736 O O      . ARG B 1 147 ? 20.53300 2.25900   -51.89600 1.000 23.15100  ? 138 ARG B O      1 
ATOM   3737 C CB     . ARG B 1 147 ? 17.84500 3.28800   -53.28300 1.000 32.66595  ? 138 ARG B CB     1 
ATOM   3738 C CG     . ARG B 1 147 ? 16.44200 3.85600   -53.13300 1.000 39.27401  ? 138 ARG B CG     1 
ATOM   3739 C CD     . ARG B 1 147 ? 15.38400 2.79200   -53.37900 1.000 40.95496  ? 138 ARG B CD     1 
ATOM   3740 N NE     . ARG B 1 147 ? 14.05400 3.24800   -52.99400 1.000 47.85412  ? 138 ARG B NE     1 
ATOM   3741 C CZ     . ARG B 1 147 ? 13.23100 3.91700   -53.79100 1.000 51.51407  ? 138 ARG B CZ     1 
ATOM   3742 N NH1    . ARG B 1 147 ? 13.57100 4.22700   -55.03100 1.000 54.53191  ? 138 ARG B NH1    1 
ATOM   3743 N NH2    . ARG B 1 147 ? 12.03800 4.28300   -53.33100 1.000 48.36081  ? 138 ARG B NH2    1 
ATOM   3744 N N      . ILE B 1 148 ? 19.79000 0.67800   -53.32200 1.000 28.61799  ? 139 ILE B N      1 
ATOM   3745 C CA     . ILE B 1 148 ? 21.10800 0.10600   -53.57200 1.000 24.96094  ? 139 ILE B CA     1 
ATOM   3746 C C      . ILE B 1 148 ? 21.70300 0.74500   -54.81900 1.000 28.09715  ? 139 ILE B C      1 
ATOM   3747 O O      . ILE B 1 148 ? 20.99100 1.05000   -55.78300 1.000 26.74375  ? 139 ILE B O      1 
ATOM   3748 C CB     . ILE B 1 148 ? 21.02500 -1.42800  -53.70700 1.000 24.98005  ? 139 ILE B CB     1 
ATOM   3749 C CG1    . ILE B 1 148 ? 22.42700 -2.04000  -53.76700 1.000 27.33118  ? 139 ILE B CG1    1 
ATOM   3750 C CG2    . ILE B 1 148 ? 20.19800 -1.82900  -54.92300 1.000 27.12706  ? 139 ILE B CG2    1 
ATOM   3751 C CD1    . ILE B 1 148 ? 22.43300 -3.55100  -53.83600 1.000 23.67376  ? 139 ILE B CD1    1 
ATOM   3752 N N      . LEU B 1 149 ? 23.01600 0.96300   -54.79400 1.000 25.88636  ? 140 LEU B N      1 
ATOM   3753 C CA     . LEU B 1 149 ? 23.72500 1.50400   -55.94500 1.000 28.63844  ? 140 LEU B CA     1 
ATOM   3754 C C      . LEU B 1 149 ? 23.92000 0.41800   -56.99600 1.000 25.59578  ? 140 LEU B C      1 
ATOM   3755 O O      . LEU B 1 149 ? 24.42400 -0.66800  -56.69400 1.000 28.16896  ? 140 LEU B O      1 
ATOM   3756 C CB     . LEU B 1 149 ? 25.07600 2.07800   -55.51600 1.000 20.59202  ? 140 LEU B CB     1 
ATOM   3757 C CG     . LEU B 1 149 ? 26.00100 2.57500   -56.62800 1.000 28.38405  ? 140 LEU B CG     1 
ATOM   3758 C CD1    . LEU B 1 149 ? 25.36800 3.73400   -57.38500 1.000 24.60768  ? 140 LEU B CD1    1 
ATOM   3759 C CD2    . LEU B 1 149 ? 27.35500 2.97300   -56.06000 1.000 28.88099  ? 140 LEU B CD2    1 
ATOM   3760 N N      . MET B 1 150 ? 23.52100 0.71300   -58.23000 1.000 28.89324  ? 141 MET B N      1 
ATOM   3761 C CA     . MET B 1 150 ? 23.61400 -0.21900  -59.34300 1.000 28.96429  ? 141 MET B CA     1 
ATOM   3762 C C      . MET B 1 150 ? 24.91800 -0.01500  -60.10500 1.000 24.40771  ? 141 MET B C      1 
ATOM   3763 O O      . MET B 1 150 ? 25.54400 1.04500   -60.01300 1.000 25.20390  ? 141 MET B O      1 
ATOM   3764 C CB     . MET B 1 150 ? 22.41500 -0.03500  -60.27500 1.000 28.35601  ? 141 MET B CB     1 
ATOM   3765 C CG     . MET B 1 150 ? 21.07390 -0.36133  -59.62876 1.000 29.79360  ? 141 MET B CG     1 
ATOM   3766 S SD     . MET B 1 150 ? 20.92791 -2.08711  -59.11676 1.000 33.85024  ? 141 MET B SD     1 
ATOM   3767 C CE     . MET B 1 150 ? 20.67423 -2.88826  -60.70056 1.000 33.16069  ? 141 MET B CE     1 
ATOM   3768 N N      . PRO B 1 151 ? 25.36900 -1.02200  -60.86000 1.000 24.79196  ? 142 PRO B N      1 
ATOM   3769 C CA     . PRO B 1 151 ? 26.65500 -0.88700  -61.56700 1.000 24.68734  ? 142 PRO B CA     1 
ATOM   3770 C C      . PRO B 1 151 ? 26.69600 0.24100   -62.58600 1.000 28.25763  ? 142 PRO B C      1 
ATOM   3771 O O      . PRO B 1 151 ? 27.79500 0.66000   -62.97000 1.000 28.22911  ? 142 PRO B O      1 
ATOM   3772 C CB     . PRO B 1 151 ? 26.82900 -2.25300  -62.24400 1.000 21.93153  ? 142 PRO B CB     1 
ATOM   3773 C CG     . PRO B 1 151 ? 26.02200 -3.18900  -61.41200 1.000 24.08662  ? 142 PRO B CG     1 
ATOM   3774 C CD     . PRO B 1 151 ? 24.83400 -2.39300  -60.95500 1.000 23.62511  ? 142 PRO B CD     1 
ATOM   3775 N N      . ASP B 1 152 ? 25.55000 0.74600   -63.04400 1.000 26.67858  ? 143 ASP B N      1 
ATOM   3776 C CA     . ASP B 1 152 ? 25.52300 1.81000   -64.03900 1.000 28.55955  ? 143 ASP B CA     1 
ATOM   3777 C C      . ASP B 1 152 ? 25.39200 3.19700   -63.42000 1.000 29.75006  ? 143 ASP B C      1 
ATOM   3778 O O      . ASP B 1 152 ? 25.16500 4.17000   -64.14700 1.000 25.87060  ? 143 ASP B O      1 
ATOM   3779 C CB     . ASP B 1 152 ? 24.39300 1.57300   -65.04600 1.000 26.06581  ? 143 ASP B CB     1 
ATOM   3780 C CG     . ASP B 1 152 ? 23.01203 1.74391   -64.43941 1.000 34.21538  ? 143 ASP B CG     1 
ATOM   3781 O OD1    . ASP B 1 152 ? 22.91111 2.06481   -63.23494 1.000 39.30940  ? 143 ASP B OD1    1 
ATOM   3782 O OD2    . ASP B 1 152 ? 22.02196 1.55231   -65.17522 1.000 32.46744  ? 143 ASP B OD2    1 
ATOM   3783 N N      . GLY B 1 153 ? 25.53100 3.31200   -62.10000 1.000 25.84610  ? 144 GLY B N      1 
ATOM   3784 C CA     . GLY B 1 153 ? 25.44900 4.58500   -61.42200 1.000 26.22655  ? 144 GLY B CA     1 
ATOM   3785 C C      . GLY B 1 153 ? 24.07400 4.95200   -60.90600 1.000 29.24216  ? 144 GLY B C      1 
ATOM   3786 O O      . GLY B 1 153 ? 23.96700 5.82000   -60.03300 1.000 32.23025  ? 144 GLY B O      1 
ATOM   3787 N N      . THR B 1 154 ? 23.01900 4.32600   -61.42200 1.000 26.28755  ? 145 THR B N      1 
ATOM   3788 C CA     . THR B 1 154 ? 21.67800 4.55700   -60.91300 1.000 29.99016  ? 145 THR B CA     1 
ATOM   3789 C C      . THR B 1 154 ? 21.49700 3.83300   -59.58100 1.000 34.70580  ? 145 THR B C      1 
ATOM   3790 O O      . THR B 1 154 ? 22.40200 3.16300   -59.07400 1.000 28.06966  ? 145 THR B O      1 
ATOM   3791 C CB     . THR B 1 154 ? 20.63100 4.10000   -61.92600 1.000 33.76118  ? 145 THR B CB     1 
ATOM   3792 O OG1    . THR B 1 154 ? 20.74200 2.68500   -62.12300 1.000 39.75922  ? 145 THR B OG1    1 
ATOM   3793 C CG2    . THR B 1 154 ? 20.82600 4.81000   -63.25900 1.000 26.68276  ? 145 THR B CG2    1 
ATOM   3794 N N      . HIS B 1 155 ? 20.30700 3.96500   -59.00400 1.000 32.75847  ? 146 HIS B N      1 
ATOM   3795 C CA     . HIS B 1 155 ? 19.97900 3.32200   -57.74300 1.000 31.06039  ? 146 HIS B CA     1 
ATOM   3796 C C      . HIS B 1 155 ? 18.76500 2.42500   -57.92400 1.000 35.01134  ? 146 HIS B C      1 
ATOM   3797 O O      . HIS B 1 155 ? 17.79600 2.79900   -58.59300 1.000 37.31615  ? 146 HIS B O      1 
ATOM   3798 C CB     . HIS B 1 155 ? 19.72600 4.35500   -56.64100 1.000 30.96726  ? 146 HIS B CB     1 
ATOM   3799 C CG     . HIS B 1 155 ? 20.95700 5.10100   -56.23000 1.000 33.85722  ? 146 HIS B CG     1 
ATOM   3800 N ND1    . HIS B 1 155 ? 21.48800 6.12800   -56.97900 1.000 34.01166  ? 146 HIS B ND1    1 
ATOM   3801 C CD2    . HIS B 1 155 ? 21.77400 4.95400   -55.15900 1.000 31.90756  ? 146 HIS B CD2    1 
ATOM   3802 C CE1    . HIS B 1 155 ? 22.57300 6.59000   -56.38200 1.000 34.84950  ? 146 HIS B CE1    1 
ATOM   3803 N NE2    . HIS B 1 155 ? 22.76800 5.89500   -55.27600 1.000 37.72932  ? 146 HIS B NE2    1 
ATOM   3804 N N      . GLY B 1 156 ? 18.83200 1.23600   -57.33200 1.000 32.26135  ? 147 GLY B N      1 
ATOM   3805 C CA     . GLY B 1 156 ? 17.77400 0.25800   -57.47000 1.000 33.33177  ? 147 GLY B CA     1 
ATOM   3806 C C      . GLY B 1 156 ? 17.06300 -0.05200  -56.17000 1.000 36.39839  ? 147 GLY B C      1 
ATOM   3807 O O      . GLY B 1 156 ? 17.26900 0.62700   -55.16100 1.000 30.22158  ? 147 GLY B O      1 
ATOM   3808 N N      . ILE B 1 157 ? 16.23700 -1.09400  -56.18300 1.000 37.86127  ? 148 ILE B N      1 
ATOM   3809 C CA     . ILE B 1 157 ? 15.40500 -1.47300  -55.04800 1.000 31.61483  ? 148 ILE B CA     1 
ATOM   3810 C C      . ILE B 1 157 ? 15.89400 -2.81300  -54.50900 1.000 29.05184  ? 148 ILE B C      1 
ATOM   3811 O O      . ILE B 1 157 ? 16.13100 -3.75100  -55.28000 1.000 34.80012  ? 148 ILE B O      1 
ATOM   3812 C CB     . ILE B 1 157 ? 13.92000 -1.54100  -55.44800 1.000 41.78488  ? 148 ILE B CB     1 
ATOM   3813 C CG1    . ILE B 1 157 ? 13.47204 -0.22410  -56.09422 1.000 47.32889  ? 148 ILE B CG1    1 
ATOM   3814 C CG2    . ILE B 1 157 ? 13.05966 -1.86017  -54.24491 1.000 39.31252  ? 148 ILE B CG2    1 
ATOM   3815 C CD1    . ILE B 1 157 ? 14.00150 -0.00683  -57.51085 1.000 44.78457  ? 148 ILE B CD1    1 
ATOM   3816 N N      . TYR B 1 158 ? 16.04900 -2.90000  -53.19200 1.000 25.80435  ? 149 TYR B N      1 
ATOM   3817 C CA     . TYR B 1 158 ? 16.48400 -4.15000  -52.57700 1.000 30.54091  ? 149 TYR B CA     1 
ATOM   3818 C C      . TYR B 1 158 ? 15.40600 -5.21600  -52.74500 1.000 29.09338  ? 149 TYR B C      1 
ATOM   3819 O O      . TYR B 1 158 ? 14.23000 -4.95100  -52.46700 1.000 29.77285  ? 149 TYR B O      1 
ATOM   3820 C CB     . TYR B 1 158 ? 16.79300 -3.94300  -51.09800 1.000 24.33631  ? 149 TYR B CB     1 
ATOM   3821 C CG     . TYR B 1 158 ? 18.03200 -3.12000  -50.83000 1.000 28.09282  ? 149 TYR B CG     1 
ATOM   3822 C CD1    . TYR B 1 158 ? 19.29500 -3.69600  -50.88500 1.000 21.07448  ? 149 TYR B CD1    1 
ATOM   3823 C CD2    . TYR B 1 158 ? 17.94100 -1.77200  -50.50700 1.000 28.32133  ? 149 TYR B CD2    1 
ATOM   3824 C CE1    . TYR B 1 158 ? 20.43100 -2.95300  -50.63100 1.000 24.24412  ? 149 TYR B CE1    1 
ATOM   3825 C CE2    . TYR B 1 158 ? 19.07300 -1.01800  -50.25400 1.000 25.75710  ? 149 TYR B CE2    1 
ATOM   3826 C CZ     . TYR B 1 158 ? 20.31500 -1.61400  -50.31600 1.000 22.49973  ? 149 TYR B CZ     1 
ATOM   3827 O OH     . TYR B 1 158 ? 21.44400 -0.87000  -50.06500 1.000 22.57398  ? 149 TYR B OH     1 
ATOM   3828 N N      . PRO B 1 159 ? 15.75600 -6.41700  -53.20400 1.000 25.53812  ? 150 PRO B N      1 
ATOM   3829 C CA     . PRO B 1 159 ? 14.74500 -7.46700  -53.38000 1.000 29.47416  ? 150 PRO B CA     1 
ATOM   3830 C C      . PRO B 1 159 ? 14.53400 -8.28800  -52.11900 1.000 30.32401  ? 150 PRO B C      1 
ATOM   3831 O O      . PRO B 1 159 ? 15.22600 -8.08800  -51.11600 1.000 24.80764  ? 150 PRO B O      1 
ATOM   3832 C CB     . PRO B 1 159 ? 15.33400 -8.31700  -54.50900 1.000 30.01720  ? 150 PRO B CB     1 
ATOM   3833 C CG     . PRO B 1 159 ? 16.81800 -8.21300  -54.28200 1.000 27.45243  ? 150 PRO B CG     1 
ATOM   3834 C CD     . PRO B 1 159 ? 17.07500 -6.82900  -53.71800 1.000 29.18349  ? 150 PRO B CD     1 
ATOM   3835 N N      . LYS B 1 160 ? 13.58600 -9.21500  -52.16200 1.000 26.90545  ? 151 LYS B N      1 
ATOM   3836 C CA     . LYS B 1 160 ? 13.37000 -10.11200 -51.03400 1.000 27.89623  ? 151 LYS B CA     1 
ATOM   3837 C C      . LYS B 1 160 ? 14.50400 -11.12900 -50.95600 1.000 33.53172  ? 151 LYS B C      1 
ATOM   3838 O O      . LYS B 1 160 ? 14.77400 -11.82600 -51.94200 1.000 31.22659  ? 151 LYS B O      1 
ATOM   3839 C CB     . LYS B 1 160 ? 12.02700 -10.83100 -51.16200 1.000 32.98963  ? 151 LYS B CB     1 
ATOM   3840 C CG     . LYS B 1 160 ? 10.86604 -10.13496 -50.46122 1.000 42.97725  ? 151 LYS B CG     1 
ATOM   3841 C CD     . LYS B 1 160 ? 9.63197  -11.03055 -50.41606 1.000 44.60750  ? 151 LYS B CD     1 
ATOM   3842 C CE     . LYS B 1 160 ? 8.52853  -10.42781 -49.55281 1.000 51.29880  ? 151 LYS B CE     1 
ATOM   3843 N NZ     . LYS B 1 160 ? 8.66181  -10.79196 -48.10875 1.000 45.29646  ? 151 LYS B NZ     1 
ATOM   3844 N N      . PRO B 1 161 ? 15.18300 -11.24300 -49.82400 1.000 28.05552  ? 152 PRO B N      1 
ATOM   3845 C CA     . PRO B 1 161 ? 16.25100 -12.23500 -49.67900 1.000 27.29064  ? 152 PRO B CA     1 
ATOM   3846 C C      . PRO B 1 161 ? 15.67000 -13.62100 -49.41800 1.000 28.82252  ? 152 PRO B C      1 
ATOM   3847 O O      . PRO B 1 161 ? 14.46100 -13.81000 -49.30800 1.000 29.75955  ? 152 PRO B O      1 
ATOM   3848 C CB     . PRO B 1 161 ? 17.03500 -11.72000 -48.47300 1.000 28.24666  ? 152 PRO B CB     1 
ATOM   3849 C CG     . PRO B 1 161 ? 15.99300 -11.04600 -47.63800 1.000 28.15873  ? 152 PRO B CG     1 
ATOM   3850 C CD     . PRO B 1 161 ? 15.03400 -10.41100 -48.61700 1.000 26.94769  ? 152 PRO B CD     1 
ATOM   3851 N N      . ARG B 1 162 ? 16.56700 -14.59700 -49.31200 1.000 33.80277  ? 153 ARG B N      1 
ATOM   3852 C CA     . ARG B 1 162 ? 16.21300 -15.97800 -49.01200 1.000 32.08057  ? 153 ARG B CA     1 
ATOM   3853 C C      . ARG B 1 162 ? 16.73200 -16.32200 -47.62000 1.000 33.46440  ? 153 ARG B C      1 
ATOM   3854 O O      . ARG B 1 162 ? 17.92900 -16.17700 -47.34800 1.000 30.81987  ? 153 ARG B O      1 
ATOM   3855 C CB     . ARG B 1 162 ? 16.79300 -16.92900 -50.06100 1.000 30.16074  ? 153 ARG B CB     1 
ATOM   3856 C CG     . ARG B 1 162 ? 16.58600 -18.40200 -49.75300 1.000 36.48256  ? 153 ARG B CG     1 
ATOM   3857 C CD     . ARG B 1 162 ? 17.02700 -19.28700 -50.91300 1.000 35.50981  ? 153 ARG B CD     1 
ATOM   3858 N NE     . ARG B 1 162 ? 18.43200 -19.10200 -51.25800 1.000 32.81218  ? 153 ARG B NE     1 
ATOM   3859 C CZ     . ARG B 1 162 ? 19.44000 -19.72200 -50.65800 1.000 36.85659  ? 153 ARG B CZ     1 
ATOM   3860 N NH1    . ARG B 1 162 ? 19.23900 -20.55700 -49.65300 1.000 30.89144  ? 153 ARG B NH1    1 
ATOM   3861 N NH2    . ARG B 1 162 ? 20.68200 -19.49900 -51.08000 1.000 31.08174  ? 153 ARG B NH2    1 
ATOM   3862 N N      . ALA B 1 163 ? 15.83200 -16.76100 -46.74200 1.000 31.63298  ? 154 ALA B N      1 
ATOM   3863 C CA     . ALA B 1 163 ? 16.21400 -17.15100 -45.39000 1.000 32.45940  ? 154 ALA B CA     1 
ATOM   3864 C C      . ALA B 1 163 ? 16.90000 -18.51100 -45.43300 1.000 33.02013  ? 154 ALA B C      1 
ATOM   3865 O O      . ALA B 1 163 ? 16.28700 -19.51100 -45.82400 1.000 38.93302  ? 154 ALA B O      1 
ATOM   3866 C CB     . ALA B 1 163 ? 14.99200 -17.18800 -44.47600 1.000 25.35523  ? 154 ALA B CB     1 
ATOM   3867 N N      . ILE B 1 164 ? 18.15900 -18.55000 -45.03100 1.000 26.97236  ? 155 ILE B N      1 
ATOM   3868 C CA     . ILE B 1 164 ? 18.96800 -19.75900 -45.12000 1.000 30.08491  ? 155 ILE B CA     1 
ATOM   3869 C C      . ILE B 1 164 ? 18.73300 -20.62500 -43.89200 1.000 32.86272  ? 155 ILE B C      1 
ATOM   3870 O O      . ILE B 1 164 ? 18.42200 -20.13400 -42.80200 1.000 30.80447  ? 155 ILE B O      1 
ATOM   3871 C CB     . ILE B 1 164 ? 20.46200 -19.40900 -45.27800 1.000 30.56219  ? 155 ILE B CB     1 
ATOM   3872 C CG1    . ILE B 1 164 ? 20.91900 -18.50200 -44.13400 1.000 26.05958  ? 155 ILE B CG1    1 
ATOM   3873 C CG2    . ILE B 1 164 ? 20.70800 -18.74800 -46.61800 1.000 30.95444  ? 155 ILE B CG2    1 
ATOM   3874 C CD1    . ILE B 1 164 ? 22.38700 -18.13700 -44.19300 1.000 26.44468  ? 155 ILE B CD1    1 
ATOM   3875 N N      . GLY B 1 165 ? 18.88500 -21.93500 -44.07600 1.000 28.12770  ? 156 GLY B N      1 
ATOM   3876 C CA     . GLY B 1 165 ? 18.82700 -22.87000 -42.97600 1.000 30.58330  ? 156 GLY B CA     1 
ATOM   3877 C C      . GLY B 1 165 ? 20.16100 -22.99600 -42.26800 1.000 29.40356  ? 156 GLY B C      1 
ATOM   3878 O O      . GLY B 1 165 ? 21.16900 -22.40300 -42.65100 1.000 25.67987  ? 156 GLY B O      1 
ATOM   3879 N N      . THR B 1 166 ? 20.15800 -23.80600 -41.20600 1.000 24.87118  ? 157 THR B N      1 
ATOM   3880 C CA     . THR B 1 166 ? 21.34600 -23.92600 -40.36800 1.000 26.41478  ? 157 THR B CA     1 
ATOM   3881 C C      . THR B 1 166 ? 22.48800 -24.62500 -41.09400 1.000 25.68915  ? 157 THR B C      1 
ATOM   3882 O O      . THR B 1 166 ? 23.65900 -24.35200 -40.80600 1.000 26.59478  ? 157 THR B O      1 
ATOM   3883 C CB     . THR B 1 166 ? 21.00600 -24.66700 -39.07500 1.000 27.81351  ? 157 THR B CB     1 
ATOM   3884 O OG1    . THR B 1 166 ? 20.55900 -25.99200 -39.38300 1.000 31.93184  ? 157 THR B OG1    1 
ATOM   3885 C CG2    . THR B 1 166 ? 19.91000 -23.93300 -38.32000 1.000 23.76868  ? 157 THR B CG2    1 
ATOM   3886 N N      . TYR B 1 167 ? 22.17900 -25.52600 -42.02900 1.000 27.96581  ? 158 TYR B N      1 
ATOM   3887 C CA     . TYR B 1 167 ? 23.24200 -26.16000 -42.80300 1.000 29.32469  ? 158 TYR B CA     1 
ATOM   3888 C C      . TYR B 1 167 ? 23.95700 -25.14800 -43.68800 1.000 25.63709  ? 158 TYR B C      1 
ATOM   3889 O O      . TYR B 1 167 ? 25.19000 -25.15900 -43.78200 1.000 21.44706  ? 158 TYR B O      1 
ATOM   3890 C CB     . TYR B 1 167 ? 22.68200 -27.30500 -43.64600 1.000 27.53060  ? 158 TYR B CB     1 
ATOM   3891 C CG     . TYR B 1 167 ? 23.70200 -27.91100 -44.58300 1.000 29.25515  ? 158 TYR B CG     1 
ATOM   3892 C CD1    . TYR B 1 167 ? 24.68900 -28.76400 -44.10600 1.000 31.28422  ? 158 TYR B CD1    1 
ATOM   3893 C CD2    . TYR B 1 167 ? 23.68200 -27.62600 -45.94200 1.000 34.03977  ? 158 TYR B CD2    1 
ATOM   3894 C CE1    . TYR B 1 167 ? 25.62600 -29.31800 -44.95600 1.000 31.52081  ? 158 TYR B CE1    1 
ATOM   3895 C CE2    . TYR B 1 167 ? 24.61500 -28.17600 -46.80100 1.000 36.22325  ? 158 TYR B CE2    1 
ATOM   3896 C CZ     . TYR B 1 167 ? 25.58500 -29.02100 -46.30200 1.000 36.91400  ? 158 TYR B CZ     1 
ATOM   3897 O OH     . TYR B 1 167 ? 26.51600 -29.57200 -47.15200 1.000 37.51519  ? 158 TYR B OH     1 
ATOM   3898 N N      . GLU B 1 168 ? 23.20200 -24.26500 -44.34500 1.000 24.32271  ? 159 GLU B N      1 
ATOM   3899 C CA     . GLU B 1 168 ? 23.83100 -23.23500 -45.16200 1.000 28.79847  ? 159 GLU B CA     1 
ATOM   3900 C C      . GLU B 1 168 ? 24.53800 -22.19600 -44.30000 1.000 26.69453  ? 159 GLU B C      1 
ATOM   3901 O O      . GLU B 1 168 ? 25.49900 -21.56500 -44.75600 1.000 27.40292  ? 159 GLU B O      1 
ATOM   3902 C CB     . GLU B 1 168 ? 22.79200 -22.57200 -46.06900 1.000 28.76691  ? 159 GLU B CB     1 
ATOM   3903 C CG     . GLU B 1 168 ? 23.38800 -21.67300 -47.14600 1.000 35.28303  ? 159 GLU B CG     1 
ATOM   3904 C CD     . GLU B 1 168 ? 22.38000 -21.28300 -48.21100 1.000 37.95856  ? 159 GLU B CD     1 
ATOM   3905 O OE1    . GLU B 1 168 ? 21.32000 -21.93800 -48.29900 1.000 35.04972  ? 159 GLU B OE1    1 
ATOM   3906 O OE2    . GLU B 1 168 ? 22.64900 -20.31800 -48.96100 1.000 33.33907  ? 159 GLU B OE2    1 
ATOM   3907 N N      . ILE B 1 169 ? 24.08600 -22.01000 -43.05700 1.000 24.77869  ? 160 ILE B N      1 
ATOM   3908 C CA     . ILE B 1 169 ? 24.77400 -21.10200 -42.14400 1.000 24.68194  ? 160 ILE B CA     1 
ATOM   3909 C C      . ILE B 1 169 ? 26.20200 -21.57300 -41.90100 1.000 25.74140  ? 160 ILE B C      1 
ATOM   3910 O O      . ILE B 1 169 ? 27.14800 -20.77600 -41.92900 1.000 27.15198  ? 160 ILE B O      1 
ATOM   3911 C CB     . ILE B 1 169 ? 23.98900 -20.96900 -40.82500 1.000 23.79304  ? 160 ILE B CB     1 
ATOM   3912 C CG1    . ILE B 1 169 ? 22.72600 -20.13300 -41.03700 1.000 24.52914  ? 160 ILE B CG1    1 
ATOM   3913 C CG2    . ILE B 1 169 ? 24.85800 -20.35600 -39.73700 1.000 26.17523  ? 160 ILE B CG2    1 
ATOM   3914 C CD1    . ILE B 1 169 ? 21.89300 -19.96300 -39.78600 1.000 31.28566  ? 160 ILE B CD1    1 
ATOM   3915 N N      . SER B 1 170 ? 26.38500 -22.87700 -41.67500 1.000 24.42323  ? 161 SER B N      1 
ATOM   3916 C CA     . SER B 1 170 ? 27.73000 -23.40100 -41.46000 1.000 26.92309  ? 161 SER B CA     1 
ATOM   3917 C C      . SER B 1 170 ? 28.57600 -23.31300 -42.72500 1.000 28.03451  ? 161 SER B C      1 
ATOM   3918 O O      . SER B 1 170 ? 29.80600 -23.21700 -42.63800 1.000 26.78614  ? 161 SER B O      1 
ATOM   3919 C CB     . SER B 1 170 ? 27.66200 -24.84600 -40.96300 1.000 26.76518  ? 161 SER B CB     1 
ATOM   3920 O OG     . SER B 1 170 ? 27.12700 -25.70600 -41.95300 1.000 34.00009  ? 161 SER B OG     1 
ATOM   3921 N N      . GLN B 1 171 ? 27.94400 -23.34200 -43.90200 1.000 27.73682  ? 162 GLN B N      1 
ATOM   3922 C CA     . GLN B 1 171 ? 28.69500 -23.17900 -45.14300 1.000 26.83730  ? 162 GLN B CA     1 
ATOM   3923 C C      . GLN B 1 171 ? 29.19800 -21.74900 -45.29700 1.000 26.84431  ? 162 GLN B C      1 
ATOM   3924 O O      . GLN B 1 171 ? 30.29800 -21.52400 -45.81400 1.000 28.07036  ? 162 GLN B O      1 
ATOM   3925 C CB     . GLN B 1 171 ? 27.83500 -23.57900 -46.34100 1.000 28.40547  ? 162 GLN B CB     1 
ATOM   3926 C CG     . GLN B 1 171 ? 27.53100 -25.06700 -46.42000 1.000 33.39942  ? 162 GLN B CG     1 
ATOM   3927 C CD     . GLN B 1 171 ? 26.79600 -25.44500 -47.69400 1.000 43.54155  ? 162 GLN B CD     1 
ATOM   3928 O OE1    . GLN B 1 171 ? 25.99600 -24.67000 -48.21900 1.000 39.21447  ? 162 GLN B OE1    1 
ATOM   3929 N NE2    . GLN B 1 171 ? 27.07300 -26.64100 -48.20200 1.000 45.60046  ? 162 GLN B NE2    1 
ATOM   3930 N N      . VAL B 1 172 ? 28.40600 -20.76900 -44.85700 1.000 23.13121  ? 163 VAL B N      1 
ATOM   3931 C CA     . VAL B 1 172 ? 28.87200 -19.38700 -44.85800 1.000 25.61823  ? 163 VAL B CA     1 
ATOM   3932 C C      . VAL B 1 172 ? 30.00000 -19.20800 -43.84900 1.000 27.92818  ? 163 VAL B C      1 
ATOM   3933 O O      . VAL B 1 172 ? 30.98100 -18.50000 -44.11200 1.000 25.70373  ? 163 VAL B O      1 
ATOM   3934 C CB     . VAL B 1 172 ? 27.69900 -18.42800 -44.57800 1.000 28.86499  ? 163 VAL B CB     1 
ATOM   3935 C CG1    . VAL B 1 172 ? 28.18400 -16.98600 -44.54000 1.000 25.81272  ? 163 VAL B CG1    1 
ATOM   3936 C CG2    . VAL B 1 172 ? 26.61300 -18.60200 -45.62900 1.000 19.02970  ? 163 VAL B CG2    1 
ATOM   3937 N N      . VAL B 1 173 ? 29.88400 -19.85000 -42.68300 1.000 27.52651  ? 164 VAL B N      1 
ATOM   3938 C CA     . VAL B 1 173 ? 30.96300 -19.81000 -41.69800 1.000 24.72517  ? 164 VAL B CA     1 
ATOM   3939 C C      . VAL B 1 173 ? 32.24200 -20.38600 -42.29000 1.000 28.78532  ? 164 VAL B C      1 
ATOM   3940 O O      . VAL B 1 173 ? 33.33800 -19.85000 -42.08200 1.000 27.14903  ? 164 VAL B O      1 
ATOM   3941 C CB     . VAL B 1 173 ? 30.54600 -20.55400 -40.41600 1.000 29.58341  ? 164 VAL B CB     1 
ATOM   3942 C CG1    . VAL B 1 173 ? 31.71300 -20.63500 -39.44400 1.000 24.55488  ? 164 VAL B CG1    1 
ATOM   3943 C CG2    . VAL B 1 173 ? 29.35800 -19.86300 -39.76600 1.000 24.49347  ? 164 VAL B CG2    1 
ATOM   3944 N N      . GLU B 1 174 ? 32.12500 -21.48000 -43.04700 1.000 25.99408  ? 165 GLU B N      1 
ATOM   3945 C CA     . GLU B 1 174 ? 33.29900 -22.04500 -43.70200 1.000 25.98555  ? 165 GLU B CA     1 
ATOM   3946 C C      . GLU B 1 174 ? 33.87600 -21.07700 -44.72900 1.000 30.93366  ? 165 GLU B C      1 
ATOM   3947 O O      . GLU B 1 174 ? 35.09900 -21.00000 -44.89800 1.000 26.23016  ? 165 GLU B O      1 
ATOM   3948 C CB     . GLU B 1 174 ? 32.94300 -23.38300 -44.35300 1.000 31.87850  ? 165 GLU B CB     1 
ATOM   3949 C CG     . GLU B 1 174 ? 34.08900 -24.04400 -45.11200 1.000 40.00000  ? 165 GLU B CG     1 
ATOM   3950 C CD     . GLU B 1 174 ? 35.26400 -24.41500 -44.21900 1.000 48.73700  ? 165 GLU B CD     1 
ATOM   3951 O OE1    . GLU B 1 174 ? 35.07000 -24.56500 -42.99200 1.000 43.15980  ? 165 GLU B OE1    1 
ATOM   3952 O OE2    . GLU B 1 174 ? 36.38600 -24.55700 -44.75100 1.000 46.19153  ? 165 GLU B OE2    1 
ATOM   3953 N N      . ASP B 1 175 ? 33.01500 -20.32400 -45.42100 1.000 24.32212  ? 166 ASP B N      1 
ATOM   3954 C CA     . ASP B 1 175 ? 33.50500 -19.30500 -46.34500 1.000 30.79922  ? 166 ASP B CA     1 
ATOM   3955 C C      . ASP B 1 175 ? 34.33500 -18.25500 -45.61500 1.000 27.93431  ? 166 ASP B C      1 
ATOM   3956 O O      . ASP B 1 175 ? 35.37100 -17.81100 -46.12200 1.000 25.41594  ? 166 ASP B O      1 
ATOM   3957 C CB     . ASP B 1 175 ? 32.33800 -18.64800 -47.08500 1.000 26.41192  ? 166 ASP B CB     1 
ATOM   3958 C CG     . ASP B 1 175 ? 31.67500 -19.58200 -48.08200 1.000 32.26847  ? 166 ASP B CG     1 
ATOM   3959 O OD1    . ASP B 1 175 ? 32.34000 -20.52900 -48.55100 1.000 40.36890  ? 166 ASP B OD1    1 
ATOM   3960 O OD2    . ASP B 1 175 ? 30.48800 -19.36100 -48.40300 1.000 30.79896  ? 166 ASP B OD2    1 
ATOM   3961 N N      . TYR B 1 176 ? 33.89600 -17.84600 -44.42000 1.000 27.78103  ? 167 TYR B N      1 
ATOM   3962 C CA     . TYR B 1 176 ? 34.71000 -16.95000 -43.60300 1.000 25.93300  ? 167 TYR B CA     1 
ATOM   3963 C C      . TYR B 1 176 ? 36.04800 -17.58900 -43.25300 1.000 26.58326  ? 167 TYR B C      1 
ATOM   3964 O O      . TYR B 1 176 ? 37.08200 -16.91100 -43.22800 1.000 27.96506  ? 167 TYR B O      1 
ATOM   3965 C CB     . TYR B 1 176 ? 33.96200 -16.56500 -42.32600 1.000 22.45225  ? 167 TYR B CB     1 
ATOM   3966 C CG     . TYR B 1 176 ? 32.95600 -15.44900 -42.49200 1.000 21.80032  ? 167 TYR B CG     1 
ATOM   3967 C CD1    . TYR B 1 176 ? 33.36800 -14.12700 -42.61100 1.000 21.30461  ? 167 TYR B CD1    1 
ATOM   3968 C CD2    . TYR B 1 176 ? 31.59400 -15.71400 -42.50700 1.000 19.84892  ? 167 TYR B CD2    1 
ATOM   3969 C CE1    . TYR B 1 176 ? 32.45300 -13.10500 -42.75400 1.000 20.62891  ? 167 TYR B CE1    1 
ATOM   3970 C CE2    . TYR B 1 176 ? 30.67100 -14.69700 -42.64800 1.000 18.26676  ? 167 TYR B CE2    1 
ATOM   3971 C CZ     . TYR B 1 176 ? 31.10500 -13.39600 -42.77000 1.000 21.48985  ? 167 TYR B CZ     1 
ATOM   3972 O OH     . TYR B 1 176 ? 30.18800 -12.38100 -42.90900 1.000 23.00561  ? 167 TYR B OH     1 
ATOM   3973 N N      . ARG B 1 177 ? 36.04600 -18.89600 -42.98200 1.000 28.15244  ? 168 ARG B N      1 
ATOM   3974 C CA     . ARG B 1 177 ? 37.28000 -19.57800 -42.60400 1.000 32.43373  ? 168 ARG B CA     1 
ATOM   3975 C C      . ARG B 1 177 ? 38.24000 -19.67700 -43.78300 1.000 31.04704  ? 168 ARG B C      1 
ATOM   3976 O O      . ARG B 1 177 ? 39.44200 -19.42300 -43.63800 1.000 31.84554  ? 168 ARG B O      1 
ATOM   3977 C CB     . ARG B 1 177 ? 36.96200 -20.96600 -42.04900 1.000 34.77125  ? 168 ARG B CB     1 
ATOM   3978 C CG     . ARG B 1 177 ? 38.18700 -21.73600 -41.59200 1.000 41.09891  ? 168 ARG B CG     1 
ATOM   3979 C CD     . ARG B 1 177 ? 37.89200 -23.21800 -41.42000 1.000 34.89102  ? 168 ARG B CD     1 
ATOM   3980 N NE     . ARG B 1 177 ? 38.95100 -24.03300 -42.00300 1.000 53.25968  ? 168 ARG B NE     1 
ATOM   3981 C CZ     . ARG B 1 177 ? 40.07500 -24.36200 -41.38100 1.000 51.42469  ? 168 ARG B CZ     1 
ATOM   3982 N NH1    . ARG B 1 177 ? 40.31500 -23.97800 -40.13700 1.000 49.77732  ? 168 ARG B NH1    1 
ATOM   3983 N NH2    . ARG B 1 177 ? 40.98200 -25.09300 -42.02300 1.000 55.87726  ? 168 ARG B NH2    1 
ATOM   3984 N N      . ARG B 1 178 ? 37.72800 -20.04700 -44.96000 1.000 30.53161  ? 169 ARG B N      1 
ATOM   3985 C CA     . ARG B 1 178 ? 38.58700 -20.16500 -46.13500 1.000 30.78911  ? 169 ARG B CA     1 
ATOM   3986 C C      . ARG B 1 178 ? 39.14600 -18.80800 -46.55200 1.000 31.25660  ? 169 ARG B C      1 
ATOM   3987 O O      . ARG B 1 178 ? 40.30200 -18.71000 -46.98100 1.000 30.53174  ? 169 ARG B O      1 
ATOM   3988 C CB     . ARG B 1 178 ? 37.81200 -20.80200 -47.28900 1.000 32.70432  ? 169 ARG B CB     1 
ATOM   3989 C CG     . ARG B 1 178 ? 37.04191 -22.05872 -46.91156 1.000 43.97893  ? 169 ARG B CG     1 
ATOM   3990 C CD     . ARG B 1 178 ? 37.64893 -23.29855 -47.55284 1.000 50.98801  ? 169 ARG B CD     1 
ATOM   3991 N NE     . ARG B 1 178 ? 39.10680 -23.24786 -47.59392 1.000 59.04656  ? 169 ARG B NE     1 
ATOM   3992 C CZ     . ARG B 1 178 ? 39.90163 -23.87934 -46.74072 1.000 59.93123  ? 169 ARG B CZ     1 
ATOM   3993 N NH1    . ARG B 1 178 ? 39.41094 -24.63169 -45.76948 1.000 62.24690  ? 169 ARG B NH1    1 
ATOM   3994 N NH2    . ARG B 1 178 ? 41.21989 -23.74883 -46.86163 1.000 47.76068  ? 169 ARG B NH2    1 
ATOM   3995 N N      . SER B 1 179 ? 38.34200 -17.75000 -46.43200 1.000 31.41379  ? 170 SER B N      1 
ATOM   3996 C CA     . SER B 1 179 ? 38.80700 -16.42100 -46.81400 1.000 28.65314  ? 170 SER B CA     1 
ATOM   3997 C C      . SER B 1 179 ? 39.88700 -15.91400 -45.86900 1.000 26.90024  ? 170 SER B C      1 
ATOM   3998 O O      . SER B 1 179 ? 40.80900 -15.21200 -46.30000 1.000 26.63356  ? 170 SER B O      1 
ATOM   3999 C CB     . SER B 1 179 ? 37.63300 -15.44500 -46.86100 1.000 26.31369  ? 170 SER B CB     1 
ATOM   4000 O OG     . SER B 1 179 ? 36.68100 -15.85100 -47.82900 1.000 31.88263  ? 170 SER B OG     1 
ATOM   4001 N N      . ALA B 1 180 ? 39.79200 -16.25800 -44.58200 1.000 26.59364  ? 171 ALA B N      1 
ATOM   4002 C CA     . ALA B 1 180 ? 40.83000 -15.86600 -43.63600 1.000 23.37742  ? 171 ALA B CA     1 
ATOM   4003 C C      . ALA B 1 180 ? 42.14500 -16.57100 -43.94200 1.000 26.43620  ? 171 ALA B C      1 
ATOM   4004 O O      . ALA B 1 180 ? 43.22000 -15.96900 -43.83500 1.000 29.59488  ? 171 ALA B O      1 
ATOM   4005 C CB     . ALA B 1 180 ? 40.37900 -16.16500 -42.20700 1.000 24.36158  ? 171 ALA B CB     1 
ATOM   4006 N N      . LEU B 1 181 ? 42.07900 -17.84900 -44.32400 1.000 28.57633  ? 172 LEU B N      1 
ATOM   4007 C CA     . LEU B 1 181 ? 43.28500 -18.56100 -44.73400 1.000 29.15477  ? 172 LEU B CA     1 
ATOM   4008 C C      . LEU B 1 181 ? 43.85900 -17.97600 -46.01900 1.000 26.99087  ? 172 LEU B C      1 
ATOM   4009 O O      . LEU B 1 181 ? 45.08100 -17.84600 -46.15700 1.000 26.58986  ? 172 LEU B O      1 
ATOM   4010 C CB     . LEU B 1 181 ? 42.98300 -20.05000 -44.90500 1.000 24.21307  ? 172 LEU B CB     1 
ATOM   4011 C CG     . LEU B 1 181 ? 42.62300 -20.81700 -43.63200 1.000 29.65630  ? 172 LEU B CG     1 
ATOM   4012 C CD1    . LEU B 1 181 ? 42.12900 -22.21600 -43.96000 1.000 31.47357  ? 172 LEU B CD1    1 
ATOM   4013 C CD2    . LEU B 1 181 ? 43.82000 -20.87900 -42.69800 1.000 31.23186  ? 172 LEU B CD2    1 
ATOM   4014 N N      . ASN B 1 182 ? 42.99200 -17.61400 -46.97000 1.000 24.53230  ? 173 ASN B N      1 
ATOM   4015 C CA     . ASN B 1 182 ? 43.46000 -16.99000 -48.20400 1.000 27.99732  ? 173 ASN B CA     1 
ATOM   4016 C C      . ASN B 1 182 ? 44.09900 -15.63200 -47.94300 1.000 26.26065  ? 173 ASN B C      1 
ATOM   4017 O O      . ASN B 1 182 ? 45.04100 -15.24800 -48.64500 1.000 24.45250  ? 173 ASN B O      1 
ATOM   4018 C CB     . ASN B 1 182 ? 42.30700 -16.84600 -49.20000 1.000 25.20893  ? 173 ASN B CB     1 
ATOM   4019 C CG     . ASN B 1 182 ? 41.84400 -18.18000 -49.76200 1.000 28.73183  ? 173 ASN B CG     1 
ATOM   4020 O OD1    . ASN B 1 182 ? 42.55400 -19.18200 -49.68300 1.000 29.24409  ? 173 ASN B OD1    1 
ATOM   4021 N ND2    . ASN B 1 182 ? 40.65100 -18.19200 -50.34700 1.000 26.41394  ? 173 ASN B ND2    1 
ATOM   4022 N N      . ALA B 1 183 ? 43.60300 -14.89100 -46.94800 1.000 25.27862  ? 174 ALA B N      1 
ATOM   4023 C CA     . ALA B 1 183 ? 44.20900 -13.60500 -46.62100 1.000 27.23567  ? 174 ALA B CA     1 
ATOM   4024 C C      . ALA B 1 183 ? 45.61900 -13.78400 -46.07200 1.000 25.10071  ? 174 ALA B C      1 
ATOM   4025 O O      . ALA B 1 183 ? 46.52300 -13.00800 -46.40400 1.000 25.83314  ? 174 ALA B O      1 
ATOM   4026 C CB     . ALA B 1 183 ? 43.33600 -12.84800 -45.62200 1.000 24.40522  ? 174 ALA B CB     1 
ATOM   4027 N N      . ILE B 1 184 ? 45.82600 -14.80000 -45.23200 1.000 26.30132  ? 175 ILE B N      1 
ATOM   4028 C CA     . ILE B 1 184 ? 47.16200 -15.06800 -44.71200 1.000 28.25062  ? 175 ILE B CA     1 
ATOM   4029 C C      . ILE B 1 184 ? 48.09100 -15.51000 -45.83500 1.000 30.08225  ? 175 ILE B C      1 
ATOM   4030 O O      . ILE B 1 184 ? 49.26700 -15.12800 -45.87300 1.000 29.38140  ? 175 ILE B O      1 
ATOM   4031 C CB     . ILE B 1 184 ? 47.09800 -16.11000 -43.58100 1.000 33.86566  ? 175 ILE B CB     1 
ATOM   4032 C CG1    . ILE B 1 184 ? 46.25400 -15.58100 -42.42100 1.000 29.08823  ? 175 ILE B CG1    1 
ATOM   4033 C CG2    . ILE B 1 184 ? 48.49800 -16.47900 -43.10700 1.000 29.67569  ? 175 ILE B CG2    1 
ATOM   4034 C CD1    . ILE B 1 184 ? 46.76800 -14.28900 -41.82700 1.000 25.54407  ? 175 ILE B CD1    1 
ATOM   4035 N N      . GLU B 1 185 ? 47.58100 -16.31600 -46.77100 1.000 30.19162  ? 176 GLU B N      1 
ATOM   4036 C CA     . GLU B 1 185 ? 48.38900 -16.69800 -47.92400 1.000 32.40317  ? 176 GLU B CA     1 
