data_8Z63
# 
_entry.id   8Z63 
# 
_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   8Z63         pdb_00008z63 10.2210/pdb8z63/pdb 
WWPDB D_1300046473 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_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                        8Z63 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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              bailiping@caas.cn 
_pdbx_contact_author.name_first         Liping 
_pdbx_contact_author.name_last          Bai 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2146-6526 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhao, P.' 1 0009-0002-2347-9256 
'Bai, L.'  2 0000-0002-2146-6526 
'Wang, S.' 3 0000-0003-1417-2041 
# 
_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                     
;Study on the function and diversity of key enzymes degrading fucoidan in                        
Kiritimatiellaeota
;
_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 'Zhao, P.' 1 0009-0002-2347-9256 
primary 'Bai, L.'  2 0000-0002-2146-6526 
# 
_entity.id                         1 
_entity.type                       polymer 
_entity.src_method                 man 
_entity.pdbx_description           Alpha-L-fucosidase 
_entity.formula_weight             42337.754 
_entity.pdbx_number_of_molecules   2 
_entity.pdbx_ec                    ? 
_entity.pdbx_mutation              ? 
_entity.pdbx_fragment              ? 
_entity.details                    ? 
# 
_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       
;MPIQNINRRSLLCSGAATTAALAVSPSVFGDSAVPSYLKDYAALYKKDPRAAALQYFKEAKFGLFIHYGLYSLLGRGEWV
QLQGKIPVREYAKLENDFTAKNFDADFITDMALEAGMKYVNITTRHHDSFCLFESKYTDFTSTNSPAKRDLVAELAEECR
KKGLGFYLYYSHGRDWRHPHAPNNGDWGGNARPKYDSPEPFYKYGEDQDLQIYVEFMKNQITELLTNYGPVGGIWLDGVA
TPASRKGKLHLFETQELYDHIHSLQPQVLVSYKQGLIGTEDFKAPERHFKGTSDVPLEFCDTLQPWKWGYDKSLDGKHKT
ADQVMEMLSKANKMDANLLLNVGPLPDGSIHPEDVKTLAEVGRKLKAHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPIQNINRRSLLCSGAATTAALAVSPSVFGDSAVPSYLKDYAALYKKDPRAAALQYFKEAKFGLFIHYGLYSLLGRGEWV
QLQGKIPVREYAKLENDFTAKNFDADFITDMALEAGMKYVNITTRHHDSFCLFESKYTDFTSTNSPAKRDLVAELAEECR
KKGLGFYLYYSHGRDWRHPHAPNNGDWGGNARPKYDSPEPFYKYGEDQDLQIYVEFMKNQITELLTNYGPVGGIWLDGVA
TPASRKGKLHLFETQELYDHIHSLQPQVLVSYKQGLIGTEDFKAPERHFKGTSDVPLEFCDTLQPWKWGYDKSLDGKHKT
ADQVMEMLSKANKMDANLLLNVGPLPDGSIHPEDVKTLAEVGRKLKAHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
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   PRO n 
1 3   ILE n 
1 4   GLN n 
1 5   ASN n 
1 6   ILE n 
1 7   ASN n 
1 8   ARG n 
1 9   ARG n 
1 10  SER n 
1 11  LEU n 
1 12  LEU n 
1 13  CYS n 
1 14  SER n 
1 15  GLY n 
1 16  ALA n 
1 17  ALA n 
1 18  THR n 
1 19  THR n 
1 20  ALA n 
1 21  ALA n 
1 22  LEU n 
1 23  ALA n 
1 24  VAL n 
1 25  SER n 
1 26  PRO n 
1 27  SER n 
1 28  VAL n 
1 29  PHE n 
1 30  GLY n 
1 31  ASP n 
1 32  SER n 
1 33  ALA n 
1 34  VAL n 
1 35  PRO n 
1 36  SER n 
1 37  TYR n 
1 38  LEU n 
1 39  LYS n 
1 40  ASP n 
1 41  TYR n 
1 42  ALA n 
1 43  ALA n 
1 44  LEU n 
1 45  TYR n 
1 46  LYS n 
1 47  LYS n 
1 48  ASP n 
1 49  PRO n 
1 50  ARG n 
1 51  ALA n 
1 52  ALA n 
1 53  ALA n 
1 54  LEU n 
1 55  GLN n 
1 56  TYR n 
1 57  PHE n 
1 58  LYS n 
1 59  GLU n 
1 60  ALA n 
1 61  LYS n 
1 62  PHE n 
1 63  GLY n 
1 64  LEU n 
1 65  PHE n 
1 66  ILE n 
1 67  HIS n 
1 68  TYR n 
1 69  GLY n 
1 70  LEU n 
1 71  TYR n 
1 72  SER n 
1 73  LEU n 
1 74  LEU n 
1 75  GLY n 
1 76  ARG n 
1 77  GLY n 
1 78  GLU n 
1 79  TRP n 
1 80  VAL n 
1 81  GLN n 
1 82  LEU n 
1 83  GLN n 
1 84  GLY n 
1 85  LYS n 
1 86  ILE n 
1 87  PRO n 
1 88  VAL n 
1 89  ARG n 
1 90  GLU n 
1 91  TYR n 
1 92  ALA n 
1 93  LYS n 
1 94  LEU n 
1 95  GLU n 
1 96  ASN n 
1 97  ASP n 
1 98  PHE n 
1 99  THR n 
1 100 ALA n 
1 101 LYS n 
1 102 ASN n 
1 103 PHE n 
1 104 ASP n 
1 105 ALA n 
1 106 ASP n 
1 107 PHE n 
1 108 ILE n 
1 109 THR n 
1 110 ASP n 
1 111 MET n 
1 112 ALA n 
1 113 LEU n 
1 114 GLU n 
1 115 ALA n 
1 116 GLY n 
1 117 MET n 
1 118 LYS n 
1 119 TYR n 
1 120 VAL n 
1 121 ASN n 
1 122 ILE n 
1 123 THR n 
1 124 THR n 
1 125 ARG n 
1 126 HIS n 
1 127 HIS n 
1 128 ASP n 
1 129 SER n 
1 130 PHE n 
1 131 CYS n 
1 132 LEU n 
1 133 PHE n 
1 134 GLU n 
1 135 SER n 
1 136 LYS n 
1 137 TYR n 
1 138 THR n 
1 139 ASP n 
1 140 PHE n 
1 141 THR n 
1 142 SER n 
1 143 THR n 
1 144 ASN n 
1 145 SER n 
1 146 PRO n 
1 147 ALA n 
1 148 LYS n 
1 149 ARG n 
1 150 ASP n 
1 151 LEU n 
1 152 VAL n 
1 153 ALA n 
1 154 GLU n 
1 155 LEU n 
1 156 ALA n 
1 157 GLU n 
1 158 GLU n 
1 159 CYS n 
1 160 ARG n 
1 161 LYS n 
1 162 LYS n 
1 163 GLY n 
1 164 LEU n 
1 165 GLY n 
1 166 PHE n 
1 167 TYR n 
1 168 LEU n 
1 169 TYR n 
1 170 TYR n 
1 171 SER n 
1 172 HIS n 
1 173 GLY n 
1 174 ARG n 
1 175 ASP n 
1 176 TRP n 
1 177 ARG n 
1 178 HIS n 
1 179 PRO n 
1 180 HIS n 
1 181 ALA n 
1 182 PRO n 
1 183 ASN n 
1 184 ASN n 
1 185 GLY n 
1 186 ASP n 
1 187 TRP n 
1 188 GLY n 
1 189 GLY n 
1 190 ASN n 
1 191 ALA n 
1 192 ARG n 
1 193 PRO n 
1 194 LYS n 
1 195 TYR n 
1 196 ASP n 
1 197 SER n 
1 198 PRO n 
1 199 GLU n 
1 200 PRO n 
1 201 PHE n 
1 202 TYR n 
1 203 LYS n 
1 204 TYR n 
1 205 GLY n 
1 206 GLU n 
1 207 ASP n 
1 208 GLN n 
1 209 ASP n 
1 210 LEU n 
1 211 GLN n 
1 212 ILE n 
1 213 TYR n 
1 214 VAL n 
1 215 GLU n 
1 216 PHE n 
1 217 MET n 
1 218 LYS n 
1 219 ASN n 
1 220 GLN n 
1 221 ILE n 
1 222 THR n 
1 223 GLU n 
1 224 LEU n 
1 225 LEU n 
1 226 THR n 
1 227 ASN n 
1 228 TYR n 
1 229 GLY n 
1 230 PRO n 
1 231 VAL n 
1 232 GLY n 
1 233 GLY n 
1 234 ILE n 
1 235 TRP n 
1 236 LEU n 
1 237 ASP n 
1 238 GLY n 
1 239 VAL n 
1 240 ALA n 
1 241 THR n 
1 242 PRO n 
1 243 ALA n 
1 244 SER n 
1 245 ARG n 
1 246 LYS n 
1 247 GLY n 
1 248 LYS n 
1 249 LEU n 
1 250 HIS n 
1 251 LEU n 
1 252 PHE n 
1 253 GLU n 
1 254 THR n 
1 255 GLN n 
1 256 GLU n 
1 257 LEU n 
1 258 TYR n 
1 259 ASP n 
1 260 HIS n 
1 261 ILE n 
1 262 HIS n 
1 263 SER n 
1 264 LEU n 
1 265 GLN n 
1 266 PRO n 
1 267 GLN n 
1 268 VAL n 
1 269 LEU n 
1 270 VAL n 
1 271 SER n 
1 272 TYR n 
1 273 LYS n 
1 274 GLN n 
1 275 GLY n 
1 276 LEU n 
1 277 ILE n 
1 278 GLY n 
1 279 THR n 
1 280 GLU n 
1 281 ASP n 
1 282 PHE n 
1 283 LYS n 
1 284 ALA n 
1 285 PRO n 
1 286 GLU n 
1 287 ARG n 
1 288 HIS n 
1 289 PHE n 
1 290 LYS n 
1 291 GLY n 
1 292 THR n 
1 293 SER n 
1 294 ASP n 
1 295 VAL n 
1 296 PRO n 
1 297 LEU n 
1 298 GLU n 
1 299 PHE n 
1 300 CYS n 
1 301 ASP n 
1 302 THR n 
1 303 LEU n 
1 304 GLN n 
1 305 PRO n 
1 306 TRP n 
1 307 LYS n 
1 308 TRP n 
1 309 GLY n 
1 310 TYR n 
1 311 ASP n 
1 312 LYS n 
1 313 SER n 
1 314 LEU n 
1 315 ASP n 
1 316 GLY n 
1 317 LYS n 
1 318 HIS n 
1 319 LYS n 
1 320 THR n 
1 321 ALA n 
1 322 ASP n 
1 323 GLN n 
1 324 VAL n 
1 325 MET n 
1 326 GLU n 
1 327 MET n 
1 328 LEU n 
1 329 SER n 
1 330 LYS n 
1 331 ALA n 
1 332 ASN n 
1 333 LYS n 
1 334 MET n 
1 335 ASP n 
1 336 ALA n 
1 337 ASN n 
1 338 LEU n 
1 339 LEU n 
1 340 LEU n 
1 341 ASN n 
1 342 VAL n 
1 343 GLY n 
1 344 PRO n 
1 345 LEU n 
1 346 PRO n 
1 347 ASP n 
1 348 GLY n 
1 349 SER n 
1 350 ILE n 
1 351 HIS n 
1 352 PRO n 
1 353 GLU n 
1 354 ASP n 
1 355 VAL n 
1 356 LYS n 
1 357 THR n 
1 358 LEU n 
1 359 ALA n 
1 360 GLU n 
1 361 VAL n 
1 362 GLY n 
1 363 ARG n 
1 364 LYS n 
1 365 LEU n 
1 366 LYS n 
1 367 ALA n 
1 368 HIS n 
1 369 HIS n 
1 370 HIS n 
1 371 HIS n 
1 372 HIS n 
1 373 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   373 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SCARR_01449 
_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      'Pontiella sulfatireligans' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2750658 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
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 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   ILE 3   3   ?   ?   ?   A . n 
A 1 4   GLN 4   4   ?   ?   ?   A . n 
A 1 5   ASN 5   5   ?   ?   ?   A . n 
A 1 6   ILE 6   6   ?   ?   ?   A . n 
A 1 7   ASN 7   7   ?   ?   ?   A . n 
A 1 8   ARG 8   8   ?   ?   ?   A . n 
A 1 9   ARG 9   9   ?   ?   ?   A . n 
A 1 10  SER 10  10  ?   ?   ?   A . n 
A 1 11  LEU 11  11  ?   ?   ?   A . n 
A 1 12  LEU 12  12  ?   ?   ?   A . n 
A 1 13  CYS 13  13  ?   ?   ?   A . n 
A 1 14  SER 14  14  ?   ?   ?   A . n 
A 1 15  GLY 15  15  ?   ?   ?   A . n 
A 1 16  ALA 16  16  ?   ?   ?   A . n 
A 1 17  ALA 17  17  ?   ?   ?   A . n 
A 1 18  THR 18  18  ?   ?   ?   A . n 
A 1 19  THR 19  19  ?   ?   ?   A . n 
A 1 20  ALA 20  20  ?   ?   ?   A . n 
A 1 21  ALA 21  21  ?   ?   ?   A . n 
A 1 22  LEU 22  22  ?   ?   ?   A . n 
A 1 23  ALA 23  23  ?   ?   ?   A . n 
A 1 24  VAL 24  24  ?   ?   ?   A . n 
A 1 25  SER 25  25  ?   ?   ?   A . n 
A 1 26  PRO 26  26  ?   ?   ?   A . n 
A 1 27  SER 27  27  ?   ?   ?   A . n 
A 1 28  VAL 28  28  ?   ?   ?   A . n 
A 1 29  PHE 29  29  ?   ?   ?   A . n 
A 1 30  GLY 30  30  ?   ?   ?   A . n 
A 1 31  ASP 31  31  ?   ?   ?   A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  TYR 41  41  41  TYR TYR A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  TYR 45  45  45  TYR TYR A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  TYR 56  56  56  TYR TYR A . n 
A 1 57  PHE 57  57  57  PHE PHE A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  GLU 59  59  59  GLU GLU A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  PHE 62  62  62  PHE PHE A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  PHE 65  65  65  PHE PHE A . n 
A 1 66  ILE 66  66  66  ILE ILE A . n 
A 1 67  HIS 67  67  67  HIS HIS A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  TRP 79  79  79  TRP TRP A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  ILE 86  86  86  ILE ILE A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  GLU 95  95  95  GLU GLU A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 ASP 106 106 106 ASP ASP A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 MET 111 111 111 MET MET A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 TYR 119 119 119 TYR TYR A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 ASN 121 121 121 ASN ASN A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 THR 124 124 124 THR THR A . n 
A 1 125 ARG 125 125 125 ARG ARG A . n 
A 1 126 HIS 126 126 126 HIS HIS A . n 
A 1 127 HIS 127 127 127 HIS HIS A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 CYS 131 131 131 CYS CYS A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 GLU 134 134 134 GLU GLU A . n 
A 1 135 SER 135 135 135 SER SER A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 THR 138 138 138 THR THR A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 THR 141 141 141 THR THR A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 PRO 146 146 146 PRO PRO A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 ARG 149 149 149 ARG ARG A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 ALA 156 156 156 ALA ALA A . n 
A 1 157 GLU 157 157 157 GLU GLU A . n 
A 1 158 GLU 158 158 158 GLU GLU A . n 
A 1 159 CYS 159 159 159 CYS CYS A . n 
A 1 160 ARG 160 160 160 ARG ARG A . n 
A 1 161 LYS 161 161 161 LYS LYS A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 PHE 166 166 166 PHE PHE A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 ARG 174 174 174 ARG ARG A . n 
A 1 175 ASP 175 175 175 ASP ASP A . n 
A 1 176 TRP 176 176 176 TRP TRP A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 HIS 178 178 178 HIS HIS A . n 
A 1 179 PRO 179 179 179 PRO PRO A . n 
A 1 180 HIS 180 180 180 HIS HIS A . n 
A 1 181 ALA 181 181 181 ALA ALA A . n 
A 1 182 PRO 182 182 182 PRO PRO A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 ASN 184 184 184 ASN ASN A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 TRP 187 187 187 TRP TRP A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 ASN 190 190 190 ASN ASN A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 PRO 193 193 193 PRO PRO A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 TYR 195 195 195 TYR TYR A . n 
A 1 196 ASP 196 196 196 ASP ASP A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PHE 201 201 201 PHE PHE A . n 
A 1 202 TYR 202 202 202 TYR TYR A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 TYR 204 204 204 TYR TYR A . n 
A 1 205 GLY 205 205 205 GLY GLY A . n 
A 1 206 GLU 206 206 206 GLU GLU A . n 
A 1 207 ASP 207 207 207 ASP ASP A . n 
A 1 208 GLN 208 208 208 GLN GLN A . n 
A 1 209 ASP 209 209 209 ASP ASP A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 GLN 211 211 211 GLN GLN A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 TYR 213 213 213 TYR TYR A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 PHE 216 216 216 PHE PHE A . n 
A 1 217 MET 217 217 217 MET MET A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 ASN 219 219 219 ASN ASN A . n 
A 1 220 GLN 220 220 220 GLN GLN A . n 
A 1 221 ILE 221 221 221 ILE ILE A . n 
A 1 222 THR 222 222 222 THR THR A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 ASN 227 227 227 ASN ASN A . n 
A 1 228 TYR 228 228 228 TYR TYR A . n 
A 1 229 GLY 229 229 229 GLY GLY A . n 
A 1 230 PRO 230 230 230 PRO PRO A . n 
A 1 231 VAL 231 231 231 VAL VAL A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 GLY 233 233 233 GLY GLY A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 TRP 235 235 235 TRP TRP A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 ASP 237 237 237 ASP ASP A . n 
A 1 238 GLY 238 238 238 GLY GLY A . n 
A 1 239 VAL 239 239 239 VAL VAL A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 THR 241 241 241 THR THR A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 ALA 243 243 243 ALA ALA A . n 
A 1 244 SER 244 244 244 SER SER A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 LYS 246 246 246 LYS LYS A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 LYS 248 248 248 LYS LYS A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 PHE 252 252 252 PHE PHE A . n 
A 1 253 GLU 253 253 253 GLU GLU A . n 
A 1 254 THR 254 254 254 THR THR A . n 
A 1 255 GLN 255 255 255 GLN GLN A . n 
A 1 256 GLU 256 256 256 GLU GLU A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 TYR 258 258 258 TYR TYR A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 HIS 260 260 260 HIS HIS A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 HIS 262 262 262 HIS HIS A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 GLN 265 265 265 GLN GLN A . n 
A 1 266 PRO 266 266 266 PRO PRO A . n 
A 1 267 GLN 267 267 267 GLN GLN A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 VAL 270 270 270 VAL VAL A . n 
A 1 271 SER 271 271 271 SER SER A . n 
A 1 272 TYR 272 272 272 TYR TYR A . n 
A 1 273 LYS 273 273 273 LYS LYS A . n 
A 1 274 GLN 274 274 274 GLN GLN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 ILE 277 277 277 ILE ILE A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 THR 279 279 279 THR THR A . n 
A 1 280 GLU 280 280 280 GLU GLU A . n 
A 1 281 ASP 281 281 281 ASP ASP A . n 
A 1 282 PHE 282 282 282 PHE PHE A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
A 1 284 ALA 284 284 284 ALA ALA A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 GLU 286 286 286 GLU GLU A . n 
A 1 287 ARG 287 287 287 ARG ARG A . n 
A 1 288 HIS 288 288 288 HIS HIS A . n 
A 1 289 PHE 289 289 289 PHE PHE A . n 
A 1 290 LYS 290 290 290 LYS LYS A . n 
A 1 291 GLY 291 291 291 GLY GLY A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 SER 293 293 293 SER SER A . n 
A 1 294 ASP 294 294 294 ASP ASP A . n 
A 1 295 VAL 295 295 295 VAL VAL A . n 
A 1 296 PRO 296 296 296 PRO PRO A . n 
A 1 297 LEU 297 297 297 LEU LEU A . n 
A 1 298 GLU 298 298 298 GLU GLU A . n 
A 1 299 PHE 299 299 299 PHE PHE A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 ASP 301 301 301 ASP ASP A . n 
A 1 302 THR 302 302 302 THR THR A . n 
A 1 303 LEU 303 303 303 LEU LEU A . n 
A 1 304 GLN 304 304 304 GLN GLN A . n 
A 1 305 PRO 305 305 305 PRO PRO A . n 
A 1 306 TRP 306 306 306 TRP TRP A . n 
A 1 307 LYS 307 307 307 LYS LYS A . n 
A 1 308 TRP 308 308 308 TRP TRP A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 TYR 310 310 310 TYR TYR A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 LYS 312 312 312 LYS LYS A . n 
A 1 313 SER 313 313 313 SER SER A . n 
A 1 314 LEU 314 314 314 LEU LEU A . n 
A 1 315 ASP 315 315 315 ASP ASP A . n 
A 1 316 GLY 316 316 316 GLY GLY A . n 
A 1 317 LYS 317 317 317 LYS LYS A . n 
A 1 318 HIS 318 318 318 HIS HIS A . n 
A 1 319 LYS 319 319 319 LYS LYS A . n 
A 1 320 THR 320 320 320 THR THR A . n 
A 1 321 ALA 321 321 321 ALA ALA A . n 
A 1 322 ASP 322 322 322 ASP ASP A . n 
A 1 323 GLN 323 323 323 GLN GLN A . n 
A 1 324 VAL 324 324 324 VAL VAL A . n 
A 1 325 MET 325 325 325 MET MET A . n 
A 1 326 GLU 326 326 326 GLU GLU A . n 
A 1 327 MET 327 327 327 MET MET A . n 
A 1 328 LEU 328 328 328 LEU LEU A . n 
A 1 329 SER 329 329 329 SER SER A . n 
A 1 330 LYS 330 330 330 LYS LYS A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 ASN 332 332 332 ASN ASN A . n 
A 1 333 LYS 333 333 333 LYS LYS A . n 
A 1 334 MET 334 334 334 MET MET A . n 
A 1 335 ASP 335 335 335 ASP ASP A . n 
A 1 336 ALA 336 336 336 ALA ALA A . n 
A 1 337 ASN 337 337 337 ASN ASN A . n 
A 1 338 LEU 338 338 338 LEU LEU A . n 
A 1 339 LEU 339 339 339 LEU LEU A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 ASN 341 341 341 ASN ASN A . n 
A 1 342 VAL 342 342 342 VAL VAL A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 PRO 344 344 344 PRO PRO A . n 
A 1 345 LEU 345 345 345 LEU LEU A . n 
A 1 346 PRO 346 346 346 PRO PRO A . n 
A 1 347 ASP 347 347 347 ASP ASP A . n 
A 1 348 GLY 348 348 348 GLY GLY A . n 
A 1 349 SER 349 349 349 SER SER A . n 
A 1 350 ILE 350 350 350 ILE ILE A . n 
A 1 351 HIS 351 351 351 HIS HIS A . n 
A 1 352 PRO 352 352 352 PRO PRO A . n 
A 1 353 GLU 353 353 353 GLU GLU A . n 
A 1 354 ASP 354 354 354 ASP ASP A . n 
A 1 355 VAL 355 355 355 VAL VAL A . n 
A 1 356 LYS 356 356 356 LYS LYS A . n 
A 1 357 THR 357 357 357 THR THR A . n 
A 1 358 LEU 358 358 358 LEU LEU A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 GLU 360 360 360 GLU GLU A . n 
A 1 361 VAL 361 361 361 VAL VAL A . n 
A 1 362 GLY 362 362 362 GLY GLY A . n 
A 1 363 ARG 363 363 363 ARG ARG A . n 
A 1 364 LYS 364 364 364 LYS LYS A . n 
A 1 365 LEU 365 365 365 LEU LEU A . n 
A 1 366 LYS 366 366 366 LYS LYS A . n 
A 1 367 ALA 367 367 367 ALA ALA A . n 
A 1 368 HIS 368 368 ?   ?   ?   A . n 
A 1 369 HIS 369 369 ?   ?   ?   A . n 
A 1 370 HIS 370 370 ?   ?   ?   A . n 
A 1 371 HIS 371 371 ?   ?   ?   A . n 
A 1 372 HIS 372 372 ?   ?   ?   A . n 
A 1 373 HIS 373 373 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   ILE 3   3   ?   ?   ?   B . n 
B 1 4   GLN 4   4   ?   ?   ?   B . n 
B 1 5   ASN 5   5   ?   ?   ?   B . n 
B 1 6   ILE 6   6   ?   ?   ?   B . n 
B 1 7   ASN 7   7   ?   ?   ?   B . n 
B 1 8   ARG 8   8   ?   ?   ?   B . n 
B 1 9   ARG 9   9   ?   ?   ?   B . n 
B 1 10  SER 10  10  ?   ?   ?   B . n 
B 1 11  LEU 11  11  ?   ?   ?   B . n 
B 1 12  LEU 12  12  ?   ?   ?   B . n 
B 1 13  CYS 13  13  ?   ?   ?   B . n 
B 1 14  SER 14  14  ?   ?   ?   B . n 
B 1 15  GLY 15  15  ?   ?   ?   B . n 
B 1 16  ALA 16  16  ?   ?   ?   B . n 
B 1 17  ALA 17  17  ?   ?   ?   B . n 
B 1 18  THR 18  18  ?   ?   ?   B . n 
B 1 19  THR 19  19  ?   ?   ?   B . n 
B 1 20  ALA 20  20  ?   ?   ?   B . n 
B 1 21  ALA 21  21  ?   ?   ?   B . n 
B 1 22  LEU 22  22  ?   ?   ?   B . n 
B 1 23  ALA 23  23  ?   ?   ?   B . n 
B 1 24  VAL 24  24  ?   ?   ?   B . n 
B 1 25  SER 25  25  ?   ?   ?   B . n 
B 1 26  PRO 26  26  ?   ?   ?   B . n 
B 1 27  SER 27  27  ?   ?   ?   B . n 
B 1 28  VAL 28  28  ?   ?   ?   B . n 
B 1 29  PHE 29  29  ?   ?   ?   B . n 
B 1 30  GLY 30  30  ?   ?   ?   B . n 
B 1 31  ASP 31  31  ?   ?   ?   B . n 
B 1 32  SER 32  32  ?   ?   ?   B . n 
B 1 33  ALA 33  33  ?   ?   ?   B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  PRO 35  35  35  PRO PRO B . n 
B 1 36  SER 36  36  36  SER SER B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  TYR 41  41  41  TYR TYR B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  LEU 44  44  44  LEU LEU B . n 
B 1 45  TYR 45  45  45  TYR TYR B . n 
B 1 46  LYS 46  46  46  LYS LYS B . n 
B 1 47  LYS 47  47  47  LYS LYS B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  PRO 49  49  49  PRO PRO B . n 
B 1 50  ARG 50  50  50  ARG ARG B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  ALA 53  53  53  ALA ALA B . n 
B 1 54  LEU 54  54  54  LEU LEU B . n 
B 1 55  GLN 55  55  55  GLN GLN B . n 
B 1 56  TYR 56  56  56  TYR TYR B . n 
B 1 57  PHE 57  57  57  PHE PHE B . n 
B 1 58  LYS 58  58  58  LYS LYS B . n 
B 1 59  GLU 59  59  59  GLU GLU B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  PHE 62  62  62  PHE PHE B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  LEU 64  64  64  LEU LEU B . n 
B 1 65  PHE 65  65  65  PHE PHE B . n 
B 1 66  ILE 66  66  66  ILE ILE B . n 
B 1 67  HIS 67  67  67  HIS HIS B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  GLY 69  69  69  GLY GLY B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  TYR 71  71  71  TYR TYR B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  LEU 73  73  73  LEU LEU B . n 
B 1 74  LEU 74  74  74  LEU LEU B . n 
B 1 75  GLY 75  75  75  GLY GLY B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  TRP 79  79  79  TRP TRP B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  GLN 81  81  81  GLN GLN B . n 
B 1 82  LEU 82  82  82  LEU LEU B . n 
B 1 83  GLN 83  83  83  GLN GLN B . n 
B 1 84  GLY 84  84  84  GLY GLY B . n 
B 1 85  LYS 85  85  85  LYS LYS B . n 
B 1 86  ILE 86  86  86  ILE ILE B . n 
B 1 87  PRO 87  87  87  PRO PRO B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  ARG 89  89  89  ARG ARG B . n 
B 1 90  GLU 90  90  90  GLU GLU B . n 
B 1 91  TYR 91  91  91  TYR TYR B . n 
B 1 92  ALA 92  92  92  ALA ALA B . n 
B 1 93  LYS 93  93  93  LYS LYS B . n 
B 1 94  LEU 94  94  94  LEU LEU B . n 
B 1 95  GLU 95  95  95  GLU GLU B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  ASP 97  97  97  ASP ASP B . n 
B 1 98  PHE 98  98  98  PHE PHE B . n 
B 1 99  THR 99  99  99  THR THR B . n 
B 1 100 ALA 100 100 100 ALA ALA B . n 
B 1 101 LYS 101 101 101 LYS LYS B . n 
B 1 102 ASN 102 102 102 ASN ASN B . n 
B 1 103 PHE 103 103 103 PHE PHE B . n 
B 1 104 ASP 104 104 104 ASP ASP B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 ASP 106 106 106 ASP ASP B . n 
B 1 107 PHE 107 107 107 PHE PHE B . n 
B 1 108 ILE 108 108 108 ILE ILE B . n 
B 1 109 THR 109 109 109 THR THR B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 MET 111 111 111 MET MET B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 GLY 116 116 116 GLY GLY B . n 
B 1 117 MET 117 117 117 MET MET B . n 
B 1 118 LYS 118 118 118 LYS LYS B . n 
B 1 119 TYR 119 119 119 TYR TYR B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 ASN 121 121 121 ASN ASN B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 THR 123 123 123 THR THR B . n 
B 1 124 THR 124 124 124 THR THR B . n 
B 1 125 ARG 125 125 125 ARG ARG B . n 
B 1 126 HIS 126 126 126 HIS HIS B . n 
B 1 127 HIS 127 127 127 HIS HIS B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 SER 129 129 129 SER SER B . n 
B 1 130 PHE 130 130 130 PHE PHE B . n 
B 1 131 CYS 131 131 131 CYS CYS B . n 
B 1 132 LEU 132 132 132 LEU LEU B . n 
B 1 133 PHE 133 133 133 PHE PHE B . n 
B 1 134 GLU 134 134 134 GLU GLU B . n 
B 1 135 SER 135 135 135 SER SER B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 TYR 137 137 137 TYR TYR B . n 
B 1 138 THR 138 138 138 THR THR B . n 
B 1 139 ASP 139 139 139 ASP ASP B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 THR 141 141 141 THR THR B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 THR 143 143 143 THR THR B . n 
B 1 144 ASN 144 144 144 ASN ASN B . n 
B 1 145 SER 145 145 145 SER SER B . n 
B 1 146 PRO 146 146 146 PRO PRO B . n 
B 1 147 ALA 147 147 147 ALA ALA B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 ARG 149 149 149 ARG ARG B . n 
B 1 150 ASP 150 150 150 ASP ASP B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 VAL 152 152 152 VAL VAL B . n 
B 1 153 ALA 153 153 153 ALA ALA B . n 
B 1 154 GLU 154 154 154 GLU GLU B . n 
B 1 155 LEU 155 155 155 LEU LEU B . n 
B 1 156 ALA 156 156 156 ALA ALA B . n 
B 1 157 GLU 157 157 157 GLU GLU B . n 
B 1 158 GLU 158 158 158 GLU GLU B . n 
B 1 159 CYS 159 159 159 CYS CYS B . n 
B 1 160 ARG 160 160 160 ARG ARG B . n 
B 1 161 LYS 161 161 161 LYS LYS B . n 
B 1 162 LYS 162 162 162 LYS LYS B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 GLY 165 165 165 GLY GLY B . n 
B 1 166 PHE 166 166 166 PHE PHE B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 LEU 168 168 168 LEU LEU B . n 
B 1 169 TYR 169 169 169 TYR TYR B . n 
B 1 170 TYR 170 170 170 TYR TYR B . n 
B 1 171 SER 171 171 171 SER SER B . n 
B 1 172 HIS 172 172 172 HIS HIS B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 ARG 174 174 174 ARG ARG B . n 
B 1 175 ASP 175 175 175 ASP ASP B . n 
B 1 176 TRP 176 176 176 TRP TRP B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 HIS 178 178 178 HIS HIS B . n 
B 1 179 PRO 179 179 179 PRO PRO B . n 
B 1 180 HIS 180 180 180 HIS HIS B . n 
B 1 181 ALA 181 181 181 ALA ALA B . n 
B 1 182 PRO 182 182 182 PRO PRO B . n 
B 1 183 ASN 183 183 183 ASN ASN B . n 
B 1 184 ASN 184 184 184 ASN ASN B . n 
B 1 185 GLY 185 185 185 GLY GLY B . n 
B 1 186 ASP 186 186 186 ASP ASP B . n 
B 1 187 TRP 187 187 187 TRP TRP B . n 
B 1 188 GLY 188 188 188 GLY GLY B . n 
B 1 189 GLY 189 189 189 GLY GLY B . n 
B 1 190 ASN 190 190 190 ASN ASN B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 ARG 192 192 192 ARG ARG B . n 
B 1 193 PRO 193 193 193 PRO PRO B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 TYR 195 195 195 TYR TYR B . n 
B 1 196 ASP 196 196 196 ASP ASP B . n 
B 1 197 SER 197 197 197 SER SER B . n 
B 1 198 PRO 198 198 198 PRO PRO B . n 
B 1 199 GLU 199 199 199 GLU GLU B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 PHE 201 201 201 PHE PHE B . n 
B 1 202 TYR 202 202 202 TYR TYR B . n 
B 1 203 LYS 203 203 203 LYS LYS B . n 
B 1 204 TYR 204 204 204 TYR TYR B . n 
B 1 205 GLY 205 205 205 GLY GLY B . n 
B 1 206 GLU 206 206 206 GLU GLU B . n 
B 1 207 ASP 207 207 207 ASP ASP B . n 
B 1 208 GLN 208 208 208 GLN GLN B . n 
B 1 209 ASP 209 209 209 ASP ASP B . n 
B 1 210 LEU 210 210 210 LEU LEU B . n 
B 1 211 GLN 211 211 211 GLN GLN B . n 
B 1 212 ILE 212 212 212 ILE ILE B . n 
B 1 213 TYR 213 213 213 TYR TYR B . n 
B 1 214 VAL 214 214 214 VAL VAL B . n 
B 1 215 GLU 215 215 215 GLU GLU B . n 
B 1 216 PHE 216 216 216 PHE PHE B . n 
B 1 217 MET 217 217 217 MET MET B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 ASN 219 219 219 ASN ASN B . n 
B 1 220 GLN 220 220 220 GLN GLN B . n 
B 1 221 ILE 221 221 221 ILE ILE B . n 
B 1 222 THR 222 222 222 THR THR B . n 
B 1 223 GLU 223 223 223 GLU GLU B . n 
B 1 224 LEU 224 224 224 LEU LEU B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 ASN 227 227 227 ASN ASN B . n 
B 1 228 TYR 228 228 228 TYR TYR B . n 
B 1 229 GLY 229 229 229 GLY GLY B . n 
B 1 230 PRO 230 230 230 PRO PRO B . n 
B 1 231 VAL 231 231 231 VAL VAL B . n 
B 1 232 GLY 232 232 232 GLY GLY B . n 
B 1 233 GLY 233 233 233 GLY GLY B . n 
B 1 234 ILE 234 234 234 ILE ILE B . n 
B 1 235 TRP 235 235 235 TRP TRP B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 ASP 237 237 237 ASP ASP B . n 
B 1 238 GLY 238 238 238 GLY GLY B . n 
B 1 239 VAL 239 239 239 VAL VAL B . n 
B 1 240 ALA 240 240 240 ALA ALA B . n 
B 1 241 THR 241 241 241 THR THR B . n 
B 1 242 PRO 242 242 242 PRO PRO B . n 
B 1 243 ALA 243 243 243 ALA ALA B . n 
B 1 244 SER 244 244 244 SER SER B . n 
B 1 245 ARG 245 245 245 ARG ARG B . n 
B 1 246 LYS 246 246 246 LYS LYS B . n 
B 1 247 GLY 247 247 247 GLY GLY B . n 
B 1 248 LYS 248 248 248 LYS LYS B . n 
B 1 249 LEU 249 249 249 LEU LEU B . n 
B 1 250 HIS 250 250 250 HIS HIS B . n 
B 1 251 LEU 251 251 251 LEU LEU B . n 
B 1 252 PHE 252 252 252 PHE PHE B . n 
B 1 253 GLU 253 253 253 GLU GLU B . n 
B 1 254 THR 254 254 254 THR THR B . n 
B 1 255 GLN 255 255 255 GLN GLN B . n 
B 1 256 GLU 256 256 256 GLU GLU B . n 
B 1 257 LEU 257 257 257 LEU LEU B . n 
B 1 258 TYR 258 258 258 TYR TYR B . n 
B 1 259 ASP 259 259 259 ASP ASP B . n 
B 1 260 HIS 260 260 260 HIS HIS B . n 
B 1 261 ILE 261 261 261 ILE ILE B . n 
B 1 262 HIS 262 262 262 HIS HIS B . n 
B 1 263 SER 263 263 263 SER SER B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 GLN 265 265 265 GLN GLN B . n 
B 1 266 PRO 266 266 266 PRO PRO B . n 
B 1 267 GLN 267 267 267 GLN GLN B . n 
B 1 268 VAL 268 268 268 VAL VAL B . n 
B 1 269 LEU 269 269 269 LEU LEU B . n 
B 1 270 VAL 270 270 270 VAL VAL B . n 
B 1 271 SER 271 271 271 SER SER B . n 
B 1 272 TYR 272 272 272 TYR TYR B . n 
B 1 273 LYS 273 273 273 LYS LYS B . n 
B 1 274 GLN 274 274 274 GLN GLN B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 LEU 276 276 276 LEU LEU B . n 
B 1 277 ILE 277 277 277 ILE ILE B . n 
B 1 278 GLY 278 278 278 GLY GLY B . n 
B 1 279 THR 279 279 279 THR THR B . n 
B 1 280 GLU 280 280 280 GLU GLU B . n 
B 1 281 ASP 281 281 281 ASP ASP B . n 
B 1 282 PHE 282 282 282 PHE PHE B . n 
B 1 283 LYS 283 283 283 LYS LYS B . n 
B 1 284 ALA 284 284 284 ALA ALA B . n 
B 1 285 PRO 285 285 285 PRO PRO B . n 
B 1 286 GLU 286 286 286 GLU GLU B . n 
B 1 287 ARG 287 287 287 ARG ARG B . n 
B 1 288 HIS 288 288 288 HIS HIS B . n 
B 1 289 PHE 289 289 289 PHE PHE B . n 
B 1 290 LYS 290 290 290 LYS LYS B . n 
B 1 291 GLY 291 291 291 GLY GLY B . n 
B 1 292 THR 292 292 292 THR THR B . n 
B 1 293 SER 293 293 293 SER SER B . n 
B 1 294 ASP 294 294 294 ASP ASP B . n 
B 1 295 VAL 295 295 295 VAL VAL B . n 
B 1 296 PRO 296 296 296 PRO PRO B . n 
B 1 297 LEU 297 297 297 LEU LEU B . n 
B 1 298 GLU 298 298 298 GLU GLU B . n 
B 1 299 PHE 299 299 299 PHE PHE B . n 
B 1 300 CYS 300 300 300 CYS CYS B . n 
B 1 301 ASP 301 301 301 ASP ASP B . n 
B 1 302 THR 302 302 302 THR THR B . n 
B 1 303 LEU 303 303 303 LEU LEU B . n 
B 1 304 GLN 304 304 304 GLN GLN B . n 
B 1 305 PRO 305 305 305 PRO PRO B . n 
B 1 306 TRP 306 306 306 TRP TRP B . n 
B 1 307 LYS 307 307 307 LYS LYS B . n 
B 1 308 TRP 308 308 308 TRP TRP B . n 
B 1 309 GLY 309 309 309 GLY GLY B . n 
B 1 310 TYR 310 310 310 TYR TYR B . n 
B 1 311 ASP 311 311 311 ASP ASP B . n 
B 1 312 LYS 312 312 312 LYS LYS B . n 
B 1 313 SER 313 313 313 SER SER B . n 
B 1 314 LEU 314 314 314 LEU LEU B . n 
B 1 315 ASP 315 315 315 ASP ASP B . n 
B 1 316 GLY 316 316 316 GLY GLY B . n 
B 1 317 LYS 317 317 317 LYS LYS B . n 
B 1 318 HIS 318 318 318 HIS HIS B . n 
B 1 319 LYS 319 319 319 LYS LYS B . n 
B 1 320 THR 320 320 320 THR THR B . n 
B 1 321 ALA 321 321 321 ALA ALA B . n 
B 1 322 ASP 322 322 322 ASP ASP B . n 
B 1 323 GLN 323 323 323 GLN GLN B . n 
B 1 324 VAL 324 324 324 VAL VAL B . n 
B 1 325 MET 325 325 325 MET MET B . n 
B 1 326 GLU 326 326 326 GLU GLU B . n 
B 1 327 MET 327 327 327 MET MET B . n 
B 1 328 LEU 328 328 328 LEU LEU B . n 
B 1 329 SER 329 329 329 SER SER B . n 
B 1 330 LYS 330 330 330 LYS LYS B . n 
B 1 331 ALA 331 331 331 ALA ALA B . n 
B 1 332 ASN 332 332 332 ASN ASN B . n 
B 1 333 LYS 333 333 333 LYS LYS B . n 
B 1 334 MET 334 334 334 MET MET B . n 
B 1 335 ASP 335 335 335 ASP ASP B . n 
B 1 336 ALA 336 336 336 ALA ALA B . n 
B 1 337 ASN 337 337 337 ASN ASN B . n 
B 1 338 LEU 338 338 338 LEU LEU B . n 
B 1 339 LEU 339 339 339 LEU LEU B . n 
B 1 340 LEU 340 340 340 LEU LEU B . n 
B 1 341 ASN 341 341 341 ASN ASN B . n 
B 1 342 VAL 342 342 342 VAL VAL B . n 
B 1 343 GLY 343 343 343 GLY GLY B . n 
B 1 344 PRO 344 344 344 PRO PRO B . n 
B 1 345 LEU 345 345 345 LEU LEU B . n 
B 1 346 PRO 346 346 346 PRO PRO B . n 
B 1 347 ASP 347 347 347 ASP ASP B . n 
B 1 348 GLY 348 348 348 GLY GLY B . n 
B 1 349 SER 349 349 349 SER SER B . n 
B 1 350 ILE 350 350 350 ILE ILE B . n 
B 1 351 HIS 351 351 351 HIS HIS B . n 
B 1 352 PRO 352 352 352 PRO PRO B . n 
B 1 353 GLU 353 353 353 GLU GLU B . n 
B 1 354 ASP 354 354 354 ASP ASP B . n 
B 1 355 VAL 355 355 355 VAL VAL B . n 
B 1 356 LYS 356 356 356 LYS LYS B . n 
B 1 357 THR 357 357 357 THR THR B . n 
B 1 358 LEU 358 358 358 LEU LEU B . n 
B 1 359 ALA 359 359 359 ALA ALA B . n 
B 1 360 GLU 360 360 360 GLU GLU B . n 
B 1 361 VAL 361 361 361 VAL VAL B . n 
B 1 362 GLY 362 362 362 GLY GLY B . n 
B 1 363 ARG 363 363 363 ARG ARG B . n 
B 1 364 LYS 364 364 364 LYS LYS B . n 
B 1 365 LEU 365 365 365 LEU LEU B . n 
B 1 366 LYS 366 366 366 LYS LYS B . n 
B 1 367 ALA 367 367 367 ALA ALA B . n 
B 1 368 HIS 368 368 ?   ?   ?   B . n 
B 1 369 HIS 369 369 ?   ?   ?   B . n 
B 1 370 HIS 370 370 ?   ?   ?   B . n 
B 1 371 HIS 371 371 ?   ?   ?   B . n 
B 1 372 HIS 372 372 ?   ?   ?   B . n 
B 1 373 HIS 373 373 ?   ?   ?   B . n 
# 
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   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   98.85 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z63 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.061 
_cell.length_a_esd                 ? 
_cell.length_b                     79.822 
_cell.length_b_esd                 ? 
_cell.length_c                     89.724 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Z63 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Z63 
_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             2.18 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.46 
_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              ? 
_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    'PEG 4000, Sodium acetate trihydrate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_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         2023-09-14 
_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   0.978 
_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                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.978 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Z63 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.82 
_reflns.d_resolution_low                               47.8 
_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                                     16715 
_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                           94.78 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.27 
_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                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1097 
_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                                    2.822 
_reflns_shell.d_res_low                                     2.922 
_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                             16715 
_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                                  0.997 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8Z63 
_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                            2.82 
_refine.ls_d_res_low                             47.80 
_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                     16715 
_refine.ls_number_reflns_R_free                  817 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.80 
_refine.ls_percent_reflns_R_free                 4.89 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2194 
_refine.ls_R_factor_R_free                       0.2754 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2165 
_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                          0.01 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.12 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.36 
_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                       2.82 
_refine_hist.d_res_low                        47.80 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               5407 
_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        5407 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.004 ? 5448 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.933 ? 7370 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.707 ? 716  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.046 ? 752  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011 ? 958  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.82 3.00  . . 119 2388 86.00 . . . . 0.2895 . . . . . . . . . . . 0.3676 
'X-RAY DIFFRACTION' 3.00 3.23  . . 140 2544 92.00 . . . . 0.2800 . . . . . . . . . . . 0.3595 
'X-RAY DIFFRACTION' 3.23 3.55  . . 141 2662 96.00 . . . . 0.2488 . . . . . . . . . . . 0.2999 
'X-RAY DIFFRACTION' 3.56 4.07  . . 147 2731 98.00 . . . . 0.2133 . . . . . . . . . . . 0.2476 
'X-RAY DIFFRACTION' 4.07 5.12  . . 143 2754 99.00 . . . . 0.1847 . . . . . . . . . . . 0.2579 
'X-RAY DIFFRACTION' 5.13 47.80 . . 127 2819 98.00 . . . . 0.2004 . . . . . . . . . . . 0.2506 
# 
_struct.entry_id                     8Z63 
_struct.title                        'alpha-L-fucosidase from Pontiella sulfatireligans F21' 
_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        8Z63 
_struct_keywords.text            'GH family 29, Pontiella sulfatireligans F21, Kiritmatiellaeota, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A6C2UIZ6_9BACT 
_struct_ref.pdbx_db_accession          A0A6C2UIZ6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPIQNINRRSLLCSGAATTAALAVSPSVFGDSAVPSYLKDYAALYKKDPRAAALQYFKEAKFGLFIHYGLYSLLGRGEWV
QLQGKIPVREYAKLENDFTAKNFDADFITDMALEAGMKYVNITTRHHDSFCLFESKYTDFTSTNSPAKRDLVAELAEECR
KKGLGFYLYYSHGRDWRHPHAPNNGDWGGNARPKYDSPEPFYKYGEDQDLQIYVEFMKNQITELLTNYGPVGGIWLDGVA
TPASRKGKLHLFETQELYDHIHSLQPQVLVSYKQGLIGTEDFKAPERHFKGTSDVPLEFCDTLQPWKWGYDKSLDGKHKT
ADQVMEMLSKANKMDANLLLNVGPLPDGSIHPEDVKTLAEVGRKLKA
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8Z63 A 1 ? 367 ? A0A6C2UIZ6 1 ? 367 ? 1 367 
2 1 8Z63 B 1 ? 367 ? A0A6C2UIZ6 1 ? 367 ? 1 367 
# 
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 8Z63 HIS A 368 ? UNP A0A6C2UIZ6 ? ? 'expression tag' 368 1  
1 8Z63 HIS A 369 ? UNP A0A6C2UIZ6 ? ? 'expression tag' 369 2  
1 8Z63 HIS A 370 ? UNP A0A6C2UIZ6 ? ? 'expression tag' 370 3  
1 8Z63 HIS A 371 ? UNP A0A6C2UIZ6 ? ? 'expression tag' 371 4  
1 8Z63 HIS A 372 ? UNP A0A6C2UIZ6 ? ? 'expression tag' 372 5  
1 8Z63 HIS A 373 ? UNP A0A6C2UIZ6 ? ? 'expression tag' 373 6  
2 8Z63 HIS B 368 ? UNP A0A6C2UIZ6 ? ? 'expression tag' 368 7  
2 8Z63 HIS B 369 ? UNP A0A6C2UIZ6 ? ? 'expression tag' 369 8  
2 8Z63 HIS B 370 ? UNP A0A6C2UIZ6 ? ? 'expression tag' 370 9  
2 8Z63 HIS B 371 ? UNP A0A6C2UIZ6 ? ? 'expression tag' 371 10 
2 8Z63 HIS B 372 ? UNP A0A6C2UIZ6 ? ? 'expression tag' 372 11 
2 8Z63 HIS B 373 ? UNP A0A6C2UIZ6 ? ? 'expression tag' 373 12 
# 
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 
2 1 B 
# 
_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 PRO A 35  ? LYS A 39  ? PRO A 35  LYS A 39  5 ? 5  
HELX_P HELX_P2  AA2 TYR A 41  ? LYS A 46  ? TYR A 41  LYS A 46  1 ? 6  
HELX_P HELX_P3  AA3 ASP A 48  ? LYS A 61  ? ASP A 48  LYS A 61  1 ? 14 
HELX_P HELX_P4  AA4 LEU A 70  ? GLY A 75  ? LEU A 70  GLY A 75  1 ? 6  
HELX_P HELX_P5  AA5 TRP A 79  ? GLY A 84  ? TRP A 79  GLY A 84  1 ? 6  
HELX_P HELX_P6  AA6 PRO A 87  ? ALA A 92  ? PRO A 87  ALA A 92  1 ? 6  
HELX_P HELX_P7  AA7 LYS A 93  ? PHE A 98  ? LYS A 93  PHE A 98  5 ? 6  
HELX_P HELX_P8  AA8 ASP A 104 ? GLY A 116 ? ASP A 104 GLY A 116 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 150 ? GLY A 163 ? ASP A 150 GLY A 163 1 ? 14 
HELX_P HELX_P10 AB1 TYR A 204 ? GLN A 208 ? TYR A 204 GLN A 208 5 ? 5  
HELX_P HELX_P11 AB2 ASP A 209 ? ASN A 227 ? ASP A 209 ASN A 227 1 ? 19 
HELX_P HELX_P12 AB3 THR A 241 ? LYS A 246 ? THR A 241 LYS A 246 5 ? 6  
HELX_P HELX_P13 AB4 LYS A 248 ? PHE A 252 ? LYS A 248 PHE A 252 5 ? 5  
HELX_P HELX_P14 AB5 GLU A 253 ? GLN A 265 ? GLU A 253 GLN A 265 1 ? 13 
HELX_P HELX_P15 AB6 ASP A 311 ? ASP A 315 ? ASP A 311 ASP A 315 5 ? 5  
HELX_P HELX_P16 AB7 THR A 320 ? MET A 334 ? THR A 320 MET A 334 1 ? 15 
HELX_P HELX_P17 AB8 HIS A 351 ? LYS A 366 ? HIS A 351 LYS A 366 1 ? 16 
HELX_P HELX_P18 AB9 TYR B 41  ? ASP B 48  ? TYR B 41  ASP B 48  1 ? 8  
HELX_P HELX_P19 AC1 ASP B 48  ? LYS B 61  ? ASP B 48  LYS B 61  1 ? 14 
HELX_P HELX_P20 AC2 GLY B 69  ? GLY B 75  ? GLY B 69  GLY B 75  1 ? 7  
HELX_P HELX_P21 AC3 TRP B 79  ? GLY B 84  ? TRP B 79  GLY B 84  1 ? 6  
HELX_P HELX_P22 AC4 PRO B 87  ? ALA B 92  ? PRO B 87  ALA B 92  1 ? 6  
HELX_P HELX_P23 AC5 LYS B 93  ? PHE B 98  ? LYS B 93  PHE B 98  5 ? 6  
HELX_P HELX_P24 AC6 ASP B 104 ? GLY B 116 ? ASP B 104 GLY B 116 1 ? 13 
HELX_P HELX_P25 AC7 ASP B 150 ? GLY B 163 ? ASP B 150 GLY B 163 1 ? 14 
HELX_P HELX_P26 AC8 TYR B 204 ? GLN B 208 ? TYR B 204 GLN B 208 5 ? 5  
HELX_P HELX_P27 AC9 ASP B 209 ? ASN B 227 ? ASP B 209 ASN B 227 1 ? 19 
HELX_P HELX_P28 AD1 THR B 241 ? ARG B 245 ? THR B 241 ARG B 245 5 ? 5  
HELX_P HELX_P29 AD2 LYS B 248 ? PHE B 252 ? LYS B 248 PHE B 252 5 ? 5  
HELX_P HELX_P30 AD3 GLU B 253 ? GLN B 265 ? GLU B 253 GLN B 265 1 ? 13 
HELX_P HELX_P31 AD4 ASP B 311 ? ASP B 315 ? ASP B 311 ASP B 315 5 ? 5  
HELX_P HELX_P32 AD5 THR B 320 ? MET B 334 ? THR B 320 MET B 334 1 ? 15 
HELX_P HELX_P33 AD6 HIS B 351 ? LYS B 366 ? HIS B 351 LYS B 366 1 ? 16 
# 
_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 ? 7 ? 
AA2 ? 7 ? 