ATOM   4037 C C      . GLU B 1 185 ? 48.79700 -15.47500 -48.73400 1.000 31.76767  ? 176 GLU B C      1 
ATOM   4038 O O      . GLU B 1 185 ? 49.94200 -15.37500 -49.19000 1.000 34.35395  ? 176 GLU B O      1 
ATOM   4039 C CB     . GLU B 1 185 ? 47.63200 -17.69700 -48.79800 1.000 33.46109  ? 176 GLU B CB     1 
ATOM   4040 C CG     . GLU B 1 185 ? 48.17222 -17.77949 -50.21877 1.000 43.08765  ? 176 GLU B CG     1 
ATOM   4041 C CD     . GLU B 1 185 ? 47.89020 -19.10913 -50.88419 1.000 51.19060  ? 176 GLU B CD     1 
ATOM   4042 O OE1    . GLU B 1 185 ? 48.61569 -19.46684 -51.83588 1.000 62.93853  ? 176 GLU B OE1    1 
ATOM   4043 O OE2    . GLU B 1 185 ? 46.93865 -19.79673 -50.45581 1.000 52.25313  ? 176 GLU B OE2    1 
ATOM   4044 N N      . ALA B 1 186 ? 47.87800 -14.52400 -48.91000 1.000 27.02991  ? 177 ALA B N      1 
ATOM   4045 C CA     . ALA B 1 186 ? 48.20400 -13.28900 -49.60900 1.000 31.51184  ? 177 ALA B CA     1 
ATOM   4046 C C      . ALA B 1 186 ? 49.21200 -12.43400 -48.85200 1.000 29.25482  ? 177 ALA B C      1 
ATOM   4047 O O      . ALA B 1 186 ? 49.75300 -11.48800 -49.43300 1.000 28.74564  ? 177 ALA B O      1 
ATOM   4048 C CB     . ALA B 1 186 ? 46.93100 -12.48100 -49.86900 1.000 28.07180  ? 177 ALA B CB     1 
ATOM   4049 N N      . GLY B 1 187 ? 49.47400 -12.74100 -47.58200 1.000 29.43129  ? 178 GLY B N      1 
ATOM   4050 C CA     . GLY B 1 187 ? 50.42700 -12.00200 -46.78400 1.000 24.75238  ? 178 GLY B CA     1 
ATOM   4051 C C      . GLY B 1 187 ? 49.82100 -11.04600 -45.78200 1.000 30.87021  ? 178 GLY B C      1 
ATOM   4052 O O      . GLY B 1 187 ? 50.57100 -10.32200 -45.11400 1.000 29.65312  ? 178 GLY B O      1 
ATOM   4053 N N      . PHE B 1 188 ? 48.49500 -11.01600 -45.65400 1.000 23.91622  ? 179 PHE B N      1 
ATOM   4054 C CA     . PHE B 1 188 ? 47.85800 -10.09200 -44.72500 1.000 24.46508  ? 179 PHE B CA     1 
ATOM   4055 C C      . PHE B 1 188 ? 48.26200 -10.41300 -43.29200 1.000 26.41492  ? 179 PHE B C      1 
ATOM   4056 O O      . PHE B 1 188 ? 48.40200 -11.57900 -42.91400 1.000 26.70412  ? 179 PHE B O      1 
ATOM   4057 C CB     . PHE B 1 188 ? 46.33500 -10.15300 -44.86500 1.000 26.77435  ? 179 PHE B CB     1 
ATOM   4058 C CG     . PHE B 1 188 ? 45.78700 -9.29100  -45.96800 1.000 25.34971  ? 179 PHE B CG     1 
ATOM   4059 C CD1    . PHE B 1 188 ? 45.68400 -7.92000  -45.80400 1.000 18.57458  ? 179 PHE B CD1    1 
ATOM   4060 C CD2    . PHE B 1 188 ? 45.36300 -9.85200  -47.16300 1.000 22.75763  ? 179 PHE B CD2    1 
ATOM   4061 C CE1    . PHE B 1 188 ? 45.17800 -7.12300  -46.81100 1.000 22.25767  ? 179 PHE B CE1    1 
ATOM   4062 C CE2    . PHE B 1 188 ? 44.85200 -9.05800  -48.17500 1.000 23.53068  ? 179 PHE B CE2    1 
ATOM   4063 C CZ     . PHE B 1 188 ? 44.76000 -7.69200  -47.99700 1.000 20.85645  ? 179 PHE B CZ     1 
ATOM   4064 N N      . ASP B 1 189 ? 48.45800 -9.36500  -42.49100 1.000 30.01163  ? 180 ASP B N      1 
ATOM   4065 C CA     . ASP B 1 189 ? 48.78800 -9.58300  -41.08800 1.000 26.80385  ? 180 ASP B CA     1 
ATOM   4066 C C      . ASP B 1 189 ? 47.60800 -10.16700 -40.32400 1.000 28.96431  ? 180 ASP B C      1 
ATOM   4067 O O      . ASP B 1 189 ? 47.80000 -10.83800 -39.30600 1.000 28.79128  ? 180 ASP B O      1 
ATOM   4068 C CB     . ASP B 1 189 ? 49.25100 -8.27200  -40.45500 1.000 28.46813  ? 180 ASP B CB     1 
ATOM   4069 C CG     . ASP B 1 189 ? 50.50700 -7.72600  -41.10800 1.000 32.51596  ? 180 ASP B CG     1 
ATOM   4070 O OD1    . ASP B 1 189 ? 51.51900 -8.46100  -41.16600 1.000 28.30580  ? 180 ASP B OD1    1 
ATOM   4071 O OD2    . ASP B 1 189 ? 50.47500 -6.57400  -41.58500 1.000 32.84807  ? 180 ASP B OD2    1 
ATOM   4072 N N      . GLY B 1 190 ? 46.39200 -9.94000  -40.80700 1.000 25.85878  ? 181 GLY B N      1 
ATOM   4073 C CA     . GLY B 1 190 ? 45.21700 -10.47800 -40.15200 1.000 22.40359  ? 181 GLY B CA     1 
ATOM   4074 C C      . GLY B 1 190 ? 43.96800 -10.10600 -40.91600 1.000 25.19963  ? 181 GLY B C      1 
ATOM   4075 O O      . GLY B 1 190 ? 44.03300 -9.54200  -42.00900 1.000 26.07283  ? 181 GLY B O      1 
ATOM   4076 N N      . ILE B 1 191 ? 42.82000 -10.43200 -40.32500 1.000 22.61281  ? 182 ILE B N      1 
ATOM   4077 C CA     . ILE B 1 191 ? 41.52600 -10.12500 -40.91600 1.000 21.50131  ? 182 ILE B CA     1 
ATOM   4078 C C      . ILE B 1 191 ? 40.65500 -9.43600  -39.87800 1.000 25.93535  ? 182 ILE B C      1 
ATOM   4079 O O      . ILE B 1 191 ? 40.82900 -9.61800  -38.66800 1.000 26.46616  ? 182 ILE B O      1 
ATOM   4080 C CB     . ILE B 1 191 ? 40.81400 -11.38500 -41.46400 1.000 21.11630  ? 182 ILE B CB     1 
ATOM   4081 C CG1    . ILE B 1 191 ? 40.60100 -12.41800 -40.35400 1.000 22.64329  ? 182 ILE B CG1    1 
ATOM   4082 C CG2    . ILE B 1 191 ? 41.59700 -11.98400 -42.61700 1.000 20.19899  ? 182 ILE B CG2    1 
ATOM   4083 C CD1    . ILE B 1 191 ? 39.16500 -12.51700 -39.88100 1.000 26.06687  ? 182 ILE B CD1    1 
ATOM   4084 N N      . GLU B 1 192 ? 39.71400 -8.63200  -40.36400 1.000 23.52922  ? 183 GLU B N      1 
ATOM   4085 C CA     . GLU B 1 192 ? 38.66700 -8.04100  -39.54400 1.000 23.72835  ? 183 GLU B CA     1 
ATOM   4086 C C      . GLU B 1 192 ? 37.32200 -8.58800  -39.99600 1.000 25.50927  ? 183 GLU B C      1 
ATOM   4087 O O      . GLU B 1 192 ? 37.01800 -8.58800  -41.19400 1.000 22.55861  ? 183 GLU B O      1 
ATOM   4088 C CB     . GLU B 1 192 ? 38.67300 -6.51400  -39.63900 1.000 21.68212  ? 183 GLU B CB     1 
ATOM   4089 C CG     . GLU B 1 192 ? 37.41500 -5.87000  -39.07300 1.000 25.25532  ? 183 GLU B CG     1 
ATOM   4090 C CD     . GLU B 1 192 ? 37.46100 -4.35600  -39.09400 1.000 26.86763  ? 183 GLU B CD     1 
ATOM   4091 O OE1    . GLU B 1 192 ? 38.30500 -3.77700  -38.38000 1.000 27.88526  ? 183 GLU B OE1    1 
ATOM   4092 O OE2    . GLU B 1 192 ? 36.65500 -3.74700  -39.82900 1.000 26.14824  ? 183 GLU B OE2    1 
ATOM   4093 N N      . ILE B 1 193 ? 36.52600 -9.05500  -39.03900 1.000 24.88625  ? 184 ILE B N      1 
ATOM   4094 C CA     . ILE B 1 193 ? 35.19000 -9.56500  -39.32400 1.000 22.27573  ? 184 ILE B CA     1 
ATOM   4095 C C      . ILE B 1 193 ? 34.22200 -8.38900  -39.39000 1.000 26.44581  ? 184 ILE B C      1 
ATOM   4096 O O      . ILE B 1 193 ? 33.99500 -7.70200  -38.38900 1.000 25.70079  ? 184 ILE B O      1 
ATOM   4097 C CB     . ILE B 1 193 ? 34.75000 -10.58300 -38.26300 1.000 20.50623  ? 184 ILE B CB     1 
ATOM   4098 C CG1    . ILE B 1 193 ? 35.57500 -11.86500 -38.37600 1.000 20.76186  ? 184 ILE B CG1    1 
ATOM   4099 C CG2    . ILE B 1 193 ? 33.27700 -10.89300 -38.40600 1.000 19.87291  ? 184 ILE B CG2    1 
ATOM   4100 C CD1    . ILE B 1 193 ? 35.45700 -12.54700 -39.72200 1.000 22.17810  ? 184 ILE B CD1    1 
ATOM   4101 N N      . HIS B 1 194 ? 33.65000 -8.15600  -40.56900 1.000 21.08682  ? 185 HIS B N      1 
ATOM   4102 C CA     . HIS B 1 194 ? 32.68800 -7.07300  -40.76500 1.000 22.14807  ? 185 HIS B CA     1 
ATOM   4103 C C      . HIS B 1 194 ? 31.32600 -7.54400  -40.27400 1.000 23.13453  ? 185 HIS B C      1 
ATOM   4104 O O      . HIS B 1 194 ? 30.60700 -8.25500  -40.98100 1.000 19.62302  ? 185 HIS B O      1 
ATOM   4105 C CB     . HIS B 1 194 ? 32.63600 -6.65500  -42.23100 1.000 23.61354  ? 185 HIS B CB     1 
ATOM   4106 C CG     . HIS B 1 194 ? 31.85300 -5.40100  -42.48000 1.000 22.92922  ? 185 HIS B CG     1 
ATOM   4107 N ND1    . HIS B 1 194 ? 31.05000 -4.81700  -41.52300 1.000 25.14100  ? 185 HIS B ND1    1 
ATOM   4108 C CD2    . HIS B 1 194 ? 31.75800 -4.61500  -43.57800 1.000 22.54912  ? 185 HIS B CD2    1 
ATOM   4109 C CE1    . HIS B 1 194 ? 30.49100 -3.73000  -42.02300 1.000 26.07793  ? 185 HIS B CE1    1 
ATOM   4110 N NE2    . HIS B 1 194 ? 30.90400 -3.58500  -43.26900 1.000 20.73775  ? 185 HIS B NE2    1 
ATOM   4111 N N      . GLY B 1 195 ? 30.96600 -7.14600  -39.05800 1.000 18.75023  ? 186 GLY B N      1 
ATOM   4112 C CA     . GLY B 1 195 ? 29.67000 -7.48500  -38.50800 1.000 23.92038  ? 186 GLY B CA     1 
ATOM   4113 C C      . GLY B 1 195 ? 28.87600 -6.25600  -38.12100 1.000 25.50373  ? 186 GLY B C      1 
ATOM   4114 O O      . GLY B 1 195 ? 28.26500 -6.21300  -37.04900 1.000 24.79801  ? 186 GLY B O      1 
ATOM   4115 N N      . ALA B 1 196 ? 28.86100 -5.28100  -39.02500 1.000 19.85997  ? 187 ALA B N      1 
ATOM   4116 C CA     . ALA B 1 196 ? 28.17500 -4.00300  -38.76600 1.000 21.74790  ? 187 ALA B CA     1 
ATOM   4117 C C      . ALA B 1 196 ? 27.42300 -3.47400  -39.99100 1.000 22.78881  ? 187 ALA B C      1 
ATOM   4118 O O      . ALA B 1 196 ? 27.40700 -4.16700  -41.02000 1.000 20.67337  ? 187 ALA B O      1 
ATOM   4119 C CB     . ALA B 1 196 ? 29.23300 -3.01800  -38.34800 1.000 22.57906  ? 187 ALA B CB     1 
ATOM   4120 N N      . HIS B 1 197 ? 26.80100 -2.30000  -39.86800 1.000 18.99622  ? 188 HIS B N      1 
ATOM   4121 C CA     . HIS B 1 197 ? 26.16800 -1.57900  -41.01000 1.000 24.00946  ? 188 HIS B CA     1 
ATOM   4122 C C      . HIS B 1 197 ? 25.01300 -2.36500  -41.64300 1.000 22.41377  ? 188 HIS B C      1 
ATOM   4123 O O      . HIS B 1 197 ? 24.75500 -2.14800  -42.82200 1.000 27.41925  ? 188 HIS B O      1 
ATOM   4124 C CB     . HIS B 1 197 ? 27.26600 -1.08800  -41.96500 1.000 21.78713  ? 188 HIS B CB     1 
ATOM   4125 C CG     . HIS B 1 197 ? 28.31700 -0.25000  -41.32300 1.000 27.79229  ? 188 HIS B CG     1 
ATOM   4126 N ND1    . HIS B 1 197 ? 29.63700 -0.28800  -41.71000 1.000 33.56841  ? 188 HIS B ND1    1 
ATOM   4127 C CD2    . HIS B 1 197 ? 28.25200 0.64000   -40.33100 1.000 31.47324  ? 188 HIS B CD2    1 
ATOM   4128 C CE1    . HIS B 1 197 ? 30.33400 0.55500   -40.96800 1.000 28.88435  ? 188 HIS B CE1    1 
ATOM   4129 N NE2    . HIS B 1 197 ? 29.51100 1.12900   -40.12600 1.000 33.06529  ? 188 HIS B NE2    1 
ATOM   4130 N N      . GLY B 1 198 ? 24.35600 -3.23400  -40.88100 1.000 21.81731  ? 189 GLY B N      1 
ATOM   4131 C CA     . GLY B 1 198 ? 23.17900 -3.97400  -41.36100 1.000 26.65349  ? 189 GLY B CA     1 
ATOM   4132 C C      . GLY B 1 198 ? 23.47800 -4.96900  -42.45700 1.000 24.18323  ? 189 GLY B C      1 
ATOM   4133 O O      . GLY B 1 198 ? 22.57200 -5.26800  -43.22600 1.000 18.51584  ? 189 GLY B O      1 
ATOM   4134 N N      . TYR B 1 199 ? 24.70300 -5.48500  -42.49500 1.000 20.76622  ? 190 TYR B N      1 
ATOM   4135 C CA     . TYR B 1 199 ? 24.97900 -6.51700  -43.48300 1.000 19.38810  ? 190 TYR B CA     1 
ATOM   4136 C C      . TYR B 1 199 ? 24.71000 -7.88600  -42.85300 1.000 25.20104  ? 190 TYR B C      1 
ATOM   4137 O O      . TYR B 1 199 ? 24.00300 -7.98000  -41.84600 1.000 21.89169  ? 190 TYR B O      1 
ATOM   4138 C CB     . TYR B 1 199 ? 26.39700 -6.33600  -44.02900 1.000 19.33765  ? 190 TYR B CB     1 
ATOM   4139 C CG     . TYR B 1 199 ? 26.54800 -5.04400  -44.80100 1.000 24.68377  ? 190 TYR B CG     1 
ATOM   4140 C CD1    . TYR B 1 199 ? 25.98200 -4.89700  -46.06100 1.000 25.62451  ? 190 TYR B CD1    1 
ATOM   4141 C CD2    . TYR B 1 199 ? 27.23900 -3.96500  -44.26600 1.000 19.94567  ? 190 TYR B CD2    1 
ATOM   4142 C CE1    . TYR B 1 199 ? 26.10700 -3.71800  -46.77200 1.000 24.63924  ? 190 TYR B CE1    1 
ATOM   4143 C CE2    . TYR B 1 199 ? 27.37100 -2.78200  -44.97000 1.000 22.74589  ? 190 TYR B CE2    1 
ATOM   4144 C CZ     . TYR B 1 199 ? 26.80200 -2.66300  -46.22000 1.000 31.66946  ? 190 TYR B CZ     1 
ATOM   4145 O OH     . TYR B 1 199 ? 26.93100 -1.48700  -46.92200 1.000 28.35388  ? 190 TYR B OH     1 
ATOM   4146 N N      . LEU B 1 200 ? 25.27500 -8.95400  -43.42800 1.000 23.42913  ? 191 LEU B N      1 
ATOM   4147 C CA     . LEU B 1 200 ? 24.82100 -10.31000 -43.11900 1.000 24.94653  ? 191 LEU B CA     1 
ATOM   4148 C C      . LEU B 1 200 ? 24.88300 -10.60600 -41.62500 1.000 21.57249  ? 191 LEU B C      1 
ATOM   4149 O O      . LEU B 1 200 ? 23.92200 -11.12500 -41.04400 1.000 22.46613  ? 191 LEU B O      1 
ATOM   4150 C CB     . LEU B 1 200 ? 25.64700 -11.33600 -43.89500 1.000 24.04932  ? 191 LEU B CB     1 
ATOM   4151 C CG     . LEU B 1 200 ? 25.22200 -12.78100 -43.61800 1.000 25.21512  ? 191 LEU B CG     1 
ATOM   4152 C CD1    . LEU B 1 200 ? 23.77400 -12.99000 -44.03300 1.000 22.53222  ? 191 LEU B CD1    1 
ATOM   4153 C CD2    . LEU B 1 200 ? 26.13500 -13.78000 -44.31100 1.000 26.70490  ? 191 LEU B CD2    1 
ATOM   4154 N N      . ILE B 1 201 ? 26.00900 -10.29000 -40.98500 1.000 24.82176  ? 192 ILE B N      1 
ATOM   4155 C CA     . ILE B 1 201 ? 26.16100 -10.60300 -39.56800 1.000 22.47160  ? 192 ILE B CA     1 
ATOM   4156 C C      . ILE B 1 201 ? 25.21800 -9.75300  -38.72700 1.000 24.14961  ? 192 ILE B C      1 
ATOM   4157 O O      . ILE B 1 201 ? 24.59700 -10.24500 -37.77700 1.000 23.48523  ? 192 ILE B O      1 
ATOM   4158 C CB     . ILE B 1 201 ? 27.62800 -10.42600 -39.14100 1.000 22.43086  ? 192 ILE B CB     1 
ATOM   4159 C CG1    . ILE B 1 201 ? 28.50100 -11.46700 -39.84100 1.000 25.61822  ? 192 ILE B CG1    1 
ATOM   4160 C CG2    . ILE B 1 201 ? 27.76500 -10.53400 -37.63300 1.000 21.52559  ? 192 ILE B CG2    1 
ATOM   4161 C CD1    . ILE B 1 201 ? 29.93800 -11.43900 -39.40800 1.000 23.62865  ? 192 ILE B CD1    1 
ATOM   4162 N N      . ASP B 1 202 ? 25.08800 -8.46800  -39.06300 1.000 22.60985  ? 193 ASP B N      1 
ATOM   4163 C CA     . ASP B 1 202 ? 24.14400 -7.60900  -38.35800 1.000 23.59934  ? 193 ASP B CA     1 
ATOM   4164 C C      . ASP B 1 202 ? 22.70000 -8.03500  -38.59500 1.000 24.87569  ? 193 ASP B C      1 
ATOM   4165 O O      . ASP B 1 202 ? 21.83600 -7.74800  -37.75900 1.000 24.46424  ? 193 ASP B O      1 
ATOM   4166 C CB     . ASP B 1 202 ? 24.34200 -6.15300  -38.78600 1.000 21.89277  ? 193 ASP B CB     1 
ATOM   4167 C CG     . ASP B 1 202 ? 24.20400 -5.17700  -37.63000 1.000 27.73111  ? 193 ASP B CG     1 
ATOM   4168 O OD1    . ASP B 1 202 ? 24.29300 -5.61100  -36.46100 1.000 25.40182  ? 193 ASP B OD1    1 
ATOM   4169 O OD2    . ASP B 1 202 ? 24.00500 -3.97100  -37.89300 1.000 26.44374  ? 193 ASP B OD2    1 
ATOM   4170 N N      . GLN B 1 203 ? 22.42300 -8.71900  -39.71000 1.000 21.52109  ? 194 GLN B N      1 
ATOM   4171 C CA     . GLN B 1 203 ? 21.08100 -9.22500  -39.97200 1.000 25.30791  ? 194 GLN B CA     1 
ATOM   4172 C C      . GLN B 1 203 ? 20.70200 -10.36200 -39.03200 1.000 24.86065  ? 194 GLN B C      1 
ATOM   4173 O O      . GLN B 1 203 ? 19.51100 -10.65300 -38.87800 1.000 22.67669  ? 194 GLN B O      1 
ATOM   4174 C CB     . GLN B 1 203 ? 20.96800 -9.67600  -41.43100 1.000 19.96503  ? 194 GLN B CB     1 
ATOM   4175 C CG     . GLN B 1 203 ? 20.99300 -8.52300  -42.42700 1.000 23.34184  ? 194 GLN B CG     1 
ATOM   4176 C CD     . GLN B 1 203 ? 21.42200 -8.94800  -43.82000 1.000 24.19163  ? 194 GLN B CD     1 
ATOM   4177 O OE1    . GLN B 1 203 ? 21.19600 -10.08400 -44.23600 1.000 27.05687  ? 194 GLN B OE1    1 
ATOM   4178 N NE2    . GLN B 1 203 ? 22.04900 -8.03300  -44.54900 1.000 23.28140  ? 194 GLN B NE2    1 
ATOM   4179 N N      . PHE B 1 204 ? 21.68400 -11.01400 -38.40800 1.000 22.00350  ? 195 PHE B N      1 
ATOM   4180 C CA     . PHE B 1 204 ? 21.40900 -11.96800 -37.34100 1.000 24.04596  ? 195 PHE B CA     1 
ATOM   4181 C C      . PHE B 1 204 ? 21.39600 -11.31200 -35.96800 1.000 24.33634  ? 195 PHE B C      1 
ATOM   4182 O O      . PHE B 1 204 ? 20.63200 -11.73600 -35.09400 1.000 29.36012  ? 195 PHE B O      1 
ATOM   4183 C CB     . PHE B 1 204 ? 22.44500 -13.09700 -37.35300 1.000 23.21833  ? 195 PHE B CB     1 
ATOM   4184 C CG     . PHE B 1 204 ? 22.17200 -14.16700 -38.37400 1.000 26.40977  ? 195 PHE B CG     1 
ATOM   4185 C CD1    . PHE B 1 204 ? 22.61800 -14.03300 -39.67800 1.000 22.99821  ? 195 PHE B CD1    1 
ATOM   4186 C CD2    . PHE B 1 204 ? 21.47600 -15.31400 -38.02400 1.000 25.28420  ? 195 PHE B CD2    1 
ATOM   4187 C CE1    . PHE B 1 204 ? 22.37100 -15.01800 -40.61700 1.000 26.67966  ? 195 PHE B CE1    1 
ATOM   4188 C CE2    . PHE B 1 204 ? 21.22600 -16.30300 -38.95800 1.000 22.73497  ? 195 PHE B CE2    1 
ATOM   4189 C CZ     . PHE B 1 204 ? 21.67500 -16.15400 -40.25800 1.000 23.45869  ? 195 PHE B CZ     1 
ATOM   4190 N N      . LEU B 1 205 ? 22.21400 -10.27600 -35.76600 1.000 25.58249  ? 196 LEU B N      1 
ATOM   4191 C CA     . LEU B 1 205 ? 22.32800 -9.65400  -34.45000 1.000 24.80972  ? 196 LEU B CA     1 
ATOM   4192 C C      . LEU B 1 205 ? 21.08900 -8.83300  -34.10900 1.000 28.13661  ? 196 LEU B C      1 
ATOM   4193 O O      . LEU B 1 205 ? 20.49400 -9.00500  -33.03800 1.000 29.64110  ? 196 LEU B O      1 
ATOM   4194 C CB     . LEU B 1 205 ? 23.57900 -8.77700  -34.39400 1.000 22.97326  ? 196 LEU B CB     1 
ATOM   4195 C CG     . LEU B 1 205 ? 24.94100 -9.47400  -34.37400 1.000 21.53091  ? 196 LEU B CG     1 
ATOM   4196 C CD1    . LEU B 1 205 ? 26.05600 -8.45000  -34.50500 1.000 21.82834  ? 196 LEU B CD1    1 
ATOM   4197 C CD2    . LEU B 1 205 ? 25.10700 -10.28400 -33.09800 1.000 23.06395  ? 196 LEU B CD2    1 
ATOM   4198 N N      . LYS B 1 206 ? 20.69000 -7.93000  -35.00300 1.000 26.77593  ? 197 LYS B N      1 
ATOM   4199 C CA     . LYS B 1 206 ? 19.61600 -6.99000  -34.70600 1.000 28.10449  ? 197 LYS B CA     1 
ATOM   4200 C C      . LYS B 1 206 ? 18.26500 -7.69600  -34.69800 1.000 29.26540  ? 197 LYS B C      1 
ATOM   4201 O O      . LYS B 1 206 ? 17.90700 -8.38400  -35.65900 1.000 25.89206  ? 197 LYS B O      1 
ATOM   4202 C CB     . LYS B 1 206 ? 19.61300 -5.85500  -35.73000 1.000 27.20245  ? 197 LYS B CB     1 
ATOM   4203 C CG     . LYS B 1 206 ? 20.92300 -5.08100  -35.81600 1.000 29.91919  ? 197 LYS B CG     1 
ATOM   4204 C CD     . LYS B 1 206 ? 21.16000 -4.25100  -34.56600 1.000 27.57118  ? 197 LYS B CD     1 
ATOM   4205 C CE     . LYS B 1 206 ? 22.51400 -3.55100  -34.59800 1.000 26.67292  ? 197 LYS B CE     1 
ATOM   4206 N NZ     . LYS B 1 206 ? 22.61600 -2.53500  -35.68200 1.000 26.15140  ? 197 LYS B NZ     1 
ATOM   4207 N N      . ASP B 1 207 ? 17.50600 -7.51500  -33.61200 1.000 27.12226  ? 198 ASP B N      1 
ATOM   4208 C CA     . ASP B 1 207 ? 16.17700 -8.11200  -33.53700 1.000 28.04442  ? 198 ASP B CA     1 
ATOM   4209 C C      . ASP B 1 207 ? 15.18100 -7.41400  -34.45400 1.000 26.76266  ? 198 ASP B C      1 
ATOM   4210 O O      . ASP B 1 207 ? 14.10900 -7.96700  -34.72000 1.000 33.55371  ? 198 ASP B O      1 
ATOM   4211 C CB     . ASP B 1 207 ? 15.66400 -8.11000  -32.09300 1.000 28.53564  ? 198 ASP B CB     1 
ATOM   4212 C CG     . ASP B 1 207 ? 15.53800 -6.71300  -31.50900 1.000 30.54926  ? 198 ASP B CG     1 
ATOM   4213 O OD1    . ASP B 1 207 ? 15.90000 -5.73600  -32.19200 1.000 35.05152  ? 198 ASP B OD1    1 
ATOM   4214 O OD2    . ASP B 1 207 ? 15.07500 -6.59400  -30.35600 1.000 34.00398  ? 198 ASP B OD2    1 
ATOM   4215 N N      . GLY B 1 208 ? 15.50400 -6.21400  -34.93600 1.000 30.68305  ? 199 GLY B N      1 
ATOM   4216 C CA     . GLY B 1 208 ? 14.68900 -5.57900  -35.95600 1.000 27.41037  ? 199 GLY B CA     1 
ATOM   4217 C C      . GLY B 1 208 ? 14.77700 -6.23400  -37.31800 1.000 30.60008  ? 199 GLY B C      1 
ATOM   4218 O O      . GLY B 1 208 ? 13.94600 -5.94000  -38.18400 1.000 28.09665  ? 199 GLY B O      1 
ATOM   4219 N N      . ILE B 1 209 ? 15.76000 -7.10600  -37.52500 1.000 28.73684  ? 200 ILE B N      1 
ATOM   4220 C CA     . ILE B 1 209 ? 15.90000 -7.87500  -38.75400 1.000 25.97412  ? 200 ILE B CA     1 
ATOM   4221 C C      . ILE B 1 209 ? 15.67800 -9.36200  -38.50100 1.000 27.89584  ? 200 ILE B C      1 
ATOM   4222 O O      . ILE B 1 209 ? 14.93100 -10.02000 -39.22600 1.000 29.80336  ? 200 ILE B O      1 
ATOM   4223 C CB     . ILE B 1 209 ? 17.27900 -7.62700  -39.40800 1.000 24.37679  ? 200 ILE B CB     1 
ATOM   4224 C CG1    . ILE B 1 209 ? 17.48900 -6.13500  -39.66600 1.000 22.61629  ? 200 ILE B CG1    1 
ATOM   4225 C CG2    . ILE B 1 209 ? 17.40900 -8.41700  -40.70200 1.000 22.14652  ? 200 ILE B CG2    1 
ATOM   4226 C CD1    . ILE B 1 209 ? 18.86800 -5.79300  -40.18900 1.000 21.83046  ? 200 ILE B CD1    1 
ATOM   4227 N N      . ASN B 1 210 ? 16.31300 -9.90200  -37.46400 1.000 28.36585  ? 201 ASN B N      1 
ATOM   4228 C CA     . ASN B 1 210 ? 16.24400 -11.33100 -37.17300 1.000 26.11860  ? 201 ASN B CA     1 
ATOM   4229 C C      . ASN B 1 210 ? 14.86600 -11.67500 -36.62200 1.000 35.27498  ? 201 ASN B C      1 
ATOM   4230 O O      . ASN B 1 210 ? 14.54700 -11.35400 -35.47200 1.000 32.81399  ? 201 ASN B O      1 
ATOM   4231 C CB     . ASN B 1 210 ? 17.34300 -11.71500 -36.18600 1.000 27.42776  ? 201 ASN B CB     1 
ATOM   4232 C CG     . ASN B 1 210 ? 17.54800 -13.21700 -36.08700 1.000 28.53072  ? 201 ASN B CG     1 
ATOM   4233 O OD1    . ASN B 1 210 ? 16.61500 -13.99900 -36.26200 1.000 26.97665  ? 201 ASN B OD1    1 
ATOM   4234 N ND2    . ASN B 1 210 ? 18.77900 -13.62500 -35.79900 1.000 27.05785  ? 201 ASN B ND2    1 
ATOM   4235 N N      . ASP B 1 211 ? 14.04500 -12.32700 -37.44600 1.000 31.10926  ? 202 ASP B N      1 
ATOM   4236 C CA     . ASP B 1 211 ? 12.73200 -12.81100 -37.03800 1.000 30.22952  ? 202 ASP B CA     1 
ATOM   4237 C C      . ASP B 1 211 ? 12.67500 -14.33500 -37.02300 1.000 32.94729  ? 202 ASP B C      1 
ATOM   4238 O O      . ASP B 1 211 ? 11.59300 -14.92000 -37.14700 1.000 34.21858  ? 202 ASP B O      1 
ATOM   4239 C CB     . ASP B 1 211 ? 11.64700 -12.23800 -37.95100 1.000 25.80649  ? 202 ASP B CB     1 
ATOM   4240 C CG     . ASP B 1 211 ? 11.81200 -12.66600 -39.40100 1.000 35.47388  ? 202 ASP B CG     1 
ATOM   4241 O OD1    . ASP B 1 211 ? 12.92400 -13.09000 -39.78100 1.000 31.95812  ? 202 ASP B OD1    1 
ATOM   4242 O OD2    . ASP B 1 211 ? 10.82700 -12.57500 -40.16400 1.000 38.52358  ? 202 ASP B OD2    1 
ATOM   4243 N N      . ARG B 1 212 ? 13.82600 -14.98600 -36.87000 1.000 32.61281  ? 203 ARG B N      1 
ATOM   4244 C CA     . ARG B 1 212 ? 13.89300 -16.43500 -36.92900 1.000 35.77798  ? 203 ARG B CA     1 
ATOM   4245 C C      . ARG B 1 212 ? 13.28000 -17.06100 -35.68000 1.000 35.85861  ? 203 ARG B C      1 
ATOM   4246 O O      . ARG B 1 212 ? 13.17200 -16.43700 -34.62100 1.000 34.59147  ? 203 ARG B O      1 
ATOM   4247 C CB     . ARG B 1 212 ? 15.34000 -16.89600 -37.08300 1.000 27.94206  ? 203 ARG B CB     1 
ATOM   4248 C CG     . ARG B 1 212 ? 16.02500 -16.37100 -38.33000 1.000 27.13335  ? 203 ARG B CG     1 
ATOM   4249 C CD     . ARG B 1 212 ? 17.48700 -16.77700 -38.36400 1.000 27.05385  ? 203 ARG B CD     1 
ATOM   4250 N NE     . ARG B 1 212 ? 17.64900 -18.20800 -38.58600 1.000 25.61291  ? 203 ARG B NE     1 
ATOM   4251 C CZ     . ARG B 1 212 ? 17.82000 -18.76400 -39.77700 1.000 27.97237  ? 203 ARG B CZ     1 
ATOM   4252 N NH1    . ARG B 1 212 ? 17.86100 -18.03400 -40.88100 1.000 28.35716  ? 203 ARG B NH1    1 
ATOM   4253 N NH2    . ARG B 1 212 ? 17.95300 -20.08500 -39.86400 1.000 27.72220  ? 203 ARG B NH2    1 
ATOM   4254 N N      . THR B 1 213 ? 12.87900 -18.32200 -35.82200 1.000 34.81613  ? 204 THR B N      1 
ATOM   4255 C CA     . THR B 1 213 ? 12.31900 -19.09200 -34.72400 1.000 34.34613  ? 204 THR B CA     1 
ATOM   4256 C C      . THR B 1 213 ? 13.16100 -20.30700 -34.36300 1.000 34.44802  ? 204 THR B C      1 
ATOM   4257 O O      . THR B 1 213 ? 12.77800 -21.06000 -33.46100 1.000 35.78674  ? 204 THR B O      1 
ATOM   4258 C CB     . THR B 1 213 ? 10.89100 -19.54000 -35.06200 1.000 40.48918  ? 204 THR B CB     1 
ATOM   4259 O OG1    . THR B 1 213 ? 10.89600 -20.26300 -36.30000 1.000 36.09904  ? 204 THR B OG1    1 
ATOM   4260 C CG2    . THR B 1 213 ? 9.96900  -18.33400 -35.19000 1.000 36.39121  ? 204 THR B CG2    1 
ATOM   4261 N N      . ASP B 1 214 ? 14.28900 -20.52200 -35.03300 1.000 35.80478  ? 205 ASP B N      1 
ATOM   4262 C CA     . ASP B 1 214 ? 15.16800 -21.64000 -34.72200 1.000 33.52159  ? 205 ASP B CA     1 
ATOM   4263 C C      . ASP B 1 214 ? 16.20200 -21.18700 -33.69000 1.000 30.31188  ? 205 ASP B C      1 
ATOM   4264 O O      . ASP B 1 214 ? 16.02300 -20.16600 -33.02000 1.000 32.29130  ? 205 ASP B O      1 
ATOM   4265 C CB     . ASP B 1 214 ? 15.80200 -22.18100 -36.00800 1.000 34.32838  ? 205 ASP B CB     1 
ATOM   4266 C CG     . ASP B 1 214 ? 16.63100 -21.13900 -36.73800 1.000 37.17388  ? 205 ASP B CG     1 
ATOM   4267 O OD1    . ASP B 1 214 ? 16.60400 -19.95600 -36.33800 1.000 32.44602  ? 205 ASP B OD1    1 
ATOM   4268 O OD2    . ASP B 1 214 ? 17.31400 -21.50700 -37.71700 1.000 34.80858  ? 205 ASP B OD2    1 
ATOM   4269 N N      . GLU B 1 215 ? 17.30200 -21.92900 -33.55900 1.000 32.63666  ? 206 GLU B N      1 
ATOM   4270 C CA     . GLU B 1 215 ? 18.30900 -21.60900 -32.55300 1.000 36.68650  ? 206 GLU B CA     1 
ATOM   4271 C C      . GLU B 1 215 ? 19.16100 -20.39900 -32.91800 1.000 35.25635  ? 206 GLU B C      1 
ATOM   4272 O O      . GLU B 1 215 ? 20.05600 -20.04800 -32.14300 1.000 33.62667  ? 206 GLU B O      1 
ATOM   4273 C CB     . GLU B 1 215 ? 19.21200 -22.82100 -32.30700 1.000 38.13655  ? 206 GLU B CB     1 
ATOM   4274 C CG     . GLU B 1 215 ? 20.29507 -23.03114 -33.35629 1.000 39.40194  ? 206 GLU B CG     1 
ATOM   4275 C CD     . GLU B 1 215 ? 20.07713 -24.28277 -34.18308 1.000 47.40926  ? 206 GLU B CD     1 
ATOM   4276 O OE1    . GLU B 1 215 ? 18.95261 -24.47508 -34.69283 1.000 46.13778  ? 206 GLU B OE1    1 
ATOM   4277 O OE2    . GLU B 1 215 ? 21.03183 -25.07775 -34.31693 1.000 43.22523  ? 206 GLU B OE2    1 
ATOM   4278 N N      . TYR B 1 216 ? 18.91500 -19.75500 -34.05900 1.000 31.62354  ? 207 TYR B N      1 
ATOM   4279 C CA     . TYR B 1 216 ? 19.65900 -18.56700 -34.45900 1.000 28.06636  ? 207 TYR B CA     1 
ATOM   4280 C C      . TYR B 1 216 ? 18.86200 -17.27900 -34.30500 1.000 28.75337  ? 207 TYR B C      1 
ATOM   4281 O O      . TYR B 1 216 ? 19.36200 -16.21200 -34.67500 1.000 32.92452  ? 207 TYR B O      1 
ATOM   4282 C CB     . TYR B 1 216 ? 20.14300 -18.70500 -35.90800 1.000 27.48485  ? 207 TYR B CB     1 
ATOM   4283 C CG     . TYR B 1 216 ? 21.34200 -19.61200 -36.05700 1.000 28.35196  ? 207 TYR B CG     1 
ATOM   4284 C CD1    . TYR B 1 216 ? 21.18600 -20.97400 -36.26800 1.000 31.54606  ? 207 TYR B CD1    1 
ATOM   4285 C CD2    . TYR B 1 216 ? 22.63200 -19.10500 -35.97500 1.000 26.25850  ? 207 TYR B CD2    1 
ATOM   4286 C CE1    . TYR B 1 216 ? 22.28100 -21.80700 -36.39900 1.000 28.80799  ? 207 TYR B CE1    1 
ATOM   4287 C CE2    . TYR B 1 216 ? 23.73300 -19.92800 -36.10400 1.000 26.54537  ? 207 TYR B CE2    1 
ATOM   4288 C CZ     . TYR B 1 216 ? 23.55200 -21.27800 -36.31600 1.000 26.84894  ? 207 TYR B CZ     1 
ATOM   4289 O OH     . TYR B 1 216 ? 24.64600 -22.10200 -36.44500 1.000 31.33460  ? 207 TYR B OH     1 
ATOM   4290 N N      . GLY B 1 217 ? 17.64500 -17.34400 -33.76700 1.000 30.34635  ? 208 GLY B N      1 
ATOM   4291 C CA     . GLY B 1 217 ? 16.83400 -16.15700 -33.59900 1.000 28.27515  ? 208 GLY B CA     1 
ATOM   4292 C C      . GLY B 1 217 ? 16.16400 -16.14400 -32.24000 1.000 32.23403  ? 208 GLY B C      1 
ATOM   4293 O O      . GLY B 1 217 ? 16.09200 -17.15800 -31.54300 1.000 34.46314  ? 208 GLY B O      1 
ATOM   4294 N N      . GLY B 1 218 ? 15.67300 -14.96300 -31.87300 1.000 30.56063  ? 209 GLY B N      1 
ATOM   4295 C CA     . GLY B 1 218 ? 14.97000 -14.80100 -30.61600 1.000 27.65220  ? 209 GLY B CA     1 
ATOM   4296 C C      . GLY B 1 218 ? 15.81500 -14.18500 -29.52000 1.000 33.09534  ? 209 GLY B C      1 
ATOM   4297 O O      . GLY B 1 218 ? 16.01500 -12.96700 -29.49200 1.000 31.78611  ? 209 GLY B O      1 
ATOM   4298 N N      . SER B 1 219 ? 16.31800 -15.02100 -28.61500 1.000 28.54403  ? 210 SER B N      1 
ATOM   4299 C CA     . SER B 1 219 ? 17.06500 -14.53900 -27.46500 1.000 29.56852  ? 210 SER B CA     1 
ATOM   4300 C C      . SER B 1 219 ? 18.39300 -13.91800 -27.89600 1.000 33.50210  ? 210 SER B C      1 
ATOM   4301 O O      . SER B 1 219 ? 18.86100 -14.09300 -29.02500 1.000 29.88877  ? 210 SER B O      1 
ATOM   4302 C CB     . SER B 1 219 ? 17.31900 -15.68100 -26.48100 1.000 29.86948  ? 210 SER B CB     1 
ATOM   4303 O OG     . SER B 1 219 ? 18.04400 -16.72500 -27.10700 1.000 31.88986  ? 210 SER B OG     1 
ATOM   4304 N N      . LEU B 1 220 ? 19.00300 -13.18200 -26.96400 1.000 30.54239  ? 211 LEU B N      1 
ATOM   4305 C CA     . LEU B 1 220 ? 20.30900 -12.58500 -27.22500 1.000 31.66151  ? 211 LEU B CA     1 
ATOM   4306 C C      . LEU B 1 220 ? 21.35200 -13.65000 -27.53500 1.000 29.54979  ? 211 LEU B C      1 
ATOM   4307 O O      . LEU B 1 220 ? 22.20900 -13.45400 -28.40500 1.000 27.09684  ? 211 LEU B O      1 
ATOM   4308 C CB     . LEU B 1 220 ? 20.74900 -11.73700 -26.03100 1.000 27.37871  ? 211 LEU B CB     1 
ATOM   4309 C CG     . LEU B 1 220 ? 20.14300 -10.33900 -25.90200 1.000 32.12414  ? 211 LEU B CG     1 
ATOM   4310 C CD1    . LEU B 1 220 ? 20.51000 -9.72900  -24.56100 1.000 30.34631  ? 211 LEU B CD1    1 
ATOM   4311 C CD2    . LEU B 1 220 ? 20.61100 -9.44500  -27.04100 1.000 30.44293  ? 211 LEU B CD2    1 
ATOM   4312 N N      . ALA B 1 221 ? 21.29800 -14.78500 -26.83300 1.000 28.90734  ? 212 ALA B N      1 
ATOM   4313 C CA     . ALA B 1 221 ? 22.25300 -15.85800 -27.09000 1.000 28.93492  ? 212 ALA B CA     1 
ATOM   4314 C C      . ALA B 1 221 ? 22.07500 -16.43000 -28.49000 1.000 31.62576  ? 212 ALA B C      1 
ATOM   4315 O O      . ALA B 1 221 ? 23.05900 -16.71100 -29.18500 1.000 28.68808  ? 212 ALA B O      1 
ATOM   4316 C CB     . ALA B 1 221 ? 22.10700 -16.95700 -26.03800 1.000 30.15640  ? 212 ALA B CB     1 
ATOM   4317 N N      . ASN B 1 222 ? 20.82500 -16.60400 -28.92300 1.000 30.42318  ? 213 ASN B N      1 
ATOM   4318 C CA     . ASN B 1 222 ? 20.57300 -17.12200 -30.26400 1.000 30.46596  ? 213 ASN B CA     1 
ATOM   4319 C C      . ASN B 1 222 ? 20.99500 -16.12100 -31.33300 1.000 27.64368  ? 213 ASN B C      1 
ATOM   4320 O O      . ASN B 1 222 ? 21.55600 -16.50800 -32.36500 1.000 29.40714  ? 213 ASN B O      1 
ATOM   4321 C CB     . ASN B 1 222 ? 19.09600 -17.48200 -30.41700 1.000 31.56962  ? 213 ASN B CB     1 
ATOM   4322 C CG     . ASN B 1 222 ? 18.71900 -18.73500 -29.65200 1.000 31.67902  ? 213 ASN B CG     1 
ATOM   4323 O OD1    . ASN B 1 222 ? 19.52200 -19.27800 -28.89000 1.000 30.04819  ? 213 ASN B OD1    1 
ATOM   4324 N ND2    . ASN B 1 222 ? 17.49300 -19.20200 -29.85000 1.000 26.91894  ? 213 ASN B ND2    1 
ATOM   4325 N N      . ARG B 1 223 ? 20.73900 -14.83100 -31.10600 1.000 26.39121  ? 214 ARG B N      1 
ATOM   4326 C CA     . ARG B 1 223 ? 21.08500 -13.82300 -32.10100 1.000 28.96512  ? 214 ARG B CA     1 
ATOM   4327 C C      . ARG B 1 223 ? 22.58400 -13.56400 -32.17400 1.000 26.17290  ? 214 ARG B C      1 
ATOM   4328 O O      . ARG B 1 223 ? 23.06000 -13.04400 -33.18900 1.000 25.99455  ? 214 ARG B O      1 
ATOM   4329 C CB     . ARG B 1 223 ? 20.33400 -12.52000 -31.81400 1.000 27.47694  ? 214 ARG B CB     1 
ATOM   4330 C CG     . ARG B 1 223 ? 18.84000 -12.61100 -32.08600 1.000 27.97189  ? 214 ARG B CG     1 
ATOM   4331 C CD     . ARG B 1 223 ? 18.16100 -11.24800 -32.05600 1.000 28.75253  ? 214 ARG B CD     1 
ATOM   4332 N NE     . ARG B 1 223 ? 17.75200 -10.85600 -30.71200 1.000 37.25132  ? 214 ARG B NE     1 
ATOM   4333 C CZ     . ARG B 1 223 ? 18.27200 -9.84400  -30.03000 1.000 30.94390  ? 214 ARG B CZ     1 
ATOM   4334 N NH1    . ARG B 1 223 ? 19.22900 -9.08700  -30.53900 1.000 28.24850  ? 214 ARG B NH1    1 
ATOM   4335 N NH2    . ARG B 1 223 ? 17.81100 -9.58000  -28.81100 1.000 32.69882  ? 214 ARG B NH2    1 
ATOM   4336 N N      . CYS B 1 224 ? 23.33500 -13.90900 -31.13200 1.000 24.25499  ? 215 CYS B N      1 
ATOM   4337 C CA     . CYS B 1 224 ? 24.78800 -13.79900 -31.15300 1.000 27.89823  ? 215 CYS B CA     1 