# 
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 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? 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 
# 
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 LEU A 269 ? TYR A 272 ? LEU A 269 TYR A 272 
AA1 2 GLY A 233 ? ASP A 237 ? GLY A 233 ASP A 237 
AA1 3 GLY A 165 ? SER A 171 ? GLY A 165 SER A 171 
AA1 4 TYR A 119 ? ARG A 125 ? TYR A 119 ARG A 125 
AA1 5 PHE A 62  ? ILE A 66  ? PHE A 62  ILE A 66  
AA1 6 ALA A 336 ? VAL A 342 ? ALA A 336 VAL A 342 
AA1 7 LEU A 297 ? THR A 302 ? LEU A 297 THR A 302 
AA2 1 LEU B 269 ? TYR B 272 ? LEU B 269 TYR B 272 
AA2 2 GLY B 233 ? ASP B 237 ? GLY B 233 ASP B 237 
AA2 3 GLY B 165 ? SER B 171 ? GLY B 165 SER B 171 
AA2 4 TYR B 119 ? ARG B 125 ? TYR B 119 ARG B 125 
AA2 5 PHE B 62  ? ILE B 66  ? PHE B 62  ILE B 66  
AA2 6 ALA B 336 ? VAL B 342 ? ALA B 336 VAL B 342 
AA2 7 LEU B 297 ? THR B 302 ? LEU B 297 THR B 302 
# 
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 O LEU A 269 ? O LEU A 269 N ILE A 234 ? N ILE A 234 
AA1 2 3 O TRP A 235 ? O TRP A 235 N LEU A 168 ? N LEU A 168 
AA1 3 4 O GLY A 165 ? O GLY A 165 N VAL A 120 ? N VAL A 120 
AA1 4 5 O ASN A 121 ? O ASN A 121 N LEU A 64  ? N LEU A 64  
AA1 5 6 N PHE A 65  ? N PHE A 65  O VAL A 342 ? O VAL A 342 
AA1 6 7 O LEU A 339 ? O LEU A 339 N PHE A 299 ? N PHE A 299 
AA2 1 2 O SER B 271 ? O SER B 271 N LEU B 236 ? N LEU B 236 
AA2 2 3 O TRP B 235 ? O TRP B 235 N LEU B 168 ? N LEU B 168 
AA2 3 4 O GLY B 165 ? O GLY B 165 N VAL B 120 ? N VAL B 120 
AA2 4 5 O ASN B 121 ? O ASN B 121 N LEU B 64  ? N LEU B 64  
AA2 5 6 N PHE B 65  ? N PHE B 65  O LEU B 340 ? O LEU B 340 
AA2 6 7 O LEU B 339 ? O LEU B 339 N PHE B 299 ? N PHE B 299 
# 
_pdbx_entry_details.entry_id                   8Z63 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_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   NH2 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    125 
_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   B 
_pdbx_validate_close_contact.auth_comp_id_2   SER 
_pdbx_validate_close_contact.auth_seq_id_2    171 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LEU A 38  ? ? -119.33 65.53   
2  1 TYR A 41  ? ? -141.16 30.06   
3  1 LYS A 61  ? ? 74.94   -38.04  
4  1 ARG A 125 ? ? -163.57 117.83  
5  1 ARG A 177 ? ? -125.52 -53.36  
6  1 LYS A 273 ? ? 56.01   -129.21 
7  1 ALA A 284 ? ? -119.30 72.07   
8  1 ARG A 287 ? ? 71.43   -52.38  
9  1 PRO A 305 ? ? -53.19  104.23  
10 1 TRP A 306 ? ? 77.51   -34.84  
11 1 ASP B 48  ? ? -161.79 105.40  
12 1 LYS B 61  ? ? 76.83   -35.72  
13 1 ARG B 125 ? ? -164.99 118.80  
14 1 ARG B 177 ? ? -126.82 -53.34  
15 1 TRP B 187 ? ? -119.27 53.04   
16 1 LYS B 273 ? ? 56.91   -128.84 
17 1 ALA B 284 ? ? -119.44 71.48   
18 1 ARG B 287 ? ? 71.79   -51.04  
19 1 TRP B 306 ? ? 78.67   -32.97  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    189 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   ASN 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    190 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            108.08 
# 
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 1   ? A MET 1   
2  1 Y 1 A PRO 2   ? A PRO 2   
3  1 Y 1 A ILE 3   ? A ILE 3   
4  1 Y 1 A GLN 4   ? A GLN 4   
5  1 Y 1 A ASN 5   ? A ASN 5   
6  1 Y 1 A ILE 6   ? A ILE 6   
7  1 Y 1 A ASN 7   ? A ASN 7   
8  1 Y 1 A ARG 8   ? A ARG 8   
9  1 Y 1 A ARG 9   ? A ARG 9   
10 1 Y 1 A SER 10  ? A SER 10  
11 1 Y 1 A LEU 11  ? A LEU 11  
12 1 Y 1 A LEU 12  ? A LEU 12  
13 1 Y 1 A CYS 13  ? A CYS 13  
14 1 Y 1 A SER 14  ? A SER 14  
15 1 Y 1 A GLY 15  ? A GLY 15  
16 1 Y 1 A ALA 16  ? A ALA 16  
17 1 Y 1 A ALA 17  ? A ALA 17  
18 1 Y 1 A THR 18  ? A THR 18  
19 1 Y 1 A THR 19  ? A THR 19  
20 1 Y 1 A ALA 20  ? A ALA 20  
21 1 Y 1 A ALA 21  ? A ALA 21  
22 1 Y 1 A LEU 22  ? A LEU 22  
23 1 Y 1 A ALA 23  ? A ALA 23  
24 1 Y 1 A VAL 24  ? A VAL 24  
25 1 Y 1 A SER 25  ? A SER 25  
26 1 Y 1 A PRO 26  ? A PRO 26  
27 1 Y 1 A SER 27  ? A SER 27  
28 1 Y 1 A VAL 28  ? A VAL 28  
29 1 Y 1 A PHE 29  ? A PHE 29  
30 1 Y 1 A GLY 30  ? A GLY 30  
31 1 Y 1 A ASP 31  ? A ASP 31  
32 1 Y 1 A HIS 368 ? A HIS 368 
33 1 Y 1 A HIS 369 ? A HIS 369 
34 1 Y 1 A HIS 370 ? A HIS 370 
35 1 Y 1 A HIS 371 ? A HIS 371 
36 1 Y 1 A HIS 372 ? A HIS 372 
37 1 Y 1 A HIS 373 ? A HIS 373 
38 1 Y 1 B MET 1   ? B MET 1   
39 1 Y 1 B PRO 2   ? B PRO 2   
40 1 Y 1 B ILE 3   ? B ILE 3   
41 1 Y 1 B GLN 4   ? B GLN 4   
42 1 Y 1 B ASN 5   ? B ASN 5   
43 1 Y 1 B ILE 6   ? B ILE 6   
44 1 Y 1 B ASN 7   ? B ASN 7   
45 1 Y 1 B ARG 8   ? B ARG 8   
46 1 Y 1 B ARG 9   ? B ARG 9   
47 1 Y 1 B SER 10  ? B SER 10  
48 1 Y 1 B LEU 11  ? B LEU 11  
49 1 Y 1 B LEU 12  ? B LEU 12  
50 1 Y 1 B CYS 13  ? B CYS 13  
51 1 Y 1 B SER 14  ? B SER 14  
52 1 Y 1 B GLY 15  ? B GLY 15  
53 1 Y 1 B ALA 16  ? B ALA 16  
54 1 Y 1 B ALA 17  ? B ALA 17  
55 1 Y 1 B THR 18  ? B THR 18  
56 1 Y 1 B THR 19  ? B THR 19  
57 1 Y 1 B ALA 20  ? B ALA 20  
58 1 Y 1 B ALA 21  ? B ALA 21  
59 1 Y 1 B LEU 22  ? B LEU 22  
60 1 Y 1 B ALA 23  ? B ALA 23  
61 1 Y 1 B VAL 24  ? B VAL 24  
62 1 Y 1 B SER 25  ? B SER 25  
63 1 Y 1 B PRO 26  ? B PRO 26  
64 1 Y 1 B SER 27  ? B SER 27  
65 1 Y 1 B VAL 28  ? B VAL 28  
66 1 Y 1 B PHE 29  ? B PHE 29  
67 1 Y 1 B GLY 30  ? B GLY 30  
68 1 Y 1 B ASP 31  ? B ASP 31  
69 1 Y 1 B SER 32  ? B SER 32  
70 1 Y 1 B ALA 33  ? B ALA 33  
71 1 Y 1 B HIS 368 ? B HIS 368 
72 1 Y 1 B HIS 369 ? B HIS 369 
73 1 Y 1 B HIS 370 ? B HIS 370 
74 1 Y 1 B HIS 371 ? B HIS 371 
75 1 Y 1 B HIS 372 ? B HIS 372 
76 1 Y 1 B HIS 373 ? B HIS 373 
# 
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  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
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  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_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             'integrative model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   A0A6C2UIZ6_9BACT 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8Z63 
_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]   0.019208 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002991 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012528 
_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]   0.011280 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1    N N   . SER A 1 32  ? 24.188 26.311  15.151  1.00 30.00  ? 32  SER A N   1 
ATOM 2    C CA  . SER A 1 32  ? 22.810 26.023  15.626  1.00 30.00  ? 32  SER A CA  1 
ATOM 3    C C   . SER A 1 32  ? 22.021 25.297  14.531  1.00 30.00  ? 32  SER A C   1 
ATOM 4    O O   . SER A 1 32  ? 21.997 24.052  14.557  1.00 30.00  ? 32  SER A O   1 
ATOM 5    C CB  . SER A 1 32  ? 22.122 27.283  16.058  1.00 30.00  ? 32  SER A CB  1 
ATOM 6    O OG  . SER A 1 32  ? 22.932 28.015  16.965  1.00 30.00  ? 32  SER A OG  1 
ATOM 7    N N   . ALA A 1 33  ? 21.408 26.041  13.604  1.00 30.00  ? 33  ALA A N   1 
ATOM 8    C CA  . ALA A 1 33  ? 20.682 25.406  12.478  1.00 30.00  ? 33  ALA A CA  1 
ATOM 9    C C   . ALA A 1 33  ? 21.615 24.405  11.803  1.00 30.00  ? 33  ALA A C   1 
ATOM 10   O O   . ALA A 1 33  ? 21.112 23.421  11.236  1.00 30.00  ? 33  ALA A O   1 
ATOM 11   C CB  . ALA A 1 33  ? 20.202 26.443  11.497  1.00 30.00  ? 33  ALA A CB  1 
ATOM 12   N N   . VAL A 1 34  ? 22.920 24.665  11.853  1.00 30.00  ? 34  VAL A N   1 
ATOM 13   C CA  . VAL A 1 34  ? 23.907 23.703  11.291  1.00 30.00  ? 34  VAL A CA  1 
ATOM 14   C C   . VAL A 1 34  ? 23.932 22.482  12.211  1.00 30.00  ? 34  VAL A C   1 
ATOM 15   O O   . VAL A 1 34  ? 24.327 22.627  13.380  1.00 30.00  ? 34  VAL A O   1 
ATOM 16   C CB  . VAL A 1 34  ? 25.292 24.356  11.151  1.00 30.00  ? 34  VAL A CB  1 
ATOM 17   C CG1 . VAL A 1 34  ? 26.410 23.331  11.137  1.00 30.00  ? 34  VAL A CG1 1 
ATOM 18   C CG2 . VAL A 1 34  ? 25.365 25.254  9.928   1.00 30.00  ? 34  VAL A CG2 1 
ATOM 19   N N   . PRO A 1 35  ? 23.481 21.304  11.741  1.00 30.00  ? 35  PRO A N   1 
ATOM 20   C CA  . PRO A 1 35  ? 23.487 20.107  12.562  1.00 30.00  ? 35  PRO A CA  1 
ATOM 21   C C   . PRO A 1 35  ? 24.916 19.687  12.927  1.00 30.00  ? 35  PRO A C   1 
ATOM 22   O O   . PRO A 1 35  ? 25.801 19.901  12.133  1.00 30.00  ? 35  PRO A O   1 
ATOM 23   C CB  . PRO A 1 35  ? 22.836 19.065  11.652  1.00 30.00  ? 35  PRO A CB  1 
ATOM 24   C CG  . PRO A 1 35  ? 22.058 19.874  10.642  1.00 30.00  ? 35  PRO A CG  1 
ATOM 25   C CD  . PRO A 1 35  ? 22.929 21.086  10.408  1.00 30.00  ? 35  PRO A CD  1 
ATOM 26   N N   . SER A 1 36  ? 25.101 19.095  14.107  1.00 30.00  ? 36  SER A N   1 
ATOM 27   C CA  . SER A 1 36  ? 26.454 18.710  14.587  1.00 30.00  ? 36  SER A CA  1 
ATOM 28   C C   . SER A 1 36  ? 27.206 17.913  13.526  1.00 30.00  ? 36  SER A C   1 
ATOM 29   O O   . SER A 1 36  ? 28.360 18.258  13.243  1.00 30.00  ? 36  SER A O   1 
ATOM 30   C CB  . SER A 1 36  ? 26.348 17.918  15.856  1.00 30.00  ? 36  SER A CB  1 
ATOM 31   O OG  . SER A 1 36  ? 25.574 16.747  15.651  1.00 30.00  ? 36  SER A OG  1 
ATOM 32   N N   . TYR A 1 37  ? 26.575 16.884  12.968  1.00 30.00  ? 37  TYR A N   1 
ATOM 33   C CA  . TYR A 1 37  ? 27.301 15.996  12.022  1.00 30.00  ? 37  TYR A CA  1 
ATOM 34   C C   . TYR A 1 37  ? 28.078 16.845  11.010  1.00 30.00  ? 37  TYR A C   1 
ATOM 35   O O   . TYR A 1 37  ? 29.217 16.486  10.682  1.00 30.00  ? 37  TYR A O   1 
ATOM 36   C CB  . TYR A 1 37  ? 26.352 14.923  11.472  1.00 30.00  ? 37  TYR A CB  1 
ATOM 37   C CG  . TYR A 1 37  ? 25.615 15.163  10.181  1.00 30.00  ? 37  TYR A CG  1 
ATOM 38   C CD1 . TYR A 1 37  ? 24.255 15.420  10.185  1.00 30.00  ? 37  TYR A CD1 1 
ATOM 39   C CD2 . TYR A 1 37  ? 26.244 15.017  8.958   1.00 30.00  ? 37  TYR A CD2 1 
ATOM 40   C CE1 . TYR A 1 37  ? 23.549 15.593  9.007   1.00 30.00  ? 37  TYR A CE1 1 
ATOM 41   C CE2 . TYR A 1 37  ? 25.554 15.189  7.771   1.00 30.00  ? 37  TYR A CE2 1 
ATOM 42   C CZ  . TYR A 1 37  ? 24.202 15.478  7.796   1.00 30.00  ? 37  TYR A CZ  1 
ATOM 43   O OH  . TYR A 1 37  ? 23.517 15.646  6.630   1.00 30.00  ? 37  TYR A OH  1 
ATOM 44   N N   . LEU A 1 38  ? 27.498 17.961  10.580  1.00 30.00  ? 38  LEU A N   1 
ATOM 45   C CA  . LEU A 1 38  ? 28.164 18.809  9.562   1.00 30.00  ? 38  LEU A CA  1 
ATOM 46   C C   . LEU A 1 38  ? 28.412 20.196  10.163  1.00 30.00  ? 38  LEU A C   1 
ATOM 47   O O   . LEU A 1 38  ? 27.833 21.166  9.668   1.00 30.00  ? 38  LEU A O   1 
ATOM 48   C CB  . LEU A 1 38  ? 27.334 18.817  8.271   1.00 30.00  ? 38  LEU A CB  1 
ATOM 49   C CG  . LEU A 1 38  ? 25.913 19.372  8.312   1.00 30.00  ? 38  LEU A CG  1 
ATOM 50   C CD1 . LEU A 1 38  ? 25.328 19.371  6.911   1.00 30.00  ? 38  LEU A CD1 1 
ATOM 51   C CD2 . LEU A 1 38  ? 25.028 18.553  9.225   1.00 30.00  ? 38  LEU A CD2 1 
ATOM 52   N N   . LYS A 1 39  ? 29.272 20.265  11.183  1.00 30.00  ? 39  LYS A N   1 
ATOM 53   C CA  . LYS A 1 39  ? 29.576 21.545  11.871  1.00 30.00  ? 39  LYS A CA  1 
ATOM 54   C C   . LYS A 1 39  ? 30.881 22.122  11.329  1.00 30.00  ? 39  LYS A C   1 
ATOM 55   O O   . LYS A 1 39  ? 31.131 23.315  11.544  1.00 30.00  ? 39  LYS A O   1 
ATOM 56   C CB  . LYS A 1 39  ? 29.730 21.306  13.373  1.00 30.00  ? 39  LYS A CB  1 
ATOM 57   C CG  . LYS A 1 39  ? 31.140 20.969  13.835  1.00 30.00  ? 39  LYS A CG  1 
ATOM 58   C CD  . LYS A 1 39  ? 31.279 19.556  14.351  1.00 30.00  ? 39  LYS A CD  1 
ATOM 59   C CE  . LYS A 1 39  ? 31.724 18.574  13.288  1.00 30.00  ? 39  LYS A CE  1 
ATOM 60   N NZ  . LYS A 1 39  ? 32.352 17.374  13.889  1.00 30.00  ? 39  LYS A NZ  1 
ATOM 61   N N   . ASP A 1 40  ? 31.687 21.288  10.682  1.00 50.37  ? 40  ASP A N   1 
ATOM 62   C CA  . ASP A 1 40  ? 32.958 21.760  10.086  1.00 51.27  ? 40  ASP A CA  1 
ATOM 63   C C   . ASP A 1 40  ? 32.671 22.104  8.629   1.00 56.09  ? 40  ASP A C   1 
ATOM 64   O O   . ASP A 1 40  ? 33.624 22.193  7.851   1.00 51.96  ? 40  ASP A O   1 
ATOM 65   C CB  . ASP A 1 40  ? 34.061 20.719  10.264  1.00 50.36  ? 40  ASP A CB  1 
ATOM 66   C CG  . ASP A 1 40  ? 34.449 20.499  11.713  1.00 66.13  ? 40  ASP A CG  1 
ATOM 67   O OD1 . ASP A 1 40  ? 34.455 21.485  12.470  1.00 73.21  ? 40  ASP A OD1 1 
ATOM 68   O OD2 . ASP A 1 40  ? 34.745 19.346  12.070  1.00 61.95  ? 40  ASP A OD2 1 
ATOM 69   N N   . TYR A 1 41  ? 31.394 22.272  8.290   1.00 53.27  ? 41  TYR A N   1 
ATOM 70   C CA  . TYR A 1 41  ? 31.001 22.658  6.912   1.00 49.61  ? 41  TYR A CA  1 
ATOM 71   C C   . TYR A 1 41  ? 29.844 23.645  7.017   1.00 54.44  ? 41  TYR A C   1 
ATOM 72   O O   . TYR A 1 41  ? 29.014 23.700  6.101   1.00 58.59  ? 41  TYR A O   1 
ATOM 73   C CB  . TYR A 1 41  ? 30.608 21.431  6.091   1.00 56.16  ? 41  TYR A CB  1 
ATOM 74   C CG  . TYR A 1 41  ? 31.671 20.374  5.946   1.00 60.44  ? 41  TYR A CG  1 
ATOM 75   C CD1 . TYR A 1 41  ? 31.897 19.445  6.946   1.00 57.51  ? 41  TYR A CD1 1 
ATOM 76   C CD2 . TYR A 1 41  ? 32.438 20.289  4.798   1.00 57.40  ? 41  TYR A CD2 1 
ATOM 77   C CE1 . TYR A 1 41  ? 32.871 18.470  6.818   1.00 54.38  ? 41  TYR A CE1 1 
ATOM 78   C CE2 . TYR A 1 41  ? 33.413 19.318  4.651   1.00 61.78  ? 41  TYR A CE2 1 
ATOM 79   C CZ  . TYR A 1 41  ? 33.630 18.405  5.665   1.00 62.18  ? 41  TYR A CZ  1 
ATOM 80   O OH  . TYR A 1 41  ? 34.589 17.446  5.530   1.00 63.29  ? 41  TYR A OH  1 
ATOM 81   N N   . ALA A 1 42  ? 29.813 24.416  8.099   1.00 50.21  ? 42  ALA A N   1 
ATOM 82   C CA  . ALA A 1 42  ? 28.697 25.358  8.336   1.00 59.17  ? 42  ALA A CA  1 
ATOM 83   C C   . ALA A 1 42  ? 28.566 26.366  7.196   1.00 57.34  ? 42  ALA A C   1 
ATOM 84   O O   . ALA A 1 42  ? 27.496 26.437  6.591   1.00 59.52  ? 42  ALA A O   1 
ATOM 85   C CB  . ALA A 1 42  ? 28.927 26.055  9.644   1.00 58.88  ? 42  ALA A CB  1 
ATOM 86   N N   . ALA A 1 43  ? 29.615 27.138  6.946   1.00 57.56  ? 43  ALA A N   1 
ATOM 87   C CA  . ALA A 1 43  ? 29.597 28.120  5.846   1.00 54.76  ? 43  ALA A CA  1 
ATOM 88   C C   . ALA A 1 43  ? 28.931 27.515  4.607   1.00 60.17  ? 43  ALA A C   1 
ATOM 89   O O   . ALA A 1 43  ? 27.892 28.034  4.185   1.00 62.67  ? 43  ALA A O   1 
ATOM 90   C CB  . ALA A 1 43  ? 31.007 28.533  5.564   1.00 57.15  ? 43  ALA A CB  1 
ATOM 91   N N   . LEU A 1 44  ? 29.522 26.462  4.049   1.00 56.77  ? 44  LEU A N   1 
ATOM 92   C CA  . LEU A 1 44  ? 28.943 25.805  2.858   1.00 55.86  ? 44  LEU A CA  1 
ATOM 93   C C   . LEU A 1 44  ? 27.485 25.482  3.152   1.00 60.81  ? 44  LEU A C   1 
ATOM 94   O O   . LEU A 1 44  ? 26.644 25.673  2.265   1.00 64.05  ? 44  LEU A O   1 
ATOM 95   C CB  . LEU A 1 44  ? 29.726 24.529  2.559   1.00 65.48  ? 44  LEU A CB  1 
ATOM 96   C CG  . LEU A 1 44  ? 29.285 23.760  1.316   1.00 61.49  ? 44  LEU A CG  1 
ATOM 97   C CD1 . LEU A 1 44  ? 28.933 24.712  0.184   1.00 52.78  ? 44  LEU A CD1 1 
ATOM 98   C CD2 . LEU A 1 44  ? 30.366 22.787  0.876   1.00 64.37  ? 44  LEU A CD2 1 
ATOM 99   N N   . TYR A 1 45  ? 27.208 25.003  4.359   1.00 60.20  ? 45  TYR A N   1 
ATOM 100  C CA  . TYR A 1 45  ? 25.817 24.630  4.703   1.00 60.53  ? 45  TYR A CA  1 
ATOM 101  C C   . TYR A 1 45  ? 24.916 25.847  4.518   1.00 66.47  ? 45  TYR A C   1 
ATOM 102  O O   . TYR A 1 45  ? 23.835 25.702  3.934   1.00 66.15  ? 45  TYR A O   1 
ATOM 103  C CB  . TYR A 1 45  ? 25.720 24.122  6.139   1.00 53.96  ? 45  TYR A CB  1 
ATOM 104  C CG  . TYR A 1 45  ? 24.407 23.459  6.459   1.00 68.92  ? 45  TYR A CG  1 
ATOM 105  C CD1 . TYR A 1 45  ? 24.075 22.236  5.906   1.00 70.38  ? 45  TYR A CD1 1 
ATOM 106  C CD2 . TYR A 1 45  ? 23.486 24.064  7.295   1.00 68.66  ? 45  TYR A CD2 1 
ATOM 107  C CE1 . TYR A 1 45  ? 22.866 21.622  6.185   1.00 67.98  ? 45  TYR A CE1 1 
ATOM 108  C CE2 . TYR A 1 45  ? 22.273 23.464  7.585   1.00 68.85  ? 45  TYR A CE2 1 
ATOM 109  C CZ  . TYR A 1 45  ? 21.962 22.239  7.027   1.00 67.62  ? 45  TYR A CZ  1 
ATOM 110  O OH  . TYR A 1 45  ? 20.768 21.642  7.308   1.00 78.51  ? 45  TYR A OH  1 
ATOM 111  N N   . LYS A 1 46  ? 25.360 27.007  4.998   1.00 63.53  ? 46  LYS A N   1 
ATOM 112  C CA  . LYS A 1 46  ? 24.524 28.230  4.935   1.00 59.51  ? 46  LYS A CA  1 
ATOM 113  C C   . LYS A 1 46  ? 24.436 28.720  3.489   1.00 62.57  ? 46  LYS A C   1 
ATOM 114  O O   . LYS A 1 46  ? 23.820 29.771  3.262   1.00 60.98  ? 46  LYS A O   1 
ATOM 115  C CB  . LYS A 1 46  ? 25.117 29.279  5.874   1.00 56.81  ? 46  LYS A CB  1 
ATOM 116  C CG  . LYS A 1 46  ? 25.122 28.893  7.345   1.00 55.76  ? 46  LYS A CG  1 
ATOM 117  C CD  . LYS A 1 46  ? 26.280 29.489  8.108   1.00 58.56  ? 46  LYS A CD  1 
ATOM 118  C CE  . LYS A 1 46  ? 26.005 29.612  9.591   1.00 71.33  ? 46  LYS A CE  1 
ATOM 119  N NZ  . LYS A 1 46  ? 25.395 30.920  9.931   1.00 74.21  ? 46  LYS A NZ  1 
ATOM 120  N N   . LYS A 1 47  ? 25.007 27.965  2.554   1.00 59.57  ? 47  LYS A N   1 
ATOM 121  C CA  . LYS A 1 47  ? 24.939 28.338  1.123   1.00 65.08  ? 47  LYS A CA  1 
ATOM 122  C C   . LYS A 1 47  ? 24.277 27.206  0.343   1.00 62.46  ? 47  LYS A C   1 
ATOM 123  O O   . LYS A 1 47  ? 23.488 27.504  -0.561  1.00 58.55  ? 47  LYS A O   1 
ATOM 124  C CB  . LYS A 1 47  ? 26.347 28.618  0.603   1.00 65.15  ? 47  LYS A CB  1 
ATOM 125  C CG  . LYS A 1 47  ? 27.192 29.530  1.480   1.00 60.86  ? 47  LYS A CG  1 
ATOM 126  C CD  . LYS A 1 47  ? 28.649 29.551  1.083   1.00 58.16  ? 47  LYS A CD  1 
ATOM 127  C CE  . LYS A 1 47  ? 29.287 30.912  1.260   1.00 64.05  ? 47  LYS A CE  1 
ATOM 128  N NZ  . LYS A 1 47  ? 29.440 31.622  -0.031  1.00 55.89  ? 47  LYS A NZ  1 
ATOM 129  N N   . ASP A 1 48  ? 24.611 25.959  0.670   1.00 68.11  ? 48  ASP A N   1 
ATOM 130  C CA  . ASP A 1 48  ? 23.978 24.783  0.016   1.00 72.80  ? 48  ASP A CA  1 
ATOM 131  C C   . ASP A 1 48  ? 24.008 23.629  1.011   1.00 69.88  ? 48  ASP A C   1 
ATOM 132  O O   . ASP A 1 48  ? 25.029 22.933  1.086   1.00 72.94  ? 48  ASP A O   1 
ATOM 133  C CB  . ASP A 1 48  ? 24.637 24.411  -1.313  1.00 62.92  ? 48  ASP A CB  1 
ATOM 134  C CG  . ASP A 1 48  ? 23.816 23.448  -2.149  1.00 60.94  ? 48  ASP A CG  1 
ATOM 135  O OD1 . ASP A 1 48  ? 23.009 22.706  -1.563  1.00 67.29  ? 48  ASP A OD1 1 
ATOM 136  O OD2 . ASP A 1 48  ? 23.994 23.449  -3.379  1.00 52.60  ? 48  ASP A OD2 1 
ATOM 137  N N   . PRO A 1 49  ? 22.932 23.429  1.792   1.00 69.56  ? 49  PRO A N   1 
ATOM 138  C CA  . PRO A 1 49  ? 22.888 22.352  2.766   1.00 59.49  ? 49  PRO A CA  1 
ATOM 139  C C   . PRO A 1 49  ? 23.332 21.007  2.177   1.00 68.43  ? 49  PRO A C   1 
ATOM 140  O O   . PRO A 1 49  ? 24.187 20.387  2.760   1.00 64.51  ? 49  PRO A O   1 
ATOM 141  C CB  . PRO A 1 49  ? 21.398 22.333  3.102   1.00 65.43  ? 49  PRO A CB  1 
ATOM 142  C CG  . PRO A 1 49  ? 20.991 23.776  3.012   1.00 63.55  ? 49  PRO A CG  1 
ATOM 143  C CD  . PRO A 1 49  ? 21.728 24.260  1.786   1.00 68.46  ? 49  PRO A CD  1 
ATOM 144  N N   . ARG A 1 50  ? 22.762 20.598  1.043   1.00 67.20  ? 50  ARG A N   1 
ATOM 145  C CA  . ARG A 1 50  ? 23.080 19.255  0.491   1.00 62.39  ? 50  ARG A CA  1 
ATOM 146  C C   . ARG A 1 50  ? 24.544 19.225  0.066   1.00 61.15  ? 50  ARG A C   1 
ATOM 147  O O   . ARG A 1 50  ? 25.190 18.189  0.266   1.00 67.25  ? 50  ARG A O   1 
ATOM 148  C CB  . ARG A 1 50  ? 22.148 18.884  -0.665  1.00 68.18  ? 50  ARG A CB  1 
ATOM 149  C CG  . ARG A 1 50  ? 21.463 17.535  -0.498  1.00 62.37  ? 50  ARG A CG  1 
ATOM 150  C CD  . ARG A 1 50  ? 20.042 17.524  -1.028  1.00 67.70  ? 50  ARG A CD  1 
ATOM 151  N NE  . ARG A 1 50  ? 19.434 18.846  -0.981  1.00 79.25  ? 50  ARG A NE  1 
ATOM 152  C CZ  . ARG A 1 50  ? 18.996 19.519  -2.039  1.00 79.37  ? 50  ARG A CZ  1 
ATOM 153  N NH1 . ARG A 1 50  ? 19.091 18.994  -3.248  1.00 64.66  ? 50  ARG A NH1 1 
ATOM 154  N NH2 . ARG A 1 50  ? 18.464 20.718  -1.885  1.00 75.09  ? 50  ARG A NH2 1 
ATOM 155  N N   . ALA A 1 51  ? 25.043 20.317  -0.501  1.00 61.53  ? 51  ALA A N   1 
ATOM 156  C CA  . ALA A 1 51  ? 26.482 20.367  -0.825  1.00 64.37  ? 51  ALA A CA  1 
ATOM 157  C C   . ALA A 1 51  ? 27.258 20.035  0.441   1.00 63.56  ? 51  ALA A C   1 
ATOM 158  O O   . ALA A 1 51  ? 28.120 19.148  0.401   1.00 67.80  ? 51  ALA A O   1 
ATOM 159  C CB  . ALA A 1 51  ? 26.855 21.727  -1.323  1.00 60.23  ? 51  ALA A CB  1 
ATOM 160  N N   . ALA A 1 52  ? 26.944 20.734  1.523   1.00 54.91  ? 52  ALA A N   1 
ATOM 161  C CA  . ALA A 1 52  ? 27.666 20.504  2.786   1.00 61.04  ? 52  ALA A CA  1 
ATOM 162  C C   . ALA A 1 52  ? 27.621 19.014  3.104   1.00 63.63  ? 52  ALA A C   1 
ATOM 163  O O   . ALA A 1 52  ? 28.662 18.453  3.478   1.00 61.77  ? 52  ALA A O   1 
ATOM 164  C CB  . ALA A 1 52  ? 27.030 21.319  3.868   1.00 57.06  ? 52  ALA A CB  1 
ATOM 165  N N   . ALA A 1 53  ? 26.455 18.401  2.940   1.00 57.36  ? 53  ALA A N   1 
ATOM 166  C CA  . ALA A 1 53  ? 26.299 16.972  3.267   1.00 53.00  ? 53  ALA A CA  1 
ATOM 167  C C   . ALA A 1 53  ? 27.247 16.138  2.404   1.00 67.03  ? 53  ALA A C   1 
ATOM 168  O O   . ALA A 1 53  ? 28.023 15.351  2.963   1.00 63.55  ? 53  ALA A O   1 
ATOM 169  C CB  . ALA A 1 53  ? 24.869 16.583  3.041   1.00 55.63  ? 53  ALA A CB  1 
ATOM 170  N N   . LEU A 1 54  ? 27.168 16.301  1.086   1.00 66.91  ? 54  LEU A N   1 
ATOM 171  C CA  . LEU A 1 54  ? 28.039 15.529  0.171   1.00 63.67  ? 54  LEU A CA  1 
ATOM 172  C C   . LEU A 1 54  ? 29.496 15.741  0.585   1.00 64.88  ? 54  LEU A C   1 
ATOM 173  O O   . LEU A 1 54  ? 30.211 14.746  0.742   1.00 64.45  ? 54  LEU A O   1 
ATOM 174  C CB  . LEU A 1 54  ? 27.781 16.008  -1.258  1.00 62.50  ? 54  LEU A CB  1 
ATOM 175  C CG  . LEU A 1 54  ? 26.911 15.093  -2.113  1.00 59.59  ? 54  LEU A CG  1 
ATOM 176  C CD1 . LEU A 1 54  ? 26.923 13.676  -1.566  1.00 63.97  ? 54  LEU A CD1 1 
ATOM 177  C CD2 . LEU A 1 54  ? 25.490 15.625  -2.191  1.00 61.15  ? 54  LEU A CD2 1 
ATOM 178  N N   . GLN A 1 55  ? 29.905 16.991  0.772   1.00 55.74  ? 55  GLN A N   1 
ATOM 179  C CA  . GLN A 1 55  ? 31.299 17.297  1.174   1.00 59.28  ? 55  GLN A CA  1 
ATOM 180  C C   . GLN A 1 55  ? 31.656 16.494  2.420   1.00 58.75  ? 55  GLN A C   1 
ATOM 181  O O   . GLN A 1 55  ? 32.583 15.682  2.345   1.00 59.00  ? 55  GLN A O   1 
ATOM 182  C CB  . GLN A 1 55  ? 31.447 18.788  1.465   1.00 66.45  ? 55  GLN A CB  1 
ATOM 183  C CG  . GLN A 1 55  ? 32.602 19.445  0.728   1.00 62.12  ? 55  GLN A CG  1 
ATOM 184  C CD  . GLN A 1 55  ? 32.744 18.929  -0.681  1.00 63.00  ? 55  GLN A CD  1 
ATOM 185  O OE1 . GLN A 1 55  ? 31.804 18.955  -1.471  1.00 60.62  ? 55  GLN A OE1 1 
ATOM 186  N NE2 . GLN A 1 55  ? 33.933 18.453  -1.008  1.00 63.16  ? 55  GLN A NE2 1 
ATOM 187  N N   . TYR A 1 56  ? 30.953 16.740  3.521   1.00 55.97  ? 56  TYR A N   1 
ATOM 188  C CA  . TYR A 1 56  ? 31.184 15.953  4.752   1.00 51.70  ? 56  TYR A CA  1 
ATOM 189  C C   . TYR A 1 56  ? 31.295 14.483  4.388   1.00 58.42  ? 56  TYR A C   1 
ATOM 190  O O   . TYR A 1 56  ? 32.219 13.821  4.882   1.00 59.16  ? 56  TYR A O   1 
ATOM 191  C CB  . TYR A 1 56  ? 30.022 16.103  5.727   1.00 51.44  ? 56  TYR A CB  1 
ATOM 192  C CG  . TYR A 1 56  ? 29.961 15.052  6.804   1.00 53.52  ? 56  TYR A CG  1 
ATOM 193  C CD1 . TYR A 1 56  ? 30.710 15.175  7.960   1.00 50.37  ? 56  TYR A CD1 1 
ATOM 194  C CD2 . TYR A 1 56  ? 29.149 13.939  6.675   1.00 52.37  ? 56  TYR A CD2 1 
ATOM 195  C CE1 . TYR A 1 56  ? 30.659 14.219  8.959   1.00 44.43  ? 56  TYR A CE1 1 
ATOM 196  C CE2 . TYR A 1 56  ? 29.090 12.970  7.662   1.00 42.70  ? 56  TYR A CE2 1 
ATOM 197  C CZ  . TYR A 1 56  ? 29.847 13.113  8.809   1.00 39.49  ? 56  TYR A CZ  1 
ATOM 198  O OH  . TYR A 1 56  ? 29.797 12.171  9.791   1.00 46.47  ? 56  TYR A OH  1 
ATOM 199  N N   . PHE A 1 57  ? 30.391 13.993  3.540   1.00 52.63  ? 57  PHE A N   1 
ATOM 200  C CA  . PHE A 1 57  ? 30.421 12.558  3.280   1.00 60.70  ? 57  PHE A CA  1 
ATOM 201  C C   . PHE A 1 57  ? 31.689 12.146  2.539   1.00 54.87  ? 57  PHE A C   1 
ATOM 202  O O   . PHE A 1 57  ? 32.376 11.205  2.954   1.00 53.02  ? 57  PHE A O   1 
ATOM 203  C CB  . PHE A 1 57  ? 29.183 12.129  2.498   1.00 63.65  ? 57  PHE A CB  1 
ATOM 204  C CG  . PHE A 1 57  ? 29.056 10.643  2.363   1.00 52.29  ? 57  PHE A CG  1 
ATOM 205  C CD1 . PHE A 1 57  ? 28.879 9.847   3.482   1.00 59.40  ? 57  PHE A CD1 1 
ATOM 206  C CD2 . PHE A 1 57  ? 29.144 10.038  1.124   1.00 54.09  ? 57  PHE A CD2 1 
ATOM 207  C CE1 . PHE A 1 57  ? 28.774 8.475   3.364   1.00 55.03  ? 57  PHE A CE1 1 
ATOM 208  C CE2 . PHE A 1 57  ? 29.042 8.670   1.000   1.00 54.41  ? 57  PHE A CE2 1 
ATOM 209  C CZ  . PHE A 1 57  ? 28.855 7.887   2.121   1.00 46.32  ? 57  PHE A CZ  1 
ATOM 210  N N   . LYS A 1 58  ? 32.005 12.841  1.459   1.00 59.85  ? 58  LYS A N   1 
ATOM 211  C CA  . LYS A 1 58  ? 33.201 12.497  0.656   1.00 57.83  ? 58  LYS A CA  1 
ATOM 212  C C   . LYS A 1 58  ? 34.449 12.529  1.528   1.00 53.33  ? 58  LYS A C   1 
ATOM 213  O O   . LYS A 1 58  ? 35.441 11.900  1.145   1.00 61.14  ? 58  LYS A O   1 
ATOM 214  C CB  . LYS A 1 58  ? 33.390 13.526  -0.458  1.00 61.68  ? 58  LYS A CB  1 
ATOM 215  C CG  . LYS A 1 58  ? 32.171 13.802  -1.324  1.00 69.08  ? 58  LYS A CG  1 
ATOM 216  C CD  . LYS A 1 58  ? 32.218 15.160  -1.991  1.00 70.53  ? 58  LYS A CD  1 
ATOM 217  C CE  . LYS A 1 58  ? 31.789 15.130  -3.442  1.00 67.14  ? 58  LYS A CE  1 
ATOM 218  N NZ  . LYS A 1 58  ? 30.982 16.319  -3.799  1.00 66.14  ? 58  LYS A NZ  1 
ATOM 219  N N   . GLU A 1 59  ? 34.398 13.213  2.663   1.00 55.45  ? 59  GLU A N   1 
ATOM 220  C CA  . GLU A 1 59  ? 35.634 13.400  3.460   1.00 58.99  ? 59  GLU A CA  1 
ATOM 221  C C   . GLU A 1 59  ? 35.593 12.605  4.766   1.00 58.66  ? 59  GLU A C   1 
ATOM 222  O O   . GLU A 1 59  ? 36.629 12.556  5.438   1.00 60.68  ? 59  GLU A O   1 
ATOM 223  C CB  . GLU A 1 59  ? 35.814 14.897  3.700   1.00 55.86  ? 59  GLU A CB  1 
ATOM 224  C CG  . GLU A 1 59  ? 35.870 15.687  2.406   1.00 68.29  ? 59  GLU A CG  1 
ATOM 225  C CD  . GLU A 1 59  ? 36.080 17.186  2.530   1.00 69.17  ? 59  GLU A CD  1 
ATOM 226  O OE1 . GLU A 1 59  ? 36.344 17.655  3.649   1.00 65.63  ? 59  GLU A OE1 1 
ATOM 227  O OE2 . GLU A 1 59  ? 35.985 17.879  1.499   1.00 67.73  ? 59  GLU A OE2 1 
ATOM 228  N N   . ALA A 1 60  ? 34.450 12.011  5.105   1.00 57.23  ? 60  ALA A N   1 
ATOM 229  C CA  . ALA A 1 60  ? 34.320 11.252  6.368   1.00 54.71  ? 60  ALA A CA  1 
ATOM 230  C C   . ALA A 1 60  ? 35.262 10.055  6.328   1.00 49.11  ? 60  ALA A C   1 
ATOM 231  O O   . ALA A 1 60  ? 35.891 9.788   7.358   1.00 43.90  ? 60  ALA A O   1 
ATOM 232  C CB  . ALA A 1 60  ? 32.892 10.839  6.556   1.00 48.24  ? 60  ALA A CB  1 
ATOM 233  N N   . LYS A 1 61  ? 35.296 9.333   5.212   1.00 47.33  ? 61  LYS A N   1 
ATOM 234  C CA  . LYS A 1 61  ? 36.275 8.227   5.011   1.00 56.28  ? 61  LYS A CA  1 
ATOM 235  C C   . LYS A 1 61  ? 35.942 6.953   5.799   1.00 50.29  ? 61  LYS A C   1 
ATOM 236  O O   . LYS A 1 61  ? 36.160 5.874   5.238   1.00 50.04  ? 61  LYS A O   1 
ATOM 237  C CB  . LYS A 1 61  ? 37.685 8.740   5.317   1.00 54.32  ? 61  LYS A CB  1 
ATOM 238  C CG  . LYS A 1 61  ? 38.201 9.818   4.374   1.00 56.09  ? 61  LYS A CG  1 
ATOM 239  C CD  . LYS A 1 61  ? 37.548 9.780   3.009   1.00 68.19  ? 61  LYS A CD  1 
ATOM 240  C CE  . LYS A 1 61  ? 38.540 9.886   1.870   1.00 74.59  ? 61  LYS A CE  1 
ATOM 241  N NZ  . LYS A 1 61  ? 38.560 8.664   1.033   1.00 66.28  ? 61  LYS A NZ  1 
ATOM 242  N N   . PHE A 1 62  ? 35.442 7.061   7.028   1.00 50.26  ? 62  PHE A N   1 
ATOM 243  C CA  . PHE A 1 62  ? 35.235 5.850   7.864   1.00 46.21  ? 62  PHE A CA  1 
ATOM 244  C C   . PHE A 1 62  ? 33.904 5.931   8.612   1.00 48.27  ? 62  PHE A C   1 
ATOM 245  O O   . PHE A 1 62  ? 33.558 7.011   9.094   1.00 53.65  ? 62  PHE A O   1 
ATOM 246  C CB  . PHE A 1 62  ? 36.418 5.698   8.819   1.00 46.59  ? 62  PHE A CB  1 
ATOM 247  C CG  . PHE A 1 62  ? 36.657 4.314   9.362   1.00 53.99  ? 62  PHE A CG  1 
ATOM 248  C CD1 . PHE A 1 62  ? 36.025 3.211   8.814   1.00 49.31  ? 62  PHE A CD1 1 
ATOM 249  C CD2 . PHE A 1 62  ? 37.523 4.116   10.424  1.00 46.63  ? 62  PHE A CD2 1 
ATOM 250  C CE1 . PHE A 1 62  ? 36.250 1.943   9.322   1.00 41.90  ? 62  PHE A CE1 1 
ATOM 251  C CE2 . PHE A 1 62  ? 37.750 2.846   10.928  1.00 46.03  ? 62  PHE A CE2 1 
ATOM 252  C CZ  . PHE A 1 62  ? 37.115 1.762   10.374  1.00 38.00  ? 62  PHE A CZ  1 
ATOM 253  N N   . GLY A 1 63  ? 33.196 4.806   8.710   1.00 42.70  ? 63  GLY A N   1 
ATOM 254  C CA  . GLY A 1 63  ? 31.888 4.780   9.384   1.00 45.17  ? 63  GLY A CA  1 
ATOM 255  C C   . GLY A 1 63  ? 31.532 3.419   9.932   1.00 45.28  ? 63  GLY A C   1 
ATOM 256  O O   . GLY A 1 63  ? 32.131 2.436   9.497   1.00 45.96  ? 63  GLY A O   1 
ATOM 257  N N   . LEU A 1 64  ? 30.566 3.371   10.847  1.00 43.87  ? 64  LEU A N   1 
ATOM 258  C CA  . LEU A 1 64  ? 30.166 2.098   11.493  1.00 43.02  ? 64  LEU A CA  1 
ATOM 259  C C   . LEU A 1 64  ? 28.819 1.613   10.971  1.00 42.94  ? 64  LEU A C   1 
ATOM 260  O O   . LEU A 1 64  ? 27.856 2.374   11.042  1.00 41.26  ? 64  LEU A O   1 
ATOM 261  C CB  . LEU A 1 64  ? 30.073 2.323   13.002  1.00 41.28  ? 64  LEU A CB  1 
ATOM 262  C CG  . LEU A 1 64  ? 29.697 1.098   13.831  1.00 49.80  ? 64  LEU A CG  1 
ATOM 263  C CD1 . LEU A 1 64  ? 30.846 0.105   13.878  1.00 43.81  ? 64  LEU A CD1 1 
ATOM 264  C CD2 . LEU A 1 64  ? 29.291 1.505   15.236  1.00 38.57  ? 64  LEU A CD2 1 
ATOM 265  N N   . PHE A 1 65  ? 28.770 0.380   10.476  1.00 36.91  ? 65  PHE A N   1 
ATOM 266  C CA  . PHE A 1 65  ? 27.477 -0.212  10.065  1.00 41.78  ? 65  PHE A CA  1 
ATOM 267  C C   . PHE A 1 65  ? 27.031 -1.148  11.186  1.00 47.81  ? 65  PHE A C   1 
ATOM 268  O O   . PHE A 1 65  ? 27.874 -1.848  11.750  1.00 43.61  ? 65  PHE A O   1 
ATOM 269  C CB  . PHE A 1 65  ? 27.609 -0.933  8.724   1.00 45.41  ? 65  PHE A CB  1 
ATOM 270  C CG  . PHE A 1 65  ? 26.402 -0.880  7.825   1.00 42.40  ? 65  PHE A CG  1 
ATOM 271  C CD1 . PHE A 1 65  ? 25.208 -0.338  8.264   1.00 43.36  ? 65  PHE A CD1 1 
ATOM 272  C CD2 . PHE A 1 65  ? 26.464 -1.380  6.536   1.00 36.01  ? 65  PHE A CD2 1 
ATOM 273  C CE1 . PHE A 1 65  ? 24.103 -0.293  7.431   1.00 37.31  ? 65  PHE A CE1 1 
ATOM 274  C CE2 . PHE A 1 65  ? 25.358 -1.331  5.703   1.00 41.03  ? 65  PHE A CE2 1 
ATOM 275  C CZ  . PHE A 1 65  ? 24.181 -0.785  6.152   1.00 34.68  ? 65  PHE A CZ  1 
ATOM 276  N N   . ILE A 1 66  ? 25.742 -1.113  11.518  1.00 47.27  ? 66  ILE A N   1 
ATOM 277  C CA  . ILE A 1 66  ? 25.198 -1.964  12.609  1.00 41.20  ? 66  ILE A CA  1 
ATOM 278  C C   . ILE A 1 66  ? 24.040 -2.777  12.048  1.00 41.19  ? 66  ILE A C   1 
ATOM 279  O O   . ILE A 1 66  ? 23.115 -2.178  11.503  1.00 43.54  ? 66  ILE A O   1 
ATOM 280  C CB  . ILE A 1 66  ? 24.764 -1.106  13.808  1.00 32.61  ? 66  ILE A CB  1 
ATOM 281  C CG1 . ILE A 1 66  ? 25.838 -0.086  14.187  1.00 46.01  ? 66  ILE A CG1 1 
ATOM 282  C CG2 . ILE A 1 66  ? 24.382 -1.984  14.984  1.00 37.75  ? 66  ILE A CG2 1 
ATOM 283  C CD1 . ILE A 1 66  ? 25.321 1.055   15.022  1.00 53.63  ? 66  ILE A CD1 1 
ATOM 284  N N   . HIS A 1 67  ? 24.122 -4.099  12.166  1.00 44.66  ? 67  HIS A N   1 
ATOM 285  C CA  . HIS A 1 67  ? 23.008 -4.973  11.726  1.00 48.15  ? 67  HIS A CA  1 
ATOM 286  C C   . HIS A 1 67  ? 22.439 -5.681  12.954  1.00 49.22  ? 67  HIS A C   1 
ATOM 287  O O   . HIS A 1 67  ? 22.932 -6.766  13.281  1.00 52.76  ? 67  HIS A O   1 
ATOM 288  C CB  . HIS A 1 67  ? 23.466 -5.940  10.629  1.00 39.62  ? 67  HIS A CB  1 
ATOM 289  C CG  . HIS A 1 67  ? 23.520 -5.342  9.265   1.00 41.40  ? 67  HIS A CG  1 
ATOM 290  N ND1 . HIS A 1 67  ? 24.301 -4.249  8.971   1.00 46.94  ? 67  HIS A ND1 1 
ATOM 291  C CD2 . HIS A 1 67  ? 22.903 -5.685  8.116   1.00 51.20  ? 67  HIS A CD2 1 
ATOM 292  C CE1 . HIS A 1 67  ? 24.161 -3.940  7.700   1.00 44.16  ? 67  HIS A CE1 1 
ATOM 293  N NE2 . HIS A 1 67  ? 23.307 -4.803  7.154   1.00 46.02  ? 67  HIS A NE2 1 
ATOM 294  N N   . TYR A 1 68  ? 21.461 -5.061  13.617  1.00 47.79  ? 68  TYR A N   1 
ATOM 295  C CA  . TYR A 1 68  ? 20.787 -5.693  14.778  1.00 47.46  ? 68  TYR A CA  1 
ATOM 296  C C   . TYR A 1 68  ? 19.313 -5.902  14.445  1.00 52.23  ? 68  TYR A C   1 
ATOM 297  O O   . TYR A 1 68  ? 18.714 -5.028  13.816  1.00 49.65  ? 68  TYR A O   1 
ATOM 298  C CB  . TYR A 1 68  ? 20.941 -4.845  16.038  1.00 48.09  ? 68  TYR A CB  1 
ATOM 299  C CG  . TYR A 1 68  ? 20.531 -5.522  17.320  1.00 49.94  ? 68  TYR A CG  1 
ATOM 300  C CD1 . TYR A 1 68  ? 21.024 -6.769  17.661  1.00 51.22  ? 68  TYR A CD1 1 
ATOM 301  C CD2 . TYR A 1 68  ? 19.654 -4.910  18.198  1.00 51.72  ? 68  TYR A CD2 1 
ATOM 302  C CE1 . TYR A 1 68  ? 20.652 -7.393  18.839  1.00 54.39  ? 68  TYR A CE1 1 
ATOM 303  C CE2 . TYR A 1 68  ? 19.273 -5.519  19.380  1.00 47.16  ? 68  TYR A CE2 1 
ATOM 304  C CZ  . TYR A 1 68  ? 19.773 -6.766  19.701  1.00 47.52  ? 68  TYR A CZ  1 
ATOM 305  O OH  . TYR A 1 68  ? 19.398 -7.368  20.865  1.00 46.06  ? 68  TYR A OH  1 
ATOM 306  N N   . GLY A 1 69  ? 18.761 -7.040  14.858  1.00 53.63  ? 69  GLY A N   1 
ATOM 307  C CA  . GLY A 1 69  ? 17.353 -7.361  14.578  1.00 49.13  ? 69  GLY A CA  1 
ATOM 308  C C   . GLY A 1 69  ? 16.999 -8.735  15.099  1.00 52.61  ? 69  GLY A C   1 
ATOM 309  O O   . GLY A 1 69  ? 17.799 -9.300  15.856  1.00 51.84  ? 69  GLY A O   1 
ATOM 310  N N   . LEU A 1 70  ? 15.848 -9.260  14.692  1.00 51.50  ? 70  LEU A N   1 
ATOM 311  C CA  . LEU A 1 70  ? 15.384 -10.567 15.214  1.00 47.10  ? 70  LEU A CA  1 
ATOM 312  C C   . LEU A 1 70  ? 16.350 -11.658 14.759  1.00 49.75  ? 70  LEU A C   1 
ATOM 313  O O   . LEU A 1 70  ? 16.505 -12.644 15.483  1.00 55.15  ? 70  LEU A O   1 
ATOM 314  C CB  . LEU A 1 70  ? 13.959 -10.812 14.707  1.00 36.41  ? 70  LEU A CB  1 
ATOM 315  C CG  . LEU A 1 70  ? 12.909 -9.796  15.147  1.00 48.01  ? 70  LEU A CG  1 
ATOM 316  C CD1 . LEU A 1 70  ? 11.518 -10.257 14.745  1.00 45.12  ? 70  LEU A CD1 1 
ATOM 317  C CD2 . LEU A 1 70  ? 12.975 -9.563  16.645  1.00 48.62  ? 70  LEU A CD2 1 
ATOM 318  N N   . TYR A 1 71  ? 16.986 -11.468 13.610  1.00 48.86  ? 71  TYR A N   1 
ATOM 319  C CA  . TYR A 1 71  ? 17.918 -12.477 13.053  1.00 51.27  ? 71  TYR A CA  1 
ATOM 320  C C   . TYR A 1 71  ? 19.088 -12.689 14.007  1.00 52.27  ? 71  TYR A C   1 
ATOM 321  O O   . TYR A 1 71  ? 19.691 -13.772 14.001  1.00 46.93  ? 71  TYR A O   1 
ATOM 322  C CB  . TYR A 1 71  ? 18.409 -12.005 11.685  1.00 48.81  ? 71  TYR A CB  1 
ATOM 323  C CG  . TYR A 1 71  ? 18.735 -10.540 11.554  1.00 46.67  ? 71  TYR A CG  1 
ATOM 324  C CD1 . TYR A 1 71  ? 19.960 -10.038 11.959  1.00 51.88  ? 71  TYR A CD1 1 
ATOM 325  C CD2 . TYR A 1 71  ? 17.835 -9.658  10.984  1.00 49.77  ? 71  TYR A CD2 1 
ATOM 326  C CE1 . TYR A 1 71  ? 20.272 -8.696  11.827  1.00 47.52  ? 71  TYR A CE1 1 
ATOM 327  C CE2 . TYR A 1 71  ? 18.131 -8.314  10.842  1.00 47.23  ? 71  TYR A CE2 1 
ATOM 328  C CZ  . TYR A 1 71  ? 19.354 -7.830  11.264  1.00 45.63  ? 71  TYR A CZ  1 
ATOM 329  O OH  . TYR A 1 71  ? 19.647 -6.507  11.126  1.00 52.14  ? 71  TYR A OH  1 
ATOM 330  N N   . SER A 1 72  ? 19.391 -11.671 14.802  1.00 46.84  ? 72  SER A N   1 
ATOM 331  C CA  . SER A 1 72  ? 20.553 -11.738 15.717  1.00 49.30  ? 72  SER A CA  1 
ATOM 332  C C   . SER A 1 72  ? 20.292 -12.780 16.805  1.00 58.91  ? 72  SER A C   1 
ATOM 333  O O   . SER A 1 72  ? 21.262 -13.250 17.408  1.00 57.61  ? 72  SER A O   1 
ATOM 334  C CB  . SER A 1 72  ? 20.822 -10.378 16.285  1.00 51.61  ? 72  SER A CB  1 
ATOM 335  O OG  . SER A 1 72  ? 20.393 -9.362  15.394  1.00 42.35  ? 72  SER A OG  1 
ATOM 336  N N   . LEU A 1 73  ? 19.029 -13.155 17.004  1.00 58.24  ? 73  LEU A N   1 
ATOM 337  C CA  . LEU A 1 73  ? 18.667 -14.116 18.073  1.00 53.71  ? 73  LEU A CA  1 
ATOM 338  C C   . LEU A 1 73  ? 18.949 -15.541 17.601  1.00 54.13  ? 73  LEU A C   1 
ATOM 339  O O   . LEU A 1 73  ? 19.300 -16.374 18.444  1.00 63.69  ? 73  LEU A O   1 
ATOM 340  C CB  . LEU A 1 73  ? 17.183 -13.934 18.401  1.00 55.52  ? 73  LEU A CB  1 
ATOM 341  C CG  . LEU A 1 73  ? 16.720 -12.493 18.605  1.00 59.89  ? 73  LEU A CG  1 
ATOM 342  C CD1 . LEU A 1 73  ? 15.216 -12.437 18.818  1.00 60.58  ? 73  LEU A CD1 1 
ATOM 343  C CD2 . LEU A 1 73  ? 17.447 -11.848 19.772  1.00 54.15  ? 73  LEU A CD2 1 
ATOM 344  N N   . LEU A 1 74  ? 18.784 -15.804 16.305  1.00 57.66  ? 74  LEU A N   1 
ATOM 345  C CA  . LEU A 1 74  ? 19.043 -17.154 15.744  1.00 47.80  ? 74  LEU A CA  1 
ATOM 346  C C   . LEU A 1 74  ? 20.539 -17.299 15.485  1.00 53.11  ? 74  LEU A C   1 
ATOM 347  O O   . LEU A 1 74  ? 21.015 -18.440 15.479  1.00 62.53  ? 74  LEU A O   1 
ATOM 348  C CB  . LEU A 1 74  ? 18.229 -17.319 14.463  1.00 43.10  ? 74  LEU A CB  1 
ATOM 349  C CG  . LEU A 1 74  ? 16.716 -17.281 14.650  1.00 49.51  ? 74  LEU A CG  1 
ATOM 350  C CD1 . LEU A 1 74  ? 16.000 -17.486 13.326  1.00 44.76  ? 74  LEU A CD1 1 
ATOM 351  C CD2 . LEU A 1 74  ? 16.277 -18.328 15.659  1.00 50.96  ? 74  LEU A CD2 1 
ATOM 352  N N   . GLY A 1 75  ? 21.247 -16.191 15.272  1.00 50.40  ? 75  GLY A N   1 
ATOM 353  C CA  . GLY A 1 75  ? 22.716 -16.238 15.127  1.00 52.80  ? 75  GLY A CA  1 
ATOM 354  C C   . GLY A 1 75  ? 23.180 -17.084 13.965  1.00 51.40  ? 75  GLY A C   1 
ATOM 355  O O   . GLY A 1 75  ? 24.215 -17.746 14.100  1.00 51.61  ? 75  GLY A O   1 
ATOM 356  N N   . ARG A 1 76  ? 22.453 -17.042 12.856  1.00 48.80  ? 76  ARG A N   1 
ATOM 357  C CA  . ARG A 1 76  ? 22.811 -17.841 11.662  1.00 52.79  ? 76  ARG A CA  1 
ATOM 358  C C   . ARG A 1 76  ? 22.919 -16.905 10.459  1.00 51.24  ? 76  ARG A C   1 
ATOM 359  O O   . ARG A 1 76  ? 22.943 -17.403 9.326   1.00 46.10  ? 76  ARG A O   1 
ATOM 360  C CB  . ARG A 1 76  ? 21.740 -18.906 11.415  1.00 53.14  ? 76  ARG A CB  1 
ATOM 361  C CG  . ARG A 1 76  ? 21.453 -19.816 12.598  1.00 53.97  ? 76  ARG A CG  1 
ATOM 362  C CD  . ARG A 1 76  ? 20.668 -21.019 12.116  1.00 48.27  ? 76  ARG A CD  1 
ATOM 363  N NE  . ARG A 1 76  ? 19.416 -21.199 12.833  1.00 63.45  ? 76  ARG A NE  1 
ATOM 364  C CZ  . ARG A 1 76  ? 18.264 -21.523 12.262  1.00 68.18  ? 76  ARG A CZ  1 
ATOM 365  N NH1 . ARG A 1 76  ? 18.200 -21.701 10.954  1.00 61.83  ? 76  ARG A NH1 1 
ATOM 366  N NH2 . ARG A 1 76  ? 17.178 -21.670 13.000  1.00 59.68  ? 76  ARG A NH2 1 
ATOM 367  N N   . GLY A 1 77  ? 22.977 -15.601 10.707  1.00 44.88  ? 77  GLY A N   1 
ATOM 368  C CA  . GLY A 1 77  ? 23.009 -14.625 9.609   1.00 44.89  ? 77  GLY A CA  1 
ATOM 369  C C   . GLY A 1 77  ? 21.766 -13.762 9.600   1.00 51.88  ? 77  GLY A C   1 
ATOM 370  O O   . GLY A 1 77  ? 20.911 -13.964 10.464  1.00 50.68  ? 77  GLY A O   1 
ATOM 371  N N   . GLU A 1 78  ? 21.661 -12.855 8.634   1.00 57.88  ? 78  GLU A N   1 
ATOM 372  C CA  . GLU A 1 78  ? 20.519 -11.910 8.558   1.00 54.05  ? 78  GLU A CA  1 
ATOM 373  C C   . GLU A 1 78  ? 19.522 -12.399 7.507   1.00 53.88  ? 78  GLU A C   1 
ATOM 374  O O   . GLU A 1 78  ? 18.436 -11.809 7.402   1.00 51.77  ? 78  GLU A O   1 
ATOM 375  C CB  . GLU A 1 78  ? 21.051 -10.520 8.210   1.00 52.06  ? 78  GLU A CB  1 
ATOM 376  C CG  . GLU A 1 78  ? 21.411 -10.341 6.749   1.00 49.67  ? 78  GLU A CG  1 
ATOM 377  C CD  . GLU A 1 78  ? 22.820 -10.777 6.393   1.00 51.51  ? 78  GLU A CD  1 
ATOM 378  O OE1 . GLU A 1 78  ? 23.563 -11.148 7.309   1.00 48.38  ? 78  GLU A OE1 1 
ATOM 379  O OE2 . GLU A 1 78  ? 23.162 -10.752 5.200   1.00 50.81  ? 78  GLU A OE2 1 
ATOM 380  N N   . TRP A 1 79  ? 19.890 -13.442 6.769   1.00 47.65  ? 79  TRP A N   1 
ATOM 381  C CA  . TRP A 1 79  ? 19.013 -13.953 5.695   1.00 46.94  ? 79  TRP A CA  1 
ATOM 382  C C   . TRP A 1 79  ? 18.397 -15.267 6.152   1.00 50.11  ? 79  TRP A C   1 
ATOM 383  O O   . TRP A 1 79  ? 17.866 -15.988 5.306   1.00 51.12  ? 79  TRP A O   1 
ATOM 384  C CB  . TRP A 1 79  ? 19.821 -14.121 4.409   1.00 52.08  ? 79  TRP A CB  1 
ATOM 385  C CG  . TRP A 1 79  ? 19.911 -12.888 3.567   1.00 61.42  ? 79  TRP A CG  1 
ATOM 386  C CD1 . TRP A 1 79  ? 20.450 -11.686 3.919   1.00 65.58  ? 79  TRP A CD1 1 
ATOM 387  C CD2 . TRP A 1 79  ? 19.455 -12.737 2.212   1.00 62.46  ? 79  TRP A CD2 1 
ATOM 388  N NE1 . TRP A 1 79  ? 20.356 -10.798 2.883   1.00 59.41  ? 79  TRP A NE1 1 
ATOM 389  C CE2 . TRP A 1 79  ? 19.749 -11.415 1.823   1.00 64.22  ? 79  TRP A CE2 1 
ATOM 390  C CE3 . TRP A 1 79  ? 18.826 -13.586 1.297   1.00 63.07  ? 79  TRP A CE3 1 
ATOM 391  C CZ2 . TRP A 1 79  ? 19.434 -10.925 0.558   1.00 62.79  ? 79  TRP A CZ2 1 
ATOM 392  C CZ3 . TRP A 1 79  ? 18.517 -13.101 0.047   1.00 64.87  ? 79  TRP A CZ3 1 
ATOM 393  C CH2 . TRP A 1 79  ? 18.817 -11.789 -0.315  1.00 63.05  ? 79  TRP A CH2 1 
ATOM 394  N N   . VAL A 1 80  ? 18.421 -15.528 7.452   1.00 47.64  ? 80  VAL A N   1 
ATOM 395  C CA  . VAL A 1 80  ? 17.931 -16.832 7.985   1.00 51.12  ? 80  VAL A CA  1 
ATOM 396  C C   . VAL A 1 80  ? 16.482 -17.080 7.551   1.00 56.20  ? 80  VAL A C   1 
ATOM 397  O O   . VAL A 1 80  ? 16.152 -18.245 7.300   1.00 57.36  ? 80  VAL A O   1 
ATOM 398  C CB  . VAL A 1 80  ? 18.105 -16.901 9.514   1.00 51.60  ? 80  VAL A CB  1 
ATOM 399  C CG1 . VAL A 1 80  ? 17.328 -15.812 10.234  1.00 49.90  ? 80  VAL A CG1 1 
ATOM 400  C CG2 . VAL A 1 80  ? 17.775 -18.275 10.070  1.00 47.52  ? 80  VAL A CG2 1 
ATOM 401  N N   . GLN A 1 81  ? 15.645 -16.044 7.473   1.00 50.78  ? 81  GLN A N   1 
ATOM 402  C CA  . GLN A 1 81  ? 14.220 -16.279 7.142   1.00 48.98  ? 81  GLN A CA  1 
ATOM 403  C C   . GLN A 1 81  ? 14.182 -16.964 5.783   1.00 60.19  ? 81  GLN A C   1 
ATOM 404  O O   . GLN A 1 81  ? 13.356 -17.866 5.598   1.00 59.11  ? 81  GLN A O   1 
ATOM 405  C CB  . GLN A 1 81  ? 13.433 -14.972 7.111   1.00 45.42  ? 81  GLN A CB  1 
ATOM 406  C CG  . GLN A 1 81  ? 12.012 -15.130 6.594   1.00 51.48  ? 81  GLN A CG  1 
ATOM 407  C CD  . GLN A 1 81  ? 11.178 -13.891 6.800   1.00 56.04  ? 81  GLN A CD  1 
ATOM 408  O OE1 . GLN A 1 81  ? 11.603 -12.932 7.438   1.00 62.30  ? 81  GLN A OE1 1 
ATOM 409  N NE2 . GLN A 1 81  ? 9.972  -13.903 6.260   1.00 50.92  ? 81  GLN A NE2 1 
ATOM 410  N N   . LEU A 1 82  ? 15.071 -16.551 4.883   1.00 57.36  ? 82  LEU A N   1 
ATOM 411  C CA  . LEU A 1 82  ? 15.133 -17.163 3.538   1.00 56.54  ? 82  LEU A CA  1 
ATOM 412  C C   . LEU A 1 82  ? 15.970 -18.435 3.614   1.00 58.81  ? 82  LEU A C   1 
ATOM 413  O O   . LEU A 1 82  ? 15.466 -19.494 3.222   1.00 60.13  ? 82  LEU A O   1 
ATOM 414  C CB  . LEU A 1 82  ? 15.763 -16.148 2.584   1.00 52.55  ? 82  LEU A CB  1 
ATOM 415  C CG  . LEU A 1 82  ? 15.638 -16.473 1.097   1.00 54.01  ? 82  LEU A CG  1 
ATOM 416  C CD1 . LEU A 1 82  ? 15.258 -15.238 0.300   1.00 48.02  ? 82  LEU A CD1 1 
ATOM 417  C CD2 . LEU A 1 82  ? 16.929 -17.067 0.564   1.00 61.18  ? 82  LEU A CD2 1 
ATOM 418  N N   . GLN A 1 83  ? 17.186 -18.333 4.137   1.00 57.53  ? 83  GLN A N   1 
ATOM 419  C CA  . GLN A 1 83  ? 18.112 -19.490 4.164   1.00 57.31  ? 83  GLN A CA  1 
ATOM 420  C C   . GLN A 1 83  ? 17.574 -20.597 5.069   1.00 59.02  ? 83  GLN A C   1 
ATOM 421  O O   . GLN A 1 83  ? 18.161 -21.686 5.062   1.00 61.31  ? 83  GLN A O   1 
ATOM 422  C CB  . GLN A 1 83  ? 19.484 -19.003 4.620   1.00 53.05  ? 83  GLN A CB  1 
ATOM 423  C CG  . GLN A 1 83  ? 19.989 -17.800 3.841   1.00 53.79  ? 83  GLN A CG  1 
ATOM 424  C CD  . GLN A 1 83  ? 21.257 -17.245 4.437   1.00 49.01  ? 83  GLN A CD  1 
ATOM 425  O OE1 . GLN A 1 83  ? 21.531 -17.407 5.622   1.00 51.10  ? 83  GLN A OE1 1 
ATOM 426  N NE2 . GLN A 1 83  ? 22.046 -16.581 3.611   1.00 56.99  ? 83  GLN A NE2 1 
ATOM 427  N N   . GLY A 1 84  ? 16.505 -20.330 5.814   1.00 57.27  ? 84  GLY A N   1 
ATOM 428  C CA  . GLY A 1 84  ? 15.894 -21.361 6.672   1.00 54.21  ? 84  GLY A CA  1 
ATOM 429  C C   . GLY A 1 84  ? 14.446 -21.577 6.297   1.00 63.65  ? 84  GLY A C   1 
ATOM 430  O O   . GLY A 1 84  ? 13.790 -22.402 6.946   1.00 60.40  ? 84  GLY A O   1 
ATOM 431  N N   . LYS A 1 85  ? 13.966 -20.848 5.291   1.00 63.70  ? 85  LYS A N   1 
ATOM 432  C CA  . LYS A 1 85  ? 12.563 -20.981 4.832   1.00 60.28  ? 85  LYS A CA  1 
ATOM 433  C C   . LYS A 1 85  ? 11.642 -20.920 6.046   1.00 58.42  ? 85  LYS A C   1 
ATOM 434  O O   . LYS A 1 85  ? 10.597 -21.574 6.019   1.00 69.13  ? 85  LYS A O   1 
ATOM 435  C CB  . LYS A 1 85  ? 12.393 -22.274 4.036   1.00 63.03  ? 85  LYS A CB  1 
ATOM 436  C CG  . LYS A 1 85  ? 12.861 -22.209 2.589   1.00 67.55  ? 85  LYS A CG  1 
ATOM 437  C CD  . LYS A 1 85  ? 13.451 -23.510 2.094   1.00 76.63  ? 85  LYS A CD  1 
ATOM 438  C CE  . LYS A 1 85  ? 12.640 -24.143 0.984   1.00 89.48  ? 85  LYS A CE  1 
ATOM 439  N NZ  . LYS A 1 85  ? 12.991 -25.569 0.779   1.00 82.04  ? 85  LYS A NZ  1 
ATOM 440  N N   . ILE A 1 86  ? 12.021 -20.143 7.057   1.00 60.14  ? 86  ILE A N   1 
ATOM 441  C CA  . ILE A 1 86  ? 11.154 -19.970 8.257   1.00 64.31  ? 86  ILE A CA  1 
ATOM 442  C C   . ILE A 1 86  ? 9.910  -19.200 7.824   1.00 66.37  ? 86  ILE A C   1 
ATOM 443  O O   . ILE A 1 86  ? 10.044 -18.079 7.324   1.00 65.85  ? 86  ILE A O   1 
ATOM 444  C CB  . ILE A 1 86  ? 11.908 -19.253 9.390   1.00 59.27  ? 86  ILE A CB  1 
ATOM 445  C CG1 . ILE A 1 86  ? 13.246 -19.930 9.693   1.00 53.21  ? 86  ILE A CG1 1 
ATOM 446  C CG2 . ILE A 1 86  ? 11.033 -19.140 10.627  1.00 52.41  ? 86  ILE A CG2 1 
ATOM 447  C CD1 . ILE A 1 86  ? 14.255 -19.019 10.340  1.00 44.91  ? 86  ILE A CD1 1 
ATOM 448  N N   . PRO A 1 87  ? 8.708  -19.780 7.970   1.00 71.79  ? 87  PRO A N   1 
ATOM 449  C CA  . PRO A 1 87  ? 7.481  -19.108 7.568   1.00 74.97  ? 87  PRO A CA  1 
ATOM 450  C C   . PRO A 1 87  ? 7.296  -17.784 8.317   1.00 66.14  ? 87  PRO A C   1 
ATOM 451  O O   . PRO A 1 87  ? 7.855  -17.644 9.377   1.00 68.18  ? 87  PRO A O   1 
ATOM 452  C CB  . PRO A 1 87  ? 6.402  -20.120 7.972   1.00 73.90  ? 87  PRO A CB  1 
ATOM 453  C CG  . PRO A 1 87  ? 7.113  -21.447 7.951   1.00 69.31  ? 87  PRO A CG  1 
ATOM 454  C CD  . PRO A 1 87  ? 8.483  -21.122 8.499   1.00 72.80  ? 87  PRO A CD  1 
ATOM 455  N N   . VAL A 1 88  ? 6.497  -16.872 7.767   1.00 63.91  ? 88  VAL A N   1 
ATOM 456  C CA  . VAL A 1 88  ? 6.312  -15.519 8.371   1.00 63.92  ? 88  VAL A CA  1 
ATOM 457  C C   . VAL A 1 88  ? 5.848  -15.615 9.830   1.00 65.61  ? 88  VAL A C   1 
ATOM 458  O O   . VAL A 1 88  ? 6.396  -14.872 10.661  1.00 60.67  ? 88  VAL A O   1 
ATOM 459  C CB  . VAL A 1 88  ? 5.331  -14.689 7.524   1.00 61.45  ? 88  VAL A CB  1 
ATOM 460  C CG1 . VAL A 1 88  ? 4.938  -13.396 8.217   1.00 64.93  ? 88  VAL A CG1 1 
ATOM 461  C CG2 . VAL A 1 88  ? 5.877  -14.411 6.135   1.00 58.56  ? 88  VAL A CG2 1 
ATOM 462  N N   . ARG A 1 89  ? 4.896  -16.496 10.138  1.00 70.49  ? 89  ARG A N   1 
ATOM 463  C CA  . ARG A 1 89  ? 4.317  -16.564 11.508  1.00 69.25  ? 89  ARG A CA  1 
ATOM 464  C C   . ARG A 1 89  ? 5.331  -17.109 12.505  1.00 64.71  ? 89  ARG A C   1 
ATOM 465  O O   . ARG A 1 89  ? 5.415  -16.583 13.624  1.00 62.04  ? 89  ARG A O   1 
ATOM 466  C CB  . ARG A 1 89  ? 3.097  -17.482 11.505  1.00 83.95  ? 89  ARG A CB  1 
ATOM 467  C CG  . ARG A 1 89  ? 2.735  -18.031 12.878  1.00 98.43  ? 89  ARG A CG  1 
ATOM 468  C CD  . ARG A 1 89  ? 1.698  -19.134 12.803  1.00 105.58 ? 89  ARG A CD  1 
ATOM 469  N NE  . ARG A 1 89  ? 1.464  -19.763 14.095  1.00 111.43 ? 89  ARG A NE  1 
ATOM 470  C CZ  . ARG A 1 89  ? 2.155  -20.794 14.565  1.00 116.49 ? 89  ARG A CZ  1 
ATOM 471  N NH1 . ARG A 1 89  ? 3.136  -21.317 13.850  1.00 108.76 ? 89  ARG A NH1 1 
ATOM 472  N NH2 . ARG A 1 89  ? 1.865  -21.297 15.751  1.00 121.88 ? 89  ARG A NH2 1 
ATOM 473  N N   . GLU A 1 90  ? 6.056  -18.139 12.103  1.00 66.75  ? 90  GLU A N   1 
ATOM 474  C CA  . GLU A 1 90  ? 7.069  -18.740 12.996  1.00 70.23  ? 90  GLU A CA  1 
ATOM 475  C C   . GLU A 1 90  ? 8.151  -17.704 13.309  1.00 65.38  ? 90  GLU A C   1 
ATOM 476  O O   . GLU A 1 90  ? 8.613  -17.675 14.453  1.00 58.17  ? 90  GLU A O   1 
ATOM 477  C CB  . GLU A 1 90  ? 7.631  -19.978 12.302  1.00 76.77  ? 90  GLU A CB  1 
ATOM 478  C CG  . GLU A 1 90  ? 7.717  -21.196 13.201  1.00 83.60  ? 90  GLU A CG  1 
ATOM 479  C CD  . GLU A 1 90  ? 8.743  -22.224 12.755  1.00 95.17  ? 90  GLU A CD  1 
ATOM 480  O OE1 . GLU A 1 90  ? 8.366  -23.400 12.588  1.00 97.05  ? 90  GLU A OE1 1 
ATOM 481  O OE2 . GLU A 1 90  ? 9.916  -21.845 12.574  1.00 93.85  ? 90  GLU A OE2 1 
ATOM 482  N N   . TYR A 1 91  ? 8.533  -16.891 12.324  1.00 65.24  ? 91  TYR A N   1 
ATOM 483  C CA  . TYR A 1 91  ? 9.606  -15.881 12.508  1.00 60.52  ? 91  TYR A CA  1 
ATOM 484  C C   . TYR A 1 91  ? 9.100  -14.761 13.411  1.00 63.40  ? 91  TYR A C   1 
ATOM 485  O O   . TYR A 1 91  ? 9.886  -14.229 14.204  1.00 59.14  ? 91  TYR A O   1 
ATOM 486  C CB  . TYR A 1 91  ? 10.038 -15.327 11.149  1.00 52.78  ? 91  TYR A CB  1 
ATOM 487  C CG  . TYR A 1 91  ? 11.303 -14.509 11.153  1.00 56.23  ? 91  TYR A CG  1 
ATOM 488  C CD1 . TYR A 1 91  ? 12.537 -15.103 10.960  1.00 53.46  ? 91  TYR A CD1 1 
ATOM 489  C CD2 . TYR A 1 91  ? 11.265 -13.138 11.332  1.00 57.80  ? 91  TYR A CD2 1 
ATOM 490  C CE1 . TYR A 1 91  ? 13.703 -14.357 10.958  1.00 58.37  ? 91  TYR A CE1 1 
ATOM 491  C CE2 . TYR A 1 91  ? 12.421 -12.377 11.334  1.00 48.37  ? 91  TYR A CE2 1 
ATOM 492  C CZ  . TYR A 1 91  ? 13.646 -12.989 11.145  1.00 53.58  ? 91  TYR A CZ  1 
ATOM 493  O OH  . TYR A 1 91  ? 14.790 -12.247 11.142  1.00 48.40  ? 91  TYR A OH  1 
ATOM 494  N N   . ALA A 1 92  ? 7.818  -14.426 13.303  1.00 63.63  ? 92  ALA A N   1 
ATOM 495  C CA  . ALA A 1 92  ? 7.261  -13.300 14.081  1.00 55.16  ? 92  ALA A CA  1 
ATOM 496  C C   . ALA A 1 92  ? 7.246  -13.626 15.572  1.00 56.62  ? 92  ALA A C   1 
ATOM 497  O O   . ALA A 1 92  ? 6.981  -12.715 16.364  1.00 57.03  ? 92  ALA A O   1 
ATOM 498  C CB  . ALA A 1 92  ? 5.881  -12.996 13.580  1.00 53.46  ? 92  ALA A CB  1 
ATOM 499  N N   . LYS A 1 93  ? 7.520  -14.878 15.930  1.00 56.48  ? 93  LYS A N   1 
ATOM 500  C CA  . LYS A 1 93  ? 7.510  -15.285 17.355  1.00 54.34  ? 93  LYS A CA  1 
ATOM 501  C C   . LYS A 1 93  ? 8.832  -14.877 17.991  1.00 53.80  ? 93  LYS A C   1 
ATOM 502  O O   . LYS A 1 93  ? 8.963  -15.012 19.209  1.00 53.61  ? 93  LYS A O   1 
ATOM 503  C CB  . LYS A 1 93  ? 7.297  -16.793 17.482  1.00 59.43  ? 93  LYS A CB  1 
ATOM 504  C CG  . LYS A 1 93  ? 6.049  -17.334 16.802  1.00 65.23  ? 93  LYS A CG  1 
ATOM 505  C CD  . LYS A 1 93  ? 6.121  -18.821 16.542  1.00 75.59  ? 93  LYS A CD  1 
ATOM 506  C CE  . LYS A 1 93  ? 4.771  -19.442 16.255  1.00 75.21  ? 93  LYS A CE  1 
ATOM 507  N NZ  . LYS A 1 93  ? 4.586  -20.711 16.996  1.00 77.61  ? 93  LYS A NZ  1 
ATOM 508  N N   . LEU A 1 94  ? 9.763  -14.387 17.181  1.00 58.48  ? 94  LEU A N   1 
ATOM 509  C CA  . LEU A 1 94  ? 11.092 -13.978 17.696  1.00 57.54  ? 94  LEU A CA  1 
ATOM 510  C C   . LEU A 1 94  ? 10.952 -12.661 18.454  1.00 52.53  ? 94  LEU A C   1 
ATOM 511  O O   . LEU A 1 94  ? 11.801 -12.380 19.301  1.00 57.66  ? 94  LEU A O   1 
ATOM 512  C CB  . LEU A 1 94  ? 12.053 -13.839 16.516  1.00 47.09  ? 94  LEU A CB  1 
ATOM 513  C CG  . LEU A 1 94  ? 12.639 -15.142 15.981  1.00 58.76  ? 94  LEU A CG  1 
ATOM 514  C CD1 . LEU A 1 94  ? 13.112 -14.969 14.547  1.00 50.78  ? 94  LEU A CD1 1 
ATOM 515  C CD2 . LEU A 1 94  ? 13.782 -15.617 16.861  1.00 52.11  ? 94  LEU A CD2 1 
ATOM 516  N N   . GLU A 1 95  ? 9.907  -11.896 18.157  1.00 49.64  ? 95  GLU A N   1 
ATOM 517  C CA  . GLU A 1 95  ? 9.679  -10.614 18.862  1.00 56.24  ? 95  GLU A CA  1 
ATOM 518  C C   . GLU A 1 95  ? 9.478  -10.922 20.337  1.00 58.19  ? 95  GLU A C   1 
ATOM 519  O O   . GLU A 1 95  ? 9.853  -10.096 21.171  1.00 58.60  ? 95  GLU A O   1 
ATOM 520  C CB  . GLU A 1 95  ? 8.460  -9.898  18.287  1.00 60.71  ? 95  GLU A CB  1 
ATOM 521  C CG  . GLU A 1 95  ? 8.096  -8.620  19.014  1.00 59.60  ? 95  GLU A CG  1 
ATOM 522  C CD  . GLU A 1 95  ? 7.062  -7.769  18.300  1.00 68.29  ? 95  GLU A CD  1 
ATOM 523  O OE1 . GLU A 1 95  ? 6.464  -8.263  17.330  1.00 71.84  ? 95  GLU A OE1 1 
ATOM 524  O OE2 . GLU A 1 95  ? 6.859  -6.615  18.715  1.00 69.94  ? 95  GLU A OE2 1 
ATOM 525  N N   . ASN A 1 96  ? 8.940  -12.098 20.632  1.00 60.32  ? 96  ASN A N   1 
ATOM 526  C CA  . ASN A 1 96  ? 8.640  -12.461 22.035  1.00 57.87  ? 96  ASN A CA  1 
ATOM 527  C C   . ASN A 1 96  ? 9.956  -12.631 22.782  1.00 65.39  ? 96  ASN A C   1 
ATOM 528  O O   . ASN A 1 96  ? 9.923  -12.700 24.019  1.00 71.10  ? 96  ASN A O   1 
ATOM 529  C CB  . ASN A 1 96  ? 7.768  -13.713 22.101  1.00 62.83  ? 96  ASN A CB  1 
ATOM 530  C CG  . ASN A 1 96  ? 6.625  -13.691 21.109  1.00 64.37  ? 96  ASN A CG  1 
ATOM 531  O OD1 . ASN A 1 96  ? 6.354  -14.687 20.446  1.00 76.77  ? 96  ASN A OD1 1 
ATOM 532  N ND2 . ASN A 1 96  ? 5.947  -12.561 21.001  1.00 55.93  ? 96  ASN A ND2 1 
ATOM 533  N N   . ASP A 1 97  ? 11.067 -12.671 22.049  1.00 68.89  ? 97  ASP A N   1 
ATOM 534  C CA  . ASP A 1 97  ? 12.399 -12.857 22.680  1.00 68.93  ? 97  ASP A CA  1 
ATOM 535  C C   . ASP A 1 97  ? 13.278 -11.635 22.402  1.00 62.37  ? 97  ASP A C   1 
ATOM 536  O O   . ASP A 1 97  ? 14.484 -11.715 22.673  1.00 58.50  ? 97  ASP A O   1 
ATOM 537  C CB  . ASP A 1 97  ? 13.048 -14.156 22.205  1.00 63.05  ? 97  ASP A CB  1 
ATOM 538  C CG  . ASP A 1 97  ? 12.248 -15.393 22.565  1.00 74.89  ? 97  ASP A CG  1 
ATOM 539  O OD1 . ASP A 1 97  ? 12.151 -15.692 23.768  1.00 77.86  ? 97  ASP A OD1 1 
ATOM 540  O OD2 . ASP A 1 97  ? 11.732 -16.046 21.639  1.00 76.32  ? 97  ASP A OD2 1 
ATOM 541  N N   . PHE A 1 98  ? 12.683 -10.545 21.917  1.00 54.98  ? 98  PHE A N   1 
ATOM 542  C CA  . PHE A 1 98  ? 13.460 -9.312  21.630  1.00 58.44  ? 98  PHE A CA  1 
ATOM 543  C C   . PHE A 1 98  ? 13.386 -8.340  22.811  1.00 57.39  ? 98  PHE A C   1 
ATOM 544  O O   . PHE A 1 98  ? 12.330 -7.730  23.016  1.00 55.90  ? 98  PHE A O   1 
ATOM 545  C CB  . PHE A 1 98  ? 12.997 -8.653  20.332  1.00 55.63  ? 98  PHE A CB  1 
ATOM 546  C CG  . PHE A 1 98  ? 13.998 -7.683  19.763  1.00 50.67  ? 98  PHE A CG  1 
ATOM 547  C CD1 . PHE A 1 98  ? 15.123 -8.138  19.097  1.00 54.84  ? 98  PHE A CD1 1 
ATOM 548  C CD2 . PHE A 1 98  ? 13.831 -6.319  19.918  1.00 57.48  ? 98  PHE A CD2 1 
ATOM 549  C CE1 . PHE A 1 98  ? 16.050 -7.248  18.582  1.00 46.80  ? 98  PHE A CE1 1 
ATOM 550  C CE2 . PHE A 1 98  ? 14.759 -5.430  19.403  1.00 60.82  ? 98  PHE A CE2 1 
ATOM 551  C CZ  . PHE A 1 98  ? 15.866 -5.896  18.736  1.00 58.68  ? 98  PHE A CZ  1 
ATOM 552  N N   . THR A 1 99  ? 14.498 -8.181  23.529  1.00 54.66  ? 99  THR A N   1 
ATOM 553  C CA  . THR A 1 99  ? 14.545 -7.289  24.713  1.00 56.52  ? 99  THR A CA  1 
ATOM 554  C C   . THR A 1 99  ? 15.628 -6.223  24.527  1.00 56.29  ? 99  THR A C   1 
ATOM 555  O O   . THR A 1 99  ? 15.499 -5.154  25.133  1.00 53.57  ? 99  THR A O   1 
ATOM 556  C CB  . THR A 1 99  ? 14.809 -8.122  25.968  1.00 55.63  ? 99  THR A CB  1 
ATOM 557  O OG1 . THR A 1 99  ? 16.213 -8.372  26.036  1.00 62.71  ? 99  THR A OG1 1 
ATOM 558  C CG2 . THR A 1 99  ? 14.058 -9.434  25.967  1.00 52.39  ? 99  THR A CG2 1 
ATOM 559  N N   . ALA A 1 100 ? 16.662 -6.519  23.739  1.00 64.90  ? 100 ALA A N   1 
ATOM 560  C CA  . ALA A 1 100 ? 17.765 -5.563  23.490  1.00 57.17  ? 100 ALA A CA  1 
ATOM 561  C C   . ALA A 1 100 ? 18.346 -5.099  24.820  1.00 59.77  ? 100 ALA A C   1 
ATOM 562  O O   . ALA A 1 100 ? 18.813 -3.959  24.888  1.00 62.93  ? 100 ALA A O   1 
ATOM 563  C CB  . ALA A 1 100 ? 17.263 -4.404  22.679  1.00 52.48  ? 100 ALA A CB  1 
ATOM 564  N N   . LYS A 1 101 ? 18.354 -5.973  25.819  1.00 62.25  ? 101 LYS A N   1 
ATOM 565  C CA  . LYS A 1 101 ? 18.823 -5.603  27.179  1.00 66.15  ? 101 LYS A CA  1 
ATOM 566  C C   . LYS A 1 101 ? 20.152 -4.854  27.153  1.00 63.15  ? 101 LYS A C   1 
ATOM 567  O O   . LYS A 1 101 ? 20.239 -3.818  27.825  1.00 67.06  ? 101 LYS A O   1 
ATOM 568  C CB  . LYS A 1 101 ? 18.999 -6.873  28.014  1.00 66.57  ? 101 LYS A CB  1 
ATOM 569  C CG  . LYS A 1 101 ? 19.917 -6.738  29.221  1.00 77.22  ? 101 LYS A CG  1 
ATOM 570  C CD  . LYS A 1 101 ? 19.859 -7.928  30.153  1.00 79.75  ? 101 LYS A CD  1 
ATOM 571  C CE  . LYS A 1 101 ? 19.658 -7.535  31.600  1.00 74.27  ? 101 LYS A CE  1 
ATOM 572  N NZ  . LYS A 1 101 ? 18.700 -6.414  31.735  1.00 64.13  ? 101 LYS A NZ  1 
ATOM 573  N N   . ASN A 1 102 ? 21.143 -5.340  26.405  1.00 62.21  ? 102 ASN A N   1 
ATOM 574  C CA  . ASN A 1 102 ? 22.496 -4.730  26.495  1.00 55.86  ? 102 ASN A CA  1 
ATOM 575  C C   . ASN A 1 102 ? 22.842 -3.897  25.261  1.00 54.65  ? 102 ASN A C   1 
ATOM 576  O O   . ASN A 1 102 ? 24.038 -3.726  25.000  1.00 55.97  ? 102 ASN A O   1 
ATOM 577  C CB  . ASN A 1 102 ? 23.531 -5.811  26.794  1.00 58.52  ? 102 ASN A CB  1 
ATOM 578  C CG  . ASN A 1 102 ? 23.449 -6.298  28.223  1.00 65.52  ? 102 ASN A CG  1 
ATOM 579  O OD1 . ASN A 1 102 ? 23.167 -7.466  28.472  1.00 65.95  ? 102 ASN A OD1 1 
ATOM 580  N ND2 . ASN A 1 102 ? 23.680 -5.403  29.167  1.00 63.97  ? 102 ASN A ND2 1 
ATOM 581  N N   . PHE A 1 103 ? 21.841 -3.368  24.563  1.00 54.59  ? 103 PHE A N   1 
ATOM 582  C CA  . PHE A 1 103 ? 22.121 -2.460  23.427  1.00 47.93  ? 103 PHE A CA  1 
ATOM 583  C C   . PHE A 1 103 ? 22.415 -1.074  23.989  1.00 51.65  ? 103 PHE A C   1 
ATOM 584  O O   . PHE A 1 103 ? 21.472 -0.410  24.436  1.00 52.58  ? 103 PHE A O   1 
ATOM 585  C CB  . PHE A 1 103 ? 20.938 -2.441  22.464  1.00 55.35  ? 103 PHE A CB  1 
ATOM 586  C CG  . PHE A 1 103 ? 21.094 -1.551  21.258  1.00 56.80  ? 103 PHE A CG  1 
ATOM 587  C CD1 . PHE A 1 103 ? 20.798 -0.201  21.327  1.00 51.23  ? 103 PHE A CD1 1 
ATOM 588  C CD2 . PHE A 1 103 ? 21.517 -2.070  20.046  1.00 56.65  ? 103 PHE A CD2 1 
ATOM 589  C CE1 . PHE A 1 103 ? 20.937 0.614   20.216  1.00 50.93  ? 103 PHE A CE1 1 
ATOM 590  C CE2 . PHE A 1 103 ? 21.655 -1.255  18.935  1.00 56.03  ? 103 PHE A CE2 1 
ATOM 591  C CZ  . PHE A 1 103 ? 21.364 0.085   19.022  1.00 57.93  ? 103 PHE A CZ  1 
ATOM 592  N N   . ASP A 1 104 ? 23.683 -0.664  23.971  1.00 50.51  ? 104 ASP A N   1 
ATOM 593  C CA  . ASP A 1 104 ? 24.079 0.642   24.552  1.00 44.83  ? 104 ASP A CA  1 
ATOM 594  C C   . ASP A 1 104 ? 24.542 1.579   23.443  1.00 49.95  ? 104 ASP A C   1 
ATOM 595  O O   . ASP A 1 104 ? 25.671 1.416   22.969  1.00 49.54  ? 104 ASP A O   1 
ATOM 596  C CB  . ASP A 1 104 ? 25.170 0.471   25.606  1.00 51.79  ? 104 ASP A CB  1 
ATOM 597  C CG  . ASP A 1 104 ? 25.427 1.710   26.435  1.00 54.55  ? 104 ASP A CG  1 
ATOM 598  O OD1 . ASP A 1 104 ? 24.853 2.765   26.114  1.00 59.88  ? 104 ASP A OD1 1 
ATOM 599  O OD2 . ASP A 1 104 ? 26.197 1.599   27.394  1.00 56.10  ? 104 ASP A OD2 1 
ATOM 600  N N   . ALA A 1 105 ? 23.704 2.547   23.089  1.00 49.32  ? 105 ALA A N   1 
ATOM 601  C CA  . ALA A 1 105 ? 24.055 3.515   22.034  1.00 49.66  ? 105 ALA A CA  1 
ATOM 602  C C   . ALA A 1 105 ? 25.225 4.382   22.493  1.00 50.44  ? 105 ALA A C   1 
ATOM 603  O O   . ALA A 1 105 ? 25.980 4.835   21.635  1.00 53.31  ? 105 ALA A O   1 
ATOM 604  C CB  . ALA A 1 105 ? 22.850 4.344   21.704  1.00 46.38  ? 105 ALA A CB  1 
ATOM 605  N N   . ASP A 1 106 ? 25.378 4.572   23.799  1.00 56.39  ? 106 ASP A N   1 
ATOM 606  C CA  . ASP A 1 106 ? 26.517 5.365   24.326  1.00 60.40  ? 106 ASP A CA  1 
ATOM 607  C C   . ASP A 1 106 ? 27.821 4.633   24.015  1.00 60.96  ? 106 ASP A C   1 
ATOM 608  O O   . ASP A 1 106 ? 28.728 5.264   23.462  1.00 59.65  ? 106 ASP A O   1 
ATOM 609  C CB  . ASP A 1 106 ? 26.358 5.656   25.818  1.00 63.36  ? 106 ASP A CB  1 
ATOM 610  C CG  . ASP A 1 106 ? 27.247 6.778   26.318  1.00 66.35  ? 106 ASP A CG  1 
ATOM 611  O OD1 . ASP A 1 106 ? 27.988 7.346   25.499  1.00 64.93  ? 106 ASP A OD1 1 
ATOM 612  O OD2 . ASP A 1 106 ? 27.187 7.071   27.523  1.00 73.02  ? 106 ASP A OD2 1 
ATOM 613  N N   . PHE A 1 107 ? 27.894 3.347   24.349  1.00 57.33  ? 107 PHE A N   1 
ATOM 614  C CA  . PHE A 1 107 ? 29.127 2.563   24.104  1.00 59.11  ? 107 PHE A CA  1 
ATOM 615  C C   . PHE A 1 107 ? 29.385 2.495   22.608  1.00 59.63  ? 107 PHE A C   1 
ATOM 616  O O   . PHE A 1 107 ? 30.535 2.660   22.187  1.00 55.14  ? 107 PHE A O   1 
ATOM 617  C CB  . PHE A 1 107 ? 28.983 1.138   24.630  1.00 56.36  ? 107 PHE A CB  1 
ATOM 618  C CG  . PHE A 1 107 ? 30.031 0.185   24.120  1.00 54.89  ? 107 PHE A CG  1 
ATOM 619  C CD1 . PHE A 1 107 ? 31.332 0.250   24.587  1.00 53.93  ? 107 PHE A CD1 1 
ATOM 620  C CD2 . PHE A 1 107 ? 29.720 -0.769  23.167  1.00 55.89  ? 107 PHE A CD2 1 
ATOM 621  C CE1 . PHE A 1 107 ? 32.298 -0.624  24.118  1.00 60.09  ? 107 PHE A CE1 1 
ATOM 622  C CE2 . PHE A 1 107 ? 30.687 -1.641  22.698  1.00 51.90  ? 107 PHE A CE2 1 
ATOM 623  C CZ  . PHE A 1 107 ? 31.973 -1.566  23.173  1.00 47.36  ? 107 PHE A CZ  1 
ATOM 624  N N   . ILE A 1 108 ? 28.332 2.244   21.838  1.00 58.88  ? 108 ILE A N   1 
ATOM 625  C CA  . ILE A 1 108 ? 28.491 2.087   20.368  1.00 57.32  ? 108 ILE A CA  1 
ATOM 626  C C   . ILE A 1 108 ? 29.027 3.396   19.804  1.00 52.78  ? 108 ILE A C   1 
ATOM 627  O O   . ILE A 1 108 ? 30.013 3.354   19.055  1.00 53.67  ? 108 ILE A O   1 
ATOM 628  C CB  . ILE A 1 108 ? 27.151 1.683   19.734  1.00 51.80  ? 108 ILE A CB  1 
ATOM 629  C CG1 . ILE A 1 108 ? 26.779 0.239   20.075  1.00 52.13  ? 108 ILE A CG1 1 
ATOM 630  C CG2 . ILE A 1 108 ? 27.170 1.921   18.234  1.00 50.55  ? 108 ILE A CG2 1 
ATOM 631  C CD1 . ILE A 1 108 ? 25.302 -0.052  19.966  1.00 52.64  ? 108 ILE A CD1 1 
ATOM 632  N N   . THR A 1 109 ? 28.411 4.513   20.177  1.00 51.00  ? 109 THR A N   1 
ATOM 633  C CA  . THR A 1 109 ? 28.822 5.824   19.621  1.00 54.98  ? 109 THR A CA  1 
ATOM 634  C C   . THR A 1 109 ? 30.258 6.101   20.063  1.00 54.22  ? 109 THR A C   1 
ATOM 635  O O   . THR A 1 109 ? 31.039 6.621   19.251  1.00 51.08  ? 109 THR A O   1 
ATOM 636  C CB  . THR A 1 109 ? 27.811 6.906   20.012  1.00 45.87  ? 109 THR A CB  1 
ATOM 637  O OG1 . THR A 1 109 ? 27.516 6.747   21.398  1.00 55.90  ? 109 THR A OG1 1 
ATOM 638  C CG2 . THR A 1 109 ? 26.540 6.835   19.196  1.00 46.55  ? 109 THR A CG2 1 
ATOM 639  N N   . ASP A 1 110 ? 30.588 5.723   21.292  1.00 54.36  ? 110 ASP A N   1 
ATOM 640  C CA  . ASP A 1 110 ? 31.954 5.940   21.825  1.00 54.81  ? 110 ASP A CA  1 
ATOM 641  C C   . ASP A 1 110 ? 32.929 5.041   21.069  1.00 54.48  ? 110 ASP A C   1 
ATOM 642  O O   . ASP A 1 110 ? 33.937 5.553   20.581  1.00 56.76  ? 110 ASP A O   1 
ATOM 643  C CB  . ASP A 1 110 ? 31.980 5.678   23.330  1.00 61.45  ? 110 ASP A CB  1 
ATOM 644  C CG  . ASP A 1 110 ? 31.617 6.881   24.178  1.00 65.47  ? 110 ASP A CG  1 
ATOM 645  O OD1 . ASP A 1 110 ? 31.615 8.000   23.636  1.00 65.18  ? 110 ASP A OD1 1 
ATOM 646  O OD2 . ASP A 1 110 ? 31.348 6.685   25.376  1.00 67.86  ? 110 ASP A OD2 1 
ATOM 647  N N   . MET A 1 111 ? 32.625 3.749   20.981  1.00 57.53  ? 111 MET A N   1 
ATOM 648  C CA  . MET A 1 111 ? 33.494 2.788   20.262  1.00 57.23  ? 111 MET A CA  1 
ATOM 649  C C   . MET A 1 111 ? 33.847 3.366   18.897  1.00 56.29  ? 111 MET A C   1 
ATOM 650  O O   . MET A 1 111 ? 35.039 3.453   18.581  1.00 60.96  ? 111 MET A O   1 
ATOM 651  C CB  . MET A 1 111 ? 32.761 1.459   20.067  1.00 51.97  ? 111 MET A CB  1 
ATOM 652  C CG  . MET A 1 111 ? 33.579 0.398   19.367  1.00 46.65  ? 111 MET A CG  1 
ATOM 653  S SD  . MET A 1 111 ? 32.667 -1.156  19.242  1.00 61.02  ? 111 MET A SD  1 
ATOM 654  C CE  . MET A 1 111 ? 31.067 -0.555  18.708  1.00 46.82  ? 111 MET A CE  1 
ATOM 655  N N   . ALA A 1 112 ? 32.835 3.730   18.119  1.00 47.19  ? 112 ALA A N   1 
ATOM 656  C CA  . ALA A 1 112 ? 33.079 4.275   16.772  1.00 52.34  ? 112 ALA A CA  1 
ATOM 657  C C   . ALA A 1 112 ? 34.085 5.407   16.875  1.00 57.53  ? 112 ALA A C   1 
ATOM 658  O O   . ALA A 1 112 ? 35.139 5.327   16.239  1.00 58.34  ? 112 ALA A O   1 
ATOM 659  C CB  . ALA A 1 112 ? 31.787 4.785   16.210  1.00 48.40  ? 112 ALA A CB  1 
ATOM 660  N N   . LEU A 1 113 ? 33.737 6.434   17.639  1.00 59.50  ? 113 LEU A N   1 
ATOM 661  C CA  . LEU A 1 113 ? 34.616 7.618   17.755  1.00 57.29  ? 113 LEU A CA  1 
ATOM 662  C C   . LEU A 1 113 ? 36.051 7.158   18.011  1.00 56.53  ? 113 LEU A C   1 
ATOM 663  O O   . LEU A 1 113 ? 36.923 7.492   17.201  1.00 61.50  ? 113 LEU A O   1 
ATOM 664  C CB  . LEU A 1 113 ? 34.082 8.493   18.890  1.00 51.92  ? 113 LEU A CB  1 
ATOM 665  C CG  . LEU A 1 113 ? 32.941 9.433   18.513  1.00 49.49  ? 113 LEU A CG  1 
ATOM 666  C CD1 . LEU A 1 113 ? 32.444 10.192  19.731  1.00 40.60  ? 113 LEU A CD1 1 
ATOM 667  C CD2 . LEU A 1 113 ? 33.382 10.400  17.430  1.00 43.56  ? 113 LEU A CD2 1 
ATOM 668  N N   . GLU A 1 114 ? 36.274 6.410   19.085  1.00 48.94  ? 114 GLU A N   1 
ATOM 669  C CA  . GLU A 1 114 ? 37.646 5.980   19.441  1.00 52.18  ? 114 GLU A CA  1 
ATOM 670  C C   . GLU A 1 114 ? 38.287 5.253   18.261  1.00 61.84  ? 114 GLU A C   1 
ATOM 671  O O   . GLU A 1 114 ? 39.491 5.431   18.046  1.00 67.17  ? 114 GLU A O   1 
ATOM 672  C CB  . GLU A 1 114 ? 37.612 5.068   20.664  1.00 65.41  ? 114 GLU A CB  1 
ATOM 673  C CG  . GLU A 1 114 ? 36.760 5.590   21.803  1.00 63.31  ? 114 GLU A CG  1 
ATOM 674  C CD  . GLU A 1 114 ? 36.305 4.509   22.769  1.00 80.64  ? 114 GLU A CD  1 
ATOM 675  O OE1 . GLU A 1 114 ? 36.944 3.440   22.799  1.00 85.54  ? 114 GLU A OE1 1 
ATOM 676  O OE2 . GLU A 1 114 ? 35.315 4.736   23.487  1.00 79.56  ? 114 GLU A OE2 1 
ATOM 677  N N   . ALA A 1 115 ? 37.506 4.471   17.527  1.00 59.79  ? 115 ALA A N   1 
ATOM 678  C CA  . ALA A 1 115 ? 38.049 3.681   16.403  1.00 59.47  ? 115 ALA A CA  1 
ATOM 679  C C   . ALA A 1 115 ? 38.507 4.588   15.260  1.00 62.93  ? 115 ALA A C   1 
ATOM 680  O O   . ALA A 1 115 ? 39.295 4.120   14.429  1.00 65.71  ? 115 ALA A O   1 
ATOM 681  C CB  . ALA A 1 115 ? 36.998 2.724   15.929  1.00 56.68  ? 115 ALA A CB  1 
ATOM 682  N N   . GLY A 1 116 ? 38.003 5.820   15.205  1.00 61.20  ? 116 GLY A N   1 
ATOM 683  C CA  . GLY A 1 116 ? 38.390 6.762   14.139  1.00 53.61  ? 116 GLY A CA  1 
ATOM 684  C C   . GLY A 1 116 ? 37.300 6.911   13.108  1.00 49.47  ? 116 GLY A C   1 
ATOM 685  O O   . GLY A 1 116 ? 37.575 7.445   12.028  1.00 47.19  ? 116 GLY A O   1 
ATOM 686  N N   . MET A 1 117 ? 36.100 6.454   13.443  1.00 54.75  ? 117 MET A N   1 
ATOM 687  C CA  . MET A 1 117 ? 34.958 6.541   12.506  1.00 53.65  ? 117 MET A CA  1 
ATOM 688  C C   . MET A 1 117 ? 34.252 7.873   12.742  1.00 47.67  ? 117 MET A C   1 
ATOM 689  O O   . MET A 1 117 ? 34.348 8.394   13.857  1.00 53.40  ? 117 MET A O   1 
ATOM 690  C CB  . MET A 1 117 ? 33.998 5.368   12.715  1.00 50.34  ? 117 MET A CB  1 
ATOM 691  C CG  . MET A 1 117 ? 34.614 4.017   12.431  1.00 51.49  ? 117 MET A CG  1 
ATOM 692  S SD  . MET A 1 117 ? 33.754 2.663   13.265  1.00 51.11  ? 117 MET A SD  1 
ATOM 693  C CE  . MET A 1 117 ? 33.957 1.352   12.063  1.00 44.49  ? 117 MET A CE  1 
ATOM 694  N N   . LYS A 1 118 ? 33.591 8.408   11.721  1.00 49.50  ? 118 LYS A N   1 
ATOM 695  C CA  . LYS A 1 118 ? 32.990 9.756   11.849  1.00 49.15  ? 118 LYS A CA  1 
ATOM 696  C C   . LYS A 1 118 ? 31.479 9.679   11.665  1.00 49.04  ? 118 LYS A C   1 
ATOM 697  O O   . LYS A 1 118 ? 30.829 10.716  11.819  1.00 53.28  ? 118 LYS A O   1 
ATOM 698  C CB  . LYS A 1 118 ? 33.593 10.691  10.802  1.00 44.08  ? 118 LYS A CB  1 
ATOM 699  C CG  . LYS A 1 118 ? 35.090 10.544  10.577  1.00 46.34  ? 118 LYS A CG  1 
ATOM 700  C CD  . LYS A 1 118 ? 35.881 11.708  11.123  1.00 53.35  ? 118 LYS A CD  1 
ATOM 701  C CE  . LYS A 1 118 ? 37.322 11.712  10.662  1.00 63.09  ? 118 LYS A CE  1 
ATOM 702  N NZ  . LYS A 1 118 ? 37.498 12.491  9.414   1.00 69.04  ? 118 LYS A NZ  1 
ATOM 703  N N   . TYR A 1 119 ? 30.945 8.499   11.355  1.00 46.14  ? 119 TYR A N   1 
ATOM 704  C CA  . TYR A 1 119 ? 29.496 8.406   11.241  1.00 39.69  ? 119 TYR A CA  1 
ATOM 705  C C   . TYR A 1 119 ? 29.059 6.966   11.478  1.00 43.41  ? 119 TYR A C   1 
ATOM 706  O O   . TYR A 1 119 ? 29.876 6.043   11.524  1.00 43.76  ? 119 TYR A O   1 
ATOM 707  C CB  . TYR A 1 119 ? 29.008 8.920   9.882   1.00 44.88  ? 119 TYR A CB  1 
ATOM 708  C CG  . TYR A 1 119 ? 29.455 8.101   8.695   1.00 46.91  ? 119 TYR A CG  1 
ATOM 709  C CD1 . TYR A 1 119 ? 30.690 8.324   8.098   1.00 45.91  ? 119 TYR A CD1 1 
ATOM 710  C CD2 . TYR A 1 119 ? 28.637 7.115   8.160   1.00 48.66  ? 119 TYR A CD2 1 
ATOM 711  C CE1 . TYR A 1 119 ? 31.100 7.581   7.007   1.00 45.27  ? 119 TYR A CE1 1 
ATOM 712  C CE2 . TYR A 1 119 ? 29.038 6.367   7.071   1.00 52.37  ? 119 TYR A CE2 1 
ATOM 713  C CZ  . TYR A 1 119 ? 30.270 6.605   6.498   1.00 50.59  ? 119 TYR A CZ  1 
ATOM 714  O OH  . TYR A 1 119 ? 30.670 5.862   5.412   1.00 53.38  ? 119 TYR A OH  1 
ATOM 715  N N   . VAL A 1 120 ? 27.746 6.792   11.626  1.00 42.70  ? 120 VAL A N   1 
ATOM 716  C CA  . VAL A 1 120 ? 27.144 5.527   12.028  1.00 37.85  ? 120 VAL A CA  1 
ATOM 717  C C   . VAL A 1 120 ? 25.948 5.242   11.128  1.00 38.01  ? 120 VAL A C   1 
ATOM 718  O O   . VAL A 1 120 ? 25.219 6.161   10.738  1.00 38.95  ? 120 VAL A O   1 
ATOM 719  C CB  . VAL A 1 120 ? 26.727 5.559   13.517  1.00 36.48  ? 120 VAL A CB  1 
ATOM 720  C CG1 . VAL A 1 120 ? 25.768 4.422   13.855  1.00 34.03  ? 120 VAL A CG1 1 
ATOM 721  C CG2 . VAL A 1 120 ? 27.957 5.506   14.411  1.00 34.70  ? 120 VAL A CG2 1 
ATOM 722  N N   . ASN A 1 121 ? 25.754 3.968   10.792  1.00 43.29  ? 121 ASN A N   1 
ATOM 723  C CA  . ASN A 1 121 ? 24.662 3.519   9.938   1.00 41.01  ? 121 ASN A CA  1 
ATOM 724  C C   . ASN A 1 121 ? 24.027 2.294   10.581  1.00 42.04  ? 121 ASN A C   1 
ATOM 725  O O   . ASN A 1 121 ? 24.731 1.330   10.899  1.00 41.64  ? 121 ASN A O   1 
ATOM 726  C CB  . ASN A 1 121 ? 25.173 3.188   8.529   1.00 38.07  ? 121 ASN A CB  1 
ATOM 727  C CG  . ASN A 1 121 ? 24.055 3.025   7.516   1.00 42.93  ? 121 ASN A CG  1 
ATOM 728  O OD1 . ASN A 1 121 ? 22.985 2.501   7.825   1.00 43.02  ? 121 ASN A OD1 1 
ATOM 729  N ND2 . ASN A 1 121 ? 24.307 3.468   6.289   1.00 41.61  ? 121 ASN A ND2 1 
ATOM 730  N N   . ILE A 1 122 ? 22.708 2.326   10.775  1.00 41.51  ? 122 ILE A N   1 
ATOM 731  C CA  . ILE A 1 122 ? 21.992 1.210   11.387  1.00 44.49  ? 122 ILE A CA  1 
ATOM 732  C C   . ILE A 1 122 ? 20.845 0.766   10.489  1.00 44.07  ? 122 ILE A C   1 
ATOM 733  O O   . ILE A 1 122 ? 20.173 1.588   9.854   1.00 44.50  ? 122 ILE A O   1 
ATOM 734  C CB  . ILE A 1 122 ? 21.460 1.541   12.800  1.00 50.61  ? 122 ILE A CB  1 
ATOM 735  C CG1 . ILE A 1 122 ? 20.771 0.300   13.383  1.00 41.12  ? 122 ILE A CG1 1 
ATOM 736  C CG2 . ILE A 1 122 ? 20.502 2.728   12.762  1.00 37.63  ? 122 ILE A CG2 1 
ATOM 737  C CD1 . ILE A 1 122 ? 20.869 0.142   14.867  1.00 38.03  ? 122 ILE A CD1 1 
ATOM 738  N N   . THR A 1 123 ? 20.643 -0.546  10.430  1.00 40.69  ? 123 THR A N   1 
ATOM 739  C CA  . THR A 1 123 ? 19.480 -1.156  9.798   1.00 42.73  ? 123 THR A CA  1 
ATOM 740  C C   . THR A 1 123 ? 18.235 -0.820  10.609  1.00 45.48  ? 123 THR A C   1 
ATOM 741  O O   . THR A 1 123 ? 17.976 -1.429  11.649  1.00 42.62  ? 123 THR A O   1 
ATOM 742  C CB  . THR A 1 123 ? 19.677 -2.664  9.704   1.00 43.01  ? 123 THR A CB  1 
ATOM 743  O OG1 . THR A 1 123 ? 20.158 -3.156  10.961  1.00 36.58  ? 123 THR A OG1 1 
ATOM 744  C CG2 . THR A 1 123 ? 20.696 -2.995  8.627   1.00 40.27  ? 123 THR A CG2 1 
ATOM 745  N N   . THR A 1 124 ? 17.459 0.164   10.146  1.00 44.39  ? 124 THR A N   1 
ATOM 746  C CA  . THR A 1 124 ? 16.180 0.436   10.794  1.00 42.09  ? 124 THR A CA  1 
ATOM 747  C C   . THR A 1 124 ? 15.179 -0.677  10.518  1.00 39.60  ? 124 THR A C   1 
ATOM 748  O O   . THR A 1 124 ? 14.326 -0.965  11.365  1.00 48.10  ? 124 THR A O   1 
ATOM 749  C CB  . THR A 1 124 ? 15.610 1.782   10.339  1.00 49.76  ? 124 THR A CB  1 
ATOM 750  O OG1 . THR A 1 124 ? 15.158 1.683   8.982   1.00 53.21  ? 124 THR A OG1 1 
ATOM 751  C CG2 . THR A 1 124 ? 16.663 2.877   10.444  1.00 44.23  ? 124 THR A CG2 1 
ATOM 752  N N   . ARG A 1 125 ? 15.274 -1.314  9.352   1.00 43.90  ? 125 ARG A N   1 
ATOM 753  C CA  . ARG A 1 125 ? 14.367 -2.399  8.984   1.00 43.72  ? 125 ARG A CA  1 
ATOM 754  C C   . ARG A 1 125 ? 14.979 -3.162  7.821   1.00 40.77  ? 125 ARG A C   1 
ATOM 755  O O   . ARG A 1 125 ? 15.172 -2.593  6.742   1.00 43.75  ? 125 ARG A O   1 
ATOM 756  C CB  . ARG A 1 125 ? 12.989 -1.856  8.612   1.00 43.10  ? 125 ARG A CB  1 
ATOM 757  C CG  . ARG A 1 125 ? 12.097 -2.868  7.927   1.00 47.41  ? 125 ARG A CG  1 
ATOM 758  C CD  . ARG A 1 125 ? 10.797 -2.234  7.466   1.00 54.33  ? 125 ARG A CD  1 
ATOM 759  N NE  . ARG A 1 125 ? 10.345 -2.786  6.195   1.00 55.00  ? 125 ARG A NE  1 
ATOM 760  C CZ  . ARG A 1 125 ? 10.874 -2.484  5.018   1.00 57.73  ? 125 ARG A CZ  1 
ATOM 761  N NH1 . ARG A 1 125 ? 11.888 -1.641  4.911   1.00 56.91  ? 125 ARG A NH1 1 
ATOM 762  N NH2 . ARG A 1 125 ? 10.376 -3.045  3.919   1.00 60.62  ? 125 ARG A NH2 1 
ATOM 763  N N   . HIS A 1 126 ? 15.272 -4.443  8.034   1.00 45.66  ? 126 HIS A N   1 
ATOM 764  C CA  . HIS A 1 126 ? 15.915 -5.282  7.036   1.00 41.37  ? 126 HIS A CA  1 
ATOM 765  C C   . HIS A 1 126 ? 14.854 -6.027  6.223   1.00 46.74  ? 126 HIS A C   1 
ATOM 766  O O   . HIS A 1 126 ? 13.668 -5.687  6.243   1.00 46.23  ? 126 HIS A O   1 
ATOM 767  C CB  . HIS A 1 126 ? 16.898 -6.236  7.716   1.00 44.13  ? 126 HIS A CB  1 
ATOM 768  C CG  . HIS A 1 126 ? 18.064 -6.629  6.860   1.00 51.55  ? 126 HIS A CG  1 
ATOM 769  N ND1 . HIS A 1 126 ? 18.009 -7.667  5.954   1.00 52.00  ? 126 HIS A ND1 1 
ATOM 770  C CD2 . HIS A 1 126 ? 19.321 -6.130  6.782   1.00 50.91  ? 126 HIS A CD2 1 
ATOM 771  C CE1 . HIS A 1 126 ? 19.179 -7.786  5.351   1.00 43.70  ? 126 HIS A CE1 1 
ATOM 772  N NE2 . HIS A 1 126 ? 19.993 -6.866  5.836   1.00 50.01  ? 126 HIS A NE2 1 
ATOM 773  N N   . HIS A 1 127 ? 15.284 -7.055  5.487   1.00 48.12  ? 127 HIS A N   1 
ATOM 774  C CA  . HIS A 1 127 ? 14.369 -7.826  4.650   1.00 54.50  ? 127 HIS A CA  1 
ATOM 775  C C   . HIS A 1 127 ? 13.266 -8.501  5.460   1.00 59.38  ? 127 HIS A C   1 
ATOM 776  O O   . HIS A 1 127 ? 12.175 -8.740  4.930   1.00 58.87  ? 127 HIS A O   1 
ATOM 777  C CB  . HIS A 1 127 ? 15.150 -8.865  3.844   1.00 53.86  ? 127 HIS A CB  1 
ATOM 778  C CG  . HIS A 1 127 ? 16.252 -8.283  3.013   1.00 51.94  ? 127 HIS A CG  1 
ATOM 779  N ND1 . HIS A 1 127 ? 16.141 -7.066  2.377   1.00 49.44  ? 127 HIS A ND1 1 
ATOM 780  C CD2 . HIS A 1 127 ? 17.485 -8.755  2.710   1.00 52.85  ? 127 HIS A CD2 1 
ATOM 781  C CE1 . HIS A 1 127 ? 17.260 -6.811  1.721   1.00 56.06  ? 127 HIS A CE1 1 
ATOM 782  N NE2 . HIS A 1 127 ? 18.092 -7.820  1.907   1.00 55.23  ? 127 HIS A NE2 1 
ATOM 783  N N   . ASP A 1 128 ? 13.519 -8.825  6.732   1.00 54.22  ? 128 ASP A N   1 
ATOM 784  C CA  . ASP A 1 128 ? 12.478 -9.461  7.534   1.00 53.33  ? 128 ASP A CA  1 
ATOM 785  C C   . ASP A 1 128 ? 11.368 -8.496  7.936   1.00 57.55  ? 128 ASP A C   1 
ATOM 786  O O   . ASP A 1 128 ? 10.354 -8.943  8.485   1.00 55.26  ? 128 ASP A O   1 
ATOM 787  C CB  . ASP A 1 128 ? 13.084 -10.134 8.777   1.00 51.74  ? 128 ASP A CB  1 
ATOM 788  C CG  . ASP A 1 128 ? 13.658 -9.143  9.791   1.00 59.09  ? 128 ASP A CG  1 
ATOM 789  O OD1 . ASP A 1 128 ? 13.475 -7.915  9.650   1.00 64.30  ? 128 ASP A OD1 1 
ATOM 790  O OD2 . ASP A 1 128 ? 14.300 -9.611  10.757  1.00 49.27  ? 128 ASP A OD2 1 
ATOM 791  N N   . SER A 1 129 ? 11.550 -7.196  7.694   1.00 59.02  ? 129 SER A N   1 
ATOM 792  C CA  . SER A 1 129 ? 10.576 -6.116  7.882   1.00 55.54  ? 129 SER A CA  1 