ATOM   4338 C C      . CYS B 1 224 ? 25.46400 -15.06700 -31.64900 1.000 23.74905  ? 215 CYS B C      1 
ATOM   4339 O O      . CYS B 1 224 ? 26.69500 -15.10100 -31.74100 1.000 24.48240  ? 215 CYS B O      1 
ATOM   4340 C CB     . CYS B 1 224 ? 25.31900 -13.45800 -29.75600 1.000 20.09090  ? 215 CYS B CB     1 
ATOM   4341 S SG     . CYS B 1 224 ? 24.96700 -11.78000 -29.20700 1.000 29.84342  ? 215 CYS B SG     1 
ATOM   4342 N N      . LYS B 1 225 ? 24.69200 -16.10600 -31.96900 1.000 22.66061  ? 216 LYS B N      1 
ATOM   4343 C CA     . LYS B 1 225 ? 25.28900 -17.39000 -32.31500 1.000 29.96994  ? 216 LYS B CA     1 
ATOM   4344 C C      . LYS B 1 225 ? 26.03500 -17.32300 -33.64300 1.000 27.73745  ? 216 LYS B C      1 
ATOM   4345 O O      . LYS B 1 225 ? 27.09400 -17.94200 -33.79500 1.000 28.06661  ? 216 LYS B O      1 
ATOM   4346 C CB     . LYS B 1 225 ? 24.20700 -18.46800 -32.35100 1.000 35.16869  ? 216 LYS B CB     1 
ATOM   4347 C CG     . LYS B 1 225 ? 24.73100 -19.88200 -32.49700 1.000 34.57140  ? 216 LYS B CG     1 
ATOM   4348 C CD     . LYS B 1 225 ? 23.61900 -20.88900 -32.25400 1.000 39.76039  ? 216 LYS B CD     1 
ATOM   4349 C CE     . LYS B 1 225 ? 23.00000 -20.68700 -30.87900 1.000 40.61839  ? 216 LYS B CE     1 
ATOM   4350 N NZ     . LYS B 1 225 ? 21.84200 -21.59300 -30.63900 1.000 38.52090  ? 216 LYS B NZ     1 
ATOM   4351 N N      . PHE B 1 226 ? 25.51100 -16.56900 -34.61300 1.000 22.20464  ? 217 PHE B N      1 
ATOM   4352 C CA     . PHE B 1 226 ? 26.14800 -16.53100 -35.92700 1.000 24.91392  ? 217 PHE B CA     1 
ATOM   4353 C C      . PHE B 1 226 ? 27.50700 -15.84400 -35.86500 1.000 24.53064  ? 217 PHE B C      1 
ATOM   4354 O O      . PHE B 1 226 ? 28.50600 -16.38400 -36.35300 1.000 28.58153  ? 217 PHE B O      1 
ATOM   4355 C CB     . PHE B 1 226 ? 25.24400 -15.84200 -36.94800 1.000 21.61994  ? 217 PHE B CB     1 
ATOM   4356 C CG     . PHE B 1 226 ? 25.82500 -15.80400 -38.33500 1.000 28.31824  ? 217 PHE B CG     1 
ATOM   4357 C CD1    . PHE B 1 226 ? 26.03900 -16.97600 -39.04200 1.000 23.57486  ? 217 PHE B CD1    1 
ATOM   4358 C CD2    . PHE B 1 226 ? 26.15900 -14.59800 -38.93000 1.000 22.58646  ? 217 PHE B CD2    1 
ATOM   4359 C CE1    . PHE B 1 226 ? 26.57700 -16.94800 -40.31600 1.000 25.94187  ? 217 PHE B CE1    1 
ATOM   4360 C CE2    . PHE B 1 226 ? 26.69500 -14.56300 -40.20400 1.000 31.61396  ? 217 PHE B CE2    1 
ATOM   4361 C CZ     . PHE B 1 226 ? 26.90400 -15.74000 -40.89900 1.000 25.35535  ? 217 PHE B CZ     1 
ATOM   4362 N N      . ILE B 1 227 ? 27.56900 -14.65000 -35.26700 1.000 24.94139  ? 218 ILE B N      1 
ATOM   4363 C CA     . ILE B 1 227 ? 28.84800 -13.94700 -35.19100 1.000 23.14870  ? 218 ILE B CA     1 
ATOM   4364 C C      . ILE B 1 227 ? 29.83500 -14.71400 -34.31900 1.000 22.87533  ? 218 ILE B C      1 
ATOM   4365 O O      . ILE B 1 227 ? 31.04400 -14.69600 -34.58100 1.000 24.86331  ? 218 ILE B O      1 
ATOM   4366 C CB     . ILE B 1 227 ? 28.65400 -12.50100 -34.69300 1.000 22.87311  ? 218 ILE B CB     1 
ATOM   4367 C CG1    . ILE B 1 227 ? 29.97100 -11.72200 -34.79000 1.000 21.48684  ? 218 ILE B CG1    1 
ATOM   4368 C CG2    . ILE B 1 227 ? 28.11600 -12.47800 -33.27000 1.000 22.84555  ? 218 ILE B CG2    1 
ATOM   4369 C CD1    . ILE B 1 227 ? 29.86000 -10.26500 -34.38000 1.000 21.63060  ? 218 ILE B CD1    1 
ATOM   4370 N N      . THR B 1 228 ? 29.34900 -15.40600 -33.28700 1.000 24.81892  ? 219 THR B N      1 
ATOM   4371 C CA     . THR B 1 228 ? 30.23300 -16.21700 -32.45500 1.000 24.25212  ? 219 THR B CA     1 
ATOM   4372 C C      . THR B 1 228 ? 30.89300 -17.31900 -33.27500 1.000 24.76093  ? 219 THR B C      1 
ATOM   4373 O O      . THR B 1 228 ? 32.11900 -17.48300 -33.24800 1.000 25.79756  ? 219 THR B O      1 
ATOM   4374 C CB     . THR B 1 228 ? 29.45000 -16.81500 -31.28400 1.000 27.14798  ? 219 THR B CB     1 
ATOM   4375 O OG1    . THR B 1 228 ? 28.98300 -15.76500 -30.42700 1.000 27.44231  ? 219 THR B OG1    1 
ATOM   4376 C CG2    . THR B 1 228 ? 30.32300 -17.76600 -30.48400 1.000 27.13474  ? 219 THR B CG2    1 
ATOM   4377 N N      . GLN B 1 229 ? 30.09000 -18.08200 -34.02200 1.000 27.08813  ? 220 GLN B N      1 
ATOM   4378 C CA     . GLN B 1 229 ? 30.63300 -19.18800 -34.80600 1.000 27.45378  ? 220 GLN B CA     1 
ATOM   4379 C C      . GLN B 1 229 ? 31.56300 -18.69700 -35.90800 1.000 27.65525  ? 220 GLN B C      1 
ATOM   4380 O O      . GLN B 1 229 ? 32.49900 -19.40900 -36.28900 1.000 27.48126  ? 220 GLN B O      1 
ATOM   4381 C CB     . GLN B 1 229 ? 29.49200 -20.02000 -35.39800 1.000 25.87356  ? 220 GLN B CB     1 
ATOM   4382 C CG     . GLN B 1 229 ? 28.64200 -20.73100 -34.35300 1.000 29.43057  ? 220 GLN B CG     1 
ATOM   4383 C CD     . GLN B 1 229 ? 27.37800 -21.33500 -34.93500 1.000 35.03944  ? 220 GLN B CD     1 
ATOM   4384 O OE1    . GLN B 1 229 ? 27.05600 -21.12700 -36.10500 1.000 36.41795  ? 220 GLN B OE1    1 
ATOM   4385 N NE2    . GLN B 1 229 ? 26.65400 -22.08800 -34.11700 1.000 40.05424  ? 220 GLN B NE2    1 
ATOM   4386 N N      . VAL B 1 230 ? 31.33100 -17.49200 -36.42800 1.000 26.71184  ? 221 VAL B N      1 
ATOM   4387 C CA     . VAL B 1 230 ? 32.23500 -16.93600 -37.42900 1.000 25.78917  ? 221 VAL B CA     1 
ATOM   4388 C C      . VAL B 1 230 ? 33.58500 -16.61100 -36.80100 1.000 24.24088  ? 221 VAL B C      1 
ATOM   4389 O O      . VAL B 1 230 ? 34.64000 -16.96800 -37.33800 1.000 24.41310  ? 221 VAL B O      1 
ATOM   4390 C CB     . VAL B 1 230 ? 31.60900 -15.69800 -38.09600 1.000 25.94933  ? 221 VAL B CB     1 
ATOM   4391 C CG1    . VAL B 1 230 ? 32.63400 -14.99200 -38.97100 1.000 24.24753  ? 221 VAL B CG1    1 
ATOM   4392 C CG2    . VAL B 1 230 ? 30.39500 -16.09700 -38.91900 1.000 25.06851  ? 221 VAL B CG2    1 
ATOM   4393 N N      . VAL B 1 231 ? 33.57300 -15.95000 -35.65000 1.000 28.55260  ? 222 VAL B N      1 
ATOM   4394 C CA     . VAL B 1 231 ? 34.84900 -15.54800 -34.98200 1.000 28.04479  ? 222 VAL B CA     1 
ATOM   4395 C C      . VAL B 1 231 ? 35.59500 -16.82100 -34.55200 1.000 26.24426  ? 222 VAL B C      1 
ATOM   4396 O O      . VAL B 1 231 ? 36.80400 -16.88600 -34.75200 1.000 29.29653  ? 222 VAL B O      1 
ATOM   4397 C CB     . VAL B 1 231 ? 34.64700 -14.56100 -33.81300 1.000 24.00511  ? 222 VAL B CB     1 
ATOM   4398 C CG1    . VAL B 1 231 ? 35.95000 -14.25200 -33.09200 1.000 21.43567  ? 222 VAL B CG1    1 
ATOM   4399 C CG2    . VAL B 1 231 ? 33.96900 -13.27700 -34.26700 1.000 24.19583  ? 222 VAL B CG2    1 
ATOM   4400 N N      . GLN B 1 232 ? 34.86200 -17.81000 -34.04800 1.000 26.41063  ? 223 GLN B N      1 
ATOM   4401 C CA     . GLN B 1 232 ? 35.49600 -19.07400 -33.60600 1.000 29.68683  ? 223 GLN B CA     1 
ATOM   4402 C C      . GLN B 1 232 ? 36.22900 -19.71900 -34.79300 1.000 29.74673  ? 223 GLN B C      1 
ATOM   4403 O O      . GLN B 1 232 ? 37.37500 -20.14300 -34.59800 1.000 32.56728  ? 223 GLN B O      1 
ATOM   4404 C CB     . GLN B 1 232 ? 34.50000 -20.03400 -32.95300 1.000 25.74383  ? 223 GLN B CB     1 
ATOM   4405 C CG     . GLN B 1 232 ? 33.81439 -19.47400 -31.71398 1.000 35.94755  ? 223 GLN B CG     1 
ATOM   4406 C CD     . GLN B 1 232 ? 32.93893 -20.48346 -31.00201 1.000 45.40866  ? 223 GLN B CD     1 
ATOM   4407 O OE1    . GLN B 1 232 ? 31.88651 -20.89761 -31.49980 1.000 38.06107  ? 223 GLN B OE1    1 
ATOM   4408 N NE2    . GLN B 1 232 ? 33.36864 -20.88466 -29.81650 1.000 38.45558  ? 223 GLN B NE2    1 
ATOM   4409 N N      . ALA B 1 233 ? 35.59000 -19.78400 -35.95700 1.000 24.16318  ? 224 ALA B N      1 
ATOM   4410 C CA     . ALA B 1 233 ? 36.21300 -20.45200 -37.12400 1.000 26.53422  ? 224 ALA B CA     1 
ATOM   4411 C C      . ALA B 1 233 ? 37.48200 -19.71400 -37.56900 1.000 27.00969  ? 224 ALA B C      1 
ATOM   4412 O O      . ALA B 1 233 ? 38.48200 -20.39200 -37.83100 1.000 26.97472  ? 224 ALA B O      1 
ATOM   4413 C CB     . ALA B 1 233 ? 35.21800 -20.59600 -38.24100 1.000 20.47047  ? 224 ALA B CB     1 
ATOM   4414 N N      . VAL B 1 234 ? 37.44200 -18.38200 -37.63200 1.000 22.88229  ? 225 VAL B N      1 
ATOM   4415 C CA     . VAL B 1 234 ? 38.62800 -17.67200 -38.10100 1.000 27.98499  ? 225 VAL B CA     1 
ATOM   4416 C C      . VAL B 1 234 ? 39.72200 -17.68200 -37.04100 1.000 24.34258  ? 225 VAL B C      1 
ATOM   4417 O O      . VAL B 1 234 ? 40.91300 -17.64100 -37.37200 1.000 27.75916  ? 225 VAL B O      1 
ATOM   4418 C CB     . VAL B 1 234 ? 38.26500 -16.23900 -38.54000 1.000 27.18767  ? 225 VAL B CB     1 
ATOM   4419 C CG1    . VAL B 1 234 ? 37.33900 -16.27300 -39.74700 1.000 28.05372  ? 225 VAL B CG1    1 
ATOM   4420 C CG2    . VAL B 1 234 ? 37.62300 -15.46700 -37.39900 1.000 23.77392  ? 225 VAL B CG2    1 
ATOM   4421 N N      . VAL B 1 235 ? 39.35100 -17.74200 -35.76000 1.000 26.91569  ? 226 VAL B N      1 
ATOM   4422 C CA     . VAL B 1 235 ? 40.35200 -17.86100 -34.70200 1.000 27.12844  ? 226 VAL B CA     1 
ATOM   4423 C C      . VAL B 1 235 ? 41.06900 -19.20200 -34.80000 1.000 25.47702  ? 226 VAL B C      1 
ATOM   4424 O O      . VAL B 1 235 ? 42.30300 -19.27000 -34.76400 1.000 28.45114  ? 226 VAL B O      1 
ATOM   4425 C CB     . VAL B 1 235 ? 39.70300 -17.66600 -33.31900 1.000 28.04097  ? 226 VAL B CB     1 
ATOM   4426 C CG1    . VAL B 1 235 ? 40.56700 -18.28500 -32.23000 1.000 22.99462  ? 226 VAL B CG1    1 
ATOM   4427 C CG2    . VAL B 1 235 ? 39.48700 -16.18700 -33.04100 1.000 26.36589  ? 226 VAL B CG2    1 
ATOM   4428 N N      . SER B 1 236 ? 40.30600 -20.28900 -34.93600 1.000 22.98524  ? 227 SER B N      1 
ATOM   4429 C CA     . SER B 1 236 ? 40.90900 -21.61200 -35.03900 1.000 27.66924  ? 227 SER B CA     1 
ATOM   4430 C C      . SER B 1 236 ? 41.74400 -21.77400 -36.30200 1.000 26.76975  ? 227 SER B C      1 
ATOM   4431 O O      . SER B 1 236 ? 42.61600 -22.64800 -36.34700 1.000 30.35335  ? 227 SER B O      1 
ATOM   4432 C CB     . SER B 1 236 ? 39.82200 -22.68700 -34.99700 1.000 25.51480  ? 227 SER B CB     1 
ATOM   4433 O OG     . SER B 1 236 ? 38.92238 -22.45765 -33.92781 1.000 45.18202  ? 227 SER B OG     1 
ATOM   4434 N N      . ALA B 1 237 ? 41.50400 -20.95200 -37.32200 1.000 26.60979  ? 228 ALA B N      1 
ATOM   4435 C CA     . ALA B 1 237 ? 42.20700 -21.09200 -38.59100 1.000 27.48224  ? 228 ALA B CA     1 
ATOM   4436 C C      . ALA B 1 237 ? 43.53100 -20.33300 -38.61100 1.000 25.86960  ? 228 ALA B C      1 
ATOM   4437 O O      . ALA B 1 237 ? 44.55100 -20.87700 -39.04500 1.000 25.54319  ? 228 ALA B O      1 
ATOM   4438 C CB     . ALA B 1 237 ? 41.31100 -20.62100 -39.74100 1.000 26.85559  ? 228 ALA B CB     1 
ATOM   4439 N N      . ILE B 1 238 ? 43.53500 -19.08100 -38.15100 1.000 23.75630  ? 229 ILE B N      1 
ATOM   4440 C CA     . ILE B 1 238 ? 44.69900 -18.21200 -38.27100 1.000 26.08804  ? 229 ILE B CA     1 
ATOM   4441 C C      . ILE B 1 238 ? 45.17200 -17.65900 -36.93500 1.000 26.76843  ? 229 ILE B C      1 
ATOM   4442 O O      . ILE B 1 238 ? 46.18500 -16.95300 -36.89700 1.000 29.87945  ? 229 ILE B O      1 
ATOM   4443 C CB     . ILE B 1 238 ? 44.43500 -17.05600 -39.25900 1.000 25.82437  ? 229 ILE B CB     1 
ATOM   4444 C CG1    . ILE B 1 238 ? 43.45200 -16.05000 -38.66300 1.000 26.13197  ? 229 ILE B CG1    1 
ATOM   4445 C CG2    . ILE B 1 238 ? 43.89300 -17.58900 -40.57500 1.000 26.58932  ? 229 ILE B CG2    1 
ATOM   4446 C CD1    . ILE B 1 238 ? 43.21100 -14.84600 -39.54800 1.000 30.71047  ? 229 ILE B CD1    1 
ATOM   4447 N N      . GLY B 1 239 ? 44.47700 -17.95000 -35.83800 1.000 24.49881  ? 230 GLY B N      1 
ATOM   4448 C CA     . GLY B 1 239 ? 44.87800 -17.43900 -34.54000 1.000 24.93195  ? 230 GLY B CA     1 
ATOM   4449 C C      . GLY B 1 239 ? 44.13600 -16.18500 -34.12000 1.000 27.88869  ? 230 GLY B C      1 
ATOM   4450 O O      . GLY B 1 239 ? 43.87600 -15.30400 -34.94500 1.000 26.45234  ? 230 GLY B O      1 
ATOM   4451 N N      . ALA B 1 240 ? 43.80300 -16.09200 -32.82800 1.000 27.64091  ? 231 ALA B N      1 
ATOM   4452 C CA     . ALA B 1 240 ? 43.02100 -14.96200 -32.33200 1.000 25.29678  ? 231 ALA B CA     1 
ATOM   4453 C C      . ALA B 1 240 ? 43.75800 -13.63800 -32.49100 1.000 29.98691  ? 231 ALA B C      1 
ATOM   4454 O O      . ALA B 1 240 ? 43.12800 -12.60600 -32.74900 1.000 26.30332  ? 231 ALA B O      1 
ATOM   4455 C CB     . ALA B 1 240 ? 42.65000 -15.18500 -30.86500 1.000 24.85642  ? 231 ALA B CB     1 
ATOM   4456 N N      . ASP B 1 241 ? 45.08600 -13.64300 -32.34400 1.000 22.30360  ? 232 ASP B N      1 
ATOM   4457 C CA     . ASP B 1 241 ? 45.86800 -12.41500 -32.43200 1.000 24.48231  ? 232 ASP B CA     1 
ATOM   4458 C C      . ASP B 1 241 ? 45.87700 -11.80700 -33.82900 1.000 28.01357  ? 232 ASP B C      1 
ATOM   4459 O O      . ASP B 1 241 ? 46.38700 -10.69500 -33.99600 1.000 25.85353  ? 232 ASP B O      1 
ATOM   4460 C CB     . ASP B 1 241 ? 47.30300 -12.67700 -31.97500 1.000 32.23939  ? 232 ASP B CB     1 
ATOM   4461 C CG     . ASP B 1 241 ? 47.90686 -13.90211 -32.63330 1.000 37.09791  ? 232 ASP B CG     1 
ATOM   4462 O OD1    . ASP B 1 241 ? 47.94092 -14.97302 -31.99211 1.000 56.30445  ? 232 ASP B OD1    1 
ATOM   4463 O OD2    . ASP B 1 241 ? 48.35037 -13.79198 -33.79472 1.000 46.63603  ? 232 ASP B OD2    1 
ATOM   4464 N N      . ARG B 1 242 ? 45.33700 -12.50300 -34.83000 1.000 27.18467  ? 233 ARG B N      1 
ATOM   4465 C CA     . ARG B 1 242 ? 45.23600 -11.96900 -36.18200 1.000 24.93974  ? 233 ARG B CA     1 
ATOM   4466 C C      . ARG B 1 242 ? 43.78400 -11.78800 -36.61200 1.000 27.10488  ? 233 ARG B C      1 
ATOM   4467 O O      . ARG B 1 242 ? 43.49400 -11.77500 -37.81200 1.000 25.10980  ? 233 ARG B O      1 
ATOM   4468 C CB     . ARG B 1 242 ? 45.98300 -12.87300 -37.16700 1.000 22.80838  ? 233 ARG B CB     1 
ATOM   4469 C CG     . ARG B 1 242 ? 47.43525 -13.10858 -36.78271 1.000 30.85003  ? 233 ARG B CG     1 
ATOM   4470 C CD     . ARG B 1 242 ? 48.24600 -13.73349 -37.90723 1.000 37.19042  ? 233 ARG B CD     1 
ATOM   4471 N NE     . ARG B 1 242 ? 47.88300 -15.12148 -38.16443 1.000 44.13841  ? 233 ARG B NE     1 
ATOM   4472 C CZ     . ARG B 1 242 ? 48.66574 -15.99235 -38.78871 1.000 49.71256  ? 233 ARG B CZ     1 
ATOM   4473 N NH1    . ARG B 1 242 ? 49.87205 -15.65554 -39.21544 1.000 49.71541  ? 233 ARG B NH1    1 
ATOM   4474 N NH2    . ARG B 1 242 ? 48.22799 -17.23241 -38.98583 1.000 39.51633  ? 233 ARG B NH2    1 
ATOM   4475 N N      . VAL B 1 243 ? 42.86700 -11.64100 -35.65700 1.000 24.35437  ? 234 VAL B N      1 
ATOM   4476 C CA     . VAL B 1 243 ? 41.43800 -11.54400 -35.93900 1.000 25.48839  ? 234 VAL B CA     1 
ATOM   4477 C C      . VAL B 1 243 ? 40.88200 -10.30200 -35.25600 1.000 22.59151  ? 234 VAL B C      1 
ATOM   4478 O O      . VAL B 1 243 ? 40.95400 -10.18100 -34.02700 1.000 27.42793  ? 234 VAL B O      1 
ATOM   4479 C CB     . VAL B 1 243 ? 40.67100 -12.79200 -35.47600 1.000 20.06746  ? 234 VAL B CB     1 
ATOM   4480 C CG1    . VAL B 1 243 ? 39.17300 -12.55200 -35.57400 1.000 22.12039  ? 234 VAL B CG1    1 
ATOM   4481 C CG2    . VAL B 1 243 ? 41.07700 -14.00400 -36.29900 1.000 17.36419  ? 234 VAL B CG2    1 
ATOM   4482 N N      . GLY B 1 244 ? 40.32100 -9.39200  -36.04700 1.000 24.71214  ? 235 GLY B N      1 
ATOM   4483 C CA     . GLY B 1 244 ? 39.58800 -8.26100  -35.51200 1.000 21.35800  ? 235 GLY B CA     1 
ATOM   4484 C C      . GLY B 1 244 ? 38.10000 -8.41100  -35.75400 1.000 22.96219  ? 235 GLY B C      1 
ATOM   4485 O O      . GLY B 1 244 ? 37.68900 -9.16900  -36.63800 1.000 22.51961  ? 235 GLY B O      1 
ATOM   4486 N N      . VAL B 1 245 ? 37.27800 -7.71200  -34.97500 1.000 23.68765  ? 236 VAL B N      1 
ATOM   4487 C CA     . VAL B 1 245 ? 35.82600 -7.78500  -35.09600 1.000 23.14471  ? 236 VAL B CA     1 
ATOM   4488 C C      . VAL B 1 245 ? 35.27100 -6.36900  -35.05800 1.000 25.02082  ? 236 VAL B C      1 
ATOM   4489 O O      . VAL B 1 245 ? 35.63300 -5.58000  -34.17700 1.000 27.96541  ? 236 VAL B O      1 
ATOM   4490 C CB     . VAL B 1 245 ? 35.19800 -8.64400  -33.98000 1.000 19.40737  ? 236 VAL B CB     1 
ATOM   4491 C CG1    . VAL B 1 245 ? 33.67800 -8.62900  -34.08300 1.000 18.05251  ? 236 VAL B CG1    1 
ATOM   4492 C CG2    . VAL B 1 245 ? 35.72100 -10.07100 -34.04500 1.000 17.97484  ? 236 VAL B CG2    1 
ATOM   4493 N N      . ARG B 1 246 ? 34.39900 -6.04400  -36.01200 1.000 22.43299  ? 237 ARG B N      1 
ATOM   4494 C CA     . ARG B 1 246 ? 33.77700 -4.73000  -36.08200 1.000 22.17299  ? 237 ARG B CA     1 
ATOM   4495 C C      . ARG B 1 246 ? 32.26700 -4.86800  -35.96300 1.000 24.43910  ? 237 ARG B C      1 
ATOM   4496 O O      . ARG B 1 246 ? 31.65600 -5.68100  -36.66400 1.000 24.20582  ? 237 ARG B O      1 
ATOM   4497 C CB     . ARG B 1 246 ? 34.13400 -3.99800  -37.37900 1.000 21.85635  ? 237 ARG B CB     1 
ATOM   4498 C CG     . ARG B 1 246 ? 33.91400 -2.49500  -37.27200 1.000 21.96552  ? 237 ARG B CG     1 
ATOM   4499 C CD     . ARG B 1 246 ? 34.13900 -1.76300  -38.58100 1.000 22.32872  ? 237 ARG B CD     1 
ATOM   4500 N NE     . ARG B 1 246 ? 34.59500 -0.39800  -38.34400 1.000 21.34679  ? 237 ARG B NE     1 
ATOM   4501 C CZ     . ARG B 1 246 ? 34.41000 0.61300   -39.18100 1.000 26.01098  ? 237 ARG B CZ     1 
ATOM   4502 N NH1    . ARG B 1 246 ? 33.73600 0.46300   -40.30800 1.000 27.04506  ? 237 ARG B NH1    1 
ATOM   4503 N NH2    . ARG B 1 246 ? 34.91200 1.80800   -38.87800 1.000 20.86629  ? 237 ARG B NH2    1 
ATOM   4504 N N      . VAL B 1 247 ? 31.67100 -4.06800  -35.07600 1.000 23.72642  ? 238 VAL B N      1 
ATOM   4505 C CA     . VAL B 1 247 ? 30.22800 -4.04200  -34.87800 1.000 23.24465  ? 238 VAL B CA     1 
ATOM   4506 C C      . VAL B 1 247 ? 29.77300 -2.59400  -34.75700 1.000 22.76796  ? 238 VAL B C      1 
ATOM   4507 O O      . VAL B 1 247 ? 30.57100 -1.68200  -34.52700 1.000 20.76812  ? 238 VAL B O      1 
ATOM   4508 C CB     . VAL B 1 247 ? 29.78400 -4.84400  -33.63300 1.000 25.08176  ? 238 VAL B CB     1 
ATOM   4509 C CG1    . VAL B 1 247 ? 30.07600 -6.32800  -33.81500 1.000 21.59138  ? 238 VAL B CG1    1 
ATOM   4510 C CG2    . VAL B 1 247 ? 30.46700 -4.30600  -32.38400 1.000 22.60593  ? 238 VAL B CG2    1 
ATOM   4511 N N      . SER B 1 248 ? 28.46700 -2.39300  -34.91900 1.000 26.65928  ? 239 SER B N      1 
ATOM   4512 C CA     . SER B 1 248 ? 27.85500 -1.06900  -34.78800 1.000 23.85953  ? 239 SER B CA     1 
ATOM   4513 C C      . SER B 1 248 ? 26.44600 -1.24200  -34.24600 1.000 24.40060  ? 239 SER B C      1 
ATOM   4514 O O      . SER B 1 248 ? 25.46000 -1.19300  -34.99100 1.000 23.38635  ? 239 SER B O      1 
ATOM   4515 C CB     . SER B 1 248 ? 27.83900 -0.32800  -36.12500 1.000 23.78664  ? 239 SER B CB     1 
ATOM   4516 O OG     . SER B 1 248 ? 27.06400 -1.02000  -37.08900 1.000 21.99472  ? 239 SER B OG     1 
ATOM   4517 N N      . PRO B 1 249 ? 26.31100 -1.44400  -32.93300 1.000 25.48173  ? 240 PRO B N      1 
ATOM   4518 C CA     . PRO B 1 249 ? 24.98500 -1.76000  -32.37600 1.000 23.12327  ? 240 PRO B CA     1 
ATOM   4519 C C      . PRO B 1 249 ? 23.96700 -0.64300  -32.53000 1.000 26.74339  ? 240 PRO B C      1 
ATOM   4520 O O      . PRO B 1 249 ? 22.76700 -0.93000  -32.63600 1.000 25.27665  ? 240 PRO B O      1 
ATOM   4521 C CB     . PRO B 1 249 ? 25.28600 -2.04600  -30.89600 1.000 26.24336  ? 240 PRO B CB     1 
ATOM   4522 C CG     . PRO B 1 249 ? 26.75400 -2.34800  -30.84500 1.000 28.40331  ? 240 PRO B CG     1 
ATOM   4523 C CD     . PRO B 1 249 ? 27.36800 -1.49400  -31.90900 1.000 25.22329  ? 240 PRO B CD     1 
ATOM   4524 N N      . ALA B 1 250 ? 24.39800 0.61900   -32.55500 1.000 22.49662  ? 241 ALA B N      1 
ATOM   4525 C CA     . ALA B 1 250 ? 23.48300 1.75400   -32.54400 1.000 26.63279  ? 241 ALA B CA     1 
ATOM   4526 C C      . ALA B 1 250 ? 23.45800 2.50800   -33.87200 1.000 27.33400  ? 241 ALA B C      1 
ATOM   4527 O O      . ALA B 1 250 ? 23.16900 3.70600   -33.90300 1.000 38.02299  ? 241 ALA B O      1 
ATOM   4528 C CB     . ALA B 1 250 ? 23.83100 2.70700   -31.40200 1.000 24.16640  ? 241 ALA B CB     1 
ATOM   4529 N N      . ILE B 1 251 ? 23.75200 1.82700   -34.97500 1.000 29.85439  ? 242 ILE B N      1 
ATOM   4530 C CA     . ILE B 1 251 ? 23.63000 2.40000   -36.31200 1.000 27.75335  ? 242 ILE B CA     1 
ATOM   4531 C C      . ILE B 1 251 ? 22.49400 1.67700   -37.02300 1.000 28.42684  ? 242 ILE B C      1 
ATOM   4532 O O      . ILE B 1 251 ? 22.51000 0.44600   -37.14300 1.000 32.47605  ? 242 ILE B O      1 
ATOM   4533 C CB     . ILE B 1 251 ? 24.94200 2.29700   -37.10400 1.000 29.45076  ? 242 ILE B CB     1 
ATOM   4534 C CG1    . ILE B 1 251 ? 26.03000 3.14600   -36.44100 1.000 28.44996  ? 242 ILE B CG1    1 
ATOM   4535 C CG2    . ILE B 1 251 ? 24.73200 2.74300   -38.54400 1.000 29.22162  ? 242 ILE B CG2    1 
ATOM   4536 C CD1    . ILE B 1 251 ? 27.31200 3.23300   -37.24100 1.000 30.48950  ? 242 ILE B CD1    1 
ATOM   4537 N N      . ASP B 1 252 ? 21.50700 2.44300   -37.49200 1.000 32.67532  ? 243 ASP B N      1 
ATOM   4538 C CA     . ASP B 1 252 ? 20.29400 1.90000   -38.09200 1.000 38.99724  ? 243 ASP B CA     1 
ATOM   4539 C C      . ASP B 1 252 ? 20.37800 1.81900   -39.61400 1.000 39.37277  ? 243 ASP B C      1 
ATOM   4540 O O      . ASP B 1 252 ? 19.35200 1.91900   -40.29700 1.000 43.95211  ? 243 ASP B O      1 
ATOM   4541 C CB     . ASP B 1 252 ? 19.08300 2.73500   -37.67700 1.000 45.52640  ? 243 ASP B CB     1 
ATOM   4542 C CG     . ASP B 1 252 ? 19.20200 4.18500   -38.10800 1.000 62.74778  ? 243 ASP B CG     1 
ATOM   4543 O OD1    . ASP B 1 252 ? 20.27800 4.78500   -37.89300 1.000 60.67830  ? 243 ASP B OD1    1 
ATOM   4544 O OD2    . ASP B 1 252 ? 18.22400 4.72300   -38.67000 1.000 61.79113  ? 243 ASP B OD2    1 
ATOM   4545 N N      . HIS B 1 253 ? 21.57700 1.63700   -40.15800 1.000 36.78872  ? 244 HIS B N      1 
ATOM   4546 C CA     . HIS B 1 253 ? 21.74500 1.56200   -41.60300 1.000 40.14968  ? 244 HIS B CA     1 
ATOM   4547 C C      . HIS B 1 253 ? 21.08100 0.30400   -42.15200 1.000 36.98779  ? 244 HIS B C      1 
ATOM   4548 O O      . HIS B 1 253 ? 21.31000 -0.80000  -41.64800 1.000 36.01392  ? 244 HIS B O      1 
ATOM   4549 C CB     . HIS B 1 253 ? 23.23200 1.58000   -41.95800 1.000 34.77728  ? 244 HIS B CB     1 
ATOM   4550 C CG     . HIS B 1 253 ? 23.50500 1.70300   -43.42500 1.000 38.60567  ? 244 HIS B CG     1 
ATOM   4551 N ND1    . HIS B 1 253 ? 24.20600 0.75200   -44.13400 1.000 33.29522  ? 244 HIS B ND1    1 
ATOM   4552 C CD2    . HIS B 1 253 ? 23.17600 2.66900   -44.31500 1.000 36.04660  ? 244 HIS B CD2    1 
ATOM   4553 C CE1    . HIS B 1 253 ? 24.29700 1.12700   -45.39700 1.000 39.45004  ? 244 HIS B CE1    1 
ATOM   4554 N NE2    . HIS B 1 253 ? 23.67800 2.28600   -45.53400 1.000 38.92940  ? 244 HIS B NE2    1 
ATOM   4555 N N      . LEU B 1 254 ? 20.25000 0.47700   -43.18300 1.000 36.02723  ? 245 LEU B N      1 
ATOM   4556 C CA     . LEU B 1 254 ? 19.55100 -0.62900  -43.84500 1.000 31.83646  ? 245 LEU B CA     1 
ATOM   4557 C C      . LEU B 1 254 ? 18.64700 -1.38000  -42.86600 1.000 32.99448  ? 245 LEU B C      1 
ATOM   4558 O O      . LEU B 1 254 ? 18.64100 -2.61200  -42.80900 1.000 26.35626  ? 245 LEU B O      1 
ATOM   4559 C CB     . LEU B 1 254 ? 20.54300 -1.58100  -44.52000 1.000 29.18638  ? 245 LEU B CB     1 
ATOM   4560 C CG     . LEU B 1 254 ? 21.56400 -0.95300  -45.47200 1.000 36.58127  ? 245 LEU B CG     1 
ATOM   4561 C CD1    . LEU B 1 254 ? 22.58000 -1.99000  -45.93100 1.000 29.10560  ? 245 LEU B CD1    1 
ATOM   4562 C CD2    . LEU B 1 254 ? 20.87700 -0.30400  -46.66800 1.000 29.00605  ? 245 LEU B CD2    1 
ATOM   4563 N N      . ASP B 1 255 ? 17.87500 -0.61500  -42.08800 1.000 34.99825  ? 246 ASP B N      1 
ATOM   4564 C CA     . ASP B 1 255 ? 16.91000 -1.15200  -41.12300 1.000 29.81329  ? 246 ASP B CA     1 
ATOM   4565 C C      . ASP B 1 255 ? 17.57400 -2.02700  -40.06400 1.000 29.07085  ? 246 ASP B C      1 
ATOM   4566 O O      . ASP B 1 255 ? 16.98000 -2.99800  -39.59100 1.000 33.54690  ? 246 ASP B O      1 
ATOM   4567 C CB     . ASP B 1 255 ? 15.79400 -1.93900  -41.81700 1.000 38.25131  ? 246 ASP B CB     1 
ATOM   4568 C CG     . ASP B 1 255 ? 15.02400 -1.10500  -42.81000 1.000 39.05705  ? 246 ASP B CG     1 
ATOM   4569 O OD1    . ASP B 1 255 ? 14.99500 0.13400   -42.65700 1.000 42.77200  ? 246 ASP B OD1    1 
ATOM   4570 O OD2    . ASP B 1 255 ? 14.44400 -1.69400  -43.74500 1.000 41.93561  ? 246 ASP B OD2    1 
ATOM   4571 N N      . ALA B 1 256 ? 18.80200 -1.69500  -39.67500 1.000 31.81397  ? 247 ALA B N      1 
ATOM   4572 C CA     . ALA B 1 256 ? 19.52700 -2.48000  -38.67600 1.000 33.38948  ? 247 ALA B CA     1 
ATOM   4573 C C      . ALA B 1 256 ? 19.33100 -1.89000  -37.27900 1.000 27.11091  ? 247 ALA B C      1 
ATOM   4574 O O      . ALA B 1 256 ? 20.26800 -1.45200  -36.61300 1.000 32.48420  ? 247 ALA B O      1 
ATOM   4575 C CB     . ALA B 1 256 ? 21.00500 -2.55900  -39.03600 1.000 27.93720  ? 247 ALA B CB     1 
ATOM   4576 N N      . MET B 1 257 ? 18.07900 -1.89400  -36.83700 1.000 29.17858  ? 248 MET B N      1 
ATOM   4577 C CA     . MET B 1 257 ? 17.71600 -1.36900  -35.53000 1.000 31.53462  ? 248 MET B CA     1 
ATOM   4578 C C      . MET B 1 257 ? 17.50700 -2.50900  -34.54200 1.000 32.50705  ? 248 MET B C      1 
ATOM   4579 O O      . MET B 1 257 ? 16.93000 -3.54500  -34.88300 1.000 30.43716  ? 248 MET B O      1 
ATOM   4580 C CB     . MET B 1 257 ? 16.45100 -0.51200  -35.61700 1.000 30.25241  ? 248 MET B CB     1 
ATOM   4581 C CG     . MET B 1 257 ? 15.95605 0.00136   -34.27292 1.000 48.18786  ? 248 MET B CG     1 
ATOM   4582 S SD     . MET B 1 257 ? 15.02166 1.53436   -34.41076 1.000 82.08034  ? 248 MET B SD     1 
ATOM   4583 C CE     . MET B 1 257 ? 16.25988 2.61221   -35.13192 1.000 58.30436  ? 248 MET B CE     1 
ATOM   4584 N N      . ASP B 1 258 ? 17.99500 -2.31500  -33.32000 1.000 32.80835  ? 249 ASP B N      1 
ATOM   4585 C CA     . ASP B 1 258 ? 17.74200 -3.22700  -32.21600 1.000 29.86717  ? 249 ASP B CA     1 
ATOM   4586 C C      . ASP B 1 258 ? 16.98600 -2.48700  -31.12300 1.000 30.55397  ? 249 ASP B C      1 
ATOM   4587 O O      . ASP B 1 258 ? 17.23800 -1.30300  -30.87400 1.000 27.23094  ? 249 ASP B O      1 
ATOM   4588 C CB     . ASP B 1 258 ? 19.04100 -3.80900  -31.65100 1.000 26.95426  ? 249 ASP B CB     1 
ATOM   4589 C CG     . ASP B 1 258 ? 18.79700 -5.00900  -30.75300 1.000 32.09338  ? 249 ASP B CG     1 
ATOM   4590 O OD1    . ASP B 1 258 ? 18.60700 -6.12200  -31.28700 1.000 30.66098  ? 249 ASP B OD1    1 
ATOM   4591 O OD2    . ASP B 1 258 ? 18.78500 -4.83800  -29.51500 1.000 33.97798  ? 249 ASP B OD2    1 
ATOM   4592 N N      . SER B 1 259 ? 16.05500 -3.19100  -30.47300 1.000 29.14999  ? 250 SER B N      1 
ATOM   4593 C CA     . SER B 1 259 ? 15.26100 -2.57800  -29.41400 1.000 32.54989  ? 250 SER B CA     1 
ATOM   4594 C C      . SER B 1 259 ? 16.11200 -2.15300  -28.22500 1.000 29.94996  ? 250 SER B C      1 
ATOM   4595 O O      . SER B 1 259 ? 15.70400 -1.26300  -27.47100 1.000 27.43733  ? 250 SER B O      1 
ATOM   4596 C CB     . SER B 1 259 ? 14.16500 -3.54100  -28.95400 1.000 34.14583  ? 250 SER B CB     1 
ATOM   4597 O OG     . SER B 1 259 ? 14.72100 -4.75200  -28.47100 1.000 33.97480  ? 250 SER B OG     1 
ATOM   4598 N N      . ASN B 1 260 ? 17.28000 -2.76300  -28.04100 1.000 28.57972  ? 251 ASN B N      1 
ATOM   4599 C CA     . ASN B 1 260 ? 18.18700 -2.41900  -26.94600 1.000 26.25155  ? 251 ASN B CA     1 
ATOM   4600 C C      . ASN B 1 260 ? 19.61300 -2.51600  -27.46300 1.000 28.49866  ? 251 ASN B C      1 
ATOM   4601 O O      . ASN B 1 260 ? 20.30100 -3.52400  -27.25800 1.000 26.37015  ? 251 ASN B O      1 
ATOM   4602 C CB     . ASN B 1 260 ? 17.96400 -3.33400  -25.73900 1.000 28.45279  ? 251 ASN B CB     1 
ATOM   4603 C CG     . ASN B 1 260 ? 18.51900 -2.75200  -24.45400 1.000 32.24855  ? 251 ASN B CG     1 
ATOM   4604 O OD1    . ASN B 1 260 ? 19.47300 -1.97400  -24.47100 1.000 32.73459  ? 251 ASN B OD1    1 
ATOM   4605 N ND2    . ASN B 1 260 ? 17.92100 -3.12900  -23.32900 1.000 28.03576  ? 251 ASN B ND2    1 
ATOM   4606 N N      . PRO B 1 261 ? 20.09500 -1.47500  -28.14900 1.000 28.39946  ? 252 PRO B N      1 
ATOM   4607 C CA     . PRO B 1 261 ? 21.44500 -1.54800  -28.73500 1.000 28.64132  ? 252 PRO B CA     1 
ATOM   4608 C C      . PRO B 1 261 ? 22.54200 -1.69400  -27.69900 1.000 27.59207  ? 252 PRO B C      1 
ATOM   4609 O O      . PRO B 1 261 ? 23.57600 -2.31200  -27.98400 1.000 26.73838  ? 252 PRO B O      1 
ATOM   4610 C CB     . PRO B 1 261 ? 21.56800 -0.22200  -29.50100 1.000 30.70815  ? 252 PRO B CB     1 
ATOM   4611 C CG     . PRO B 1 261 ? 20.15500 0.25600   -29.68600 1.000 34.70612  ? 252 PRO B CG     1 
ATOM   4612 C CD     . PRO B 1 261 ? 19.41900 -0.20800  -28.47000 1.000 24.33438  ? 252 PRO B CD     1 
ATOM   4613 N N      . LEU B 1 262 ? 22.34500 -1.14300  -26.50200 1.000 28.85413  ? 253 LEU B N      1 
ATOM   4614 C CA     . LEU B 1 262 ? 23.35700 -1.25400  -25.45800 1.000 27.16400  ? 253 LEU B CA     1 
ATOM   4615 C C      . LEU B 1 262 ? 23.45700 -2.68200  -24.93600 1.000 27.42411  ? 253 LEU B C      1 
ATOM   4616 O O      . LEU B 1 262 ? 24.56000 -3.18700  -24.69700 1.000 27.01517  ? 253 LEU B O      1 
ATOM   4617 C CB     . LEU B 1 262 ? 23.03600 -0.27500  -24.32900 1.000 30.70350  ? 253 LEU B CB     1 
ATOM   4618 C CG     . LEU B 1 262 ? 24.01500 -0.15400  -23.16300 1.000 34.02380  ? 253 LEU B CG     1 
ATOM   4619 C CD1    . LEU B 1 262 ? 25.43500 -0.00300  -23.67100 1.000 36.71337  ? 253 LEU B CD1    1 
ATOM   4620 C CD2    . LEU B 1 262 ? 23.63200 1.03400   -22.30000 1.000 34.43130  ? 253 LEU B CD2    1 
ATOM   4621 N N      . SER B 1 263 ? 22.31500 -3.35400  -24.76400 1.000 26.46741  ? 254 SER B N      1 
ATOM   4622 C CA     . SER B 1 263 ? 22.33400 -4.74500  -24.32100 1.000 24.77459  ? 254 SER B CA     1 
ATOM   4623 C C      . SER B 1 263 ? 22.92500 -5.65800  -25.38800 1.000 30.83947  ? 254 SER B C      1 
ATOM   4624 O O      . SER B 1 263 ? 23.64600 -6.61100  -25.06800 1.000 23.75168  ? 254 SER B O      1 
ATOM   4625 C CB     . SER B 1 263 ? 20.92100 -5.19800  -23.95500 1.000 27.36899  ? 254 SER B CB     1 
ATOM   4626 O OG     . SER B 1 263 ? 20.89800 -6.57500  -23.62200 1.000 29.90830  ? 254 SER B OG     1 
ATOM   4627 N N      . LEU B 1 264 ? 22.62800 -5.38600  -26.66000 1.000 26.49073  ? 255 LEU B N      1 
ATOM   4628 C CA     . LEU B 1 264 ? 23.16100 -6.21100  -27.73900 1.000 22.02570  ? 255 LEU B CA     1 
ATOM   4629 C C      . LEU B 1 264 ? 24.67800 -6.09600  -27.81800 1.000 21.25541  ? 255 LEU B C      1 
ATOM   4630 O O      . LEU B 1 264 ? 25.38400 -7.10400  -27.94100 1.000 22.99541  ? 255 LEU B O      1 
ATOM   4631 C CB     . LEU B 1 264 ? 22.51400 -5.81400  -29.06500 1.000 24.66893  ? 255 LEU B CB     1 
ATOM   4632 C CG     . LEU B 1 264 ? 23.04900 -6.48800  -30.32900 1.000 23.99610  ? 255 LEU B CG     1 
ATOM   4633 C CD1    . LEU B 1 264 ? 22.88300 -7.99900  -30.25200 1.000 25.51822  ? 255 LEU B CD1    1 
ATOM   4634 C CD2    . LEU B 1 264 ? 22.35000 -5.92900  -31.55600 1.000 27.53287  ? 255 LEU B CD2    1 
ATOM   4635 N N      . GLY B 1 265 ? 25.20000 -4.87000  -27.74100 1.000 20.59217  ? 256 GLY B N      1 
ATOM   4636 C CA     . GLY B 1 265 ? 26.64200 -4.68600  -27.77800 1.000 21.05137  ? 256 GLY B CA     1 
ATOM   4637 C C      . GLY B 1 265 ? 27.35200 -5.38400  -26.63300 1.000 25.60452  ? 256 GLY B C      1 
ATOM   4638 O O      . GLY B 1 265 ? 28.40300 -5.99900  -26.82600 1.000 28.22904  ? 256 GLY B O      1 