ATOM 793  C C   . SER A 1 129 ? 10.371 -5.737  9.345   1.00 55.62  ? 129 SER A C   1 
ATOM 794  O O   . SER A 1 129 ? 9.471  -4.937  9.639   1.00 63.42  ? 129 SER A O   1 
ATOM 795  C CB  . SER A 1 129 ? 9.216  -6.443  7.257   1.00 54.65  ? 129 SER A CB  1 
ATOM 796  O OG  . SER A 1 129 ? 8.246  -5.474  7.611   1.00 68.09  ? 129 SER A OG  1 
ATOM 797  N N   . PHE A 1 130 ? 11.163 -6.274  10.270  1.00 54.25  ? 130 PHE A N   1 
ATOM 798  C CA  . PHE A 1 130 ? 11.103 -5.851  11.663  1.00 50.70  ? 130 PHE A CA  1 
ATOM 799  C C   . PHE A 1 130 ? 11.804 -4.507  11.830  1.00 49.00  ? 130 PHE A C   1 
ATOM 800  O O   . PHE A 1 130 ? 12.915 -4.312  11.327  1.00 51.35  ? 130 PHE A O   1 
ATOM 801  C CB  . PHE A 1 130 ? 11.743 -6.905  12.567  1.00 51.40  ? 130 PHE A CB  1 
ATOM 802  C CG  . PHE A 1 130 ? 11.624 -6.603  14.033  1.00 52.25  ? 130 PHE A CG  1 
ATOM 803  C CD1 . PHE A 1 130 ? 10.421 -6.784  14.697  1.00 53.99  ? 130 PHE A CD1 1 
ATOM 804  C CD2 . PHE A 1 130 ? 12.717 -6.145  14.750  1.00 52.55  ? 130 PHE A CD2 1 
ATOM 805  C CE1 . PHE A 1 130 ? 10.309 -6.509  16.047  1.00 53.97  ? 130 PHE A CE1 1 
ATOM 806  C CE2 . PHE A 1 130 ? 12.612 -5.868  16.100  1.00 55.56  ? 130 PHE A CE2 1 
ATOM 807  C CZ  . PHE A 1 130 ? 11.406 -6.051  16.750  1.00 57.25  ? 130 PHE A CZ  1 
ATOM 808  N N   . CYS A 1 131 ? 11.160 -3.584  12.538  1.00 49.53  ? 131 CYS A N   1 
ATOM 809  C CA  . CYS A 1 131 ? 11.650 -2.219  12.679  1.00 54.83  ? 131 CYS A CA  1 
ATOM 810  C C   . CYS A 1 131 ? 12.203 -1.988  14.078  1.00 52.72  ? 131 CYS A C   1 
ATOM 811  O O   . CYS A 1 131 ? 11.616 -2.432  15.070  1.00 50.27  ? 131 CYS A O   1 
ATOM 812  C CB  . CYS A 1 131 ? 10.543 -1.200  12.395  1.00 50.58  ? 131 CYS A CB  1 
ATOM 813  S SG  . CYS A 1 131 ? 9.764  -1.362  10.775  1.00 54.92  ? 131 CYS A SG  1 
ATOM 814  N N   . LEU A 1 132 ? 13.329 -1.278  14.150  1.00 44.36  ? 132 LEU A N   1 
ATOM 815  C CA  . LEU A 1 132 ? 13.905 -0.850  15.417  1.00 46.94  ? 132 LEU A CA  1 
ATOM 816  C C   . LEU A 1 132 ? 13.412 0.531   15.833  1.00 49.74  ? 132 LEU A C   1 
ATOM 817  O O   . LEU A 1 132 ? 14.023 1.166   16.700  1.00 44.96  ? 132 LEU A O   1 
ATOM 818  C CB  . LEU A 1 132 ? 15.435 -0.860  15.346  1.00 48.13  ? 132 LEU A CB  1 
ATOM 819  C CG  . LEU A 1 132 ? 16.191 -2.061  14.768  1.00 47.35  ? 132 LEU A CG  1 
ATOM 820  C CD1 . LEU A 1 132 ? 17.630 -2.048  15.264  1.00 44.38  ? 132 LEU A CD1 1 
ATOM 821  C CD2 . LEU A 1 132 ? 15.524 -3.382  15.117  1.00 42.45  ? 132 LEU A CD2 1 
ATOM 822  N N   . PHE A 1 133 ? 12.326 1.007   15.230  1.00 53.26  ? 133 PHE A N   1 
ATOM 823  C CA  . PHE A 1 133 ? 11.779 2.319   15.531  1.00 53.61  ? 133 PHE A CA  1 
ATOM 824  C C   . PHE A 1 133 ? 10.262 2.228   15.601  1.00 59.81  ? 133 PHE A C   1 
ATOM 825  O O   . PHE A 1 133 ? 9.645  1.312   15.051  1.00 61.69  ? 133 PHE A O   1 
ATOM 826  C CB  . PHE A 1 133 ? 12.206 3.361   14.487  1.00 51.72  ? 133 PHE A CB  1 
ATOM 827  C CG  . PHE A 1 133 ? 11.646 3.115   13.113  1.00 44.51  ? 133 PHE A CG  1 
ATOM 828  C CD1 . PHE A 1 133 ? 12.173 2.124   12.301  1.00 49.99  ? 133 PHE A CD1 1 
ATOM 829  C CD2 . PHE A 1 133 ? 10.595 3.878   12.634  1.00 47.01  ? 133 PHE A CD2 1 
ATOM 830  C CE1 . PHE A 1 133 ? 11.659 1.899   11.035  1.00 51.97  ? 133 PHE A CE1 1 
ATOM 831  C CE2 . PHE A 1 133 ? 10.078 3.657   11.371  1.00 51.55  ? 133 PHE A CE2 1 
ATOM 832  C CZ  . PHE A 1 133 ? 10.610 2.667   10.571  1.00 52.55  ? 133 PHE A CZ  1 
ATOM 833  N N   . GLU A 1 134 ? 9.666  3.201   16.286  1.00 59.86  ? 134 GLU A N   1 
ATOM 834  C CA  . GLU A 1 134 ? 8.217  3.258   16.415  1.00 52.98  ? 134 GLU A CA  1 
ATOM 835  C C   . GLU A 1 134 ? 7.583  3.690   15.099  1.00 55.87  ? 134 GLU A C   1 
ATOM 836  O O   . GLU A 1 134 ? 8.000  4.681   14.493  1.00 65.37  ? 134 GLU A O   1 
ATOM 837  C CB  . GLU A 1 134 ? 7.832  4.222   17.535  1.00 56.77  ? 134 GLU A CB  1 
ATOM 838  C CG  . GLU A 1 134 ? 6.340  4.397   17.732  1.00 66.31  ? 134 GLU A CG  1 
ATOM 839  C CD  . GLU A 1 134 ? 6.020  5.545   18.665  1.00 77.81  ? 134 GLU A CD  1 
ATOM 840  O OE1 . GLU A 1 134 ? 6.050  5.337   19.897  1.00 80.46  ? 134 GLU A OE1 1 
ATOM 841  O OE2 . GLU A 1 134 ? 5.745  6.658   18.167  1.00 79.38  ? 134 GLU A OE2 1 
ATOM 842  N N   . SER A 1 135 ? 6.574  2.944   14.657  1.00 57.47  ? 135 SER A N   1 
ATOM 843  C CA  . SER A 1 135 ? 5.906  3.222   13.395  1.00 60.47  ? 135 SER A CA  1 
ATOM 844  C C   . SER A 1 135 ? 4.401  3.127   13.583  1.00 70.86  ? 135 SER A C   1 
ATOM 845  O O   . SER A 1 135 ? 3.905  2.195   14.223  1.00 70.77  ? 135 SER A O   1 
ATOM 846  C CB  . SER A 1 135 ? 6.359  2.253   12.296  1.00 58.31  ? 135 SER A CB  1 
ATOM 847  O OG  . SER A 1 135 ? 6.320  2.872   11.022  1.00 65.61  ? 135 SER A OG  1 
ATOM 848  N N   . LYS A 1 136 ? 3.680  4.091   13.016  1.00 75.94  ? 136 LYS A N   1 
ATOM 849  C CA  . LYS A 1 136 ? 2.225  4.106   13.060  1.00 72.77  ? 136 LYS A CA  1 
ATOM 850  C C   . LYS A 1 136 ? 1.605  3.269   11.952  1.00 64.67  ? 136 LYS A C   1 
ATOM 851  O O   . LYS A 1 136 ? 0.379  3.125   11.909  1.00 68.36  ? 136 LYS A O   1 
ATOM 852  C CB  . LYS A 1 136 ? 1.704  5.545   12.956  1.00 66.87  ? 136 LYS A CB  1 
ATOM 853  C CG  . LYS A 1 136 ? 1.876  6.396   14.210  1.00 76.15  ? 136 LYS A CG  1 
ATOM 854  C CD  . LYS A 1 136 ? 2.103  5.559   15.459  1.00 72.48  ? 136 LYS A CD  1 
ATOM 855  C CE  . LYS A 1 136 ? 2.448  6.441   16.647  1.00 73.58  ? 136 LYS A CE  1 
ATOM 856  N NZ  . LYS A 1 136 ? 2.586  5.655   17.904  1.00 72.99  ? 136 LYS A NZ  1 
ATOM 857  N N   . TYR A 1 137 ? 2.423  2.715   11.063  1.00 59.64  ? 137 TYR A N   1 
ATOM 858  C CA  . TYR A 1 137 ? 1.952  1.927   9.935   1.00 64.95  ? 137 TYR A CA  1 
ATOM 859  C C   . TYR A 1 137 ? 2.239  0.442   10.093  1.00 63.31  ? 137 TYR A C   1 
ATOM 860  O O   . TYR A 1 137 ? 1.891  -0.343  9.205   1.00 59.91  ? 137 TYR A O   1 
ATOM 861  C CB  . TYR A 1 137 ? 2.570  2.482   8.650   1.00 66.15  ? 137 TYR A CB  1 
ATOM 862  C CG  . TYR A 1 137 ? 2.288  3.961   8.520   1.00 71.74  ? 137 TYR A CG  1 
ATOM 863  C CD1 . TYR A 1 137 ? 0.984  4.438   8.570   1.00 69.45  ? 137 TYR A CD1 1 
ATOM 864  C CD2 . TYR A 1 137 ? 3.319  4.887   8.417   1.00 79.09  ? 137 TYR A CD2 1 
ATOM 865  C CE1 . TYR A 1 137 ? 0.710  5.788   8.476   1.00 80.59  ? 137 TYR A CE1 1 
ATOM 866  C CE2 . TYR A 1 137 ? 3.054  6.245   8.327   1.00 73.66  ? 137 TYR A CE2 1 
ATOM 867  C CZ  . TYR A 1 137 ? 1.747  6.688   8.354   1.00 73.84  ? 137 TYR A CZ  1 
ATOM 868  O OH  . TYR A 1 137 ? 1.474  8.033   8.263   1.00 71.51  ? 137 TYR A OH  1 
ATOM 869  N N   . THR A 1 138 ? 2.868  0.040   11.195  1.00 63.99  ? 138 THR A N   1 
ATOM 870  C CA  . THR A 1 138 ? 3.068  -1.365  11.515  1.00 63.75  ? 138 THR A CA  1 
ATOM 871  C C   . THR A 1 138 ? 3.277  -1.496  13.015  1.00 64.13  ? 138 THR A C   1 
ATOM 872  O O   . THR A 1 138 ? 3.825  -0.598  13.660  1.00 64.80  ? 138 THR A O   1 
ATOM 873  C CB  . THR A 1 138 ? 4.260  -1.969  10.762  1.00 64.47  ? 138 THR A CB  1 
ATOM 874  O OG1 . THR A 1 138 ? 4.455  -3.324  11.186  1.00 63.84  ? 138 THR A OG1 1 
ATOM 875  C CG2 . THR A 1 138 ? 5.528  -1.175  11.037  1.00 65.67  ? 138 THR A CG2 1 
ATOM 876  N N   . ASP A 1 139 ? 2.822  -2.619  13.563  1.00 63.75  ? 139 ASP A N   1 
ATOM 877  C CA  . ASP A 1 139 ? 3.061  -2.958  14.957  1.00 64.98  ? 139 ASP A CA  1 
ATOM 878  C C   . ASP A 1 139 ? 4.248  -3.894  15.120  1.00 70.53  ? 139 ASP A C   1 
ATOM 879  O O   . ASP A 1 139 ? 4.605  -4.237  16.249  1.00 67.83  ? 139 ASP A O   1 
ATOM 880  C CB  . ASP A 1 139 ? 1.810  -3.590  15.577  1.00 70.07  ? 139 ASP A CB  1 
ATOM 881  C CG  . ASP A 1 139 ? 0.546  -2.810  15.265  1.00 79.88  ? 139 ASP A CG  1 
ATOM 882  O OD1 . ASP A 1 139 ? 0.294  -1.786  15.936  1.00 84.41  ? 139 ASP A OD1 1 
ATOM 883  O OD2 . ASP A 1 139 ? -0.197 -3.222  14.349  1.00 89.75  ? 139 ASP A OD2 1 
ATOM 884  N N   . PHE A 1 140 ? 4.857  -4.320  14.013  1.00 70.09  ? 140 PHE A N   1 
ATOM 885  C CA  . PHE A 1 140 ? 5.981  -5.255  14.024  1.00 61.70  ? 140 PHE A CA  1 
ATOM 886  C C   . PHE A 1 140 ? 7.300  -4.519  14.280  1.00 65.67  ? 140 PHE A C   1 
ATOM 887  O O   . PHE A 1 140 ? 8.248  -4.580  13.496  1.00 68.06  ? 140 PHE A O   1 
ATOM 888  C CB  . PHE A 1 140 ? 6.015  -6.013  12.703  1.00 56.75  ? 140 PHE A CB  1 
ATOM 889  C CG  . PHE A 1 140 ? 6.865  -7.246  12.728  1.00 56.77  ? 140 PHE A CG  1 
ATOM 890  C CD1 . PHE A 1 140 ? 7.038  -7.966  13.897  1.00 56.66  ? 140 PHE A CD1 1 
ATOM 891  C CD2 . PHE A 1 140 ? 7.494  -7.685  11.576  1.00 58.70  ? 140 PHE A CD2 1 
ATOM 892  C CE1 . PHE A 1 140 ? 7.820  -9.104  13.915  1.00 56.89  ? 140 PHE A CE1 1 
ATOM 893  C CE2 . PHE A 1 140 ? 8.277  -8.820  11.587  1.00 56.13  ? 140 PHE A CE2 1 
ATOM 894  C CZ  . PHE A 1 140 ? 8.442  -9.531  12.758  1.00 54.21  ? 140 PHE A CZ  1 
ATOM 895  N N   . THR A 1 141 ? 7.353  -3.814  15.409  1.00 59.41  ? 141 THR A N   1 
ATOM 896  C CA  . THR A 1 141 ? 8.461  -2.919  15.708  1.00 55.62  ? 141 THR A CA  1 
ATOM 897  C C   . THR A 1 141 ? 9.074  -3.262  17.059  1.00 67.59  ? 141 THR A C   1 
ATOM 898  O O   . THR A 1 141 ? 8.465  -3.941  17.891  1.00 67.92  ? 141 THR A O   1 
ATOM 899  C CB  . THR A 1 141 ? 8.019  -1.450  15.709  1.00 61.55  ? 141 THR A CB  1 
ATOM 900  O OG1 . THR A 1 141 ? 7.445  -1.125  16.982  1.00 64.46  ? 141 THR A OG1 1 
ATOM 901  C CG2 . THR A 1 141 ? 6.997  -1.191  14.611  1.00 61.33  ? 141 THR A CG2 1 
ATOM 902  N N   . SER A 1 142 ? 10.300 -2.769  17.268  1.00 62.39  ? 142 SER A N   1 
ATOM 903  C CA  . SER A 1 142 ? 10.987 -3.001  18.535  1.00 59.54  ? 142 SER A CA  1 
ATOM 904  C C   . SER A 1 142 ? 10.308 -2.274  19.689  1.00 60.61  ? 142 SER A C   1 
ATOM 905  O O   . SER A 1 142 ? 10.408 -2.716  20.839  1.00 61.77  ? 142 SER A O   1 
ATOM 906  C CB  . SER A 1 142 ? 12.452 -2.578  18.430  1.00 49.99  ? 142 SER A CB  1 
ATOM 907  O OG  . SER A 1 142 ? 12.571 -1.170  18.367  1.00 53.98  ? 142 SER A OG  1 
ATOM 908  N N   . THR A 1 143 ? 9.626  -1.160  19.410  1.00 58.74  ? 143 THR A N   1 
ATOM 909  C CA  . THR A 1 143 ? 8.869  -0.487  20.459  1.00 57.89  ? 143 THR A CA  1 
ATOM 910  C C   . THR A 1 143 ? 7.712  -1.355  20.931  1.00 64.34  ? 143 THR A C   1 
ATOM 911  O O   . THR A 1 143 ? 7.351  -1.326  22.114  1.00 62.83  ? 143 THR A O   1 
ATOM 912  C CB  . THR A 1 143 ? 8.342  0.860   19.959  1.00 58.40  ? 143 THR A CB  1 
ATOM 913  O OG1 . THR A 1 143 ? 7.685  0.680   18.698  1.00 56.69  ? 143 THR A OG1 1 
ATOM 914  C CG2 . THR A 1 143 ? 9.481  1.851   19.789  1.00 61.12  ? 143 THR A CG2 1 
ATOM 915  N N   . ASN A 1 144 ? 7.132  -2.136  20.018  1.00 64.94  ? 144 ASN A N   1 
ATOM 916  C CA  . ASN A 1 144 ? 6.057  -3.055  20.371  1.00 64.75  ? 144 ASN A CA  1 
ATOM 917  C C   . ASN A 1 144 ? 6.583  -4.245  21.164  1.00 64.70  ? 144 ASN A C   1 
ATOM 918  O O   . ASN A 1 144 ? 5.901  -4.753  22.061  1.00 58.75  ? 144 ASN A O   1 
ATOM 919  C CB  . ASN A 1 144 ? 5.363  -3.529  19.097  1.00 66.24  ? 144 ASN A CB  1 
ATOM 920  C CG  . ASN A 1 144 ? 3.881  -3.759  19.284  1.00 74.83  ? 144 ASN A CG  1 
ATOM 921  O OD1 . ASN A 1 144 ? 3.094  -2.813  19.325  1.00 80.65  ? 144 ASN A OD1 1 
ATOM 922  N ND2 . ASN A 1 144 ? 3.488  -5.024  19.382  1.00 72.29  ? 144 ASN A ND2 1 
ATOM 923  N N   . SER A 1 145 ? 7.796  -4.699  20.846  1.00 64.98  ? 145 SER A N   1 
ATOM 924  C CA  . SER A 1 145 ? 8.403  -5.894  21.417  1.00 57.76  ? 145 SER A CA  1 
ATOM 925  C C   . SER A 1 145 ? 8.649  -5.727  22.913  1.00 60.97  ? 145 SER A C   1 
ATOM 926  O O   . SER A 1 145 ? 8.492  -4.622  23.448  1.00 57.59  ? 145 SER A O   1 
ATOM 927  C CB  . SER A 1 145 ? 9.722  -6.206  20.708  1.00 61.70  ? 145 SER A CB  1 
ATOM 928  O OG  . SER A 1 145 ? 10.623 -5.121  20.818  1.00 60.32  ? 145 SER A OG  1 
ATOM 929  N N   . PRO A 1 146 ? 9.013  -6.809  23.625  1.00 60.52  ? 146 PRO A N   1 
ATOM 930  C CA  . PRO A 1 146 ? 9.405  -6.680  25.037  1.00 53.46  ? 146 PRO A CA  1 
ATOM 931  C C   . PRO A 1 146 ? 10.444 -5.599  25.306  1.00 56.06  ? 146 PRO A C   1 
ATOM 932  O O   . PRO A 1 146 ? 10.564 -5.128  26.441  1.00 55.03  ? 146 PRO A O   1 
ATOM 933  C CB  . PRO A 1 146 ? 9.964  -8.073  25.372  1.00 57.17  ? 146 PRO A CB  1 
ATOM 934  C CG  . PRO A 1 146 ? 9.702  -8.949  24.147  1.00 62.82  ? 146 PRO A CG  1 
ATOM 935  C CD  . PRO A 1 146 ? 8.751  -8.211  23.270  1.00 54.59  ? 146 PRO A CD  1 
ATOM 936  N N   . ALA A 1 147 ? 11.211 -5.211  24.283  1.00 56.84  ? 147 ALA A N   1 
ATOM 937  C CA  . ALA A 1 147 ? 12.226 -4.178  24.470  1.00 48.95  ? 147 ALA A CA  1 
ATOM 938  C C   . ALA A 1 147 ? 11.597 -2.828  24.794  1.00 53.95  ? 147 ALA A C   1 
ATOM 939  O O   . ALA A 1 147 ? 12.139 -2.065  25.604  1.00 52.37  ? 147 ALA A O   1 
ATOM 940  C CB  . ALA A 1 147 ? 13.098 -4.070  23.220  1.00 51.86  ? 147 ALA A CB  1 
ATOM 941  N N   . LYS A 1 148 ? 10.451 -2.522  24.182  1.00 54.24  ? 148 LYS A N   1 
ATOM 942  C CA  . LYS A 1 148 ? 9.719  -1.276  24.426  1.00 57.94  ? 148 LYS A CA  1 
ATOM 943  C C   . LYS A 1 148 ? 10.587 -0.041  24.187  1.00 60.55  ? 148 LYS A C   1 
ATOM 944  O O   . LYS A 1 148 ? 10.391 0.998   24.820  1.00 58.77  ? 148 LYS A O   1 
ATOM 945  C CB  . LYS A 1 148 ? 9.133  -1.245  25.841  1.00 62.35  ? 148 LYS A CB  1 
ATOM 946  C CG  . LYS A 1 148 ? 8.202  -2.403  26.164  1.00 54.51  ? 148 LYS A CG  1 
ATOM 947  C CD  . LYS A 1 148 ? 6.889  -2.298  25.403  1.00 54.45  ? 148 LYS A CD  1 
ATOM 948  C CE  . LYS A 1 148 ? 6.034  -3.538  25.623  1.00 53.99  ? 148 LYS A CE  1 
ATOM 949  N NZ  . LYS A 1 148 ? 4.984  -3.690  24.578  1.00 57.15  ? 148 LYS A NZ  1 
ATOM 950  N N   . ARG A 1 149 ? 11.556 -0.141  23.276  1.00 61.69  ? 149 ARG A N   1 
ATOM 951  C CA  . ARG A 1 149 ? 12.491 0.943   23.011  1.00 54.31  ? 149 ARG A CA  1 
ATOM 952  C C   . ARG A 1 149 ? 12.494 1.292   21.529  1.00 57.17  ? 149 ARG A C   1 
ATOM 953  O O   . ARG A 1 149 ? 12.254 0.439   20.671  1.00 56.19  ? 149 ARG A O   1 
ATOM 954  C CB  . ARG A 1 149 ? 13.919 0.579   23.440  1.00 46.07  ? 149 ARG A CB  1 
ATOM 955  C CG  . ARG A 1 149 ? 14.108 0.385   24.931  1.00 43.27  ? 149 ARG A CG  1 
ATOM 956  C CD  . ARG A 1 149 ? 15.322 -0.489  25.209  1.00 52.10  ? 149 ARG A CD  1 
ATOM 957  N NE  . ARG A 1 149 ? 16.571 0.184   24.872  1.00 54.38  ? 149 ARG A NE  1 
ATOM 958  C CZ  . ARG A 1 149 ? 17.763 -0.397  24.882  1.00 54.16  ? 149 ARG A CZ  1 
ATOM 959  N NH1 . ARG A 1 149 ? 17.910 -1.668  25.218  1.00 50.49  ? 149 ARG A NH1 1 
ATOM 960  N NH2 . ARG A 1 149 ? 18.836 0.315   24.548  1.00 54.12  ? 149 ARG A NH2 1 
ATOM 961  N N   . ASP A 1 150 ? 12.775 2.563   21.243  1.00 67.15  ? 150 ASP A N   1 
ATOM 962  C CA  . ASP A 1 150 ? 13.008 3.048   19.882  1.00 53.25  ? 150 ASP A CA  1 
ATOM 963  C C   . ASP A 1 150 ? 14.518 3.185   19.713  1.00 55.18  ? 150 ASP A C   1 
ATOM 964  O O   . ASP A 1 150 ? 15.107 4.220   20.029  1.00 50.23  ? 150 ASP A O   1 
ATOM 965  C CB  . ASP A 1 150 ? 12.280 4.368   19.642  1.00 51.18  ? 150 ASP A CB  1 
ATOM 966  C CG  . ASP A 1 150 ? 12.240 4.763   18.173  1.00 56.60  ? 150 ASP A CG  1 
ATOM 967  O OD1 . ASP A 1 150 ? 13.217 4.486   17.445  1.00 60.14  ? 150 ASP A OD1 1 
ATOM 968  O OD2 . ASP A 1 150 ? 11.226 5.357   17.745  1.00 52.87  ? 150 ASP A OD2 1 
ATOM 969  N N   . LEU A 1 151 ? 15.151 2.118   19.214  1.00 50.54  ? 151 LEU A N   1 
ATOM 970  C CA  . LEU A 1 151 ? 16.608 2.098   19.123  1.00 46.16  ? 151 LEU A CA  1 
ATOM 971  C C   . LEU A 1 151 ? 17.128 3.117   18.118  1.00 46.72  ? 151 LEU A C   1 
ATOM 972  O O   . LEU A 1 151 ? 18.257 3.601   18.257  1.00 46.92  ? 151 LEU A O   1 
ATOM 973  C CB  . LEU A 1 151 ? 17.093 0.695   18.760  1.00 46.75  ? 151 LEU A CB  1 
ATOM 974  C CG  . LEU A 1 151 ? 16.634 -0.424  19.695  1.00 47.91  ? 151 LEU A CG  1 
ATOM 975  C CD1 . LEU A 1 151 ? 17.191 -1.763  19.245  1.00 54.88  ? 151 LEU A CD1 1 
ATOM 976  C CD2 . LEU A 1 151 ? 17.041 -0.125  21.130  1.00 56.92  ? 151 LEU A CD2 1 
ATOM 977  N N   . VAL A 1 152 ? 16.328 3.458   17.106  1.00 45.41  ? 152 VAL A N   1 
ATOM 978  C CA  . VAL A 1 152 ? 16.725 4.514   16.182  1.00 46.70  ? 152 VAL A CA  1 
ATOM 979  C C   . VAL A 1 152 ? 16.719 5.860   16.894  1.00 45.87  ? 152 VAL A C   1 
ATOM 980  O O   . VAL A 1 152 ? 17.625 6.682   16.709  1.00 45.78  ? 152 VAL A O   1 
ATOM 981  C CB  . VAL A 1 152 ? 15.812 4.514   14.943  1.00 42.94  ? 152 VAL A CB  1 
ATOM 982  C CG1 . VAL A 1 152 ? 16.041 5.765   14.109  1.00 39.63  ? 152 VAL A CG1 1 
ATOM 983  C CG2 . VAL A 1 152 ? 16.055 3.264   14.114  1.00 42.05  ? 152 VAL A CG2 1 
ATOM 984  N N   . ALA A 1 153 ? 15.704 6.103   17.725  1.00 40.91  ? 153 ALA A N   1 
ATOM 985  C CA  . ALA A 1 153 ? 15.683 7.313   18.538  1.00 42.21  ? 153 ALA A CA  1 
ATOM 986  C C   . ALA A 1 153 ? 16.877 7.347   19.484  1.00 43.27  ? 153 ALA A C   1 
ATOM 987  O O   . ALA A 1 153 ? 17.535 8.383   19.637  1.00 47.06  ? 153 ALA A O   1 
ATOM 988  C CB  . ALA A 1 153 ? 14.369 7.402   19.316  1.00 33.19  ? 153 ALA A CB  1 
ATOM 989  N N   . GLU A 1 154 ? 17.163 6.219   20.138  1.00 42.21  ? 154 GLU A N   1 
ATOM 990  C CA  . GLU A 1 154 ? 18.311 6.141   21.036  1.00 48.33  ? 154 GLU A CA  1 
ATOM 991  C C   . GLU A 1 154 ? 19.606 6.482   20.308  1.00 49.72  ? 154 GLU A C   1 
ATOM 992  O O   . GLU A 1 154 ? 20.389 7.322   20.766  1.00 48.50  ? 154 GLU A O   1 
ATOM 993  C CB  . GLU A 1 154 ? 18.406 4.741   21.646  1.00 53.73  ? 154 GLU A CB  1 
ATOM 994  C CG  . GLU A 1 154 ? 17.317 4.393   22.645  1.00 46.24  ? 154 GLU A CG  1 
ATOM 995  C CD  . GLU A 1 154 ? 17.586 3.072   23.344  1.00 62.58  ? 154 GLU A CD  1 
ATOM 996  O OE1 . GLU A 1 154 ? 18.775 2.715   23.502  1.00 60.11  ? 154 GLU A OE1 1 
ATOM 997  O OE2 . GLU A 1 154 ? 16.613 2.389   23.729  1.00 56.10  ? 154 GLU A OE2 1 
ATOM 998  N N   . LEU A 1 155 ? 19.845 5.835   19.163  1.00 53.60  ? 155 LEU A N   1 
ATOM 999  C CA  . LEU A 1 155 ? 21.082 6.060   18.419  1.00 47.98  ? 155 LEU A CA  1 
ATOM 1000 C C   . LEU A 1 155 ? 21.153 7.472   17.850  1.00 47.07  ? 155 LEU A C   1 
ATOM 1001 O O   . LEU A 1 155 ? 22.234 8.071   17.803  1.00 47.26  ? 155 LEU A O   1 
ATOM 1002 C CB  . LEU A 1 155 ? 21.217 5.027   17.304  1.00 46.21  ? 155 LEU A CB  1 
ATOM 1003 C CG  . LEU A 1 155 ? 22.299 3.977   17.544  1.00 48.54  ? 155 LEU A CG  1 
ATOM 1004 C CD1 . LEU A 1 155 ? 22.155 2.852   16.555  1.00 44.69  ? 155 LEU A CD1 1 
ATOM 1005 C CD2 . LEU A 1 155 ? 23.681 4.600   17.444  1.00 51.29  ? 155 LEU A CD2 1 
ATOM 1006 N N   . ALA A 1 156 ? 20.020 8.012   17.395  1.00 45.92  ? 156 ALA A N   1 
ATOM 1007 C CA  . ALA A 1 156 ? 20.018 9.351   16.813  1.00 53.08  ? 156 ALA A CA  1 
ATOM 1008 C C   . ALA A 1 156 ? 20.492 10.389  17.824  1.00 51.94  ? 156 ALA A C   1 
ATOM 1009 O O   . ALA A 1 156 ? 21.337 11.236  17.512  1.00 49.08  ? 156 ALA A O   1 
ATOM 1010 C CB  . ALA A 1 156 ? 18.622 9.699   16.296  1.00 47.49  ? 156 ALA A CB  1 
ATOM 1011 N N   . GLU A 1 157 ? 19.948 10.343  19.042  1.00 53.80  ? 157 GLU A N   1 
ATOM 1012 C CA  . GLU A 1 157 ? 20.342 11.305  20.067  1.00 59.32  ? 157 GLU A CA  1 
ATOM 1013 C C   . GLU A 1 157 ? 21.823 11.189  20.405  1.00 55.32  ? 157 GLU A C   1 
ATOM 1014 O O   . GLU A 1 157 ? 22.514 12.204  20.552  1.00 55.71  ? 157 GLU A O   1 
ATOM 1015 C CB  . GLU A 1 157 ? 19.490 11.116  21.322  1.00 68.60  ? 157 GLU A CB  1 
ATOM 1016 C CG  . GLU A 1 157 ? 20.043 11.804  22.565  1.00 70.57  ? 157 GLU A CG  1 
ATOM 1017 C CD  . GLU A 1 157 ? 19.819 13.308  22.571  1.00 77.95  ? 157 GLU A CD  1 
ATOM 1018 O OE1 . GLU A 1 157 ? 19.480 13.878  21.511  1.00 80.52  ? 157 GLU A OE1 1 
ATOM 1019 O OE2 . GLU A 1 157 ? 19.985 13.924  23.645  1.00 81.80  ? 157 GLU A OE2 1 
ATOM 1020 N N   . GLU A 1 158 ? 22.328 9.960   20.542  1.00 56.98  ? 158 GLU A N   1 
ATOM 1021 C CA  . GLU A 1 158 ? 23.747 9.784   20.834  1.00 55.16  ? 158 GLU A CA  1 
ATOM 1022 C C   . GLU A 1 158 ? 24.621 10.304  19.701  1.00 51.79  ? 158 GLU A C   1 
ATOM 1023 O O   . GLU A 1 158 ? 25.752 10.742  19.941  1.00 47.38  ? 158 GLU A O   1 
ATOM 1024 C CB  . GLU A 1 158 ? 24.053 8.313   21.118  1.00 43.20  ? 158 GLU A CB  1 
ATOM 1025 C CG  . GLU A 1 158 ? 23.564 7.825   22.476  1.00 49.76  ? 158 GLU A CG  1 
ATOM 1026 C CD  . GLU A 1 158 ? 24.102 8.646   23.642  1.00 64.02  ? 158 GLU A CD  1 
ATOM 1027 O OE1 . GLU A 1 158 ? 23.458 8.644   24.712  1.00 74.45  ? 158 GLU A OE1 1 
ATOM 1028 O OE2 . GLU A 1 158 ? 25.174 9.274   23.506  1.00 68.00  ? 158 GLU A OE2 1 
ATOM 1029 N N   . CYS A 1 159 ? 24.116 10.271  18.466  1.00 47.43  ? 159 CYS A N   1 
ATOM 1030 C CA  . CYS A 1 159 ? 24.868 10.821  17.344  1.00 46.63  ? 159 CYS A CA  1 
ATOM 1031 C C   . CYS A 1 159 ? 24.812 12.344  17.346  1.00 46.82  ? 159 CYS A C   1 
ATOM 1032 O O   . CYS A 1 159 ? 25.836 13.011  17.164  1.00 43.22  ? 159 CYS A O   1 
ATOM 1033 C CB  . CYS A 1 159 ? 24.330 10.258  16.028  1.00 42.80  ? 159 CYS A CB  1 
ATOM 1034 S SG  . CYS A 1 159 ? 24.902 8.579   15.648  1.00 53.47  ? 159 CYS A SG  1 
ATOM 1035 N N   . ARG A 1 160 ? 23.618 12.907  17.558  1.00 40.05  ? 160 ARG A N   1 
ATOM 1036 C CA  . ARG A 1 160 ? 23.484 14.354  17.693  1.00 46.10  ? 160 ARG A CA  1 
ATOM 1037 C C   . ARG A 1 160 ? 24.343 14.883  18.835  1.00 48.25  ? 160 ARG A C   1 
ATOM 1038 O O   . ARG A 1 160 ? 24.960 15.949  18.718  1.00 47.44  ? 160 ARG A O   1 
ATOM 1039 C CB  . ARG A 1 160 ? 22.016 14.720  17.917  1.00 54.36  ? 160 ARG A CB  1 
ATOM 1040 C CG  . ARG A 1 160 ? 21.736 16.213  17.962  1.00 56.19  ? 160 ARG A CG  1 
ATOM 1041 C CD  . ARG A 1 160 ? 20.670 16.541  19.001  1.00 68.48  ? 160 ARG A CD  1 
ATOM 1042 N NE  . ARG A 1 160 ? 21.251 16.802  20.314  1.00 78.80  ? 160 ARG A NE  1 
ATOM 1043 C CZ  . ARG A 1 160 ? 20.550 16.959  21.429  1.00 77.06  ? 160 ARG A CZ  1 
ATOM 1044 N NH1 . ARG A 1 160 ? 19.229 16.879  21.433  1.00 71.18  ? 160 ARG A NH1 1 
ATOM 1045 N NH2 . ARG A 1 160 ? 21.190 17.204  22.569  1.00 67.17  ? 160 ARG A NH2 1 
ATOM 1046 N N   . LYS A 1 161 ? 24.397 14.146  19.946  1.00 49.47  ? 161 LYS A N   1 
ATOM 1047 C CA  . LYS A 1 161 ? 25.193 14.573  21.092  1.00 47.61  ? 161 LYS A CA  1 
ATOM 1048 C C   . LYS A 1 161 ? 26.680 14.589  20.762  1.00 44.65  ? 161 LYS A C   1 
ATOM 1049 O O   . LYS A 1 161 ? 27.418 15.461  21.236  1.00 64.27  ? 161 LYS A O   1 
ATOM 1050 C CB  . LYS A 1 161 ? 24.933 13.644  22.278  1.00 57.83  ? 161 LYS A CB  1 
ATOM 1051 C CG  . LYS A 1 161 ? 23.968 14.171  23.322  1.00 60.74  ? 161 LYS A CG  1 
ATOM 1052 C CD  . LYS A 1 161 ? 23.424 13.022  24.161  1.00 62.57  ? 161 LYS A CD  1 
ATOM 1053 C CE  . LYS A 1 161 ? 24.542 12.322  24.923  1.00 55.49  ? 161 LYS A CE  1 
ATOM 1054 N NZ  . LYS A 1 161 ? 24.225 12.152  26.368  1.00 57.38  ? 161 LYS A NZ  1 
ATOM 1055 N N   . LYS A 1 162 ? 27.143 13.630  19.962  1.00 44.99  ? 162 LYS A N   1 
ATOM 1056 C CA  . LYS A 1 162 ? 28.568 13.414  19.756  1.00 48.08  ? 162 LYS A CA  1 
ATOM 1057 C C   . LYS A 1 162 ? 29.054 13.866  18.384  1.00 50.89  ? 162 LYS A C   1 
ATOM 1058 O O   . LYS A 1 162 ? 30.206 13.593  18.027  1.00 46.31  ? 162 LYS A O   1 
ATOM 1059 C CB  . LYS A 1 162 ? 28.902 11.936  19.972  1.00 51.69  ? 162 LYS A CB  1 
ATOM 1060 C CG  . LYS A 1 162 ? 28.632 11.450  21.386  1.00 47.72  ? 162 LYS A CG  1 
ATOM 1061 C CD  . LYS A 1 162 ? 29.187 10.055  21.609  1.00 54.89  ? 162 LYS A CD  1 
ATOM 1062 C CE  . LYS A 1 162 ? 28.929 9.585   23.029  1.00 52.57  ? 162 LYS A CE  1 
ATOM 1063 N NZ  . LYS A 1 162 ? 27.771 8.655   23.100  1.00 59.19  ? 162 LYS A NZ  1 
ATOM 1064 N N   . GLY A 1 163 ? 28.216 14.552  17.610  1.00 46.67  ? 163 GLY A N   1 
ATOM 1065 C CA  . GLY A 1 163 ? 28.648 15.057  16.321  1.00 40.65  ? 163 GLY A CA  1 
ATOM 1066 C C   . GLY A 1 163 ? 28.872 14.010  15.253  1.00 45.66  ? 163 GLY A C   1 
ATOM 1067 O O   . GLY A 1 163 ? 29.515 14.303  14.242  1.00 47.57  ? 163 GLY A O   1 
ATOM 1068 N N   . LEU A 1 164 ? 28.365 12.794  15.445  1.00 50.53  ? 164 LEU A N   1 
ATOM 1069 C CA  . LEU A 1 164 ? 28.526 11.725  14.468  1.00 47.34  ? 164 LEU A CA  1 
ATOM 1070 C C   . LEU A 1 164 ? 27.401 11.764  13.441  1.00 51.38  ? 164 LEU A C   1 
ATOM 1071 O O   . LEU A 1 164 ? 26.236 11.985  13.785  1.00 41.97  ? 164 LEU A O   1 
ATOM 1072 C CB  . LEU A 1 164 ? 28.548 10.358  15.157  1.00 45.06  ? 164 LEU A CB  1 
ATOM 1073 C CG  . LEU A 1 164 ? 29.824 9.947   15.895  1.00 48.25  ? 164 LEU A CG  1 
ATOM 1074 C CD1 . LEU A 1 164 ? 29.487 9.077   17.095  1.00 46.47  ? 164 LEU A CD1 1 
ATOM 1075 C CD2 . LEU A 1 164 ? 30.778 9.220   14.962  1.00 39.85  ? 164 LEU A CD2 1 
ATOM 1076 N N   . GLY A 1 165 ? 27.759 11.546  12.178  1.00 51.16  ? 165 GLY A N   1 
ATOM 1077 C CA  . GLY A 1 165 ? 26.748 11.405  11.145  1.00 36.65  ? 165 GLY A CA  1 
ATOM 1078 C C   . GLY A 1 165 ? 25.933 10.139  11.347  1.00 41.75  ? 165 GLY A C   1 
ATOM 1079 O O   . GLY A 1 165 ? 26.448 9.101   11.766  1.00 45.72  ? 165 GLY A O   1 
ATOM 1080 N N   . PHE A 1 166 ? 24.638 10.234  11.060  1.00 47.16  ? 166 PHE A N   1 
ATOM 1081 C CA  . PHE A 1 166 ? 23.696 9.147   11.297  1.00 39.20  ? 166 PHE A CA  1 
ATOM 1082 C C   . PHE A 1 166 ? 22.967 8.824   10.000  1.00 42.52  ? 166 PHE A C   1 
ATOM 1083 O O   . PHE A 1 166 ? 22.286 9.688   9.438   1.00 41.80  ? 166 PHE A O   1 
ATOM 1084 C CB  . PHE A 1 166 ? 22.708 9.527   12.400  1.00 39.77  ? 166 PHE A CB  1 
ATOM 1085 C CG  . PHE A 1 166 ? 21.889 8.378   12.906  1.00 45.05  ? 166 PHE A CG  1 
ATOM 1086 C CD1 . PHE A 1 166 ? 22.467 7.138   13.120  1.00 42.20  ? 166 PHE A CD1 1 
ATOM 1087 C CD2 . PHE A 1 166 ? 20.542 8.542   13.183  1.00 42.47  ? 166 PHE A CD2 1 
ATOM 1088 C CE1 . PHE A 1 166 ? 21.713 6.081   13.590  1.00 45.89  ? 166 PHE A CE1 1 
ATOM 1089 C CE2 . PHE A 1 166 ? 19.785 7.491   13.655  1.00 44.09  ? 166 PHE A CE2 1 
ATOM 1090 C CZ  . PHE A 1 166 ? 20.370 6.257   13.858  1.00 44.57  ? 166 PHE A CZ  1 
ATOM 1091 N N   . TYR A 1 167 ? 23.103 7.584   9.534   1.00 42.84  ? 167 TYR A N   1 
ATOM 1092 C CA  . TYR A 1 167 ? 22.489 7.132   8.294   1.00 42.05  ? 167 TYR A CA  1 
ATOM 1093 C C   . TYR A 1 167 ? 21.610 5.916   8.559   1.00 42.98  ? 167 TYR A C   1 
ATOM 1094 O O   . TYR A 1 167 ? 21.891 5.108   9.449   1.00 47.85  ? 167 TYR A O   1 
ATOM 1095 C CB  . TYR A 1 167 ? 23.553 6.815   7.238   1.00 32.73  ? 167 TYR A CB  1 
ATOM 1096 C CG  . TYR A 1 167 ? 24.364 8.029   6.840   1.00 37.54  ? 167 TYR A CG  1 
ATOM 1097 C CD1 . TYR A 1 167 ? 25.415 8.477   7.630   1.00 38.17  ? 167 TYR A CD1 1 
ATOM 1098 C CD2 . TYR A 1 167 ? 24.066 8.738   5.684   1.00 43.75  ? 167 TYR A CD2 1 
ATOM 1099 C CE1 . TYR A 1 167 ? 26.152 9.590   7.277   1.00 42.43  ? 167 TYR A CE1 1 
ATOM 1100 C CE2 . TYR A 1 167 ? 24.798 9.854   5.321   1.00 42.33  ? 167 TYR A CE2 1 
ATOM 1101 C CZ  . TYR A 1 167 ? 25.840 10.275  6.121   1.00 46.24  ? 167 TYR A CZ  1 
ATOM 1102 O OH  . TYR A 1 167 ? 26.574 11.385  5.766   1.00 50.16  ? 167 TYR A OH  1 
ATOM 1103 N N   . LEU A 1 168 ? 20.532 5.796   7.783   1.00 43.49  ? 168 LEU A N   1 
ATOM 1104 C CA  . LEU A 1 168 ? 19.462 4.840   8.056   1.00 42.98  ? 168 LEU A CA  1 
ATOM 1105 C C   . LEU A 1 168 ? 19.365 3.820   6.929   1.00 44.49  ? 168 LEU A C   1 
ATOM 1106 O O   . LEU A 1 168 ? 18.920 4.150   5.825   1.00 44.53  ? 168 LEU A O   1 
ATOM 1107 C CB  . LEU A 1 168 ? 18.128 5.564   8.223   1.00 39.06  ? 168 LEU A CB  1 
ATOM 1108 C CG  . LEU A 1 168 ? 18.120 6.780   9.147   1.00 41.15  ? 168 LEU A CG  1 
ATOM 1109 C CD1 . LEU A 1 168 ? 16.727 7.374   9.225   1.00 43.86  ? 168 LEU A CD1 1 
ATOM 1110 C CD2 . LEU A 1 168 ? 18.613 6.391   10.527  1.00 44.36  ? 168 LEU A CD2 1 
ATOM 1111 N N   . TYR A 1 169 ? 19.755 2.579   7.213   1.00 43.85  ? 169 TYR A N   1 
ATOM 1112 C CA  . TYR A 1 169 ? 19.458 1.481   6.305   1.00 37.37  ? 169 TYR A CA  1 
ATOM 1113 C C   . TYR A 1 169 ? 17.959 1.218   6.317   1.00 40.98  ? 169 TYR A C   1 
ATOM 1114 O O   . TYR A 1 169 ? 17.343 1.121   7.383   1.00 43.73  ? 169 TYR A O   1 
ATOM 1115 C CB  . TYR A 1 169 ? 20.229 0.222   6.712   1.00 38.37  ? 169 TYR A CB  1 
ATOM 1116 C CG  . TYR A 1 169 ? 19.926 -1.028  5.896   1.00 37.44  ? 169 TYR A CG  1 
ATOM 1117 C CD1 . TYR A 1 169 ? 18.716 -1.709  6.031   1.00 38.78  ? 169 TYR A CD1 1 
ATOM 1118 C CD2 . TYR A 1 169 ? 20.865 -1.545  5.016   1.00 39.65  ? 169 TYR A CD2 1 
ATOM 1119 C CE1 . TYR A 1 169 ? 18.444 -2.844  5.293   1.00 43.49  ? 169 TYR A CE1 1 
ATOM 1120 C CE2 . TYR A 1 169 ? 20.604 -2.686  4.280   1.00 44.40  ? 169 TYR A CE2 1 
ATOM 1121 C CZ  . TYR A 1 169 ? 19.391 -3.330  4.420   1.00 47.02  ? 169 TYR A CZ  1 
ATOM 1122 O OH  . TYR A 1 169 ? 19.123 -4.463  3.687   1.00 47.53  ? 169 TYR A OH  1 
ATOM 1123 N N   . TYR A 1 170 ? 17.371 1.091   5.131   1.00 40.25  ? 170 TYR A N   1 
ATOM 1124 C CA  . TYR A 1 170 ? 15.958 0.757   5.006   1.00 48.09  ? 170 TYR A CA  1 
ATOM 1125 C C   . TYR A 1 170 ? 15.782 -0.176  3.819   1.00 46.64  ? 170 TYR A C   1 
ATOM 1126 O O   . TYR A 1 170 ? 16.195 0.153   2.703   1.00 44.43  ? 170 TYR A O   1 
ATOM 1127 C CB  . TYR A 1 170 ? 15.107 2.020   4.841   1.00 42.89  ? 170 TYR A CB  1 
ATOM 1128 C CG  . TYR A 1 170 ? 13.618 1.773   4.913   1.00 49.90  ? 170 TYR A CG  1 
ATOM 1129 C CD1 . TYR A 1 170 ? 12.958 1.740   6.134   1.00 50.92  ? 170 TYR A CD1 1 
ATOM 1130 C CD2 . TYR A 1 170 ? 12.870 1.584   3.759   1.00 56.55  ? 170 TYR A CD2 1 
ATOM 1131 C CE1 . TYR A 1 170 ? 11.596 1.517   6.204   1.00 52.30  ? 170 TYR A CE1 1 
ATOM 1132 C CE2 . TYR A 1 170 ? 11.508 1.362   3.818   1.00 59.89  ? 170 TYR A CE2 1 
ATOM 1133 C CZ  . TYR A 1 170 ? 10.876 1.330   5.043   1.00 57.38  ? 170 TYR A CZ  1 
ATOM 1134 O OH  . TYR A 1 170 ? 9.520  1.108   5.104   1.00 59.40  ? 170 TYR A OH  1 
ATOM 1135 N N   . SER A 1 171 ? 15.178 -1.337  4.061   1.00 47.17  ? 171 SER A N   1 
ATOM 1136 C CA  . SER A 1 171 ? 14.987 -2.317  3.000   1.00 52.14  ? 171 SER A CA  1 
ATOM 1137 C C   . SER A 1 171 ? 13.960 -1.801  2.001   1.00 52.25  ? 171 SER A C   1 
ATOM 1138 O O   . SER A 1 171 ? 12.845 -1.426  2.378   1.00 55.23  ? 171 SER A O   1 
ATOM 1139 C CB  . SER A 1 171 ? 14.540 -3.655  3.588   1.00 49.80  ? 171 SER A CB  1 
ATOM 1140 O OG  . SER A 1 171 ? 14.371 -4.630  2.574   1.00 57.02  ? 171 SER A OG  1 
ATOM 1141 N N   . HIS A 1 172 ? 14.332 -1.794  0.721   1.00 53.12  ? 172 HIS A N   1 
ATOM 1142 C CA  . HIS A 1 172 ? 13.512 -1.180  -0.317  1.00 61.45  ? 172 HIS A CA  1 
ATOM 1143 C C   . HIS A 1 172 ? 13.027 -2.189  -1.349  1.00 68.17  ? 172 HIS A C   1 
ATOM 1144 O O   . HIS A 1 172 ? 11.816 -2.399  -1.476  1.00 64.09  ? 172 HIS A O   1 
ATOM 1145 C CB  . HIS A 1 172 ? 14.303 -0.065  -1.010  1.00 54.23  ? 172 HIS A CB  1 
ATOM 1146 C CG  . HIS A 1 172 ? 13.524 0.662   -2.059  1.00 56.93  ? 172 HIS A CG  1 
ATOM 1147 N ND1 . HIS A 1 172 ? 13.407 0.199   -3.352  1.00 59.76  ? 172 HIS A ND1 1 
ATOM 1148 C CD2 . HIS A 1 172 ? 12.852 1.836   -2.017  1.00 61.32  ? 172 HIS A CD2 1 
ATOM 1149 C CE1 . HIS A 1 172 ? 12.672 1.044   -4.054  1.00 65.34  ? 172 HIS A CE1 1 
ATOM 1150 N NE2 . HIS A 1 172 ? 12.323 2.046   -3.267  1.00 70.46  ? 172 HIS A NE2 1 
ATOM 1151 N N   . GLY A 1 173 ? 13.937 -2.818  -2.098  1.00 63.21  ? 173 GLY A N   1 
ATOM 1152 C CA  . GLY A 1 173 ? 13.528 -3.682  -3.191  1.00 65.50  ? 173 GLY A CA  1 
ATOM 1153 C C   . GLY A 1 173 ? 13.059 -5.053  -2.765  1.00 72.23  ? 173 GLY A C   1 
ATOM 1154 O O   . GLY A 1 173 ? 12.430 -5.755  -3.563  1.00 75.28  ? 173 GLY A O   1 
ATOM 1155 N N   . ARG A 1 174 ? 13.353 -5.450  -1.529  1.00 74.74  ? 174 ARG A N   1 
ATOM 1156 C CA  . ARG A 1 174 ? 12.961 -6.747  -0.998  1.00 62.97  ? 174 ARG A CA  1 
ATOM 1157 C C   . ARG A 1 174 ? 12.188 -6.564  0.297   1.00 70.02  ? 174 ARG A C   1 
ATOM 1158 O O   . ARG A 1 174 ? 12.567 -5.754  1.149   1.00 71.29  ? 174 ARG A O   1 
ATOM 1159 C CB  . ARG A 1 174 ? 14.172 -7.641  -0.722  1.00 55.02  ? 174 ARG A CB  1 
ATOM 1160 C CG  . ARG A 1 174 ? 14.746 -8.323  -1.936  1.00 65.93  ? 174 ARG A CG  1 
ATOM 1161 C CD  . ARG A 1 174 ? 15.838 -9.300  -1.541  1.00 60.02  ? 174 ARG A CD  1 
ATOM 1162 N NE  . ARG A 1 174 ? 17.115 -8.630  -1.331  1.00 62.19  ? 174 ARG A NE  1 
ATOM 1163 C CZ  . ARG A 1 174 ? 18.018 -8.425  -2.281  1.00 69.39  ? 174 ARG A CZ  1 
ATOM 1164 N NH1 . ARG A 1 174 ? 17.814 -8.823  -3.526  1.00 67.85  ? 174 ARG A NH1 1 
ATOM 1165 N NH2 . ARG A 1 174 ? 19.152 -7.801  -1.974  1.00 73.09  ? 174 ARG A NH2 1 
ATOM 1166 N N   . ASP A 1 175 ? 11.102 -7.318  0.434   1.00 74.34  ? 175 ASP A N   1 
ATOM 1167 C CA  . ASP A 1 175 ? 10.420 -7.459  1.712   1.00 65.96  ? 175 ASP A CA  1 
ATOM 1168 C C   . ASP A 1 175 ? 9.854  -8.867  1.782   1.00 66.76  ? 175 ASP A C   1 
ATOM 1169 O O   . ASP A 1 175 ? 9.224  -9.332  0.827   1.00 66.86  ? 175 ASP A O   1 
ATOM 1170 C CB  . ASP A 1 175 ? 9.311  -6.416  1.882   1.00 54.64  ? 175 ASP A CB  1 
ATOM 1171 C CG  . ASP A 1 175 ? 9.015  -6.116  3.338   1.00 64.25  ? 175 ASP A CG  1 
ATOM 1172 O OD1 . ASP A 1 175 ? 8.771  -7.071  4.105   1.00 68.49  ? 175 ASP A OD1 1 
ATOM 1173 O OD2 . ASP A 1 175 ? 9.027  -4.927  3.719   1.00 68.82  ? 175 ASP A OD2 1 
ATOM 1174 N N   . TRP A 1 176 ? 10.077 -9.537  2.909   1.00 64.14  ? 176 TRP A N   1 
ATOM 1175 C CA  . TRP A 1 176 ? 9.679  -10.926 3.081   1.00 57.16  ? 176 TRP A CA  1 
ATOM 1176 C C   . TRP A 1 176 ? 8.465  -11.069 3.985   1.00 66.38  ? 176 TRP A C   1 
ATOM 1177 O O   . TRP A 1 176 ? 8.104  -12.194 4.349   1.00 66.35  ? 176 TRP A O   1 
ATOM 1178 C CB  . TRP A 1 176 ? 10.842 -11.750 3.638   1.00 47.90  ? 176 TRP A CB  1 
ATOM 1179 C CG  . TRP A 1 176 ? 12.038 -11.805 2.740   1.00 55.39  ? 176 TRP A CG  1 
ATOM 1180 C CD1 . TRP A 1 176 ? 12.050 -11.686 1.382   1.00 54.57  ? 176 TRP A CD1 1 
ATOM 1181 C CD2 . TRP A 1 176 ? 13.401 -12.005 3.137   1.00 58.62  ? 176 TRP A CD2 1 
ATOM 1182 N NE1 . TRP A 1 176 ? 13.336 -11.796 0.907   1.00 49.21  ? 176 TRP A NE1 1 
ATOM 1183 C CE2 . TRP A 1 176 ? 14.184 -11.992 1.965   1.00 48.25  ? 176 TRP A CE2 1 
ATOM 1184 C CE3 . TRP A 1 176 ? 14.035 -12.192 4.370   1.00 49.37  ? 176 TRP A CE3 1 
ATOM 1185 C CZ2 . TRP A 1 176 ? 15.567 -12.158 1.989   1.00 46.73  ? 176 TRP A CZ2 1 
ATOM 1186 C CZ3 . TRP A 1 176 ? 15.407 -12.355 4.392   1.00 47.15  ? 176 TRP A CZ3 1 
ATOM 1187 C CH2 . TRP A 1 176 ? 16.159 -12.337 3.209   1.00 51.13  ? 176 TRP A CH2 1 
ATOM 1188 N N   . ARG A 1 177 ? 7.824  -9.961  4.353   1.00 62.70  ? 177 ARG A N   1 
ATOM 1189 C CA  . ARG A 1 177 ? 6.645  -10.029 5.206   1.00 64.34  ? 177 ARG A CA  1 
ATOM 1190 C C   . ARG A 1 177 ? 5.458  -9.313  4.576   1.00 70.28  ? 177 ARG A C   1 
ATOM 1191 O O   . ARG A 1 177 ? 4.384  -9.906  4.445   1.00 78.77  ? 177 ARG A O   1 
ATOM 1192 C CB  . ARG A 1 177 ? 6.939  -9.443  6.587   1.00 59.55  ? 177 ARG A CB  1 
ATOM 1193 C CG  . ARG A 1 177 ? 6.090  -10.057 7.685   1.00 57.61  ? 177 ARG A CG  1 
ATOM 1194 C CD  . ARG A 1 177 ? 5.494  -9.003  8.594   1.00 58.11  ? 177 ARG A CD  1 
ATOM 1195 N NE  . ARG A 1 177 ? 5.299  -9.512  9.947   1.00 59.57  ? 177 ARG A NE  1 
ATOM 1196 C CZ  . ARG A 1 177 ? 4.433  -9.012  10.818  1.00 63.58  ? 177 ARG A CZ  1 
ATOM 1197 N NH1 . ARG A 1 177 ? 3.671  -7.974  10.517  1.00 73.34  ? 177 ARG A NH1 1 
ATOM 1198 N NH2 . ARG A 1 177 ? 4.333  -9.566  12.023  1.00 59.78  ? 177 ARG A NH2 1 
ATOM 1199 N N   . HIS A 1 178 ? 5.639  -8.050  4.188   1.00 77.19  ? 178 HIS A N   1 
ATOM 1200 C CA  . HIS A 1 178 ? 4.560  -7.248  3.628   1.00 74.23  ? 178 HIS A CA  1 
ATOM 1201 C C   . HIS A 1 178 ? 3.862  -8.014  2.505   1.00 76.11  ? 178 HIS A C   1 
ATOM 1202 O O   . HIS A 1 178 ? 4.529  -8.456  1.557   1.00 74.25  ? 178 HIS A O   1 
ATOM 1203 C CB  . HIS A 1 178 ? 5.092  -5.916  3.104   1.00 74.26  ? 178 HIS A CB  1 
ATOM 1204 C CG  . HIS A 1 178 ? 4.055  -4.838  3.039   1.00 77.57  ? 178 HIS A CG  1 
ATOM 1205 N ND1 . HIS A 1 178 ? 3.145  -4.741  2.009   1.00 81.40  ? 178 HIS A ND1 1 
ATOM 1206 C CD2 . HIS A 1 178 ? 3.779  -3.813  3.881   1.00 68.61  ? 178 HIS A CD2 1 
ATOM 1207 C CE1 . HIS A 1 178 ? 2.356  -3.702  2.216   1.00 78.91  ? 178 HIS A CE1 1 
ATOM 1208 N NE2 . HIS A 1 178 ? 2.720  -3.122  3.346   1.00 75.33  ? 178 HIS A NE2 1 
ATOM 1209 N N   . PRO A 1 179 ? 2.542  -8.197  2.576   1.00 78.99  ? 179 PRO A N   1 
ATOM 1210 C CA  . PRO A 1 179 ? 1.869  -9.091  1.619   1.00 83.24  ? 179 PRO A CA  1 
ATOM 1211 C C   . PRO A 1 179 ? 1.933  -8.619  0.177   1.00 88.50  ? 179 PRO A C   1 
ATOM 1212 O O   . PRO A 1 179 ? 1.799  -9.447  -0.733  1.00 88.47  ? 179 PRO A O   1 
ATOM 1213 C CB  . PRO A 1 179 ? 0.418  -9.137  2.124   1.00 80.21  ? 179 PRO A CB  1 
ATOM 1214 C CG  . PRO A 1 179 ? 0.425  -8.519  3.485   1.00 79.65  ? 179 PRO A CG  1 
ATOM 1215 C CD  . PRO A 1 179 ? 1.627  -7.644  3.589   1.00 74.22  ? 179 PRO A CD  1 
ATOM 1216 N N   . HIS A 1 180 ? 2.132  -7.326  -0.066  1.00 83.77  ? 180 HIS A N   1 
ATOM 1217 C CA  . HIS A 1 180 ? 2.070  -6.771  -1.410  1.00 86.34  ? 180 HIS A CA  1 
ATOM 1218 C C   . HIS A 1 180 ? 3.441  -6.540  -2.037  1.00 83.69  ? 180 HIS A C   1 
ATOM 1219 O O   . HIS A 1 180 ? 3.512  -6.121  -3.197  1.00 84.26  ? 180 HIS A O   1 
ATOM 1220 C CB  . HIS A 1 180 ? 1.276  -5.462  -1.391  1.00 86.09  ? 180 HIS A CB  1 
ATOM 1221 C CG  . HIS A 1 180 ? -0.110 -5.610  -0.844  1.00 88.93  ? 180 HIS A CG  1 
ATOM 1222 N ND1 . HIS A 1 180 ? -1.104 -6.298  -1.507  1.00 84.94  ? 180 HIS A ND1 1 
ATOM 1223 C CD2 . HIS A 1 180 ? -0.664 -5.171  0.311   1.00 91.27  ? 180 HIS A CD2 1 
ATOM 1224 C CE1 . HIS A 1 180 ? -2.212 -6.269  -0.789  1.00 90.16  ? 180 HIS A CE1 1 
ATOM 1225 N NE2 . HIS A 1 180 ? -1.972 -5.591  0.319   1.00 88.99  ? 180 HIS A NE2 1 
ATOM 1226 N N   . ALA A 1 181 ? 4.523  -6.813  -1.311  1.00 76.29  ? 181 ALA A N   1 
ATOM 1227 C CA  . ALA A 1 181 ? 5.870  -6.605  -1.822  1.00 78.33  ? 181 ALA A CA  1 
ATOM 1228 C C   . ALA A 1 181 ? 6.205  -7.622  -2.918  1.00 76.13  ? 181 ALA A C   1 
ATOM 1229 O O   . ALA A 1 181 ? 5.538  -8.652  -3.042  1.00 82.90  ? 181 ALA A O   1 
ATOM 1230 C CB  . ALA A 1 181 ? 6.876  -6.693  -0.675  1.00 80.93  ? 181 ALA A CB  1 
ATOM 1231 N N   . PRO A 1 182 ? 7.223  -7.337  -3.737  1.00 73.42  ? 182 PRO A N   1 
ATOM 1232 C CA  . PRO A 1 182 ? 7.547  -8.206  -4.881  1.00 80.05  ? 182 PRO A CA  1 
ATOM 1233 C C   . PRO A 1 182 ? 7.609  -9.691  -4.542  1.00 83.69  ? 182 PRO A C   1 
ATOM 1234 O O   . PRO A 1 182 ? 8.249  -10.103 -3.572  1.00 78.95  ? 182 PRO A O   1 
ATOM 1235 C CB  . PRO A 1 182 ? 8.919  -7.685  -5.339  1.00 72.87  ? 182 PRO A CB  1 
ATOM 1236 C CG  . PRO A 1 182 ? 9.312  -6.601  -4.364  1.00 72.29  ? 182 PRO A CG  1 
ATOM 1237 C CD  . PRO A 1 182 ? 8.048  -6.119  -3.753  1.00 73.94  ? 182 PRO A CD  1 
ATOM 1238 N N   . ASN A 1 183 ? 6.946  -10.497 -5.369  1.00 81.06  ? 183 ASN A N   1 
ATOM 1239 C CA  . ASN A 1 183 ? 6.898  -11.945 -5.228  1.00 76.64  ? 183 ASN A CA  1 
ATOM 1240 C C   . ASN A 1 183 ? 7.894  -12.609 -6.175  1.00 80.77  ? 183 ASN A C   1 
ATOM 1241 O O   . ASN A 1 183 ? 8.407  -11.991 -7.110  1.00 80.45  ? 183 ASN A O   1 
ATOM 1242 C CB  . ASN A 1 183 ? 5.484  -12.466 -5.500  1.00 77.26  ? 183 ASN A CB  1 
ATOM 1243 C CG  . ASN A 1 183 ? 4.552  -12.257 -4.325  1.00 84.39  ? 183 ASN A CG  1 
ATOM 1244 O OD1 . ASN A 1 183 ? 4.538  -11.189 -3.713  1.00 81.13  ? 183 ASN A OD1 1 
ATOM 1245 N ND2 . ASN A 1 183 ? 3.761  -13.274 -4.006  1.00 80.80  ? 183 ASN A ND2 1 
ATOM 1246 N N   . ASN A 1 184 ? 8.157  -13.894 -5.920  1.00 78.40  ? 184 ASN A N   1 
ATOM 1247 C CA  . ASN A 1 184 ? 9.248  -14.589 -6.596  1.00 78.62  ? 184 ASN A CA  1 
ATOM 1248 C C   . ASN A 1 184 ? 8.952  -14.926 -8.050  1.00 76.95  ? 184 ASN A C   1 
ATOM 1249 O O   . ASN A 1 184 ? 9.884  -15.272 -8.784  1.00 76.18  ? 184 ASN A O   1 
ATOM 1250 C CB  . ASN A 1 184 ? 9.600  -15.867 -5.839  1.00 68.24  ? 184 ASN A CB  1 
ATOM 1251 C CG  . ASN A 1 184 ? 10.730 -15.660 -4.868  1.00 75.72  ? 184 ASN A CG  1 
ATOM 1252 O OD1 . ASN A 1 184 ? 10.739 -14.684 -4.124  1.00 68.37  ? 184 ASN A OD1 1 
ATOM 1253 N ND2 . ASN A 1 184 ? 11.697 -16.569 -4.871  1.00 72.56  ? 184 ASN A ND2 1 
ATOM 1254 N N   . GLY A 1 185 ? 7.702  -14.836 -8.485  1.00 75.63  ? 185 GLY A N   1 
ATOM 1255 C CA  . GLY A 1 185 ? 7.404  -15.030 -9.888  1.00 85.64  ? 185 GLY A CA  1 
ATOM 1256 C C   . GLY A 1 185 ? 7.697  -13.776 -10.681 1.00 84.58  ? 185 GLY A C   1 
ATOM 1257 O O   . GLY A 1 185 ? 8.563  -13.765 -11.562 1.00 80.90  ? 185 GLY A O   1 
ATOM 1258 N N   . ASP A 1 186 ? 6.972  -12.704 -10.354 1.00 85.96  ? 186 ASP A N   1 
ATOM 1259 C CA  . ASP A 1 186 ? 7.085  -11.461 -11.109 1.00 94.07  ? 186 ASP A CA  1 
ATOM 1260 C C   . ASP A 1 186 ? 8.498  -10.894 -11.048 1.00 93.62  ? 186 ASP A C   1 
ATOM 1261 O O   . ASP A 1 186 ? 9.017  -10.398 -12.054 1.00 87.48  ? 186 ASP A O   1 
ATOM 1262 C CB  . ASP A 1 186 ? 6.067  -10.447 -10.586 1.00 95.46  ? 186 ASP A CB  1 
ATOM 1263 C CG  . ASP A 1 186 ? 4.759  -11.099 -10.178 1.00 100.51 ? 186 ASP A CG  1 
ATOM 1264 O OD1 . ASP A 1 186 ? 4.278  -11.979 -10.921 1.00 107.71 ? 186 ASP A OD1 1 
ATOM 1265 O OD2 . ASP A 1 186 ? 4.214  -10.736 -9.113  1.00 99.51  ? 186 ASP A OD2 1 
ATOM 1266 N N   . TRP A 1 187 ? 9.068  -10.877 -9.844  1.00 90.08  ? 187 TRP A N   1 
ATOM 1267 C CA  . TRP A 1 187 ? 10.403 -10.258 -9.666  1.00 84.96  ? 187 TRP A CA  1 
ATOM 1268 C C   . TRP A 1 187 ? 11.397 -11.318 -9.196  1.00 79.66  ? 187 TRP A C   1 
ATOM 1269 O O   . TRP A 1 187 ? 10.964 -12.305 -8.584  1.00 78.20  ? 187 TRP A O   1 
ATOM 1270 C CB  . TRP A 1 187 ? 10.305 -9.106  -8.668  1.00 80.61  ? 187 TRP A CB  1 
ATOM 1271 C CG  . TRP A 1 187 ? 9.176  -8.153  -8.898  1.00 78.10  ? 187 TRP A CG  1 
ATOM 1272 C CD1 . TRP A 1 187 ? 7.866  -8.327  -8.561  1.00 83.79  ? 187 TRP A CD1 1 
ATOM 1273 C CD2 . TRP A 1 187 ? 9.268  -6.848  -9.492  1.00 81.39  ? 187 TRP A CD2 1 
ATOM 1274 N NE1 . TRP A 1 187 ? 7.136  -7.226  -8.918  1.00 86.16  ? 187 TRP A NE1 1 
ATOM 1275 C CE2 . TRP A 1 187 ? 7.969  -6.303  -9.491  1.00 85.34  ? 187 TRP A CE2 1 
ATOM 1276 C CE3 . TRP A 1 187 ? 10.317 -6.095  -10.028 1.00 81.09  ? 187 TRP A CE3 1 
ATOM 1277 C CZ2 . TRP A 1 187 ? 7.694  -5.038  -10.006 1.00 82.78  ? 187 TRP A CZ2 1 
ATOM 1278 C CZ3 . TRP A 1 187 ? 10.044 -4.847  -10.538 1.00 85.20  ? 187 TRP A CZ3 1 
ATOM 1279 C CH2 . TRP A 1 187 ? 8.750  -4.327  -10.524 1.00 86.38  ? 187 TRP A CH2 1 
ATOM 1280 N N   . GLY A 1 188 ? 12.680 -11.106 -9.471  1.00 75.02  ? 188 GLY A N   1 
ATOM 1281 C CA  . GLY A 1 188 ? 13.709 -12.053 -9.014  1.00 82.25  ? 188 GLY A CA  1 
ATOM 1282 C C   . GLY A 1 188 ? 14.509 -11.493 -7.859  1.00 80.67  ? 188 GLY A C   1 
ATOM 1283 O O   . GLY A 1 188 ? 13.901 -10.900 -6.963  1.00 85.99  ? 188 GLY A O   1 
ATOM 1284 N N   . GLY A 1 189 ? 15.830 -11.659 -7.886  1.00 70.80  ? 189 GLY A N   1 
ATOM 1285 C CA  . GLY A 1 189 ? 16.672 -11.223 -6.759  1.00 74.84  ? 189 GLY A CA  1 
ATOM 1286 C C   . GLY A 1 189 ? 17.152 -12.429 -5.984  1.00 73.03  ? 189 GLY A C   1 
ATOM 1287 O O   . GLY A 1 189 ? 17.774 -13.307 -6.600  1.00 68.59  ? 189 GLY A O   1 
ATOM 1288 N N   . ASN A 1 190 ? 16.846 -12.493 -4.691  1.00 62.00  ? 190 ASN A N   1 
ATOM 1289 C CA  . ASN A 1 190 ? 15.838 -13.452 -4.182  1.00 59.05  ? 190 ASN A CA  1 
ATOM 1290 C C   . ASN A 1 190 ? 14.722 -12.643 -3.528  1.00 57.25  ? 190 ASN A C   1 
ATOM 1291 O O   . ASN A 1 190 ? 14.769 -12.451 -2.312  1.00 63.28  ? 190 ASN A O   1 
ATOM 1292 C CB  . ASN A 1 190 ? 16.489 -14.490 -3.272  1.00 56.89  ? 190 ASN A CB  1 
ATOM 1293 C CG  . ASN A 1 190 ? 17.580 -15.276 -3.964  1.00 69.24  ? 190 ASN A CG  1 
ATOM 1294 O OD1 . ASN A 1 190 ? 18.607 -14.722 -4.346  1.00 69.20  ? 190 ASN A OD1 1 
ATOM 1295 N ND2 . ASN A 1 190 ? 17.367 -16.570 -4.131  1.00 68.61  ? 190 ASN A ND2 1 
ATOM 1296 N N   . ALA A 1 191 ? 13.757 -12.199 -4.324  1.00 58.33  ? 191 ALA A N   1 
ATOM 1297 C CA  . ALA A 1 191 ? 12.675 -11.337 -3.807  1.00 60.96  ? 191 ALA A CA  1 
ATOM 1298 C C   . ALA A 1 191 ? 12.144 -11.864 -2.480  1.00 66.37  ? 191 ALA A C   1 
ATOM 1299 O O   . ALA A 1 191 ? 12.184 -11.115 -1.499  1.00 67.07  ? 191 ALA A O   1 
ATOM 1300 C CB  . ALA A 1 191 ? 11.571 -11.269 -4.824  1.00 62.98  ? 191 ALA A CB  1 
ATOM 1301 N N   . ARG A 1 192 ? 11.628 -13.089 -2.472  1.00 66.85  ? 192 ARG A N   1 
ATOM 1302 C CA  . ARG A 1 192 ? 11.008 -13.637 -1.245  1.00 60.18  ? 192 ARG A CA  1 
ATOM 1303 C C   . ARG A 1 192 ? 11.547 -15.044 -1.000  1.00 55.57  ? 192 ARG A C   1 
ATOM 1304 O O   . ARG A 1 192 ? 12.038 -15.664 -1.948  1.00 55.40  ? 192 ARG A O   1 
ATOM 1305 C CB  . ARG A 1 192 ? 9.487  -13.636 -1.400  1.00 68.48  ? 192 ARG A CB  1 
ATOM 1306 C CG  . ARG A 1 192 ? 8.828  -12.265 -1.366  1.00 62.60  ? 192 ARG A CG  1 
ATOM 1307 C CD  . ARG A 1 192 ? 7.331  -12.497 -1.424  1.00 71.46  ? 192 ARG A CD  1 
ATOM 1308 N NE  . ARG A 1 192 ? 6.456  -11.335 -1.455  1.00 78.93  ? 192 ARG A NE  1 
ATOM 1309 C CZ  . ARG A 1 192 ? 6.221  -10.527 -0.428  1.00 73.89  ? 192 ARG A CZ  1 
ATOM 1310 N NH1 . ARG A 1 192 ? 6.824  -10.721 0.731   1.00 68.58  ? 192 ARG A NH1 1 
ATOM 1311 N NH2 . ARG A 1 192 ? 5.385  -9.518  -0.568  1.00 77.63  ? 192 ARG A NH2 1 
ATOM 1312 N N   . PRO A 1 193 ? 11.485 -15.559 0.242   1.00 58.12  ? 193 PRO A N   1 
ATOM 1313 C CA  . PRO A 1 193 ? 11.935 -16.910 0.529   1.00 60.68  ? 193 PRO A CA  1 
ATOM 1314 C C   . PRO A 1 193 ? 11.159 -17.909 -0.337  1.00 70.01  ? 193 PRO A C   1 
ATOM 1315 O O   . PRO A 1 193 ? 9.957  -17.791 -0.429  1.00 69.49  ? 193 PRO A O   1 
ATOM 1316 C CB  . PRO A 1 193 ? 11.623 -17.093 2.017   1.00 58.64  ? 193 PRO A CB  1 
ATOM 1317 C CG  . PRO A 1 193 ? 10.644 -15.996 2.354   1.00 58.21  ? 193 PRO A CG  1 
ATOM 1318 C CD  . PRO A 1 193 ? 10.994 -14.860 1.424   1.00 52.97  ? 193 PRO A CD  1 
ATOM 1319 N N   . LYS A 1 194 ? 11.868 -18.854 -0.955  1.00 69.49  ? 194 LYS A N   1 
ATOM 1320 C CA  . LYS A 1 194 ? 11.211 -19.846 -1.843  1.00 67.94  ? 194 LYS A CA  1 
ATOM 1321 C C   . LYS A 1 194 ? 10.584 -20.931 -0.978  1.00 70.16  ? 194 LYS A C   1 
ATOM 1322 O O   . LYS A 1 194 ? 11.247 -21.945 -0.727  1.00 79.86  ? 194 LYS A O   1 
ATOM 1323 C CB  . LYS A 1 194 ? 12.208 -20.446 -2.835  1.00 74.20  ? 194 LYS A CB  1 
ATOM 1324 C CG  . LYS A 1 194 ? 12.357 -19.686 -4.145  1.00 77.54  ? 194 LYS A CG  1 
ATOM 1325 C CD  . LYS A 1 194 ? 13.627 -20.028 -4.893  1.00 78.71  ? 194 LYS A CD  1 
ATOM 1326 C CE  . LYS A 1 194 ? 14.336 -18.814 -5.454  1.00 76.75  ? 194 LYS A CE  1 
ATOM 1327 N NZ  . LYS A 1 194 ? 15.096 -19.144 -6.682  1.00 68.97  ? 194 LYS A NZ  1 
ATOM 1328 N N   . TYR A 1 195 ? 9.352  -20.709 -0.550  1.00 64.81  ? 195 TYR A N   1 
ATOM 1329 C CA  . TYR A 1 195 ? 8.648  -21.656 0.299   1.00 68.82  ? 195 TYR A CA  1 
ATOM 1330 C C   . TYR A 1 195 ? 8.165  -22.853 -0.517  1.00 84.12  ? 195 TYR A C   1 
ATOM 1331 O O   . TYR A 1 195 ? 8.037  -22.797 -1.744  1.00 89.97  ? 195 TYR A O   1 
ATOM 1332 C CB  . TYR A 1 195 ? 7.464  -20.980 0.989   1.00 68.38  ? 195 TYR A CB  1 
ATOM 1333 C CG  . TYR A 1 195 ? 7.858  -19.986 2.057   1.00 72.38  ? 195 TYR A CG  1 
ATOM 1334 C CD1 . TYR A 1 195 ? 8.675  -20.363 3.116   1.00 69.60  ? 195 TYR A CD1 1 
ATOM 1335 C CD2 . TYR A 1 195 ? 7.411  -18.673 2.010   1.00 69.62  ? 195 TYR A CD2 1 
ATOM 1336 C CE1 . TYR A 1 195 ? 9.036  -19.458 4.096   1.00 65.03  ? 195 TYR A CE1 1 
ATOM 1337 C CE2 . TYR A 1 195 ? 7.766  -17.762 2.986   1.00 66.95  ? 195 TYR A CE2 1 
ATOM 1338 C CZ  . TYR A 1 195 ? 8.578  -18.160 4.027   1.00 69.19  ? 195 TYR A CZ  1 
ATOM 1339 O OH  . TYR A 1 195 ? 8.935  -17.257 5.001   1.00 73.28  ? 195 TYR A OH  1 
ATOM 1340 N N   . ASP A 1 196 ? 7.888  -23.950 0.187   1.00 88.32  ? 196 ASP A N   1 
ATOM 1341 C CA  . ASP A 1 196 ? 7.419  -25.168 -0.461  1.00 89.58  ? 196 ASP A CA  1 
ATOM 1342 C C   . ASP A 1 196 ? 5.913  -25.164 -0.669  1.00 87.32  ? 196 ASP A C   1 
ATOM 1343 O O   . ASP A 1 196 ? 5.422  -25.786 -1.618  1.00 94.02  ? 196 ASP A O   1 
ATOM 1344 C CB  . ASP A 1 196 ? 7.828  -26.394 0.361   1.00 91.78  ? 196 ASP A CB  1 
ATOM 1345 C CG  . ASP A 1 196 ? 9.333  -26.573 0.427   1.00 93.69  ? 196 ASP A CG  1 
ATOM 1346 O OD1 . ASP A 1 196 ? 10.018 -26.219 -0.557  1.00 93.62  ? 196 ASP A OD1 1 
ATOM 1347 O OD2 . ASP A 1 196 ? 9.830  -27.066 1.461   1.00 88.73  ? 196 ASP A OD2 1 
ATOM 1348 N N   . SER A 1 197 ? 5.174  -24.477 0.199   1.00 84.95  ? 197 SER A N   1 
ATOM 1349 C CA  . SER A 1 197 ? 3.766  -24.191 0.014   1.00 81.00  ? 197 SER A CA  1 
ATOM 1350 C C   . SER A 1 197 ? 3.547  -22.686 0.084   1.00 85.64  ? 197 SER A C   1 
ATOM 1351 O O   . SER A 1 197 ? 4.202  -22.009 0.885   1.00 88.91  ? 197 SER A O   1 
ATOM 1352 C CB  . SER A 1 197 ? 2.909  -24.885 1.082   1.00 83.08  ? 197 SER A CB  1 
ATOM 1353 O OG  . SER A 1 197 ? 3.076  -26.291 1.039   1.00 97.44  ? 197 SER A OG  1 
ATOM 1354 N N   . PRO A 1 198 ? 2.677  -22.133 -0.761  1.00 83.51  ? 198 PRO A N   1 
ATOM 1355 C CA  . PRO A 1 198 ? 2.461  -20.680 -0.769  1.00 90.95  ? 198 PRO A CA  1 
ATOM 1356 C C   . PRO A 1 198 ? 2.249  -20.125 0.633   1.00 87.73  ? 198 PRO A C   1 
ATOM 1357 O O   . PRO A 1 198 ? 1.440  -20.640 1.409   1.00 85.42  ? 198 PRO A O   1 
ATOM 1358 C CB  . PRO A 1 198 ? 1.210  -20.522 -1.636  1.00 81.17  ? 198 PRO A CB  1 
ATOM 1359 C CG  . PRO A 1 198 ? 1.289  -21.666 -2.589  1.00 73.60  ? 198 PRO A CG  1 
ATOM 1360 C CD  . PRO A 1 198 ? 1.902  -22.811 -1.815  1.00 72.08  ? 198 PRO A CD  1 
ATOM 1361 N N   . GLU A 1 199 ? 2.990  -19.075 0.957   1.00 80.48  ? 199 GLU A N   1 
ATOM 1362 C CA  . GLU A 1 199 ? 2.911  -18.494 2.291   1.00 85.34  ? 199 GLU A CA  1 
ATOM 1363 C C   . GLU A 1 199 ? 1.560  -17.816 2.468   1.00 82.36  ? 199 GLU A C   1 
ATOM 1364 O O   . GLU A 1 199 ? 1.216  -16.927 1.677   1.00 82.50  ? 199 GLU A O   1 
ATOM 1365 C CB  . GLU A 1 199 ? 4.045  -17.498 2.518   1.00 83.57  ? 199 GLU A CB  1 
ATOM 1366 C CG  . GLU A 1 199 ? 3.763  -16.480 3.618   1.00 77.09  ? 199 GLU A CG  1 
ATOM 1367 C CD  . GLU A 1 199 ? 3.806  -17.091 5.008   1.00 78.26  ? 199 GLU A CD  1 
ATOM 1368 O OE1 . GLU A 1 199 ? 4.836  -17.704 5.360   1.00 76.11  ? 199 GLU A OE1 1 
ATOM 1369 O OE2 . GLU A 1 199 ? 2.810  -16.955 5.751   1.00 70.82  ? 199 GLU A OE2 1 
ATOM 1370 N N   . PRO A 1 200 ? 0.764  -18.204 3.466   1.00 79.83  ? 200 PRO A N   1 
ATOM 1371 C CA  . PRO A 1 200 ? -0.568 -17.597 3.624   1.00 86.21  ? 200 PRO A CA  1 
ATOM 1372 C C   . PRO A 1 200 ? -0.530 -16.101 3.877   1.00 85.67  ? 200 PRO A C   1 
ATOM 1373 O O   . PRO A 1 200 ? -1.521 -15.416 3.595   1.00 86.29  ? 200 PRO A O   1 
ATOM 1374 C CB  . PRO A 1 200 ? -1.158 -18.355 4.822   1.00 80.26  ? 200 PRO A CB  1 
ATOM 1375 C CG  . PRO A 1 200 ? 0.035  -18.911 5.548   1.00 79.71  ? 200 PRO A CG  1 
ATOM 1376 C CD  . PRO A 1 200 ? 1.014  -19.253 4.468   1.00 80.66  ? 200 PRO A CD  1 
ATOM 1377 N N   . PHE A 1 201 ? 0.579  -15.572 4.399   1.00 81.52  ? 201 PHE A N   1 
ATOM 1378 C CA  . PHE A 1 201 ? 0.652  -14.148 4.704   1.00 80.80  ? 201 PHE A CA  1 
ATOM 1379 C C   . PHE A 1 201 ? 0.713  -13.298 3.438   1.00 81.04  ? 201 PHE A C   1 
ATOM 1380 O O   . PHE A 1 201 ? 0.270  -12.144 3.449   1.00 81.58  ? 201 PHE A O   1 
ATOM 1381 C CB  . PHE A 1 201 ? 1.865  -13.879 5.597   1.00 78.13  ? 201 PHE A CB  1 
ATOM 1382 C CG  . PHE A 1 201 ? 1.798  -12.581 6.354   1.00 84.01  ? 201 PHE A CG  1 
ATOM 1383 C CD1 . PHE A 1 201 ? 2.136  -11.387 5.742   1.00 76.16  ? 201 PHE A CD1 1 
ATOM 1384 C CD2 . PHE A 1 201 ? 1.407  -12.558 7.683   1.00 77.34  ? 201 PHE A CD2 1 
ATOM 1385 C CE1 . PHE A 1 201 ? 2.080  -10.194 6.436   1.00 71.02  ? 201 PHE A CE1 1 
ATOM 1386 C CE2 . PHE A 1 201 ? 1.350  -11.367 8.383   1.00 72.20  ? 201 PHE A CE2 1 
ATOM 1387 C CZ  . PHE A 1 201 ? 1.689  -10.184 7.757   1.00 71.28  ? 201 PHE A CZ  1 
ATOM 1388 N N   . TYR A 1 202 ? 1.235  -13.845 2.342   1.00 84.42  ? 202 TYR A N   1 
ATOM 1389 C CA  . TYR A 1 202 ? 1.340  -13.095 1.096   1.00 84.22  ? 202 TYR A CA  1 
ATOM 1390 C C   . TYR A 1 202 ? 0.022  -13.101 0.332   1.00 86.78  ? 202 TYR A C   1 
ATOM 1391 O O   . TYR A 1 202 ? -0.656 -14.128 0.238   1.00 92.35  ? 202 TYR A O   1 
ATOM 1392 C CB  . TYR A 1 202 ? 2.431  -13.678 0.195   1.00 80.42  ? 202 TYR A CB  1 
ATOM 1393 C CG  . TYR A 1 202 ? 3.822  -13.734 0.784   1.00 73.73  ? 202 TYR A CG  1 
ATOM 1394 C CD1 . TYR A 1 202 ? 4.211  -12.879 1.806   1.00 70.92  ? 202 TYR A CD1 1 
ATOM 1395 C CD2 . TYR A 1 202 ? 4.755  -14.639 0.297   1.00 73.91  ? 202 TYR A CD2 1 
ATOM 1396 C CE1 . TYR A 1 202 ? 5.488  -12.938 2.337   1.00 67.12  ? 202 TYR A CE1 1 
ATOM 1397 C CE2 . TYR A 1 202 ? 6.029  -14.705 0.818   1.00 76.46  ? 202 TYR A CE2 1 
ATOM 1398 C CZ  . TYR A 1 202 ? 6.395  -13.850 1.834   1.00 73.72  ? 202 TYR A CZ  1 
ATOM 1399 O OH  . TYR A 1 202 ? 7.671  -13.918 2.348   1.00 66.13  ? 202 TYR A OH  1 
ATOM 1400 N N   . LYS A 1 203 ? -0.333 -11.945 -0.222  1.00 81.95  ? 203 LYS A N   1 
ATOM 1401 C CA  . LYS A 1 203 ? -1.312 -11.901 -1.294  1.00 84.48  ? 203 LYS A CA  1 
ATOM 1402 C C   . LYS A 1 203 ? -0.621 -12.167 -2.631  1.00 92.20  ? 203 LYS A C   1 
ATOM 1403 O O   . LYS A 1 203 ? 0.591  -11.984 -2.776  1.00 91.76  ? 203 LYS A O   1 
ATOM 1404 C CB  . LYS A 1 203 ? -2.029 -10.549 -1.313  1.00 88.10  ? 203 LYS A CB  1 
ATOM 1405 C CG  . LYS A 1 203 ? -3.401 -10.567 -0.651  1.00 84.33  ? 203 LYS A CG  1 
ATOM 1406 C CD  . LYS A 1 203 ? -3.388 -9.909  0.721   1.00 81.36  ? 203 LYS A CD  1 
ATOM 1407 C CE  . LYS A 1 203 ? -4.581 -10.363 1.554   1.00 82.80  ? 203 LYS A CE  1 
ATOM 1408 N NZ  . LYS A 1 203 ? -4.664 -9.665  2.869   1.00 79.47  ? 203 LYS A NZ  1 
ATOM 1409 N N   . TYR A 1 204 ? -1.361 -12.697 -3.598  1.00 97.47  ? 204 TYR A N   1 
ATOM 1410 C CA  . TYR A 1 204 ? -0.686 -13.073 -4.865  1.00 88.04  ? 204 TYR A CA  1 
ATOM 1411 C C   . TYR A 1 204 ? -1.464 -12.538 -6.067  1.00 90.88  ? 204 TYR A C   1 
ATOM 1412 O O   . TYR A 1 204 ? -2.609 -12.091 -5.897  1.00 94.01  ? 204 TYR A O   1 
ATOM 1413 C CB  . TYR A 1 204 ? -0.530 -14.592 -4.950  1.00 81.54  ? 204 TYR A CB  1 
ATOM 1414 C CG  . TYR A 1 204 ? 0.358  -15.241 -3.917  1.00 78.37  ? 204 TYR A CG  1 
ATOM 1415 C CD1 . TYR A 1 204 ? -0.082 -15.459 -2.623  1.00 77.66  ? 204 TYR A CD1 1 
ATOM 1416 C CD2 . TYR A 1 204 ? 1.626  -15.686 -4.250  1.00 81.50  ? 204 TYR A CD2 1 
ATOM 1417 C CE1 . TYR A 1 204 ? 0.723  -16.080 -1.682  1.00 81.07  ? 204 TYR A CE1 1 
ATOM 1418 C CE2 . TYR A 1 204 ? 2.444  -16.307 -3.321  1.00 77.58  ? 204 TYR A CE2 1 
ATOM 1419 C CZ  . TYR A 1 204 ? 1.992  -16.505 -2.031  1.00 80.48  ? 204 TYR A CZ  1 
ATOM 1420 O OH  . TYR A 1 204 ? 2.797  -17.117 -1.113  1.00 76.39  ? 204 TYR A OH  1 
ATOM 1421 N N   . GLY A 1 205 ? -0.844 -12.579 -7.243  1.00 84.04  ? 205 GLY A N   1 
ATOM 1422 C CA  . GLY A 1 205 ? -1.505 -12.126 -8.478  1.00 82.87  ? 205 GLY A CA  1 
ATOM 1423 C C   . GLY A 1 205 ? -2.401 -10.920 -8.292  1.00 97.54  ? 205 GLY A C   1 
ATOM 1424 O O   . GLY A 1 205 ? -1.962 -9.951  -7.648  1.00 94.77  ? 205 GLY A O   1 
ATOM 1425 N N   . GLU A 1 206 ? -3.615 -10.975 -8.845  1.00 99.74  ? 206 GLU A N   1 
ATOM 1426 C CA  . GLU A 1 206 ? -4.549 -9.820  -8.804  1.00 101.98 ? 206 GLU A CA  1 
ATOM 1427 C C   . GLU A 1 206 ? -4.788 -9.359  -7.368  1.00 99.88  ? 206 GLU A C   1 
ATOM 1428 O O   . GLU A 1 206 ? -5.255 -8.220  -7.189  1.00 97.46  ? 206 GLU A O   1 
ATOM 1429 C CB  . GLU A 1 206 ? -5.873 -10.219 -9.453  1.00 103.84 ? 206 GLU A CB  1 
ATOM 1430 C CG  . GLU A 1 206 ? -6.858 -10.843 -8.482  1.00 107.76 ? 206 GLU A CG  1 
ATOM 1431 C CD  . GLU A 1 206 ? -7.032 -12.345 -8.620  1.00 108.47 ? 206 GLU A CD  1 
ATOM 1432 O OE1 . GLU A 1 206 ? -8.080 -12.772 -9.144  1.00 119.39 ? 206 GLU A OE1 1 
ATOM 1433 O OE2 . GLU A 1 206 ? -6.121 -13.083 -8.199  1.00 103.50 ? 206 GLU A OE2 1 
ATOM 1434 N N   . ASP A 1 207 ? -4.501 -10.219 -6.393  1.00 99.77  ? 207 ASP A N   1 
ATOM 1435 C CA  . ASP A 1 207 ? -4.764 -9.864  -4.978  1.00 99.89  ? 207 ASP A CA  1 
ATOM 1436 C C   . ASP A 1 207 ? -3.626 -8.972  -4.480  1.00 103.02 ? 207 ASP A C   1 
ATOM 1437 O O   . ASP A 1 207 ? -3.642 -8.615  -3.290  1.00 101.69 ? 207 ASP A O   1 
ATOM 1438 C CB  . ASP A 1 207 ? -4.953 -11.125 -4.134  1.00 93.90  ? 207 ASP A CB  1 
ATOM 1439 C CG  . ASP A 1 207 ? -5.569 -12.276 -4.910  1.00 101.38 ? 207 ASP A CG  1 
ATOM 1440 O OD1 . ASP A 1 207 ? -6.679 -12.093 -5.444  1.00 97.59  ? 207 ASP A OD1 1 
ATOM 1441 O OD2 . ASP A 1 207 ? -4.934 -13.346 -4.972  1.00 103.03 ? 207 ASP A OD2 1 
ATOM 1442 N N   . GLN A 1 208 ? -2.701 -8.595  -5.366  1.00 99.94  ? 208 GLN A N   1 
ATOM 1443 C CA  . GLN A 1 208 ? -1.517 -7.818  -4.921  1.00 95.09  ? 208 GLN A CA  1 
ATOM 1444 C C   . GLN A 1 208 ? -1.397 -6.495  -5.681  1.00 92.83  ? 208 GLN A C   1 
ATOM 1445 O O   . GLN A 1 208 ? -1.331 -6.538  -6.919  1.00 93.06  ? 208 GLN A O   1 
ATOM 1446 C CB  . GLN A 1 208 ? -0.257 -8.657  -5.123  1.00 88.12  ? 208 GLN A CB  1 
ATOM 1447 C CG  . GLN A 1 208 ? 0.491  -8.937  -3.834  1.00 87.62  ? 208 GLN A CG  1 
ATOM 1448 C CD  . GLN A 1 208 ? 1.858  -9.512  -4.105  1.00 90.95  ? 208 GLN A CD  1 
ATOM 1449 O OE1 . GLN A 1 208 ? 2.325  -9.554  -5.240  1.00 89.62  ? 208 GLN A OE1 1 
ATOM 1450 N NE2 . GLN A 1 208 ? 2.511  -9.970  -3.053  1.00 87.26  ? 208 GLN A NE2 1 
ATOM 1451 N N   . ASP A 1 209 ? -1.356 -5.369  -4.961  1.00 93.92  ? 209 ASP A N   1 
ATOM 1452 C CA  . ASP A 1 209 ? -1.140 -4.044  -5.598  1.00 88.95  ? 209 ASP A CA  1 
ATOM 1453 C C   . ASP A 1 209 ? 0.126  -3.429  -5.005  1.00 85.02  ? 209 ASP A C   1 
ATOM 1454 O O   . ASP A 1 209 ? 0.038  -2.813  -3.932  1.00 80.32  ? 209 ASP A O   1 
ATOM 1455 C CB  . ASP A 1 209 ? -2.330 -3.107  -5.396  1.00 93.27  ? 209 ASP A CB  1 
ATOM 1456 C CG  . ASP A 1 209 ? -2.066 -1.685  -5.860  1.00 93.39  ? 209 ASP A CG  1 
ATOM 1457 O OD1 . ASP A 1 209 ? -1.517 -1.524  -6.965  1.00 97.07  ? 209 ASP A OD1 1 
ATOM 1458 O OD2 . ASP A 1 209 ? -2.408 -0.752  -5.110  1.00 82.90  ? 209 ASP A OD2 1 
ATOM 1459 N N   . LEU A 1 210 ? 1.271  -3.563  -5.670  1.00 84.72  ? 210 LEU A N   1 
ATOM 1460 C CA  . LEU A 1 210 ? 2.544  -3.065  -5.077  1.00 82.67  ? 210 LEU A CA  1 
ATOM 1461 C C   . LEU A 1 210 ? 2.342  -1.667  -4.496  1.00 81.72  ? 210 LEU A C   1 
ATOM 1462 O O   . LEU A 1 210 ? 3.018  -1.338  -3.516  1.00 80.07  ? 210 LEU A O   1 
ATOM 1463 C CB  . LEU A 1 210 ? 3.636  -3.035  -6.147  1.00 74.79  ? 210 LEU A CB  1 
ATOM 1464 C CG  . LEU A 1 210 ? 5.051  -2.809  -5.622  1.00 81.04  ? 210 LEU A CG  1 
ATOM 1465 C CD1 . LEU A 1 210 ? 5.479  -3.963  -4.732  1.00 82.60  ? 210 LEU A CD1 1 
ATOM 1466 C CD2 . LEU A 1 210 ? 6.035  -2.624  -6.767  1.00 81.16  ? 210 LEU A CD2 1 
ATOM 1467 N N   . GLN A 1 211 ? 1.462  -0.869  -5.094  1.00 84.32  ? 211 GLN A N   1 
ATOM 1468 C CA  . GLN A 1 211 ? 1.328  0.506   -4.618  1.00 85.07  ? 211 GLN A CA  1 
ATOM 1469 C C   . GLN A 1 211 ? 1.012  0.568   -3.129  1.00 87.36  ? 211 GLN A C   1 
ATOM 1470 O O   . GLN A 1 211 ? 1.333  1.564   -2.470  1.00 93.31  ? 211 GLN A O   1 
ATOM 1471 C CB  . GLN A 1 211 ? 0.258  1.239   -5.425  1.00 87.25  ? 211 GLN A CB  1 
ATOM 1472 C CG  . GLN A 1 211 ? 0.634  1.438   -6.885  1.00 97.76  ? 211 GLN A CG  1 
ATOM 1473 C CD  . GLN A 1 211 ? 1.975  2.131   -7.049  1.00 88.96  ? 211 GLN A CD  1 
ATOM 1474 O OE1 . GLN A 1 211 ? 2.181  3.237   -6.549  1.00 84.13  ? 211 GLN A OE1 1 
ATOM 1475 N NE2 . GLN A 1 211 ? 2.898  1.477   -7.747  1.00 90.10  ? 211 GLN A NE2 1 
ATOM 1476 N N   . ILE A 1 212 ? 0.379  -0.473  -2.581  1.00 84.31  ? 212 ILE A N   1 
ATOM 1477 C CA  . ILE A 1 212 ? 0.180  -0.533  -1.136  1.00 82.11  ? 212 ILE A CA  1 
ATOM 1478 C C   . ILE A 1 212 ? 1.528  -0.594  -0.433  1.00 81.63  ? 212 ILE A C   1 
ATOM 1479 O O   . ILE A 1 212 ? 1.748  0.062   0.593   1.00 82.08  ? 212 ILE A O   1 
ATOM 1480 C CB  . ILE A 1 212 ? -0.705 -1.738  -0.764  1.00 94.32  ? 212 ILE A CB  1 
ATOM 1481 C CG1 . ILE A 1 212 ? -2.036 -1.688  -1.521  1.00 92.48  ? 212 ILE A CG1 1 
ATOM 1482 C CG2 . ILE A 1 212 ? -0.930 -1.784  0.744   1.00 95.50  ? 212 ILE A CG2 1 
ATOM 1483 C CD1 . ILE A 1 212 ? -3.175 -2.412  -0.825  1.00 87.58  ? 212 ILE A CD1 1 
ATOM 1484 N N   . TYR A 1 213 ? 2.453  -1.382  -0.983  1.00 83.51  ? 213 TYR A N   1 
ATOM 1485 C CA  . TYR A 1 213 ? 3.796  -1.487  -0.426  1.00 79.53  ? 213 TYR A CA  1 
ATOM 1486 C C   . TYR A 1 213 ? 4.605  -0.223  -0.696  1.00 80.23  ? 213 TYR A C   1 
ATOM 1487 O O   . TYR A 1 213 ? 5.262  0.309   0.206   1.00 76.52  ? 213 TYR A O   1 
ATOM 1488 C CB  . TYR A 1 213 ? 4.491  -2.719  -1.009  1.00 82.30  ? 213 TYR A CB  1 
ATOM 1489 C CG  . TYR A 1 213 ? 5.948  -2.870  -0.638  1.00 77.94  ? 213 TYR A CG  1 
ATOM 1490 C CD1 . TYR A 1 213 ? 6.372  -2.733  0.677   1.00 72.64  ? 213 TYR A CD1 1 
ATOM 1491 C CD2 . TYR A 1 213 ? 6.899  -3.160  -1.608  1.00 75.42  ? 213 TYR A CD2 1 
ATOM 1492 C CE1 . TYR A 1 213 ? 7.704  -2.876  1.014   1.00 68.49  ? 213 TYR A CE1 1 
ATOM 1493 C CE2 . TYR A 1 213 ? 8.231  -3.304  -1.281  1.00 73.20  ? 213 TYR A CE2 1 
ATOM 1494 C CZ  . TYR A 1 213 ? 8.629  -3.162  0.031   1.00 71.06  ? 213 TYR A CZ  1 
ATOM 1495 O OH  . TYR A 1 213 ? 9.958  -3.303  0.362   1.00 70.71  ? 213 TYR A OH  1 
ATOM 1496 N N   . VAL A 1 214 ? 4.583  0.256   -1.946  1.00 84.09  ? 214 VAL A N   1 
ATOM 1497 C CA  . VAL A 1 214 ? 5.305  1.476   -2.316  1.00 75.73  ? 214 VAL A CA  1 
ATOM 1498 C C   . VAL A 1 214 ? 4.966  2.615   -1.361  1.00 75.00  ? 214 VAL A C   1 
ATOM 1499 O O   . VAL A 1 214 ? 5.854  3.280   -0.815  1.00 80.85  ? 214 VAL A O   1 
ATOM 1500 C CB  . VAL A 1 214 ? 4.997  1.856   -3.776  1.00 77.99  ? 214 VAL A CB  1 
ATOM 1501 C CG1 . VAL A 1 214 ? 5.529  3.248   -4.088  1.00 69.98  ? 214 VAL A CG1 1 
ATOM 1502 C CG2 . VAL A 1 214 ? 5.584  0.826   -4.729  1.00 77.22  ? 214 VAL A CG2 1 
ATOM 1503 N N   . GLU A 1 215 ? 3.671  2.854   -1.146  1.00 74.25  ? 215 GLU A N   1 
ATOM 1504 C CA  . GLU A 1 215 ? 3.260  3.915   -0.234  1.00 71.32  ? 215 GLU A CA  1 
ATOM 1505 C C   . GLU A 1 215 ? 3.661  3.599   1.202   1.00 74.06  ? 215 GLU A C   1 
ATOM 1506 O O   . GLU A 1 215 ? 3.971  4.513   1.975   1.00 71.52  ? 215 GLU A O   1 
ATOM 1507 C CB  . GLU A 1 215 ? 1.751  4.137   -0.344  1.00 76.18  ? 215 GLU A CB  1 
ATOM 1508 C CG  . GLU A 1 215 ? 1.084  4.661   0.915   1.00 81.97  ? 215 GLU A CG  1 
ATOM 1509 C CD  . GLU A 1 215 ? -0.353 4.200   1.044   1.00 96.85  ? 215 GLU A CD  1 
ATOM 1510 O OE1 . GLU A 1 215 ? -0.769 3.327   0.253   1.00 96.49  ? 215 GLU A OE1 1 
ATOM 1511 O OE2 . GLU A 1 215 ? -1.066 4.710   1.934   1.00 99.40  ? 215 GLU A OE2 1 
ATOM 1512 N N   . PHE A 1 216 ? 3.682  2.314   1.567   1.00 80.54  ? 216 PHE A N   1 
ATOM 1513 C CA  . PHE A 1 216 ? 4.042  1.931   2.929   1.00 75.85  ? 216 PHE A CA  1 
ATOM 1514 C C   . PHE A 1 216 ? 5.473  2.337   3.255   1.00 68.20  ? 216 PHE A C   1 
ATOM 1515 O O   . PHE A 1 216 ? 5.755  2.824   4.356   1.00 66.68  ? 216 PHE A O   1 
ATOM 1516 C CB  . PHE A 1 216 ? 3.852  0.425   3.112   1.00 73.00  ? 216 PHE A CB  1 
ATOM 1517 C CG  . PHE A 1 216 ? 4.687  -0.163  4.211   1.00 67.10  ? 216 PHE A CG  1 
ATOM 1518 C CD1 . PHE A 1 216 ? 4.433  0.150   5.536   1.00 62.33  ? 216 PHE A CD1 1 
ATOM 1519 C CD2 . PHE A 1 216 ? 5.727  -1.030  3.919   1.00 63.20  ? 216 PHE A CD2 1 
ATOM 1520 C CE1 . PHE A 1 216 ? 5.201  -0.391  6.548   1.00 62.73  ? 216 PHE A CE1 1 
ATOM 1521 C CE2 . PHE A 1 216 ? 6.498  -1.574  4.927   1.00 57.93  ? 216 PHE A CE2 1 
ATOM 1522 C CZ  . PHE A 1 216 ? 6.234  -1.254  6.243   1.00 54.10  ? 216 PHE A CZ  1 
ATOM 1523 N N   . MET A 1 217 ? 6.393  2.135   2.311   1.00 62.34  ? 217 MET A N   1 
ATOM 1524 C CA  . MET A 1 217 ? 7.763  2.599   2.499   1.00 63.55  ? 217 MET A CA  1 
ATOM 1525 C C   . MET A 1 217 ? 7.814  4.118   2.599   1.00 66.94  ? 217 MET A C   1 
ATOM 1526 O O   . MET A 1 217 ? 8.393  4.671   3.541   1.00 68.22  ? 217 MET A O   1 
ATOM 1527 C CB  . MET A 1 217 ? 8.636  2.095   1.355   1.00 69.22  ? 217 MET A CB  1 
ATOM 1528 C CG  . MET A 1 217 ? 8.403  0.637   1.017   1.00 64.89  ? 217 MET A CG  1 
ATOM 1529 S SD  . MET A 1 217 ? 9.740  0.007   -0.002  1.00 70.67  ? 217 MET A SD  1 
ATOM 1530 C CE  . MET A 1 217 ? 9.720  1.250   -1.288  1.00 63.35  ? 217 MET A CE  1 
ATOM 1531 N N   . LYS A 1 218 ? 7.228  4.810   1.615   1.00 72.50  ? 218 LYS A N   1 
ATOM 1532 C CA  . LYS A 1 218 ? 7.211  6.270   1.627   1.00 64.56  ? 218 LYS A CA  1 
ATOM 1533 C C   . LYS A 1 218 ? 6.587  6.819   2.904   1.00 61.52  ? 218 LYS A C   1 
ATOM 1534 O O   . LYS A 1 218 ? 6.992  7.884   3.386   1.00 69.56  ? 218 LYS A O   1 
ATOM 1535 C CB  . LYS A 1 218 ? 6.457  6.787   0.401   1.00 62.30  ? 218 LYS A CB  1 
ATOM 1536 C CG  . LYS A 1 218 ? 6.333  8.299   0.328   1.00 66.53  ? 218 LYS A CG  1 
ATOM 1537 C CD  . LYS A 1 218 ? 5.566  8.726   -0.911  1.00 64.18  ? 218 LYS A CD  1 
ATOM 1538 C CE  . LYS A 1 218 ? 5.024  10.137  -0.764  1.00 72.34  ? 218 LYS A CE  1 
ATOM 1539 N NZ  . LYS A 1 218 ? 4.269  10.566  -1.972  1.00 79.81  ? 218 LYS A NZ  1 
ATOM 1540 N N   . ASN A 1 219 ? 5.619  6.102   3.479   1.00 60.90  ? 219 ASN A N   1 
ATOM 1541 C CA  . ASN A 1 219 ? 5.053  6.517   4.758   1.00 71.27  ? 219 ASN A CA  1 
ATOM 1542 C C   . ASN A 1 219 ? 6.055  6.332   5.890   1.00 70.84  ? 219 ASN A C   1 
ATOM 1543 O O   . ASN A 1 219 ? 6.182  7.199   6.764   1.00 59.93  ? 219 ASN A O   1 
ATOM 1544 C CB  . ASN A 1 219 ? 3.778  5.723   5.045   1.00 77.16  ? 219 ASN A CB  1 
ATOM 1545 C CG  . ASN A 1 219 ? 2.587  6.218   4.252   1.00 82.39  ? 219 ASN A CG  1 
ATOM 1546 O OD1 . ASN A 1 219 ? 2.579  7.343   3.751   1.00 74.80  ? 219 ASN A OD1 1 
ATOM 1547 N ND2 . ASN A 1 219 ? 1.564  5.376   4.138   1.00 82.03  ? 219 ASN A ND2 1 
ATOM 1548 N N   . GLN A 1 220 ? 6.775  5.208   5.888   1.00 69.82  ? 220 GLN A N   1 
ATOM 1549 C CA  . GLN A 1 220 ? 7.739  4.932   6.948   1.00 66.78  ? 220 GLN A CA  1 
ATOM 1550 C C   . GLN A 1 220 ? 8.949  5.854   6.856   1.00 61.71  ? 220 GLN A C   1 
ATOM 1551 O O   . GLN A 1 220 ? 9.441  6.346   7.878   1.00 55.80  ? 220 GLN A O   1 
ATOM 1552 C CB  . GLN A 1 220 ? 8.171  3.469   6.883   1.00 63.41  ? 220 GLN A CB  1 
ATOM 1553 C CG  . GLN A 1 220 ? 7.173  2.503   7.489   1.00 60.49  ? 220 GLN A CG  1 
ATOM 1554 C CD  . GLN A 1 220 ? 7.827  1.231   7.983   1.00 55.46  ? 220 GLN A CD  1 
ATOM 1555 O OE1 . GLN A 1 220 ? 8.635  0.623   7.282   1.00 53.22  ? 220 GLN A OE1 1 
ATOM 1556 N NE2 . GLN A 1 220 ? 7.481  0.820   9.197   1.00 55.30  ? 220 GLN A NE2 1 
ATOM 1557 N N   . ILE A 1 221 ? 9.447  6.090   5.639   1.00 59.99  ? 221 ILE A N   1 
ATOM 1558 C CA  . ILE A 1 221 ? 10.589 6.981   5.455   1.00 60.09  ? 221 ILE A CA  1 
ATOM 1559 C C   . ILE A 1 221 ? 10.248 8.394   5.906   1.00 58.95  ? 221 ILE A C   1 
ATOM 1560 O O   . ILE A 1 221 ? 11.102 9.106   6.450   1.00 54.81  ? 221 ILE A O   1 
ATOM 1561 C CB  . ILE A 1 221 ? 11.049 6.941   3.983   1.00 58.88  ? 221 ILE A CB  1 
ATOM 1562 C CG1 . ILE A 1 221 ? 11.915 5.705   3.730   1.00 62.84  ? 221 ILE A CG1 1 
ATOM 1563 C CG2 . ILE A 1 221 ? 11.812 8.201   3.607   1.00 53.15  ? 221 ILE A CG2 1 
ATOM 1564 C CD1 . ILE A 1 221 ? 12.135 5.404   2.263   1.00 65.79  ? 221 ILE A CD1 1 
ATOM 1565 N N   . THR A 1 222 ? 8.992  8.812   5.720   1.00 59.86  ? 222 THR A N   1 
ATOM 1566 C CA  . THR A 1 222 ? 8.556  10.109  6.229   1.00 59.46  ? 222 THR A CA  1 
ATOM 1567 C C   . THR A 1 222 ? 8.694  10.183  7.745   1.00 57.40  ? 222 THR A C   1 
ATOM 1568 O O   . THR A 1 222 ? 9.042  11.235  8.294   1.00 54.57  ? 222 THR A O   1 
ATOM 1569 C CB  . THR A 1 222 ? 7.111  10.382  5.810   1.00 61.11  ? 222 THR A CB  1 
ATOM 1570 O OG1 . THR A 1 222 ? 6.945  10.068  4.421   1.00 67.58  ? 222 THR A OG1 1 
ATOM 1571 C CG2 . THR A 1 222 ? 6.755  11.842  6.039   1.00 48.96  ? 222 THR A CG2 1 
ATOM 1572 N N   . GLU A 1 223 ? 8.431  9.073   8.436   1.00 58.75  ? 223 GLU A N   1 
ATOM 1573 C CA  . GLU A 1 223 ? 8.583  9.052   9.887   1.00 55.91  ? 223 GLU A CA  1 
ATOM 1574 C C   . GLU A 1 223 ? 10.044 9.210   10.287  1.00 53.50  ? 223 GLU A C   1 
ATOM 1575 O O   . GLU A 1 223 ? 10.359 9.939   11.235  1.00 53.36  ? 223 GLU A O   1 
ATOM 1576 C CB  . GLU A 1 223 ? 8.002  7.758   10.456  1.00 58.71  ? 223 GLU A CB  1 
ATOM 1577 C CG  . GLU A 1 223 ? 6.528  7.553   10.138  1.00 64.83  ? 223 GLU A CG  1 
ATOM 1578 C CD  . GLU A 1 223 ? 5.940  6.343   10.840  1.00 73.66  ? 223 GLU A CD  1 
ATOM 1579 O OE1 . GLU A 1 223 ? 6.313  5.205   10.482  1.00 76.61  ? 223 GLU A OE1 1 
ATOM 1580 O OE2 . GLU A 1 223 ? 5.104  6.529   11.748  1.00 71.55  ? 223 GLU A OE2 1 
ATOM 1581 N N   . LEU A 1 224 ? 10.948 8.529   9.577   1.00 52.19  ? 224 LEU A N   1 
ATOM 1582 C CA  . LEU A 1 224 ? 12.361 8.556   9.942   1.00 48.74  ? 224 LEU A CA  1 
ATOM 1583 C C   . LEU A 1 224 ? 12.953 9.949   9.775   1.00 48.11  ? 224 LEU A C   1 
ATOM 1584 O O   . LEU A 1 224 ? 13.780 10.381  10.587  1.00 42.13  ? 224 LEU A O   1 
ATOM 1585 C CB  . LEU A 1 224 ? 13.133 7.547   9.093   1.00 56.55  ? 224 LEU A CB  1 
ATOM 1586 C CG  . LEU A 1 224 ? 12.795 6.072   9.298   1.00 49.47  ? 224 LEU A CG  1 
ATOM 1587 C CD1 . LEU A 1 224 ? 13.481 5.223   8.240   1.00 44.22  ? 224 LEU A CD1 1 
ATOM 1588 C CD2 . LEU A 1 224 ? 13.197 5.628   10.693  1.00 45.15  ? 224 LEU A CD2 1 
ATOM 1589 N N   . LEU A 1 225 ? 12.548 10.663  8.727   1.00 52.52  ? 225 LEU A N   1 
ATOM 1590 C CA  . LEU A 1 225 ? 13.097 11.986  8.465   1.00 51.84  ? 225 LEU A CA  1 
ATOM 1591 C C   . LEU A 1 225 ? 12.503 13.060  9.366   1.00 54.52  ? 225 LEU A C   1 
ATOM 1592 O O   . LEU A 1 225 ? 13.079 14.147  9.472   1.00 65.29  ? 225 LEU A O   1 
ATOM 1593 C CB  . LEU A 1 225 ? 12.894 12.346  6.993   1.00 52.85  ? 225 LEU A CB  1 
ATOM 1594 C CG  . LEU A 1 225 ? 13.877 11.600  6.087   1.00 54.06  ? 225 LEU A CG  1 
ATOM 1595 C CD1 . LEU A 1 225 ? 13.603 11.875  4.619   1.00 56.35  ? 225 LEU A CD1 1 
ATOM 1596 C CD2 . LEU A 1 225 ? 15.311 11.964  6.449   1.00 50.14  ? 225 LEU A CD2 1 
ATOM 1597 N N   . THR A 1 226 ? 11.370 12.785  10.010  1.00 55.26  ? 226 THR A N   1 
ATOM 1598 C CA  . THR A 1 226 ? 10.653 13.783  10.797  1.00 57.64  ? 226 THR A CA  1 
ATOM 1599 C C   . THR A 1 226 ? 10.843 13.616  12.299  1.00 56.43  ? 226 THR A C   1 
ATOM 1600 O O   . THR A 1 226 ? 11.001 14.613  13.011  1.00 56.79  ? 226 THR A O   1 
ATOM 1601 C CB  . THR A 1 226 ? 9.156  13.736  10.476  1.00 56.36  ? 226 THR A CB  1 
ATOM 1602 O OG1 . THR A 1 226 ? 8.701  12.378  10.516  1.00 63.12  ? 226 THR A OG1 1 
ATOM 1603 C CG2 . THR A 1 226 ? 8.883  14.323  9.098   1.00 58.10  ? 226 THR A CG2 1 
ATOM 1604 N N   . ASN A 1 227 ? 10.836 12.382  12.797  1.00 52.60  ? 227 ASN A N   1 
ATOM 1605 C CA  . ASN A 1 227 ? 10.790 12.117  14.230  1.00 49.36  ? 227 ASN A CA  1 
ATOM 1606 C C   . ASN A 1 227 ? 12.161 12.010  14.886  1.00 47.64  ? 227 ASN A C   1 
ATOM 1607 O O   . ASN A 1 227 ? 12.229 11.726  16.086  1.00 54.39  ? 227 ASN A O   1 
ATOM 1608 C CB  . ASN A 1 227 ? 10.013 10.823  14.492  1.00 47.03  ? 227 ASN A CB  1 
ATOM 1609 C CG  . ASN A 1 227 ? 8.518  11.002  14.346  1.00 55.32  ? 227 ASN A CG  1 
ATOM 1610 O OD1 . ASN A 1 227 ? 7.995  11.065  13.233  1.00 50.92  ? 227 ASN A OD1 1 
ATOM 1611 N ND2 . ASN A 1 227 ? 7.819  11.083  15.473  1.00 62.91  ? 227 ASN A ND2 1 
ATOM 1612 N N   . TYR A 1 228 ? 13.252 12.219  14.148  1.00 43.56  ? 228 TYR A N   1 
ATOM 1613 C CA  . TYR A 1 228 ? 14.582 12.009  14.711  1.00 43.51  ? 228 TYR A CA  1 
ATOM 1614 C C   . TYR A 1 228 ? 15.528 13.167  14.418  1.00 51.56  ? 228 TYR A C   1 
ATOM 1615 O O   . TYR A 1 228 ? 16.749 12.998  14.499  1.00 57.00  ? 228 TYR A O   1 
ATOM 1616 C CB  . TYR A 1 228 ? 15.164 10.687  14.206  1.00 40.32  ? 228 TYR A CB  1 
ATOM 1617 C CG  . TYR A 1 228 ? 14.229 9.527   14.453  1.00 43.35  ? 228 TYR A CG  1 
ATOM 1618 C CD1 . TYR A 1 228 ? 14.184 8.900   15.690  1.00 43.64  ? 228 TYR A CD1 1 
ATOM 1619 C CD2 . TYR A 1 228 ? 13.364 9.084   13.462  1.00 41.09  ? 228 TYR A CD2 1 
ATOM 1620 C CE1 . TYR A 1 228 ? 13.319 7.850   15.927  1.00 46.02  ? 228 TYR A CE1 1 
ATOM 1621 C CE2 . TYR A 1 228 ? 12.495 8.035   13.690  1.00 44.52  ? 228 TYR A CE2 1 
ATOM 1622 C CZ  . TYR A 1 228 ? 12.477 7.422   14.924  1.00 47.54  ? 228 TYR A CZ  1 
ATOM 1623 O OH  . TYR A 1 228 ? 11.613 6.378   15.157  1.00 49.74  ? 228 TYR A OH  1 
ATOM 1624 N N   . GLY A 1 229 ? 14.995 14.339  14.090  1.00 54.39  ? 229 GLY A N   1 
ATOM 1625 C CA  . GLY A 1 229 ? 15.817 15.494  13.831  1.00 44.19  ? 229 GLY A CA  1 
ATOM 1626 C C   . GLY A 1 229 ? 16.524 15.373  12.499  1.00 52.16  ? 229 GLY A C   1 
ATOM 1627 O O   . GLY A 1 229 ? 16.168 14.543  11.655  1.00 43.94  ? 229 GLY A O   1 
ATOM 1628 N N   . PRO A 1 230 ? 17.545 16.200  12.283  1.00 55.25  ? 230 PRO A N   1 
ATOM 1629 C CA  . PRO A 1 230 ? 18.292 16.130  11.022  1.00 50.97  ? 230 PRO A CA  1 
ATOM 1630 C C   . PRO A 1 230 ? 18.984 14.783  10.876  1.00 52.57  ? 230 PRO A C   1 
ATOM 1631 O O   . PRO A 1 230 ? 19.667 14.312  11.789  1.00 47.96  ? 230 PRO A O   1 
ATOM 1632 C CB  . PRO A 1 230 ? 19.301 17.280  11.140  1.00 41.51  ? 230 PRO A CB  1 
ATOM 1633 C CG  . PRO A 1 230 ? 18.740 18.185  12.191  1.00 43.23  ? 230 PRO A CG  1 
ATOM 1634 C CD  . PRO A 1 230 ? 18.010 17.297  13.147  1.00 53.26  ? 230 PRO A CD  1 
ATOM 1635 N N   . VAL A 1 231 ? 18.800 14.164  9.713   1.00 49.76  ? 231 VAL A N   1 
ATOM 1636 C CA  . VAL A 1 231 ? 19.305 12.826  9.440   1.00 43.39  ? 231 VAL A CA  1 
ATOM 1637 C C   . VAL A 1 231 ? 20.300 12.915  8.290   1.00 41.04  ? 231 VAL A C   1 
ATOM 1638 O O   . VAL A 1 231 ? 20.153 13.735  7.378   1.00 42.21  ? 231 VAL A O   1 
ATOM 1639 C CB  . VAL A 1 231 ? 18.141 11.853  9.124   1.00 35.75  ? 231 VAL A CB  1 
ATOM 1640 C CG1 . VAL A 1 231 ? 18.587 10.694  8.245   1.00 37.57  ? 231 VAL A CG1 1 
ATOM 1641 C CG2 . VAL A 1 231 ? 17.524 11.337  10.415  1.00 39.73  ? 231 VAL A CG2 1 
ATOM 1642 N N   . GLY A 1 232 ? 21.329 12.067  8.346   1.00 44.55  ? 232 GLY A N   1 
ATOM 1643 C CA  . GLY A 1 232 ? 22.370 12.121  7.332   1.00 42.01  ? 232 GLY A CA  1 
ATOM 1644 C C   . GLY A 1 232 ? 21.891 11.654  5.971   1.00 43.88  ? 232 GLY A C   1 
ATOM 1645 O O   . GLY A 1 232 ? 22.025 12.370  4.975   1.00 52.49  ? 232 GLY A O   1 
ATOM 1646 N N   . GLY A 1 233 ? 21.320 10.454  5.906   1.00 40.68  ? 233 GLY A N   1 
ATOM 1647 C CA  . GLY A 1 233 ? 20.850 9.941   4.634   1.00 45.42  ? 233 GLY A CA  1 
ATOM 1648 C C   . GLY A 1 233 ? 19.906 8.774   4.792   1.00 49.79  ? 233 GLY A C   1 
ATOM 1649 O O   . GLY A 1 233 ? 19.837 8.137   5.849   1.00 50.68  ? 233 GLY A O   1 
ATOM 1650 N N   . ILE A 1 234 ? 19.171 8.502   3.718   1.00 53.34  ? 234 ILE A N   1 
ATOM 1651 C CA  . ILE A 1 234 ? 18.332 7.315   3.604   1.00 47.12  ? 234 ILE A CA  1 
ATOM 1652 C C   . ILE A 1 234 ? 19.090 6.295   2.766   1.00 45.83  ? 234 ILE A C   1 
ATOM 1653 O O   . ILE A 1 234 ? 19.372 6.533   1.586   1.00 43.46  ? 234 ILE A O   1 
ATOM 1654 C CB  . ILE A 1 234 ? 16.966 7.643   2.981   1.00 49.48  ? 234 ILE A CB  1 
ATOM 1655 C CG1 . ILE A 1 234 ? 16.193 8.626   3.866   1.00 46.34  ? 234 ILE A CG1 1 
ATOM 1656 C CG2 . ILE A 1 234 ? 16.161 6.369   2.762   1.00 49.71  ? 234 ILE A CG2 1 
ATOM 1657 C CD1 . ILE A 1 234 ? 15.855 8.085   5.239   1.00 42.23  ? 234 ILE A CD1 1 
ATOM 1658 N N   . TRP A 1 235 ? 19.420 5.163   3.378   1.00 49.54  ? 235 TRP A N   1 