ATOM   4639 N N      . LEU B 1 266 ? 26.79000 -5.29500  -25.42400 1.000 24.89721  ? 257 LEU B N      1 
ATOM   4640 C CA     . LEU B 1 266 ? 27.37500 -5.99800  -24.28800 1.000 25.02026  ? 257 LEU B CA     1 
ATOM   4641 C C      . LEU B 1 266 ? 27.27700 -7.50800  -24.45300 1.000 25.29176  ? 257 LEU B C      1 
ATOM   4642 O O      . LEU B 1 266 ? 28.17700 -8.23800  -24.02100 1.000 29.56755  ? 257 LEU B O      1 
ATOM   4643 C CB     . LEU B 1 266 ? 26.69800 -5.56300  -22.98900 1.000 25.56353  ? 257 LEU B CB     1 
ATOM   4644 C CG     . LEU B 1 266 ? 26.91400 -4.11100  -22.56100 1.000 23.38099  ? 257 LEU B CG     1 
ATOM   4645 C CD1    . LEU B 1 266 ? 26.06700 -3.78100  -21.34100 1.000 24.62728  ? 257 LEU B CD1    1 
ATOM   4646 C CD2    . LEU B 1 266 ? 28.38600 -3.85700  -22.27800 1.000 24.67398  ? 257 LEU B CD2    1 
ATOM   4647 N N      . ALA B 1 267 ? 26.19700 -7.99600  -25.06700 1.000 23.34306  ? 258 ALA B N      1 
ATOM   4648 C CA     . ALA B 1 267 ? 26.08500 -9.42600  -25.33200 1.000 20.86187  ? 258 ALA B CA     1 
ATOM   4649 C C      . ALA B 1 267 ? 27.17700 -9.89400  -26.28500 1.000 24.79423  ? 258 ALA B C      1 
ATOM   4650 O O      . ALA B 1 267 ? 27.78400 -10.95000 -26.07400 1.000 28.68757  ? 258 ALA B O      1 
ATOM   4651 C CB     . ALA B 1 267 ? 24.70100 -9.75200  -25.89300 1.000 23.37228  ? 258 ALA B CB     1 
ATOM   4652 N N      . VAL B 1 268 ? 27.45000 -9.11600  -27.33600 1.000 24.76392  ? 259 VAL B N      1 
ATOM   4653 C CA     . VAL B 1 268 ? 28.52400 -9.47100  -28.26100 1.000 25.60452  ? 259 VAL B CA     1 
ATOM   4654 C C      . VAL B 1 268 ? 29.86600 -9.47900  -27.54100 1.000 23.78973  ? 259 VAL B C      1 
ATOM   4655 O O      . VAL B 1 268 ? 30.67900 -10.39500 -27.71800 1.000 24.12378  ? 259 VAL B O      1 
ATOM   4656 C CB     . VAL B 1 268 ? 28.53500 -8.51200  -29.46600 1.000 25.80554  ? 259 VAL B CB     1 
ATOM   4657 C CG1    . VAL B 1 268 ? 29.75000 -8.77800  -30.34500 1.000 23.30318  ? 259 VAL B CG1    1 
ATOM   4658 C CG2    . VAL B 1 268 ? 27.25300 -8.65400  -30.26900 1.000 22.07017  ? 259 VAL B CG2    1 
ATOM   4659 N N      . VAL B 1 269 ? 30.11700 -8.46000  -26.71600 1.000 23.19155  ? 260 VAL B N      1 
ATOM   4660 C CA     . VAL B 1 269 ? 31.37600 -8.38000  -25.98200 1.000 28.22057  ? 260 VAL B CA     1 
ATOM   4661 C C      . VAL B 1 269 ? 31.53900 -9.58600  -25.06400 1.000 26.83195  ? 260 VAL B C      1 
ATOM   4662 O O      . VAL B 1 269 ? 32.64100 -10.13000 -24.91700 1.000 27.14649  ? 260 VAL B O      1 
ATOM   4663 C CB     . VAL B 1 269 ? 31.44700 -7.05400  -25.20200 1.000 31.20309  ? 260 VAL B CB     1 
ATOM   4664 C CG1    . VAL B 1 269 ? 32.55500 -7.09700  -24.16700 1.000 23.60077  ? 260 VAL B CG1    1 
ATOM   4665 C CG2    . VAL B 1 269 ? 31.64900 -5.89000  -26.16200 1.000 25.84796  ? 260 VAL B CG2    1 
ATOM   4666 N N      . GLU B 1 270 ? 30.44200 -10.03000 -24.44500 1.000 24.85712  ? 261 GLU B N      1 
ATOM   4667 C CA     . GLU B 1 270 ? 30.50300 -11.18200 -23.55100 1.000 34.46488  ? 261 GLU B CA     1 
ATOM   4668 C C      . GLU B 1 270 ? 30.97300 -12.43200 -24.28800 1.000 31.50107  ? 261 GLU B C      1 
ATOM   4669 O O      . GLU B 1 270 ? 31.79800 -13.19300 -23.76900 1.000 32.36051  ? 261 GLU B O      1 
ATOM   4670 C CB     . GLU B 1 270 ? 29.13500 -11.41400 -22.90900 1.000 29.63309  ? 261 GLU B CB     1 
ATOM   4671 C CG     . GLU B 1 270 ? 29.00400 -12.72700 -22.15300 1.000 37.24141  ? 261 GLU B CG     1 
ATOM   4672 C CD     . GLU B 1 270 ? 27.57000 -13.02200 -21.74600 1.000 38.98473  ? 261 GLU B CD     1 
ATOM   4673 O OE1    . GLU B 1 270 ? 26.78700 -12.06400 -21.57800 1.000 36.78552  ? 261 GLU B OE1    1 
ATOM   4674 O OE2    . GLU B 1 270 ? 27.22300 -14.21400 -21.60300 1.000 41.36193  ? 261 GLU B OE2    1 
ATOM   4675 N N      . ARG B 1 271 ? 30.46700 -12.65700 -25.50300 1.000 27.23985  ? 262 ARG B N      1 
ATOM   4676 C CA     . ARG B 1 271 ? 30.89600 -13.82400 -26.26800 1.000 29.75757  ? 262 ARG B CA     1 
ATOM   4677 C C      . ARG B 1 271 ? 32.33900 -13.68100 -26.73600 1.000 29.69754  ? 262 ARG B C      1 
ATOM   4678 O O      . ARG B 1 271 ? 33.07800 -14.67100 -26.79400 1.000 29.20735  ? 262 ARG B O      1 
ATOM   4679 C CB     . ARG B 1 271 ? 29.96400 -14.05600 -27.45900 1.000 31.86410  ? 262 ARG B CB     1 
ATOM   4680 C CG     . ARG B 1 271 ? 28.71000 -14.86200 -27.13200 1.000 29.74944  ? 262 ARG B CG     1 
ATOM   4681 C CD     . ARG B 1 271 ? 27.70200 -14.03000 -26.36500 1.000 33.32819  ? 262 ARG B CD     1 
ATOM   4682 N NE     . ARG B 1 271 ? 26.56400 -14.80800 -25.89300 1.000 33.71675  ? 262 ARG B NE     1 
ATOM   4683 C CZ     . ARG B 1 271 ? 25.59100 -14.31900 -25.13600 1.000 32.32787  ? 262 ARG B CZ     1 
ATOM   4684 N NH1    . ARG B 1 271 ? 25.58200 -13.05100 -24.75700 1.000 31.68940  ? 262 ARG B NH1    1 
ATOM   4685 N NH2    . ARG B 1 271 ? 24.60500 -15.12100 -24.74600 1.000 33.76572  ? 262 ARG B NH2    1 
ATOM   4686 N N      . LEU B 1 272 ? 32.76300 -12.45800 -27.07100 1.000 23.26916  ? 263 LEU B N      1 
ATOM   4687 C CA     . LEU B 1 272 ? 34.14800 -12.25000 -27.48400 1.000 26.12602  ? 263 LEU B CA     1 
ATOM   4688 C C      . LEU B 1 272 ? 35.11300 -12.52400 -26.33700 1.000 31.22398  ? 263 LEU B C      1 
ATOM   4689 O O      . LEU B 1 272 ? 36.17700 -13.11900 -26.54400 1.000 30.69559  ? 263 LEU B O      1 
ATOM   4690 C CB     . LEU B 1 272 ? 34.33700 -10.83000 -28.01900 1.000 20.02859  ? 263 LEU B CB     1 
ATOM   4691 C CG     . LEU B 1 272 ? 33.57200 -10.45900 -29.29200 1.000 26.10733  ? 263 LEU B CG     1 
ATOM   4692 C CD1    . LEU B 1 272 ? 33.91800 -9.04500  -29.73900 1.000 19.97439  ? 263 LEU B CD1    1 
ATOM   4693 C CD2    . LEU B 1 272 ? 33.85000 -11.45900 -30.40400 1.000 22.69356  ? 263 LEU B CD2    1 
ATOM   4694 N N      . ASN B 1 273 ? 34.76100 -12.09700 -25.12100 1.000 30.99253  ? 264 ASN B N      1 
ATOM   4695 C CA     . ASN B 1 273 ? 35.59900 -12.39700 -23.96400 1.000 32.90464  ? 264 ASN B CA     1 
ATOM   4696 C C      . ASN B 1 273 ? 35.65800 -13.89700 -23.70200 1.000 30.03811  ? 264 ASN B C      1 
ATOM   4697 O O      . ASN B 1 273 ? 36.71200 -14.42900 -23.33400 1.000 29.83912  ? 264 ASN B O      1 
ATOM   4698 C CB     . ASN B 1 273 ? 35.08400 -11.65600 -22.72800 1.000 26.25210  ? 264 ASN B CB     1 
ATOM   4699 C CG     . ASN B 1 273 ? 35.29400 -10.15300 -22.81200 1.000 32.25092  ? 264 ASN B CG     1 
ATOM   4700 O OD1    . ASN B 1 273 ? 36.12200 -9.67000  -23.58500 1.000 29.92669  ? 264 ASN B OD1    1 
ATOM   4701 N ND2    . ASN B 1 273 ? 34.54800 -9.40600  -22.00500 1.000 28.13033  ? 264 ASN B ND2    1 
ATOM   4702 N N      . LYS B 1 274 ? 34.53600 -14.59600 -23.89200 1.000 25.09531  ? 265 LYS B N      1 
ATOM   4703 C CA     . LYS B 1 274 ? 34.52000 -16.04000 -23.67700 1.000 29.99259  ? 265 LYS B CA     1 
ATOM   4704 C C      . LYS B 1 274 ? 35.38200 -16.76300 -24.70600 1.000 32.98725  ? 265 LYS B C      1 
ATOM   4705 O O      . LYS B 1 274 ? 36.05100 -17.75000 -24.38000 1.000 35.21253  ? 265 LYS B O      1 
ATOM   4706 C CB     . LYS B 1 274 ? 33.08300 -16.56300 -23.71800 1.000 34.52349  ? 265 LYS B CB     1 
ATOM   4707 C CG     . LYS B 1 274 ? 32.93300 -17.99500 -23.22900 1.000 43.31845  ? 265 LYS B CG     1 
ATOM   4708 C CD     . LYS B 1 274 ? 31.65900 -18.63500 -23.75700 1.000 45.53656  ? 265 LYS B CD     1 
ATOM   4709 C CE     . LYS B 1 274 ? 30.42900 -17.82500 -23.38200 1.000 52.48368  ? 265 LYS B CE     1 
ATOM   4710 N NZ     . LYS B 1 274 ? 29.18500 -18.41100 -23.95900 1.000 53.92223  ? 265 LYS B NZ     1 
ATOM   4711 N N      . ILE B 1 275 ? 35.37500 -16.29000 -25.95500 1.000 30.13100  ? 266 ILE B N      1 
ATOM   4712 C CA     . ILE B 1 275 ? 36.23500 -16.88100 -26.97800 1.000 30.18743  ? 266 ILE B CA     1 
ATOM   4713 C C      . ILE B 1 275 ? 37.70100 -16.68900 -26.61500 1.000 31.91249  ? 266 ILE B C      1 
ATOM   4714 O O      . ILE B 1 275 ? 38.52700 -17.59200 -26.79900 1.000 33.62589  ? 266 ILE B O      1 
ATOM   4715 C CB     . ILE B 1 275 ? 35.90800 -16.28500 -28.36000 1.000 33.19395  ? 266 ILE B CB     1 
ATOM   4716 C CG1    . ILE B 1 275 ? 34.51400 -16.72000 -28.81300 1.000 33.11219  ? 266 ILE B CG1    1 
ATOM   4717 C CG2    . ILE B 1 275 ? 36.95500 -16.69500 -29.38600 1.000 33.79531  ? 266 ILE B CG2    1 
ATOM   4718 C CD1    . ILE B 1 275 ? 34.09700 -16.13400 -30.14000 1.000 29.66005  ? 266 ILE B CD1    1 
ATOM   4719 N N      . GLN B 1 276 ? 38.04700 -15.51400 -26.08000 1.000 32.38485  ? 267 GLN B N      1 
ATOM   4720 C CA     . GLN B 1 276 ? 39.43300 -15.25100 -25.70800 1.000 33.36884  ? 267 GLN B CA     1 
ATOM   4721 C C      . GLN B 1 276 ? 39.87600 -16.13400 -24.54700 1.000 33.37459  ? 267 GLN B C      1 
ATOM   4722 O O      . GLN B 1 276 ? 41.02400 -16.59100 -24.51200 1.000 37.36184  ? 267 GLN B O      1 
ATOM   4723 C CB     . GLN B 1 276 ? 39.61200 -13.77200 -25.36400 1.000 28.46178  ? 267 GLN B CB     1 
ATOM   4724 C CG     . GLN B 1 276 ? 39.47800 -12.84900 -26.56400 1.000 29.76736  ? 267 GLN B CG     1 
ATOM   4725 C CD     . GLN B 1 276 ? 39.63300 -11.38500 -26.20200 1.000 32.83701  ? 267 GLN B CD     1 
ATOM   4726 O OE1    . GLN B 1 276 ? 39.89600 -10.54600 -27.06500 1.000 31.14037  ? 267 GLN B OE1    1 
ATOM   4727 N NE2    . GLN B 1 276 ? 39.46300 -11.06800 -24.92400 1.000 30.01906  ? 267 GLN B NE2    1 
ATOM   4728 N N      . LEU B 1 277 ? 38.98100 -16.38900 -23.58900 1.000 37.86151  ? 268 LEU B N      1 
ATOM   4729 C CA     . LEU B 1 277 ? 39.33200 -17.26300 -22.47500 1.000 37.89770  ? 268 LEU B CA     1 
ATOM   4730 C C      . LEU B 1 277 ? 39.38800 -18.72500 -22.89900 1.000 40.29129  ? 268 LEU B C      1 
ATOM   4731 O O      . LEU B 1 277 ? 40.18900 -19.49400 -22.35600 1.000 41.05202  ? 268 LEU B O      1 
ATOM   4732 C CB     . LEU B 1 277 ? 38.34000 -17.08600 -21.32500 1.000 34.18411  ? 268 LEU B CB     1 
ATOM   4733 C CG     . LEU B 1 277 ? 38.51411 -15.84454 -20.45098 1.000 40.76236  ? 268 LEU B CG     1 
ATOM   4734 C CD1    . LEU B 1 277 ? 37.62683 -15.93379 -19.21856 1.000 42.96472  ? 268 LEU B CD1    1 
ATOM   4735 C CD2    . LEU B 1 277 ? 39.97161 -15.66870 -20.05326 1.000 43.54000  ? 268 LEU B CD2    1 
ATOM   4736 N N      . HIS B 1 278 ? 38.55100 -19.12800 -23.85800 1.000 38.20696  ? 269 HIS B N      1 
ATOM   4737 C CA     . HIS B 1 278 ? 38.55700 -20.51900 -24.30100 1.000 40.39385  ? 269 HIS B CA     1 
ATOM   4738 C C      . HIS B 1 278 ? 39.79300 -20.83000 -25.13600 1.000 40.28058  ? 269 HIS B C      1 
ATOM   4739 O O      . HIS B 1 278 ? 40.42300 -21.87800 -24.95500 1.000 44.29510  ? 269 HIS B O      1 
ATOM   4740 C CB     . HIS B 1 278 ? 37.28400 -20.82500 -25.09000 1.000 41.49376  ? 269 HIS B CB     1 
ATOM   4741 N N      . SER B 1 279 ? 40.15600 -19.93500 -26.05500 1.000 41.83362  ? 270 SER B N      1 
ATOM   4742 C CA     . SER B 1 279 ? 41.31600 -20.15500 -26.91000 1.000 35.74254  ? 270 SER B CA     1 
ATOM   4743 C C      . SER B 1 279 ? 42.63300 -19.81300 -26.22700 1.000 38.41903  ? 270 SER B C      1 
ATOM   4744 O O      . SER B 1 279 ? 43.69400 -20.10700 -26.78800 1.000 40.68745  ? 270 SER B O      1 
ATOM   4745 C CB     . SER B 1 279 ? 41.18500 -19.33800 -28.19700 1.000 40.30180  ? 270 SER B CB     1 
ATOM   4746 O OG     . SER B 1 279 ? 41.26600 -17.94900 -27.92600 1.000 44.81568  ? 270 SER B OG     1 
ATOM   4747 N N      . GLY B 1 280 ? 42.59500 -19.20300 -25.04500 1.000 40.16108  ? 271 GLY B N      1 
ATOM   4748 C CA     . GLY B 1 280 ? 43.81800 -18.84300 -24.35500 1.000 40.14457  ? 271 GLY B CA     1 
ATOM   4749 C C      . GLY B 1 280 ? 44.60100 -17.72000 -24.99200 1.000 43.03045  ? 271 GLY B C      1 
ATOM   4750 O O      . GLY B 1 280 ? 45.78900 -17.56400 -24.70100 1.000 45.22986  ? 271 GLY B O      1 
ATOM   4751 N N      . SER B 1 281 ? 43.97000 -16.92900 -25.85700 1.000 41.34979  ? 272 SER B N      1 
ATOM   4752 C CA     . SER B 1 281 ? 44.64300 -15.82100 -26.51700 1.000 36.89206  ? 272 SER B CA     1 
ATOM   4753 C C      . SER B 1 281 ? 43.63700 -14.70600 -26.75400 1.000 36.26917  ? 272 SER B C      1 
ATOM   4754 O O      . SER B 1 281 ? 42.43000 -14.94300 -26.84600 1.000 38.62985  ? 272 SER B O      1 
ATOM   4755 C CB     . SER B 1 281 ? 45.28600 -16.25600 -27.84000 1.000 38.99906  ? 272 SER B CB     1 
ATOM   4756 O OG     . SER B 1 281 ? 45.99331 -15.18343 -28.43817 1.000 51.05125  ? 272 SER B OG     1 
ATOM   4757 N N      . LYS B 1 282 ? 44.14800 -13.48400 -26.85600 1.000 32.86538  ? 273 LYS B N      1 
ATOM   4758 C CA     . LYS B 1 282 ? 43.29800 -12.31700 -27.04100 1.000 32.35249  ? 273 LYS B CA     1 
ATOM   4759 C C      . LYS B 1 282 ? 43.12000 -12.00700 -28.52000 1.000 32.00535  ? 273 LYS B C      1 
ATOM   4760 O O      . LYS B 1 282 ? 44.04600 -12.16800 -29.32100 1.000 30.39023  ? 273 LYS B O      1 
ATOM   4761 C CB     . LYS B 1 282 ? 43.88100 -11.09900 -26.32400 1.000 33.96656  ? 273 LYS B CB     1 
ATOM   4762 C CG     . LYS B 1 282 ? 43.82900 -11.19000 -24.80900 1.000 39.45000  ? 273 LYS B CG     1 
ATOM   4763 C CD     . LYS B 1 282 ? 43.74400 -9.81000  -24.17400 1.000 37.45693  ? 273 LYS B CD     1 
ATOM   4764 C CE     . LYS B 1 282 ? 43.66700 -9.90800  -22.66000 1.000 37.89868  ? 273 LYS B CE     1 
ATOM   4765 N NZ     . LYS B 1 282 ? 42.56200 -10.80600 -22.22100 1.000 40.67511  ? 273 LYS B NZ     1 
ATOM   4766 N N      . LEU B 1 283 ? 41.91500 -11.56700 -28.87600 1.000 28.85243  ? 274 LEU B N      1 
ATOM   4767 C CA     . LEU B 1 283 ? 41.67000 -11.06600 -30.21700 1.000 27.98790  ? 274 LEU B CA     1 
ATOM   4768 C C      . LEU B 1 283 ? 42.55700 -9.85700  -30.49400 1.000 25.32247  ? 274 LEU B C      1 
ATOM   4769 O O      . LEU B 1 283 ? 43.03500 -9.17900  -29.57900 1.000 25.57125  ? 274 LEU B O      1 
ATOM   4770 C CB     . LEU B 1 283 ? 40.20000 -10.68400 -30.39000 1.000 22.41416  ? 274 LEU B CB     1 
ATOM   4771 C CG     . LEU B 1 283 ? 39.18600 -11.82600 -30.42300 1.000 24.70395  ? 274 LEU B CG     1 
ATOM   4772 C CD1    . LEU B 1 283 ? 37.77300 -11.27600 -30.53200 1.000 22.91693  ? 274 LEU B CD1    1 
ATOM   4773 C CD2    . LEU B 1 283 ? 39.48700 -12.76700 -31.57600 1.000 22.46964  ? 274 LEU B CD2    1 
ATOM   4774 N N      . ALA B 1 284 ? 42.78100 -9.59400  -31.78300 1.000 23.85733  ? 275 ALA B N      1 
ATOM   4775 C CA     . ALA B 1 284 ? 43.57600 -8.43400  -32.17200 1.000 25.58842  ? 275 ALA B CA     1 
ATOM   4776 C C      . ALA B 1 284 ? 42.98400 -7.15100  -31.60200 1.000 25.14388  ? 275 ALA B C      1 
ATOM   4777 O O      . ALA B 1 284 ? 43.69700 -6.33900  -30.99900 1.000 21.47178  ? 275 ALA B O      1 
ATOM   4778 C CB     . ALA B 1 284 ? 43.67800 -8.35400  -33.69500 1.000 22.80684  ? 275 ALA B CB     1 
ATOM   4779 N N      . TYR B 1 285 ? 41.67700 -6.96000  -31.76400 1.000 18.76080  ? 276 TYR B N      1 
ATOM   4780 C CA     . TYR B 1 285 ? 41.00900 -5.75700  -31.28300 1.000 20.92140  ? 276 TYR B CA     1 
ATOM   4781 C C      . TYR B 1 285 ? 39.50400 -5.93800  -31.41000 1.000 26.92417  ? 276 TYR B C      1 
ATOM   4782 O O      . TYR B 1 285 ? 39.01800 -6.83900  -32.09800 1.000 21.47652  ? 276 TYR B O      1 
ATOM   4783 C CB     . TYR B 1 285 ? 41.45400 -4.51400  -32.05800 1.000 20.42295  ? 276 TYR B CB     1 
ATOM   4784 C CG     . TYR B 1 285 ? 41.22400 -4.61200  -33.55100 1.000 21.73915  ? 276 TYR B CG     1 
ATOM   4785 C CD1    . TYR B 1 285 ? 40.00000 -4.26100  -34.11400 1.000 24.15885  ? 276 TYR B CD1    1 
ATOM   4786 C CD2    . TYR B 1 285 ? 42.23000 -5.05500  -34.39900 1.000 25.31429  ? 276 TYR B CD2    1 
ATOM   4787 C CE1    . TYR B 1 285 ? 39.78900 -4.34900  -35.47800 1.000 23.48145  ? 276 TYR B CE1    1 
ATOM   4788 C CE2    . TYR B 1 285 ? 42.02700 -5.14700  -35.76200 1.000 21.77210  ? 276 TYR B CE2    1 
ATOM   4789 C CZ     . TYR B 1 285 ? 40.80700 -4.79300  -36.29600 1.000 22.15865  ? 276 TYR B CZ     1 
ATOM   4790 O OH     . TYR B 1 285 ? 40.60800 -4.88300  -37.65300 1.000 25.74777  ? 276 TYR B OH     1 
ATOM   4791 N N      . LEU B 1 286 ? 38.77500 -5.05600  -30.73400 1.000 26.71558  ? 277 LEU B N      1 
ATOM   4792 C CA     . LEU B 1 286 ? 37.35600 -4.83800  -30.96700 1.000 23.82952  ? 277 LEU B CA     1 
ATOM   4793 C C      . LEU B 1 286 ? 37.19500 -3.47000  -31.61400 1.000 27.47954  ? 277 LEU B C      1 
ATOM   4794 O O      . LEU B 1 286 ? 37.78100 -2.48700  -31.14800 1.000 22.81666  ? 277 LEU B O      1 
ATOM   4795 C CB     . LEU B 1 286 ? 36.55600 -4.91300  -29.66500 1.000 24.54488  ? 277 LEU B CB     1 
ATOM   4796 C CG     . LEU B 1 286 ? 35.08000 -4.51400  -29.75900 1.000 24.73444  ? 277 LEU B CG     1 
ATOM   4797 C CD1    . LEU B 1 286 ? 34.33600 -5.41300  -30.73400 1.000 22.37552  ? 277 LEU B CD1    1 
ATOM   4798 C CD2    . LEU B 1 286 ? 34.41800 -4.53900  -28.38800 1.000 24.08481  ? 277 LEU B CD2    1 
ATOM   4799 N N      . HIS B 1 287 ? 36.41700 -3.41000  -32.69000 1.000 23.65160  ? 278 HIS B N      1 
ATOM   4800 C CA     . HIS B 1 287 ? 36.24400 -2.19000  -33.47000 1.000 21.27382  ? 278 HIS B CA     1 
ATOM   4801 C C      . HIS B 1 287 ? 34.76900 -1.81500  -33.43700 1.000 22.89868  ? 278 HIS B C      1 
ATOM   4802 O O      . HIS B 1 287 ? 33.92800 -2.53500  -33.98300 1.000 23.56549  ? 278 HIS B O      1 
ATOM   4803 C CB     . HIS B 1 287 ? 36.74000 -2.39200  -34.90200 1.000 21.71756  ? 278 HIS B CB     1 
ATOM   4804 C CG     . HIS B 1 287 ? 36.94600 -1.11900  -35.66200 1.000 23.01792  ? 278 HIS B CG     1 
ATOM   4805 N ND1    . HIS B 1 287 ? 37.45500 -1.09500  -36.94300 1.000 20.92136  ? 278 HIS B ND1    1 
ATOM   4806 C CD2    . HIS B 1 287 ? 36.71500 0.17100   -35.32500 1.000 23.59224  ? 278 HIS B CD2    1 
ATOM   4807 C CE1    . HIS B 1 287 ? 37.52800 0.15600   -37.36200 1.000 23.44052  ? 278 HIS B CE1    1 
ATOM   4808 N NE2    . HIS B 1 287 ? 37.08400 0.94400   -36.39900 1.000 21.30601  ? 278 HIS B NE2    1 
ATOM   4809 N N      . VAL B 1 288 ? 34.44900 -0.69900  -32.79100 1.000 22.20860  ? 279 VAL B N      1 
ATOM   4810 C CA     . VAL B 1 288 ? 33.07400 -0.23300  -32.66800 1.000 26.46801  ? 279 VAL B CA     1 
ATOM   4811 C C      . VAL B 1 288 ? 32.95700 1.11000   -33.37100 1.000 27.89246  ? 279 VAL B C      1 
ATOM   4812 O O      . VAL B 1 288 ? 33.72500 2.03600   -33.08600 1.000 27.39214  ? 279 VAL B O      1 
ATOM   4813 C CB     . VAL B 1 288 ? 32.63400 -0.12200  -31.19700 1.000 29.02588  ? 279 VAL B CB     1 
ATOM   4814 C CG1    . VAL B 1 288 ? 31.21900 0.43500   -31.11000 1.000 22.77511  ? 279 VAL B CG1    1 
ATOM   4815 C CG2    . VAL B 1 288 ? 32.71900 -1.48000  -30.51900 1.000 27.08297  ? 279 VAL B CG2    1 
ATOM   4816 N N      . THR B 1 289 ? 32.00300 1.21100   -34.29000 1.000 25.59753  ? 280 THR B N      1 
ATOM   4817 C CA     . THR B 1 289 ? 31.71300 2.45800   -34.97600 1.000 29.31192  ? 280 THR B CA     1 
ATOM   4818 C C      . THR B 1 289 ? 30.30800 2.91400   -34.61000 1.000 24.93509  ? 280 THR B C      1 
ATOM   4819 O O      . THR B 1 289 ? 29.44000 2.10100   -34.27600 1.000 26.99726  ? 280 THR B O      1 
ATOM   4820 C CB     . THR B 1 289 ? 31.85900 2.30800   -36.50100 1.000 25.69010  ? 280 THR B CB     1 
ATOM   4821 O OG1    . THR B 1 289 ? 31.55900 3.55400   -37.14000 1.000 36.71727  ? 280 THR B OG1    1 
ATOM   4822 C CG2    . THR B 1 289 ? 30.93400 1.22700   -37.03100 1.000 24.97954  ? 280 THR B CG2    1 
ATOM   4823 N N      . ALA B 1 290 ? 30.09700 4.22900   -34.65200 1.000 29.68996  ? 281 ALA B N      1 
ATOM   4824 C CA     . ALA B 1 290 ? 28.82900 4.82900   -34.26400 1.000 31.82733  ? 281 ALA B CA     1 
ATOM   4825 C C      . ALA B 1 290 ? 28.52500 5.99000   -35.20100 1.000 33.39915  ? 281 ALA B C      1 
ATOM   4826 O O      . ALA B 1 290 ? 29.31300 6.31700   -36.09400 1.000 35.67584  ? 281 ALA B O      1 
ATOM   4827 C CB     . ALA B 1 290 ? 28.85700 5.29200   -32.80300 1.000 27.09413  ? 281 ALA B CB     1 
ATOM   4828 N N      . GLU B 1 291 ? 27.36600 6.61300   -34.99100 1.000 36.22713  ? 282 GLU B N      1 
ATOM   4829 C CA     . GLU B 1 291 ? 26.97600 7.76500   -35.79300 1.000 36.52552  ? 282 GLU B CA     1 
ATOM   4830 C C      . GLU B 1 291 ? 27.98600 8.89400   -35.63200 1.000 40.38058  ? 282 GLU B C      1 
ATOM   4831 O O      . GLU B 1 291 ? 28.42600 9.20500   -34.52200 1.000 43.95573  ? 282 GLU B O      1 
ATOM   4832 C CB     . GLU B 1 291 ? 25.58400 8.25000   -35.38800 1.000 38.79638  ? 282 GLU B CB     1 
ATOM   4833 C CG     . GLU B 1 291 ? 24.45378 7.29381   -35.72483 1.000 46.21349  ? 282 GLU B CG     1 
ATOM   4834 C CD     . GLU B 1 291 ? 23.53266 7.84157   -36.79897 1.000 65.92564  ? 282 GLU B CD     1 
ATOM   4835 O OE1    . GLU B 1 291 ? 22.63381 8.64045   -36.46111 1.000 69.19705  ? 282 GLU B OE1    1 
ATOM   4836 O OE2    . GLU B 1 291 ? 23.70103 7.46312   -37.97783 1.000 62.67362  ? 282 GLU B OE2    1 
ATOM   4837 N N      . ALA B 1 292 ? 28.34800 9.51400   -36.75700 1.000 45.67549  ? 283 ALA B N      1 
ATOM   4838 C CA     . ALA B 1 292 ? 29.35900 10.56500  -36.76200 1.000 40.21687  ? 283 ALA B CA     1 
ATOM   4839 C C      . ALA B 1 292 ? 28.86000 11.88000  -36.17700 1.000 44.33802  ? 283 ALA B C      1 
ATOM   4840 O O      . ALA B 1 292 ? 29.66900 12.79200  -35.97800 1.000 50.86913  ? 283 ALA B O      1 
ATOM   4841 C CB     . ALA B 1 292 ? 29.86100 10.79300  -38.18900 1.000 41.69850  ? 283 ALA B CB     1 
ATOM   4842 N N      . ASP B 1 293 ? 27.56500 12.00000  -35.89400 1.000 42.28149  ? 284 ASP B N      1 
ATOM   4843 C CA     . ASP B 1 293 ? 26.98400 13.23300  -35.38000 1.000 46.35429  ? 284 ASP B CA     1 
ATOM   4844 C C      . ASP B 1 293 ? 27.04800 13.33800  -33.86000 1.000 47.82161  ? 284 ASP B C      1 
ATOM   4845 O O      . ASP B 1 293 ? 26.44800 14.25600  -33.29200 1.000 55.19126  ? 284 ASP B O      1 
ATOM   4846 C CB     . ASP B 1 293 ? 25.53100 13.36300  -35.84500 1.000 49.00652  ? 284 ASP B CB     1 
ATOM   4847 N N      . TRP B 1 294 ? 27.75500 12.43000  -33.19200 1.000 46.56371  ? 285 TRP B N      1 
ATOM   4848 C CA     . TRP B 1 294 ? 27.85000 12.46200  -31.73400 1.000 45.76484  ? 285 TRP B CA     1 
ATOM   4849 C C      . TRP B 1 294 ? 28.63500 13.68000  -31.25900 1.000 45.57325  ? 285 TRP B C      1 
ATOM   4850 O O      . TRP B 1 294 ? 28.52000 14.09200  -30.10400 1.000 49.37599  ? 285 TRP B O      1 
ATOM   4851 C CB     . TRP B 1 294 ? 28.50100 11.18100  -31.20400 1.000 36.93615  ? 285 TRP B CB     1 
ATOM   4852 C CG     . TRP B 1 294 ? 29.94700 11.04100  -31.57300 1.000 42.03063  ? 285 TRP B CG     1 
ATOM   4853 C CD1    . TRP B 1 294 ? 30.45100 10.47900  -32.71000 1.000 44.43270  ? 285 TRP B CD1    1 
ATOM   4854 C CD2    . TRP B 1 294 ? 31.07700 11.46700  -30.80200 1.000 46.48020  ? 285 TRP B CD2    1 
ATOM   4855 N NE1    . TRP B 1 294 ? 31.82400 10.53000  -32.69500 1.000 40.92905  ? 285 TRP B NE1    1 
ATOM   4856 C CE2    . TRP B 1 294 ? 32.23300 11.13200  -31.53400 1.000 42.81498  ? 285 TRP B CE2    1 
ATOM   4857 C CE3    . TRP B 1 294 ? 31.22300 12.10000  -29.56300 1.000 44.84605  ? 285 TRP B CE3    1 
ATOM   4858 C CZ2    . TRP B 1 294 ? 33.51800 11.40700  -31.07000 1.000 40.92489  ? 285 TRP B CZ2    1 
ATOM   4859 C CZ3    . TRP B 1 294 ? 32.50000 12.37300  -29.10500 1.000 40.33093  ? 285 TRP B CZ3    1 
ATOM   4860 C CH2    . TRP B 1 294 ? 33.63000 12.02600  -29.85600 1.000 40.03019  ? 285 TRP B CH2    1 
ATOM   4861 N N      . GLU B 1 305 ? 25.14600 10.63000  -18.96500 1.000 45.25616  ? 296 GLU B N      1 
ATOM   4862 C CA     . GLU B 1 305 ? 25.11400 9.26300   -19.47200 1.000 52.85083  ? 296 GLU B CA     1 
ATOM   4863 C C      . GLU B 1 305 ? 26.31800 8.98500   -20.36700 1.000 51.74530  ? 296 GLU B C      1 
ATOM   4864 O O      . GLU B 1 305 ? 26.59500 9.73700   -21.30200 1.000 54.92720  ? 296 GLU B O      1 
ATOM   4865 C CB     . GLU B 1 305 ? 23.81500 9.00300   -20.23800 1.000 45.04168  ? 296 GLU B CB     1 
ATOM   4866 N N      . ALA B 1 306 ? 27.03000 7.90100   -20.07300 1.000 49.12756  ? 297 ALA B N      1 
ATOM   4867 C CA     . ALA B 1 306 ? 28.20200 7.54000   -20.85600 1.000 43.73028  ? 297 ALA B CA     1 
ATOM   4868 C C      . ALA B 1 306 ? 27.79700 7.05900   -22.24500 1.000 42.52620  ? 297 ALA B C      1 
ATOM   4869 O O      . ALA B 1 306 ? 26.70800 6.51600   -22.44800 1.000 39.39794  ? 297 ALA B O      1 
ATOM   4870 C CB     . ALA B 1 306 ? 29.00900 6.45600   -20.14200 1.000 31.52126  ? 297 ALA B CB     1 
ATOM   4871 N N      . ARG B 1 307 ? 28.69200 7.26800   -23.20700 1.000 38.33404  ? 298 ARG B N      1 
ATOM   4872 C CA     . ARG B 1 307 ? 28.44400 6.82500   -24.56900 1.000 36.75320  ? 298 ARG B CA     1 
ATOM   4873 C C      . ARG B 1 307 ? 28.40900 5.30100   -24.64500 1.000 33.08307  ? 298 ARG B C      1 
ATOM   4874 O O      . ARG B 1 307 ? 28.97400 4.59300   -23.80700 1.000 39.27713  ? 298 ARG B O      1 
ATOM   4875 C CB     . ARG B 1 307 ? 29.52100 7.35100   -25.51800 1.000 38.59129  ? 298 ARG B CB     1 
ATOM   4876 C CG     . ARG B 1 307 ? 29.54500 8.85800   -25.70000 1.000 40.34527  ? 298 ARG B CG     1 
ATOM   4877 C CD     . ARG B 1 307 ? 30.56400 9.24200   -26.76300 1.000 40.70242  ? 298 ARG B CD     1 
ATOM   4878 N NE     . ARG B 1 307 ? 30.26900 8.61300   -28.04500 1.000 40.75008  ? 298 ARG B NE     1 
ATOM   4879 C CZ     . ARG B 1 307 ? 31.12900 8.51600   -29.05100 1.000 45.01783  ? 298 ARG B CZ     1 
ATOM   4880 N NH1    . ARG B 1 307 ? 32.36100 8.98700   -28.95600 1.000 46.81125  ? 298 ARG B NH1    1 
ATOM   4881 N NH2    . ARG B 1 307 ? 30.74300 7.92600   -30.18000 1.000 38.42162  ? 298 ARG B NH2    1 
ATOM   4882 N N      . LEU B 1 308 ? 27.72700 4.80100   -25.67800 1.000 36.86531  ? 299 LEU B N      1 
ATOM   4883 C CA     . LEU B 1 308 ? 27.80400 3.38000   -26.00300 1.000 34.03814  ? 299 LEU B CA     1 
ATOM   4884 C C      . LEU B 1 308 ? 29.24500 2.95200   -26.24700 1.000 32.50277  ? 299 LEU B C      1 
ATOM   4885 O O      . LEU B 1 308 ? 29.62600 1.82600   -25.90600 1.000 31.60809  ? 299 LEU B O      1 
ATOM   4886 C CB     . LEU B 1 308 ? 26.92800 3.08600   -27.22600 1.000 36.18329  ? 299 LEU B CB     1 
ATOM   4887 C CG     . LEU B 1 308 ? 26.86200 1.71500   -27.92000 1.000 40.07275  ? 299 LEU B CG     1 
ATOM   4888 C CD1    . LEU B 1 308 ? 28.00700 1.50100   -28.91400 1.000 33.87526  ? 299 LEU B CD1    1 
ATOM   4889 C CD2    . LEU B 1 308 ? 26.80600 0.58200   -26.91400 1.000 44.49038  ? 299 LEU B CD2    1 
ATOM   4890 N N      . MET B 1 309 ? 30.05900 3.84000   -26.82400 1.000 31.21452  ? 300 MET B N      1 
ATOM   4891 C CA     . MET B 1 309 ? 31.44300 3.50000   -27.13500 1.000 33.83197  ? 300 MET B CA     1 
ATOM   4892 C C      . MET B 1 309 ? 32.22800 3.16900   -25.87100 1.000 28.78485  ? 300 MET B C      1 
ATOM   4893 O O      . MET B 1 309 ? 32.96100 2.17400   -25.82300 1.000 26.70592  ? 300 MET B O      1 
ATOM   4894 C CB     . MET B 1 309 ? 32.10200 4.65600   -27.89200 1.000 33.42408  ? 300 MET B CB     1 
ATOM   4895 C CG     . MET B 1 309 ? 33.37928 4.28019   -28.62451 1.000 26.70892  ? 300 MET B CG     1 
ATOM   4896 S SD     . MET B 1 309 ? 33.06313 3.34269   -30.13262 1.000 34.91776  ? 300 MET B SD     1 
ATOM   4897 C CE     . MET B 1 309 ? 32.64142 4.65956   -31.27187 1.000 29.95206  ? 300 MET B CE     1 
ATOM   4898 N N      . ARG B 1 310 ? 32.08400 3.99400   -24.83100 1.000 29.84504  ? 301 ARG B N      1 
ATOM   4899 C CA     . ARG B 1 310 ? 32.84900 3.77400   -23.60800 1.000 28.58463  ? 301 ARG B CA     1 
ATOM   4900 C C      . ARG B 1 310 ? 32.34400 2.55900   -22.83700 1.000 29.79710  ? 301 ARG B C      1 
ATOM   4901 O O      . ARG B 1 310 ? 33.14000 1.85500   -22.20500 1.000 26.33563  ? 301 ARG B O      1 
ATOM   4902 C CB     . ARG B 1 310 ? 32.80500 5.02600   -22.73000 1.000 37.07450  ? 301 ARG B CB     1 
ATOM   4903 C CG     . ARG B 1 310 ? 33.67200 4.94500   -21.48100 1.000 36.61615  ? 301 ARG B CG     1 
ATOM   4904 C CD     . ARG B 1 310 ? 35.11300 4.60200   -21.83400 1.000 34.75143  ? 301 ARG B CD     1 
ATOM   4905 N NE     . ARG B 1 310 ? 35.91600 4.31200   -20.65200 1.000 42.63085  ? 301 ARG B NE     1 
ATOM   4906 C CZ     . ARG B 1 310 ? 36.76200 5.16300   -20.08900 1.000 42.04641  ? 301 ARG B CZ     1 
ATOM   4907 N NH1    . ARG B 1 310 ? 36.95000 6.37700   -20.58000 1.000 38.06505  ? 301 ARG B NH1    1 
ATOM   4908 N NH2    . ARG B 1 310 ? 37.44100 4.78500   -19.01000 1.000 43.01942  ? 301 ARG B NH2    1 
ATOM   4909 N N      . THR B 1 311 ? 31.03600 2.29400   -22.88000 1.000 26.08041  ? 302 THR B N      1 
ATOM   4910 C CA     . THR B 1 311 ? 30.49300 1.13700   -22.17500 1.000 26.17956  ? 302 THR B CA     1 
ATOM   4911 C C      . THR B 1 311 ? 31.01600 -0.16800  -22.76500 1.000 27.58415  ? 302 THR B C      1 
ATOM   4912 O O      . THR B 1 311 ? 31.38400 -1.08700  -22.02400 1.000 29.56683  ? 302 THR B O      1 
ATOM   4913 C CB     . THR B 1 311 ? 28.96500 1.16800   -22.20900 1.000 30.32120  ? 302 THR B CB     1 
ATOM   4914 O OG1    . THR B 1 311 ? 28.49500 2.34300   -21.53600 1.000 33.42113  ? 302 THR B OG1    1 
ATOM   4915 C CG2    . THR B 1 311 ? 28.39100 -0.06300  -21.52800 1.000 27.40571  ? 302 THR B CG2    1 
ATOM   4916 N N      . LEU B 1 312 ? 31.05700 -0.27100  -24.09600 1.000 23.35743  ? 303 LEU B N      1 
ATOM   4917 C CA     . LEU B 1 312 ? 31.60300 -1.47700  -24.70900 1.000 25.40858  ? 303 LEU B CA     1 
ATOM   4918 C C      . LEU B 1 312 ? 33.10500 -1.58200  -24.49100 1.000 27.38835  ? 303 LEU B C      1 
ATOM   4919 O O      . LEU B 1 312 ? 33.63700 -2.69200  -24.37200 1.000 30.18927  ? 303 LEU B O      1 
ATOM   4920 C CB     . LEU B 1 312 ? 31.27900 -1.50900  -26.20200 1.000 23.76819  ? 303 LEU B CB     1 
ATOM   4921 C CG     . LEU B 1 312 ? 29.79500 -1.48700  -26.56800 1.000 32.47902  ? 303 LEU B CG     1 
ATOM   4922 C CD1    . LEU B 1 312 ? 29.60900 -1.74500  -28.05400 1.000 31.86289  ? 303 LEU B CD1    1 
ATOM   4923 C CD2    . LEU B 1 312 ? 29.01200 -2.49500  -25.73800 1.000 22.97877  ? 303 LEU B CD2    1 
ATOM   4924 N N      . ARG B 1 313 ? 33.80300 -0.44600  -24.43400 1.000 26.23067  ? 304 ARG B N      1 
ATOM   4925 C CA     . ARG B 1 313 ? 35.23700 -0.47100  -24.16900 1.000 28.16988  ? 304 ARG B CA     1 
ATOM   4926 C C      . ARG B 1 313 ? 35.52500 -0.99700  -22.76900 1.000 25.77526  ? 304 ARG B C      1 
ATOM   4927 O O      . ARG B 1 313 ? 36.45600 -1.78800  -22.57700 1.000 25.15142  ? 304 ARG B O      1 
ATOM   4928 C CB     . ARG B 1 313 ? 35.82500 0.92900   -24.35800 1.000 24.87729  ? 304 ARG B CB     1 
ATOM   4929 C CG     . ARG B 1 313 ? 37.34600 0.99100   -24.46800 1.000 28.91775  ? 304 ARG B CG     1 
ATOM   4930 C CD     . ARG B 1 313 ? 38.04000 1.05900   -23.11100 1.000 31.41866  ? 304 ARG B CD     1 
ATOM   4931 N NE     . ARG B 1 313 ? 39.35800 1.67300   -23.21600 1.000 36.34807  ? 304 ARG B NE     1 
ATOM   4932 C CZ     . ARG B 1 313 ? 40.45200 1.04200   -23.62000 1.000 31.09760  ? 304 ARG B CZ     1 
ATOM   4933 N NH1    . ARG B 1 313 ? 40.42800 -0.23700  -23.95700 1.000 28.58816  ? 304 ARG B NH1    1 
ATOM   4934 N NH2    . ARG B 1 313 ? 41.59800 1.71200   -23.69100 1.000 31.91564  ? 304 ARG B NH2    1 
ATOM   4935 N N      . ASN B 1 314 ? 34.73500 -0.57200  -21.78000 1.000 28.12272  ? 305 ASN B N      1 
ATOM   4936 C CA     . ASN B 1 314 ? 34.95000 -1.02600  -20.41000 1.000 28.29595  ? 305 ASN B CA     1 
ATOM   4937 C C      . ASN B 1 314 ? 34.65600 -2.51200  -20.25300 1.000 25.50901  ? 305 ASN B C      1 
ATOM   4938 O O      . ASN B 1 314 ? 35.28400 -3.18100  -19.42400 1.000 27.68743  ? 305 ASN B O      1 
ATOM   4939 C CB     . ASN B 1 314 ? 34.08400 -0.21700  -19.44400 1.000 28.44053  ? 305 ASN B CB     1 