ATOM 1659 C CA  . TRP A 1 235 ? 20.319 4.158   2.815   1.00 43.75  ? 235 TRP A CA  1 
ATOM 1660 C C   . TRP A 1 235 ? 19.469 2.978   2.345   1.00 47.29  ? 235 TRP A C   1 
ATOM 1661 O O   . TRP A 1 235 ? 19.161 2.070   3.119   1.00 53.17  ? 235 TRP A O   1 
ATOM 1662 C CB  . TRP A 1 235 ? 21.344 3.743   3.870   1.00 44.16  ? 235 TRP A CB  1 
ATOM 1663 C CG  . TRP A 1 235 ? 22.653 3.235   3.361   1.00 44.43  ? 235 TRP A CG  1 
ATOM 1664 C CD1 . TRP A 1 235 ? 23.813 3.942   3.235   1.00 43.41  ? 235 TRP A CD1 1 
ATOM 1665 C CD2 . TRP A 1 235 ? 22.956 1.894   2.960   1.00 38.84  ? 235 TRP A CD2 1 
ATOM 1666 N NE1 . TRP A 1 235 ? 24.813 3.130   2.759   1.00 43.95  ? 235 TRP A NE1 1 
ATOM 1667 C CE2 . TRP A 1 235 ? 24.313 1.867   2.583   1.00 38.57  ? 235 TRP A CE2 1 
ATOM 1668 C CE3 . TRP A 1 235 ? 22.209 0.717   2.871   1.00 38.66  ? 235 TRP A CE3 1 
ATOM 1669 C CZ2 . TRP A 1 235 ? 24.937 0.709   2.126   1.00 44.60  ? 235 TRP A CZ2 1 
ATOM 1670 C CZ3 . TRP A 1 235 ? 22.831 -0.431  2.416   1.00 42.84  ? 235 TRP A CZ3 1 
ATOM 1671 C CH2 . TRP A 1 235 ? 24.181 -0.427  2.050   1.00 40.20  ? 235 TRP A CH2 1 
ATOM 1672 N N   . LEU A 1 236 ? 19.089 2.994   1.070   1.00 50.33  ? 236 LEU A N   1 
ATOM 1673 C CA  . LEU A 1 236 ? 18.196 1.982   0.523   1.00 46.72  ? 236 LEU A CA  1 
ATOM 1674 C C   . LEU A 1 236 ? 18.980 0.751   0.082   1.00 46.99  ? 236 LEU A C   1 
ATOM 1675 O O   . LEU A 1 236 ? 20.115 0.850   -0.391  1.00 46.68  ? 236 LEU A O   1 
ATOM 1676 C CB  . LEU A 1 236 ? 17.401 2.546   -0.655  1.00 53.09  ? 236 LEU A CB  1 
ATOM 1677 C CG  . LEU A 1 236 ? 16.477 3.726   -0.340  1.00 49.53  ? 236 LEU A CG  1 
ATOM 1678 C CD1 . LEU A 1 236 ? 15.833 4.266   -1.610  1.00 48.79  ? 236 LEU A CD1 1 
ATOM 1679 C CD2 . LEU A 1 236 ? 15.418 3.330   0.677   1.00 44.16  ? 236 LEU A CD2 1 
ATOM 1680 N N   . ASP A 1 237 ? 18.358 -0.418  0.246   1.00 51.93  ? 237 ASP A N   1 
ATOM 1681 C CA  . ASP A 1 237 ? 18.974 -1.690  -0.112  1.00 49.94  ? 237 ASP A CA  1 
ATOM 1682 C C   . ASP A 1 237 ? 17.958 -2.572  -0.827  1.00 54.86  ? 237 ASP A C   1 
ATOM 1683 O O   . ASP A 1 237 ? 16.757 -2.290  -0.845  1.00 58.64  ? 237 ASP A O   1 
ATOM 1684 C CB  . ASP A 1 237 ? 19.533 -2.410  1.121   1.00 54.19  ? 237 ASP A CB  1 
ATOM 1685 C CG  . ASP A 1 237 ? 20.507 -3.519  0.762   1.00 59.08  ? 237 ASP A CG  1 
ATOM 1686 O OD1 . ASP A 1 237 ? 21.041 -3.494  -0.365  1.00 59.98  ? 237 ASP A OD1 1 
ATOM 1687 O OD2 . ASP A 1 237 ? 20.737 -4.415  1.602   1.00 55.12  ? 237 ASP A OD2 1 
ATOM 1688 N N   . GLY A 1 238 ? 18.457 -3.658  -1.408  1.00 53.80  ? 238 GLY A N   1 
ATOM 1689 C CA  . GLY A 1 238 ? 17.630 -4.595  -2.136  1.00 60.22  ? 238 GLY A CA  1 
ATOM 1690 C C   . GLY A 1 238 ? 17.605 -4.378  -3.631  1.00 61.84  ? 238 GLY A C   1 
ATOM 1691 O O   . GLY A 1 238 ? 16.639 -4.794  -4.280  1.00 71.36  ? 238 GLY A O   1 
ATOM 1692 N N   . VAL A 1 239 ? 18.644 -3.756  -4.194  1.00 56.57  ? 239 VAL A N   1 
ATOM 1693 C CA  . VAL A 1 239 ? 18.597 -3.242  -5.561  1.00 66.78  ? 239 VAL A CA  1 
ATOM 1694 C C   . VAL A 1 239 ? 18.405 -4.347  -6.593  1.00 62.93  ? 239 VAL A C   1 
ATOM 1695 O O   . VAL A 1 239 ? 17.853 -4.103  -7.673  1.00 64.46  ? 239 VAL A O   1 
ATOM 1696 C CB  . VAL A 1 239 ? 19.867 -2.409  -5.840  1.00 65.92  ? 239 VAL A CB  1 
ATOM 1697 C CG1 . VAL A 1 239 ? 21.032 -3.301  -6.251  1.00 72.82  ? 239 VAL A CG1 1 
ATOM 1698 C CG2 . VAL A 1 239 ? 19.592 -1.355  -6.898  1.00 60.28  ? 239 VAL A CG2 1 
ATOM 1699 N N   . ALA A 1 240 ? 18.847 -5.572  -6.292  1.00 66.58  ? 240 ALA A N   1 
ATOM 1700 C CA  . ALA A 1 240 ? 18.825 -6.629  -7.299  1.00 66.82  ? 240 ALA A CA  1 
ATOM 1701 C C   . ALA A 1 240 ? 17.403 -7.009  -7.711  1.00 72.58  ? 240 ALA A C   1 
ATOM 1702 O O   . ALA A 1 240 ? 17.189 -7.441  -8.847  1.00 67.68  ? 240 ALA A O   1 
ATOM 1703 C CB  . ALA A 1 240 ? 19.571 -7.860  -6.787  1.00 64.86  ? 240 ALA A CB  1 
ATOM 1704 N N   . THR A 1 241 ? 16.436 -6.842  -6.808  1.00 71.67  ? 241 THR A N   1 
ATOM 1705 C CA  . THR A 1 241 ? 15.060 -7.282  -7.137  1.00 70.77  ? 241 THR A CA  1 
ATOM 1706 C C   . THR A 1 241 ? 14.373 -6.320  -8.107  1.00 76.92  ? 241 THR A C   1 
ATOM 1707 O O   . THR A 1 241 ? 13.879 -6.800  -9.140  1.00 80.03  ? 241 THR A O   1 
ATOM 1708 C CB  . THR A 1 241 ? 14.263 -7.481  -5.849  1.00 68.67  ? 241 THR A CB  1 
ATOM 1709 O OG1 . THR A 1 241 ? 14.965 -8.381  -4.988  1.00 67.55  ? 241 THR A OG1 1 
ATOM 1710 C CG2 . THR A 1 241 ? 12.893 -8.056  -6.166  1.00 65.72  ? 241 THR A CG2 1 
ATOM 1711 N N   . PRO A 1 242 ? 14.285 -5.013  -7.844  1.00 76.94  ? 242 PRO A N   1 
ATOM 1712 C CA  . PRO A 1 242 ? 13.666 -4.134  -8.857  1.00 75.15  ? 242 PRO A CA  1 
ATOM 1713 C C   . PRO A 1 242 ? 14.389 -4.173  -10.187 1.00 74.14  ? 242 PRO A C   1 
ATOM 1714 O O   . PRO A 1 242 ? 13.755 -3.998  -11.236 1.00 78.44  ? 242 PRO A O   1 
ATOM 1715 C CB  . PRO A 1 242 ? 13.741 -2.739  -8.215  1.00 77.03  ? 242 PRO A CB  1 
ATOM 1716 C CG  . PRO A 1 242 ? 14.727 -2.857  -7.115  1.00 71.66  ? 242 PRO A CG  1 
ATOM 1717 C CD  . PRO A 1 242 ? 14.645 -4.259  -6.634  1.00 71.25  ? 242 PRO A CD  1 
ATOM 1718 N N   . ALA A 1 243 ? 15.702 -4.397  -10.176 1.00 75.44  ? 243 ALA A N   1 
ATOM 1719 C CA  . ALA A 1 243 ? 16.488 -4.446  -11.400 1.00 78.67  ? 243 ALA A CA  1 
ATOM 1720 C C   . ALA A 1 243 ? 16.354 -5.768  -12.147 1.00 84.64  ? 243 ALA A C   1 
ATOM 1721 O O   . ALA A 1 243 ? 16.845 -5.869  -13.276 1.00 82.41  ? 243 ALA A O   1 
ATOM 1722 C CB  . ALA A 1 243 ? 17.963 -4.182  -11.087 1.00 68.79  ? 243 ALA A CB  1 
ATOM 1723 N N   . SER A 1 244 ? 15.711 -6.779  -11.556 1.00 86.01  ? 244 SER A N   1 
ATOM 1724 C CA  . SER A 1 244 ? 15.547 -8.047  -12.258 1.00 86.42  ? 244 SER A CA  1 
ATOM 1725 C C   . SER A 1 244 ? 14.482 -7.974  -13.343 1.00 84.55  ? 244 SER A C   1 
ATOM 1726 O O   . SER A 1 244 ? 14.483 -8.812  -14.251 1.00 92.68  ? 244 SER A O   1 
ATOM 1727 C CB  . SER A 1 244 ? 15.205 -9.163  -11.267 1.00 81.77  ? 244 SER A CB  1 
ATOM 1728 O OG  . SER A 1 244 ? 13.875 -9.044  -10.791 1.00 81.90  ? 244 SER A OG  1 
ATOM 1729 N N   . ARG A 1 245 ? 13.576 -6.995  -13.267 1.00 79.85  ? 245 ARG A N   1 
ATOM 1730 C CA  . ARG A 1 245 ? 12.589 -6.720  -14.312 1.00 86.46  ? 245 ARG A CA  1 
ATOM 1731 C C   . ARG A 1 245 ? 12.613 -5.206  -14.500 1.00 98.56  ? 245 ARG A C   1 
ATOM 1732 O O   . ARG A 1 245 ? 11.718 -4.506  -14.022 1.00 102.96 ? 245 ARG A O   1 
ATOM 1733 C CB  . ARG A 1 245 ? 11.199 -7.206  -13.914 1.00 88.81  ? 245 ARG A CB  1 
ATOM 1734 C CG  . ARG A 1 245 ? 11.093 -8.657  -13.486 1.00 90.31  ? 245 ARG A CG  1 
ATOM 1735 C CD  . ARG A 1 245 ? 11.418 -9.629  -14.602 1.00 81.24  ? 245 ARG A CD  1 
ATOM 1736 N NE  . ARG A 1 245 ? 12.370 -10.645 -14.170 1.00 80.39  ? 245 ARG A NE  1 
ATOM 1737 C CZ  . ARG A 1 245 ? 12.080 -11.647 -13.349 1.00 87.12  ? 245 ARG A CZ  1 
ATOM 1738 N NH1 . ARG A 1 245 ? 10.862 -11.811 -12.858 1.00 92.02  ? 245 ARG A NH1 1 
ATOM 1739 N NH2 . ARG A 1 245 ? 13.037 -12.509 -13.015 1.00 83.76  ? 245 ARG A NH2 1 
ATOM 1740 N N   . LYS A 1 246 ? 13.628 -4.693  -15.193 1.00 98.84  ? 246 LYS A N   1 
ATOM 1741 C CA  . LYS A 1 246 ? 13.815 -3.247  -15.155 1.00 101.94 ? 246 LYS A CA  1 
ATOM 1742 C C   . LYS A 1 246 ? 12.947 -2.498  -16.161 1.00 96.08  ? 246 LYS A C   1 
ATOM 1743 O O   . LYS A 1 246 ? 12.996 -1.264  -16.195 1.00 93.84  ? 246 LYS A O   1 
ATOM 1744 C CB  . LYS A 1 246 ? 15.300 -2.878  -15.273 1.00 101.06 ? 246 LYS A CB  1 
ATOM 1745 C CG  . LYS A 1 246 ? 16.055 -3.154  -16.545 1.00 91.85  ? 246 LYS A CG  1 
ATOM 1746 C CD  . LYS A 1 246 ? 17.483 -2.657  -16.294 1.00 104.21 ? 246 LYS A CD  1 
ATOM 1747 C CE  . LYS A 1 246 ? 18.400 -2.785  -17.491 1.00 103.79 ? 246 LYS A CE  1 
ATOM 1748 N NZ  . LYS A 1 246 ? 18.661 -1.451  -18.102 1.00 93.11  ? 246 LYS A NZ  1 
ATOM 1749 N N   . GLY A 1 247 ? 12.164 -3.202  -16.984 1.00 95.67  ? 247 GLY A N   1 
ATOM 1750 C CA  . GLY A 1 247 ? 11.071 -2.530  -17.662 1.00 98.57  ? 247 GLY A CA  1 
ATOM 1751 C C   . GLY A 1 247 ? 9.866  -2.371  -16.766 1.00 99.04  ? 247 GLY A C   1 
ATOM 1752 O O   . GLY A 1 247 ? 8.978  -1.561  -17.055 1.00 97.36  ? 247 GLY A O   1 
ATOM 1753 N N   . LYS A 1 248 ? 9.846  -3.122  -15.665 1.00 98.26  ? 248 LYS A N   1 
ATOM 1754 C CA  . LYS A 1 248 ? 8.864  -3.029  -14.599 1.00 96.51  ? 248 LYS A CA  1 
ATOM 1755 C C   . LYS A 1 248 ? 9.381  -2.173  -13.450 1.00 92.49  ? 248 LYS A C   1 
ATOM 1756 O O   . LYS A 1 248 ? 8.636  -1.904  -12.502 1.00 91.23  ? 248 LYS A O   1 
ATOM 1757 C CB  . LYS A 1 248 ? 8.524  -4.440  -14.094 1.00 91.15  ? 248 LYS A CB  1 
ATOM 1758 C CG  . LYS A 1 248 ? 7.052  -4.705  -13.854 1.00 89.99  ? 248 LYS A CG  1 
ATOM 1759 C CD  . LYS A 1 248 ? 6.804  -6.104  -13.297 1.00 91.25  ? 248 LYS A CD  1 
ATOM 1760 C CE  . LYS A 1 248 ? 7.746  -7.130  -13.907 1.00 95.94  ? 248 LYS A CE  1 
ATOM 1761 N NZ  . LYS A 1 248 ? 7.660  -8.461  -13.240 1.00 91.77  ? 248 LYS A NZ  1 
ATOM 1762 N N   . LEU A 1 249 ? 10.654 -1.772  -13.523 1.00 88.85  ? 249 LEU A N   1 
ATOM 1763 C CA  . LEU A 1 249 ? 11.313 -0.982  -12.486 1.00 89.59  ? 249 LEU A CA  1 
ATOM 1764 C C   . LEU A 1 249 ? 10.501 0.241   -12.071 1.00 87.76  ? 249 LEU A C   1 
ATOM 1765 O O   . LEU A 1 249 ? 10.505 0.630   -10.897 1.00 83.02  ? 249 LEU A O   1 
ATOM 1766 C CB  . LEU A 1 249 ? 12.693 -0.559  -12.996 1.00 96.41  ? 249 LEU A CB  1 
ATOM 1767 C CG  . LEU A 1 249 ? 13.794 -0.100  -12.043 1.00 92.59  ? 249 LEU A CG  1 
ATOM 1768 C CD1 . LEU A 1 249 ? 15.149 -0.522  -12.582 1.00 86.40  ? 249 LEU A CD1 1 
ATOM 1769 C CD2 . LEU A 1 249 ? 13.740 1.404   -11.878 1.00 84.07  ? 249 LEU A CD2 1 
ATOM 1770 N N   . HIS A 1 250 ? 9.806  0.867   -13.023 1.00 93.39  ? 250 HIS A N   1 
ATOM 1771 C CA  . HIS A 1 250 ? 9.159  2.147   -12.759 1.00 91.19  ? 250 HIS A CA  1 
ATOM 1772 C C   . HIS A 1 250 ? 7.960  2.044   -11.822 1.00 87.82  ? 250 HIS A C   1 
ATOM 1773 O O   . HIS A 1 250 ? 7.559  3.063   -11.248 1.00 82.70  ? 250 HIS A O   1 
ATOM 1774 C CB  . HIS A 1 250 ? 8.725  2.788   -14.077 1.00 92.02  ? 250 HIS A CB  1 
ATOM 1775 C CG  . HIS A 1 250 ? 7.568  2.100   -14.728 1.00 88.45  ? 250 HIS A CG  1 
ATOM 1776 N ND1 . HIS A 1 250 ? 7.727  1.095   -15.658 1.00 86.43  ? 250 HIS A ND1 1 
ATOM 1777 C CD2 . HIS A 1 250 ? 6.232  2.270   -14.582 1.00 91.63  ? 250 HIS A CD2 1 
ATOM 1778 C CE1 . HIS A 1 250 ? 6.539  0.676   -16.057 1.00 94.76  ? 250 HIS A CE1 1 
ATOM 1779 N NE2 . HIS A 1 250 ? 5.616  1.372   -15.419 1.00 93.99  ? 250 HIS A NE2 1 
ATOM 1780 N N   . LEU A 1 251 ? 7.370  0.855   -11.652 1.00 79.21  ? 251 LEU A N   1 
ATOM 1781 C CA  . LEU A 1 251 ? 6.219  0.745   -10.760 1.00 84.20  ? 251 LEU A CA  1 
ATOM 1782 C C   . LEU A 1 251 ? 6.580  1.035   -9.312  1.00 88.18  ? 251 LEU A C   1 
ATOM 1783 O O   . LEU A 1 251 ? 5.684  1.299   -8.502  1.00 83.35  ? 251 LEU A O   1 
ATOM 1784 C CB  . LEU A 1 251 ? 5.573  -0.635  -10.836 1.00 89.77  ? 251 LEU A CB  1 
ATOM 1785 C CG  . LEU A 1 251 ? 5.565  -1.432  -12.130 1.00 85.70  ? 251 LEU A CG  1 
ATOM 1786 C CD1 . LEU A 1 251 ? 5.170  -2.844  -11.769 1.00 76.35  ? 251 LEU A CD1 1 
ATOM 1787 C CD2 . LEU A 1 251 ? 4.609  -0.832  -13.143 1.00 87.04  ? 251 LEU A CD2 1 
ATOM 1788 N N   . PHE A 1 252 ? 7.866  0.986   -8.965  1.00 91.94  ? 252 PHE A N   1 
ATOM 1789 C CA  . PHE A 1 252 ? 8.268  1.252   -7.593  1.00 87.37  ? 252 PHE A CA  1 
ATOM 1790 C C   . PHE A 1 252 ? 8.136  2.727   -7.252  1.00 84.93  ? 252 PHE A C   1 
ATOM 1791 O O   . PHE A 1 252 ? 8.135  3.077   -6.066  1.00 80.92  ? 252 PHE A O   1 
ATOM 1792 C CB  . PHE A 1 252 ? 9.712  0.800   -7.368  1.00 78.36  ? 252 PHE A CB  1 
ATOM 1793 C CG  . PHE A 1 252 ? 9.845  -0.644  -6.975  1.00 79.61  ? 252 PHE A CG  1 
ATOM 1794 C CD1 . PHE A 1 252 ? 9.643  -1.042  -5.664  1.00 79.47  ? 252 PHE A CD1 1 
ATOM 1795 C CD2 . PHE A 1 252 ? 10.177 -1.602  -7.918  1.00 79.51  ? 252 PHE A CD2 1 
ATOM 1796 C CE1 . PHE A 1 252 ? 9.768  -2.371  -5.302  1.00 75.43  ? 252 PHE A CE1 1 
ATOM 1797 C CE2 . PHE A 1 252 ? 10.301 -2.931  -7.563  1.00 78.60  ? 252 PHE A CE2 1 
ATOM 1798 C CZ  . PHE A 1 252 ? 10.098 -3.316  -6.253  1.00 75.94  ? 252 PHE A CZ  1 
ATOM 1799 N N   . GLU A 1 253 ? 8.008  3.588   -8.264  1.00 87.20  ? 253 GLU A N   1 
ATOM 1800 C CA  . GLU A 1 253 ? 7.959  5.035   -8.077  1.00 85.69  ? 253 GLU A CA  1 
ATOM 1801 C C   . GLU A 1 253 ? 9.150  5.491   -7.237  1.00 81.69  ? 253 GLU A C   1 
ATOM 1802 O O   . GLU A 1 253 ? 9.015  6.213   -6.246  1.00 74.03  ? 253 GLU A O   1 
ATOM 1803 C CB  . GLU A 1 253 ? 6.626  5.466   -7.460  1.00 87.38  ? 253 GLU A CB  1 
ATOM 1804 C CG  . GLU A 1 253 ? 5.408  4.966   -8.235  1.00 89.33  ? 253 GLU A CG  1 
ATOM 1805 C CD  . GLU A 1 253 ? 4.166  5.808   -8.004  1.00 84.50  ? 253 GLU A CD  1 
ATOM 1806 O OE1 . GLU A 1 253 ? 4.047  6.412   -6.917  1.00 76.39  ? 253 GLU A OE1 1 
ATOM 1807 O OE2 . GLU A 1 253 ? 3.307  5.862   -8.910  1.00 77.68  ? 253 GLU A OE2 1 
ATOM 1808 N N   . THR A 1 254 ? 10.337 5.044   -7.655  1.00 78.51  ? 254 THR A N   1 
ATOM 1809 C CA  . THR A 1 254 ? 11.547 5.269   -6.870  1.00 77.98  ? 254 THR A CA  1 
ATOM 1810 C C   . THR A 1 254 ? 12.022 6.714   -6.960  1.00 77.13  ? 254 THR A C   1 
ATOM 1811 O O   . THR A 1 254 ? 12.424 7.300   -5.949  1.00 71.21  ? 254 THR A O   1 
ATOM 1812 C CB  . THR A 1 254 ? 12.646 4.313   -7.331  1.00 75.16  ? 254 THR A CB  1 
ATOM 1813 O OG1 . THR A 1 254 ? 12.196 2.962   -7.176  1.00 69.42  ? 254 THR A OG1 1 
ATOM 1814 C CG2 . THR A 1 254 ? 13.911 4.517   -6.510  1.00 67.74  ? 254 THR A CG2 1 
ATOM 1815 N N   . GLN A 1 255 ? 11.998 7.306   -8.158  1.00 78.21  ? 255 GLN A N   1 
ATOM 1816 C CA  . GLN A 1 255 ? 12.431 8.694   -8.288  1.00 72.67  ? 255 GLN A CA  1 
ATOM 1817 C C   . GLN A 1 255 ? 11.542 9.616   -7.465  1.00 71.53  ? 255 GLN A C   1 
ATOM 1818 O O   . GLN A 1 255 ? 12.021 10.587  -6.867  1.00 76.74  ? 255 GLN A O   1 
ATOM 1819 C CB  . GLN A 1 255 ? 12.435 9.119   -9.755  1.00 68.27  ? 255 GLN A CB  1 
ATOM 1820 C CG  . GLN A 1 255 ? 12.702 10.601  -9.952  1.00 71.85  ? 255 GLN A CG  1 
ATOM 1821 C CD  . GLN A 1 255 ? 14.047 11.021  -9.389  1.00 73.59  ? 255 GLN A CD  1 
ATOM 1822 O OE1 . GLN A 1 255 ? 15.080 10.438  -9.718  1.00 67.18  ? 255 GLN A OE1 1 
ATOM 1823 N NE2 . GLN A 1 255 ? 14.038 12.032  -8.526  1.00 70.39  ? 255 GLN A NE2 1 
ATOM 1824 N N   . GLU A 1 256 ? 10.244 9.316   -7.415  1.00 68.42  ? 256 GLU A N   1 
ATOM 1825 C CA  . GLU A 1 256 ? 9.333  10.066  -6.562  1.00 76.40  ? 256 GLU A CA  1 
ATOM 1826 C C   . GLU A 1 256 ? 9.698  9.904   -5.093  1.00 76.07  ? 256 GLU A C   1 
ATOM 1827 O O   . GLU A 1 256 ? 9.475  10.819  -4.292  1.00 75.63  ? 256 GLU A O   1 
ATOM 1828 C CB  . GLU A 1 256 ? 7.888  9.617   -6.812  1.00 75.02  ? 256 GLU A CB  1 
ATOM 1829 C CG  . GLU A 1 256 ? 7.398  9.676   -8.275  1.00 80.63  ? 256 GLU A CG  1 
ATOM 1830 C CD  . GLU A 1 256 ? 8.116  8.723   -9.228  1.00 84.02  ? 256 GLU A CD  1 
ATOM 1831 O OE1 . GLU A 1 256 ? 9.006  7.970   -8.782  1.00 84.14  ? 256 GLU A OE1 1 
ATOM 1832 O OE2 . GLU A 1 256 ? 7.788  8.730   -10.434 1.00 83.67  ? 256 GLU A OE2 1 
ATOM 1833 N N   . LEU A 1 257 ? 10.258 8.750   -4.723  1.00 77.40  ? 257 LEU A N   1 
ATOM 1834 C CA  . LEU A 1 257 ? 10.736 8.562   -3.357  1.00 73.86  ? 257 LEU A CA  1 
ATOM 1835 C C   . LEU A 1 257 ? 11.932 9.463   -3.076  1.00 73.99  ? 257 LEU A C   1 
ATOM 1836 O O   . LEU A 1 257 ? 11.991 10.124  -2.032  1.00 74.05  ? 257 LEU A O   1 
ATOM 1837 C CB  . LEU A 1 257 ? 11.094 7.097   -3.112  1.00 69.66  ? 257 LEU A CB  1 
ATOM 1838 C CG  . LEU A 1 257 ? 11.500 6.787   -1.670  1.00 66.21  ? 257 LEU A CG  1 
ATOM 1839 C CD1 . LEU A 1 257 ? 10.329 7.027   -0.730  1.00 63.17  ? 257 LEU A CD1 1 
ATOM 1840 C CD2 . LEU A 1 257 ? 12.023 5.366   -1.538  1.00 62.27  ? 257 LEU A CD2 1 
ATOM 1841 N N   . TYR A 1 258 ? 12.906 9.487   -3.994  1.00 67.51  ? 258 TYR A N   1 
ATOM 1842 C CA  . TYR A 1 258 ? 14.047 10.386  -3.851  1.00 66.90  ? 258 TYR A CA  1 
ATOM 1843 C C   . TYR A 1 258 ? 13.583 11.824  -3.679  1.00 74.64  ? 258 TYR A C   1 
ATOM 1844 O O   . TYR A 1 258 ? 14.098 12.559  -2.827  1.00 72.93  ? 258 TYR A O   1 
ATOM 1845 C CB  . TYR A 1 258 ? 14.962 10.294  -5.074  1.00 64.92  ? 258 TYR A CB  1 
ATOM 1846 C CG  . TYR A 1 258 ? 15.693 8.983   -5.260  1.00 65.08  ? 258 TYR A CG  1 
ATOM 1847 C CD1 . TYR A 1 258 ? 15.574 7.951   -4.340  1.00 65.70  ? 258 TYR A CD1 1 
ATOM 1848 C CD2 . TYR A 1 258 ? 16.506 8.782   -6.366  1.00 64.36  ? 258 TYR A CD2 1 
ATOM 1849 C CE1 . TYR A 1 258 ? 16.244 6.754   -4.520  1.00 62.40  ? 258 TYR A CE1 1 
ATOM 1850 C CE2 . TYR A 1 258 ? 17.181 7.594   -6.553  1.00 68.41  ? 258 TYR A CE2 1 
ATOM 1851 C CZ  . TYR A 1 258 ? 17.045 6.583   -5.629  1.00 66.85  ? 258 TYR A CZ  1 
ATOM 1852 O OH  . TYR A 1 258 ? 17.714 5.397   -5.817  1.00 63.47  ? 258 TYR A OH  1 
ATOM 1853 N N   . ASP A 1 259 ? 12.608 12.242  -4.489  1.00 75.77  ? 259 ASP A N   1 
ATOM 1854 C CA  . ASP A 1 259 ? 12.099 13.606  -4.408  1.00 72.95  ? 259 ASP A CA  1 
ATOM 1855 C C   . ASP A 1 259 ? 11.453 13.877  -3.055  1.00 68.72  ? 259 ASP A C   1 
ATOM 1856 O O   . ASP A 1 259 ? 11.642 14.953  -2.475  1.00 65.46  ? 259 ASP A O   1 
ATOM 1857 C CB  . ASP A 1 259 ? 11.110 13.856  -5.546  1.00 70.73  ? 259 ASP A CB  1 
ATOM 1858 C CG  . ASP A 1 259 ? 11.743 13.681  -6.915  1.00 81.76  ? 259 ASP A CG  1 
ATOM 1859 O OD1 . ASP A 1 259 ? 12.991 13.657  -6.998  1.00 73.80  ? 259 ASP A OD1 1 
ATOM 1860 O OD2 . ASP A 1 259 ? 10.993 13.560  -7.908  1.00 84.48  ? 259 ASP A OD2 1 
ATOM 1861 N N   . HIS A 1 260 ? 10.682 12.917  -2.538  1.00 67.10  ? 260 HIS A N   1 
ATOM 1862 C CA  . HIS A 1 260 ? 10.090 13.087  -1.215  1.00 67.59  ? 260 HIS A CA  1 
ATOM 1863 C C   . HIS A 1 260 ? 11.160 13.239  -0.140  1.00 69.28  ? 260 HIS A C   1 
ATOM 1864 O O   . HIS A 1 260 ? 10.996 14.026  0.800   1.00 65.22  ? 260 HIS A O   1 
ATOM 1865 C CB  . HIS A 1 260 ? 9.164  11.915  -0.886  1.00 63.83  ? 260 HIS A CB  1 
ATOM 1866 C CG  . HIS A 1 260 ? 8.383  12.105  0.378   1.00 72.57  ? 260 HIS A CG  1 
ATOM 1867 N ND1 . HIS A 1 260 ? 7.081  12.556  0.388   1.00 77.41  ? 260 HIS A ND1 1 
ATOM 1868 C CD2 . HIS A 1 260 ? 8.725  11.916  1.674   1.00 73.59  ? 260 HIS A CD2 1 
ATOM 1869 C CE1 . HIS A 1 260 ? 6.653  12.632  1.636   1.00 72.07  ? 260 HIS A CE1 1 
ATOM 1870 N NE2 . HIS A 1 260 ? 7.632  12.250  2.436   1.00 74.36  ? 260 HIS A NE2 1 
ATOM 1871 N N   . ILE A 1 261 ? 12.266 12.498  -0.260  1.00 67.48  ? 261 ILE A N   1 
ATOM 1872 C CA  . ILE A 1 261 ? 13.322 12.575  0.746   1.00 61.18  ? 261 ILE A CA  1 
ATOM 1873 C C   . ILE A 1 261 ? 13.992 13.944  0.718   1.00 66.07  ? 261 ILE A C   1 
ATOM 1874 O O   . ILE A 1 261 ? 14.181 14.581  1.762   1.00 68.22  ? 261 ILE A O   1 
ATOM 1875 C CB  . ILE A 1 261 ? 14.348 11.447  0.541   1.00 56.89  ? 261 ILE A CB  1 
ATOM 1876 C CG1 . ILE A 1 261 ? 13.683 10.079  0.695   1.00 58.46  ? 261 ILE A CG1 1 
ATOM 1877 C CG2 . ILE A 1 261 ? 15.501 11.595  1.521   1.00 57.16  ? 261 ILE A CG2 1 
ATOM 1878 C CD1 . ILE A 1 261 ? 14.443 8.957   0.024   1.00 50.90  ? 261 ILE A CD1 1 
ATOM 1879 N N   . HIS A 1 262 ? 14.363 14.418  -0.475  1.00 69.01  ? 262 HIS A N   1 
ATOM 1880 C CA  . HIS A 1 262 ? 15.008 15.723  -0.576  1.00 61.02  ? 262 HIS A CA  1 
ATOM 1881 C C   . HIS A 1 262 ? 14.070 16.839  -0.143  1.00 65.60  ? 262 HIS A C   1 
ATOM 1882 O O   . HIS A 1 262 ? 14.516 17.841  0.428   1.00 70.46  ? 262 HIS A O   1 
ATOM 1883 C CB  . HIS A 1 262 ? 15.499 15.960  -2.003  1.00 63.46  ? 262 HIS A CB  1 
ATOM 1884 C CG  . HIS A 1 262 ? 16.639 15.077  -2.403  1.00 70.25  ? 262 HIS A CG  1 
ATOM 1885 N ND1 . HIS A 1 262 ? 16.602 14.277  -3.525  1.00 70.94  ? 262 HIS A ND1 1 
ATOM 1886 C CD2 . HIS A 1 262 ? 17.847 14.866  -1.829  1.00 63.70  ? 262 HIS A CD2 1 
ATOM 1887 C CE1 . HIS A 1 262 ? 17.740 13.612  -3.626  1.00 67.20  ? 262 HIS A CE1 1 
ATOM 1888 N NE2 . HIS A 1 262 ? 18.512 13.952  -2.610  1.00 66.85  ? 262 HIS A NE2 1 
ATOM 1889 N N   . SER A 1 263 ? 12.771 16.686  -0.406  1.00 61.99  ? 263 SER A N   1 
ATOM 1890 C CA  . SER A 1 263 ? 11.800 17.677  0.036   1.00 54.99  ? 263 SER A CA  1 
ATOM 1891 C C   . SER A 1 263 ? 11.595 17.639  1.543   1.00 55.21  ? 263 SER A C   1 
ATOM 1892 O O   . SER A 1 263 ? 11.158 18.638  2.122   1.00 62.67  ? 263 SER A O   1 
ATOM 1893 C CB  . SER A 1 263 ? 10.465 17.461  -0.677  1.00 60.58  ? 263 SER A CB  1 
ATOM 1894 O OG  . SER A 1 263 ? 9.950  16.170  -0.407  1.00 69.40  ? 263 SER A OG  1 
ATOM 1895 N N   . LEU A 1 264 ? 11.893 16.508  2.187   1.00 57.27  ? 264 LEU A N   1 
ATOM 1896 C CA  . LEU A 1 264 ? 11.599 16.354  3.607   1.00 56.65  ? 264 LEU A CA  1 
ATOM 1897 C C   . LEU A 1 264 ? 12.623 17.051  4.493   1.00 48.02  ? 264 LEU A C   1 
ATOM 1898 O O   . LEU A 1 264 ? 12.267 17.533  5.573   1.00 49.07  ? 264 LEU A O   1 
ATOM 1899 C CB  . LEU A 1 264 ? 11.517 14.871  3.965   1.00 58.36  ? 264 LEU A CB  1 
ATOM 1900 C CG  . LEU A 1 264 ? 10.121 14.251  3.871   1.00 62.10  ? 264 LEU A CG  1 
ATOM 1901 C CD1 . LEU A 1 264 ? 10.006 13.061  4.801   1.00 55.77  ? 264 LEU A CD1 1 
ATOM 1902 C CD2 . LEU A 1 264 ? 9.045  15.284  4.179   1.00 66.80  ? 264 LEU A CD2 1 
ATOM 1903 N N   . GLN A 1 265 ? 13.881 17.117  4.066   1.00 51.37  ? 265 GLN A N   1 
ATOM 1904 C CA  . GLN A 1 265 ? 14.911 17.868  4.769   1.00 59.84  ? 265 GLN A CA  1 
ATOM 1905 C C   . GLN A 1 265 ? 15.915 18.374  3.729   1.00 57.77  ? 265 GLN A C   1 
ATOM 1906 O O   . GLN A 1 265 ? 16.149 17.694  2.734   1.00 60.73  ? 265 GLN A O   1 
ATOM 1907 C CB  . GLN A 1 265 ? 15.657 17.035  5.821   1.00 52.17  ? 265 GLN A CB  1 
ATOM 1908 C CG  . GLN A 1 265 ? 14.842 16.408  6.929   1.00 44.83  ? 265 GLN A CG  1 
ATOM 1909 C CD  . GLN A 1 265 ? 15.705 15.544  7.832   1.00 47.99  ? 265 GLN A CD  1 
ATOM 1910 O OE1 . GLN A 1 265 ? 16.929 15.679  7.851   1.00 50.35  ? 265 GLN A OE1 1 
ATOM 1911 N NE2 . GLN A 1 265 ? 15.075 14.651  8.580   1.00 44.14  ? 265 GLN A NE2 1 
ATOM 1912 N N   . PRO A 1 266 ? 16.498 19.549  3.964   1.00 55.64  ? 266 PRO A N   1 
ATOM 1913 C CA  . PRO A 1 266 ? 17.412 20.105  2.940   1.00 58.56  ? 266 PRO A CA  1 
ATOM 1914 C C   . PRO A 1 266 ? 18.639 19.251  2.663   1.00 62.15  ? 266 PRO A C   1 
ATOM 1915 O O   . PRO A 1 266 ? 19.053 19.147  1.503   1.00 72.11  ? 266 PRO A O   1 
ATOM 1916 C CB  . PRO A 1 266 ? 17.802 21.473  3.527   1.00 58.52  ? 266 PRO A CB  1 
ATOM 1917 C CG  . PRO A 1 266 ? 17.379 21.451  4.960   1.00 50.20  ? 266 PRO A CG  1 
ATOM 1918 C CD  . PRO A 1 266 ? 16.260 20.475  5.076   1.00 52.66  ? 266 PRO A CD  1 
ATOM 1919 N N   . GLN A 1 267 ? 19.238 18.641  3.686   1.00 64.70  ? 267 GLN A N   1 
ATOM 1920 C CA  . GLN A 1 267 ? 20.576 18.069  3.575   1.00 65.09  ? 267 GLN A CA  1 
ATOM 1921 C C   . GLN A 1 267 ? 20.618 16.547  3.453   1.00 59.39  ? 267 GLN A C   1 
ATOM 1922 O O   . GLN A 1 267 ? 21.710 15.991  3.304   1.00 59.42  ? 267 GLN A O   1 
ATOM 1923 C CB  . GLN A 1 267 ? 21.421 18.500  4.781   1.00 61.04  ? 267 GLN A CB  1 
ATOM 1924 C CG  . GLN A 1 267 ? 21.257 17.618  6.015   1.00 58.40  ? 267 GLN A CG  1 
ATOM 1925 C CD  . GLN A 1 267 ? 19.814 17.496  6.477   1.00 56.05  ? 267 GLN A CD  1 
ATOM 1926 O OE1 . GLN A 1 267 ? 19.000 18.396  6.265   1.00 57.37  ? 267 GLN A OE1 1 
ATOM 1927 N NE2 . GLN A 1 267 ? 19.491 16.374  7.111   1.00 56.37  ? 267 GLN A NE2 1 
ATOM 1928 N N   . VAL A 1 268 ? 19.480 15.853  3.508   1.00 59.51  ? 268 VAL A N   1 
ATOM 1929 C CA  . VAL A 1 268 ? 19.518 14.393  3.481   1.00 55.40  ? 268 VAL A CA  1 
ATOM 1930 C C   . VAL A 1 268 ? 20.014 13.893  2.133   1.00 51.88  ? 268 VAL A C   1 
ATOM 1931 O O   . VAL A 1 268 ? 19.664 14.432  1.074   1.00 57.35  ? 268 VAL A O   1 
ATOM 1932 C CB  . VAL A 1 268 ? 18.141 13.792  3.803   1.00 54.23  ? 268 VAL A CB  1 
ATOM 1933 C CG1 . VAL A 1 268 ? 18.279 12.328  4.167   1.00 54.54  ? 268 VAL A CG1 1 
ATOM 1934 C CG2 . VAL A 1 268 ? 17.544 14.505  4.952   1.00 60.53  ? 268 VAL A CG2 1 
ATOM 1935 N N   . LEU A 1 269 ? 20.839 12.855  2.175   1.00 55.76  ? 269 LEU A N   1 
ATOM 1936 C CA  . LEU A 1 269 ? 21.285 12.137  0.995   1.00 52.25  ? 269 LEU A CA  1 
ATOM 1937 C C   . LEU A 1 269 ? 20.415 10.903  0.794   1.00 51.04  ? 269 LEU A C   1 
ATOM 1938 O O   . LEU A 1 269 ? 19.689 10.472  1.693   1.00 49.11  ? 269 LEU A O   1 
ATOM 1939 C CB  . LEU A 1 269 ? 22.754 11.731  1.131   1.00 47.95  ? 269 LEU A CB  1 
ATOM 1940 C CG  . LEU A 1 269 ? 23.727 12.882  1.381   1.00 49.79  ? 269 LEU A CG  1 
ATOM 1941 C CD1 . LEU A 1 269 ? 25.163 12.387  1.377   1.00 61.85  ? 269 LEU A CD1 1 
ATOM 1942 C CD2 . LEU A 1 269 ? 23.527 13.968  0.343   1.00 59.70  ? 269 LEU A CD2 1 
ATOM 1943 N N   . VAL A 1 270 ? 20.487 10.339  -0.408  1.00 50.34  ? 270 VAL A N   1 
ATOM 1944 C CA  . VAL A 1 270 ? 19.852 9.062   -0.710  1.00 41.49  ? 270 VAL A CA  1 
ATOM 1945 C C   . VAL A 1 270 ? 20.838 8.212   -1.494  1.00 48.99  ? 270 VAL A C   1 
ATOM 1946 O O   . VAL A 1 270 ? 21.387 8.661   -2.505  1.00 49.12  ? 270 VAL A O   1 
ATOM 1947 C CB  . VAL A 1 270 ? 18.545 9.218   -1.513  1.00 51.79  ? 270 VAL A CB  1 
ATOM 1948 C CG1 . VAL A 1 270 ? 17.712 7.948   -1.409  1.00 55.56  ? 270 VAL A CG1 1 
ATOM 1949 C CG2 . VAL A 1 270 ? 17.748 10.419  -1.037  1.00 61.99  ? 270 VAL A CG2 1 
ATOM 1950 N N   . SER A 1 271 ? 21.068 6.990   -1.023  1.00 57.68  ? 271 SER A N   1 
ATOM 1951 C CA  . SER A 1 271 ? 21.872 6.012   -1.733  1.00 46.00  ? 271 SER A CA  1 
ATOM 1952 C C   . SER A 1 271 ? 21.053 4.749   -1.951  1.00 49.79  ? 271 SER A C   1 
ATOM 1953 O O   . SER A 1 271 ? 20.077 4.487   -1.243  1.00 50.77  ? 271 SER A O   1 
ATOM 1954 C CB  . SER A 1 271 ? 23.151 5.673   -0.966  1.00 43.82  ? 271 SER A CB  1 
ATOM 1955 O OG  . SER A 1 271 ? 22.854 5.267   0.358   1.00 57.59  ? 271 SER A OG  1 
ATOM 1956 N N   . TYR A 1 272 ? 21.463 3.966   -2.951  1.00 53.88  ? 272 TYR A N   1 
ATOM 1957 C CA  . TYR A 1 272 ? 20.781 2.725   -3.288  1.00 49.95  ? 272 TYR A CA  1 
ATOM 1958 C C   . TYR A 1 272 ? 21.818 1.750   -3.850  1.00 49.30  ? 272 TYR A C   1 
ATOM 1959 O O   . TYR A 1 272 ? 21.774 1.352   -5.014  1.00 56.19  ? 272 TYR A O   1 
ATOM 1960 C CB  . TYR A 1 272 ? 19.637 2.968   -4.274  1.00 54.47  ? 272 TYR A CB  1 
ATOM 1961 C CG  . TYR A 1 272 ? 18.531 1.942   -4.208  1.00 54.52  ? 272 TYR A CG  1 
ATOM 1962 C CD1 . TYR A 1 272 ? 18.806 0.608   -3.940  1.00 54.98  ? 272 TYR A CD1 1 
ATOM 1963 C CD2 . TYR A 1 272 ? 17.208 2.307   -4.422  1.00 54.71  ? 272 TYR A CD2 1 
ATOM 1964 C CE1 . TYR A 1 272 ? 17.798 -0.331  -3.880  1.00 55.42  ? 272 TYR A CE1 1 
ATOM 1965 C CE2 . TYR A 1 272 ? 16.192 1.372   -4.368  1.00 60.74  ? 272 TYR A CE2 1 
ATOM 1966 C CZ  . TYR A 1 272 ? 16.494 0.053   -4.097  1.00 64.78  ? 272 TYR A CZ  1 
ATOM 1967 O OH  . TYR A 1 272 ? 15.488 -0.886  -4.040  1.00 61.57  ? 272 TYR A OH  1 
ATOM 1968 N N   . LYS A 1 273 ? 22.760 1.357   -2.997  1.00 54.09  ? 273 LYS A N   1 
ATOM 1969 C CA  . LYS A 1 273 ? 23.858 0.443   -3.349  1.00 52.68  ? 273 LYS A CA  1 
ATOM 1970 C C   . LYS A 1 273 ? 24.610 1.035   -4.539  1.00 61.06  ? 273 LYS A C   1 
ATOM 1971 O O   . LYS A 1 273 ? 24.993 2.216   -4.489  1.00 59.59  ? 273 LYS A O   1 
ATOM 1972 C CB  . LYS A 1 273 ? 23.293 -0.955  -3.559  1.00 54.76  ? 273 LYS A CB  1 
ATOM 1973 C CG  . LYS A 1 273 ? 22.566 -1.510  -2.353  1.00 54.22  ? 273 LYS A CG  1 
ATOM 1974 C CD  . LYS A 1 273 ? 23.520 -1.700  -1.189  1.00 51.34  ? 273 LYS A CD  1 
ATOM 1975 C CE  . LYS A 1 273 ? 24.126 -3.091  -1.209  1.00 49.91  ? 273 LYS A CE  1 
ATOM 1976 N NZ  . LYS A 1 273 ? 23.853 -3.841  0.049   1.00 56.34  ? 273 LYS A NZ  1 
ATOM 1977 N N   . GLN A 1 274 ? 24.844 0.277   -5.609  1.00 68.58  ? 274 GLN A N   1 
ATOM 1978 C CA  . GLN A 1 274 ? 25.548 0.777   -6.781  1.00 63.40  ? 274 GLN A CA  1 
ATOM 1979 C C   . GLN A 1 274 ? 24.665 1.643   -7.668  1.00 62.14  ? 274 GLN A C   1 
ATOM 1980 O O   . GLN A 1 274 ? 25.154 2.181   -8.667  1.00 67.29  ? 274 GLN A O   1 
ATOM 1981 C CB  . GLN A 1 274 ? 26.108 -0.393  -7.594  1.00 59.92  ? 274 GLN A CB  1 
ATOM 1982 C CG  . GLN A 1 274 ? 25.055 -1.151  -8.389  1.00 70.46  ? 274 GLN A CG  1 
ATOM 1983 C CD  . GLN A 1 274 ? 24.581 -2.408  -7.685  1.00 66.58  ? 274 GLN A CD  1 
ATOM 1984 O OE1 . GLN A 1 274 ? 24.926 -2.654  -6.529  1.00 58.72  ? 274 GLN A OE1 1 
ATOM 1985 N NE2 . GLN A 1 274 ? 23.783 -3.210  -8.381  1.00 60.66  ? 274 GLN A NE2 1 
ATOM 1986 N N   . GLY A 1 275 ? 23.385 1.778   -7.335  1.00 58.69  ? 275 GLY A N   1 
ATOM 1987 C CA  . GLY A 1 275 ? 22.475 2.614   -8.091  1.00 60.14  ? 275 GLY A CA  1 
ATOM 1988 C C   . GLY A 1 275 ? 21.370 1.815   -8.746  1.00 64.36  ? 275 GLY A C   1 
ATOM 1989 O O   . GLY A 1 275 ? 21.620 0.744   -9.305  1.00 77.44  ? 275 GLY A O   1 
ATOM 1990 N N   . LEU A 1 276 ? 20.140 2.321   -8.681  1.00 67.12  ? 276 LEU A N   1 
ATOM 1991 C CA  . LEU A 1 276 ? 19.008 1.701   -9.355  1.00 72.44  ? 276 LEU A CA  1 
ATOM 1992 C C   . LEU A 1 276 ? 18.503 2.524   -10.530 1.00 77.85  ? 276 LEU A C   1 
ATOM 1993 O O   . LEU A 1 276 ? 18.262 1.978   -11.611 1.00 87.15  ? 276 LEU A O   1 
ATOM 1994 C CB  . LEU A 1 276 ? 17.862 1.463   -8.362  1.00 74.31  ? 276 LEU A CB  1 
ATOM 1995 C CG  . LEU A 1 276 ? 16.616 0.810   -8.967  1.00 74.13  ? 276 LEU A CG  1 
ATOM 1996 C CD1 . LEU A 1 276 ? 16.881 -0.656  -9.279  1.00 69.76  ? 276 LEU A CD1 1 
ATOM 1997 C CD2 . LEU A 1 276 ? 15.418 0.958   -8.041  1.00 65.28  ? 276 LEU A CD2 1 
ATOM 1998 N N   . ILE A 1 277 ? 18.334 3.833   -10.345 1.00 76.65  ? 277 ILE A N   1 
ATOM 1999 C CA  . ILE A 1 277 ? 17.844 4.715   -11.393 1.00 75.88  ? 277 ILE A CA  1 
ATOM 2000 C C   . ILE A 1 277 ? 18.851 5.804   -11.740 1.00 71.26  ? 277 ILE A C   1 
ATOM 2001 O O   . ILE A 1 277 ? 18.548 6.689   -12.541 1.00 76.92  ? 277 ILE A O   1 
ATOM 2002 C CB  . ILE A 1 277 ? 16.479 5.326   -11.019 1.00 71.43  ? 277 ILE A CB  1 
ATOM 2003 C CG1 . ILE A 1 277 ? 16.637 6.372   -9.918  1.00 66.16  ? 277 ILE A CG1 1 
ATOM 2004 C CG2 . ILE A 1 277 ? 15.513 4.241   -10.572 1.00 73.98  ? 277 ILE A CG2 1 
ATOM 2005 C CD1 . ILE A 1 277 ? 15.321 6.887   -9.396  1.00 63.60  ? 277 ILE A CD1 1 
ATOM 2006 N N   . GLY A 1 278 ? 20.047 5.757   -11.155 1.00 67.50  ? 278 GLY A N   1 
ATOM 2007 C CA  . GLY A 1 278 ? 21.128 6.638   -11.544 1.00 64.38  ? 278 GLY A CA  1 
ATOM 2008 C C   . GLY A 1 278 ? 21.119 8.023   -10.935 1.00 67.28  ? 278 GLY A C   1 
ATOM 2009 O O   . GLY A 1 278 ? 22.065 8.785   -11.173 1.00 69.86  ? 278 GLY A O   1 
ATOM 2010 N N   . THR A 1 279 ? 20.095 8.384   -10.159 1.00 62.99  ? 279 THR A N   1 
ATOM 2011 C CA  . THR A 1 279 ? 19.953 9.742   -9.645  1.00 65.98  ? 279 THR A CA  1 
ATOM 2012 C C   . THR A 1 279 ? 20.237 9.841   -8.148  1.00 68.22  ? 279 THR A C   1 
ATOM 2013 O O   . THR A 1 279 ? 19.785 10.789  -7.497  1.00 69.02  ? 279 THR A O   1 
ATOM 2014 C CB  . THR A 1 279 ? 18.554 10.280  -9.952  1.00 66.88  ? 279 THR A CB  1 
ATOM 2015 O OG1 . THR A 1 279 ? 17.575 9.500   -9.254  1.00 69.97  ? 279 THR A OG1 1 
ATOM 2016 C CG2 . THR A 1 279 ? 18.274 10.212  -11.445 1.00 65.64  ? 279 THR A CG2 1 
ATOM 2017 N N   . GLU A 1 280 ? 20.979 8.889   -7.589  1.00 64.00  ? 280 GLU A N   1 
ATOM 2018 C CA  . GLU A 1 280 ? 21.298 8.910   -6.170  1.00 62.41  ? 280 GLU A CA  1 
ATOM 2019 C C   . GLU A 1 280 ? 22.409 9.915   -5.874  1.00 55.24  ? 280 GLU A C   1 
ATOM 2020 O O   . GLU A 1 280 ? 23.159 10.337  -6.758  1.00 50.93  ? 280 GLU A O   1 
ATOM 2021 C CB  . GLU A 1 280 ? 21.715 7.520   -5.688  1.00 53.54  ? 280 GLU A CB  1 
ATOM 2022 C CG  . GLU A 1 280 ? 20.661 6.444   -5.889  1.00 57.97  ? 280 GLU A CG  1 
ATOM 2023 C CD  . GLU A 1 280 ? 20.601 5.933   -7.316  1.00 67.01  ? 280 GLU A CD  1 
ATOM 2024 O OE1 . GLU A 1 280 ? 21.495 6.289   -8.114  1.00 61.61  ? 280 GLU A OE1 1 
ATOM 2025 O OE2 . GLU A 1 280 ? 19.659 5.180   -7.640  1.00 65.57  ? 280 GLU A OE2 1 
ATOM 2026 N N   . ASP A 1 281 ? 22.508 10.297  -4.598  1.00 48.61  ? 281 ASP A N   1 
ATOM 2027 C CA  . ASP A 1 281 ? 23.516 11.268  -4.190  1.00 46.68  ? 281 ASP A CA  1 
ATOM 2028 C C   . ASP A 1 281 ? 24.890 10.635  -4.008  1.00 50.72  ? 281 ASP A C   1 
ATOM 2029 O O   . ASP A 1 281 ? 25.905 11.324  -4.158  1.00 52.89  ? 281 ASP A O   1 
ATOM 2030 C CB  . ASP A 1 281 ? 23.080 11.969  -2.903  1.00 49.35  ? 281 ASP A CB  1 
ATOM 2031 C CG  . ASP A 1 281 ? 21.796 12.758  -3.078  1.00 57.18  ? 281 ASP A CG  1 
ATOM 2032 O OD1 . ASP A 1 281 ? 21.615 13.371  -4.152  1.00 54.07  ? 281 ASP A OD1 1 
ATOM 2033 O OD2 . ASP A 1 281 ? 20.969 12.766  -2.143  1.00 58.03  ? 281 ASP A OD2 1 
ATOM 2034 N N   . PHE A 1 282 ? 24.951 9.344   -3.686  1.00 48.53  ? 282 PHE A N   1 
ATOM 2035 C CA  . PHE A 1 282 ? 26.213 8.619   -3.717  1.00 50.53  ? 282 PHE A CA  1 
ATOM 2036 C C   . PHE A 1 282 ? 25.936 7.149   -3.998  1.00 51.20  ? 282 PHE A C   1 
ATOM 2037 O O   . PHE A 1 282 ? 24.789 6.697   -3.996  1.00 49.97  ? 282 PHE A O   1 
ATOM 2038 C CB  . PHE A 1 282 ? 27.017 8.802   -2.418  1.00 53.04  ? 282 PHE A CB  1 
ATOM 2039 C CG  . PHE A 1 282 ? 26.318 8.319   -1.171  1.00 48.95  ? 282 PHE A CG  1 
ATOM 2040 C CD1 . PHE A 1 282 ? 25.360 9.100   -0.545  1.00 48.52  ? 282 PHE A CD1 1 
ATOM 2041 C CD2 . PHE A 1 282 ? 26.652 7.098   -0.605  1.00 50.91  ? 282 PHE A CD2 1 
ATOM 2042 C CE1 . PHE A 1 282 ? 24.733 8.664   0.612   1.00 55.93  ? 282 PHE A CE1 1 
ATOM 2043 C CE2 . PHE A 1 282 ? 26.034 6.658   0.554   1.00 53.34  ? 282 PHE A CE2 1 
ATOM 2044 C CZ  . PHE A 1 282 ? 25.072 7.442   1.164   1.00 50.74  ? 282 PHE A CZ  1 
ATOM 2045 N N   . LYS A 1 283 ? 27.010 6.407   -4.259  1.00 47.20  ? 283 LYS A N   1 
ATOM 2046 C CA  . LYS A 1 283 ? 26.939 4.988   -4.579  1.00 56.76  ? 283 LYS A CA  1 
ATOM 2047 C C   . LYS A 1 283 ? 27.555 4.185   -3.441  1.00 57.05  ? 283 LYS A C   1 
ATOM 2048 O O   . LYS A 1 283 ? 28.672 4.480   -3.002  1.00 53.53  ? 283 LYS A O   1 
ATOM 2049 C CB  . LYS A 1 283 ? 27.658 4.686   -5.896  1.00 55.87  ? 283 LYS A CB  1 
ATOM 2050 C CG  . LYS A 1 283 ? 26.744 4.701   -7.112  1.00 65.31  ? 283 LYS A CG  1 
ATOM 2051 C CD  . LYS A 1 283 ? 27.532 4.634   -8.411  1.00 71.54  ? 283 LYS A CD  1 
ATOM 2052 C CE  . LYS A 1 283 ? 26.621 4.807   -9.619  1.00 64.82  ? 283 LYS A CE  1 
ATOM 2053 N NZ  . LYS A 1 283 ? 27.363 4.705   -10.905 1.00 75.02  ? 283 LYS A NZ  1 
ATOM 2054 N N   . ALA A 1 284 ? 26.825 3.173   -2.966  1.00 57.00  ? 284 ALA A N   1 
ATOM 2055 C CA  . ALA A 1 284 ? 27.247 2.342   -1.839  1.00 64.46  ? 284 ALA A CA  1 
ATOM 2056 C C   . ALA A 1 284 ? 27.381 0.884   -2.271  1.00 59.91  ? 284 ALA A C   1 
ATOM 2057 O O   . ALA A 1 284 ? 26.565 0.035   -1.889  1.00 53.79  ? 284 ALA A O   1 
ATOM 2058 C CB  . ALA A 1 284 ? 26.266 2.469   -0.675  1.00 50.05  ? 284 ALA A CB  1 
ATOM 2059 N N   . PRO A 1 285 ? 28.406 0.554   -3.053  1.00 58.78  ? 285 PRO A N   1 
ATOM 2060 C CA  . PRO A 1 285 ? 28.635 -0.850  -3.406  1.00 62.46  ? 285 PRO A CA  1 
ATOM 2061 C C   . PRO A 1 285 ? 29.083 -1.663  -2.203  1.00 58.16  ? 285 PRO A C   1 
ATOM 2062 O O   . PRO A 1 285 ? 29.658 -1.140  -1.245  1.00 60.43  ? 285 PRO A O   1 
ATOM 2063 C CB  . PRO A 1 285 ? 29.742 -0.773  -4.461  1.00 71.46  ? 285 PRO A CB  1 
ATOM 2064 C CG  . PRO A 1 285 ? 30.458 0.483   -4.129  1.00 60.53  ? 285 PRO A CG  1 
ATOM 2065 C CD  . PRO A 1 285 ? 29.415 1.439   -3.659  1.00 55.48  ? 285 PRO A CD  1 
ATOM 2066 N N   . GLU A 1 286 ? 28.812 -2.964  -2.264  1.00 66.39  ? 286 GLU A N   1 
ATOM 2067 C CA  . GLU A 1 286 ? 29.297 -3.890  -1.249  1.00 68.16  ? 286 GLU A CA  1 
ATOM 2068 C C   . GLU A 1 286 ? 30.763 -4.212  -1.515  1.00 70.30  ? 286 GLU A C   1 
ATOM 2069 O O   . GLU A 1 286 ? 31.111 -4.682  -2.605  1.00 70.90  ? 286 GLU A O   1 
ATOM 2070 C CB  . GLU A 1 286 ? 28.463 -5.169  -1.235  1.00 59.05  ? 286 GLU A CB  1 
ATOM 2071 C CG  . GLU A 1 286 ? 27.121 -5.043  -0.531  1.00 57.11  ? 286 GLU A CG  1 
ATOM 2072 C CD  . GLU A 1 286 ? 26.243 -6.266  -0.731  1.00 53.73  ? 286 GLU A CD  1 
ATOM 2073 O OE1 . GLU A 1 286 ? 26.792 -7.386  -0.797  1.00 57.69  ? 286 GLU A OE1 1 
ATOM 2074 O OE2 . GLU A 1 286 ? 25.007 -6.109  -0.820  1.00 41.92  ? 286 GLU A OE2 1 
ATOM 2075 N N   . ARG A 1 287 ? 31.618 -3.929  -0.528  1.00 69.52  ? 287 ARG A N   1 
ATOM 2076 C CA  . ARG A 1 287 ? 33.011 -4.371  -0.497  1.00 78.24  ? 287 ARG A CA  1 
ATOM 2077 C C   . ARG A 1 287 ? 33.878 -3.640  -1.517  1.00 82.99  ? 287 ARG A C   1 
ATOM 2078 O O   . ARG A 1 287 ? 34.921 -3.083  -1.164  1.00 78.95  ? 287 ARG A O   1 
ATOM 2079 C CB  . ARG A 1 287 ? 33.107 -5.885  -0.722  1.00 74.46  ? 287 ARG A CB  1 
ATOM 2080 C CG  . ARG A 1 287 ? 32.118 -6.704  0.093   1.00 67.66  ? 287 ARG A CG  1 
ATOM 2081 C CD  . ARG A 1 287 ? 32.771 -7.920  0.729   1.00 64.97  ? 287 ARG A CD  1 
ATOM 2082 N NE  . ARG A 1 287 ? 32.051 -8.369  1.916   1.00 64.69  ? 287 ARG A NE  1 
ATOM 2083 C CZ  . ARG A 1 287 ? 30.837 -8.902  1.908   1.00 65.32  ? 287 ARG A CZ  1 
ATOM 2084 N NH1 . ARG A 1 287 ? 30.170 -9.092  0.780   1.00 58.92  ? 287 ARG A NH1 1 
ATOM 2085 N NH2 . ARG A 1 287 ? 30.277 -9.260  3.060   1.00 63.70  ? 287 ARG A NH2 1 
ATOM 2086 N N   . HIS A 1 288 ? 33.458 -3.625  -2.778  1.00 81.74  ? 288 HIS A N   1 
ATOM 2087 C CA  . HIS A 1 288 ? 34.289 -3.072  -3.836  1.00 80.98  ? 288 HIS A CA  1 
ATOM 2088 C C   . HIS A 1 288 ? 33.406 -2.526  -4.945  1.00 87.23  ? 288 HIS A C   1 
ATOM 2089 O O   . HIS A 1 288 ? 32.235 -2.893  -5.069  1.00 89.16  ? 288 HIS A O   1 
ATOM 2090 C CB  . HIS A 1 288 ? 35.250 -4.129  -4.396  1.00 89.14  ? 288 HIS A CB  1 
ATOM 2091 C CG  . HIS A 1 288 ? 34.561 -5.273  -5.077  1.00 89.29  ? 288 HIS A CG  1 
ATOM 2092 N ND1 . HIS A 1 288 ? 34.315 -5.299  -6.434  1.00 92.72  ? 288 HIS A ND1 1 
ATOM 2093 C CD2 . HIS A 1 288 ? 34.060 -6.430  -4.584  1.00 94.19  ? 288 HIS A CD2 1 
ATOM 2094 C CE1 . HIS A 1 288 ? 33.697 -6.424  -6.746  1.00 97.57  ? 288 HIS A CE1 1 
ATOM 2095 N NE2 . HIS A 1 288 ? 33.529 -7.128  -5.641  1.00 102.43 ? 288 HIS A NE2 1 
ATOM 2096 N N   . PHE A 1 289 ? 33.991 -1.661  -5.771  1.00 86.95  ? 289 PHE A N   1 
ATOM 2097 C CA  . PHE A 1 289 ? 33.299 -1.118  -6.930  1.00 90.08  ? 289 PHE A CA  1 
ATOM 2098 C C   . PHE A 1 289 ? 34.265 -1.070  -8.102  1.00 98.62  ? 289 PHE A C   1 
ATOM 2099 O O   . PHE A 1 289 ? 35.358 -0.503  -7.997  1.00 95.81  ? 289 PHE A O   1 
ATOM 2100 C CB  . PHE A 1 289 ? 32.720 0.283   -6.661  1.00 80.83  ? 289 PHE A CB  1 
ATOM 2101 C CG  . PHE A 1 289 ? 31.764 0.761   -7.722  1.00 85.31  ? 289 PHE A CG  1 
ATOM 2102 C CD1 . PHE A 1 289 ? 30.804 -0.089  -8.242  1.00 90.55  ? 289 PHE A CD1 1 
ATOM 2103 C CD2 . PHE A 1 289 ? 31.830 2.059   -8.203  1.00 82.39  ? 289 PHE A CD2 1 
ATOM 2104 C CE1 . PHE A 1 289 ? 29.925 0.344   -9.224  1.00 95.74  ? 289 PHE A CE1 1 
ATOM 2105 C CE2 . PHE A 1 289 ? 30.954 2.502   -9.184  1.00 86.47  ? 289 PHE A CE2 1 
ATOM 2106 C CZ  . PHE A 1 289 ? 30.000 1.640   -9.696  1.00 83.22  ? 289 PHE A CZ  1 
ATOM 2107 N N   . LYS A 1 290 ? 33.815 -1.692  -9.186  1.00 103.63 ? 290 LYS A N   1 
ATOM 2108 C CA  . LYS A 1 290 ? 34.597 -1.637  -10.428 1.00 105.45 ? 290 LYS A CA  1 
ATOM 2109 C C   . LYS A 1 290 ? 34.135 -0.374  -11.138 1.00 110.21 ? 290 LYS A C   1 
ATOM 2110 O O   . LYS A 1 290 ? 33.002 0.063   -10.888 1.00 109.06 ? 290 LYS A O   1 
ATOM 2111 C CB  . LYS A 1 290 ? 34.329 -2.887  -11.263 1.00 105.55 ? 290 LYS A CB  1 
ATOM 2112 C CG  . LYS A 1 290 ? 33.025 -3.605  -10.943 1.00 109.84 ? 290 LYS A CG  1 
ATOM 2113 C CD  . LYS A 1 290 ? 33.199 -4.773  -9.996  1.00 105.52 ? 290 LYS A CD  1 
ATOM 2114 C CE  . LYS A 1 290 ? 34.612 -5.314  -9.981  1.00 105.75 ? 290 LYS A CE  1 
ATOM 2115 N NZ  . LYS A 1 290 ? 34.849 -6.258  -11.098 1.00 110.66 ? 290 LYS A NZ  1 
ATOM 2116 N N   . GLY A 1 291 ? 34.976 0.173   -11.994 1.00 113.37 ? 291 GLY A N   1 
ATOM 2117 C CA  . GLY A 1 291 ? 34.690 1.416   -12.697 1.00 107.77 ? 291 GLY A CA  1 
ATOM 2118 C C   . GLY A 1 291 ? 34.810 2.617   -11.782 1.00 109.15 ? 291 GLY A C   1 
ATOM 2119 O O   . GLY A 1 291 ? 35.218 2.519   -10.621 1.00 112.38 ? 291 GLY A O   1 
ATOM 2120 N N   . THR A 1 292 ? 34.439 3.782   -12.314 1.00 110.19 ? 292 THR A N   1 
ATOM 2121 C CA  . THR A 1 292 ? 34.414 5.019   -11.544 1.00 102.76 ? 292 THR A CA  1 
ATOM 2122 C C   . THR A 1 292 ? 33.016 5.617   -11.635 1.00 105.27 ? 292 THR A C   1 
ATOM 2123 O O   . THR A 1 292 ? 32.209 5.241   -12.491 1.00 103.06 ? 292 THR A O   1 
ATOM 2124 C CB  . THR A 1 292 ? 35.467 6.035   -12.021 1.00 91.13  ? 292 THR A CB  1 
ATOM 2125 O OG1 . THR A 1 292 ? 34.963 6.764   -13.147 1.00 104.97 ? 292 THR A OG1 1 
ATOM 2126 C CG2 . THR A 1 292 ? 36.769 5.345   -12.396 1.00 93.22  ? 292 THR A CG2 1 
ATOM 2127 N N   . SER A 1 293 ? 32.733 6.569   -10.746 1.00 101.66 ? 293 SER A N   1 
ATOM 2128 C CA  . SER A 1 293 ? 31.379 7.072   -10.559 1.00 91.16  ? 293 SER A CA  1 
ATOM 2129 C C   . SER A 1 293 ? 31.347 8.593   -10.506 1.00 82.05  ? 293 SER A C   1 
ATOM 2130 O O   . SER A 1 293 ? 32.280 9.242   -10.024 1.00 83.61  ? 293 SER A O   1 
ATOM 2131 C CB  . SER A 1 293 ? 30.744 6.511   -9.283  1.00 85.44  ? 293 SER A CB  1 
ATOM 2132 O OG  . SER A 1 293 ? 29.430 7.010   -9.112  1.00 84.05  ? 293 SER A OG  1 
ATOM 2133 N N   . ASP A 1 294 ? 30.239 9.148   -11.007 1.00 80.52  ? 294 ASP A N   1 
ATOM 2134 C CA  . ASP A 1 294 ? 29.985 10.583  -10.938 1.00 81.48  ? 294 ASP A CA  1 
ATOM 2135 C C   . ASP A 1 294 ? 29.906 11.099  -9.506  1.00 82.23  ? 294 ASP A C   1 
ATOM 2136 O O   . ASP A 1 294 ? 30.138 12.292  -9.276  1.00 89.25  ? 294 ASP A O   1 
ATOM 2137 C CB  . ASP A 1 294 ? 28.686 10.910  -11.680 1.00 86.21  ? 294 ASP A CB  1 
ATOM 2138 C CG  . ASP A 1 294 ? 28.804 12.141  -12.555 1.00 92.87  ? 294 ASP A CG  1 
ATOM 2139 O OD1 . ASP A 1 294 ? 28.595 13.260  -12.042 1.00 96.25  ? 294 ASP A OD1 1 
ATOM 2140 O OD2 . ASP A 1 294 ? 29.103 11.987  -13.758 1.00 99.31  ? 294 ASP A OD2 1 
ATOM 2141 N N   . VAL A 1 295 ? 29.581 10.240  -8.544  1.00 78.86  ? 295 VAL A N   1 
ATOM 2142 C CA  . VAL A 1 295 ? 29.168 10.673  -7.210  1.00 62.90  ? 295 VAL A CA  1 
ATOM 2143 C C   . VAL A 1 295 ? 30.125 10.083  -6.176  1.00 66.38  ? 295 VAL A C   1 
ATOM 2144 O O   . VAL A 1 295 ? 31.023 9.312   -6.547  1.00 65.17  ? 295 VAL A O   1 
ATOM 2145 C CB  . VAL A 1 295 ? 27.708 10.268  -6.938  1.00 64.65  ? 295 VAL A CB  1 
ATOM 2146 C CG1 . VAL A 1 295 ? 26.753 11.241  -7.613  1.00 64.17  ? 295 VAL A CG1 1 
ATOM 2147 C CG2 . VAL A 1 295 ? 27.448 8.846   -7.407  1.00 65.79  ? 295 VAL A CG2 1 
ATOM 2148 N N   . PRO A 1 296 ? 30.000 10.424  -4.888  1.00 57.11  ? 296 PRO A N   1 
ATOM 2149 C CA  . PRO A 1 296 ? 30.834 9.770   -3.869  1.00 61.03  ? 296 PRO A CA  1 
ATOM 2150 C C   . PRO A 1 296 ? 30.651 8.258   -3.823  1.00 52.32  ? 296 PRO A C   1 
ATOM 2151 O O   . PRO A 1 296 ? 29.588 7.723   -4.145  1.00 42.01  ? 296 PRO A O   1 
ATOM 2152 C CB  . PRO A 1 296 ? 30.369 10.422  -2.562  1.00 55.61  ? 296 PRO A CB  1 
ATOM 2153 C CG  . PRO A 1 296 ? 29.899 11.762  -2.970  1.00 57.90  ? 296 PRO A CG  1 
ATOM 2154 C CD  . PRO A 1 296 ? 29.312 11.611  -4.344  1.00 49.68  ? 296 PRO A CD  1 
ATOM 2155 N N   . LEU A 1 297 ? 31.718 7.574   -3.408  1.00 50.96  ? 297 LEU A N   1 
ATOM 2156 C CA  . LEU A 1 297 ? 31.740 6.127   -3.248  1.00 59.63  ? 297 LEU A CA  1 
ATOM 2157 C C   . LEU A 1 297 ? 31.863 5.764   -1.774  1.00 51.98  ? 297 LEU A C   1 
ATOM 2158 O O   . LEU A 1 297 ? 32.580 6.428   -1.019  1.00 41.83  ? 297 LEU A O   1 
ATOM 2159 C CB  . LEU A 1 297 ? 32.908 5.497   -4.012  1.00 65.80  ? 297 LEU A CB  1 
ATOM 2160 C CG  . LEU A 1 297 ? 32.674 5.054   -5.451  1.00 62.05  ? 297 LEU A CG  1 
ATOM 2161 C CD1 . LEU A 1 297 ? 31.419 4.200   -5.539  1.00 56.20  ? 297 LEU A CD1 1 
ATOM 2162 C CD2 . LEU A 1 297 ? 32.592 6.262   -6.359  1.00 67.81  ? 297 LEU A CD2 1 
ATOM 2163 N N   . GLU A 1 298 ? 31.163 4.706   -1.370  1.00 53.56  ? 298 GLU A N   1 
ATOM 2164 C CA  . GLU A 1 298 ? 31.300 4.154   -0.024  1.00 53.32  ? 298 GLU A CA  1 
ATOM 2165 C C   . GLU A 1 298 ? 31.245 2.636   -0.118  1.00 50.97  ? 298 GLU A C   1 
ATOM 2166 O O   . GLU A 1 298 ? 30.207 2.074   -0.483  1.00 49.46  ? 298 GLU A O   1 
ATOM 2167 C CB  . GLU A 1 298 ? 30.210 4.693   0.903   1.00 56.99  ? 298 GLU A CB  1 
ATOM 2168 C CG  . GLU A 1 298 ? 30.177 4.055   2.278   1.00 46.27  ? 298 GLU A CG  1 
ATOM 2169 C CD  . GLU A 1 298 ? 28.787 4.071   2.880   1.00 50.34  ? 298 GLU A CD  1 
ATOM 2170 O OE1 . GLU A 1 298 ? 27.887 3.414   2.313   1.00 51.88  ? 298 GLU A OE1 1 
ATOM 2171 O OE2 . GLU A 1 298 ? 28.594 4.744   3.915   1.00 46.30  ? 298 GLU A OE2 1 
ATOM 2172 N N   . PHE A 1 299 ? 32.353 1.974   0.211   1.00 50.81  ? 299 PHE A N   1 
ATOM 2173 C CA  . PHE A 1 299 ? 32.388 0.519   0.282   1.00 49.81  ? 299 PHE A CA  1 
ATOM 2174 C C   . PHE A 1 299 ? 31.985 0.075   1.680   1.00 43.44  ? 299 PHE A C   1 
ATOM 2175 O O   . PHE A 1 299 ? 32.555 0.538   2.673   1.00 41.49  ? 299 PHE A O   1 
ATOM 2176 C CB  . PHE A 1 299 ? 33.778 -0.029  -0.046  1.00 55.83  ? 299 PHE A CB  1 
ATOM 2177 C CG  . PHE A 1 299 ? 34.318 0.414   -1.375  1.00 66.71  ? 299 PHE A CG  1 
ATOM 2178 C CD1 . PHE A 1 299 ? 33.471 0.672   -2.437  1.00 64.49  ? 299 PHE A CD1 1 
ATOM 2179 C CD2 . PHE A 1 299 ? 35.681 0.568   -1.560  1.00 66.42  ? 299 PHE A CD2 1 
ATOM 2180 C CE1 . PHE A 1 299 ? 33.974 1.080   -3.654  1.00 64.19  ? 299 PHE A CE1 1 
ATOM 2181 C CE2 . PHE A 1 299 ? 36.189 0.969   -2.777  1.00 60.61  ? 299 PHE A CE2 1 
ATOM 2182 C CZ  . PHE A 1 299 ? 35.334 1.227   -3.826  1.00 65.23  ? 299 PHE A CZ  1 
ATOM 2183 N N   . CYS A 1 300 ? 31.019 -0.834  1.755   1.00 49.58  ? 300 CYS A N   1 
ATOM 2184 C CA  . CYS A 1 300 ? 30.591 -1.419  3.017   1.00 44.41  ? 300 CYS A CA  1 
ATOM 2185 C C   . CYS A 1 300 ? 31.115 -2.844  3.113   1.00 54.50  ? 300 CYS A C   1 
ATOM 2186 O O   . CYS A 1 300 ? 30.978 -3.626  2.166   1.00 61.06  ? 300 CYS A O   1 
ATOM 2187 C CB  . CYS A 1 300 ? 29.067 -1.393  3.147   1.00 39.29  ? 300 CYS A CB  1 
ATOM 2188 S SG  . CYS A 1 300 ? 28.184 -1.931  1.669   1.00 57.29  ? 300 CYS A SG  1 
ATOM 2189 N N   . ASP A 1 301 ? 31.705 -3.179  4.258   1.00 52.45  ? 301 ASP A N   1 
ATOM 2190 C CA  . ASP A 1 301 ? 32.299 -4.489  4.471   1.00 53.47  ? 301 ASP A CA  1 
ATOM 2191 C C   . ASP A 1 301 ? 32.038 -4.930  5.904   1.00 49.14  ? 301 ASP A C   1 
ATOM 2192 O O   . ASP A 1 301 ? 31.582 -4.152  6.746   1.00 49.74  ? 301 ASP A O   1 
ATOM 2193 C CB  . ASP A 1 301 ? 33.804 -4.486  4.186   1.00 51.56  ? 301 ASP A CB  1 
ATOM 2194 C CG  . ASP A 1 301 ? 34.273 -5.777  3.554   1.00 68.11  ? 301 ASP A CG  1 
ATOM 2195 O OD1 . ASP A 1 301 ? 34.534 -6.746  4.298   1.00 73.02  ? 301 ASP A OD1 1 
ATOM 2196 O OD2 . ASP A 1 301 ? 34.399 -5.818  2.313   1.00 68.00  ? 301 ASP A OD2 1 
ATOM 2197 N N   . THR A 1 302 ? 32.343 -6.194  6.177   1.00 53.57  ? 302 THR A N   1 
ATOM 2198 C CA  . THR A 1 302 ? 31.926 -6.856  7.403   1.00 54.97  ? 302 THR A CA  1 
ATOM 2199 C C   . THR A 1 302 ? 33.123 -7.176  8.288   1.00 51.07  ? 302 THR A C   1 
ATOM 2200 O O   . THR A 1 302 ? 34.221 -7.460  7.801   1.00 55.14  ? 302 THR A O   1 
ATOM 2201 C CB  . THR A 1 302 ? 31.179 -8.153  7.090   1.00 53.76  ? 302 THR A CB  1 
ATOM 2202 O OG1 . THR A 1 302 ? 32.030 -9.015  6.323   1.00 61.36  ? 302 THR A OG1 1 
ATOM 2203 C CG2 . THR A 1 302 ? 29.944 -7.870  6.289   1.00 40.95  ? 302 THR A CG2 1 
ATOM 2204 N N   . LEU A 1 303 ? 32.920 -7.153  9.602   1.00 48.52  ? 303 LEU A N   1 
ATOM 2205 C CA  . LEU A 1 303 ? 34.013 -7.561  10.522  1.00 55.24  ? 303 LEU A CA  1 
ATOM 2206 C C   . LEU A 1 303 ? 33.892 -9.070  10.725  1.00 55.84  ? 303 LEU A C   1 
ATOM 2207 O O   . LEU A 1 303 ? 34.829 -9.670  11.260  1.00 55.74  ? 303 LEU A O   1 
ATOM 2208 C CB  . LEU A 1 303 ? 33.897 -6.784  11.835  1.00 50.49  ? 303 LEU A CB  1 
ATOM 2209 C CG  . LEU A 1 303 ? 34.811 -5.568  11.954  1.00 52.60  ? 303 LEU A CG  1 
ATOM 2210 C CD1 . LEU A 1 303 ? 34.753 -4.981  13.354  1.00 52.26  ? 303 LEU A CD1 1 
ATOM 2211 C CD2 . LEU A 1 303 ? 36.239 -5.933  11.590  1.00 51.85  ? 303 LEU A CD2 1 
ATOM 2212 N N   . GLN A 1 304 ? 32.765 -9.643  10.314  1.00 53.93  ? 304 GLN A N   1 
ATOM 2213 C CA  . GLN A 1 304 ? 32.588 -11.110 10.348  1.00 53.49  ? 304 GLN A CA  1 
ATOM 2214 C C   . GLN A 1 304 ? 32.847 -11.595 8.930   1.00 55.35  ? 304 GLN A C   1 
ATOM 2215 O O   . GLN A 1 304 ? 32.421 -10.909 8.000   1.00 59.66  ? 304 GLN A O   1 
ATOM 2216 C CB  . GLN A 1 304 ? 31.151 -11.473 10.703  1.00 45.92  ? 304 GLN A CB  1 
ATOM 2217 C CG  . GLN A 1 304 ? 30.883 -11.658 12.185  1.00 49.87  ? 304 GLN A CG  1 
ATOM 2218 C CD  . GLN A 1 304 ? 29.426 -11.970 12.421  1.00 51.82  ? 304 GLN A CD  1 
ATOM 2219 O OE1 . GLN A 1 304 ? 28.942 -11.957 13.549  1.00 61.94  ? 304 GLN A OE1 1 
ATOM 2220 N NE2 . GLN A 1 304 ? 28.711 -12.252 11.345  1.00 40.50  ? 304 GLN A NE2 1 
ATOM 2221 N N   . PRO A 1 305 ? 33.513 -12.741 8.713   1.00 61.52  ? 305 PRO A N   1 
ATOM 2222 C CA  . PRO A 1 305 ? 33.702 -13.262 7.362   1.00 56.67  ? 305 PRO A CA  1 
ATOM 2223 C C   . PRO A 1 305 ? 32.416 -13.414 6.534   1.00 53.14  ? 305 PRO A C   1 
ATOM 2224 O O   . PRO A 1 305 ? 31.662 -14.312 6.819   1.00 52.04  ? 305 PRO A O   1 
ATOM 2225 C CB  . PRO A 1 305 ? 34.346 -14.637 7.580   1.00 47.85  ? 305 PRO A CB  1 
ATOM 2226 C CG  . PRO A 1 305 ? 34.184 -14.925 9.058   1.00 61.31  ? 305 PRO A CG  1 
ATOM 2227 C CD  . PRO A 1 305 ? 34.126 -13.575 9.737   1.00 60.48  ? 305 PRO A CD  1 
ATOM 2228 N N   . TRP A 1 306 ? 32.179 -12.509 5.582   1.00 55.41  ? 306 TRP A N   1 
ATOM 2229 C CA  . TRP A 1 306 ? 31.045 -12.640 4.623   1.00 56.32  ? 306 TRP A CA  1 
ATOM 2230 C C   . TRP A 1 306 ? 29.687 -12.263 5.212   1.00 54.24  ? 306 TRP A C   1 
ATOM 2231 O O   . TRP A 1 306 ? 28.872 -11.696 4.474   1.00 55.57  ? 306 TRP A O   1 
ATOM 2232 C CB  . TRP A 1 306 ? 31.008 -14.062 4.047   1.00 60.77  ? 306 TRP A CB  1 
ATOM 2233 C CG  . TRP A 1 306 ? 32.008 -14.313 2.964   1.00 57.71  ? 306 TRP A CG  1 
ATOM 2234 C CD1 . TRP A 1 306 ? 33.045 -15.197 2.989   1.00 55.17  ? 306 TRP A CD1 1 
ATOM 2235 C CD2 . TRP A 1 306 ? 32.063 -13.667 1.682   1.00 58.38  ? 306 TRP A CD2 1 
ATOM 2236 N NE1 . TRP A 1 306 ? 33.744 -15.143 1.814   1.00 57.06  ? 306 TRP A NE1 1 
ATOM 2237 C CE2 . TRP A 1 306 ? 33.164 -14.214 0.993   1.00 52.34  ? 306 TRP A CE2 1 
ATOM 2238 C CE3 . TRP A 1 306 ? 31.295 -12.683 1.053   1.00 62.75  ? 306 TRP A CE3 1 
ATOM 2239 C CZ2 . TRP A 1 306 ? 33.511 -13.809 -0.293  1.00 49.22  ? 306 TRP A CZ2 1 
ATOM 2240 C CZ3 . TRP A 1 306 ? 31.639 -12.282 -0.217  1.00 59.31  ? 306 TRP A CZ3 1 
ATOM 2241 C CH2 . TRP A 1 306 ? 32.732 -12.839 -0.879  1.00 53.56  ? 306 TRP A CH2 1 
ATOM 2242 N N   . LYS A 1 307 ? 29.456 -12.542 6.487   1.00 57.03  ? 307 LYS A N   1 
ATOM 2243 C CA  . LYS A 1 307 ? 28.087 -12.342 7.027   1.00 56.06  ? 307 LYS A CA  1 
ATOM 2244 C C   . LYS A 1 307 ? 27.922 -11.073 7.848   1.00 47.40  ? 307 LYS A C   1 
ATOM 2245 O O   . LYS A 1 307 ? 28.573 -10.953 8.887   1.00 52.68  ? 307 LYS A O   1 
ATOM 2246 C CB  . LYS A 1 307 ? 27.679 -13.527 7.911   1.00 57.51  ? 307 LYS A CB  1 
ATOM 2247 C CG  . LYS A 1 307 ? 27.630 -14.877 7.216   1.00 49.06  ? 307 LYS A CG  1 
ATOM 2248 C CD  . LYS A 1 307 ? 26.329 -15.119 6.491   1.00 60.12  ? 307 LYS A CD  1 
ATOM 2249 C CE  . LYS A 1 307 ? 26.067 -16.589 6.248   1.00 61.58  ? 307 LYS A CE  1 
ATOM 2250 N NZ  . LYS A 1 307 ? 26.970 -17.445 7.053   1.00 65.01  ? 307 LYS A NZ  1 
ATOM 2251 N N   . TRP A 1 308 ? 27.073 -10.166 7.377   1.00 44.64  ? 308 TRP A N   1 
ATOM 2252 C CA  . TRP A 1 308 ? 26.693 -9.010  8.215   1.00 47.50  ? 308 TRP A CA  1 
ATOM 2253 C C   . TRP A 1 308 ? 25.797 -9.677  9.236   1.00 48.63  ? 308 TRP A C   1 
ATOM 2254 O O   . TRP A 1 308 ? 25.512 -10.860 9.045   1.00 46.43  ? 308 TRP A O   1 
ATOM 2255 C CB  . TRP A 1 308 ? 25.928 -7.980  7.393   1.00 41.99  ? 308 TRP A CB  1 
ATOM 2256 C CG  . TRP A 1 308 ? 26.469 -7.770  6.014   1.00 54.93  ? 308 TRP A CG  1 
ATOM 2257 C CD1 . TRP A 1 308 ? 26.393 -8.629  4.957   1.00 50.80  ? 308 TRP A CD1 1 
ATOM 2258 C CD2 . TRP A 1 308 ? 27.169 -6.610  5.536   1.00 58.89  ? 308 TRP A CD2 1 
ATOM 2259 N NE1 . TRP A 1 308 ? 27.006 -8.090  3.860   1.00 55.05  ? 308 TRP A NE1 1 
ATOM 2260 C CE2 . TRP A 1 308 ? 27.492 -6.852  4.184   1.00 56.11  ? 308 TRP A CE2 1 
ATOM 2261 C CE3 . TRP A 1 308 ? 27.561 -5.401  6.118   1.00 50.59  ? 308 TRP A CE3 1 
ATOM 2262 C CZ2 . TRP A 1 308 ? 28.185 -5.926  3.409   1.00 51.75  ? 308 TRP A CZ2 1 
ATOM 2263 C CZ3 . TRP A 1 308 ? 28.246 -4.487  5.352   1.00 49.95  ? 308 TRP A CZ3 1 
ATOM 2264 C CH2 . TRP A 1 308 ? 28.552 -4.749  4.017   1.00 52.74  ? 308 TRP A CH2 1 
ATOM 2265 N N   . GLY A 1 309 ? 25.369 -9.012  10.292  1.00 50.78  ? 309 GLY A N   1 
ATOM 2266 C CA  . GLY A 1 309 ? 24.496 -9.776  11.198  1.00 48.54  ? 309 GLY A CA  1 
ATOM 2267 C C   . GLY A 1 309 ? 25.253 -10.861 11.936  1.00 50.07  ? 309 GLY A C   1 
ATOM 2268 O O   . GLY A 1 309 ? 26.103 -11.521 11.338  1.00 47.80  ? 309 GLY A O   1 
ATOM 2269 N N   . TYR A 1 310 ? 24.928 -11.073 13.200  1.00 47.98  ? 310 TYR A N   1 
ATOM 2270 C CA  . TYR A 1 310 ? 25.685 -11.999 14.037  1.00 46.57  ? 310 TYR A CA  1 
ATOM 2271 C C   . TYR A 1 310 ? 25.548 -13.436 13.546  1.00 50.93  ? 310 TYR A C   1 
ATOM 2272 O O   . TYR A 1 310 ? 24.437 -13.946 13.372  1.00 47.14  ? 310 TYR A O   1 
ATOM 2273 C CB  . TYR A 1 310 ? 25.214 -11.886 15.487  1.00 54.23  ? 310 TYR A CB  1 
ATOM 2274 C CG  . TYR A 1 310 ? 25.749 -12.962 16.402  1.00 58.45  ? 310 TYR A CG  1 
ATOM 2275 C CD1 . TYR A 1 310 ? 27.115 -13.122 16.596  1.00 56.93  ? 310 TYR A CD1 1 
ATOM 2276 C CD2 . TYR A 1 310 ? 24.886 -13.811 17.083  1.00 56.98  ? 310 TYR A CD2 1 
ATOM 2277 C CE1 . TYR A 1 310 ? 27.607 -14.104 17.436  1.00 57.16  ? 310 TYR A CE1 1 
ATOM 2278 C CE2 . TYR A 1 310 ? 25.368 -14.794 17.925  1.00 56.32  ? 310 TYR A CE2 1 
ATOM 2279 C CZ  . TYR A 1 310 ? 26.729 -14.936 18.098  1.00 59.09  ? 310 TYR A CZ  1 
ATOM 2280 O OH  . TYR A 1 310 ? 27.212 -15.915 18.935  1.00 70.52  ? 310 TYR A OH  1 
ATOM 2281 N N   . ASP A 1 311 ? 26.692 -14.082 13.325  1.00 50.42  ? 311 ASP A N   1 
ATOM 2282 C CA  . ASP A 1 311 ? 26.778 -15.495 12.962  1.00 56.22  ? 311 ASP A CA  1 
ATOM 2283 C C   . ASP A 1 311 ? 27.637 -16.197 14.007  1.00 60.63  ? 311 ASP A C   1 
ATOM 2284 O O   . ASP A 1 311 ? 28.847 -15.956 14.084  1.00 60.53  ? 311 ASP A O   1 
ATOM 2285 C CB  . ASP A 1 311 ? 27.361 -15.664 11.558  1.00 53.38  ? 311 ASP A CB  1 
ATOM 2286 C CG  . ASP A 1 311 ? 27.294 -17.101 11.053  1.00 59.78  ? 311 ASP A CG  1 
ATOM 2287 O OD1 . ASP A 1 311 ? 27.331 -18.044 11.872  1.00 61.66  ? 311 ASP A OD1 1 
ATOM 2288 O OD2 . ASP A 1 311 ? 27.208 -17.288 9.822   1.00 67.15  ? 311 ASP A OD2 1 
ATOM 2289 N N   . LYS A 1 312 ? 27.012 -17.063 14.811  1.00 65.73  ? 312 LYS A N   1 
ATOM 2290 C CA  . LYS A 1 312 ? 27.734 -17.715 15.900  1.00 69.81  ? 312 LYS A CA  1 
ATOM 2291 C C   . LYS A 1 312 ? 28.803 -18.672 15.382  1.00 66.06  ? 312 LYS A C   1 
ATOM 2292 O O   . LYS A 1 312 ? 29.847 -18.837 16.024  1.00 66.32  ? 312 LYS A O   1 
ATOM 2293 C CB  . LYS A 1 312 ? 26.751 -18.457 16.810  1.00 63.67  ? 312 LYS A CB  1 
ATOM 2294 C CG  . LYS A 1 312 ? 27.410 -19.265 17.922  1.00 72.29  ? 312 LYS A CG  1 
ATOM 2295 C CD  . LYS A 1 312 ? 26.421 -20.190 18.621  1.00 81.73  ? 312 LYS A CD  1 
ATOM 2296 C CE  . LYS A 1 312 ? 26.779 -20.361 20.092  1.00 70.06  ? 312 LYS A CE  1 
ATOM 2297 N NZ  . LYS A 1 312 ? 25.834 -21.259 20.811  1.00 50.64  ? 312 LYS A NZ  1 
ATOM 2298 N N   . SER A 1 313 ? 28.572 -19.300 14.227  1.00 59.16  ? 313 SER A N   1 
ATOM 2299 C CA  . SER A 1 313 ? 29.548 -20.215 13.646  1.00 52.32  ? 313 SER A CA  1 
ATOM 2300 C C   . SER A 1 313 ? 30.840 -19.533 13.208  1.00 65.59  ? 313 SER A C   1 
ATOM 2301 O O   . SER A 1 313 ? 31.780 -20.233 12.814  1.00 57.64  ? 313 SER A O   1 
ATOM 2302 C CB  . SER A 1 313 ? 28.931 -20.940 12.448  1.00 56.02  ? 313 SER A CB  1 
ATOM 2303 O OG  . SER A 1 313 ? 28.836 -20.078 11.326  1.00 55.84  ? 313 SER A OG  1 
ATOM 2304 N N   . LEU A 1 314 ? 30.919 -18.203 13.262  1.00 67.04  ? 314 LEU A N   1 
ATOM 2305 C CA  . LEU A 1 314 ? 32.097 -17.474 12.807  1.00 64.27  ? 314 LEU A CA  1 
ATOM 2306 C C   . LEU A 1 314 ? 32.948 -16.928 13.948  1.00 63.18  ? 314 LEU A C   1 
ATOM 2307 O O   . LEU A 1 314 ? 33.901 -16.185 13.691  1.00 70.68  ? 314 LEU A O   1 
ATOM 2308 C CB  . LEU A 1 314 ? 31.675 -16.330 11.880  1.00 58.91  ? 314 LEU A CB  1 
ATOM 2309 C CG  . LEU A 1 314 ? 30.961 -16.718 10.582  1.00 62.86  ? 314 LEU A CG  1 
ATOM 2310 C CD1 . LEU A 1 314 ? 30.604 -15.482 9.770   1.00 51.53  ? 314 LEU A CD1 1 
ATOM 2311 C CD2 . LEU A 1 314 ? 31.809 -17.679 9.760   1.00 60.11  ? 314 LEU A CD2 1 
ATOM 2312 N N   . ASP A 1 315 ? 32.631 -17.272 15.195  1.00 58.14  ? 315 ASP A N   1 
ATOM 2313 C CA  . ASP A 1 315 ? 33.404 -16.779 16.329  1.00 63.39  ? 315 ASP A CA  1 
ATOM 2314 C C   . ASP A 1 315 ? 34.849 -17.261 16.264  1.00 74.00  ? 315 ASP A C   1 
ATOM 2315 O O   . ASP A 1 315 ? 35.131 -18.391 15.855  1.00 69.03  ? 315 ASP A O   1 
ATOM 2316 C CB  . ASP A 1 315 ? 32.757 -17.215 17.642  1.00 62.47  ? 315 ASP A CB  1 
ATOM 2317 C CG  . ASP A 1 315 ? 31.421 -16.545 17.877  1.00 73.32  ? 315 ASP A CG  1 
ATOM 2318 O OD1 . ASP A 1 315 ? 31.071 -15.629 17.101  1.00 73.16  ? 315 ASP A OD1 1 
ATOM 2319 O OD2 . ASP A 1 315 ? 30.721 -16.931 18.836  1.00 79.00  ? 315 ASP A OD2 1 
ATOM 2320 N N   . GLY A 1 316 ? 35.768 -16.386 16.665  1.00 68.44  ? 316 GLY A N   1 
ATOM 2321 C CA  . GLY A 1 316 ? 37.183 -16.666 16.546  1.00 68.44  ? 316 GLY A CA  1 
ATOM 2322 C C   . GLY A 1 316 ? 37.714 -16.529 15.141  1.00 66.93  ? 316 GLY A C   1 
ATOM 2323 O O   . GLY A 1 316 ? 38.876 -16.870 14.893  1.00 64.11  ? 316 GLY A O   1 
ATOM 2324 N N   . LYS A 1 317 ? 36.894 -16.028 14.216  1.00 68.07  ? 317 LYS A N   1 
ATOM 2325 C CA  . LYS A 1 317 ? 37.262 -15.894 12.814  1.00 64.03  ? 317 LYS A CA  1 
ATOM 2326 C C   . LYS A 1 317 ? 36.924 -14.503 12.292  1.00 67.82  ? 317 LYS A C   1 
ATOM 2327 O O   . LYS A 1 317 ? 36.884 -14.294 11.075  1.00 66.05  ? 317 LYS A O   1 
ATOM 2328 C CB  . LYS A 1 317 ? 36.578 -16.972 11.970  1.00 72.12  ? 317 LYS A CB  1 
ATOM 2329 C CG  . LYS A 1 317 ? 36.899 -18.390 12.422  1.00 70.44  ? 317 LYS A CG  1 
ATOM 2330 C CD  . LYS A 1 317 ? 36.237 -19.430 11.538  1.00 72.53  ? 317 LYS A CD  1 
ATOM 2331 C CE  . LYS A 1 317 ? 37.093 -19.754 10.328  1.00 72.52  ? 317 LYS A CE  1 
ATOM 2332 N NZ  . LYS A 1 317 ? 36.331 -19.588 9.061   1.00 78.93  ? 317 LYS A NZ  1 
ATOM 2333 N N   . HIS A 1 318 ? 36.668 -13.555 13.190  1.00 61.50  ? 318 HIS A N   1 
ATOM 2334 C CA  . HIS A 1 318 ? 36.406 -12.189 12.776  1.00 64.08  ? 318 HIS A CA  1 
ATOM 2335 C C   . HIS A 1 318 ? 37.690 -11.565 12.241  1.00 61.32  ? 318 HIS A C   1 
ATOM 2336 O O   . HIS A 1 318 ? 38.801 -11.997 12.561  1.00 61.32  ? 318 HIS A O   1 
ATOM 2337 C CB  . HIS A 1 318 ? 35.869 -11.358 13.945  1.00 64.58  ? 318 HIS A CB  1 
ATOM 2338 C CG  . HIS A 1 318 ? 34.521 -11.789 14.435  1.00 64.10  ? 318 HIS A CG  1 
ATOM 2339 N ND1 . HIS A 1 318 ? 33.759 -11.016 15.285  1.00 63.21  ? 318 HIS A ND1 1 
ATOM 2340 C CD2 . HIS A 1 318 ? 33.799 -12.910 14.200  1.00 63.03  ? 318 HIS A CD2 1 
ATOM 2341 C CE1 . HIS A 1 318 ? 32.627 -11.641 15.552  1.00 57.19  ? 318 HIS A CE1 1 
ATOM 2342 N NE2 . HIS A 1 318 ? 32.626 -12.793 14.906  1.00 61.40  ? 318 HIS A NE2 1 
ATOM 2343 N N   . LYS A 1 319 ? 37.530 -10.543 11.406  1.00 63.65  ? 319 LYS A N   1 
ATOM 2344 C CA  . LYS A 1 319 ? 38.692 -9.875  10.841  1.00 64.47  ? 319 LYS A CA  1 
ATOM 2345 C C   . LYS A 1 319 ? 39.495 -9.182  11.940  1.00 62.68  ? 319 LYS A C   1 
ATOM 2346 O O   . LYS A 1 319 ? 38.990 -8.875  13.023  1.00 62.47  ? 319 LYS A O   1 
ATOM 2347 C CB  . LYS A 1 319 ? 38.265 -8.874  9.768   1.00 56.74  ? 319 LYS A CB  1 
ATOM 2348 C CG  . LYS A 1 319 ? 38.256 -9.459  8.363   1.00 53.06  ? 319 LYS A CG  1 
ATOM 2349 C CD  . LYS A 1 319 ? 36.868 -9.412  7.747   1.00 58.57  ? 319 LYS A CD  1 
ATOM 2350 C CE  . LYS A 1 319 ? 36.860 -10.024 6.352   1.00 70.37  ? 319 LYS A CE  1 
ATOM 2351 N NZ  . LYS A 1 319 ? 35.785 -9.450  5.491   1.00 68.10  ? 319 LYS A NZ  1 
ATOM 2352 N N   . THR A 1 320 ? 40.767 -8.937  11.644  1.00 62.81  ? 320 THR A N   1 
ATOM 2353 C CA  . THR A 1 320 ? 41.701 -8.353  12.591  1.00 62.24  ? 320 THR A CA  1 
ATOM 2354 C C   . THR A 1 320 ? 41.993 -6.907  12.218  1.00 60.04  ? 320 THR A C   1 
ATOM 2355 O O   . THR A 1 320 ? 41.771 -6.477  11.082  1.00 58.22  ? 320 THR A O   1 
ATOM 2356 C CB  . THR A 1 320 ? 43.012 -9.147  12.644  1.00 55.29  ? 320 THR A CB  1 
ATOM 2357 O OG1 . THR A 1 320 ? 43.911 -8.654  11.642  1.00 60.99  ? 320 THR A OG1 1 
ATOM 2358 C CG2 . THR A 1 320 ? 42.754 -10.626 12.411  1.00 59.77  ? 320 THR A CG2 1 
ATOM 2359 N N   . ALA A 1 321 ? 42.470 -6.152  13.214  1.00 63.11  ? 321 ALA A N   1 
ATOM 2360 C CA  . ALA A 1 321 ? 42.785 -4.741  13.007  1.00 62.93  ? 321 ALA A CA  1 
ATOM 2361 C C   . ALA A 1 321 ? 43.689 -4.535  11.799  1.00 64.38  ? 321 ALA A C   1 
ATOM 2362 O O   . ALA A 1 321 ? 43.549 -3.545  11.072  1.00 64.34  ? 321 ALA A O   1 
ATOM 2363 C CB  . ALA A 1 321 ? 43.436 -4.164  14.265  1.00 59.81  ? 321 ALA A CB  1 
ATOM 2364 N N   . ASP A 1 322 ? 44.610 -5.470  11.555  1.00 68.72  ? 322 ASP A N   1 
ATOM 2365 C CA  . ASP A 1 322 ? 45.498 -5.349  10.404  1.00 67.56  ? 322 ASP A CA  1 
ATOM 2366 C C   . ASP A 1 322 ? 44.757 -5.568  9.090   1.00 59.46  ? 322 ASP A C   1 
ATOM 2367 O O   . ASP A 1 322 ? 45.138 -4.995  8.063   1.00 64.89  ? 322 ASP A O   1 
ATOM 2368 C CB  . ASP A 1 322 ? 46.663 -6.329  10.533  1.00 75.22  ? 322 ASP A CB  1 
ATOM 2369 C CG  . ASP A 1 322 ? 47.913 -5.674  11.089  1.00 76.96  ? 322 ASP A CG  1 
ATOM 2370 O OD1 . ASP A 1 322 ? 48.184 -4.509  10.725  1.00 77.06  ? 322 ASP A OD1 1 
ATOM 2371 O OD2 . ASP A 1 322 ? 48.621 -6.320  11.890  1.00 81.17  ? 322 ASP A OD2 1 
ATOM 2372 N N   . GLN A 1 323 ? 43.701 -6.383  9.100   1.00 57.71  ? 323 GLN A N   1 
ATOM 2373 C CA  . GLN A 1 323 ? 42.880 -6.537  7.904   1.00 56.48  ? 323 GLN A CA  1 
ATOM 2374 C C   . GLN A 1 323 ? 42.023 -5.302  7.665   1.00 55.87  ? 323 GLN A C   1 
ATOM 2375 O O   . GLN A 1 323 ? 41.776 -4.924  6.514   1.00 56.41  ? 323 GLN A O   1 
ATOM 2376 C CB  . GLN A 1 323 ? 42.002 -7.781  8.023   1.00 61.66  ? 323 GLN A CB  1 
ATOM 2377 C CG  . GLN A 1 323 ? 42.701 -9.077  7.661   1.00 59.23  ? 323 GLN A CG  1 
ATOM 2378 C CD  . GLN A 1 323 ? 41.966 -10.290 8.187   1.00 57.04  ? 323 GLN A CD  1 
ATOM 2379 O OE1 . GLN A 1 323 ? 41.819 -10.463 9.396   1.00 61.42  ? 323 GLN A OE1 1 
ATOM 2380 N NE2 . GLN A 1 323 ? 41.495 -11.136 7.281   1.00 51.87  ? 323 GLN A NE2 1 
ATOM 2381 N N   . VAL A 1 324 ? 41.546 -4.672  8.741   1.00 54.52  ? 324 VAL A N   1 
ATOM 2382 C CA  . VAL A 1 324 ? 40.790 -3.429  8.608   1.00 59.02  ? 324 VAL A CA  1 
ATOM 2383 C C   . VAL A 1 324 ? 41.660 -2.338  7.995   1.00 58.12  ? 324 VAL A C   1 
ATOM 2384 O O   . VAL A 1 324 ? 41.208 -1.578  7.129   1.00 60.55  ? 324 VAL A O   1 
ATOM 2385 C CB  . VAL A 1 324 ? 40.221 -3.001  9.973   1.00 62.40  ? 324 VAL A CB  1 
ATOM 2386 C CG1 . VAL A 1 324 ? 39.482 -1.680  9.848   1.00 55.82  ? 324 VAL A CG1 1 
ATOM 2387 C CG2 . VAL A 1 324 ? 39.304 -4.081  10.527  1.00 51.31  ? 324 VAL A CG2 1 
ATOM 2388 N N   . MET A 1 325 ? 42.916 -2.233  8.443   1.00 54.94  ? 325 MET A N   1 
ATOM 2389 C CA  . MET A 1 325 ? 43.851 -1.294  7.829   1.00 52.45  ? 325 MET A CA  1 
ATOM 2390 C C   . MET A 1 325 ? 43.967 -1.519  6.327   1.00 57.56  ? 325 MET A C   1 
ATOM 2391 O O   . MET A 1 325 ? 44.026 -0.559  5.550   1.00 56.02  ? 325 MET A O   1 
ATOM 2392 C CB  . MET A 1 325 ? 45.225 -1.410  8.487   1.00 52.42  ? 325 MET A CB  1 
ATOM 2393 C CG  . MET A 1 325 ? 45.214 -1.176  9.979   1.00 63.30  ? 325 MET A CG  1 
ATOM 2394 S SD  . MET A 1 325 ? 44.176 0.234   10.391  1.00 64.74  ? 325 MET A SD  1 
ATOM 2395 C CE  . MET A 1 325 ? 45.422 1.431   10.846  1.00 69.04  ? 325 MET A CE  1 
ATOM 2396 N N   . GLU A 1 326 ? 44.017 -2.782  5.901   1.00 58.65  ? 326 GLU A N   1 
ATOM 2397 C CA  . GLU A 1 326 ? 43.997 -3.078  4.473   1.00 55.52  ? 326 GLU A CA  1 
ATOM 2398 C C   . GLU A 1 326 ? 42.719 -2.557  3.827   1.00 59.01  ? 326 GLU A C   1 
ATOM 2399 O O   . GLU A 1 326 ? 42.767 -1.854  2.811   1.00 62.01  ? 326 GLU A O   1 
ATOM 2400 C CB  . GLU A 1 326 ? 44.151 -4.582  4.246   1.00 66.41  ? 326 GLU A CB  1 
ATOM 2401 C CG  . GLU A 1 326 ? 45.592 -5.028  4.063   1.00 71.84  ? 326 GLU A CG  1 
ATOM 2402 C CD  . GLU A 1 326 ? 46.180 -4.559  2.745   1.00 89.32  ? 326 GLU A CD  1 
ATOM 2403 O OE1 . GLU A 1 326 ? 47.295 -3.994  2.757   1.00 88.25  ? 326 GLU A OE1 1 
ATOM 2404 O OE2 . GLU A 1 326 ? 45.525 -4.753  1.698   1.00 80.57  ? 326 GLU A OE2 1 
ATOM 2405 N N   . MET A 1 327 ? 41.562 -2.895  4.407   1.00 56.16  ? 327 MET A N   1 
ATOM 2406 C CA  . MET A 1 327 ? 40.286 -2.448  3.853   1.00 52.50  ? 327 MET A CA  1 
ATOM 2407 C C   . MET A 1 327 ? 40.237 -0.932  3.737   1.00 60.71  ? 327 MET A C   1 
ATOM 2408 O O   . MET A 1 327 ? 39.776 -0.391  2.724   1.00 58.34  ? 327 MET A O   1 
ATOM 2409 C CB  . MET A 1 327 ? 39.131 -2.943  4.721   1.00 46.56  ? 327 MET A CB  1 
ATOM 2410 C CG  . MET A 1 327 ? 39.013 -4.449  4.807   1.00 64.64  ? 327 MET A CG  1 
ATOM 2411 S SD  . MET A 1 327 ? 37.927 -4.954  6.154   1.00 75.12  ? 327 MET A SD  1 
ATOM 2412 C CE  . MET A 1 327 ? 37.370 -6.536  5.542   1.00 57.43  ? 327 MET A CE  1 
ATOM 2413 N N   . LEU A 1 328 ? 40.699 -0.231  4.774   1.00 58.45  ? 328 LEU A N   1 
ATOM 2414 C CA  . LEU A 1 328 ? 40.749 1.226   4.735   1.00 48.20  ? 328 LEU A CA  1 
ATOM 2415 C C   . LEU A 1 328 ? 41.663 1.712   3.617   1.00 57.56  ? 328 LEU A C   1 
ATOM 2416 O O   . LEU A 1 328 ? 41.286 2.585   2.827   1.00 60.41  ? 328 LEU A O   1 
ATOM 2417 C CB  . LEU A 1 328 ? 41.215 1.760   6.089   1.00 47.09  ? 328 LEU A CB  1 
ATOM 2418 C CG  . LEU A 1 328 ? 40.183 2.543   6.900   1.00 53.99  ? 328 LEU A CG  1 
ATOM 2419 C CD1 . LEU A 1 328 ? 40.739 2.891   8.272   1.00 57.16  ? 328 LEU A CD1 1 
ATOM 2420 C CD2 . LEU A 1 328 ? 39.760 3.798   6.153   1.00 55.25  ? 328 LEU A CD2 1 
ATOM 2421 N N   . SER A 1 329 ? 42.879 1.164   3.550   1.00 60.09  ? 329 SER A N   1 
ATOM 2422 C CA  . SER A 1 329 ? 43.825 1.520   2.495   1.00 61.80  ? 329 SER A CA  1 
ATOM 2423 C C   . SER A 1 329 ? 43.207 1.353   1.110   1.00 64.48  ? 329 SER A C   1 
ATOM 2424 O O   . SER A 1 329 ? 43.184 2.293   0.308   1.00 60.36  ? 329 SER A O   1 
ATOM 2425 C CB  . SER A 1 329 ? 45.091 0.671   2.628   1.00 65.22  ? 329 SER A CB  1 
ATOM 2426 O OG  . SER A 1 329 ? 45.756 0.551   1.381   1.00 69.60  ? 329 SER A OG  1 
ATOM 2427 N N   . LYS A 1 330 ? 42.728 0.141   0.807   1.00 57.40  ? 330 LYS A N   1 
ATOM 2428 C CA  . LYS A 1 330 ? 42.051 -0.109  -0.464  1.00 59.79  ? 330 LYS A CA  1 
ATOM 2429 C C   . LYS A 1 330 ? 40.971 0.930   -0.738  1.00 64.83  ? 330 LYS A C   1 
ATOM 2430 O O   . LYS A 1 330 ? 40.823 1.400   -1.873  1.00 69.35  ? 330 LYS A O   1 
ATOM 2431 C CB  . LYS A 1 330 ? 41.453 -1.518  -0.476  1.00 51.65  ? 330 LYS A CB  1 
ATOM 2432 C CG  . LYS A 1 330 ? 42.459 -2.636  -0.255  1.00 60.41  ? 330 LYS A CG  1 
ATOM 2433 C CD  . LYS A 1 330 ? 42.036 -3.907  -0.979  1.00 64.22  ? 330 LYS A CD  1 
ATOM 2434 C CE  . LYS A 1 330 ? 41.662 -5.008  0.003   1.00 69.66  ? 330 LYS A CE  1 
ATOM 2435 N NZ  . LYS A 1 330 ? 41.667 -6.356  -0.632  1.00 80.31  ? 330 LYS A NZ  1 
ATOM 2436 N N   . ALA A 1 331 ? 40.195 1.292   0.288   1.00 62.57  ? 331 ALA A N   1 
ATOM 2437 C CA  . ALA A 1 331 ? 39.098 2.233   0.091   1.00 63.75  ? 331 ALA A CA  1 
ATOM 2438 C C   . ALA A 1 331 ? 39.609 3.619   -0.290  1.00 67.38  ? 331 ALA A C   1 
ATOM 2439 O O   . ALA A 1 331 ? 39.051 4.264   -1.186  1.00 63.27  ? 331 ALA A O   1 
ATOM 2440 C CB  . ALA A 1 331 ? 38.239 2.305   1.352   1.00 66.12  ? 331 ALA A CB  1 
ATOM 2441 N N   . ASN A 1 332 ? 40.658 4.100   0.384   1.00 68.23  ? 332 ASN A N   1 
ATOM 2442 C CA  . ASN A 1 332 ? 41.204 5.415   0.056   1.00 77.87  ? 332 ASN A CA  1 
ATOM 2443 C C   . ASN A 1 332 ? 41.751 5.446   -1.365  1.00 77.16  ? 332 ASN A C   1 
ATOM 2444 O O   . ASN A 1 332 ? 41.558 6.430   -2.091  1.00 83.07  ? 332 ASN A O   1 
ATOM 2445 C CB  . ASN A 1 332 ? 42.290 5.810   1.057   1.00 88.55  ? 332 ASN A CB  1 
ATOM 2446 C CG  . ASN A 1 332 ? 42.328 7.308   1.316   1.00 97.28  ? 332 ASN A CG  1 
ATOM 2447 O OD1 . ASN A 1 332 ? 42.189 8.113   0.394   1.00 91.58  ? 332 ASN A OD1 1 
ATOM 2448 N ND2 . ASN A 1 332 ? 42.518 7.687   2.574   1.00 99.03  ? 332 ASN A ND2 1 
ATOM 2449 N N   . LYS A 1 333 ? 42.457 4.389   -1.768  1.00 75.31  ? 333 LYS A N   1 
ATOM 2450 C CA  . LYS A 1 333 ? 42.887 4.192   -3.148  1.00 75.67  ? 333 LYS A CA  1 
ATOM 2451 C C   . LYS A 1 333 ? 41.758 4.439   -4.142  1.00 72.06  ? 333 LYS A C   1 
ATOM 2452 O O   . LYS A 1 333 ? 41.972 5.047   -5.196  1.00 78.64  ? 333 LYS A O   1 
ATOM 2453 C CB  . LYS A 1 333 ? 43.438 2.773   -3.328  1.00 81.23  ? 333 LYS A CB  1 
ATOM 2454 C CG  . LYS A 1 333 ? 44.370 2.606   -4.518  1.00 90.01  ? 333 LYS A CG  1 
ATOM 2455 C CD  . LYS A 1 333 ? 43.679 1.872   -5.660  1.00 79.80  ? 333 LYS A CD  1 
ATOM 2456 C CE  . LYS A 1 333 ? 44.181 2.355   -7.012  1.00 85.05  ? 333 LYS A CE  1 
ATOM 2457 N NZ  . LYS A 1 333 ? 43.458 1.704   -8.141  1.00 77.06  ? 333 LYS A NZ  1 
ATOM 2458 N N   . MET A 1 334 ? 40.554 3.982   -3.809  1.00 71.73  ? 334 MET A N   1 
ATOM 2459 C CA  . MET A 1 334 ? 39.408 4.073   -4.701  1.00 68.18  ? 334 MET A CA  1 
ATOM 2460 C C   . MET A 1 334 ? 38.618 5.364   -4.526  1.00 65.00  ? 334 MET A C   1 
ATOM 2461 O O   . MET A 1 334 ? 37.562 5.513   -5.151  1.00 63.65  ? 334 MET A O   1 
ATOM 2462 C CB  . MET A 1 334 ? 38.479 2.873   -4.483  1.00 68.87  ? 334 MET A CB  1 
ATOM 2463 C CG  . MET A 1 334 ? 38.851 1.631   -5.280  1.00 84.44  ? 334 MET A CG  1 
ATOM 2464 S SD  . MET A 1 334 ? 39.252 1.965   -7.007  1.00 107.25 ? 334 MET A SD  1 
ATOM 2465 C CE  . MET A 1 334 ? 37.701 2.647   -7.593  1.00 90.64  ? 334 MET A CE  1 
ATOM 2466 N N   . ASP A 1 335 ? 39.103 6.293   -3.701  1.00 63.70  ? 335 ASP A N   1 
ATOM 2467 C CA  . ASP A 1 335 ? 38.362 7.502   -3.338  1.00 68.80  ? 335 ASP A CA  1 
ATOM 2468 C C   . ASP A 1 335 ? 36.983 7.153   -2.784  1.00 67.72  ? 335 ASP A C   1 
ATOM 2469 O O   . ASP A 1 335 ? 35.960 7.718   -3.179  1.00 71.88  ? 335 ASP A O   1 
ATOM 2470 C CB  . ASP A 1 335 ? 38.249 8.457   -4.527  1.00 69.96  ? 335 ASP A CB  1 
ATOM 2471 C CG  . ASP A 1 335 ? 38.337 9.912   -4.114  1.00 67.82  ? 335 ASP A CG  1 
ATOM 2472 O OD1 . ASP A 1 335 ? 39.151 10.226  -3.221  1.00 68.64  ? 335 ASP A OD1 1 
ATOM 2473 O OD2 . ASP A 1 335 ? 37.589 10.738  -4.679  1.00 74.09  ? 335 ASP A OD2 1 
ATOM 2474 N N   . ALA A 1 336 ? 36.961 6.200   -1.856  1.00 57.68  ? 336 ALA A N   1 
ATOM 2475 C CA  . ALA A 1 336 ? 35.724 5.717   -1.267  1.00 56.04  ? 336 ALA A CA  1 
ATOM 2476 C C   . ALA A 1 336 ? 35.838 5.702   0.249   1.00 58.41  ? 336 ALA A C   1 
ATOM 2477 O O   . ALA A 1 336 ? 36.930 5.554   0.806   1.00 56.19  ? 336 ALA A O   1 
ATOM 2478 C CB  . ALA A 1 336 ? 35.376 4.309   -1.768  1.00 61.85  ? 336 ALA A CB  1 
ATOM 2479 N N   . ASN A 1 337 ? 34.696 5.854   0.913   1.00 54.74  ? 337 ASN A N   1 
ATOM 2480 C CA  . ASN A 1 337 ? 34.644 5.622   2.345   1.00 46.80  ? 337 ASN A CA  1 
ATOM 2481 C C   . ASN A 1 337 ? 34.670 4.123   2.623   1.00 50.65  ? 337 ASN A C   1 
ATOM 2482 O O   . ASN A 1 337 ? 34.399 3.296   1.748   1.00 49.37  ? 337 ASN A O   1 
ATOM 2483 C CB  . ASN A 1 337 ? 33.377 6.225   2.955   1.00 44.30  ? 337 ASN A CB  1 
ATOM 2484 C CG  . ASN A 1 337 ? 33.366 7.740   2.917   1.00 51.22  ? 337 ASN A CG  1 
ATOM 2485 O OD1 . ASN A 1 337 ? 34.358 8.374   2.559   1.00 49.66  ? 337 ASN A OD1 1 
ATOM 2486 N ND2 . ASN A 1 337 ? 32.236 8.329   3.293   1.00 44.56  ? 337 ASN A ND2 1 
ATOM 2487 N N   . LEU A 1 338 ? 35.003 3.775   3.859   1.00 49.51  ? 338 LEU A N   1 
ATOM 2488 C CA  . LEU A 1 338 ? 34.823 2.419   4.356   1.00 40.50  ? 338 LEU A CA  1 
ATOM 2489 C C   . LEU A 1 338 ? 33.732 2.451   5.416   1.00 41.58  ? 338 LEU A C   1 
ATOM 2490 O O   . LEU A 1 338 ? 33.893 3.093   6.459   1.00 41.30  ? 338 LEU A O   1 
ATOM 2491 C CB  . LEU A 1 338 ? 36.123 1.850   4.923   1.00 42.85  ? 338 LEU A CB  1 
ATOM 2492 C CG  . LEU A 1 338 ? 35.976 0.566   5.743   1.00 41.55  ? 338 LEU A CG  1 
ATOM 2493 C CD1 . LEU A 1 338 ? 35.625 -0.604  4.839   1.00 40.46  ? 338 LEU A CD1 1 
ATOM 2494 C CD2 . LEU A 1 338 ? 37.248 0.270   6.521   1.00 39.79  ? 338 LEU A CD2 1 
ATOM 2495 N N   . LEU A 1 339 ? 32.620 1.779   5.139   1.00 39.34  ? 339 LEU A N   1 
ATOM 2496 C CA  . LEU A 1 339 ? 31.545 1.600   6.109   1.00 41.77  ? 339 LEU A CA  1 
ATOM 2497 C C   . LEU A 1 339 ? 31.662 0.173   6.636   1.00 43.43  ? 339 LEU A C   1 
ATOM 2498 O O   . LEU A 1 339 ? 31.239 -0.782  5.980   1.00 36.40  ? 339 LEU A O   1 
ATOM 2499 C CB  . LEU A 1 339 ? 30.190 1.882   5.468   1.00 38.10  ? 339 LEU A CB  1 
ATOM 2500 C CG  . LEU A 1 339 ? 28.914 1.476   6.204   1.00 32.80  ? 339 LEU A CG  1 
ATOM 2501 C CD1 . LEU A 1 339 ? 28.781 2.268   7.486   1.00 39.38  ? 339 LEU A CD1 1 
ATOM 2502 C CD2 . LEU A 1 339 ? 27.706 1.703   5.311   1.00 25.42  ? 339 LEU A CD2 1 
ATOM 2503 N N   . LEU A 1 340 ? 32.236 0.030   7.827   1.00 40.83  ? 340 LEU A N   1 
ATOM 2504 C CA  . LEU A 1 340 ? 32.605 -1.270  8.371   1.00 45.70  ? 340 LEU A CA  1 
ATOM 2505 C C   . LEU A 1 340 ? 31.551 -1.719  9.374   1.00 42.89  ? 340 LEU A C   1 
ATOM 2506 O O   . LEU A 1 340 ? 31.155 -0.947  10.254  1.00 46.93  ? 340 LEU A O   1 
ATOM 2507 C CB  . LEU A 1 340 ? 33.985 -1.205  9.026   1.00 49.43  ? 340 LEU A CB  1 
ATOM 2508 C CG  . LEU A 1 340 ? 34.511 -2.489  9.661   1.00 42.67  ? 340 LEU A CG  1 
ATOM 2509 C CD1 . LEU A 1 340 ? 34.497 -3.620  8.648   1.00 47.14  ? 340 LEU A CD1 1 
ATOM 2510 C CD2 . LEU A 1 340 ? 35.915 -2.263  10.188  1.00 38.59  ? 340 LEU A CD2 1 
ATOM 2511 N N   . ASN A 1 341 ? 31.107 -2.966  9.240   1.00 43.49  ? 341 ASN A N   1 
ATOM 2512 C CA  . ASN A 1 341 ? 29.915 -3.461  9.915   1.00 45.20  ? 341 ASN A CA  1 
ATOM 2513 C C   . ASN A 1 341 ? 30.237 -4.231  11.189  1.00 46.78  ? 341 ASN A C   1 
ATOM 2514 O O   . ASN A 1 341 ? 31.184 -5.023  11.232  1.00 48.46  ? 341 ASN A O   1 
ATOM 2515 C CB  . ASN A 1 341 ? 29.107 -4.359  8.976   1.00 45.98  ? 341 ASN A CB  1 
ATOM 2516 C CG  . ASN A 1 341 ? 27.977 -5.074  9.687   1.00 49.00  ? 341 ASN A CG  1 
ATOM 2517 O OD1 . ASN A 1 341 ? 26.909 -4.503  9.910   1.00 48.99  ? 341 ASN A OD1 1 
ATOM 2518 N ND2 . ASN A 1 341 ? 28.207 -6.331  10.054  1.00 44.41  ? 341 ASN A ND2 1 
ATOM 2519 N N   . VAL A 1 342 ? 29.434 -3.994  12.227  1.00 47.35  ? 342 VAL A N   1 
ATOM 2520 C CA  . VAL A 1 342 ? 29.329 -4.882  13.379  1.00 49.84  ? 342 VAL A CA  1 
ATOM 2521 C C   . VAL A 1 342 ? 27.907 -5.429  13.447  1.00 46.90  ? 342 VAL A C   1 
ATOM 2522 O O   . VAL A 1 342 ? 26.934 -4.696  13.233  1.00 46.62  ? 342 VAL A O   1 
ATOM 2523 C CB  . VAL A 1 342 ? 29.714 -4.180  14.700  1.00 40.94  ? 342 VAL A CB  1 
ATOM 2524 C CG1 . VAL A 1 342 ? 31.169 -3.747  14.664  1.00 41.87  ? 342 VAL A CG1 1 