ATOM   4940 C CG     . ASN B 1 314 ? 34.53000 1.22600   -19.32700 1.000 26.47897  ? 305 ASN B CG     1 
ATOM   4941 O OD1    . ASN B 1 314 ? 35.71200 1.53700   -19.46900 1.000 30.32001  ? 305 ASN B OD1    1 
ATOM   4942 N ND2    . ASN B 1 314 ? 33.58400 2.11700   -19.05800 1.000 34.04994  ? 305 ASN B ND2    1 
ATOM   4943 N N      . ALA B 1 315 ? 33.71400 -3.04500  -21.03100 1.000 24.58428  ? 306 ALA B N      1 
ATOM   4944 C CA     . ALA B 1 315 ? 33.31900 -4.44000  -20.88500 1.000 24.60542  ? 306 ALA B CA     1 
ATOM   4945 C C      . ALA B 1 315 ? 34.23900 -5.40000  -21.62500 1.000 24.60837  ? 306 ALA B C      1 
ATOM   4946 O O      . ALA B 1 315 ? 34.29600 -6.57900  -21.26200 1.000 21.46684  ? 306 ALA B O      1 
ATOM   4947 C CB     . ALA B 1 315 ? 31.88100 -4.63500  -21.37200 1.000 26.33968  ? 306 ALA B CB     1 
ATOM   4948 N N      . TYR B 1 316 ? 34.95400 -4.93000  -22.64500 1.000 25.96038  ? 307 TYR B N      1 
ATOM   4949 C CA     . TYR B 1 316 ? 35.79700 -5.79700  -23.45600 1.000 26.75779  ? 307 TYR B CA     1 
ATOM   4950 C C      . TYR B 1 316 ? 37.21100 -5.86700  -22.89600 1.000 29.14500  ? 307 TYR B C      1 
ATOM   4951 O O      . TYR B 1 316 ? 37.79500 -4.85000  -22.51000 1.000 31.91299  ? 307 TYR B O      1 
ATOM   4952 C CB     . TYR B 1 316 ? 35.83800 -5.31500  -24.90600 1.000 25.79329  ? 307 TYR B CB     1 
ATOM   4953 C CG     . TYR B 1 316 ? 36.79600 -6.10800  -25.76200 1.000 26.32778  ? 307 TYR B CG     1 
ATOM   4954 C CD1    . TYR B 1 316 ? 36.59100 -7.46300  -25.99200 1.000 26.88303  ? 307 TYR B CD1    1 
ATOM   4955 C CD2    . TYR B 1 316 ? 37.90800 -5.50800  -26.33600 1.000 26.06781  ? 307 TYR B CD2    1 
ATOM   4956 C CE1    . TYR B 1 316 ? 37.46700 -8.19700  -26.77000 1.000 28.22991  ? 307 TYR B CE1    1 
ATOM   4957 C CE2    . TYR B 1 316 ? 38.78700 -6.23300  -27.11700 1.000 27.32321  ? 307 TYR B CE2    1 
ATOM   4958 C CZ     . TYR B 1 316 ? 38.56200 -7.57700  -27.33000 1.000 28.52981  ? 307 TYR B CZ     1 
ATOM   4959 O OH     . TYR B 1 316 ? 39.43700 -8.30100  -28.10700 1.000 31.25530  ? 307 TYR B OH     1 
ATOM   4960 N N      . GLN B 1 317 ? 37.76200 -7.08000  -22.87100 1.000 26.82659  ? 308 GLN B N      1 
ATOM   4961 C CA     . GLN B 1 317 ? 39.10200 -7.34000  -22.34500 1.000 29.79636  ? 308 GLN B CA     1 
ATOM   4962 C C      . GLN B 1 317 ? 40.07000 -7.40800  -23.52200 1.000 30.69702  ? 308 GLN B C      1 
ATOM   4963 O O      . GLN B 1 317 ? 40.35900 -8.48200  -24.05200 1.000 32.38614  ? 308 GLN B O      1 
ATOM   4964 C CB     . GLN B 1 317 ? 39.11600 -8.63000  -21.53300 1.000 27.92598  ? 308 GLN B CB     1 
ATOM   4965 C CG     . GLN B 1 317 ? 38.06000 -8.68300  -20.44300 1.000 28.56446  ? 308 GLN B CG     1 
ATOM   4966 C CD     . GLN B 1 317 ? 37.88400 -10.07400 -19.86600 1.000 34.31326  ? 308 GLN B CD     1 
ATOM   4967 O OE1    . GLN B 1 317 ? 38.65300 -10.98800 -20.16700 1.000 35.05120  ? 308 GLN B OE1    1 
ATOM   4968 N NE2    . GLN B 1 317 ? 36.86200 -10.24300 -19.03600 1.000 33.59491  ? 308 GLN B NE2    1 
ATOM   4969 N N      . GLY B 1 318 ? 40.57700 -6.25100  -23.93200 1.000 25.49342  ? 309 GLY B N      1 
ATOM   4970 C CA     . GLY B 1 318 ? 41.55800 -6.21500  -24.99900 1.000 27.35417  ? 309 GLY B CA     1 
ATOM   4971 C C      . GLY B 1 318 ? 41.57600 -4.85500  -25.67800 1.000 26.16191  ? 309 GLY B C      1 
ATOM   4972 O O      . GLY B 1 318 ? 41.04700 -3.87600  -25.15500 1.000 27.00493  ? 309 GLY B O      1 
ATOM   4973 N N      . THR B 1 319 ? 42.20100 -4.83400  -26.85300 1.000 24.45802  ? 310 THR B N      1 
ATOM   4974 C CA     . THR B 1 319 ? 42.35900 -3.60200  -27.61200 1.000 26.02152  ? 310 THR B CA     1 
ATOM   4975 C C      . THR B 1 319 ? 41.01900 -3.14000  -28.17300 1.000 24.84889  ? 310 THR B C      1 
ATOM   4976 O O      . THR B 1 319 ? 40.21800 -3.94400  -28.65900 1.000 23.73128  ? 310 THR B O      1 
ATOM   4977 C CB     . THR B 1 319 ? 43.36500 -3.81400  -28.74500 1.000 26.77330  ? 310 THR B CB     1 
ATOM   4978 O OG1    . THR B 1 319 ? 44.60200 -4.28900  -28.20100 1.000 27.03335  ? 310 THR B OG1    1 
ATOM   4979 C CG2    . THR B 1 319 ? 43.61500 -2.51700  -29.50100 1.000 23.79499  ? 310 THR B CG2    1 
ATOM   4980 N N      . PHE B 1 320 ? 40.77700 -1.83300  -28.10300 1.000 22.45986  ? 311 PHE B N      1 
ATOM   4981 C CA     . PHE B 1 320 ? 39.51500 -1.24200  -28.52800 1.000 25.46413  ? 311 PHE B CA     1 
ATOM   4982 C C      . PHE B 1 320 ? 39.79300 -0.12200  -29.51700 1.000 20.30219  ? 311 PHE B C      1 
ATOM   4983 O O      . PHE B 1 320 ? 40.66900 0.71600   -29.28000 1.000 24.28387  ? 311 PHE B O      1 
ATOM   4984 C CB     . PHE B 1 320 ? 38.73000 -0.71000  -27.32300 1.000 23.11310  ? 311 PHE B CB     1 
ATOM   4985 C CG     . PHE B 1 320 ? 37.31800 -0.31000  -27.64200 1.000 26.57075  ? 311 PHE B CG     1 
ATOM   4986 C CD1    . PHE B 1 320 ? 36.28800 -1.23000  -27.55100 1.000 24.10197  ? 311 PHE B CD1    1 
ATOM   4987 C CD2    . PHE B 1 320 ? 37.01900 0.98900   -28.02100 1.000 25.77342  ? 311 PHE B CD2    1 
ATOM   4988 C CE1    . PHE B 1 320 ? 34.98600 -0.86500  -27.83800 1.000 23.06817  ? 311 PHE B CE1    1 
ATOM   4989 C CE2    . PHE B 1 320 ? 35.72000 1.36000   -28.31100 1.000 25.27310  ? 311 PHE B CE2    1 
ATOM   4990 C CZ     . PHE B 1 320 ? 34.70200 0.43200   -28.21800 1.000 24.98565  ? 311 PHE B CZ     1 
ATOM   4991 N N      . ILE B 1 321 ? 39.04900 -0.10800  -30.62000 1.000 25.24513  ? 312 ILE B N      1 
ATOM   4992 C CA     . ILE B 1 321 ? 39.18700 0.90600   -31.66100 1.000 23.14654  ? 312 ILE B CA     1 
ATOM   4993 C C      . ILE B 1 321 ? 37.86200 1.64600   -31.77600 1.000 21.58639  ? 312 ILE B C      1 
ATOM   4994 O O      . ILE B 1 321 ? 36.82700 1.03200   -32.06400 1.000 23.26304  ? 312 ILE B O      1 
ATOM   4995 C CB     . ILE B 1 321 ? 39.58300 0.29400   -33.01400 1.000 24.85975  ? 312 ILE B CB     1 
ATOM   4996 C CG1    . ILE B 1 321 ? 40.85400 -0.54400  -32.87700 1.000 22.89044  ? 312 ILE B CG1    1 
ATOM   4997 C CG2    . ILE B 1 321 ? 39.77800 1.38800   -34.05600 1.000 23.97814  ? 312 ILE B CG2    1 
ATOM   4998 C CD1    . ILE B 1 321 ? 41.37300 -1.07200  -34.19900 1.000 22.70533  ? 312 ILE B CD1    1 
ATOM   4999 N N      . CYS B 1 322 ? 37.89300 2.95600   -31.55600 1.000 21.39126  ? 313 CYS B N      1 
ATOM   5000 C CA     . CYS B 1 322 ? 36.70400 3.78200   -31.70500 1.000 28.26241  ? 313 CYS B CA     1 
ATOM   5001 C C      . CYS B 1 322 ? 36.64500 4.36800   -33.11000 1.000 24.58299  ? 313 CYS B C      1 
ATOM   5002 O O      . CYS B 1 322 ? 37.67400 4.66600   -33.72400 1.000 27.27418  ? 313 CYS B O      1 
ATOM   5003 C CB     . CYS B 1 322 ? 36.68200 4.90300   -30.66500 1.000 23.11978  ? 313 CYS B CB     1 
ATOM   5004 S SG     . CYS B 1 322 ? 38.05100 6.07000   -30.79300 1.000 27.25696  ? 313 CYS B SG     1 
ATOM   5005 N N      . SER B 1 323 ? 35.42400 4.53400   -33.61400 1.000 24.99363  ? 314 SER B N      1 
ATOM   5006 C CA     . SER B 1 323 ? 35.21700 4.93800   -34.99700 1.000 24.72464  ? 314 SER B CA     1 
ATOM   5007 C C      . SER B 1 323 ? 33.92400 5.72900   -35.12200 1.000 28.43395  ? 314 SER B C      1 
ATOM   5008 O O      . SER B 1 323 ? 32.93300 5.42500   -34.45300 1.000 23.69177  ? 314 SER B O      1 
ATOM   5009 C CB     . SER B 1 323 ? 35.16900 3.72000   -35.92400 1.000 23.31328  ? 314 SER B CB     1 
ATOM   5010 O OG     . SER B 1 323 ? 34.66700 4.07600   -37.19900 1.000 26.75415  ? 314 SER B OG     1 
ATOM   5011 N N      . GLY B 1 324 ? 33.94100 6.73600   -35.99200 1.000 31.47739  ? 315 GLY B N      1 
ATOM   5012 C CA     . GLY B 1 324 ? 32.74100 7.49200   -36.28600 1.000 28.99278  ? 315 GLY B CA     1 
ATOM   5013 C C      . GLY B 1 324 ? 32.82900 8.96100   -35.93200 1.000 30.12600  ? 315 GLY B C      1 
ATOM   5014 O O      . GLY B 1 324 ? 32.65600 9.33800   -34.77000 1.000 26.07561  ? 315 GLY B O      1 
ATOM   5015 N N      . GLY B 1 325 ? 33.09700 9.79900   -36.93000 1.000 35.42790  ? 316 GLY B N      1 
ATOM   5016 C CA     . GLY B 1 325 ? 33.11500 11.23500  -36.72500 1.000 30.54559  ? 316 GLY B CA     1 
ATOM   5017 C C      . GLY B 1 325 ? 34.21700 11.74100  -35.82300 1.000 34.41196  ? 316 GLY B C      1 
ATOM   5018 O O      . GLY B 1 325 ? 34.01700 12.72800  -35.10800 1.000 33.64186  ? 316 GLY B O      1 
ATOM   5019 N N      . TYR B 1 326 ? 35.37800 11.09600  -35.83400 1.000 27.21604  ? 317 TYR B N      1 
ATOM   5020 C CA     . TYR B 1 326 ? 36.49500 11.52900  -35.01000 1.000 29.28188  ? 317 TYR B CA     1 
ATOM   5021 C C      . TYR B 1 326 ? 37.37500 12.50800  -35.77500 1.000 29.93215  ? 317 TYR B C      1 
ATOM   5022 O O      . TYR B 1 326 ? 37.65100 12.32300  -36.96300 1.000 29.29349  ? 317 TYR B O      1 
ATOM   5023 C CB     . TYR B 1 326 ? 37.31700 10.33000  -34.53700 1.000 26.14488  ? 317 TYR B CB     1 
ATOM   5024 C CG     . TYR B 1 326 ? 36.68200 9.61100   -33.37100 1.000 27.79456  ? 317 TYR B CG     1 
ATOM   5025 C CD1    . TYR B 1 326 ? 36.91900 10.02300  -32.06500 1.000 30.04061  ? 317 TYR B CD1    1 
ATOM   5026 C CD2    . TYR B 1 326 ? 35.83200 8.53100   -33.57300 1.000 25.21123  ? 317 TYR B CD2    1 
ATOM   5027 C CE1    . TYR B 1 326 ? 36.33300 9.37500   -30.99300 1.000 30.46686  ? 317 TYR B CE1    1 
ATOM   5028 C CE2    . TYR B 1 326 ? 35.24100 7.87700   -32.50700 1.000 27.15185  ? 317 TYR B CE2    1 
ATOM   5029 C CZ     . TYR B 1 326 ? 35.49500 8.30300   -31.22000 1.000 26.99347  ? 317 TYR B CZ     1 
ATOM   5030 O OH     . TYR B 1 326 ? 34.90800 7.65400   -30.15900 1.000 36.18534  ? 317 TYR B OH     1 
ATOM   5031 N N      . THR B 1 327 ? 37.79600 13.56100  -35.08500 1.000 32.72274  ? 318 THR B N      1 
ATOM   5032 C CA     . THR B 1 327 ? 38.67600 14.58300  -35.62300 1.000 27.99133  ? 318 THR B CA     1 
ATOM   5033 C C      . THR B 1 327 ? 40.04300 14.46400  -34.95800 1.000 30.72393  ? 318 THR B C      1 
ATOM   5034 O O      . THR B 1 327 ? 40.32600 13.49800  -34.23800 1.000 30.47060  ? 318 THR B O      1 
ATOM   5035 C CB     . THR B 1 327 ? 38.06300 15.97000  -35.41700 1.000 29.95939  ? 318 THR B CB     1 
ATOM   5036 O OG1    . THR B 1 327 ? 37.89500 16.21400  -34.01400 1.000 35.41267  ? 318 THR B OG1    1 
ATOM   5037 C CG2    . THR B 1 327 ? 36.71000 16.06300  -36.10800 1.000 26.16255  ? 318 THR B CG2    1 
ATOM   5038 N N      . ARG B 1 328 ? 40.90200 15.45600  -35.19700 1.000 29.95348  ? 319 ARG B N      1 
ATOM   5039 C CA     . ARG B 1 328 ? 42.20300 15.46100  -34.53800 1.000 33.95179  ? 319 ARG B CA     1 
ATOM   5040 C C      . ARG B 1 328 ? 42.05000 15.63600  -33.03200 1.000 31.39694  ? 319 ARG B C      1 
ATOM   5041 O O      . ARG B 1 328 ? 42.58100 14.84200  -32.24800 1.000 29.10541  ? 319 ARG B O      1 
ATOM   5042 C CB     . ARG B 1 328 ? 43.09100 16.56100  -35.12100 1.000 35.09426  ? 319 ARG B CB     1 
ATOM   5043 C CG     . ARG B 1 328 ? 44.47600 16.60500  -34.49900 1.000 34.37170  ? 319 ARG B CG     1 
ATOM   5044 C CD     . ARG B 1 328 ? 45.28500 17.78400  -35.00700 1.000 36.80309  ? 319 ARG B CD     1 
ATOM   5045 N NE     . ARG B 1 328 ? 46.63900 17.77600  -34.46700 1.000 35.52492  ? 319 ARG B NE     1 
ATOM   5046 C CZ     . ARG B 1 328 ? 46.97700 18.27500  -33.28600 1.000 39.05005  ? 319 ARG B CZ     1 
ATOM   5047 N NH1    . ARG B 1 328 ? 46.08200 18.84000  -32.49200 1.000 38.22217  ? 319 ARG B NH1    1 
ATOM   5048 N NH2    . ARG B 1 328 ? 48.24500 18.20400  -32.89100 1.000 39.14754  ? 319 ARG B NH2    1 
ATOM   5049 N N      . GLU B 1 329 ? 41.31400 16.66700  -32.60900 1.000 30.91508  ? 320 GLU B N      1 
ATOM   5050 C CA     . GLU B 1 329 ? 41.14900 16.91800  -31.18000 1.000 33.67027  ? 320 GLU B CA     1 
ATOM   5051 C C      . GLU B 1 329 ? 40.35600 15.80300  -30.50700 1.000 33.15013  ? 320 GLU B C      1 
ATOM   5052 O O      . GLU B 1 329 ? 40.71900 15.35000  -29.41600 1.000 31.43987  ? 320 GLU B O      1 
ATOM   5053 C CB     . GLU B 1 329 ? 40.47200 18.27100  -30.95700 1.000 31.08480  ? 320 GLU B CB     1 
ATOM   5054 N N      . LEU B 1 330 ? 39.27200 15.34600  -31.14200 1.000 32.04022  ? 321 LEU B N      1 
ATOM   5055 C CA     . LEU B 1 330 ? 38.49000 14.25800  -30.56500 1.000 31.38270  ? 321 LEU B CA     1 
ATOM   5056 C C      . LEU B 1 330 ? 39.28800 12.96100  -30.50800 1.000 33.52305  ? 321 LEU B C      1 
ATOM   5057 O O      . LEU B 1 330 ? 39.12200 12.17500  -29.56900 1.000 31.52419  ? 321 LEU B O      1 
ATOM   5058 C CB     . LEU B 1 330 ? 37.19800 14.05700  -31.35800 1.000 31.67085  ? 321 LEU B CB     1 
ATOM   5059 C CG     . LEU B 1 330 ? 36.17700 15.19500  -31.29000 1.000 35.71532  ? 321 LEU B CG     1 
ATOM   5060 C CD1    . LEU B 1 330 ? 34.96900 14.88400  -32.15900 1.000 25.97283  ? 321 LEU B CD1    1 
ATOM   5061 C CD2    . LEU B 1 330 ? 35.75200 15.45200  -29.85000 1.000 31.37889  ? 321 LEU B CD2    1 
ATOM   5062 N N      . GLY B 1 331 ? 40.15400 12.72000  -31.49500 1.000 34.46187  ? 322 GLY B N      1 
ATOM   5063 C CA     . GLY B 1 331 ? 41.00600 11.54200  -31.44300 1.000 29.76339  ? 322 GLY B CA     1 
ATOM   5064 C C      . GLY B 1 331 ? 42.01200 11.60700  -30.31000 1.000 33.64284  ? 322 GLY B C      1 
ATOM   5065 O O      . GLY B 1 331 ? 42.21700 10.62400  -29.59100 1.000 33.63736  ? 322 GLY B O      1 
ATOM   5066 N N      . ILE B 1 332 ? 42.65400 12.76500  -30.13600 1.000 31.16502  ? 323 ILE B N      1 
ATOM   5067 C CA     . ILE B 1 332 ? 43.55400 12.96500  -29.00300 1.000 31.93378  ? 323 ILE B CA     1 
ATOM   5068 C C      . ILE B 1 332 ? 42.80100 12.79700  -27.68900 1.000 32.12307  ? 323 ILE B C      1 
ATOM   5069 O O      . ILE B 1 332 ? 43.29600 12.16900  -26.74400 1.000 31.67137  ? 323 ILE B O      1 
ATOM   5070 C CB     . ILE B 1 332 ? 44.22400 14.35000  -29.09700 1.000 33.80296  ? 323 ILE B CB     1 
ATOM   5071 C CG1    . ILE B 1 332 ? 45.14100 14.42100  -30.32100 1.000 36.55606  ? 323 ILE B CG1    1 
ATOM   5072 C CG2    . ILE B 1 332 ? 44.98900 14.66900  -27.82000 1.000 36.05879  ? 323 ILE B CG2    1 
ATOM   5073 C CD1    . ILE B 1 332 ? 45.73400 15.79400  -30.56300 1.000 36.10209  ? 323 ILE B CD1    1 
ATOM   5074 N N      . GLU B 1 333 ? 41.58600 13.34500  -27.61500 1.000 29.47603  ? 324 GLU B N      1 
ATOM   5075 C CA     . GLU B 1 333 ? 40.78800 13.26800  -26.39500 1.000 33.58793  ? 324 GLU B CA     1 
ATOM   5076 C C      . GLU B 1 333 ? 40.40600 11.82900  -26.06200 1.000 39.86537  ? 324 GLU B C      1 
ATOM   5077 O O      . GLU B 1 333 ? 40.37900 11.44300  -24.88700 1.000 36.60051  ? 324 GLU B O      1 
ATOM   5078 C CB     . GLU B 1 333 ? 39.54000 14.13700  -26.55400 1.000 42.37416  ? 324 GLU B CB     1 
ATOM   5079 C CG     . GLU B 1 333 ? 38.42218 13.86810  -25.56031 1.000 49.12508  ? 324 GLU B CG     1 
ATOM   5080 C CD     . GLU B 1 333 ? 37.18770 14.69743  -25.86619 1.000 56.93972  ? 324 GLU B CD     1 
ATOM   5081 O OE1    . GLU B 1 333 ? 37.32531 15.93367  -26.00142 1.000 61.59864  ? 324 GLU B OE1    1 
ATOM   5082 O OE2    . GLU B 1 333 ? 36.08871 14.11610  -25.99820 1.000 55.29151  ? 324 GLU B OE2    1 
ATOM   5083 N N      . ALA B 1 334 ? 40.11200 11.02200  -27.08300 1.000 35.99685  ? 325 ALA B N      1 
ATOM   5084 C CA     . ALA B 1 334 ? 39.65100 9.65900   -26.84100 1.000 31.82576  ? 325 ALA B CA     1 
ATOM   5085 C C      . ALA B 1 334 ? 40.75500 8.79200   -26.24900 1.000 33.77443  ? 325 ALA B C      1 
ATOM   5086 O O      . ALA B 1 334 ? 40.49400 7.95800   -25.37400 1.000 35.30433  ? 325 ALA B O      1 
ATOM   5087 C CB     . ALA B 1 334 ? 39.12400 9.04500   -28.13800 1.000 31.71515  ? 325 ALA B CB     1 
ATOM   5088 N N      . VAL B 1 335 ? 41.99200 8.97000   -26.71100 1.000 30.83726  ? 326 VAL B N      1 
ATOM   5089 C CA     . VAL B 1 335 ? 43.08900 8.15500   -26.20000 1.000 33.28526  ? 326 VAL B CA     1 
ATOM   5090 C C      . VAL B 1 335 ? 43.54300 8.65000   -24.83200 1.000 35.28233  ? 326 VAL B C      1 
ATOM   5091 O O      . VAL B 1 335 ? 43.81500 7.84800   -23.93100 1.000 35.56405  ? 326 VAL B O      1 
ATOM   5092 C CB     . VAL B 1 335 ? 44.24800 8.13200   -27.21200 1.000 29.69281  ? 326 VAL B CB     1 
ATOM   5093 C CG1    . VAL B 1 335 ? 45.45700 7.42200   -26.62200 1.000 35.11000  ? 326 VAL B CG1    1 
ATOM   5094 C CG2    . VAL B 1 335 ? 43.80800 7.45100   -28.49700 1.000 33.60253  ? 326 VAL B CG2    1 
ATOM   5095 N N      . ALA B 1 336 ? 43.62500 9.97000   -24.65100 1.000 34.35847  ? 327 ALA B N      1 
ATOM   5096 C CA     . ALA B 1 336 ? 44.10300 10.51400  -23.38400 1.000 35.27030  ? 327 ALA B CA     1 
ATOM   5097 C C      . ALA B 1 336 ? 43.17900 10.13500  -22.23200 1.000 32.94018  ? 327 ALA B C      1 
ATOM   5098 O O      . ALA B 1 336 ? 43.64500 9.85400   -21.12200 1.000 34.36870  ? 327 ALA B O      1 
ATOM   5099 C CB     . ALA B 1 336 ? 44.24400 12.03300  -23.48500 1.000 33.57101  ? 327 ALA B CB     1 
ATOM   5100 N N      . GLN B 1 337 ? 41.87100 10.11100  -22.47900 1.000 35.68911  ? 328 GLN B N      1 
ATOM   5101 C CA     . GLN B 1 337 ? 40.88600 9.76600   -21.46400 1.000 35.93632  ? 328 GLN B CA     1 
ATOM   5102 C C      . GLN B 1 337 ? 40.61000 8.26800   -21.39100 1.000 36.00801  ? 328 GLN B C      1 
ATOM   5103 O O      . GLN B 1 337 ? 39.69500 7.85300   -20.67100 1.000 35.42926  ? 328 GLN B O      1 
ATOM   5104 C CB     . GLN B 1 337 ? 39.58200 10.52700  -21.72000 1.000 32.72858  ? 328 GLN B CB     1 
ATOM   5105 C CG     . GLN B 1 337 ? 39.71354 12.03178  -21.54746 1.000 42.23630  ? 328 GLN B CG     1 
ATOM   5106 C CD     . GLN B 1 337 ? 38.55109 12.79882  -22.14636 1.000 48.49575  ? 328 GLN B CD     1 
ATOM   5107 O OE1    . GLN B 1 337 ? 37.59800 12.20972  -22.65840 1.000 47.15989  ? 328 GLN B OE1    1 
ATOM   5108 N NE2    . GLN B 1 337 ? 38.62582 14.12437  -22.08917 1.000 50.07326  ? 328 GLN B NE2    1 
ATOM   5109 N N      . GLY B 1 338 ? 41.37300 7.45300   -22.11700 1.000 35.43861  ? 329 GLY B N      1 
ATOM   5110 C CA     . GLY B 1 338 ? 41.21200 6.01500   -22.05900 1.000 33.09987  ? 329 GLY B CA     1 
ATOM   5111 C C      . GLY B 1 338 ? 39.99000 5.46600   -22.75700 1.000 33.08019  ? 329 GLY B C      1 
ATOM   5112 O O      . GLY B 1 338 ? 39.67800 4.28400   -22.58200 1.000 34.86393  ? 329 GLY B O      1 
ATOM   5113 N N      . ASP B 1 339 ? 39.28700 6.28100   -23.54700 1.000 33.51376  ? 330 ASP B N      1 
ATOM   5114 C CA     . ASP B 1 339 ? 38.09900 5.80100   -24.24500 1.000 39.18318  ? 330 ASP B CA     1 
ATOM   5115 C C      . ASP B 1 339 ? 38.42600 4.76000   -25.30700 1.000 34.17582  ? 330 ASP B C      1 
ATOM   5116 O O      . ASP B 1 339 ? 37.54300 3.97900   -25.67900 1.000 33.61312  ? 330 ASP B O      1 
ATOM   5117 C CB     . ASP B 1 339 ? 37.34900 6.97000   -24.88700 1.000 40.01195  ? 330 ASP B CB     1 
ATOM   5118 C CG     . ASP B 1 339 ? 36.76300 7.92200   -23.86200 1.000 43.24138  ? 330 ASP B CG     1 
ATOM   5119 O OD1    . ASP B 1 339 ? 36.49500 7.48300   -22.72500 1.000 39.06745  ? 330 ASP B OD1    1 
ATOM   5120 O OD2    . ASP B 1 339 ? 36.56800 9.11000   -24.19600 1.000 48.15552  ? 330 ASP B OD2    1 
ATOM   5121 N N      . ALA B 1 340 ? 39.66100 4.73000   -25.80100 1.000 29.68883  ? 331 ALA B N      1 
ATOM   5122 C CA     . ALA B 1 340 ? 40.04600 3.76600   -26.82200 1.000 29.21067  ? 331 ALA B CA     1 
ATOM   5123 C C      . ALA B 1 340 ? 41.56100 3.68000   -26.88400 1.000 28.53391  ? 331 ALA B C      1 
ATOM   5124 O O      . ALA B 1 340 ? 42.27500 4.59100   -26.45500 1.000 28.88372  ? 331 ALA B O      1 
ATOM   5125 C CB     . ALA B 1 340 ? 39.48000 4.13900   -28.19600 1.000 26.82938  ? 331 ALA B CB     1 
ATOM   5126 N N      . ASP B 1 341 ? 42.04000 2.56400   -27.42800 1.000 24.46389  ? 332 ASP B N      1 
ATOM   5127 C CA     . ASP B 1 341 ? 43.46400 2.38000   -27.67300 1.000 27.59738  ? 332 ASP B CA     1 
ATOM   5128 C C      . ASP B 1 341 ? 43.87500 2.84800   -29.06100 1.000 29.52416  ? 332 ASP B C      1 
ATOM   5129 O O      . ASP B 1 341 ? 45.00000 3.32600   -29.23900 1.000 21.70484  ? 332 ASP B O      1 
ATOM   5130 C CB     . ASP B 1 341 ? 43.83900 0.90600   -27.49700 1.000 25.37716  ? 332 ASP B CB     1 
ATOM   5131 C CG     . ASP B 1 341 ? 43.41600 0.35800   -26.15000 1.000 28.87455  ? 332 ASP B CG     1 
ATOM   5132 O OD1    . ASP B 1 341 ? 43.81900 0.93700   -25.11800 1.000 27.56904  ? 332 ASP B OD1    1 
ATOM   5133 O OD2    . ASP B 1 341 ? 42.67000 -0.64400  -26.12300 1.000 27.62275  ? 332 ASP B OD2    1 
ATOM   5134 N N      . LEU B 1 342 ? 42.98500 2.72000   -30.04200 1.000 27.53616  ? 333 LEU B N      1 
ATOM   5135 C CA     . LEU B 1 342 ? 43.23600 3.15400   -31.40700 1.000 25.71415  ? 333 LEU B CA     1 
ATOM   5136 C C      . LEU B 1 342 ? 42.02800 3.93100   -31.91100 1.000 25.60057  ? 333 LEU B C      1 
ATOM   5137 O O      . LEU B 1 342 ? 40.90300 3.72800   -31.44400 1.000 24.96467  ? 333 LEU B O      1 
ATOM   5138 C CB     . LEU B 1 342 ? 43.51900 1.96000   -32.33200 1.000 23.67112  ? 333 LEU B CB     1 
ATOM   5139 C CG     . LEU B 1 342 ? 44.63900 1.01100   -31.89500 1.000 25.86791  ? 333 LEU B CG     1 
ATOM   5140 C CD1    . LEU B 1 342 ? 44.60900 -0.27600  -32.70200 1.000 24.93514  ? 333 LEU B CD1    1 
ATOM   5141 C CD2    . LEU B 1 342 ? 45.99200 1.68700   -32.02100 1.000 27.72649  ? 333 LEU B CD2    1 
ATOM   5142 N N      . VAL B 1 343 ? 42.27000 4.82700   -32.86500 1.000 30.82549  ? 334 VAL B N      1 
ATOM   5143 C CA     . VAL B 1 343 ? 41.22400 5.64600   -33.47000 1.000 25.85210  ? 334 VAL B CA     1 
ATOM   5144 C C      . VAL B 1 343 ? 41.31700 5.48700   -34.98100 1.000 24.68926  ? 334 VAL B C      1 
ATOM   5145 O O      . VAL B 1 343 ? 42.36300 5.77700   -35.57400 1.000 24.94195  ? 334 VAL B O      1 
ATOM   5146 C CB     . VAL B 1 343 ? 41.34600 7.12900   -33.08100 1.000 21.89383  ? 334 VAL B CB     1 
ATOM   5147 C CG1    . VAL B 1 343 ? 40.20200 7.92700   -33.68200 1.000 19.49743  ? 334 VAL B CG1    1 
ATOM   5148 C CG2    . VAL B 1 343 ? 41.38300 7.28900   -31.56700 1.000 22.32133  ? 334 VAL B CG2    1 
ATOM   5149 N N      . SER B 1 344 ? 40.23000 5.03900   -35.60200 1.000 21.20918  ? 335 SER B N      1 
ATOM   5150 C CA     . SER B 1 344 ? 40.18000 4.85900   -37.04600 1.000 20.85428  ? 335 SER B CA     1 
ATOM   5151 C C      . SER B 1 344 ? 39.47200 6.04100   -37.69600 1.000 20.42335  ? 335 SER B C      1 
ATOM   5152 O O      . SER B 1 344 ? 38.44700 6.51700   -37.20000 1.000 26.88682  ? 335 SER B O      1 
ATOM   5153 C CB     . SER B 1 344 ? 39.47300 3.55300   -37.41700 1.000 22.93155  ? 335 SER B CB     1 
ATOM   5154 O OG     . SER B 1 344 ? 38.08000 3.62700   -37.17300 1.000 22.83333  ? 335 SER B OG     1 
ATOM   5155 N N      . TYR B 1 345 ? 40.03200 6.51600   -38.80500 1.000 24.18601  ? 336 TYR B N      1 
ATOM   5156 C CA     . TYR B 1 345 ? 39.48500 7.63800   -39.55500 1.000 24.46963  ? 336 TYR B CA     1 
ATOM   5157 C C      . TYR B 1 345 ? 39.06900 7.15600   -40.93700 1.000 25.84233  ? 336 TYR B C      1 
ATOM   5158 O O      . TYR B 1 345 ? 39.82300 6.43300   -41.59800 1.000 22.08389  ? 336 TYR B O      1 
ATOM   5159 C CB     . TYR B 1 345 ? 40.50200 8.77700   -39.66500 1.000 22.35519  ? 336 TYR B CB     1 
ATOM   5160 C CG     . TYR B 1 345 ? 40.84300 9.42700   -38.34100 1.000 28.35957  ? 336 TYR B CG     1 
ATOM   5161 C CD1    . TYR B 1 345 ? 41.80600 8.88000   -37.50300 1.000 26.31887  ? 336 TYR B CD1    1 
ATOM   5162 C CD2    . TYR B 1 345 ? 40.20300 10.59100  -37.93100 1.000 28.07343  ? 336 TYR B CD2    1 
ATOM   5163 C CE1    . TYR B 1 345 ? 42.12100 9.47100   -36.29300 1.000 22.63836  ? 336 TYR B CE1    1 
ATOM   5164 C CE2    . TYR B 1 345 ? 40.51300 11.19000  -36.72200 1.000 23.68769  ? 336 TYR B CE2    1 
ATOM   5165 C CZ     . TYR B 1 345 ? 41.47100 10.62500  -35.90700 1.000 25.28838  ? 336 TYR B CZ     1 
ATOM   5166 O OH     . TYR B 1 345 ? 41.78100 11.21600  -34.70400 1.000 20.82571  ? 336 TYR B OH     1 
ATOM   5167 N N      . GLY B 1 346 ? 37.87800 7.55600   -41.36700 1.000 24.96278  ? 337 GLY B N      1 
ATOM   5168 C CA     . GLY B 1 346 ? 37.27900 7.11300   -42.60900 1.000 22.64543  ? 337 GLY B CA     1 
ATOM   5169 C C      . GLY B 1 346 ? 37.39400 8.19100   -43.66800 1.000 23.57338  ? 337 GLY B C      1 
ATOM   5170 O O      . GLY B 1 346 ? 38.38800 8.25800   -44.41300 1.000 22.24308  ? 337 GLY B O      1 
ATOM   5171 N N      . ARG B 1 347 ? 36.38300 9.05800   -43.75800 1.000 23.23855  ? 338 ARG B N      1 
ATOM   5172 C CA     . ARG B 1 347 ? 36.28400 10.00000  -44.87000 1.000 22.85798  ? 338 ARG B CA     1 
ATOM   5173 C C      . ARG B 1 347 ? 37.47300 10.95000  -44.94100 1.000 26.54293  ? 338 ARG B C      1 
ATOM   5174 O O      . ARG B 1 347 ? 37.89700 11.32200  -46.04100 1.000 26.12387  ? 338 ARG B O      1 
ATOM   5175 C CB     . ARG B 1 347 ? 34.97200 10.77800  -44.77100 1.000 24.76594  ? 338 ARG B CB     1 
ATOM   5176 C CG     . ARG B 1 347 ? 33.74400 9.93800   -45.08900 1.000 26.37668  ? 338 ARG B CG     1 
ATOM   5177 C CD     . ARG B 1 347 ? 32.48200 10.58200  -44.54600 1.000 26.78247  ? 338 ARG B CD     1 
ATOM   5178 N NE     . ARG B 1 347 ? 32.46900 10.59300  -43.08800 1.000 27.45590  ? 338 ARG B NE     1 
ATOM   5179 C CZ     . ARG B 1 347 ? 31.57300 11.24000  -42.35500 1.000 28.46986  ? 338 ARG B CZ     1 
ATOM   5180 N NH1    . ARG B 1 347 ? 30.60600 11.94600  -42.91500 1.000 31.96567  ? 338 ARG B NH1    1 
ATOM   5181 N NH2    . ARG B 1 347 ? 31.65200 11.17800  -41.02900 1.000 34.47515  ? 338 ARG B NH2    1 
ATOM   5182 N N      . LEU B 1 348 ? 38.02000 11.36300  -43.79700 1.000 22.72371  ? 339 LEU B N      1 
ATOM   5183 C CA     . LEU B 1 348 ? 39.19200 12.23400  -43.84200 1.000 24.84673  ? 339 LEU B CA     1 
ATOM   5184 C C      . LEU B 1 348 ? 40.39000 11.52600  -44.46000 1.000 28.79319  ? 339 LEU B C      1 
ATOM   5185 O O      . LEU B 1 348 ? 41.25900 12.17700  -45.05200 1.000 28.03726  ? 339 LEU B O      1 
ATOM   5186 C CB     . LEU B 1 348 ? 39.54800 12.73600  -42.44400 1.000 24.13121  ? 339 LEU B CB     1 
ATOM   5187 C CG     . LEU B 1 348 ? 38.62300 13.79800  -41.84700 1.000 28.19268  ? 339 LEU B CG     1 
ATOM   5188 C CD1    . LEU B 1 348 ? 39.07800 14.18100  -40.44500 1.000 25.77930  ? 339 LEU B CD1    1 
ATOM   5189 C CD2    . LEU B 1 348 ? 38.55800 15.02000  -42.74800 1.000 24.97022  ? 339 LEU B CD2    1 
ATOM   5190 N N      . PHE B 1 349 ? 40.45300 10.20000  -44.34000 1.000 24.47174  ? 340 PHE B N      1 
ATOM   5191 C CA     . PHE B 1 349 ? 41.55300 9.44800   -44.92600 1.000 27.32669  ? 340 PHE B CA     1 
ATOM   5192 C C      . PHE B 1 349 ? 41.40900 9.29100   -46.43400 1.000 23.68831  ? 340 PHE B C      1 
ATOM   5193 O O      . PHE B 1 349 ? 42.40100 8.99700   -47.11000 1.000 22.15044  ? 340 PHE B O      1 
ATOM   5194 C CB     . PHE B 1 349 ? 41.66100 8.07500   -44.26000 1.000 22.59882  ? 340 PHE B CB     1 
ATOM   5195 C CG     . PHE B 1 349 ? 43.03500 7.75800   -43.73800 1.000 24.93675  ? 340 PHE B CG     1 
ATOM   5196 C CD1    . PHE B 1 349 ? 44.16300 8.06100   -44.48100 1.000 22.52354  ? 340 PHE B CD1    1 
ATOM   5197 C CD2    . PHE B 1 349 ? 43.19700 7.16200   -42.49800 1.000 27.77075  ? 340 PHE B CD2    1 
ATOM   5198 C CE1    . PHE B 1 349 ? 45.42800 7.76800   -44.00000 1.000 29.18461  ? 340 PHE B CE1    1 
ATOM   5199 C CE2    . PHE B 1 349 ? 44.45800 6.86600   -42.01100 1.000 25.85344  ? 340 PHE B CE2    1 
ATOM   5200 C CZ     . PHE B 1 349 ? 45.57500 7.17000   -42.76200 1.000 25.99456  ? 340 PHE B CZ     1 
ATOM   5201 N N      . ILE B 1 350 ? 40.20200 9.48100   -46.97200 1.000 24.46905  ? 341 ILE B N      1 
ATOM   5202 C CA     . ILE B 1 350 ? 40.01700 9.46000   -48.42000 1.000 25.76584  ? 341 ILE B CA     1 
ATOM   5203 C C      . ILE B 1 350 ? 40.73600 10.63700  -49.06500 1.000 25.72551  ? 341 ILE B C      1 
ATOM   5204 O O      . ILE B 1 350 ? 41.47500 10.47500  -50.04300 1.000 22.23635  ? 341 ILE B O      1 
ATOM   5205 C CB     . ILE B 1 350 ? 38.51700 9.46500   -48.77200 1.000 24.90220  ? 341 ILE B CB     1 
ATOM   5206 C CG1    . ILE B 1 350 ? 37.86500 8.13700   -48.38900 1.000 26.94461  ? 341 ILE B CG1    1 
ATOM   5207 C CG2    . ILE B 1 350 ? 38.31700 9.75400   -50.25400 1.000 21.72226  ? 341 ILE B CG2    1 
ATOM   5208 C CD1    . ILE B 1 350 ? 36.36600 8.10200   -48.62900 1.000 27.04256  ? 341 ILE B CD1    1 
ATOM   5209 N N      . SER B 1 351 ? 40.53700 11.83600  -48.52400 1.000 24.96244  ? 342 SER B N      1 
ATOM   5210 C CA     . SER B 1 351 ? 41.06400 13.05000  -49.13000 1.000 25.16109  ? 342 SER B CA     1 
ATOM   5211 C C      . SER B 1 351 ? 42.41500 13.47500  -48.57200 1.000 25.44702  ? 342 SER B C      1 
ATOM   5212 O O      . SER B 1 351 ? 42.99600 14.44400  -49.07300 1.000 25.08112  ? 342 SER B O      1 
ATOM   5213 C CB     . SER B 1 351 ? 40.06600 14.19500  -48.96300 1.000 24.58877  ? 342 SER B CB     1 
ATOM   5214 O OG     . SER B 1 351 ? 39.68200 14.34300  -47.60700 1.000 25.97599  ? 342 SER B OG     1 
ATOM   5215 N N      . ASN B 1 352 ? 42.92800 12.78700  -47.55500 1.000 25.45263  ? 343 ASN B N      1 
ATOM   5216 C CA     . ASN B 1 352 ? 44.22100 13.11500  -46.95800 1.000 26.89953  ? 343 ASN B CA     1 
ATOM   5217 C C      . ASN B 1 352 ? 45.06000 11.84600  -46.91900 1.000 25.07237  ? 343 ASN B C      1 
ATOM   5218 O O      . ASN B 1 352 ? 45.02700 11.09700  -45.93300 1.000 24.60343  ? 343 ASN B O      1 
ATOM   5219 C CB     . ASN B 1 352 ? 44.05200 13.71800  -45.56600 1.000 26.27510  ? 343 ASN B CB     1 
ATOM   5220 C CG     . ASN B 1 352 ? 43.23200 14.99400  -45.58200 1.000 29.12408  ? 343 ASN B CG     1 
ATOM   5221 O OD1    . ASN B 1 352 ? 43.77700 16.09500  -45.67700 1.000 26.64314  ? 343 ASN B OD1    1 
ATOM   5222 N ND2    . ASN B 1 352 ? 41.91400 14.85200  -45.49400 1.000 23.21461  ? 343 ASN B ND2    1 
ATOM   5223 N N      . PRO B 1 353 ? 45.81900 11.56600  -47.98300 1.000 26.91815  ? 344 PRO B N      1 
ATOM   5224 C CA     . PRO B 1 353 ? 46.66400 10.36100  -47.97000 1.000 25.46272  ? 344 PRO B CA     1 
ATOM   5225 C C      . PRO B 1 353 ? 47.69100 10.37400  -46.85400 1.000 26.05034  ? 344 PRO B C      1 
ATOM   5226 O O      . PRO B 1 353 ? 47.99600 9.32000   -46.28200 1.000 24.89483  ? 344 PRO B O      1 
ATOM   5227 C CB     . PRO B 1 353 ? 47.31900 10.38100  -49.35900 1.000 27.84761  ? 344 PRO B CB     1 
ATOM   5228 C CG     . PRO B 1 353 ? 47.26900 11.81400  -49.78100 1.000 25.54801  ? 344 PRO B CG     1 
ATOM   5229 C CD     . PRO B 1 353 ? 45.98600 12.34800  -49.21900 1.000 27.97579  ? 344 PRO B CD     1 
ATOM   5230 N N      . ASP B 1 354 ? 48.22500 11.54300  -46.52400 1.000 24.97035  ? 345 ASP B N      1 
ATOM   5231 C CA     . ASP B 1 354 ? 49.13300 11.70400  -45.38800 1.000 27.30276  ? 345 ASP B CA     1 
ATOM   5232 C C      . ASP B 1 354 ? 48.38800 12.23100  -44.16800 1.000 29.26220  ? 345 ASP B C      1 
ATOM   5233 O O      . ASP B 1 354 ? 48.81000 13.19000  -43.52100 1.000 29.89065  ? 345 ASP B O      1 
ATOM   5234 C CB     . ASP B 1 354 ? 50.29100 12.61800  -45.76600 1.000 28.61379  ? 345 ASP B CB     1 
ATOM   5235 C CG     . ASP B 1 354 ? 49.83000 13.91100  -46.41100 1.000 33.81688  ? 345 ASP B CG     1 
ATOM   5236 O OD1    . ASP B 1 354 ? 48.60900 14.08000  -46.61400 1.000 32.06950  ? 345 ASP B OD1    1 
ATOM   5237 O OD2    . ASP B 1 354 ? 50.69300 14.75900  -46.71800 1.000 32.29256  ? 345 ASP B OD2    1 
ATOM   5238 N N      . LEU B 1 355 ? 47.25800 11.59400  -43.84800 1.000 27.12520  ? 346 LEU B N      1 
ATOM   5239 C CA     . LEU B 1 355 ? 46.44800 12.02900  -42.71400 1.000 26.83876  ? 346 LEU B CA     1 
ATOM   5240 C C      . LEU B 1 355 ? 47.19400 11.85700  -41.39800 1.000 26.26609  ? 346 LEU B C      1 
ATOM   5241 O O      . LEU B 1 355 ? 47.06800 12.69200  -40.49400 1.000 26.25946  ? 346 LEU B O      1 
ATOM   5242 C CB     . LEU B 1 355 ? 45.12800 11.25900  -42.68500 1.000 27.06715  ? 346 LEU B CB     1 
ATOM   5243 C CG     . LEU B 1 355 ? 44.18200 11.59600  -41.53100 1.000 26.28757  ? 346 LEU B CG     1 
ATOM   5244 C CD1    . LEU B 1 355 ? 43.73600 13.04900  -41.60900 1.000 20.58839  ? 346 LEU B CD1    1 
ATOM   5245 C CD2    . LEU B 1 355 ? 42.98500 10.66000  -41.52200 1.000 24.61183  ? 346 LEU B CD2    1 
ATOM   5246 N N      . VAL B 1 356 ? 47.96900 10.77700  -41.27000 1.000 26.75326  ? 347 VAL B N      1 
ATOM   5247 C CA     . VAL B 1 356 ? 48.77200 10.57700  -40.06600 1.000 32.14183  ? 347 VAL B CA     1 
ATOM   5248 C C      . VAL B 1 356 ? 49.74300 11.73500  -39.87700 1.000 32.50835  ? 347 VAL B C      1 
ATOM   5249 O O      . VAL B 1 356 ? 49.92000 12.24200  -38.76200 1.000 32.65231  ? 347 VAL B O      1 
ATOM   5250 C CB     . VAL B 1 356 ? 49.51000 9.22700   -40.13200 1.000 32.75815  ? 347 VAL B CB     1 
ATOM   5251 C CG1    . VAL B 1 356 ? 50.31900 8.99900   -38.86200 1.000 31.33171  ? 347 VAL B CG1    1 
ATOM   5252 C CG2    . VAL B 1 356 ? 48.52500 8.08900   -40.35700 1.000 27.51868  ? 347 VAL B CG2    1 
ATOM   5253 N N      . MET B 1 357 ? 50.37600 12.18200  -40.96300 1.000 25.84989  ? 348 MET B N      1 
ATOM   5254 C CA     . MET B 1 357 ? 51.31800 13.29200  -40.87000 1.000 30.30786  ? 348 MET B CA     1 
ATOM   5255 C C      . MET B 1 357 ? 50.60200 14.60100  -40.55900 1.000 30.26586  ? 348 MET B C      1 
ATOM   5256 O O      . MET B 1 357 ? 51.10800 15.42500  -39.78900 1.000 33.28712  ? 348 MET B O      1 
ATOM   5257 C CB     . MET B 1 357 ? 52.11000 13.41000  -42.17100 1.000 31.59793  ? 348 MET B CB     1 
ATOM   5258 C CG     . MET B 1 357 ? 53.30209 14.34741  -42.10690 1.000 42.43802  ? 348 MET B CG     1 
ATOM   5259 S SD     . MET B 1 357 ? 54.56202 13.79945  -40.93745 1.000 67.11330  ? 348 MET B SD     1 
ATOM   5260 C CE     . MET B 1 357 ? 54.62170 15.18917  -39.80946 1.000 48.29168  ? 348 MET B CE     1 
ATOM   5261 N N      . ARG B 1 358 ? 49.42500 14.81300  -41.15200 1.000 27.35988  ? 349 ARG B N      1 
ATOM   5262 C CA     . ARG B 1 358 ? 48.68300 16.04200  -40.89500 1.000 28.57189  ? 349 ARG B CA     1 
ATOM   5263 C C      . ARG B 1 358 ? 48.18000 16.10600  -39.45800 1.000 31.54841  ? 349 ARG B C      1 
ATOM   5264 O O      . ARG B 1 358 ? 48.08900 17.19700  -38.88500 1.000 31.08044  ? 349 ARG B O      1 
ATOM   5265 C CB     . ARG B 1 358 ? 47.51500 16.16600  -41.87400 1.000 28.76180  ? 349 ARG B CB     1 
ATOM   5266 C CG     . ARG B 1 358 ? 47.93300 16.33000  -43.33000 1.000 26.69247  ? 349 ARG B CG     1 
ATOM   5267 C CD     . ARG B 1 358 ? 46.72900 16.26000  -44.26000 1.000 27.14489  ? 349 ARG B CD     1 
ATOM   5268 N NE     . ARG B 1 358 ? 47.11100 16.28100  -45.66800 1.000 33.43370  ? 349 ARG B NE     1 
ATOM   5269 C CZ     . ARG B 1 358 ? 46.92100 17.30900  -46.48500 1.000 29.80024  ? 349 ARG B CZ     1 
ATOM   5270 N NH1    . ARG B 1 358 ? 46.34300 18.42500  -46.07000 1.000 28.48087  ? 349 ARG B NH1    1 
ATOM   5271 N NH2    . ARG B 1 358 ? 47.31300 17.21100  -47.75200 1.000 31.65220  ? 349 ARG B NH2    1 
ATOM   5272 N N      . ILE B 1 359 ? 47.85200 14.95900  -38.86100 1.000 28.37377  ? 350 ILE B N      1 
ATOM   5273 C CA     . ILE B 1 359 ? 47.42000 14.94800  -37.46800 1.000 32.59869  ? 350 ILE B CA     1 
ATOM   5274 C C      . ILE B 1 359 ? 48.58900 15.26700  -36.54000 1.000 33.75852  ? 350 ILE B C      1 
ATOM   5275 O O      . ILE B 1 359 ? 48.42200 15.95100  -35.52300 1.000 33.15478  ? 350 ILE B O      1 
ATOM   5276 C CB     . ILE B 1 359 ? 46.76200 13.59700  -37.12700 1.000 28.10773  ? 350 ILE B CB     1 
ATOM   5277 C CG1    . ILE B 1 359 ? 45.42000 13.46600  -37.85100 1.000 26.01462  ? 350 ILE B CG1    1 
ATOM   5278 C CG2    . ILE B 1 359 ? 46.56800 13.44500  -35.62600 1.000 33.70586  ? 350 ILE B CG2    1 
ATOM   5279 C CD1    . ILE B 1 359 ? 44.67000 12.19200  -37.52600 1.000 24.01099  ? 350 ILE B CD1    1 
ATOM   5280 N N      . LYS B 1 360 ? 49.79200 14.79400  -36.88000 1.000 32.76308  ? 351 LYS B N      1 
ATOM   5281 C CA     . LYS B 1 360 ? 50.95400 15.08200  -36.04200 1.000 40.05883  ? 351 LYS B CA     1 
ATOM   5282 C C      . LYS B 1 360 ? 51.31900 16.56000  -36.08800 1.000 36.73432  ? 351 LYS B C      1 
ATOM   5283 O O      . LYS B 1 360 ? 51.68300 17.14700  -35.06200 1.000 43.36535  ? 351 LYS B O      1 
ATOM   5284 C CB     . LYS B 1 360 ? 52.14500 14.22800  -36.47600 1.000 35.71844  ? 351 LYS B CB     1 
ATOM   5285 C CG     . LYS B 1 360 ? 53.38193 14.40370  -35.60576 1.000 35.73842  ? 351 LYS B CG     1 
ATOM   5286 C CD     . LYS B 1 360 ? 54.54523 13.57439  -36.12323 1.000 42.29221  ? 351 LYS B CD     1 
ATOM   5287 C CE     . LYS B 1 360 ? 54.21975 12.09045  -36.09604 1.000 54.10924  ? 351 LYS B CE     1 
ATOM   5288 N NZ     . LYS B 1 360 ? 54.35055 11.45620  -37.43910 1.000 64.59813  ? 351 LYS B NZ     1 
ATOM   5289 N N      . LEU B 1 361 ? 51.22700 17.17600  -37.26400 1.000 34.93500  ? 352 LEU B N      1 
ATOM   5290 C CA     . LEU B 1 361 ? 51.59400 18.57200  -37.44600 1.000 35.84718  ? 352 LEU B CA     1 
ATOM   5291 C C      . LEU B 1 361 ? 50.45300 19.53600  -37.15400 1.000 36.08668  ? 352 LEU B C      1 
ATOM   5292 O O      . LEU B 1 361 ? 50.68800 20.75000  -37.11900 1.000 35.15502  ? 352 LEU B O      1 
ATOM   5293 C CB     . LEU B 1 361 ? 52.08500 18.80200  -38.88200 1.000 29.11638  ? 352 LEU B CB     1 
ATOM   5294 C CG     . LEU B 1 361 ? 53.22900 17.91700  -39.37700 1.000 36.50770  ? 352 LEU B CG     1 
ATOM   5295 C CD1    . LEU B 1 361 ? 53.49700 18.17200  -40.85300 1.000 43.21911  ? 352 LEU B CD1    1 
ATOM   5296 C CD2    . LEU B 1 361 ? 54.48500 18.14700  -38.55100 1.000 33.89518  ? 352 LEU B CD2    1 
ATOM   5297 N N      . ASN B 1 362 ? 49.23800 19.02900  -36.93900 1.000 35.48668  ? 353 ASN B N      1 
ATOM   5298 C CA     . ASN B 1 362 ? 48.04200 19.86800  -36.86700 1.000 32.66018  ? 353 ASN B CA     1 
ATOM   5299 C C      . ASN B 1 362 ? 47.91100 20.70400  -38.13600 1.000 32.33916  ? 353 ASN B C      1 
ATOM   5300 O O      . ASN B 1 362 ? 47.63100 21.90300  -38.09600 1.000 33.82360  ? 353 ASN B O      1 
ATOM   5301 C CB     . ASN B 1 362 ? 48.05400 20.75300  -35.62000 1.000 33.38238  ? 353 ASN B CB     1 
ATOM   5302 C CG     . ASN B 1 362 ? 46.71300 21.39900  -35.35000 1.000 33.60321  ? 353 ASN B CG     1 
ATOM   5303 O OD1    . ASN B 1 362 ? 45.68100 20.96900  -35.87300 1.000 35.37571  ? 353 ASN B OD1    1 
ATOM   5304 N ND2    . ASN B 1 362 ? 46.71700 22.43300  -34.52100 1.000 38.42863  ? 353 ASN B ND2    1 
ATOM   5305 N N      . ALA B 1 363 ? 48.14700 20.06200  -39.27300 1.000 29.26238  ? 354 ALA B N      1 
ATOM   5306 C CA     . ALA B 1 363 ? 48.05900 20.72900  -40.55600 1.000 29.91852  ? 354 ALA B CA     1 
ATOM   5307 C C      . ALA B 1 363 ? 46.62000 20.69100  -41.06400 1.000 33.35136  ? 354 ALA B C      1 
ATOM   5308 O O      . ALA B 1 363 ? 45.85300 19.79400  -40.70600 1.000 34.57802  ? 354 ALA B O      1 
ATOM   5309 C CB     . ALA B 1 363 ? 48.99000 20.06400  -41.56700 1.000 27.19145  ? 354 ALA B CB     1 
ATOM   5310 N N      . PRO B 1 364 ? 46.22500 21.66700  -41.88100 1.000 31.89156  ? 355 PRO B N      1 
ATOM   5311 C CA     . PRO B 1 364 ? 44.85300 21.67700  -42.39800 1.000 25.64830  ? 355 PRO B CA     1 
ATOM   5312 C C      . PRO B 1 364 ? 44.58500 20.47500  -43.29200 1.000 26.94769  ? 355 PRO B C      1 
ATOM   5313 O O      . PRO B 1 364 ? 45.48700 19.93300  -43.93500 1.000 31.44279  ? 355 PRO B O      1 
ATOM   5314 C CB     . PRO B 1 364 ? 44.77900 22.99100  -43.18200 1.000 33.85041  ? 355 PRO B CB     1 
ATOM   5315 C CG     . PRO B 1 364 ? 46.20300 23.32900  -43.49600 1.000 31.38384  ? 355 PRO B CG     1 
ATOM   5316 C CD     . PRO B 1 364 ? 46.99900 22.83600  -42.33200 1.000 25.89678  ? 355 PRO B CD     1 
ATOM   5317 N N      . LEU B 1 365 ? 43.32200 20.06300  -43.32800 1.000 24.38714  ? 356 LEU B N      1 
ATOM   5318 C CA     . LEU B 1 365 ? 42.90800 18.84500  -44.00400 1.000 26.83084  ? 356 LEU B CA     1 
ATOM   5319 C C      . LEU B 1 365 ? 42.18600 19.17100  -45.30600 1.000 30.29001  ? 356 LEU B C      1 
ATOM   5320 O O      . LEU B 1 365 ? 41.59400 20.24400  -45.45800 1.000 29.24300  ? 356 LEU B O      1 
ATOM   5321 C CB     . LEU B 1 365 ? 41.99800 18.00700  -43.10000 1.000 27.97059  ? 356 LEU B CB     1 
ATOM   5322 C CG     . LEU B 1 365 ? 42.49000 17.78900  -41.66500 1.000 25.75810  ? 356 LEU B CG     1 
ATOM   5323 C CD1    . LEU B 1 365 ? 41.48100 16.98000  -40.86400 1.000 30.19225  ? 356 LEU B CD1    1 
ATOM   5324 C CD2    . LEU B 1 365 ? 43.84900 17.11200  -41.65400 1.000 27.24087  ? 356 LEU B CD2    1 
ATOM   5325 N N      . ASN B 1 366 ? 42.23900 18.22900  -46.24300 1.000 22.85733  ? 357 ASN B N      1 
ATOM   5326 C CA     . ASN B 1 366 ? 41.57800 18.37700  -47.53100 1.000 23.66696  ? 357 ASN B CA     1 
ATOM   5327 C C      . ASN B 1 366 ? 40.13000 17.91100  -47.44800 1.000 26.98084  ? 357 ASN B C      1 
ATOM   5328 O O      . ASN B 1 366 ? 39.79000 17.00500  -46.68300 1.000 25.77207  ? 357 ASN B O      1 
ATOM   5329 C CB     . ASN B 1 366 ? 42.30200 17.57700  -48.61500 1.000 25.58769  ? 357 ASN B CB     1 
ATOM   5330 C CG     . ASN B 1 366 ? 43.74800 17.98500  -48.77600 1.000 28.37020  ? 357 ASN B CG     1 
ATOM   5331 O OD1    . ASN B 1 366 ? 44.11500 19.13300  -48.52800 1.000 34.33910  ? 357 ASN B OD1    1 
ATOM   5332 N ND2    . ASN B 1 366 ? 44.58200 17.04200  -49.19900 1.000 26.74869  ? 357 ASN B ND2    1 
ATOM   5333 N N      . LYS B 1 367 ? 39.27900 18.53700  -48.25400 1.000 25.85695  ? 358 LYS B N      1 
ATOM   5334 C CA     . LYS B 1 367 ? 37.89400 18.11000  -48.36100 1.000 30.06657  ? 358 LYS B CA     1 
ATOM   5335 C C      . LYS B 1 367 ? 37.79200 16.86600  -49.23500 1.000 28.20789  ? 358 LYS B C      1 
ATOM   5336 O O      . LYS B 1 367 ? 38.55300 16.68500  -50.19000 1.000 32.68593  ? 358 LYS B O      1 
ATOM   5337 C CB     . LYS B 1 367 ? 37.02300 19.22900  -48.93700 1.000 29.45013  ? 358 LYS B CB     1 
ATOM   5338 C CG     . LYS B 1 367 ? 37.27200 19.53000  -50.41000 1.000 35.82319  ? 358 LYS B CG     1 
ATOM   5339 C CD     . LYS B 1 367 ? 36.51900 20.77200  -50.86400 1.000 48.20223  ? 358 LYS B CD     1 
ATOM   5340 C CE     . LYS B 1 367 ? 35.02300 20.64300  -50.61700 1.000 51.80299  ? 358 LYS B CE     1 
ATOM   5341 N NZ     . LYS B 1 367 ? 34.29000 21.87500  -51.02700 1.000 51.75872  ? 358 LYS B NZ     1 
ATOM   5342 N N      . TYR B 1 368 ? 36.84600 15.99900  -48.89300 1.000 28.92754  ? 359 TYR B N      1 
ATOM   5343 C CA     . TYR B 1 368 ? 36.58400 14.79700  -49.66600 1.000 28.06143  ? 359 TYR B CA     1 
ATOM   5344 C C      . TYR B 1 368 ? 35.37500 15.00900  -50.56700 1.000 31.63389  ? 359 TYR B C      1 
ATOM   5345 O O      . TYR B 1 368 ? 34.46300 15.77600  -50.24600 1.000 30.01091  ? 359 TYR B O      1 
ATOM   5346 C CB     . TYR B 1 368 ? 36.35800 13.58900  -48.75200 1.000 24.63312  ? 359 TYR B CB     1 
ATOM   5347 C CG     . TYR B 1 368 ? 35.44500 13.85700  -47.57700 1.000 29.56945  ? 359 TYR B CG     1 
ATOM   5348 C CD1    . TYR B 1 368 ? 34.06300 13.80400  -47.71900 1.000 27.16043  ? 359 TYR B CD1    1 
ATOM   5349 C CD2    . TYR B 1 368 ? 35.96400 14.15100  -46.32300 1.000 31.67310  ? 359 TYR B CD2    1 
ATOM   5350 C CE1    . TYR B 1 368 ? 33.22700 14.04600  -46.64700 1.000 26.97754  ? 359 TYR B CE1    1 
ATOM   5351 C CE2    . TYR B 1 368 ? 35.13600 14.39300  -45.24500 1.000 27.87000  ? 359 TYR B CE2    1 
ATOM   5352 C CZ     . TYR B 1 368 ? 33.76800 14.33900  -45.41200 1.000 29.25613  ? 359 TYR B CZ     1 
ATOM   5353 O OH     . TYR B 1 368 ? 32.93900 14.57800  -44.34000 1.000 41.68993  ? 359 TYR B OH     1 
ATOM   5354 N N      . ASN B 1 369 ? 35.38100 14.32100  -51.70800 1.000 27.86666  ? 360 ASN B N      1 
ATOM   5355 C CA     . ASN B 1 369 ? 34.32800 14.43200  -52.71300 1.000 32.30691  ? 360 ASN B CA     1 
ATOM   5356 C C      . ASN B 1 369 ? 33.48400 13.16400  -52.67400 1.000 28.72353  ? 360 ASN B C      1 
ATOM   5357 O O      . ASN B 1 369 ? 33.94700 12.09000  -53.07400 1.000 31.58646  ? 360 ASN B O      1 
ATOM   5358 C CB     . ASN B 1 369 ? 34.92400 14.65200  -54.10100 1.000 31.38400  ? 360 ASN B CB     1 
ATOM   5359 C CG     . ASN B 1 369 ? 35.68972 15.95312  -54.20230 1.000 37.52999  ? 360 ASN B CG     1 
ATOM   5360 O OD1    . ASN B 1 369 ? 36.78744 15.99900  -54.75777 1.000 50.85044  ? 360 ASN B OD1    1 
ATOM   5361 N ND2    . ASN B 1 369 ? 35.10720 17.02382  -53.67409 1.000 43.76271  ? 360 ASN B ND2    1 
ATOM   5362 N N      . ARG B 1 370 ? 32.24300 13.29500  -52.19800 1.000 30.36233  ? 361 ARG B N      1 
ATOM   5363 C CA     . ARG B 1 370 ? 31.35700 12.14000  -52.10600 1.000 35.25626  ? 361 ARG B CA     1 
ATOM   5364 C C      . ARG B 1 370 ? 31.05600 11.54700  -53.47700 1.000 28.54626  ? 361 ARG B C      1 
ATOM   5365 O O      . ARG B 1 370 ? 30.83000 10.33600  -53.59100 1.000 31.18044  ? 361 ARG B O      1 
ATOM   5366 C CB     . ARG B 1 370 ? 30.06200 12.53600  -51.39200 1.000 35.23765  ? 361 ARG B CB     1 
ATOM   5367 C CG     . ARG B 1 370 ? 28.99200 11.45400  -51.37200 1.000 36.98871  ? 361 ARG B CG     1 
ATOM   5368 C CD     . ARG B 1 370 ? 27.87900 11.78500  -50.39000 1.000 45.99908  ? 361 ARG B CD     1 
ATOM   5369 N NE     . ARG B 1 370 ? 28.34000 11.73200  -49.00700 1.000 49.85432  ? 361 ARG B NE     1 
ATOM   5370 C CZ     . ARG B 1 370 ? 28.37000 10.62900  -48.27000 1.000 57.76827  ? 361 ARG B CZ     1 
ATOM   5371 N NH1    . ARG B 1 370 ? 27.97400 9.46300   -48.75400 1.000 55.75148  ? 361 ARG B NH1    1 
ATOM   5372 N NH2    . ARG B 1 370 ? 28.81000 10.69900  -47.01600 1.000 43.65039  ? 361 ARG B NH2    1 
ATOM   5373 N N      . LYS B 1 371 ? 31.06800 12.37400  -54.52700 1.000 27.76979  ? 362 LYS B N      1 
ATOM   5374 C CA     . LYS B 1 371 ? 30.71900 11.89700  -55.86300 1.000 30.39214  ? 362 LYS B CA     1 
ATOM   5375 C C      . LYS B 1 371 ? 31.61800 10.74900  -56.30600 1.000 27.27567  ? 362 LYS B C      1 
ATOM   5376 O O      . LYS B 1 371 ? 31.15200 9.79700   -56.94200 1.000 28.00790  ? 362 LYS B O      1 
ATOM   5377 C CB     . LYS B 1 371 ? 30.79400 13.04400  -56.87100 1.000 33.29377  ? 362 LYS B CB     1 
ATOM   5378 C CG     . LYS B 1 371 ? 29.61000 13.99300  -56.84000 1.000 38.49885  ? 362 LYS B CG     1 
ATOM   5379 C CD     . LYS B 1 371 ? 29.67500 14.96900  -58.00600 1.000 44.41537  ? 362 LYS B CD     1 
ATOM   5380 C CE     . LYS B 1 371 ? 28.41100 15.80500  -58.10700 1.000 53.03515  ? 362 LYS B CE     1 
ATOM   5381 N NZ     . LYS B 1 371 ? 28.42500 16.67800  -59.31400 1.000 55.73202  ? 362 LYS B NZ     1 
ATOM   5382 N N      . THR B 1 372 ? 32.91000 10.81900  -55.98500 1.000 27.08183  ? 363 THR B N      1 
ATOM   5383 C CA     . THR B 1 372 ? 33.86600 9.80500   -56.40600 1.000 25.60755  ? 363 THR B CA     1 
ATOM   5384 C C      . THR B 1 372 ? 34.15800 8.78000   -55.31200 1.000 24.64817  ? 363 THR B C      1 
ATOM   5385 O O      . THR B 1 372 ? 35.22000 8.15000   -55.33100 1.000 29.60447  ? 363 THR B O      1 
ATOM   5386 C CB     . THR B 1 372 ? 35.16500 10.46400  -56.88000 1.000 25.68715  ? 363 THR B CB     1 
ATOM   5387 O OG1    . THR B 1 372 ? 35.69400 11.29800  -55.84300 1.000 31.71197  ? 363 THR B OG1    1 
ATOM   5388 C CG2    . THR B 1 372 ? 34.90900 11.31000  -58.12000 1.000 26.22123  ? 363 THR B CG2    1 
ATOM   5389 N N      . PHE B 1 373 ? 33.23400 8.59400   -54.36400 1.000 26.17815  ? 364 PHE B N      1 
ATOM   5390 C CA     . PHE B 1 373 ? 33.42500 7.56500   -53.34400 1.000 23.64303  ? 364 PHE B CA     1 
ATOM   5391 C C      . PHE B 1 373 ? 33.37900 6.16800   -53.94800 1.000 27.80421  ? 364 PHE B C      1 
ATOM   5392 O O      . PHE B 1 373 ? 34.19900 5.30900   -53.60200 1.000 24.84934  ? 364 PHE B O      1 
ATOM   5393 C CB     . PHE B 1 373 ? 32.36600 7.69000   -52.24800 1.000 25.80402  ? 364 PHE B CB     1 
ATOM   5394 C CG     . PHE B 1 373 ? 32.69000 8.71000   -51.19500 1.000 29.64795  ? 364 PHE B CG     1 
ATOM   5395 C CD1    . PHE B 1 373 ? 33.86500 9.44000   -51.25300 1.000 29.65814  ? 364 PHE B CD1    1 
ATOM   5396 C CD2    . PHE B 1 373 ? 31.82200 8.92900   -50.13800 1.000 29.92096  ? 364 PHE B CD2    1 
ATOM   5397 C CE1    . PHE B 1 373 ? 34.16300 10.37700  -50.28200 1.000 32.36028  ? 364 PHE B CE1    1 
ATOM   5398 C CE2    . PHE B 1 373 ? 32.11400 9.86300   -49.16300 1.000 29.08340  ? 364 PHE B CE2    1 
ATOM   5399 C CZ     . PHE B 1 373 ? 33.28600 10.58800  -49.23600 1.000 33.44189  ? 364 PHE B CZ     1 
ATOM   5400 N N      . TYR B 1 374 ? 32.42700 5.92000   -54.85100 1.000 21.86798  ? 365 TYR B N      1 
ATOM   5401 C CA     . TYR B 1 374 ? 32.18100 4.58300   -55.37600 1.000 20.94245  ? 365 TYR B CA     1 
ATOM   5402 C C      . TYR B 1 374 ? 32.33200 4.51200   -56.89300 1.000 23.49152  ? 365 TYR B C      1 
ATOM   5403 O O      . TYR B 1 374 ? 31.78300 3.60200   -57.52200 1.000 23.77552  ? 365 TYR B O      1 
ATOM   5404 C CB     . TYR B 1 374 ? 30.78900 4.09900   -54.96400 1.000 24.84908  ? 365 TYR B CB     1 
ATOM   5405 C CG     . TYR B 1 374 ? 30.49400 4.25900   -53.48900 1.000 24.17820  ? 365 TYR B CG     1 
ATOM   5406 C CD1    . TYR B 1 374 ? 31.12500 3.46000   -52.54400 1.000 24.22828  ? 365 TYR B CD1    1 
ATOM   5407 C CD2    . TYR B 1 374 ? 29.58000 5.20500   -53.04200 1.000 26.51564  ? 365 TYR B CD2    1 
ATOM   5408 C CE1    . TYR B 1 374 ? 30.85800 3.60100   -51.19500 1.000 27.91533  ? 365 TYR B CE1    1 
ATOM   5409 C CE2    . TYR B 1 374 ? 29.30500 5.35300   -51.69300 1.000 23.36363  ? 365 TYR B CE2    1 
ATOM   5410 C CZ     . TYR B 1 374 ? 29.94700 4.54800   -50.77500 1.000 33.17382  ? 365 TYR B CZ     1 
ATOM   5411 O OH     . TYR B 1 374 ? 29.67800 4.68900   -49.43200 1.000 30.71836  ? 365 TYR B OH     1 
ATOM   5412 N N      . THR B 1 375 ? 33.06000 5.44800   -57.49500 1.000 25.58993  ? 366 THR B N      1 
ATOM   5413 C CA     . THR B 1 375 ? 33.30900 5.39500   -58.92700 1.000 24.44285  ? 366 THR B CA     1 
ATOM   5414 C C      . THR B 1 375 ? 34.44400 4.41300   -59.22100 1.000 30.09119  ? 366 THR B C      1 
ATOM   5415 O O      . THR B 1 375 ? 35.05800 3.84000   -58.31700 1.000 23.28608  ? 366 THR B O      1 
ATOM   5416 C CB     . THR B 1 375 ? 33.61200 6.78900   -59.46900 1.000 26.06631  ? 366 THR B CB     1 
ATOM   5417 O OG1    . THR B 1 375 ? 34.58400 7.43000   -58.63500 1.000 28.31509  ? 366 THR B OG1    1 
ATOM   5418 C CG2    . THR B 1 375 ? 32.34300 7.63000   -59.50300 1.000 24.05248  ? 366 THR B CG2    1 
ATOM   5419 N N      . GLN B 1 376 ? 34.72900 4.21000   -60.50800 1.000 24.32729  ? 367 GLN B N      1 
ATOM   5420 C CA     . GLN B 1 376 ? 35.64700 3.16200   -60.93400 1.000 26.34626  ? 367 GLN B CA     1 
ATOM   5421 C C      . GLN B 1 376 ? 36.97500 3.67600   -61.47200 1.000 28.02787  ? 367 GLN B C      1 
ATOM   5422 O O      . GLN B 1 376 ? 37.85600 2.86100   -61.76600 1.000 33.12132  ? 367 GLN B O      1 
ATOM   5423 C CB     . GLN B 1 376 ? 34.98700 2.27700   -62.00400 1.000 25.63007  ? 367 GLN B CB     1 
ATOM   5424 C CG     . GLN B 1 376 ? 34.04200 1.21900   -61.45100 1.000 24.69863  ? 367 GLN B CG     1 
ATOM   5425 C CD     . GLN B 1 376 ? 32.87500 1.81400   -60.68600 1.000 25.76994  ? 367 GLN B CD     1 
ATOM   5426 O OE1    . GLN B 1 376 ? 32.02600 2.50000   -61.25700 1.000 27.35175  ? 367 GLN B OE1    1 
ATOM   5427 N NE2    . GLN B 1 376 ? 32.83300 1.56200   -59.38300 1.000 22.25624  ? 367 GLN B NE2    1 
ATOM   5428 N N      . ASP B 1 377 ? 37.14600 4.98300   -61.61000 1.000 24.42174  ? 368 ASP B N      1 
ATOM   5429 C CA     . ASP B 1 377 ? 38.38100 5.50400   -62.18100 1.000 26.69565  ? 368 ASP B CA     1 
ATOM   5430 C C      . ASP B 1 377 ? 39.54300 5.23500   -61.23000 1.000 29.41210  ? 368 ASP B C      1 
ATOM   5431 O O      . ASP B 1 377 ? 39.43800 5.52100   -60.03100 1.000 28.59483  ? 368 ASP B O      1 
ATOM   5432 C CB     . ASP B 1 377 ? 38.25400 6.99800   -62.46700 1.000 29.22645  ? 368 ASP B CB     1 
ATOM   5433 C CG     . ASP B 1 377 ? 39.36900 7.51800   -63.35800 1.000 27.96929  ? 368 ASP B CG     1 
ATOM   5434 O OD1    . ASP B 1 377 ? 40.53900 7.52400   -62.91800 1.000 27.00705  ? 368 ASP B OD1    1 
ATOM   5435 O OD2    . ASP B 1 377 ? 39.07500 7.90700   -64.50800 1.000 29.27259  ? 368 ASP B OD2    1 
ATOM   5436 N N      . PRO B 1 378 ? 40.65800 4.68300   -61.71700 1.000 26.63013  ? 369 PRO B N      1 
ATOM   5437 C CA     . PRO B 1 378 ? 41.77700 4.34800   -60.82300 1.000 27.56844  ? 369 PRO B CA     1 
ATOM   5438 C C      . PRO B 1 378 ? 42.54300 5.55000   -60.29500 1.000 28.55455  ? 369 PRO B C      1 
ATOM   5439 O O      . PRO B 1 378 ? 43.45700 5.36400   -59.48400 1.000 31.77953  ? 369 PRO B O      1 
ATOM   5440 C CB     . PRO B 1 378 ? 42.67600 3.47400   -61.71100 1.000 25.44350  ? 369 PRO B CB     1 
ATOM   5441 C CG     . PRO B 1 378 ? 42.37000 3.91700   -63.10300 1.000 24.58781  ? 369 PRO B CG     1 
ATOM   5442 C CD     . PRO B 1 378 ? 40.90700 4.25700   -63.10600 1.000 23.45797  ? 369 PRO B CD     1 
ATOM   5443 N N      . VAL B 1 379 ? 42.21000 6.77100   -60.71400 1.000 28.46757  ? 370 VAL B N      1 
ATOM   5444 C CA     . VAL B 1 379 ? 42.95800 7.95100   -60.29200 1.000 28.53036  ? 370 VAL B CA     1 
ATOM   5445 C C      . VAL B 1 379 ? 42.01400 9.01700   -59.74800 1.000 28.53393  ? 370 VAL B C      1 
ATOM   5446 O O      . VAL B 1 379 ? 42.18900 9.49500   -58.62100 1.000 29.52669  ? 370 VAL B O      1 
ATOM   5447 C CB     . VAL B 1 379 ? 43.80300 8.51300   -61.45100 1.000 28.45582  ? 370 VAL B CB     1 
ATOM   5448 C CG1    . VAL B 1 379 ? 44.41300 9.85100   -61.06100 1.000 23.01923  ? 370 VAL B CG1    1 
ATOM   5449 C CG2    . VAL B 1 379 ? 44.89200 7.52500   -61.84400 1.000 26.54242  ? 370 VAL B CG2    1 
ATOM   5450 N N      . VAL B 1 380 ? 41.01300 9.39500   -60.54400 1.000 25.61780  ? 371 VAL B N      1 
ATOM   5451 C CA     . VAL B 1 380 ? 40.14900 10.52000  -60.19400 1.000 28.27584  ? 371 VAL B CA     1 
ATOM   5452 C C      . VAL B 1 380 ? 39.37000 10.18900  -58.93000 1.000 26.61919  ? 371 VAL B C      1 
ATOM   5453 O O      . VAL B 1 380 ? 38.63000 9.20000   -58.87800 1.000 27.69240  ? 371 VAL B O      1 
ATOM   5454 C CB     . VAL B 1 380 ? 39.21300 10.86300  -61.35700 1.000 30.31546  ? 371 VAL B CB     1 
ATOM   5455 C CG1    . VAL B 1 380 ? 38.30100 12.02200  -60.98200 1.000 21.37413  ? 371 VAL B CG1    1 
ATOM   5456 C CG2    . VAL B 1 380 ? 40.02000 11.19400  -62.60600 1.000 27.54910  ? 371 VAL B CG2    1 
ATOM   5457 N N      . GLY B 1 381 ? 39.53100 11.02300  -57.90300 1.000 24.81741  ? 372 GLY B N      1 
ATOM   5458 C CA     . GLY B 1 381 ? 38.87700 10.79200  -56.63100 1.000 26.89696  ? 372 GLY B CA     1 
ATOM   5459 C C      . GLY B 1 381 ? 39.36900 9.58500   -55.87100 1.000 28.70686  ? 372 GLY B C      1 
ATOM   5460 O O      . GLY B 1 381 ? 38.71200 9.16100   -54.91500 1.000 27.04547  ? 372 GLY B O      1 
ATOM   5461 N N      . TYR B 1 382 ? 40.50600 9.01300   -56.26300 1.000 30.39730  ? 373 TYR B N      1 
ATOM   5462 C CA     . TYR B 1 382 ? 41.04300 7.82900   -55.60600 1.000 28.34778  ? 373 TYR B CA     1 
ATOM   5463 C C      . TYR B 1 382 ? 42.46900 8.05400   -55.12200 1.000 27.56033  ? 373 TYR B C      1 
ATOM   5464 O O      . TYR B 1 382 ? 42.72200 7.98000   -53.91500 1.000 30.64482  ? 373 TYR B O      1 
ATOM   5465 C CB     . TYR B 1 382 ? 40.96200 6.63000   -56.56100 1.000 24.57123  ? 373 TYR B CB     1 
ATOM   5466 C CG     . TYR B 1 382 ? 41.16000 5.28800   -55.89400 1.000 26.96925  ? 373 TYR B CG     1 
ATOM   5467 C CD1    . TYR B 1 382 ? 40.41300 4.92700   -54.77900 1.000 23.43478  ? 373 TYR B CD1    1 
ATOM   5468 C CD2    . TYR B 1 382 ? 42.08100 4.37500   -56.38900 1.000 24.19566  ? 373 TYR B CD2    1 
ATOM   5469 C CE1    . TYR B 1 382 ? 40.58900 3.69800   -54.16800 1.000 27.95143  ? 373 TYR B CE1    1 
ATOM   5470 C CE2    . TYR B 1 382 ? 42.26200 3.14500   -55.78900 1.000 22.45743  ? 373 TYR B CE2    1 
ATOM   5471 C CZ     . TYR B 1 382 ? 41.51500 2.81100   -54.67900 1.000 27.54908  ? 373 TYR B CZ     1 
ATOM   5472 O OH     . TYR B 1 382 ? 41.69800 1.58600   -54.07900 1.000 25.73812  ? 373 TYR B OH     1 
ATOM   5473 N N      . THR B 1 383 ? 43.40800 8.34400   -56.02200 1.000 24.72029  ? 374 THR B N      1 
ATOM   5474 C CA     . THR B 1 383 ? 44.79700 8.58200   -55.64800 1.000 27.07364  ? 374 THR B CA     1 
ATOM   5475 C C      . THR B 1 383 ? 45.27500 9.98500   -56.00100 1.000 25.99037  ? 374 THR B C      1 
ATOM   5476 O O      . THR B 1 383 ? 46.46700 10.27500  -55.84800 1.000 26.04863  ? 374 THR B O      1 
ATOM   5477 C CB     . THR B 1 383 ? 45.71500 7.54900   -56.30800 1.000 27.14611  ? 374 THR B CB     1 
ATOM   5478 O OG1    . THR B 1 383 ? 45.57000 7.61900   -57.73200 1.000 27.42910  ? 374 THR B OG1    1 
ATOM   5479 C CG2    . THR B 1 383 ? 45.37000 6.14400   -55.83500 1.000 26.31311  ? 374 THR B CG2    1 
ATOM   5480 N N      . ASP B 1 384 ? 44.38800 10.86300  -56.46900 1.000 24.24959  ? 375 ASP B N      1 
ATOM   5481 C CA     . ASP B 1 384 ? 44.77700 12.20300  -56.88500 1.000 24.99154  ? 375 ASP B CA     1 
ATOM   5482 C C      . ASP B 1 384 ? 44.48200 13.26200  -55.82800 1.000 28.75796  ? 375 ASP B C      1 
ATOM   5483 O O      . ASP B 1 384 ? 44.51900 14.45700  -56.13600 1.000 23.44639  ? 375 ASP B O      1 
ATOM   5484 C CB     . ASP B 1 384 ? 44.09900 12.56700  -58.20900 1.000 28.98265  ? 375 ASP B CB     1 
ATOM   5485 C CG     . ASP B 1 384 ? 42.58800 12.63300  -58.10000 1.000 34.41114  ? 375 ASP B CG     1 
ATOM   5486 O OD1    . ASP B 1 384 ? 42.02800 12.10300  -57.11700 1.000 31.75419  ? 375 ASP B OD1    1 
ATOM   5487 O OD2    . ASP B 1 384 ? 41.95800 13.21200  -59.01200 1.000 38.04239  ? 375 ASP B OD2    1 
ATOM   5488 N N      . TYR B 1 385 ? 44.18900 12.85600  -54.60100 1.000 26.34516  ? 376 TYR B N      1 
ATOM   5489 C CA     . TYR B 1 385 ? 44.11900 13.81500  -53.50700 1.000 25.49598  ? 376 TYR B CA     1 
ATOM   5490 C C      . TYR B 1 385 ? 45.53400 14.21700  -53.10800 1.000 27.61770  ? 376 TYR B C      1 
ATOM   5491 O O      . TYR B 1 385 ? 46.37500 13.34400  -52.85900 1.000 27.14091  ? 376 TYR B O      1 
ATOM   5492 C CB     . TYR B 1 385 ? 43.37400 13.22600  -52.31400 1.000 23.49086  ? 376 TYR B CB     1 
ATOM   5493 C CG     . TYR B 1 385 ? 41.87100 13.15600  -52.49200 1.000 24.91435  ? 376 TYR B CG     1 
ATOM   5494 C CD1    . TYR B 1 385 ? 41.08400 14.29500  -52.36700 1.000 21.25282  ? 376 TYR B CD1    1 
ATOM   5495 C CD2    . TYR B 1 385 ? 41.23800 11.95100  -52.77100 1.000 20.27666  ? 376 TYR B CD2    1 
ATOM   5496 C CE1    . TYR B 1 385 ? 39.71000 14.23500  -52.52000 1.000 24.73737  ? 376 TYR B CE1    1 
ATOM   5497 C CE2    . TYR B 1 385 ? 39.86700 11.88100  -52.92600 1.000 22.76852  ? 376 TYR B CE2    1 
ATOM   5498 C CZ     . TYR B 1 385 ? 39.10700 13.02600  -52.80000 1.000 24.28515  ? 376 TYR B CZ     1 
ATOM   5499 O OH     . TYR B 1 385 ? 37.74100 12.95900  -52.95500 1.000 26.08791  ? 376 TYR B OH     1 
ATOM   5500 N N      . PRO B 1 386 ? 45.83900 15.51000  -53.03800 1.000 30.81814  ? 377 PRO B N      1 
ATOM   5501 C CA     . PRO B 1 386 ? 47.23700 15.93000  -52.89400 1.000 27.85765  ? 377 PRO B CA     1 
ATOM   5502 C C      . PRO B 1 386 ? 47.78600 15.67300  -51.50000 1.000 30.75555  ? 377 PRO B C      1 
ATOM   5503 O O      . PRO B 1 386 ? 47.05500 15.64900  -50.50700 1.000 30.74767  ? 377 PRO B O      1 
ATOM   5504 C CB     . PRO B 1 386 ? 47.18600 17.43200  -53.19700 1.000 29.32088  ? 377 PRO B CB     1 
ATOM   5505 C CG     . PRO B 1 386 ? 45.80300 17.83500  -52.80600 1.000 31.08931  ? 377 PRO B CG     1 
ATOM   5506 C CD     . PRO B 1 386 ? 44.92200 16.65800  -53.13900 1.000 26.66982  ? 377 PRO B CD     1 
ATOM   5507 N N      . PHE B 1 387 ? 49.10000 15.47700  -51.44300 1.000 37.11419  ? 378 PHE B N      1 
ATOM   5508 C CA     . PHE B 1 387 ? 49.81300 15.38900  -50.18100 1.000 33.94641  ? 378 PHE B CA     1 
ATOM   5509 C C      . PHE B 1 387 ? 50.05900 16.78500  -49.61500 1.000 36.01609  ? 378 PHE B C      1 
ATOM   5510 O O      . PHE B 1 387 ? 49.83800 17.80600  -50.27400 1.000 34.22092  ? 378 PHE B O      1 
ATOM   5511 C CB     . PHE B 1 387 ? 51.14100 14.65200  -50.35900 1.000 34.53613  ? 378 PHE B CB     1 
ATOM   5512 C CG     . PHE B 1 387 ? 51.00500 13.15900  -50.45200 1.000 35.12257  ? 378 PHE B CG     1 
ATOM   5513 C CD1    . PHE B 1 387 ? 50.72800 12.54700  -51.66400 1.000 32.82039  ? 378 PHE B CD1    1 
ATOM   5514 C CD2    . PHE B 1 387 ? 51.16700 12.36600  -49.32700 1.000 33.81365  ? 378 PHE B CD2    1 
ATOM   5515 C CE1    . PHE B 1 387 ? 50.60700 11.17100  -51.75100 1.000 28.74830  ? 378 PHE B CE1    1 
ATOM   5516 C CE2    . PHE B 1 387 ? 51.04700 10.99000  -49.40600 1.000 30.37619  ? 378 PHE B CE2    1 
ATOM   5517 C CZ     . PHE B 1 387 ? 50.76700 10.39200  -50.62000 1.000 32.94150  ? 378 PHE B CZ     1 
ATOM   5518 N N      . LEU B 1 388 ? 50.53000 16.82100  -48.37400 1.000 35.02892  ? 379 LEU B N      1 
ATOM   5519 C CA     . LEU B 1 388 ? 50.82800 18.07900  -47.70000 1.000 35.23626  ? 379 LEU B CA     1 
ATOM   5520 C C      . LEU B 1 388 ? 52.07900 18.73100  -48.28100 1.000 40.52818  ? 379 LEU B C      1 
ATOM   5521 O O      . LEU B 1 388 ? 52.00400 19.50300  -49.23800 1.000 39.13238  ? 379 LEU B O      1 
ATOM   5522 C CB     . LEU B 1 388 ? 51.00500 17.84800  -46.20000 1.000 40.01701  ? 379 LEU B CB     1 
ATOM   5523 C CG     . LEU B 1 388 ? 51.05700 19.08400  -45.30500 1.000 38.80025  ? 379 LEU B CG     1 
ATOM   5524 C CD1    . LEU B 1 388 ? 49.71100 19.78800  -45.29200 1.000 34.56181  ? 379 LEU B CD1    1 
ATOM   5525 C CD2    . LEU B 1 388 ? 51.47800 18.69100  -43.90300 1.000 35.38581  ? 379 LEU B CD2    1 
HETATM 5526 N N1     . FMN C 2 .   ? 22.15400 -4.93700  0.55500   1.000 22.65450  ? 401 FMN A N1     1 
HETATM 5527 C C2     . FMN C 2 .   ? 21.92800 -3.58200  0.43200   1.000 25.11310  ? 401 FMN A C2     1 
HETATM 5528 O O2     . FMN C 2 .   ? 21.66100 -2.91400  1.43000   1.000 23.69265  ? 401 FMN A O2     1 
HETATM 5529 N N3     . FMN C 2 .   ? 21.99800 -2.97300  -0.80500  1.000 22.63467  ? 401 FMN A N3     1 
HETATM 5530 C C4     . FMN C 2 .   ? 22.29400 -3.72000  -1.92400  1.000 23.16351  ? 401 FMN A C4     1 
HETATM 5531 O O4     . FMN C 2 .   ? 22.35600 -3.17500  -3.02500  1.000 25.84845  ? 401 FMN A O4     1 
HETATM 5532 C C4A    . FMN C 2 .   ? 22.52100 -5.08800  -1.80000  1.000 27.44458  ? 401 FMN A C4A    1 
HETATM 5533 N N5     . FMN C 2 .   ? 22.83100 -5.84700  -2.90600  1.000 27.17653  ? 401 FMN A N5     1 
HETATM 5534 C C5A    . FMN C 2 .   ? 23.05100 -7.20300  -2.78700  1.000 28.27315  ? 401 FMN A C5A    1 
HETATM 5535 C C6     . FMN C 2 .   ? 23.35000 -7.95400  -3.91800  1.000 26.88954  ? 401 FMN A C6     1 
HETATM 5536 C C7     . FMN C 2 .   ? 23.57800 -9.31900  -3.80600  1.000 27.72120  ? 401 FMN A C7     1 
HETATM 5537 C C7M    . FMN C 2 .   ? 23.90000 -10.13000 -5.02700  1.000 25.92841  ? 401 FMN A C7M    1 
HETATM 5538 C C8     . FMN C 2 .   ? 23.50700 -9.93300  -2.56100  1.000 27.51506  ? 401 FMN A C8     1 
HETATM 5539 C C8M    . FMN C 2 .   ? 23.75400 -11.40800 -2.43900  1.000 21.05885  ? 401 FMN A C8M    1 
HETATM 5540 C C9     . FMN C 2 .   ? 23.20900 -9.18100  -1.43000  1.000 28.41954  ? 401 FMN A C9     1 