ATOM 2525 C CG2 . VAL A 1 342 ? 28.807 -2.988  14.975  1.00 46.23  ? 342 VAL A CG2 1 
ATOM 2526 N N   . GLY A 1 343 ? 27.793 -6.727  13.716  1.00 51.02  ? 343 GLY A N   1 
ATOM 2527 C CA  . GLY A 1 343 ? 26.517 -7.355  13.961  1.00 47.68  ? 343 GLY A CA  1 
ATOM 2528 C C   . GLY A 1 343 ? 26.392 -7.780  15.411  1.00 39.77  ? 343 GLY A C   1 
ATOM 2529 O O   . GLY A 1 343 ? 26.979 -8.778  15.837  1.00 50.84  ? 343 GLY A O   1 
ATOM 2530 N N   . PRO A 1 344 ? 25.635 -7.018  16.200  1.00 49.02  ? 344 PRO A N   1 
ATOM 2531 C CA  . PRO A 1 344 ? 25.592 -7.257  17.648  1.00 54.48  ? 344 PRO A CA  1 
ATOM 2532 C C   . PRO A 1 344 ? 25.078 -8.644  18.014  1.00 48.50  ? 344 PRO A C   1 
ATOM 2533 O O   . PRO A 1 344 ? 24.459 -9.350  17.215  1.00 41.71  ? 344 PRO A O   1 
ATOM 2534 C CB  . PRO A 1 344 ? 24.640 -6.168  18.157  1.00 48.14  ? 344 PRO A CB  1 
ATOM 2535 C CG  . PRO A 1 344 ? 24.755 -5.079  17.149  1.00 47.13  ? 344 PRO A CG  1 
ATOM 2536 C CD  . PRO A 1 344 ? 24.933 -5.777  15.828  1.00 50.97  ? 344 PRO A CD  1 
ATOM 2537 N N   . LEU A 1 345 ? 25.345 -9.018  19.265  1.00 46.42  ? 345 LEU A N   1 
ATOM 2538 C CA  . LEU A 1 345 ? 24.893 -10.267 19.855  1.00 45.71  ? 345 LEU A CA  1 
ATOM 2539 C C   . LEU A 1 345 ? 23.414 -10.169 20.223  1.00 51.39  ? 345 LEU A C   1 
ATOM 2540 O O   . LEU A 1 345 ? 22.871 -9.067  20.336  1.00 49.74  ? 345 LEU A O   1 
ATOM 2541 C CB  . LEU A 1 345 ? 25.731 -10.582 21.093  1.00 42.89  ? 345 LEU A CB  1 
ATOM 2542 C CG  . LEU A 1 345 ? 26.920 -11.537 20.954  1.00 44.40  ? 345 LEU A CG  1 
ATOM 2543 C CD1 . LEU A 1 345 ? 27.681 -11.298 19.660  1.00 56.52  ? 345 LEU A CD1 1 
ATOM 2544 C CD2 . LEU A 1 345 ? 27.847 -11.402 22.153  1.00 42.28  ? 345 LEU A CD2 1 
ATOM 2545 N N   . PRO A 1 346 ? 22.731 -11.312 20.393  1.00 48.46  ? 346 PRO A N   1 
ATOM 2546 C CA  . PRO A 1 346 ? 21.269 -11.279 20.593  1.00 44.79  ? 346 PRO A CA  1 
ATOM 2547 C C   . PRO A 1 346 ? 20.792 -10.300 21.655  1.00 45.22  ? 346 PRO A C   1 
ATOM 2548 O O   . PRO A 1 346 ? 19.675 -9.779  21.542  1.00 42.34  ? 346 PRO A O   1 
ATOM 2549 C CB  . PRO A 1 346 ? 20.947 -12.727 20.985  1.00 45.22  ? 346 PRO A CB  1 
ATOM 2550 C CG  . PRO A 1 346 ? 21.985 -13.525 20.300  1.00 49.49  ? 346 PRO A CG  1 
ATOM 2551 C CD  . PRO A 1 346 ? 23.238 -12.697 20.340  1.00 48.11  ? 346 PRO A CD  1 
ATOM 2552 N N   . ASP A 1 347 ? 21.601 -10.026 22.678  1.00 47.27  ? 347 ASP A N   1 
ATOM 2553 C CA  . ASP A 1 347 ? 21.196 -9.104  23.731  1.00 48.76  ? 347 ASP A CA  1 
ATOM 2554 C C   . ASP A 1 347 ? 21.391 -7.645  23.342  1.00 53.21  ? 347 ASP A C   1 
ATOM 2555 O O   . ASP A 1 347 ? 20.928 -6.759  24.068  1.00 56.62  ? 347 ASP A O   1 
ATOM 2556 C CB  . ASP A 1 347 ? 21.967 -9.400  25.022  1.00 50.36  ? 347 ASP A CB  1 
ATOM 2557 C CG  . ASP A 1 347 ? 23.470 -9.224  24.865  1.00 50.30  ? 347 ASP A CG  1 
ATOM 2558 O OD1 . ASP A 1 347 ? 23.944 -9.051  23.722  1.00 49.41  ? 347 ASP A OD1 1 
ATOM 2559 O OD2 . ASP A 1 347 ? 24.181 -9.260  25.893  1.00 46.04  ? 347 ASP A OD2 1 
ATOM 2560 N N   . GLY A 1 348 ? 22.065 -7.378  22.227  1.00 47.22  ? 348 GLY A N   1 
ATOM 2561 C CA  . GLY A 1 348 ? 22.353 -6.029  21.795  1.00 45.26  ? 348 GLY A CA  1 
ATOM 2562 C C   . GLY A 1 348 ? 23.761 -5.566  22.082  1.00 46.71  ? 348 GLY A C   1 
ATOM 2563 O O   . GLY A 1 348 ? 24.096 -4.420  21.761  1.00 53.59  ? 348 GLY A O   1 
ATOM 2564 N N   . SER A 1 349 ? 24.602 -6.426  22.646  1.00 44.25  ? 349 SER A N   1 
ATOM 2565 C CA  . SER A 1 349 ? 25.976 -6.076  22.961  1.00 42.36  ? 349 SER A CA  1 
ATOM 2566 C C   . SER A 1 349 ? 26.881 -6.378  21.774  1.00 43.73  ? 349 SER A C   1 
ATOM 2567 O O   . SER A 1 349 ? 26.610 -7.275  20.971  1.00 40.64  ? 349 SER A O   1 
ATOM 2568 C CB  . SER A 1 349 ? 26.458 -6.834  24.199  1.00 38.96  ? 349 SER A CB  1 
ATOM 2569 O OG  . SER A 1 349 ? 26.596 -8.218  23.928  1.00 42.48  ? 349 SER A OG  1 
ATOM 2570 N N   . ILE A 1 350 ? 27.958 -5.608  21.665  1.00 48.52  ? 350 ILE A N   1 
ATOM 2571 C CA  . ILE A 1 350 ? 28.906 -5.776  20.571  1.00 54.11  ? 350 ILE A CA  1 
ATOM 2572 C C   . ILE A 1 350 ? 29.828 -6.949  20.874  1.00 50.87  ? 350 ILE A C   1 
ATOM 2573 O O   . ILE A 1 350 ? 30.292 -7.121  22.008  1.00 66.74  ? 350 ILE A O   1 
ATOM 2574 C CB  . ILE A 1 350 ? 29.702 -4.478  20.342  1.00 45.11  ? 350 ILE A CB  1 
ATOM 2575 C CG1 . ILE A 1 350 ? 28.752 -3.311  20.075  1.00 43.14  ? 350 ILE A CG1 1 
ATOM 2576 C CG2 . ILE A 1 350 ? 30.651 -4.635  19.169  1.00 46.34  ? 350 ILE A CG2 1 
ATOM 2577 C CD1 . ILE A 1 350 ? 27.642 -3.631  19.093  1.00 49.85  ? 350 ILE A CD1 1 
ATOM 2578 N N   . HIS A 1 351 ? 30.068 -7.773  19.857  1.00 48.71  ? 351 HIS A N   1 
ATOM 2579 C CA  . HIS A 1 351 ? 30.946 -8.928  19.984  1.00 55.05  ? 351 HIS A CA  1 
ATOM 2580 C C   . HIS A 1 351 ? 32.283 -8.515  20.599  1.00 57.78  ? 351 HIS A C   1 
ATOM 2581 O O   . HIS A 1 351 ? 32.819 -7.451  20.259  1.00 54.82  ? 351 HIS A O   1 
ATOM 2582 C CB  . HIS A 1 351 ? 31.163 -9.563  18.607  1.00 60.44  ? 351 HIS A CB  1 
ATOM 2583 C CG  . HIS A 1 351 ? 31.614 -10.989 18.655  1.00 69.91  ? 351 HIS A CG  1 
ATOM 2584 N ND1 . HIS A 1 351 ? 32.928 -11.347 18.867  1.00 66.75  ? 351 HIS A ND1 1 
ATOM 2585 C CD2 . HIS A 1 351 ? 30.928 -12.147 18.507  1.00 63.19  ? 351 HIS A CD2 1 
ATOM 2586 C CE1 . HIS A 1 351 ? 33.031 -12.664 18.852  1.00 62.27  ? 351 HIS A CE1 1 
ATOM 2587 N NE2 . HIS A 1 351 ? 31.831 -13.173 18.636  1.00 59.68  ? 351 HIS A NE2 1 
ATOM 2588 N N   . PRO A 1 352 ? 32.849 -9.318  21.504  1.00 60.72  ? 352 PRO A N   1 
ATOM 2589 C CA  . PRO A 1 352 ? 34.149 -8.951  22.092  1.00 54.61  ? 352 PRO A CA  1 
ATOM 2590 C C   . PRO A 1 352 ? 35.285 -8.924  21.086  1.00 61.92  ? 352 PRO A C   1 
ATOM 2591 O O   . PRO A 1 352 ? 36.232 -8.147  21.258  1.00 59.77  ? 352 PRO A O   1 
ATOM 2592 C CB  . PRO A 1 352 ? 34.371 -10.030 23.164  1.00 52.65  ? 352 PRO A CB  1 
ATOM 2593 C CG  . PRO A 1 352 ? 33.035 -10.692 23.354  1.00 56.94  ? 352 PRO A CG  1 
ATOM 2594 C CD  . PRO A 1 352 ? 32.340 -10.591 22.037  1.00 61.31  ? 352 PRO A CD  1 
ATOM 2595 N N   . GLU A 1 353 ? 35.224 -9.751  20.040  1.00 60.46  ? 353 GLU A N   1 
ATOM 2596 C CA  . GLU A 1 353 ? 36.264 -9.719  19.017  1.00 58.42  ? 353 GLU A CA  1 
ATOM 2597 C C   . GLU A 1 353 ? 36.252 -8.398  18.261  1.00 59.24  ? 353 GLU A C   1 
ATOM 2598 O O   . GLU A 1 353 ? 37.310 -7.812  18.003  1.00 69.04  ? 353 GLU A O   1 
ATOM 2599 C CB  . GLU A 1 353 ? 36.080 -10.882 18.044  1.00 67.33  ? 353 GLU A CB  1 
ATOM 2600 C CG  . GLU A 1 353 ? 36.848 -12.136 18.402  1.00 60.37  ? 353 GLU A CG  1 
ATOM 2601 C CD  . GLU A 1 353 ? 36.457 -13.309 17.531  1.00 65.96  ? 353 GLU A CD  1 
ATOM 2602 O OE1 . GLU A 1 353 ? 36.814 -13.307 16.333  1.00 62.78  ? 353 GLU A OE1 1 
ATOM 2603 O OE2 . GLU A 1 353 ? 35.781 -14.226 18.043  1.00 72.49  ? 353 GLU A OE2 1 
ATOM 2604 N N   . ASP A 1 354 ? 35.062 -7.920  17.892  1.00 61.48  ? 354 ASP A N   1 
ATOM 2605 C CA  . ASP A 1 354 ? 34.960 -6.670  17.150  1.00 55.41  ? 354 ASP A CA  1 
ATOM 2606 C C   . ASP A 1 354 ? 35.298 -5.464  18.018  1.00 57.29  ? 354 ASP A C   1 
ATOM 2607 O O   . ASP A 1 354 ? 35.865 -4.486  17.519  1.00 54.72  ? 354 ASP A O   1 
ATOM 2608 C CB  . ASP A 1 354 ? 33.556 -6.534  16.561  1.00 54.70  ? 354 ASP A CB  1 
ATOM 2609 C CG  . ASP A 1 354 ? 33.260 -7.590  15.508  1.00 59.78  ? 354 ASP A CG  1 
ATOM 2610 O OD1 . ASP A 1 354 ? 34.121 -8.467  15.286  1.00 63.61  ? 354 ASP A OD1 1 
ATOM 2611 O OD2 . ASP A 1 354 ? 32.166 -7.548  14.907  1.00 64.04  ? 354 ASP A OD2 1 
ATOM 2612 N N   . VAL A 1 355 ? 34.963 -5.515  19.310  1.00 57.67  ? 355 VAL A N   1 
ATOM 2613 C CA  . VAL A 1 355 ? 35.293 -4.416  20.218  1.00 54.15  ? 355 VAL A CA  1 
ATOM 2614 C C   . VAL A 1 355 ? 36.802 -4.209  20.280  1.00 60.89  ? 355 VAL A C   1 
ATOM 2615 O O   . VAL A 1 355 ? 37.298 -3.083  20.150  1.00 62.13  ? 355 VAL A O   1 
ATOM 2616 C CB  . VAL A 1 355 ? 34.699 -4.674  21.615  1.00 50.59  ? 355 VAL A CB  1 
ATOM 2617 C CG1 . VAL A 1 355 ? 35.465 -3.894  22.671  1.00 42.65  ? 355 VAL A CG1 1 
ATOM 2618 C CG2 . VAL A 1 355 ? 33.229 -4.299  21.643  1.00 55.85  ? 355 VAL A CG2 1 
ATOM 2619 N N   . LYS A 1 356 ? 37.554 -5.294  20.487  1.00 56.90  ? 356 LYS A N   1 
ATOM 2620 C CA  . LYS A 1 356 ? 39.012 -5.203  20.502  1.00 59.24  ? 356 LYS A CA  1 
ATOM 2621 C C   . LYS A 1 356 ? 39.529 -4.746  19.142  1.00 63.16  ? 356 LYS A C   1 
ATOM 2622 O O   . LYS A 1 356 ? 40.323 -3.801  19.060  1.00 69.40  ? 356 LYS A O   1 
ATOM 2623 C CB  . LYS A 1 356 ? 39.603 -6.561  20.920  1.00 61.39  ? 356 LYS A CB  1 
ATOM 2624 C CG  . LYS A 1 356 ? 40.923 -7.086  20.270  1.00 78.12  ? 356 LYS A CG  1 
ATOM 2625 C CD  . LYS A 1 356 ? 42.096 -6.107  20.115  1.00 80.68  ? 356 LYS A CD  1 
ATOM 2626 C CE  . LYS A 1 356 ? 43.326 -6.837  19.591  1.00 78.20  ? 356 LYS A CE  1 
ATOM 2627 N NZ  . LYS A 1 356 ? 43.161 -7.196  18.153  1.00 84.61  ? 356 LYS A NZ  1 
ATOM 2628 N N   . THR A 1 357 ? 39.088 -5.405  18.065  1.00 60.38  ? 357 THR A N   1 
ATOM 2629 C CA  . THR A 1 357 ? 39.542 -5.040  16.725  1.00 62.77  ? 357 THR A CA  1 
ATOM 2630 C C   . THR A 1 357 ? 39.384 -3.545  16.483  1.00 54.02  ? 357 THR A C   1 
ATOM 2631 O O   . THR A 1 357 ? 40.312 -2.876  16.019  1.00 59.55  ? 357 THR A O   1 
ATOM 2632 C CB  . THR A 1 357 ? 38.774 -5.838  15.669  1.00 62.30  ? 357 THR A CB  1 
ATOM 2633 O OG1 . THR A 1 357 ? 39.031 -7.238  15.840  1.00 63.57  ? 357 THR A OG1 1 
ATOM 2634 C CG2 . THR A 1 357 ? 39.206 -5.420  14.271  1.00 59.97  ? 357 THR A CG2 1 
ATOM 2635 N N   . LEU A 1 358 ? 38.214 -2.998  16.819  1.00 59.26  ? 358 LEU A N   1 
ATOM 2636 C CA  . LEU A 1 358 ? 37.970 -1.578  16.592  1.00 59.32  ? 358 LEU A CA  1 
ATOM 2637 C C   . LEU A 1 358 ? 38.793 -0.716  17.541  1.00 59.24  ? 358 LEU A C   1 
ATOM 2638 O O   . LEU A 1 358 ? 39.247 0.371   17.164  1.00 58.93  ? 358 LEU A O   1 
ATOM 2639 C CB  . LEU A 1 358 ? 36.480 -1.277  16.732  1.00 53.20  ? 358 LEU A CB  1 
ATOM 2640 C CG  . LEU A 1 358 ? 35.640 -1.931  15.634  1.00 56.13  ? 358 LEU A CG  1 
ATOM 2641 C CD1 . LEU A 1 358 ? 34.155 -1.839  15.946  1.00 54.36  ? 358 LEU A CD1 1 
ATOM 2642 C CD2 . LEU A 1 358 ? 35.957 -1.308  14.284  1.00 48.49  ? 358 LEU A CD2 1 
ATOM 2643 N N   . ALA A 1 359 ? 38.997 -1.182  18.776  1.00 58.12  ? 359 ALA A N   1 
ATOM 2644 C CA  . ALA A 1 359 ? 39.786 -0.412  19.732  1.00 57.76  ? 359 ALA A CA  1 
ATOM 2645 C C   . ALA A 1 359 ? 41.218 -0.245  19.246  1.00 64.18  ? 359 ALA A C   1 
ATOM 2646 O O   . ALA A 1 359 ? 41.830 0.812   19.439  1.00 74.93  ? 359 ALA A O   1 
ATOM 2647 C CB  . ALA A 1 359 ? 39.757 -1.082  21.106  1.00 56.76  ? 359 ALA A CB  1 
ATOM 2648 N N   . GLU A 1 360 ? 41.768 -1.277  18.606  1.00 59.01  ? 360 GLU A N   1 
ATOM 2649 C CA  . GLU A 1 360 ? 43.144 -1.203  18.136  1.00 64.71  ? 360 GLU A CA  1 
ATOM 2650 C C   . GLU A 1 360 ? 43.252 -0.435  16.824  1.00 67.63  ? 360 GLU A C   1 
ATOM 2651 O O   . GLU A 1 360 ? 44.221 0.303   16.620  1.00 77.24  ? 360 GLU A O   1 
ATOM 2652 C CB  . GLU A 1 360 ? 43.719 -2.613  17.982  1.00 82.77  ? 360 GLU A CB  1 
ATOM 2653 C CG  . GLU A 1 360 ? 45.178 -2.656  17.562  1.00 86.92  ? 360 GLU A CG  1 
ATOM 2654 C CD  . GLU A 1 360 ? 46.132 -2.265  18.676  1.00 93.67  ? 360 GLU A CD  1 
ATOM 2655 O OE1 . GLU A 1 360 ? 45.679 -2.101  19.829  1.00 90.53  ? 360 GLU A OE1 1 
ATOM 2656 O OE2 . GLU A 1 360 ? 47.341 -2.118  18.398  1.00 100.18 ? 360 GLU A OE2 1 
ATOM 2657 N N   . VAL A 1 361 ? 42.261 -0.573  15.935  1.00 59.54  ? 361 VAL A N   1 
ATOM 2658 C CA  . VAL A 1 361 ? 42.237 0.239   14.717  1.00 63.76  ? 361 VAL A CA  1 
ATOM 2659 C C   . VAL A 1 361 ? 42.287 1.718   15.070  1.00 63.86  ? 361 VAL A C   1 
ATOM 2660 O O   . VAL A 1 361 ? 42.918 2.522   14.372  1.00 63.76  ? 361 VAL A O   1 
ATOM 2661 C CB  . VAL A 1 361 ? 41.001 -0.098  13.861  1.00 66.72  ? 361 VAL A CB  1 
ATOM 2662 C CG1 . VAL A 1 361 ? 40.883 0.867   12.689  1.00 67.33  ? 361 VAL A CG1 1 
ATOM 2663 C CG2 . VAL A 1 361 ? 41.089 -1.517  13.344  1.00 63.86  ? 361 VAL A CG2 1 
ATOM 2664 N N   . GLY A 1 362 ? 41.635 2.097   16.169  1.00 61.99  ? 362 GLY A N   1 
ATOM 2665 C CA  . GLY A 1 362 ? 41.690 3.480   16.603  1.00 58.97  ? 362 GLY A CA  1 
ATOM 2666 C C   . GLY A 1 362 ? 43.090 3.902   17.003  1.00 68.89  ? 362 GLY A C   1 
ATOM 2667 O O   . GLY A 1 362 ? 43.549 4.983   16.635  1.00 68.49  ? 362 GLY A O   1 
ATOM 2668 N N   . ARG A 1 363 ? 43.805 3.037   17.726  1.00 74.54  ? 363 ARG A N   1 
ATOM 2669 C CA  . ARG A 1 363 ? 45.135 3.407   18.201  1.00 76.27  ? 363 ARG A CA  1 
ATOM 2670 C C   . ARG A 1 363 ? 46.138 3.471   17.055  1.00 70.45  ? 363 ARG A C   1 
ATOM 2671 O O   . ARG A 1 363 ? 46.979 4.376   17.010  1.00 74.30  ? 363 ARG A O   1 
ATOM 2672 C CB  . ARG A 1 363 ? 45.611 2.413   19.260  1.00 73.15  ? 363 ARG A CB  1 
ATOM 2673 C CG  . ARG A 1 363 ? 44.656 2.225   20.425  1.00 71.78  ? 363 ARG A CG  1 
ATOM 2674 C CD  . ARG A 1 363 ? 45.351 1.528   21.586  1.00 81.94  ? 363 ARG A CD  1 
ATOM 2675 N NE  . ARG A 1 363 ? 45.250 0.077   21.487  1.00 82.19  ? 363 ARG A NE  1 
ATOM 2676 C CZ  . ARG A 1 363 ? 44.453 -0.673  22.235  1.00 83.04  ? 363 ARG A CZ  1 
ATOM 2677 N NH1 . ARG A 1 363 ? 43.551 -0.134  23.040  1.00 88.57  ? 363 ARG A NH1 1 
ATOM 2678 N NH2 . ARG A 1 363 ? 44.523 -1.998  22.132  1.00 90.20  ? 363 ARG A NH2 1 
ATOM 2679 N N   . LYS A 1 364 ? 46.066 2.519   16.120  1.00 64.91  ? 364 LYS A N   1 
ATOM 2680 C CA  . LYS A 1 364 ? 46.906 2.584   14.928  1.00 72.94  ? 364 LYS A CA  1 
ATOM 2681 C C   . LYS A 1 364 ? 46.629 3.832   14.099  1.00 69.26  ? 364 LYS A C   1 
ATOM 2682 O O   . LYS A 1 364 ? 47.549 4.379   13.478  1.00 69.81  ? 364 LYS A O   1 
ATOM 2683 C CB  . LYS A 1 364 ? 46.706 1.334   14.070  1.00 68.46  ? 364 LYS A CB  1 
ATOM 2684 C CG  . LYS A 1 364 ? 46.674 0.023   14.833  1.00 71.33  ? 364 LYS A CG  1 
ATOM 2685 C CD  . LYS A 1 364 ? 47.845 -0.873  14.468  1.00 87.45  ? 364 LYS A CD  1 
ATOM 2686 C CE  . LYS A 1 364 ? 47.770 -2.197  15.213  1.00 81.23  ? 364 LYS A CE  1 
ATOM 2687 N NZ  . LYS A 1 364 ? 48.427 -3.305  14.470  1.00 80.71  ? 364 LYS A NZ  1 
ATOM 2688 N N   . LEU A 1 365 ? 45.379 4.300   14.075  1.00 71.31  ? 365 LEU A N   1 
ATOM 2689 C CA  . LEU A 1 365 ? 45.025 5.427   13.216  1.00 73.53  ? 365 LEU A CA  1 
ATOM 2690 C C   . LEU A 1 365 ? 45.549 6.747   13.773  1.00 65.79  ? 365 LEU A C   1 
ATOM 2691 O O   . LEU A 1 365 ? 46.126 7.553   13.035  1.00 66.21  ? 365 LEU A O   1 
ATOM 2692 C CB  . LEU A 1 365 ? 43.511 5.483   13.016  1.00 64.36  ? 365 LEU A CB  1 
ATOM 2693 C CG  . LEU A 1 365 ? 42.990 4.601   11.877  1.00 62.50  ? 365 LEU A CG  1 
ATOM 2694 C CD1 . LEU A 1 365 ? 41.547 4.941   11.544  1.00 55.69  ? 365 LEU A CD1 1 
ATOM 2695 C CD2 . LEU A 1 365 ? 43.874 4.730   10.644  1.00 55.81  ? 365 LEU A CD2 1 
ATOM 2696 N N   . LYS A 1 366 ? 45.366 6.987   15.073  1.00 67.25  ? 366 LYS A N   1 
ATOM 2697 C CA  . LYS A 1 366 ? 45.840 8.237   15.660  1.00 74.60  ? 366 LYS A CA  1 
ATOM 2698 C C   . LYS A 1 366 ? 47.359 8.310   15.749  1.00 76.40  ? 366 LYS A C   1 
ATOM 2699 O O   . LYS A 1 366 ? 47.884 9.284   16.302  1.00 73.61  ? 366 LYS A O   1 
ATOM 2700 C CB  . LYS A 1 366 ? 45.226 8.441   17.048  1.00 77.70  ? 366 LYS A CB  1 
ATOM 2701 C CG  . LYS A 1 366 ? 43.828 7.868   17.190  1.00 75.14  ? 366 LYS A CG  1 
ATOM 2702 C CD  . LYS A 1 366 ? 42.900 8.754   17.999  1.00 72.16  ? 366 LYS A CD  1 
ATOM 2703 C CE  . LYS A 1 366 ? 41.543 8.085   18.177  1.00 64.66  ? 366 LYS A CE  1 
ATOM 2704 N NZ  . LYS A 1 366 ? 41.408 7.443   19.515  1.00 56.68  ? 366 LYS A NZ  1 
ATOM 2705 N N   . ALA A 1 367 ? 48.070 7.315   15.226  1.00 81.65  ? 367 ALA A N   1 
ATOM 2706 C CA  . ALA A 1 367 ? 49.524 7.351   15.154  1.00 77.82  ? 367 ALA A CA  1 
ATOM 2707 C C   . ALA A 1 367 ? 49.977 7.880   13.797  1.00 78.93  ? 367 ALA A C   1 
ATOM 2708 O O   . ALA A 1 367 ? 49.304 8.713   13.188  1.00 79.26  ? 367 ALA A O   1 
ATOM 2709 C CB  . ALA A 1 367 ? 50.101 5.967   15.405  1.00 76.41  ? 367 ALA A CB  1 
ATOM 2710 N N   . VAL B 1 34  ? 21.745 -24.779 56.470  1.00 30.00  ? 34  VAL B N   1 
ATOM 2711 C CA  . VAL B 1 34  ? 21.588 -23.685 55.468  1.00 30.00  ? 34  VAL B CA  1 
ATOM 2712 C C   . VAL B 1 34  ? 21.572 -22.351 56.217  1.00 30.00  ? 34  VAL B C   1 
ATOM 2713 O O   . VAL B 1 34  ? 21.202 -22.348 57.407  1.00 30.00  ? 34  VAL B O   1 
ATOM 2714 C CB  . VAL B 1 34  ? 20.316 -23.875 54.618  1.00 30.00  ? 34  VAL B CB  1 
ATOM 2715 C CG1 . VAL B 1 34  ? 20.202 -25.290 54.073  1.00 30.00  ? 34  VAL B CG1 1 
ATOM 2716 C CG2 . VAL B 1 34  ? 19.056 -23.483 55.374  1.00 30.00  ? 34  VAL B CG2 1 
ATOM 2717 N N   . PRO B 1 35  ? 21.982 -21.229 55.589  1.00 30.00  ? 35  PRO B N   1 
ATOM 2718 C CA  . PRO B 1 35  ? 21.916 -19.930 56.246  1.00 30.00  ? 35  PRO B CA  1 
ATOM 2719 C C   . PRO B 1 35  ? 20.512 -19.678 56.807  1.00 30.00  ? 35  PRO B C   1 
ATOM 2720 O O   . PRO B 1 35  ? 19.557 -20.014 56.146  1.00 30.00  ? 35  PRO B O   1 
ATOM 2721 C CB  . PRO B 1 35  ? 22.271 -18.962 55.118  1.00 30.00  ? 35  PRO B CB  1 
ATOM 2722 C CG  . PRO B 1 35  ? 23.155 -19.773 54.201  1.00 30.00  ? 35  PRO B CG  1 
ATOM 2723 C CD  . PRO B 1 35  ? 22.579 -21.170 54.256  1.00 30.00  ? 35  PRO B CD  1 
ATOM 2724 N N   . SER B 1 36  ? 20.429 -19.089 57.999  1.00 30.00  ? 36  SER B N   1 
ATOM 2725 C CA  . SER B 1 36  ? 19.121 -18.870 58.671  1.00 30.00  ? 36  SER B CA  1 
ATOM 2726 C C   . SER B 1 36  ? 18.145 -18.122 57.763  1.00 30.00  ? 36  SER B C   1 
ATOM 2727 O O   . SER B 1 36  ? 17.071 -18.663 57.505  1.00 30.00  ? 36  SER B O   1 
ATOM 2728 C CB  . SER B 1 36  ? 19.316 -18.142 59.971  1.00 30.00  ? 36  SER B CB  1 
ATOM 2729 O OG  . SER B 1 36  ? 19.241 -16.737 59.790  1.00 30.00  ? 36  SER B OG  1 
ATOM 2730 N N   . TYR B 1 37  ? 18.506 -16.924 57.309  1.00 30.00  ? 37  TYR B N   1 
ATOM 2731 C CA  . TYR B 1 37  ? 17.563 -16.101 56.506  1.00 30.00  ? 37  TYR B CA  1 
ATOM 2732 C C   . TYR B 1 37  ? 16.862 -16.971 55.459  1.00 30.00  ? 37  TYR B C   1 
ATOM 2733 O O   . TYR B 1 37  ? 15.627 -16.915 55.380  1.00 30.00  ? 37  TYR B O   1 
ATOM 2734 C CB  . TYR B 1 37  ? 18.265 -14.869 55.923  1.00 30.00  ? 37  TYR B CB  1 
ATOM 2735 C CG  . TYR B 1 37  ? 19.204 -15.071 54.763  1.00 30.00  ? 37  TYR B CG  1 
ATOM 2736 C CD1 . TYR B 1 37  ? 20.488 -15.552 54.952  1.00 30.00  ? 37  TYR B CD1 1 
ATOM 2737 C CD2 . TYR B 1 37  ? 18.830 -14.713 53.480  1.00 30.00  ? 37  TYR B CD2 1 
ATOM 2738 C CE1 . TYR B 1 37  ? 21.363 -15.710 53.891  1.00 30.00  ? 37  TYR B CE1 1 
ATOM 2739 C CE2 . TYR B 1 37  ? 19.692 -14.863 52.408  1.00 30.00  ? 37  TYR B CE2 1 
ATOM 2740 C CZ  . TYR B 1 37  ? 20.964 -15.362 52.615  1.00 30.00  ? 37  TYR B CZ  1 
ATOM 2741 O OH  . TYR B 1 37  ? 21.815 -15.513 51.561  1.00 30.00  ? 37  TYR B OH  1 
ATOM 2742 N N   . LEU B 1 38  ? 17.611 -17.752 54.688  1.00 30.00  ? 38  LEU B N   1 
ATOM 2743 C CA  . LEU B 1 38  ? 16.920 -18.669 53.753  1.00 30.00  ? 38  LEU B CA  1 
ATOM 2744 C C   . LEU B 1 38  ? 16.517 -19.922 54.538  1.00 30.00  ? 38  LEU B C   1 
ATOM 2745 O O   . LEU B 1 38  ? 16.947 -21.017 54.157  1.00 30.00  ? 38  LEU B O   1 
ATOM 2746 C CB  . LEU B 1 38  ? 17.825 -18.980 52.558  1.00 30.00  ? 38  LEU B CB  1 
ATOM 2747 C CG  . LEU B 1 38  ? 19.302 -19.214 52.859  1.00 30.00  ? 38  LEU B CG  1 
ATOM 2748 C CD1 . LEU B 1 38  ? 19.612 -20.701 52.839  1.00 30.00  ? 38  LEU B CD1 1 
ATOM 2749 C CD2 . LEU B 1 38  ? 20.166 -18.492 51.840  1.00 30.00  ? 38  LEU B CD2 1 
ATOM 2750 N N   . LYS B 1 39  ? 15.739 -19.753 55.613  1.00 30.00  ? 39  LYS B N   1 
ATOM 2751 C CA  . LYS B 1 39  ? 15.248 -20.911 56.403  1.00 30.00  ? 39  LYS B CA  1 
ATOM 2752 C C   . LYS B 1 39  ? 14.396 -21.748 55.468  1.00 30.00  ? 39  LYS B C   1 
ATOM 2753 O O   . LYS B 1 39  ? 14.635 -22.958 55.370  1.00 30.00  ? 39  LYS B O   1 
ATOM 2754 C CB  . LYS B 1 39  ? 14.410 -20.446 57.595  1.00 30.00  ? 39  LYS B CB  1 
ATOM 2755 C CG  . LYS B 1 39  ? 14.092 -18.957 57.635  1.00 30.00  ? 39  LYS B CG  1 
ATOM 2756 C CD  . LYS B 1 39  ? 12.939 -18.553 56.746  1.00 30.00  ? 39  LYS B CD  1 
ATOM 2757 C CE  . LYS B 1 39  ? 11.793 -17.934 57.515  1.00 30.00  ? 39  LYS B CE  1 
ATOM 2758 N NZ  . LYS B 1 39  ? 10.511 -18.619 57.230  1.00 30.00  ? 39  LYS B NZ  1 
ATOM 2759 N N   . ASP B 1 40  ? 13.425 -21.118 54.816  1.00 56.52  ? 40  ASP B N   1 
ATOM 2760 C CA  . ASP B 1 40  ? 12.670 -21.862 53.785  1.00 62.24  ? 40  ASP B CA  1 
ATOM 2761 C C   . ASP B 1 40  ? 13.646 -22.000 52.623  1.00 61.42  ? 40  ASP B C   1 
ATOM 2762 O O   . ASP B 1 40  ? 14.808 -21.625 52.800  1.00 49.64  ? 40  ASP B O   1 
ATOM 2763 C CB  . ASP B 1 40  ? 11.359 -21.155 53.458  1.00 63.46  ? 40  ASP B CB  1 
ATOM 2764 C CG  . ASP B 1 40  ? 10.773 -20.443 54.662  1.00 61.36  ? 40  ASP B CG  1 
ATOM 2765 O OD1 . ASP B 1 40  ? 10.244 -19.334 54.486  1.00 52.59  ? 40  ASP B OD1 1 
ATOM 2766 O OD2 . ASP B 1 40  ? 10.862 -21.000 55.768  1.00 66.42  ? 40  ASP B OD2 1 
ATOM 2767 N N   . TYR B 1 41  ? 13.215 -22.500 51.477  1.00 65.56  ? 41  TYR B N   1 
ATOM 2768 C CA  . TYR B 1 41  ? 14.150 -22.555 50.322  1.00 63.80  ? 41  TYR B CA  1 
ATOM 2769 C C   . TYR B 1 41  ? 15.352 -23.452 50.653  1.00 67.39  ? 41  TYR B C   1 
ATOM 2770 O O   . TYR B 1 41  ? 16.223 -23.605 49.791  1.00 66.77  ? 41  TYR B O   1 
ATOM 2771 C CB  . TYR B 1 41  ? 14.618 -21.153 49.923  1.00 63.24  ? 41  TYR B CB  1 
ATOM 2772 C CG  . TYR B 1 41  ? 13.545 -20.100 49.846  1.00 62.42  ? 41  TYR B CG  1 
ATOM 2773 C CD1 . TYR B 1 41  ? 13.283 -19.270 50.922  1.00 60.01  ? 41  TYR B CD1 1 
ATOM 2774 C CD2 . TYR B 1 41  ? 12.809 -19.916 48.690  1.00 63.33  ? 41  TYR B CD2 1 
ATOM 2775 C CE1 . TYR B 1 41  ? 12.302 -18.296 50.859  1.00 56.93  ? 41  TYR B CE1 1 
ATOM 2776 C CE2 . TYR B 1 41  ? 11.826 -18.945 48.608  1.00 64.98  ? 41  TYR B CE2 1 
ATOM 2777 C CZ  . TYR B 1 41  ? 11.572 -18.133 49.698  1.00 67.74  ? 41  TYR B CZ  1 
ATOM 2778 O OH  . TYR B 1 41  ? 10.606 -17.172 49.627  1.00 72.01  ? 41  TYR B OH  1 
ATOM 2779 N N   . ALA B 1 42  ? 15.394 -24.035 51.851  1.00 65.32  ? 42  ALA B N   1 
ATOM 2780 C CA  . ALA B 1 42  ? 16.482 -24.971 52.210  1.00 65.78  ? 42  ALA B CA  1 
ATOM 2781 C C   . ALA B 1 42  ? 16.616 -26.033 51.125  1.00 67.01  ? 42  ALA B C   1 
ATOM 2782 O O   . ALA B 1 42  ? 17.714 -26.211 50.587  1.00 69.80  ? 42  ALA B O   1 
ATOM 2783 C CB  . ALA B 1 42  ? 16.175 -25.615 53.530  1.00 59.01  ? 42  ALA B CB  1 
ATOM 2784 N N   . ALA B 1 43  ? 15.525 -26.731 50.845  1.00 62.10  ? 43  ALA B N   1 
ATOM 2785 C CA  . ALA B 1 43  ? 15.548 -27.766 49.796  1.00 65.05  ? 43  ALA B CA  1 
ATOM 2786 C C   . ALA B 1 43  ? 16.116 -27.166 48.518  1.00 65.34  ? 43  ALA B C   1 
ATOM 2787 O O   . ALA B 1 43  ? 17.085 -27.725 47.984  1.00 65.19  ? 43  ALA B O   1 
ATOM 2788 C CB  . ALA B 1 43  ? 14.158 -28.273 49.574  1.00 67.62  ? 43  ALA B CB  1 
ATOM 2789 N N   . LEU B 1 44  ? 15.525 -26.067 48.048  1.00 68.27  ? 44  LEU B N   1 
ATOM 2790 C CA  . LEU B 1 44  ? 16.109 -25.433 46.870  1.00 66.41  ? 44  LEU B CA  1 
ATOM 2791 C C   . LEU B 1 44  ? 17.575 -25.084 47.100  1.00 65.80  ? 44  LEU B C   1 
ATOM 2792 O O   . LEU B 1 44  ? 18.387 -25.158 46.170  1.00 68.22  ? 44  LEU B O   1 
ATOM 2793 C CB  . LEU B 1 44  ? 15.309 -24.189 46.484  1.00 68.57  ? 44  LEU B CB  1 
ATOM 2794 C CG  . LEU B 1 44  ? 15.776 -23.472 45.213  1.00 67.52  ? 44  LEU B CG  1 
ATOM 2795 C CD1 . LEU B 1 44  ? 15.987 -24.462 44.073  1.00 62.14  ? 44  LEU B CD1 1 
ATOM 2796 C CD2 . LEU B 1 44  ? 14.787 -22.391 44.810  1.00 62.49  ? 44  LEU B CD2 1 
ATOM 2797 N N   . TYR B 1 45  ? 17.931 -24.690 48.326  1.00 57.64  ? 45  TYR B N   1 
ATOM 2798 C CA  . TYR B 1 45  ? 19.325 -24.378 48.627  1.00 66.38  ? 45  TYR B CA  1 
ATOM 2799 C C   . TYR B 1 45  ? 20.219 -25.591 48.410  1.00 72.31  ? 45  TYR B C   1 
ATOM 2800 O O   . TYR B 1 45  ? 21.277 -25.494 47.777  1.00 63.97  ? 45  TYR B O   1 
ATOM 2801 C CB  . TYR B 1 45  ? 19.458 -23.864 50.060  1.00 67.26  ? 45  TYR B CB  1 
ATOM 2802 C CG  . TYR B 1 45  ? 20.824 -23.291 50.360  1.00 71.69  ? 45  TYR B CG  1 
ATOM 2803 C CD1 . TYR B 1 45  ? 21.170 -22.014 49.941  1.00 63.71  ? 45  TYR B CD1 1 
ATOM 2804 C CD2 . TYR B 1 45  ? 21.775 -24.036 51.043  1.00 66.61  ? 45  TYR B CD2 1 
ATOM 2805 C CE1 . TYR B 1 45  ? 22.418 -21.490 50.209  1.00 65.84  ? 45  TYR B CE1 1 
ATOM 2806 C CE2 . TYR B 1 45  ? 23.026 -23.521 51.313  1.00 62.27  ? 45  TYR B CE2 1 
ATOM 2807 C CZ  . TYR B 1 45  ? 23.343 -22.249 50.893  1.00 62.57  ? 45  TYR B CZ  1 
ATOM 2808 O OH  . TYR B 1 45  ? 24.591 -21.735 51.161  1.00 71.80  ? 45  TYR B OH  1 
ATOM 2809 N N   . LYS B 1 46  ? 19.807 -26.748 48.933  1.00 68.42  ? 46  LYS B N   1 
ATOM 2810 C CA  . LYS B 1 46  ? 20.612 -27.955 48.805  1.00 62.92  ? 46  LYS B CA  1 
ATOM 2811 C C   . LYS B 1 46  ? 20.704 -28.431 47.362  1.00 67.94  ? 46  LYS B C   1 
ATOM 2812 O O   . LYS B 1 46  ? 21.639 -29.165 47.023  1.00 71.96  ? 46  LYS B O   1 
ATOM 2813 C CB  . LYS B 1 46  ? 20.039 -29.062 49.688  1.00 64.83  ? 46  LYS B CB  1 
ATOM 2814 C CG  . LYS B 1 46  ? 20.070 -28.744 51.174  1.00 65.45  ? 46  LYS B CG  1 
ATOM 2815 C CD  . LYS B 1 46  ? 19.265 -29.758 51.968  1.00 65.03  ? 46  LYS B CD  1 
ATOM 2816 C CE  . LYS B 1 46  ? 19.908 -30.042 53.314  1.00 73.97  ? 46  LYS B CE  1 
ATOM 2817 N NZ  . LYS B 1 46  ? 19.772 -31.474 53.701  1.00 75.43  ? 46  LYS B NZ  1 
ATOM 2818 N N   . LYS B 1 47  ? 19.766 -28.024 46.507  1.00 68.66  ? 47  LYS B N   1 
ATOM 2819 C CA  . LYS B 1 47  ? 19.821 -28.361 45.091  1.00 71.46  ? 47  LYS B CA  1 
ATOM 2820 C C   . LYS B 1 47  ? 20.554 -27.296 44.285  1.00 66.02  ? 47  LYS B C   1 
ATOM 2821 O O   . LYS B 1 47  ? 21.265 -27.624 43.329  1.00 63.50  ? 47  LYS B O   1 
ATOM 2822 C CB  . LYS B 1 47  ? 18.405 -28.551 44.540  1.00 74.89  ? 47  LYS B CB  1 
ATOM 2823 C CG  . LYS B 1 47  ? 17.607 -29.656 45.217  1.00 64.76  ? 47  LYS B CG  1 
ATOM 2824 C CD  . LYS B 1 47  ? 16.375 -30.026 44.403  1.00 62.21  ? 47  LYS B CD  1 
ATOM 2825 C CE  . LYS B 1 47  ? 15.697 -31.272 44.954  1.00 60.04  ? 47  LYS B CE  1 
ATOM 2826 N NZ  . LYS B 1 47  ? 14.978 -32.029 43.893  1.00 53.45  ? 47  LYS B NZ  1 
ATOM 2827 N N   . ASP B 1 48  ? 20.396 -26.026 44.660  1.00 69.52  ? 48  ASP B N   1 
ATOM 2828 C CA  . ASP B 1 48  ? 21.092 -24.914 44.025  1.00 72.51  ? 48  ASP B CA  1 
ATOM 2829 C C   . ASP B 1 48  ? 21.046 -23.705 44.953  1.00 67.87  ? 48  ASP B C   1 
ATOM 2830 O O   . ASP B 1 48  ? 19.998 -23.060 45.084  1.00 66.57  ? 48  ASP B O   1 
ATOM 2831 C CB  . ASP B 1 48  ? 20.479 -24.582 42.664  1.00 60.98  ? 48  ASP B CB  1 
ATOM 2832 C CG  . ASP B 1 48  ? 21.320 -23.598 41.874  1.00 65.46  ? 48  ASP B CG  1 
ATOM 2833 O OD1 . ASP B 1 48  ? 22.457 -23.308 42.301  1.00 71.96  ? 48  ASP B OD1 1 
ATOM 2834 O OD2 . ASP B 1 48  ? 20.849 -23.115 40.825  1.00 67.24  ? 48  ASP B OD2 1 
ATOM 2835 N N   . PRO B 1 49  ? 22.165 -23.370 45.612  1.00 71.38  ? 49  PRO B N   1 
ATOM 2836 C CA  . PRO B 1 49  ? 22.168 -22.269 46.586  1.00 68.58  ? 49  PRO B CA  1 
ATOM 2837 C C   . PRO B 1 49  ? 21.754 -20.925 46.014  1.00 64.67  ? 49  PRO B C   1 
ATOM 2838 O O   . PRO B 1 49  ? 20.826 -20.297 46.532  1.00 54.52  ? 49  PRO B O   1 
ATOM 2839 C CB  . PRO B 1 49  ? 23.626 -22.235 47.065  1.00 61.81  ? 49  PRO B CB  1 
ATOM 2840 C CG  . PRO B 1 49  ? 24.141 -23.600 46.810  1.00 61.90  ? 49  PRO B CG  1 
ATOM 2841 C CD  . PRO B 1 49  ? 23.468 -24.050 45.550  1.00 69.81  ? 49  PRO B CD  1 
ATOM 2842 N N   . ARG B 1 50  ? 22.431 -20.462 44.961  1.00 63.17  ? 50  ARG B N   1 
ATOM 2843 C CA  . ARG B 1 50  ? 22.085 -19.152 44.423  1.00 63.07  ? 50  ARG B CA  1 
ATOM 2844 C C   . ARG B 1 50  ? 20.653 -19.126 43.908  1.00 64.24  ? 50  ARG B C   1 
ATOM 2845 O O   . ARG B 1 50  ? 19.951 -18.128 44.097  1.00 67.28  ? 50  ARG B O   1 
ATOM 2846 C CB  . ARG B 1 50  ? 23.069 -18.743 43.323  1.00 64.04  ? 50  ARG B CB  1 
ATOM 2847 C CG  . ARG B 1 50  ? 23.333 -17.238 43.278  1.00 63.06  ? 50  ARG B CG  1 
ATOM 2848 C CD  . ARG B 1 50  ? 24.711 -16.898 42.721  1.00 59.21  ? 50  ARG B CD  1 
ATOM 2849 N NE  . ARG B 1 50  ? 25.730 -16.845 43.763  1.00 64.36  ? 50  ARG B NE  1 
ATOM 2850 C CZ  . ARG B 1 50  ? 26.969 -17.296 43.622  1.00 69.74  ? 50  ARG B CZ  1 
ATOM 2851 N NH1 . ARG B 1 50  ? 27.396 -17.798 42.476  1.00 70.54  ? 50  ARG B NH1 1 
ATOM 2852 N NH2 . ARG B 1 50  ? 27.799 -17.245 44.661  1.00 65.18  ? 50  ARG B NH2 1 
ATOM 2853 N N   . ALA B 1 51  ? 20.169 -20.238 43.345  1.00 61.78  ? 51  ALA B N   1 
ATOM 2854 C CA  . ALA B 1 51  ? 18.767 -20.299 42.946  1.00 64.75  ? 51  ALA B CA  1 
ATOM 2855 C C   . ALA B 1 51  ? 17.848 -20.083 44.143  1.00 65.94  ? 51  ALA B C   1 
ATOM 2856 O O   . ALA B 1 51  ? 16.833 -19.385 44.038  1.00 63.92  ? 51  ALA B O   1 
ATOM 2857 C CB  . ALA B 1 51  ? 18.464 -21.634 42.270  1.00 63.23  ? 51  ALA B CB  1 
ATOM 2858 N N   . ALA B 1 52  ? 18.189 -20.676 45.289  1.00 64.12  ? 52  ALA B N   1 
ATOM 2859 C CA  . ALA B 1 52  ? 17.408 -20.446 46.500  1.00 64.64  ? 52  ALA B CA  1 
ATOM 2860 C C   . ALA B 1 52  ? 17.479 -18.991 46.942  1.00 64.51  ? 52  ALA B C   1 
ATOM 2861 O O   . ALA B 1 52  ? 16.467 -18.411 47.355  1.00 62.05  ? 52  ALA B O   1 
ATOM 2862 C CB  . ALA B 1 52  ? 17.889 -21.363 47.621  1.00 61.08  ? 52  ALA B CB  1 
ATOM 2863 N N   . ALA B 1 53  ? 18.669 -18.388 46.875  1.00 64.92  ? 53  ALA B N   1 
ATOM 2864 C CA  . ALA B 1 53  ? 18.824 -16.998 47.293  1.00 57.61  ? 53  ALA B CA  1 
ATOM 2865 C C   . ALA B 1 53  ? 17.958 -16.073 46.447  1.00 62.55  ? 53  ALA B C   1 
ATOM 2866 O O   . ALA B 1 53  ? 17.228 -15.228 46.981  1.00 61.30  ? 53  ALA B O   1 
ATOM 2867 C CB  . ALA B 1 53  ? 20.293 -16.587 47.216  1.00 51.91  ? 53  ALA B CB  1 
ATOM 2868 N N   . LEU B 1 54  ? 18.038 -16.210 45.120  1.00 61.51  ? 54  LEU B N   1 
ATOM 2869 C CA  . LEU B 1 54  ? 17.155 -15.451 44.240  1.00 59.78  ? 54  LEU B CA  1 
ATOM 2870 C C   . LEU B 1 54  ? 15.692 -15.666 44.615  1.00 63.73  ? 54  LEU B C   1 
ATOM 2871 O O   . LEU B 1 54  ? 14.924 -14.707 44.743  1.00 74.21  ? 54  LEU B O   1 
ATOM 2872 C CB  . LEU B 1 54  ? 17.398 -15.829 42.774  1.00 60.62  ? 54  LEU B CB  1 
ATOM 2873 C CG  . LEU B 1 54  ? 18.562 -15.209 41.982  1.00 70.41  ? 54  LEU B CG  1 
ATOM 2874 C CD1 . LEU B 1 54  ? 18.629 -13.701 42.233  1.00 67.65  ? 54  LEU B CD1 1 
ATOM 2875 C CD2 . LEU B 1 54  ? 19.920 -15.880 42.206  1.00 71.05  ? 54  LEU B CD2 1 
ATOM 2876 N N   . GLN B 1 55  ? 15.295 -16.927 44.804  1.00 61.19  ? 55  GLN B N   1 
ATOM 2877 C CA  . GLN B 1 55  ? 13.902 -17.238 45.117  1.00 62.99  ? 55  GLN B CA  1 
ATOM 2878 C C   . GLN B 1 55  ? 13.455 -16.562 46.409  1.00 63.19  ? 55  GLN B C   1 
ATOM 2879 O O   . GLN B 1 55  ? 12.377 -15.961 46.463  1.00 65.29  ? 55  GLN B O   1 
ATOM 2880 C CB  . GLN B 1 55  ? 13.709 -18.753 45.199  1.00 72.26  ? 55  GLN B CB  1 
ATOM 2881 C CG  . GLN B 1 55  ? 12.280 -19.213 44.944  1.00 66.03  ? 55  GLN B CG  1 
ATOM 2882 C CD  . GLN B 1 55  ? 11.619 -18.476 43.793  1.00 73.07  ? 55  GLN B CD  1 
ATOM 2883 O OE1 . GLN B 1 55  ? 12.197 -18.332 42.714  1.00 68.12  ? 55  GLN B OE1 1 
ATOM 2884 N NE2 . GLN B 1 55  ? 10.398 -18.003 44.020  1.00 75.13  ? 55  GLN B NE2 1 
ATOM 2885 N N   . TYR B 1 56  ? 14.261 -16.670 47.469  1.00 63.22  ? 56  TYR B N   1 
ATOM 2886 C CA  . TYR B 1 56  ? 13.959 -15.955 48.706  1.00 54.92  ? 56  TYR B CA  1 
ATOM 2887 C C   . TYR B 1 56  ? 13.775 -14.467 48.445  1.00 64.56  ? 56  TYR B C   1 
ATOM 2888 O O   . TYR B 1 56  ? 12.834 -13.842 48.949  1.00 63.69  ? 56  TYR B O   1 
ATOM 2889 C CB  . TYR B 1 56  ? 15.069 -16.179 49.738  1.00 51.49  ? 56  TYR B CB  1 
ATOM 2890 C CG  . TYR B 1 56  ? 15.172 -15.073 50.771  1.00 56.70  ? 56  TYR B CG  1 
ATOM 2891 C CD1 . TYR B 1 56  ? 14.403 -15.105 51.927  1.00 54.34  ? 56  TYR B CD1 1 
ATOM 2892 C CD2 . TYR B 1 56  ? 16.041 -13.999 50.593  1.00 56.64  ? 56  TYR B CD2 1 
ATOM 2893 C CE1 . TYR B 1 56  ? 14.490 -14.099 52.873  1.00 51.05  ? 56  TYR B CE1 1 
ATOM 2894 C CE2 . TYR B 1 56  ? 16.131 -12.988 51.532  1.00 50.38  ? 56  TYR B CE2 1 
ATOM 2895 C CZ  . TYR B 1 56  ? 15.355 -13.045 52.670  1.00 52.37  ? 56  TYR B CZ  1 
ATOM 2896 O OH  . TYR B 1 56  ? 15.443 -12.044 53.609  1.00 58.64  ? 56  TYR B OH  1 
ATOM 2897 N N   . PHE B 1 57  ? 14.680 -13.882 47.658  1.00 59.52  ? 57  PHE B N   1 
ATOM 2898 C CA  . PHE B 1 57  ? 14.695 -12.436 47.478  1.00 59.43  ? 57  PHE B CA  1 
ATOM 2899 C C   . PHE B 1 57  ? 13.442 -11.936 46.768  1.00 58.94  ? 57  PHE B C   1 
ATOM 2900 O O   . PHE B 1 57  ? 12.788 -10.999 47.241  1.00 54.84  ? 57  PHE B O   1 
ATOM 2901 C CB  . PHE B 1 57  ? 15.947 -12.014 46.715  1.00 59.29  ? 57  PHE B CB  1 
ATOM 2902 C CG  . PHE B 1 57  ? 16.190 -10.543 46.754  1.00 57.69  ? 57  PHE B CG  1 
ATOM 2903 C CD1 . PHE B 1 57  ? 16.389 -9.899  47.963  1.00 52.83  ? 57  PHE B CD1 1 
ATOM 2904 C CD2 . PHE B 1 57  ? 16.188 -9.798  45.592  1.00 53.45  ? 57  PHE B CD2 1 
ATOM 2905 C CE1 . PHE B 1 57  ? 16.602 -8.541  48.010  1.00 53.91  ? 57  PHE B CE1 1 
ATOM 2906 C CE2 . PHE B 1 57  ? 16.398 -8.440  45.632  1.00 53.86  ? 57  PHE B CE2 1 
ATOM 2907 C CZ  . PHE B 1 57  ? 16.607 -7.809  46.842  1.00 59.57  ? 57  PHE B CZ  1 
ATOM 2908 N N   . LYS B 1 58  ? 13.116 -12.521 45.606  1.00 61.38  ? 58  LYS B N   1 
ATOM 2909 C CA  . LYS B 1 58  ? 11.901 -12.136 44.885  1.00 58.90  ? 58  LYS B CA  1 
ATOM 2910 C C   . LYS B 1 58  ? 10.698 -12.064 45.814  1.00 59.70  ? 58  LYS B C   1 
ATOM 2911 O O   . LYS B 1 58  ? 9.900  -11.122 45.745  1.00 66.49  ? 58  LYS B O   1 
ATOM 2912 C CB  . LYS B 1 58  ? 11.597 -13.123 43.755  1.00 57.25  ? 58  LYS B CB  1 
ATOM 2913 C CG  . LYS B 1 58  ? 12.752 -13.509 42.858  1.00 60.77  ? 58  LYS B CG  1 
ATOM 2914 C CD  . LYS B 1 58  ? 12.454 -14.849 42.192  1.00 70.68  ? 58  LYS B CD  1 
ATOM 2915 C CE  . LYS B 1 58  ? 13.113 -14.975 40.827  1.00 77.06  ? 58  LYS B CE  1 
ATOM 2916 N NZ  . LYS B 1 58  ? 13.413 -16.397 40.491  1.00 71.39  ? 58  LYS B NZ  1 
ATOM 2917 N N   . GLU B 1 59  ? 10.610 -12.994 46.757  1.00 58.50  ? 59  GLU B N   1 
ATOM 2918 C CA  . GLU B 1 59  ? 9.386  -13.066 47.592  1.00 61.86  ? 59  GLU B CA  1 
ATOM 2919 C C   . GLU B 1 59  ? 9.544  -12.372 48.945  1.00 56.93  ? 59  GLU B C   1 
ATOM 2920 O O   . GLU B 1 59  ? 8.589  -12.433 49.725  1.00 59.65  ? 59  GLU B O   1 
ATOM 2921 C CB  . GLU B 1 59  ? 9.030  -14.535 47.800  1.00 65.23  ? 59  GLU B CB  1 
ATOM 2922 C CG  . GLU B 1 59  ? 9.352  -15.402 46.596  1.00 69.04  ? 59  GLU B CG  1 
ATOM 2923 C CD  . GLU B 1 59  ? 8.854  -16.833 46.686  1.00 74.62  ? 59  GLU B CD  1 
ATOM 2924 O OE1 . GLU B 1 59  ? 8.751  -17.353 47.812  1.00 70.90  ? 59  GLU B OE1 1 
ATOM 2925 O OE2 . GLU B 1 59  ? 8.566  -17.423 45.630  1.00 58.43  ? 59  GLU B OE2 1 
ATOM 2926 N N   . ALA B 1 60  ? 10.683 -11.742 49.214  1.00 57.30  ? 60  ALA B N   1 
ATOM 2927 C CA  . ALA B 1 60  ? 10.836 -10.986 50.477  1.00 59.41  ? 60  ALA B CA  1 
ATOM 2928 C C   . ALA B 1 60  ? 9.855  -9.819  50.473  1.00 58.89  ? 60  ALA B C   1 
ATOM 2929 O O   . ALA B 1 60  ? 9.172  -9.637  51.493  1.00 52.75  ? 60  ALA B O   1 
ATOM 2930 C CB  . ALA B 1 60  ? 12.254 -10.520 50.612  1.00 60.59  ? 60  ALA B CB  1 
ATOM 2931 N N   . LYS B 1 61  ? 9.850  -9.027  49.402  1.00 61.70  ? 61  LYS B N   1 
ATOM 2932 C CA  . LYS B 1 61  ? 8.846  -7.942  49.226  1.00 61.43  ? 61  LYS B CA  1 
ATOM 2933 C C   . LYS B 1 61  ? 9.137  -6.702  50.079  1.00 54.44  ? 61  LYS B C   1 
ATOM 2934 O O   . LYS B 1 61  ? 8.852  -5.608  49.591  1.00 65.71  ? 61  LYS B O   1 
ATOM 2935 C CB  . LYS B 1 61  ? 7.441  -8.501  49.474  1.00 64.29  ? 61  LYS B CB  1 
ATOM 2936 C CG  . LYS B 1 61  ? 6.884  -9.370  48.355  1.00 62.30  ? 61  LYS B CG  1 
ATOM 2937 C CD  . LYS B 1 61  ? 7.667  -9.259  47.065  1.00 72.17  ? 61  LYS B CD  1 
ATOM 2938 C CE  . LYS B 1 61  ? 6.833  -8.786  45.893  1.00 76.70  ? 61  LYS B CE  1 
ATOM 2939 N NZ  . LYS B 1 61  ? 7.595  -8.842  44.624  1.00 71.95  ? 61  LYS B NZ  1 
ATOM 2940 N N   . PHE B 1 62  ? 9.659  -6.849  51.292  1.00 58.80  ? 62  PHE B N   1 
ATOM 2941 C CA  . PHE B 1 62  ? 9.832  -5.660  52.166  1.00 60.59  ? 62  PHE B CA  1 
ATOM 2942 C C   . PHE B 1 62  ? 11.163 -5.732  52.909  1.00 66.37  ? 62  PHE B C   1 
ATOM 2943 O O   . PHE B 1 62  ? 11.528 -6.819  53.376  1.00 65.55  ? 62  PHE B O   1 
ATOM 2944 C CB  . PHE B 1 62  ? 8.667  -5.552  53.149  1.00 65.21  ? 62  PHE B CB  1 
ATOM 2945 C CG  . PHE B 1 62  ? 8.402  -4.180  53.709  1.00 61.10  ? 62  PHE B CG  1 
ATOM 2946 C CD1 . PHE B 1 62  ? 9.012  -3.060  53.174  1.00 61.47  ? 62  PHE B CD1 1 
ATOM 2947 C CD2 . PHE B 1 62  ? 7.534  -4.013  54.774  1.00 66.66  ? 62  PHE B CD2 1 
ATOM 2948 C CE1 . PHE B 1 62  ? 8.763  -1.803  53.697  1.00 69.59  ? 62  PHE B CE1 1 
ATOM 2949 C CE2 . PHE B 1 62  ? 7.283  -2.756  55.295  1.00 62.02  ? 62  PHE B CE2 1 
ATOM 2950 C CZ  . PHE B 1 62  ? 7.895  -1.653  54.752  1.00 67.23  ? 62  PHE B CZ  1 
ATOM 2951 N N   . GLY B 1 63  ? 11.845 -4.590  53.029  1.00 62.60  ? 63  GLY B N   1 
ATOM 2952 C CA  . GLY B 1 63  ? 13.168 -4.578  53.671  1.00 63.10  ? 63  GLY B CA  1 
ATOM 2953 C C   . GLY B 1 63  ? 13.540 -3.241  54.264  1.00 59.07  ? 63  GLY B C   1 
ATOM 2954 O O   . GLY B 1 63  ? 12.984 -2.225  53.833  1.00 59.47  ? 63  GLY B O   1 
ATOM 2955 N N   . LEU B 1 64  ? 14.478 -3.254  55.209  1.00 57.11  ? 64  LEU B N   1 
ATOM 2956 C CA  . LEU B 1 64  ? 14.925 -2.030  55.867  1.00 54.77  ? 64  LEU B CA  1 
ATOM 2957 C C   . LEU B 1 64  ? 16.251 -1.545  55.288  1.00 53.51  