HETATM 5541 C C9A    . FMN C 2 .   ? 22.97800 -7.81200  -1.54000  1.000 27.76220  ? 401 FMN A C9A    1 
HETATM 5542 N N10    . FMN C 2 .   ? 22.68000 -7.05100  -0.42400  1.000 27.35944  ? 401 FMN A N10    1 
HETATM 5543 C C10    . FMN C 2 .   ? 22.45600 -5.69400  -0.55500  1.000 23.30609  ? 401 FMN A C10    1 
HETATM 5544 C "C1'"  . FMN C 2 .   ? 22.58400 -7.68400  0.93500   1.000 25.71366  ? 401 FMN A "C1'"  1 
HETATM 5545 C "C2'"  . FMN C 2 .   ? 21.15000 -8.18600  1.10900   1.000 22.05107  ? 401 FMN A "C2'"  1 
HETATM 5546 O "O2'"  . FMN C 2 .   ? 20.24300 -7.13000  0.88600   1.000 22.44371  ? 401 FMN A "O2'"  1 
HETATM 5547 C "C3'"  . FMN C 2 .   ? 20.88000 -8.77800  2.48900   1.000 28.26038  ? 401 FMN A "C3'"  1 
HETATM 5548 O "O3'"  . FMN C 2 .   ? 21.34600 -7.91600  3.50300   1.000 28.20127  ? 401 FMN A "O3'"  1 
HETATM 5549 C "C4'"  . FMN C 2 .   ? 21.52300 -10.14600 2.65000   1.000 28.79809  ? 401 FMN A "C4'"  1 
HETATM 5550 O "O4'"  . FMN C 2 .   ? 21.77200 -10.72300 1.38600   1.000 28.54570  ? 401 FMN A "O4'"  1 
HETATM 5551 C "C5'"  . FMN C 2 .   ? 20.57000 -11.03200 3.43400   1.000 30.20462  ? 401 FMN A "C5'"  1 
HETATM 5552 O "O5'"  . FMN C 2 .   ? 20.98600 -12.36700 3.32700   1.000 31.29767  ? 401 FMN A "O5'"  1 
HETATM 5553 P P      . FMN C 2 .   ? 19.95900 -13.45800 2.75300   1.000 28.11015  ? 401 FMN A P      1 
HETATM 5554 O O1P    . FMN C 2 .   ? 20.25400 -13.64100 1.28300   1.000 29.12951  ? 401 FMN A O1P    1 
HETATM 5555 O O2P    . FMN C 2 .   ? 18.54100 -12.96700 2.91900   1.000 29.37977  ? 401 FMN A O2P    1 
HETATM 5556 O O3P    . FMN C 2 .   ? 20.15300 -14.75800 3.49700   1.000 28.58090  ? 401 FMN A O3P    1 
HETATM 5557 O O2N    . TXP D 3 .   ? 29.13000 -12.00900 -1.69900  0.940 62.07488  ? 402 TXP A O2N    1 
HETATM 5558 P PN     . TXP D 3 .   ? 29.76900 -12.18400 -0.32600  0.940 67.54221  ? 402 TXP A PN     1 
HETATM 5559 O O1N    . TXP D 3 .   ? 29.73900 -13.66800 0.07800   0.940 68.16437  ? 402 TXP A O1N    1 
HETATM 5560 O "O5'A" . TXP D 3 .   ? 28.91600 -11.27300 0.79200   0.940 70.21364  ? 402 TXP A "O5'A" 1 
HETATM 5561 C "C5'A" . TXP D 3 .   ? 29.49700 -10.09100 1.27300   0.940 55.62753  ? 402 TXP A "C5'A" 1 
HETATM 5562 C "C4'A" . TXP D 3 .   ? 28.50000 -9.29000  1.96800   0.940 46.52880  ? 402 TXP A "C4'A" 1 
HETATM 5563 C "C3'A" . TXP D 3 .   ? 27.38500 -9.99700  2.18400   0.940 46.02860  ? 402 TXP A "C3'A" 1 
HETATM 5564 O "O3'A" . TXP D 3 .   ? 26.89200 -9.74700  3.52500   0.940 51.43335  ? 402 TXP A "O3'A" 1 
HETATM 5565 C "C2'A" . TXP D 3 .   ? 26.36000 -9.48400  1.12900   0.940 42.71818  ? 402 TXP A "C2'A" 1 
HETATM 5566 O "O2'A" . TXP D 3 .   ? 25.13200 -9.61300  1.57900   0.940 42.52214  ? 402 TXP A "O2'A" 1 
HETATM 5567 C "C1'A" . TXP D 3 .   ? 26.77100 -7.96000  0.97900   0.940 34.14696  ? 402 TXP A "C1'A" 1 
HETATM 5568 N N1N    . TXP D 3 .   ? 26.30700 -7.41500  -0.29900  0.940 34.13491  ? 402 TXP A N1N    1 
HETATM 5569 C C6N    . TXP D 3 .   ? 27.31800 -7.81100  -1.49700  0.940 36.99732  ? 402 TXP A C6N    1 
HETATM 5570 C C5N    . TXP D 3 .   ? 27.85600 -6.65300  -2.24400  0.940 39.31902  ? 402 TXP A C5N    1 
HETATM 5571 C C4N    . TXP D 3 .   ? 26.86400 -5.47100  -2.54700  0.940 28.15873  ? 402 TXP A C4N    1 
HETATM 5572 C C3N    . TXP D 3 .   ? 25.81800 -5.32200  -1.61300  0.940 33.28482  ? 402 TXP A C3N    1 
HETATM 5573 C C7N    . TXP D 3 .   ? 25.51000 -3.83400  -1.32300  0.940 28.22802  ? 402 TXP A C7N    1 
HETATM 5574 O O7N    . TXP D 3 .   ? 25.41500 -3.43400  -0.16100  0.940 30.77659  ? 402 TXP A O7N    1 
HETATM 5575 N N7N    . TXP D 3 .   ? 25.31000 -2.91500  -2.43200  0.940 27.74949  ? 402 TXP A N7N    1 
HETATM 5576 C C2N    . TXP D 3 .   ? 26.13100 -6.09800  -0.14800  0.940 30.24720  ? 402 TXP A C2N    1 
HETATM 5577 O "O4'A" . TXP D 3 .   ? 28.08100 -7.96000  1.05700   0.940 43.58046  ? 402 TXP A "O4'A" 1 
HETATM 5578 O O3     . TXP D 3 .   ? 31.38900 -11.63700 -0.36300  0.940 73.62738  ? 402 TXP A O3     1 
HETATM 5579 P PA     . TXP D 3 .   ? 32.44300 -11.89000 -1.68300  0.940 85.79580  ? 402 TXP A PA     1 
HETATM 5580 O O1A    . TXP D 3 .   ? 33.82900 -12.17200 -1.15900  0.940 87.33887  ? 402 TXP A O1A    1 
HETATM 5581 O O2A    . TXP D 3 .   ? 32.46900 -10.66100 -2.54700  0.940 79.74729  ? 402 TXP A O2A    1 
HETATM 5582 O "O5'"  . TXP D 3 .   ? 31.89600 -13.20000 -2.58500  0.940 84.72357  ? 402 TXP A "O5'"  1 
HETATM 5583 C "C5'"  . TXP D 3 .   ? 32.42300 -13.40000 -3.88300  0.940 87.91684  ? 402 TXP A "C5'"  1 
HETATM 5584 C "C4'"  . TXP D 3 .   ? 33.23800 -14.64600 -3.91400  0.940 89.40321  ? 402 TXP A "C4'"  1 
HETATM 5585 C "C3'"  . TXP D 3 .   ? 33.44400 -15.24600 -2.36800  0.940 94.49341  ? 402 TXP A "C3'"  1 
HETATM 5586 O "O3'"  . TXP D 3 .   ? 32.87000 -16.60900 -2.28100  0.940 93.49609  ? 402 TXP A "O3'"  1 
HETATM 5587 O "O4'"  . TXP D 3 .   ? 34.42800 -14.39000 -4.39800  0.940 91.59228  ? 402 TXP A "O4'"  1 
HETATM 5588 C "C1'"  . TXP D 3 .   ? 35.35100 -15.29900 -3.59900  0.940 95.88332  ? 402 TXP A "C1'"  1 
HETATM 5589 C "C2'"  . TXP D 3 .   ? 34.68400 -15.29000 -2.14600  0.940 93.51502  ? 402 TXP A "C2'"  1 
HETATM 5590 O "O2'"  . TXP D 3 .   ? 35.04500 -16.50200 -1.34000  0.940 97.02068  ? 402 TXP A "O2'"  1 
HETATM 5591 P P2     . TXP D 3 .   ? 35.21100 -16.29600 0.29900   0.940 104.71231 ? 402 TXP A P2     1 
HETATM 5592 O OP3    . TXP D 3 .   ? 36.29500 -17.23000 0.82600   0.940 101.59203 ? 402 TXP A OP3    1 
HETATM 5593 O OP2    . TXP D 3 .   ? 33.89000 -16.60400 0.99000   0.940 94.34807  ? 402 TXP A OP2    1 
HETATM 5594 O OP1    . TXP D 3 .   ? 35.59400 -14.88800 0.57900   0.940 100.70449 ? 402 TXP A OP1    1 
HETATM 5595 N N9A    . TXP D 3 .   ? 36.58300 -14.89300 -3.62300  0.940 93.84318  ? 402 TXP A N9A    1 
HETATM 5596 C C4A    . TXP D 3 .   ? 36.97000 -13.72200 -3.11800  0.940 86.22928  ? 402 TXP A C4A    1 
HETATM 5597 N N3A    . TXP D 3 .   ? 36.32100 -12.68700 -2.49600  0.940 85.69820  ? 402 TXP A N3A    1 
HETATM 5598 C C2A    . TXP D 3 .   ? 37.00800 -11.58700 -2.07700  0.940 83.39132  ? 402 TXP A C2A    1 
HETATM 5599 N N1A    . TXP D 3 .   ? 38.35500 -11.50500 -2.28200  0.940 75.54011  ? 402 TXP A N1A    1 
HETATM 5600 C C6A    . TXP D 3 .   ? 38.99600 -12.50500 -2.89000  0.940 77.85194  ? 402 TXP A C6A    1 
HETATM 5601 N N6A    . TXP D 3 .   ? 40.44700 -12.25300 -3.02900  0.940 69.47809  ? 402 TXP A N6A    1 
HETATM 5602 C C5A    . TXP D 3 .   ? 38.29100 -13.63700 -3.31800  0.940 80.76331  ? 402 TXP A C5A    1 
HETATM 5603 N N7A    . TXP D 3 .   ? 38.69600 -14.74400 -3.93500  0.940 77.72691  ? 402 TXP A N7A    1 
HETATM 5604 C C8A    . TXP D 3 .   ? 37.63900 -15.52500 -4.12700  0.940 85.76404  ? 402 TXP A C8A    1 
HETATM 5605 N N1     . FMN E 2 .   ? 32.83700 0.40700   -43.00400 1.000 24.36567  ? 401 FMN B N1     1 
HETATM 5606 C C2     . FMN E 2 .   ? 33.07200 -0.95100  -43.05300 1.000 24.64869  ? 401 FMN B C2     1 
HETATM 5607 O O2     . FMN E 2 .   ? 33.05200 -1.60900  -42.01500 1.000 24.32753  ? 401 FMN B O2     1 
HETATM 5608 N N3     . FMN E 2 .   ? 33.32700 -1.57000  -44.26000 1.000 23.81822  ? 401 FMN B N3     1 
HETATM 5609 C C4     . FMN E 2 .   ? 33.35200 -0.82800  -45.42300 1.000 26.02075  ? 401 FMN B C4     1 
HETATM 5610 O O4     . FMN E 2 .   ? 33.57800 -1.37700  -46.50000 1.000 23.78711  ? 401 FMN B O4     1 
HETATM 5611 C C4A    . FMN E 2 .   ? 33.11700 0.54200   -45.37200 1.000 27.37804  ? 401 FMN B C4A    1 
HETATM 5612 N N5     . FMN E 2 .   ? 33.12500 1.29200   -46.52500 1.000 23.09114  ? 401 FMN B N5     1 
HETATM 5613 C C5A    . FMN E 2 .   ? 32.89700 2.65100   -46.47600 1.000 27.71759  ? 401 FMN B C5A    1 
HETATM 5614 C C6     . FMN E 2 .   ? 32.92200 3.39500   -47.65000 1.000 24.48839  ? 401 FMN B C6     1 
HETATM 5615 C C7     . FMN E 2 .   ? 32.68900 4.76400   -47.61200 1.000 27.26182  ? 401 FMN B C7     1 
HETATM 5616 C C7M    . FMN E 2 .   ? 32.71700 5.56200   -48.88300 1.000 24.50690  ? 401 FMN B C7M    1 
HETATM 5617 C C8     . FMN E 2 .   ? 32.43200 5.38900   -46.39600 1.000 29.30414  ? 401 FMN B C8     1 
HETATM 5618 C C8M    . FMN E 2 .   ? 32.17900 6.86700   -46.34500 1.000 23.25216  ? 401 FMN B C8M    1 
HETATM 5619 C C9     . FMN E 2 .   ? 32.40700 4.64200   -45.22300 1.000 29.05423  ? 401 FMN B C9     1 
HETATM 5620 C C9A    . FMN E 2 .   ? 32.64200 3.27100   -45.25900 1.000 29.66249  ? 401 FMN B C9A    1 
HETATM 5621 N N10    . FMN E 2 .   ? 32.61900 2.51700   -44.09900 1.000 32.93657  ? 401 FMN B N10    1 
HETATM 5622 C C10    . FMN E 2 .   ? 32.85300 1.15700   -44.15800 1.000 27.15979  ? 401 FMN B C10    1 
HETATM 5623 C "C1'"  . FMN E 2 .   ? 32.35800 3.15900   -42.76800 1.000 24.98411  ? 401 FMN B "C1'"  1 
HETATM 5624 C "C2'"  . FMN E 2 .   ? 33.70300 3.66300   -42.24100 1.000 21.99117  ? 401 FMN B "C2'"  1 
HETATM 5625 O "O2'"  . FMN E 2 .   ? 34.63900 2.60800   -42.23000 1.000 24.39644  ? 401 FMN B "O2'"  1 
HETATM 5626 C "C3'"  . FMN E 2 .   ? 33.62300 4.27000   -40.84400 1.000 24.82513  ? 401 FMN B "C3'"  1 
HETATM 5627 O "O3'"  . FMN E 2 .   ? 32.93000 3.41300   -39.96300 1.000 28.91389  ? 401 FMN B "O3'"  1 
HETATM 5628 C "C4'"  . FMN E 2 .   ? 32.95200 5.63400   -40.86700 1.000 24.05215  ? 401 FMN B "C4'"  1 
HETATM 5629 O "O4'"  . FMN E 2 .   ? 33.03500 6.19700   -42.15900 1.000 28.05662  ? 401 FMN B "O4'"  1 
HETATM 5630 C "C5'"  . FMN E 2 .   ? 33.67000 6.53300   -39.87500 1.000 21.22855  ? 401 FMN B "C5'"  1 
HETATM 5631 O "O5'"  . FMN E 2 .   ? 33.28000 7.86200   -40.08700 1.000 29.49733  ? 401 FMN B "O5'"  1 
HETATM 5632 P P      . FMN E 2 .   ? 34.40500 8.97500   -40.35300 1.000 27.90617  ? 401 FMN B P      1 
HETATM 5633 O O1P    . FMN E 2 .   ? 34.59100 9.09400   -41.84800 1.000 23.69687  ? 401 FMN B O1P    1 
HETATM 5634 O O2P    . FMN E 2 .   ? 35.71100 8.55600   -39.72300 1.000 26.14721  ? 401 FMN B O2P    1 
HETATM 5635 O O3P    . FMN E 2 .   ? 33.93600 10.28700  -39.77100 1.000 28.15840  ? 401 FMN B O3P    1 
HETATM 5636 O O2N    . TXP F 3 .   ? 27.42100 7.24100   -46.12600 0.850 56.62218  ? 402 TXP B O2N    1 
HETATM 5637 P PN     . TXP F 3 .   ? 25.99500 7.60400   -45.87800 0.850 69.25657  ? 402 TXP B PN     1 
HETATM 5638 O O1N    . TXP F 3 .   ? 25.68400 8.93900   -45.29000 0.850 62.03145  ? 402 TXP B O1N    1 
HETATM 5639 O "O5'A" . TXP F 3 .   ? 25.30500 6.46500   -44.99000 0.850 66.87403  ? 402 TXP B "O5'A" 1 
HETATM 5640 C "C5'A" . TXP F 3 .   ? 25.71600 5.09200   -45.17900 0.850 52.17289  ? 402 TXP B "C5'A" 1 
HETATM 5641 C "C4'A" . TXP F 3 .   ? 26.16900 4.52900   -43.85500 0.850 42.34301  ? 402 TXP B "C4'A" 1 
HETATM 5642 C "C3'A" . TXP F 3 .   ? 27.17700 5.38400   -43.08000 0.850 38.41280  ? 402 TXP B "C3'A" 1 
HETATM 5643 O "O3'A" . TXP F 3 .   ? 27.06300 5.17000   -41.68000 0.850 44.83489  ? 402 TXP B "O3'A" 1 
HETATM 5644 C "C2'A" . TXP F 3 .   ? 28.49800 4.87000   -43.64400 0.850 40.58392  ? 402 TXP B "C2'A" 1 
HETATM 5645 O "O2'A" . TXP F 3 .   ? 29.58800 5.08600   -42.76400 0.850 35.85047  ? 402 TXP B "O2'A" 1 
HETATM 5646 C "C1'A" . TXP F 3 .   ? 28.21600 3.38400   -43.83200 0.850 34.79868  ? 402 TXP B "C1'A" 1 
HETATM 5647 N N1N    . TXP F 3 .   ? 28.95700 2.73300   -44.88800 0.850 30.57579  ? 402 TXP B N1N    1 
HETATM 5648 C C6N    . TXP F 3 .   ? 28.67300 3.21900   -46.25000 0.850 32.27693  ? 402 TXP B C6N    1 
HETATM 5649 C C5N    . TXP F 3 .   ? 28.62500 2.13500   -47.27000 0.850 30.54616  ? 402 TXP B C5N    1 
HETATM 5650 C C4N    . TXP F 3 .   ? 29.32200 1.02000   -47.19500 0.850 25.62466  ? 402 TXP B C4N    1 
HETATM 5651 C C3N    . TXP F 3 .   ? 29.90500 0.70100   -45.84400 0.850 31.34465  ? 402 TXP B C3N    1 
HETATM 5652 C C7N    . TXP F 3 .   ? 30.18400 -0.76000  -45.58700 0.850 28.36336  ? 402 TXP B C7N    1 
HETATM 5653 O O7N    . TXP F 3 .   ? 30.15500 -1.20900  -44.44000 0.850 27.55505  ? 402 TXP B O7N    1 
HETATM 5654 N N7N    . TXP F 3 .   ? 30.49300 -1.50300  -46.63500 0.850 26.17000  ? 402 TXP B N7N    1 
HETATM 5655 C C2N    . TXP F 3 .   ? 28.97800 1.27100   -44.77200 0.850 28.06258  ? 402 TXP B C2N    1 
HETATM 5656 O "O4'A" . TXP F 3 .   ? 26.83500 3.26300   -44.08500 0.850 42.45819  ? 402 TXP B "O4'A" 1 
HETATM 5657 O O3     . TXP F 3 .   ? 25.18100 7.43800   -47.24300 0.850 77.28289  ? 402 TXP B O3     1 
HETATM 5658 P PA     . TXP F 3 .   ? 23.63800 7.69900   -47.58200 0.850 80.39094  ? 402 TXP B PA     1 
HETATM 5659 O O1A    . TXP F 3 .   ? 23.10100 6.51000   -48.30600 0.850 71.65551  ? 402 TXP B O1A    1 
HETATM 5660 O O2A    . TXP F 3 .   ? 23.53000 9.04000   -48.22300 0.850 81.79542  ? 402 TXP B O2A    1 
HETATM 5661 O "O5'"  . TXP F 3 .   ? 22.99800 7.76100   -46.11500 0.850 69.86855  ? 402 TXP B "O5'"  1 
HETATM 5662 O "O3'"  . TXP F 3 .   ? 18.65400 10.18000  -45.27400 0.850 45.43003  ? 402 TXP B "O3'"  1 
HETATM 5663 N N9A    . TXP F 3 .   ? 20.56400 14.45100  -50.72600 0.850 47.14321  ? 402 TXP B N9A    1 
HETATM 5664 O O      . HOH G 4 .   ? 21.90700 -3.06800  -9.42000  1.000 25.97993  ? 501 HOH A O      1 
HETATM 5665 O O      . HOH G 4 .   ? 19.24800 -16.86300 3.20400   1.000 32.91541  ? 502 HOH A O      1 
HETATM 5666 O O      . HOH G 4 .   ? 0.32800  1.17900   -11.83800 1.000 33.60469  ? 503 HOH A O      1 
HETATM 5667 O O      . HOH G 4 .   ? 41.89200 9.14400   -9.83500  1.000 38.04085  ? 504 HOH A O      1 
HETATM 5668 O O      . HOH G 4 .   ? 34.55300 -5.42000  16.98800  1.000 38.45444  ? 505 HOH A O      1 
HETATM 5669 O O      . HOH G 4 .   ? 12.17600 13.05100  -15.12700 1.000 40.72128  ? 506 HOH A O      1 
HETATM 5670 O O      . HOH G 4 .   ? 29.71200 -14.55000 -13.62300 1.000 35.16706  ? 507 HOH A O      1 
HETATM 5671 O O      . HOH G 4 .   ? 31.46600 -6.59900  -14.39600 1.000 34.56577  ? 508 HOH A O      1 
HETATM 5672 O O      . HOH G 4 .   ? 17.60300 -10.09000 4.18800   1.000 27.65332  ? 509 HOH A O      1 
HETATM 5673 O O      . HOH G 4 .   ? 23.54500 -7.98200  4.44900   1.000 26.53792  ? 510 HOH A O      1 
HETATM 5674 O O      . HOH G 4 .   ? 17.30800 -6.39500  -6.75700  1.000 24.52919  ? 511 HOH A O      1 
HETATM 5675 O O      . HOH G 4 .   ? 22.45500 -14.43600 -23.04500 1.000 28.82046  ? 512 HOH A O      1 
HETATM 5676 O O      . HOH G 4 .   ? 34.90000 10.89700  -7.35800  1.000 36.78715  ? 513 HOH A O      1 
HETATM 5677 O O      . HOH G 4 .   ? 6.27400  -7.37500  -17.37700 1.000 41.39114  ? 514 HOH A O      1 
HETATM 5678 O O      . HOH G 4 .   ? 36.73100 8.30400   14.48500  1.000 36.42067  ? 515 HOH A O      1 
HETATM 5679 O O      . HOH G 4 .   ? 6.30100  1.95900   10.19000  1.000 26.16177  ? 516 HOH A O      1 
HETATM 5680 O O      . HOH G 4 .   ? 20.65800 19.36100  2.64500   1.000 37.84096  ? 517 HOH A O      1 
HETATM 5681 O O      . HOH G 4 .   ? 44.63800 7.18800   10.28900  1.000 43.14174  ? 518 HOH A O      1 
HETATM 5682 O O      . HOH G 4 .   ? 7.96400  7.84000   -17.15300 1.000 35.52810  ? 519 HOH A O      1 
HETATM 5683 O O      . HOH G 4 .   ? 23.31200 -12.94500 -16.79800 1.000 28.31210  ? 520 HOH A O      1 
HETATM 5684 O O      . HOH G 4 .   ? 13.02900 -26.07400 -6.88100  1.000 27.59006  ? 521 HOH A O      1 
HETATM 5685 O O      . HOH G 4 .   ? 37.89400 12.87700  -5.97400  1.000 37.92576  ? 522 HOH A O      1 
HETATM 5686 O O      . HOH G 4 .   ? 17.53400 -22.31800 -9.89500  1.000 28.72245  ? 523 HOH A O      1 
HETATM 5687 O O      . HOH G 4 .   ? 29.70200 -5.91000  -15.96800 1.000 35.06907  ? 524 HOH A O      1 
HETATM 5688 O O      . HOH G 4 .   ? 6.13300  -9.34100  -2.87200  1.000 23.81217  ? 525 HOH A O      1 
HETATM 5689 O O      . HOH G 4 .   ? 15.95000 -22.70700 9.14600   1.000 32.76241  ? 526 HOH A O      1 
HETATM 5690 O O      . HOH G 4 .   ? 31.68200 -1.16100  -4.56200  1.000 22.27878  ? 527 HOH A O      1 
HETATM 5691 O O      . HOH G 4 .   ? 21.44800 -15.27000 -10.57300 1.000 21.16048  ? 528 HOH A O      1 
HETATM 5692 O O      . HOH G 4 .   ? 22.24000 -1.53600  -7.19600  1.000 22.50048  ? 529 HOH A O      1 
HETATM 5693 O O      . HOH G 4 .   ? 31.22100 14.26200  21.05800  1.000 37.00941  ? 530 HOH A O      1 
HETATM 5694 O O      . HOH G 4 .   ? 31.74500 3.58300   -15.06900 1.000 22.73912  ? 531 HOH A O      1 
HETATM 5695 O O      . HOH G 4 .   ? 31.10000 14.85700  -3.57200  1.000 30.90258  ? 532 HOH A O      1 
HETATM 5696 O O      . HOH G 4 .   ? 18.68100 -13.41300 -22.40800 1.000 36.57327  ? 533 HOH A O      1 
HETATM 5697 O O      . HOH G 4 .   ? 23.13100 19.74300  3.37300   1.000 34.52773  ? 534 HOH A O      1 
HETATM 5698 O O      . HOH G 4 .   ? 40.32000 13.28000  -12.83500 1.000 44.10435  ? 535 HOH A O      1 
HETATM 5699 O O      . HOH G 4 .   ? 5.12500  5.94000   -10.68800 1.000 34.93412  ? 536 HOH A O      1 
HETATM 5700 O O      . HOH G 4 .   ? 25.87000 3.63300   -6.01300  1.000 22.15808  ? 537 HOH A O      1 
HETATM 5701 O O      . HOH G 4 .   ? 10.22000 -23.72000 -9.53800  1.000 36.15233  ? 538 HOH A O      1 
HETATM 5702 O O      . HOH G 4 .   ? 29.70300 12.68900  -3.72900  1.000 31.53516  ? 539 HOH A O      1 
HETATM 5703 O O      . HOH G 4 .   ? 23.66700 5.34500   1.09900   1.000 20.14915  ? 540 HOH A O      1 
HETATM 5704 O O      . HOH G 4 .   ? 44.86900 1.35500   -2.69800  1.000 32.83047  ? 541 HOH A O      1 
HETATM 5705 O O      . HOH G 4 .   ? 36.60300 6.66000   17.34200  1.000 40.65683  ? 542 HOH A O      1 
HETATM 5706 O O      . HOH G 4 .   ? 1.87800  -21.13000 6.13500   1.000 39.33471  ? 543 HOH A O      1 
HETATM 5707 O O      . HOH G 4 .   ? 9.19300  2.58900   12.46100  1.000 28.29739  ? 544 HOH A O      1 
HETATM 5708 O O      . HOH G 4 .   ? 25.10700 -20.15000 -6.25300  1.000 39.48780  ? 545 HOH A O      1 
HETATM 5709 O O      . HOH G 4 .   ? 29.12100 -13.51200 -8.64400  1.000 29.92483  ? 546 HOH A O      1 
HETATM 5710 O O      . HOH G 4 .   ? 27.15900 12.60900  -3.55800  1.000 24.09093  ? 547 HOH A O      1 
HETATM 5711 O O      . HOH G 4 .   ? 9.22300  -23.21100 1.76700   1.000 30.06267  ? 548 HOH A O      1 
HETATM 5712 O O      . HOH G 4 .   ? 20.45200 -11.89000 10.55400  1.000 24.76635  ? 549 HOH A O      1 
HETATM 5713 O O      . HOH G 4 .   ? 3.23800  -19.03300 -7.66200  1.000 37.32388  ? 550 HOH A O      1 
HETATM 5714 O O      . HOH G 4 .   ? 1.62100  -5.10800  -12.85000 1.000 39.38370  ? 551 HOH A O      1 
HETATM 5715 O O      . HOH G 4 .   ? 25.27800 -6.09900  12.31700  1.000 26.03520  ? 552 HOH A O      1 
HETATM 5716 O O      . HOH G 4 .   ? 43.30100 8.96400   6.68400   1.000 36.00424  ? 553 HOH A O      1 
HETATM 5717 O O      . HOH G 4 .   ? 41.99100 13.68100  1.29400   1.000 35.43894  ? 554 HOH A O      1 
HETATM 5718 O O      . HOH G 4 .   ? 31.86100 -3.87800  13.17400  1.000 26.65869  ? 555 HOH A O      1 
HETATM 5719 O O      . HOH G 4 .   ? 32.94300 -11.92000 -13.34700 1.000 35.27172  ? 556 HOH A O      1 
HETATM 5720 O O      . HOH G 4 .   ? 6.91300  -9.46300  16.08800  1.000 35.18813  ? 557 HOH A O      1 
HETATM 5721 O O      . HOH G 4 .   ? 38.59300 16.70900  -0.21900  1.000 38.17080  ? 558 HOH A O      1 
HETATM 5722 O O      . HOH G 4 .   ? 7.66900  -8.68100  -0.51300  1.000 20.47066  ? 559 HOH A O      1 
HETATM 5723 O O      . HOH G 4 .   ? 16.82400 -12.89000 -10.15400 1.000 23.03712  ? 560 HOH A O      1 
HETATM 5724 O O      . HOH G 4 .   ? 40.46300 4.12900   12.01800  1.000 37.29766  ? 561 HOH A O      1 
HETATM 5725 O O      . HOH G 4 .   ? 27.70900 -12.23000 -11.22700 1.000 28.86522  ? 562 HOH A O      1 
HETATM 5726 O O      . HOH G 4 .   ? 42.91400 -1.93300  -2.17600  1.000 26.29215  ? 563 HOH A O      1 
HETATM 5727 O O      . HOH G 4 .   ? 17.50200 -12.86300 5.42400   1.000 23.60506  ? 564 HOH A O      1 
HETATM 5728 O O      . HOH G 4 .   ? 32.93500 7.77200   -4.02800  1.000 22.81570  ? 565 HOH A O      1 
HETATM 5729 O O      . HOH G 4 .   ? 9.14100  15.07000  -5.06800  1.000 31.75577  ? 566 HOH A O      1 
HETATM 5730 O O      . HOH G 4 .   ? 32.44100 -3.54200  -3.85000  1.000 32.29124  ? 567 HOH A O      1 
HETATM 5731 O O      . HOH G 4 .   ? 6.38200  -3.57900  16.73600  1.000 33.90086  ? 568 HOH A O      1 
HETATM 5732 O O      . HOH G 4 .   ? 19.56300 -4.39500  -11.90800 1.000 27.72730  ? 569 HOH A O      1 
HETATM 5733 O O      . HOH G 4 .   ? 24.14000 -11.55700 -22.44100 1.000 31.47967  ? 570 HOH A O      1 
HETATM 5734 O O      . HOH G 4 .   ? 29.21700 16.55400  15.54000  1.000 33.45053  ? 571 HOH A O      1 
HETATM 5735 O O      . HOH G 4 .   ? 17.16300 -5.60200  -9.41600  1.000 26.42948  ? 572 HOH A O      1 
HETATM 5736 O O      . HOH G 4 .   ? 26.09800 0.07700   9.47000   1.000 23.65952  ? 573 HOH A O      1 
HETATM 5737 O O      . HOH G 4 .   ? 18.38900 -12.75300 20.80200  1.000 33.82570  ? 574 HOH A O      1 
HETATM 5738 O O      . HOH G 4 .   ? 31.96500 -3.47600  -8.51500  1.000 25.51772  ? 575 HOH A O      1 
HETATM 5739 O O      . HOH G 4 .   ? 41.40500 15.41400  2.90000   1.000 39.02443  ? 576 HOH A O      1 
HETATM 5740 O O      . HOH G 4 .   ? 19.99100 3.27300   22.26300  1.000 24.43701  ? 577 HOH A O      1 
HETATM 5741 O O      . HOH G 4 .   ? 5.64300  -7.45700  3.12400   1.000 27.62163  ? 578 HOH A O      1 
HETATM 5742 O O      . HOH G 4 .   ? 11.07900 7.98400   19.01200  1.000 30.62585  ? 579 HOH A O      1 
HETATM 5743 O O      . HOH G 4 .   ? 42.96400 1.35100   -8.14200  1.000 35.03216  ? 580 HOH A O      1 
HETATM 5744 O O      . HOH G 4 .   ? 33.46600 22.51600  9.81100   1.000 37.17349  ? 581 HOH A O      1 
HETATM 5745 O O      . HOH G 4 .   ? 11.43000 -2.12800  17.34900  1.000 26.68079  ? 582 HOH A O      1 
HETATM 5746 O O      . HOH G 4 .   ? 7.76100  13.78600  9.19800   1.000 28.15861  ? 583 HOH A O      1 
HETATM 5747 O O      . HOH G 4 .   ? 36.75500 19.16500  8.95800   1.000 33.84023  ? 584 HOH A O      1 
HETATM 5748 O O      . HOH G 4 .   ? 37.20200 -4.29600  20.12300  1.000 39.05451  ? 585 HOH A O      1 
HETATM 5749 O O      . HOH G 4 .   ? 27.33800 1.32500   -6.76800  1.000 23.10933  ? 586 HOH A O      1 
HETATM 5750 O O      . HOH G 4 .   ? 39.30100 2.37500   -1.13500  1.000 29.05318  ? 587 HOH A O      1 
HETATM 5751 O O      . HOH G 4 .   ? 30.09600 4.52000   -12.78700 1.000 27.71204  ? 588 HOH A O      1 
HETATM 5752 O O      . HOH G 4 .   ? 8.00400  -20.00600 -14.54000 1.000 36.72954  ? 589 HOH A O      1 
HETATM 5753 O O      . HOH G 4 .   ? 41.93500 -3.82400  -3.51200  1.000 31.55513  ? 590 HOH A O      1 
HETATM 5754 O O      . HOH G 4 .   ? 26.49300 -10.17900 12.21700  1.000 33.93324  ? 591 HOH A O      1 
HETATM 5755 O O      . HOH G 4 .   ? 34.51600 10.73400  -17.33200 1.000 42.95028  ? 592 HOH A O      1 
HETATM 5756 O O      . HOH G 4 .   ? 9.51600  -21.91700 12.68900  1.000 39.73954  ? 593 HOH A O      1 
HETATM 5757 O O      . HOH G 4 .   ? 34.79400 0.47200   3.33400   1.000 19.39775  ? 594 HOH A O      1 
HETATM 5758 O O      . HOH G 4 .   ? 34.67200 4.65300   -17.19400 1.000 32.98788  ? 595 HOH A O      1 
HETATM 5759 O O      . HOH G 4 .   ? 19.07200 -7.34000  24.87000  1.000 31.15808  ? 596 HOH A O      1 
HETATM 5760 O O      . HOH G 4 .   ? 12.72600 -14.99300 -12.11500 1.000 26.14056  ? 597 HOH A O      1 
HETATM 5761 O O      . HOH G 4 .   ? 27.08400 2.43100   4.31900   1.000 24.68428  ? 598 HOH A O      1 
HETATM 5762 O O      . HOH G 4 .   ? 28.54300 -11.54500 4.88000   1.000 46.35070  ? 599 HOH A O      1 
HETATM 5763 O O      . HOH G 4 .   ? 29.60700 -8.90700  -13.81000 1.000 26.41137  ? 600 HOH A O      1 
HETATM 5764 O O      . HOH G 4 .   ? 22.52000 7.45400   -16.53400 1.000 28.36579  ? 601 HOH A O      1 
HETATM 5765 O O      . HOH G 4 .   ? 18.20700 -2.90900  23.98400  1.000 22.75660  ? 602 HOH A O      1 
HETATM 5766 O O      . HOH G 4 .   ? 41.22200 12.35800  -8.22300  1.000 30.56013  ? 603 HOH A O      1 
HETATM 5767 O O      . HOH G 4 .   ? 10.53400 -5.56800  22.24300  1.000 32.55367  ? 604 HOH A O      1 
HETATM 5768 O O      . HOH G 4 .   ? 17.74300 -18.69700 -13.66800 1.000 33.27124  ? 605 HOH A O      1 
HETATM 5769 O O      . HOH G 4 .   ? 35.91700 18.47200  0.58000   1.000 30.89589  ? 606 HOH A O      1 
HETATM 5770 O O      . HOH G 4 .   ? 43.68200 7.52400   -5.32100  1.000 38.20792  ? 607 HOH A O      1 
HETATM 5771 O O      . HOH G 4 .   ? 3.96600  -27.37100 5.95200   1.000 47.65924  ? 608 HOH A O      1 
HETATM 5772 O O      . HOH G 4 .   ? 39.82600 15.00600  10.31800  1.000 37.90769  ? 609 HOH A O      1 
HETATM 5773 O O      . HOH G 4 .   ? 16.99800 8.93500   21.95200  1.000 26.09080  ? 610 HOH A O      1 
HETATM 5774 O O      . HOH G 4 .   ? 26.29900 4.60700   2.40200   1.000 30.46241  ? 611 HOH A O      1 
HETATM 5775 O O      . HOH G 4 .   ? 6.91400  -13.11000 -4.22700  1.000 28.89150  ? 612 HOH A O      1 
HETATM 5776 O O      . HOH G 4 .   ? 27.04000 -10.00500 -18.20100 1.000 28.28067  ? 613 HOH A O      1 
HETATM 5777 O O      . HOH G 4 .   ? 15.91300 -5.80500  -4.44100  1.000 18.70899  ? 614 HOH A O      1 
HETATM 5778 O O      . HOH G 4 .   ? 7.78400  -1.77000  17.63500  1.000 38.59769  ? 615 HOH A O      1 
HETATM 5779 O O      . HOH G 4 .   ? 31.28200 -7.87600  -17.93500 1.000 32.06822  ? 616 HOH A O      1 
HETATM 5780 O O      . HOH G 4 .   ? 30.36200 6.94200   -9.29300  1.000 26.71571  ? 617 HOH A O      1 
HETATM 5781 O O      . HOH G 4 .   ? 44.08500 -5.88300  -3.74500  1.000 30.18194  ? 618 HOH A O      1 
HETATM 5782 O O      . HOH G 4 .   ? 4.73600  -7.32200  14.71100  1.000 28.05694  ? 619 HOH A O      1 
HETATM 5783 O O      . HOH G 4 .   ? 34.49500 20.34500  1.89200   1.000 33.70830  ? 620 HOH A O      1 
HETATM 5784 O O      . HOH G 4 .   ? 14.67200 2.03400   -20.14900 1.000 34.15660  ? 621 HOH A O      1 
HETATM 5785 O O      . HOH G 4 .   ? 36.85200 14.80900  17.40500  1.000 43.20417  ? 622 HOH A O      1 
HETATM 5786 O O      . HOH G 4 .   ? 30.42100 -0.46200  26.04500  1.000 28.74675  ? 623 HOH A O      1 
HETATM 5787 O O      . HOH G 4 .   ? 9.33500  -13.76700 23.06900  1.000 45.97946  ? 624 HOH A O      1 
HETATM 5788 O O      . HOH G 4 .   ? 29.93900 -3.99800  -18.35500 1.000 28.60111  ? 625 HOH A O      1 
HETATM 5789 O O      . HOH G 4 .   ? 31.39900 2.84200   21.90900  1.000 33.73591  ? 626 HOH A O      1 
HETATM 5790 O O      . HOH G 4 .   ? 28.23000 1.58900   -15.10200 1.000 24.94114  ? 627 HOH A O      1 
HETATM 5791 O O      . HOH G 4 .   ? 10.45500 -16.94100 -14.92100 1.000 37.41264  ? 628 HOH A O      1 
HETATM 5792 O O      . HOH G 4 .   ? 18.91600 15.47200  -9.01000  1.000 35.66928  ? 629 HOH A O      1 
HETATM 5793 O O      . HOH G 4 .   ? 29.59500 11.13500  11.20100  1.000 23.38117  ? 630 HOH A O      1 
HETATM 5794 O O      . HOH G 4 .   ? 33.61900 -11.25600 -18.07500 1.000 39.47677  ? 631 HOH A O      1 
HETATM 5795 O O      . HOH G 4 .   ? 32.54100 2.50600   18.94500  1.000 36.76684  ? 632 HOH A O      1 
HETATM 5796 O O      . HOH G 4 .   ? 12.50800 -23.19500 6.66100   1.000 32.56683  ? 633 HOH A O      1 
HETATM 5797 O O      . HOH G 4 .   ? 16.57300 -17.96000 -20.05100 1.000 28.38381  ? 634 HOH A O      1 
HETATM 5798 O O      . HOH G 4 .   ? 29.57700 -9.29500  -16.85700 1.000 32.29153  ? 635 HOH A O      1 
HETATM 5799 O O      . HOH G 4 .   ? 40.98200 17.07800  10.52200  1.000 43.55498  ? 636 HOH A O      1 
HETATM 5800 O O      . HOH G 4 .   ? 21.54300 -21.63000 -3.97700  1.000 30.83826  ? 637 HOH A O      1 
HETATM 5801 O O      . HOH G 4 .   ? 9.03000  -4.51000  -18.62800 1.000 46.27219  ? 638 HOH A O      1 
HETATM 5802 O O      . HOH G 4 .   ? 28.68100 -6.18800  -19.30700 1.000 26.40279  ? 639 HOH A O      1 
HETATM 5803 O O      . HOH G 4 .   ? 32.57400 -5.21200  -6.21900  1.000 23.08787  ? 640 HOH A O      1 
HETATM 5804 O O      . HOH G 4 .   ? 29.44600 10.58800  22.05800  1.000 25.92069  ? 641 HOH A O      1 
HETATM 5805 O O      . HOH G 4 .   ? 17.34000 -15.28400 1.35000   1.000 31.72557  ? 642 HOH A O      1 
HETATM 5806 O O      . HOH G 4 .   ? 14.82600 16.62700  10.18300  1.000 31.17091  ? 643 HOH A O      1 
HETATM 5807 O O      . HOH G 4 .   ? 35.04700 19.10900  -3.78700  1.000 41.37986  ? 644 HOH A O      1 
HETATM 5808 O O      . HOH G 4 .   ? 21.74900 -11.14200 26.82800  1.000 32.86911  ? 645 HOH A O      1 
HETATM 5809 O O      . HOH G 4 .   ? 27.36500 8.37600   10.21200  1.000 24.83007  ? 646 HOH A O      1 
HETATM 5810 O O      . HOH G 4 .   ? 31.30800 -9.77200  8.99200   1.000 39.74054  ? 647 HOH A O      1 
HETATM 5811 O O      . HOH G 4 .   ? 33.93700 17.51300  18.59800  1.000 47.18914  ? 648 HOH A O      1 
HETATM 5812 O O      . HOH G 4 .   ? 38.43700 0.19700   15.54500  1.000 39.17503  ? 649 HOH A O      1 
HETATM 5813 O O      . HOH G 4 .   ? 13.23900 -22.04900 4.14900   1.000 29.84409  ? 650 HOH A O      1 
HETATM 5814 O O      . HOH G 4 .   ? 21.79400 7.87100   25.78100  1.000 33.14876  ? 651 HOH A O      1 
HETATM 5815 O O      . HOH G 4 .   ? 19.85500 -5.41900  -18.83400 1.000 24.79415  ? 652 HOH A O      1 
HETATM 5816 O O      . HOH G 4 .   ? 28.37700 8.83300   -13.13400 1.000 29.86959  ? 653 HOH A O      1 
HETATM 5817 O O      . HOH G 4 .   ? 11.87200 1.41900   -17.35100 1.000 33.55397  ? 654 HOH A O      1 
HETATM 5818 O O      . HOH G 4 .   ? 15.00700 -14.20300 20.40100  1.000 44.49373  ? 655 HOH A O      1 
HETATM 5819 O O      . HOH G 4 .   ? 34.37700 13.71000  -6.14600  1.000 41.76124  ? 656 HOH A O      1 
HETATM 5820 O O      . HOH G 4 .   ? 11.38800 -1.49400  24.69200  1.000 29.81221  ? 657 HOH A O      1 
HETATM 5821 O O      . HOH G 4 .   ? 20.80600 18.44900  10.14600  1.000 35.05966  ? 658 HOH A O      1 
HETATM 5822 O O      . HOH G 4 .   ? 24.567   10.581    23.929    1.000 36.82417  ? 659 HOH A O      1 
HETATM 5823 O O      . HOH G 4 .   ? 45.24400 4.96100   -5.21200  1.000 32.45569  ? 660 HOH A O      1 
HETATM 5824 O O      . HOH G 4 .   ? 42.67300 -1.76700  -10.47200 1.000 33.27737  ? 661 HOH A O      1 
HETATM 5825 O O      . HOH G 4 .   ? 28.16300 2.57400   -12.73000 1.000 19.64447  ? 662 HOH A O      1 
HETATM 5826 O O      . HOH G 4 .   ? 21.94300 4.57200   23.39200  1.000 28.08126  ? 663 HOH A O      1 
HETATM 5827 O O      . HOH G 4 .   ? 17.12800 3.90300   22.53500  1.000 30.18406  ? 664 HOH A O      1 
HETATM 5828 O O      . HOH G 4 .   ? 12.02000 -14.50700 -18.40900 1.000 34.18187  ? 665 HOH A O      1 
HETATM 5829 O O      . HOH G 4 .   ? 40.20600 11.73200  7.74600   1.000 36.55837  ? 666 HOH A O      1 
HETATM 5830 O O      . HOH G 4 .   ? 20.49600 17.73300  7.84300   1.000 27.75794  ? 667 HOH A O      1 
HETATM 5831 O O      . HOH G 4 .   ? 14.62800 -16.45300 14.19100  1.000 33.81844  ? 668 HOH A O      1 
HETATM 5832 O O      . HOH G 4 .   ? 13.330   -25.524   0.242     1.000 31.64360  ? 669 HOH A O      1 
HETATM 5833 O O      . HOH G 4 .   ? 4.57500  1.26000   -16.97200 1.000 39.45169  ? 670 HOH A O      1 
HETATM 5834 O O      . HOH G 4 .   ? 16.56500 -13.17000 18.70100  1.000 34.02348  ? 671 HOH A O      1 
HETATM 5835 O O      . HOH G 4 .   ? 17.32400 -5.24600  25.34800  1.000 25.16359  ? 672 HOH A O      1 
HETATM 5836 O O      . HOH G 4 .   ? 42.21500 -9.05800  -12.66600 1.000 38.41348  ? 673 HOH A O      1 
HETATM 5837 O O      . HOH G 4 .   ? 32.33600 -10.01700 -7.69500  1.000 35.44201  ? 674 HOH A O      1 
HETATM 5838 O O      . HOH G 4 .   ? 4.49100  8.69300   11.23400  1.000 46.66268  ? 675 HOH A O      1 
HETATM 5839 O O      . HOH G 4 .   ? 4.62900  -14.73600 -4.35300  1.000 24.51267  ? 676 HOH A O      1 
HETATM 5840 O O      . HOH G 4 .   ? 38.94300 -12.34300 -11.46300 1.000 45.32572  ? 677 HOH A O      1 
HETATM 5841 O O      . HOH G 4 .   ? -0.39700 -3.77300  12.49300  1.000 34.38399  ? 678 HOH A O      1 
HETATM 5842 O O      . HOH G 4 .   ? 15.72300 -4.05800  -20.61000 1.000 31.69624  ? 679 HOH A O      1 
HETATM 5843 O O      . HOH G 4 .   ? 33.18300 1.24100   23.43500  1.000 29.96850  ? 680 HOH A O      1 
HETATM 5844 O O      . HOH G 4 .   ? 35.77400 13.18300  19.62100  1.000 35.97155  ? 681 HOH A O      1 
HETATM 5845 O O      . HOH G 4 .   ? 40.62200 -10.66700 -12.11100 1.000 35.24924  ? 682 HOH A O      1 
HETATM 5846 O O      . HOH G 4 .   ? 26.48000 15.79200  -6.83600  1.000 43.92896  ? 683 HOH A O      1 
HETATM 5847 O O      . HOH G 4 .   ? 27.49000 3.47700   -17.10300 1.000 37.82182  ? 684 HOH A O      1 
HETATM 5848 O O      . HOH G 4 .   ? 21.66600 -18.49000 -14.17300 1.000 33.32953  ? 685 HOH A O      1 
HETATM 5849 O O      . HOH G 4 .   ? -4.42100 -13.44200 7.32500   1.000 54.51834  ? 686 HOH A O      1 
HETATM 5850 O O      . HOH G 4 .   ? 0.91500  4.06600   -9.96600  1.000 41.48223  ? 687 HOH A O      1 
HETATM 5851 O O      . HOH G 4 .   ? 32.69000 7.88200   22.45400  1.000 26.59449  ? 688 HOH A O      1 
HETATM 5852 O O      . HOH G 4 .   ? 19.32600 12.88700  16.60600  1.000 28.99363  ? 689 HOH A O      1 
HETATM 5853 O O      . HOH G 4 .   ? 41.52300 3.85000   -9.30400  1.000 40.12087  ? 690 HOH A O      1 
HETATM 5854 O O      . HOH G 4 .   ? 18.24100 19.65700  4.13500   1.000 37.12051  ? 691 HOH A O      1 
HETATM 5855 O O      . HOH G 4 .   ? 33.45000 20.93200  -2.73900  1.000 39.44251  ? 692 HOH A O      1 
HETATM 5856 O O      . HOH G 4 .   ? 23.13000 -23.44300 -5.92600  1.000 42.24477  ? 693 HOH A O      1 
HETATM 5857 O O      . HOH G 4 .   ? 21.44500 13.96800  17.36600  1.000 36.63165  ? 694 HOH A O      1 
HETATM 5858 O O      . HOH G 4 .   ? 24.99100 4.05000   22.80600  1.000 29.52266  ? 695 HOH A O      1 
HETATM 5859 O O      . HOH G 4 .   ? 22.87300 -9.97900  15.09100  1.000 31.91275  ? 696 HOH A O      1 
HETATM 5860 O O      . HOH G 4 .   ? -2.45200 -15.39200 9.42100   1.000 41.41140  ? 697 HOH A O      1 
HETATM 5861 O O      . HOH G 4 .   ? 22.93400 19.41100  11.48700  1.000 40.65939  ? 698 HOH A O      1 
HETATM 5862 O O      . HOH G 4 .   ? 16.35600 -11.38000 16.65800  1.000 39.93497  ? 699 HOH A O      1 
HETATM 5863 O O      . HOH G 4 .   ? 15.48000 -24.35700 7.06300   1.000 39.68690  ? 700 HOH A O      1 
HETATM 5864 O O      . HOH G 4 .   ? 40.44100 13.62500  -6.52300  1.000 35.74801  ? 701 HOH A O      1 
HETATM 5865 O O      . HOH G 4 .   ? -0.32500 -7.20400  -13.48400 1.000 36.65312  ? 702 HOH A O      1 
HETATM 5866 O O      . HOH G 4 .   ? -3.62500 -13.56400 10.21900  1.000 41.66774  ? 703 HOH A O      1 
HETATM 5867 O O      . HOH G 4 .   ? 39.43400 14.78700  7.93600   1.000 40.18239  ? 704 HOH A O      1 
HETATM 5868 O O      . HOH G 4 .   ? 4.06700  6.19200   10.75200  1.000 38.88238  ? 705 HOH A O      1 
HETATM 5869 O O      . HOH G 4 .   ? 33.22800 18.59300  -5.28700  1.000 39.89330  ? 706 HOH A O      1 
HETATM 5870 O O      . HOH G 4 .   ? 42.59700 11.85300  6.69400   1.000 38.07916  ? 707 HOH A O      1 
HETATM 5871 O O      . HOH G 4 .   ? 30.02100 13.13500  23.30900  1.000 32.98746  ? 708 HOH A O      1 
HETATM 5872 O O      . HOH G 4 .   ? 2.29600  0.09800   -16.35300 1.000 40.07259  ? 709 HOH A O      1 
HETATM 5873 O O      . HOH G 4 .   ? 17.38300 -9.25700  25.81700  1.000 35.89473  ? 710 HOH A O      1 
HETATM 5874 O O      . HOH G 4 .   ? 23.776   9.657     26.355    1.000 32.93848  ? 711 HOH A O      1 
HETATM 5875 O O      . HOH G 4 .   ? 29.95700 -10.88800 -12.48500 1.000 28.87584  ? 712 HOH A O      1 
HETATM 5876 O O      . HOH G 4 .   ? 42.39000 7.44300   -7.39100  1.000 38.78765  ? 713 HOH A O      1 
HETATM 5877 O O      . HOH G 4 .   ? 11.46300 -23.62700 2.70400   1.000 32.16338  ? 714 HOH A O      1 
HETATM 5878 O O      . HOH G 4 .   ? 39.33900 18.42200  9.39000   1.000 36.13561  ? 715 HOH A O      1 
HETATM 5879 O O      . HOH G 4 .   ? 31.69400 -7.77000  -6.11400  1.000 25.04904  ? 716 HOH A O      1 
HETATM 5880 O O      . HOH G 4 .   ? 37.55800 -5.48300  17.60700  1.000 42.87482  ? 717 HOH A O      1 
HETATM 5881 O O      . HOH G 4 .   ? 30.60000 0.92100   -15.36800 1.000 25.54226  ? 718 HOH A O      1 
HETATM 5882 O O      . HOH G 4 .   ? 15.09900 -23.53800 11.38100  1.000 40.48990  ? 719 HOH A O      1 
HETATM 5883 O O      . HOH G 4 .   ? 18.90300 -22.02300 9.53500   1.000 33.56711  ? 720 HOH A O      1 
HETATM 5884 O O      . HOH G 4 .   ? 32.77700 5.36300   22.37400  1.000 27.72130  ? 721 HOH A O      1 
HETATM 5885 O O      . HOH G 4 .   ? 31.11200 -11.39700 -9.64100  1.000 35.96681  ? 722 HOH A O      1 
HETATM 5886 O O      . HOH G 4 .   ? 24.93500 -8.58000  14.02300  1.000 36.25411  ? 723 HOH A O      1 
HETATM 5887 O O      . HOH G 4 .   ? 33.370   24.426    -3.568    1.000 39.23397  ? 724 HOH A O      1 
HETATM 5888 O O      . HOH G 4 .   ? 17.20800 -16.12400 -22.30600 1.000 31.56517  ? 725 HOH A O      1 
HETATM 5889 O O      . HOH G 4 .   ? 13.86500 -18.14400 -20.30800 1.000 32.78660  ? 726 HOH A O      1 
HETATM 5890 O O      . HOH G 4 .   ? 3.04700  -14.60300 -6.40300  1.000 31.03519  ? 727 HOH A O      1 
HETATM 5891 O O      . HOH G 4 .   ? 27.50900 14.17100  23.55200  1.000 31.47159  ? 728 HOH A O      1 
HETATM 5892 O O      . HOH G 4 .   ? 14.91200 -9.18400  -23.61000 1.000 35.45519  ? 729 HOH A O      1 
HETATM 5893 O O      . HOH H 4 .   ? 35.83600 -1.71700  -52.68400 1.000 21.07660  ? 501 HOH B O      1 
HETATM 5894 O O      . HOH H 4 .   ? 26.74400 -16.73400 -49.39300 1.000 29.60039  ? 502 HOH B O      1 
HETATM 5895 O O      . HOH H 4 .   ? 48.13000 -12.21300 -61.93800 1.000 58.51707  ? 503 HOH B O      1 
HETATM 5896 O O      . HOH H 4 .   ? 27.73100 -16.04900 -22.90200 1.000 43.53222  ? 504 HOH B O      1 
HETATM 5897 O O      . HOH H 4 .   ? 34.11200 -21.99100 -48.87100 1.000 38.77995  ? 505 HOH B O      1 
HETATM 5898 O O      . HOH H 4 .   ? 30.76700 -10.56800 -58.40700 1.000 27.97262  ? 506 HOH B O      1 
HETATM 5899 O O      . HOH H 4 .   ? 16.72000 -25.28900 -34.92000 1.000 44.44975  ? 507 HOH B O      1 
HETATM 5900 O O      . HOH H 4 .   ? 36.02300 7.66600   -28.03700 1.000 32.98310  ? 508 HOH B O      1 
HETATM 5901 O O      . HOH H 4 .   ? 38.58200 9.57900   -66.17000 1.000 30.69278  ? 509 HOH B O      1 
HETATM 5902 O O      . HOH H 4 .   ? 19.39200 -22.66500 -46.94800 1.000 34.58457  ? 510 HOH B O      1 
HETATM 5903 O O      . HOH H 4 .   ? 47.75000 2.88800   -36.65700 1.000 27.33443  ? 511 HOH B O      1 
HETATM 5904 O O      . HOH H 4 .   ? 54.16900 -8.99700  -47.18300 1.000 42.10164  ? 512 HOH B O      1 
HETATM 5905 O O      . HOH H 4 .   ? 22.44900 3.81500   -52.10300 1.000 31.61990  ? 513 HOH B O      1 
HETATM 5906 O O      . HOH H 4 .   ? 47.25200 4.15900   -40.02000 1.000 23.03494  ? 514 HOH B O      1 
HETATM 5907 O O      . HOH H 4 .   ? 25.21200 -0.10400  -48.07000 1.000 34.45568  ? 515 HOH B O      1 
HETATM 5908 O O      . HOH H 4 .   ? 41.40600 -13.00300 -22.04800 1.000 37.78121  ? 516 HOH B O      1 
HETATM 5909 O O      . HOH H 4 .   ? 36.51200 18.05100  -33.05700 1.000 33.44575  ? 517 HOH B O      1 
HETATM 5910 O O      . HOH H 4 .   ? 53.67300 -7.21000  -41.00000 1.000 33.70246  ? 518 HOH B O      1 
HETATM 5911 O O      . HOH H 4 .   ? 45.66700 -6.61900  -29.47700 1.000 23.94138  ? 519 HOH B O      1 
HETATM 5912 O O      . HOH H 4 .   ? 31.12000 -9.84500  -42.85200 1.000 22.50124  ? 520 HOH B O      1 
HETATM 5913 O O      . HOH H 4 .   ? 42.34700 -7.24400  -28.12800 1.000 24.56891  ? 521 HOH B O      1 
HETATM 5914 O O      . HOH H 4 .   ? 36.36700 8.38700   -60.12800 1.000 26.65976  ? 522 HOH B O      1 
HETATM 5915 O O      . HOH H 4 .   ? 23.95400 -0.74300  -49.90300 1.000 25.68351  ? 523 HOH B O      1 
HETATM 5916 O O      . HOH H 4 .   ? 36.62600 10.76700  -53.49800 1.000 20.64897  ? 524 HOH B O      1 
HETATM 5917 O O      . HOH H 4 .   ? 16.30800 -13.53800 -58.41300 1.000 42.73050  ? 525 HOH B O      1 
HETATM 5918 O O      . HOH H 4 .   ? 24.83600 -3.27100  -50.61800 1.000 24.57555  ? 526 HOH B O      1 
HETATM 5919 O O      . HOH H 4 .   ? 20.62300 1.81400   -49.41500 1.000 32.03300  ? 527 HOH B O      1 
HETATM 5920 O O      . HOH H 4 .   ? 34.81000 -3.03600  -50.50300 1.000 26.09378  ? 528 HOH B O      1 
HETATM 5921 O O      . HOH H 4 .   ? 39.48700 2.11600   -48.77800 1.000 21.71152  ? 529 HOH B O      1 
HETATM 5922 O O      . HOH H 4 .   ? 57.26100 4.08900   -44.66300 1.000 42.83846  ? 530 HOH B O      1 
HETATM 5923 O O      . HOH H 4 .   ? 15.33100 -12.51000 -33.34500 1.000 32.37445  ? 531 HOH B O      1 
HETATM 5924 O O      . HOH H 4 .   ? 30.34200 7.70800   -55.72700 1.000 26.80735  ? 532 HOH B O      1 
HETATM 5925 O O      . HOH H 4 .   ? 40.33100 1.10300   -51.55600 1.000 24.27536  ? 533 HOH B O      1 
HETATM 5926 O O      . HOH H 4 .   ? 49.37600 4.48000   -42.03400 1.000 28.47000  ? 534 HOH B O      1 
HETATM 5927 O O      . HOH H 4 .   ? 36.30800 5.60400   -38.42300 1.000 29.51368  ? 535 HOH B O      1 
HETATM 5928 O O      . HOH H 4 .   ? 38.72000 -12.39700 -22.29900 1.000 32.41449  ? 536 HOH B O      1 
HETATM 5929 O O      . HOH H 4 .   ? 33.96600 -23.71700 -40.84500 1.000 34.71872  ? 537 HOH B O      1 
HETATM 5930 O O      . HOH H 4 .   ? 13.16800 -2.86500  -50.87800 1.000 36.71285  ? 538 HOH B O      1 
HETATM 5931 O O      . HOH H 4 .   ? 31.02600 -8.14500  -50.15100 1.000 20.51601  ? 539 HOH B O      1 
HETATM 5932 O O      . HOH H 4 .   ? 47.46000 -9.11600  -32.01400 1.000 40.70923  ? 540 HOH B O      1 
HETATM 5933 O O      . HOH H 4 .   ? 30.12700 -20.27000 -50.78000 1.000 40.14080  ? 541 HOH B O      1 
HETATM 5934 O O      . HOH H 4 .   ? 29.00900 -17.06200 -48.44000 1.000 22.22838  ? 542 HOH B O      1 
HETATM 5935 O O      . HOH H 4 .   ? 30.41800 3.86000   -39.54200 1.000 24.04888  ? 543 HOH B O      1 
HETATM 5936 O O      . HOH H 4 .   ? 30.18300 7.59700   -43.00800 1.000 32.02748  ? 544 HOH B O      1 
HETATM 5937 O O      . HOH H 4 .   ? 36.03300 8.25300   -37.16600 1.000 19.73047  ? 545 HOH B O      1 
HETATM 5938 O O      . HOH H 4 .   ? 18.06500 -6.66800  -27.82100 1.000 37.66271  ? 546 HOH B O      1 
HETATM 5939 O O      . HOH H 4 .   ? 24.39500 -1.41600  -38.16600 1.000 28.34413  ? 547 HOH B O      1 
HETATM 5940 O O      . HOH H 4 .   ? 54.51200 -4.56800  -41.68200 1.000 36.99961  ? 548 HOH B O      1 
HETATM 5941 O O      . HOH H 4 .   ? 23.18000 -11.11500 -62.25400 1.000 34.00739  ? 549 HOH B O      1 
HETATM 5942 O O      . HOH H 4 .   ? 43.76700 -0.80600  -23.17300 1.000 34.58943  ? 550 HOH B O      1 
HETATM 5943 O O      . HOH H 4 .   ? 15.31200 -17.42800 -28.43800 1.000 35.06581  ? 551 HOH B O      1 
HETATM 5944 O O      . HOH H 4 .   ? 18.57600 -18.84400 -25.66900 1.000 38.51708  ? 552 HOH B O      1 
HETATM 5945 O O      . HOH H 4 .   ? 43.47700 8.28200   -19.03600 1.000 40.55290  ? 553 HOH B O      1 
HETATM 5946 O O      . HOH H 4 .   ? 38.84700 -0.16400  -54.41200 1.000 21.71325  ? 554 HOH B O      1 
HETATM 5947 O O      . HOH H 4 .   ? 21.59300 -23.60700 -50.29800 1.000 42.70358  ? 555 HOH B O      1 
HETATM 5948 O O      . HOH H 4 .   ? 12.22900 -9.02300  -36.21000 1.000 37.60309  ? 556 HOH B O      1 
HETATM 5949 O O      . HOH H 4 .   ? 53.26700 14.49500  -46.30000 1.000 36.81433  ? 557 HOH B O      1 
HETATM 5950 O O      . HOH H 4 .   ? 15.80200 -10.44300 -27.34800 1.000 33.29970  ? 558 HOH B O      1 
HETATM 5951 O O      . HOH H 4 .   ? 27.75000 -11.51800 -54.77600 1.000 21.24164  ? 559 HOH B O      1 
HETATM 5952 O O      . HOH H 4 .   ? 20.66900 -24.82700 -44.80200 1.000 28.52505  ? 560 HOH B O      1 
HETATM 5953 O O      . HOH H 4 .   ? 40.12400 1.14600   -46.12400 1.000 19.92722  ? 561 HOH B O      1 
HETATM 5954 O O      . HOH H 4 .   ? 38.252   2.384     -64.347   1.000 32.34518  ? 562 HOH B O      1 
HETATM 5955 O O      . HOH H 4 .   ? 39.99900 17.94700  -52.02300 1.000 29.13248  ? 563 HOH B O      1 
HETATM 5956 O O      . HOH H 4 .   ? 37.62900 -19.99500 -51.60700 1.000 40.20619  ? 564 HOH B O      1 
HETATM 5957 O O      . HOH H 4 .   ? 51.80600 7.66900   -46.05200 1.000 33.25812  ? 565 HOH B O      1 
HETATM 5958 O O      . HOH H 4 .   ? 50.46000 15.77800  -53.70400 1.000 37.31127  ? 566 HOH B O      1 
HETATM 5959 O O      . HOH H 4 .   ? 45.81900 2.65200   -24.78300 1.000 26.08355  ? 567 HOH B O      1 
HETATM 5960 O O      . HOH H 4 .   ? 28.54200 9.02600   -53.91800 1.000 31.50569  ? 568 HOH B O      1 
HETATM 5961 O O      . HOH H 4 .   ? 35.54700 12.38200  -39.46800 1.000 32.53310  ? 569 HOH B O      1 
HETATM 5962 O O      . HOH H 4 .   ? 40.74600 8.37000   -52.17200 1.000 23.42788  ? 570 HOH B O      1 
HETATM 5963 O O      . HOH H 4 .   ? 26.60500 -4.63900  -35.54500 1.000 18.69094  ? 571 HOH B O      1 
HETATM 5964 O O      . HOH H 4 .   ? 48.06500 12.55000  -54.76800 1.000 32.35525  ? 572 HOH B O      1 
HETATM 5965 O O      . HOH H 4 .   ? 31.79100 15.69200  -50.06500 1.000 40.97795  ? 573 HOH B O      1 
HETATM 5966 O O      . HOH H 4 .   ? 55.07800 6.33800   -38.97600 1.000 31.76857  ? 574 HOH B O      1 
HETATM 5967 O O      . HOH H 4 .   ? 51.75800 -14.26100 -37.91100 1.000 44.92246  ? 575 HOH B O      1 
HETATM 5968 O O      . HOH H 4 .   ? 19.465   -26.973   -37.137   1.000 37.20970  ? 576 HOH B O      1 
HETATM 5969 O O      . HOH H 4 .   ? 19.43200 -17.62800 -53.75400 1.000 38.69701  ? 577 HOH B O      1 
HETATM 5970 O O      . HOH H 4 .   ? 31.00100 8.41900   -22.45600 1.000 35.96686  ? 578 HOH B O      1 
HETATM 5971 O O      . HOH H 4 .   ? 19.90500 -5.21000  -43.58400 1.000 16.89614  ? 579 HOH B O      1 
HETATM 5972 O O      . HOH H 4 .   ? 28.98200 -18.16900 -26.63400 1.000 38.08541  ? 580 HOH B O      1 
HETATM 5973 O O      . HOH H 4 .   ? 25.18100 -19.53500 -49.45700 1.000 33.32164  ? 581 HOH B O      1 
HETATM 5974 O O      . HOH H 4 .   ? 56.16700 5.42500   -31.96100 1.000 37.19747  ? 582 HOH B O      1 
HETATM 5975 O O      . HOH H 4 .   ? 45.47600 -3.80400  -62.19200 1.000 37.29695  ? 583 HOH B O      1 
HETATM 5976 O O      . HOH H 4 .   ? 20.24300 -0.42300  -33.46700 1.000 32.79855  ? 584 HOH B O      1 
HETATM 5977 O O      . HOH H 4 .   ? 35.58700 -20.43000 -28.33100 1.000 38.31405  ? 585 HOH B O      1 
HETATM 5978 O O      . HOH H 4 .   ? 46.96000 -19.47800 -45.08900 1.000 28.55346  ? 586 HOH B O      1 
HETATM 5979 O O      . HOH H 4 .   ? 28.58200 -9.11500  -57.90400 1.000 28.26391  ? 587 HOH B O      1 
HETATM 5980 O O      . HOH H 4 .   ? 31.41300 -24.21500 -40.69800 1.000 37.54515  ? 588 HOH B O      1 
HETATM 5981 O O      . HOH H 4 .   ? 37.06300 -11.88100 -59.24500 1.000 25.26046  ? 589 HOH B O      1 
HETATM 5982 O O      . HOH H 4 .   ? 26.85300 1.79000   -32.63400 1.000 28.05349  ? 590 HOH B O      1 
HETATM 5983 O O      . HOH H 4 .   ? 42.56900 -2.87500  -23.13300 1.000 47.08538  ? 591 HOH B O      1 
HETATM 5984 O O      . HOH H 4 .   ? 40.73200 13.86900  -55.49500 1.000 34.08221  ? 592 HOH B O      1 
HETATM 5985 O O      . HOH H 4 .   ? 40.30600 -7.22800  -63.48100 1.000 40.48129  ? 593 HOH B O      1 
HETATM 5986 O O      . HOH H 4 .   ? 29.72200 -5.83000  -51.39700 1.000 23.96802  ? 594 HOH B O      1 
HETATM 5987 O O      . HOH H 4 .   ? 30.10200 -13.01600 -57.70300 1.000 28.33843  ? 595 HOH B O      1 
HETATM 5988 O O      . HOH H 4 .   ? 46.09300 4.65600   -59.30000 1.000 39.99523  ? 596 HOH B O      1 
HETATM 5989 O O      . HOH H 4 .   ? 27.68600 8.39700   -28.92000 1.000 36.03840  ? 597 HOH B O      1 
HETATM 5990 O O      . HOH H 4 .   ? 25.96200 6.46300   -26.94700 1.000 36.26385  ? 598 HOH B O      1 
HETATM 5991 O O      . HOH H 4 .   ? 52.33400 -10.94300 -40.34000 1.000 33.56562  ? 599 HOH B O      1 
HETATM 5992 O O      . HOH H 4 .   ? 32.29900 -13.30400 -21.07300 1.000 31.09878  ? 600 HOH B O      1 
HETATM 5993 O O      . HOH H 4 .   ? 57.27400 -6.27100  -49.10100 1.000 38.09457  ? 601 HOH B O      1 
HETATM 5994 O O      . HOH H 4 .   ? 45.33600 23.27300  -38.73200 1.000 39.04577  ? 602 HOH B O      1 
HETATM 5995 O O      . HOH H 4 .   ? 31.86300 7.42900   -32.90300 1.000 27.50139  ? 603 HOH B O      1 
HETATM 5996 O O      . HOH H 4 .   ? 38.75400 -2.40800  -24.17800 1.000 27.21317  ? 604 HOH B O      1 
HETATM 5997 O O      . HOH H 4 .   ? 25.92500 -1.00900  -54.38600 1.000 23.98786  ? 605 HOH B O      1 
HETATM 5998 O O      . HOH H 4 .   ? 16.39100 -23.83400 -38.87200 1.000 36.54069  ? 606 HOH B O      1 
HETATM 5999 O O      . HOH H 4 .   ? 41.76300 -21.40300 -48.20500 1.000 39.45492  ? 607 HOH B O      1 
HETATM 6000 O O      . HOH H 4 .   ? 43.316   21.693    -47.883   1.000 26.48516  ? 608 HOH B O      1 
HETATM 6001 O O      . HOH H 4 .   ? 31.76300 1.81800   -63.92400 1.000 26.70109  ? 609 HOH B O      1 
HETATM 6002 O O      . HOH H 4 .   ? 48.42400 -16.21400 -35.45000 1.000 41.91425  ? 610 HOH B O      1 
HETATM 6003 O O      . HOH H 4 .   ? 45.31500 10.56600  -52.86000 1.000 24.63979  ? 611 HOH B O      1 
HETATM 6004 O O      . HOH H 4 .   ? 25.92600 7.58400   -59.17400 1.000 40.99121  ? 612 HOH B O      1 
HETATM 6005 O O      . HOH H 4 .   ? 29.07400 10.09000  -58.75700 1.000 31.63167  ? 613 HOH B O      1 
HETATM 6006 O O      . HOH H 4 .   ? 14.19800 -5.18100  -41.59000 1.000 39.62993  ? 614 HOH B O      1 
HETATM 6007 O O      . HOH H 4 .   ? 55.94600 6.38400   -42.45500 1.000 37.12375  ? 615 HOH B O      1 
HETATM 6008 O O      . HOH H 4 .   ? 46.58500 19.30900  -49.79500 1.000 34.48487  ? 616 HOH B O      1 
HETATM 6009 O O      . HOH H 4 .   ? 34.81800 17.10900  -47.33600 1.000 30.40918  ? 617 HOH B O      1 
HETATM 6010 O O      . HOH H 4 .   ? 17.45800 -12.87700 -61.92000 1.000 46.94225  ? 618 HOH B O      1 
HETATM 6011 O O      . HOH H 4 .   ? 51.46900 -12.37300 -56.62100 1.000 35.79271  ? 619 HOH B O      1 
HETATM 6012 O O      . HOH H 4 .   ? 53.21100 -11.21700 -45.01500 1.000 39.92096  ? 620 HOH B O      1 
HETATM 6013 O O      . HOH H 4 .   ? 23.66100 -12.35200 -50.23900 1.000 24.55720  ? 621 HOH B O      1 
HETATM 6014 O O      . HOH H 4 .   ? 10.89000 -1.30900  -51.72600 1.000 29.92717  ? 622 HOH B O      1 
HETATM 6015 O O      . HOH H 4 .   ? 29.20800 -7.65500  -21.48900 1.000 24.76567  ? 623 HOH B O      1 
HETATM 6016 O O      . HOH H 4 .   ? 36.90000 6.95900   -66.00800 1.000 30.12587  ? 624 HOH B O      1 
HETATM 6017 O O      . HOH H 4 .   ? 42.81500 -14.76100 -23.36100 1.000 34.22341  ? 625 HOH B O      1 
HETATM 6018 O O      . HOH H 4 .   ? 26.78100 -12.33300 -18.78200 1.000 32.47241  ? 626 HOH B O      1 
HETATM 6019 O O      . HOH H 4 .   ? 10.98300 -13.61200 -42.79100 1.000 34.06186  ? 627 HOH B O      1 
HETATM 6020 O O      . HOH H 4 .   ? 42.27500 8.99300   -64.57600 1.000 34.23295  ? 628 HOH B O      1 
HETATM 6021 O O      . HOH H 4 .   ? 38.71100 -3.85600  -20.03800 1.000 34.75197  ? 629 HOH B O      1 
HETATM 6022 O O      . HOH H 4 .   ? 12.38600 -9.69300  -54.67000 1.000 31.86375  ? 630 HOH B O      1 
HETATM 6023 O O      . HOH H 4 .   ? 30.45700 -6.90300  -57.35600 1.000 23.31031  ? 631 HOH B O      1 
HETATM 6024 O O      . HOH H 4 .   ? 27.89300 -8.01600  -60.60300 1.000 27.61823  ? 632 HOH B O      1 
HETATM 6025 O O      . HOH H 4 .   ? 50.56800 -13.31800 -43.43900 1.000 33.79033  ? 633 HOH B O      1 
HETATM 6026 O O      . HOH H 4 .   ? 36.37300 -20.21900 -54.62600 1.000 41.52469  ? 634 HOH B O      1 
HETATM 6027 O O      . HOH H 4 .   ? 27.10600 -6.96700  -40.68000 1.000 25.09955  ? 635 HOH B O      1 
HETATM 6028 O O      . HOH H 4 .   ? 15.26600 -5.73400  -57.12000 1.000 35.41157  ? 636 HOH B O      1 
HETATM 6029 O O      . HOH H 4 .   ? 28.31500 -9.21200  -42.36700 1.000 25.28819  ? 637 HOH B O      1 
HETATM 6030 O O      . HOH H 4 .   ? 51.12600 -17.43600 -41.04600 1.000 42.21923  ? 638 HOH B O      1 
HETATM 6031 O O      . HOH H 4 .   ? 31.15300 -6.07200  -59.74800 1.000 24.66665  ? 639 HOH B O      1 
HETATM 6032 O O      . HOH H 4 .   ? 7.135    -8.504    -47.327   1.000 42.62013  ? 640 HOH B O      1 
HETATM 6033 O O      . HOH H 4 .   ? 45.06400 -6.83400  -61.01500 1.000 36.66992  ? 641 HOH B O      1 
HETATM 6034 O O      . HOH H 4 .   ? 32.50500 -22.23400 -35.77900 1.000 28.44513  ? 642 HOH B O      1 
HETATM 6035 O O      . HOH H 4 .   ? 13.31900 -19.34200 -38.47700 1.000 37.64857  ? 643 HOH B O      1 
HETATM 6036 O O      . HOH H 4 .   ? 38.95400 -14.17700 -59.64000 1.000 36.56547  ? 644 HOH B O      1 
HETATM 6037 O O      . HOH H 4 .   ? 36.64700 -3.15900  -16.88600 1.000 28.95144  ? 645 HOH B O      1 
HETATM 6038 O O      . HOH H 4 .   ? 56.20800 0.65200   -50.76400 1.000 34.27848  ? 646 HOH B O      1 
HETATM 6039 O O      . HOH H 4 .   ? 40.53000 18.58000  -34.61800 1.000 35.78364  ? 647 HOH B O      1 
HETATM 6040 O O      . HOH H 4 .   ? 22.11800 -19.95100 -27.82100 1.000 42.02676  ? 648 HOH B O      1 
HETATM 6041 O O      . HOH H 4 .   ? 39.91700 0.94900   -61.09600 1.000 22.88636  ? 649 HOH B O      1 
HETATM 6042 O O      . HOH H 4 .   ? 18.09400 -4.18700  -20.64300 1.000 31.49168  ? 650 HOH B O      1 
HETATM 6043 O O      . HOH H 4 .   ? 37.29400 10.64300  -41.08900 1.000 24.29286  ? 651 HOH B O      1 
HETATM 6044 O O      . HOH H 4 .   ? 51.27300 7.70700   -55.12700 1.000 37.99294  ? 652 HOH B O      1 
HETATM 6045 O O      . HOH H 4 .   ? 23.21200 3.08900   -48.27800 1.000 38.13931  ? 653 HOH B O      1 
HETATM 6046 O O      . HOH H 4 .   ? 36.68200 11.99100  -27.87700 1.000 40.70513  ? 654 HOH B O      1 
HETATM 6047 O O      . HOH H 4 .   ? 49.02000 8.89000   -43.60300 1.000 29.17082  ? 655 HOH B O      1 
HETATM 6048 O O      . HOH H 4 .   ? 25.67200 -16.82900 -27.90700 1.000 40.23364  ? 656 HOH B O      1 
HETATM 6049 O O      . HOH H 4 .   ? 16.67000 -6.61600  -49.06000 1.000 27.46584  ? 657 HOH B O      1 
HETATM 6050 O O      . HOH H 4 .   ? 46.95000 -3.08800  -24.23600 1.000 35.83578  ? 658 HOH B O      1 
HETATM 6051 O O      . HOH H 4 .   ? 30.41000 -0.52900  -63.46800 1.000 24.65480  ? 659 HOH B O      1 
HETATM 6052 O O      . HOH H 4 .   ? 26.12200 -15.27700 -63.19600 1.000 36.96852  ? 660 HOH B O      1 
HETATM 6053 O O      . HOH H 4 .   ? 13.45100 -15.82400 -40.70100 1.000 27.63163  ? 661 HOH B O      1 
HETATM 6054 O O      . HOH H 4 .   ? 22.68400 -15.62200 -34.93900 1.000 23.27697  ? 662 HOH B O      1 
HETATM 6055 O O      . HOH H 4 .   ? 31.48300 -23.29000 -47.91600 1.000 34.25404  ? 663 HOH B O      1 
HETATM 6056 O O      . HOH H 4 .   ? 24.97700 -18.01000 -24.21700 1.000 45.41575  ? 664 HOH B O      1 
HETATM 6057 O O      . HOH H 4 .   ? 43.94900 22.58500  -33.46600 1.000 47.82716  ? 665 HOH B O      1 
HETATM 6058 O O      . HOH H 4 .   ? 30.05600 4.71000   -61.53900 1.000 33.04361  ? 666 HOH B O      1 
HETATM 6059 O O      . HOH H 4 .   ? 44.67300 -0.26800  -61.67200 1.000 29.37901  ? 667 HOH B O      1 
HETATM 6060 O O      . HOH H 4 .   ? 13.44500 -20.05800 -46.56900 1.000 36.81890  ? 668 HOH B O      1 
HETATM 6061 O O      . HOH H 4 .   ? 56.83000 -1.95400  -39.25600 1.000 46.69797  ? 669 HOH B O      1 
HETATM 6062 O O      . HOH H 4 .   ? 28.84400 14.51500  -48.02300 1.000 46.04743  ? 670 HOH B O      1 
HETATM 6063 O O      . HOH H 4 .   ? 17.22200 -12.45300 -24.65800 1.000 31.24960  ? 671 HOH B O      1 
HETATM 6064 O O      . HOH H 4 .   ? 40.62900 17.33000  -37.52900 1.000 33.88072  ? 672 HOH B O      1 
HETATM 6065 O O      . HOH H 4 .   ? 30.48800 -1.84200  -19.25600 1.000 24.01558  ? 673 HOH B O      1 
HETATM 6066 O O      . HOH H 4 .   ? 25.42600 5.77000   -32.85100 1.000 41.59884  ? 674 HOH B O      1 
HETATM 6067 O O      . HOH H 4 .   ? 24.77100 0.62500   -52.36700 1.000 24.54843  ? 675 HOH B O      1 
HETATM 6068 O O      . HOH H 4 .   ? 51.13600 10.28700  -43.18200 1.000 28.55249  ? 676 HOH B O      1 
HETATM 6069 O O      . HOH H 4 .   ? 17.08300 -8.02000  -57.61700 1.000 31.75020  ? 677 HOH B O      1 
HETATM 6070 O O      . HOH H 4 .   ? 40.27900 -19.90800 -57.78600 1.000 34.24793  ? 678 HOH B O      1 
HETATM 6071 O O      . HOH H 4 .   ? 27.19200 7.96400   -40.53300 1.000 51.48301  ? 679 HOH B O      1 
HETATM 6072 O O      . HOH H 4 .   ? 12.03800 -21.65800 -38.72700 1.000 47.05160  ? 680 HOH B O      1 
HETATM 6073 O O      . HOH H 4 .   ? 44.22900 -18.48200 -31.00200 1.000 28.74240  ? 681 HOH B O      1 
HETATM 6074 O O      . HOH H 4 .   ? 37.00000 13.79800  -56.97400 1.000 33.46245  ? 682 HOH B O      1 
HETATM 6075 O O      . HOH H 4 .   ? 50.64900 -11.77500 -38.79700 1.000 37.35589  ? 683 HOH B O      1 
HETATM 6076 O O      . HOH H 4 .   ? 29.34700 4.55200   -59.07900 1.000 24.08104  ? 684 HOH B O      1 
HETATM 6077 O O      . HOH H 4 .   ? 56.57500 0.29300   -34.93500 1.000 38.29295  ? 685 HOH B O      1 
HETATM 6078 O O      . HOH H 4 .   ? 31.50100 -17.28100 -26.72400 1.000 36.26209  ? 686 HOH B O      1 
HETATM 6079 O O      . HOH H 4 .   ? 28.928   3.450     -63.502   1.000 25.08394  ? 687 HOH B O      1 
HETATM 6080 O O      . HOH H 4 .   ? 48.79500 24.29100  -36.57500 1.000 49.05194  ? 688 HOH B O      1 
HETATM 6081 O O      . HOH H 4 .   ? 29.57700 2.91800   -18.72800 1.000 34.56577  ? 689 HOH B O      1 
HETATM 6082 O O      . HOH H 4 .   ? 20.04600 -15.06600 -24.04800 1.000 25.20816  ? 690 HOH B O      1 
HETATM 6083 O O      . HOH H 4 .   ? 43.91200 13.32200  -61.37400 1.000 31.48566  ? 691 HOH B O      1 
HETATM 6084 O O      . HOH H 4 .   ? 47.38600 -5.97900  -57.70300 1.000 35.54491  ? 692 HOH B O      1 
HETATM 6085 O O      . HOH H 4 .   ? 54.32200 -5.56500  -55.49900 1.000 31.02794  ? 693 HOH B O      1 
HETATM 6086 O O      . HOH H 4 .   ? 20.474   -0.771    -63.893   1.000 35.04821  ? 694 HOH B O      1 
HETATM 6087 O O      . HOH H 4 .   ? 40.72700 -23.87600 -31.87700 1.000 43.80180  ? 695 HOH B O      1 
HETATM 6088 O O      . HOH H 4 .   ? 32.78600 5.60200   -62.45100 1.000 25.91010  ? 696 HOH B O      1 
HETATM 6089 O O      . HOH H 4 .   ? 16.31000 -5.74100  -23.60000 1.000 30.73251  ? 697 HOH B O      1 
HETATM 6090 O O      . HOH H 4 .   ? 28.39900 -18.61300 -52.48700 1.000 38.13935  ? 698 HOH B O      1 
HETATM 6091 O O      . HOH H 4 .   ? 26.90100 -9.11500  -20.61100 1.000 32.39185  ? 699 HOH B O      1 
HETATM 6092 O O      . HOH H 4 .   ? 39.78100 -20.63100 -52.07100 1.000 39.88291  ? 700 HOH B O      1 
HETATM 6093 O O      . HOH H 4 .   ? 57.92500 -5.84400  -46.22800 1.000 40.78518  ? 701 HOH B O      1 
HETATM 6094 O O      . HOH H 4 .   ? 18.17800 -7.31700  -24.99400 1.000 31.17068  ? 702 HOH B O      1 
HETATM 6095 O O      . HOH H 4 .   ? 47.03200 -19.85900 -40.69000 1.000 43.70081  ? 703 HOH B O      1 
HETATM 6096 O O      . HOH H 4 .   ? 30.99200 0.68400   -17.99400 1.000 28.68887  ? 704 HOH B O      1 
HETATM 6097 O O      . HOH H 4 .   ? 23.04600 -25.22300 -49.18400 1.000 33.22792  ? 705 HOH B O      1 
HETATM 6098 O O      . HOH H 4 .   ? 41.06700 -17.80600 -59.83100 1.000 35.36768  ? 706 HOH B O      1 
HETATM 6099 O O      . HOH H 4 .   ? 25.42500 5.58600   -53.58100 1.000 33.65974  ? 707 HOH B O      1 
HETATM 6100 O O      . HOH H 4 .   ? 20.49400 -20.81100 -26.26400 1.000 34.89016  ? 708 HOH B O      1 
HETATM 6101 O O      . HOH H 4 .   ? 35.03400 -19.50300 -50.16900 1.000 34.85680  ? 709 HOH B O      1 
HETATM 6102 O O      . HOH H 4 .   ? 32.29800 -10.91700 -20.10700 1.000 36.13578  ? 710 HOH B O      1 
HETATM 6103 O O      . HOH H 4 .   ? 44.931   20.988    -51.232   1.000 44.43279  ? 711 HOH B O      1 
HETATM 6104 O O      . HOH H 4 .   ? 28.29300 5.91500   -28.98100 1.000 41.50593  ? 712 HOH B O      1 
HETATM 6105 O O      . HOH H 4 .   ? 34.95800 -23.14700 -35.51700 1.000 38.14282  ? 713 HOH B O      1 
HETATM 6106 O O      . HOH H 4 .   ? 11.41400 6.59600   -56.57600 1.000 54.01466  ? 714 HOH B O      1 
HETATM 6107 O O      . HOH H 4 .   ? 24.33500 -8.58000  -22.08400 1.000 34.35346  ? 715 HOH B O      1 
HETATM 6108 O O      . HOH H 4 .   ? 34.20300 6.63500   -26.00700 1.000 40.96997  ? 716 HOH B O      1 
HETATM 6109 O O      . HOH H 4 .   ? 29.60100 14.13600  -45.68400 1.000 38.56077  ? 717 HOH B O      1 
HETATM 6110 O O      . HOH H 4 .   ? 24.76000 -19.66500 -51.85100 1.000 41.53918  ? 718 HOH B O      1 
HETATM 6111 O O      . HOH H 4 .   ? 45.38100 -14.29400 -23.14000 1.000 38.84733  ? 719 HOH B O      1 
HETATM 6112 O O      . HOH H 4 .   ? 12.23700 -3.29200  -40.29900 1.000 43.20976  ? 720 HOH B O      1 
HETATM 6113 O O      . HOH H 4 .   ? 24.58600 -19.91800 -27.70100 1.000 42.28533  ? 721 HOH B O      1 
HETATM 6114 O O      . HOH H 4 .   ? 58.83200 -5.31000  -51.23300 1.000 36.48135  ? 722 HOH B O      1 
HETATM 6115 O O      . HOH H 4 .   ? 57.12300 -7.96100  -45.00100 1.000 35.76836  ? 723 HOH B O      1 
HETATM 6116 O O      . HOH H 4 .   ? 24.66800 -14.48600 -18.60600 1.000 33.28254  ? 724 HOH B O      1 
HETATM 6117 O O      . HOH H 4 .   ? 29.23700 -13.66000 -18.20600 1.000 35.63682  ? 725 HOH B O      1 
HETATM 6118 O O      . HOH H 4 .   ? 19.92800 -19.78500 -54.98900 1.000 42.31126  ? 726 HOH B O      1 
HETATM 6119 O O      . HOH H 4 .   ? 57.536   -2.760    -52.739   1.000 40.53765  ? 727 HOH B O      1 
HETATM 6120 O O      . HOH H 4 .   ? 53.92500 12.23400  -46.35600 1.000 41.24477  ? 728 HOH B O      1 
HETATM 6121 O O      . HOH H 4 .   ? 28.76800 6.42300   -57.62500 1.000 27.22306  ? 729 HOH B O      1 
HETATM 6122 O O      . HOH H 4 .   ? 19.25800 -17.59100 -23.24800 1.000 33.87401  ? 730 HOH B O      1 
HETATM 6123 O O      . HOH H 4 .   ? 53.89300 -11.56400 -55.85200 1.000 40.20802  ? 731 HOH B O      1 
HETATM 6124 O O      . HOH H 4 .   ? 17.03200 -9.81300  -24.70400 1.000 35.52971  ? 732 HOH B O      1 
HETATM 6125 O O      . HOH H 4 .   ? 25.55900 3.09300   -52.16300 1.000 37.15508  ? 733 HOH B O      1 
HETATM 6126 O O      . HOH H 4 .   ? 26.91000 6.78000   -55.40600 1.000 30.25168  ? 734 HOH B O      1 
HETATM 6127 O O      . HOH H 4 .   ? 42.25700 19.29900  -37.97600 1.000 35.38379  ? 735 HOH B O      1 
HETATM 6128 O O      . HOH H 4 .   ? 29.00400 -5.50900  -60.65700 1.000 24.43690  ? 736 HOH B O      1 
HETATM 6129 O O      . HOH H 4 .   ? 12.90900 8.48500   -55.77800 1.000 47.70511  ? 737 HOH B O      1 
HETATM 6130 O O      . HOH H 4 .   ? 26.79600 3.90700   -30.72700 1.000 37.42919  ? 738 HOH B O      1 
HETATM 6131 O O      . HOH H 4 .   ? 14.73100 -13.66600 -24.50000 1.000 30.88487  ? 739 HOH B O      1 
HETATM 6132 O O      . HOH H 4 .   ? 43.50700 11.61900  -63.77600 1.000 29.98239  ? 740 HOH B O      1 
HETATM 6133 O O      . HOH H 4 .   ? 56.58600 -4.61500  -54.88200 1.000 33.37040  ? 741 HOH B O      1 
HETATM 6134 O O      . HOH H 4 .   ? 47.55600 -20.32100 -42.96500 1.000 37.99224  ? 742 HOH B O      1 
HETATM 6135 O O      . HOH H 4 .   ? 55.15300 8.80900   -43.60700 1.000 37.55172  ? 743 HOH B O      1 
HETATM 6136 O O      . HOH H 4 .   ? 46.47200 13.88100  -61.05000 1.000 38.21352  ? 744 HOH B O      1 
HETATM 6137 O O      . HOH H 4 .   ? 14.71700 -15.71300 -23.40500 1.000 34.46870  ? 745 HOH B O      1 
HETATM 6138 O O      . HOH H 4 .   ? 53.18200 10.25700  -44.76300 1.000 34.44722  ? 746 HOH B O      1 
HETATM 6139 O O      . HOH H 4 .   ? 13.21800 -8.04200  -24.76300 1.000 40.78600  ? 747 HOH B O      1 
HETATM 6140 O O      . HOH H 4 .   ? 28.76200 7.48600   -62.00900 1.000 31.69483  ? 748 HOH B O      1 
HETATM 6141 O O      . HOH H 4 .   ? 36.70600 -23.78600 -21.72300 1.000 41.84132  ? 749 HOH B O      1 
HETATM 6142 O O      . HOH H 4 .   ? 54.72400 13.67000  -50.41800 1.000 51.02914  ? 750 HOH B O      1 
# 
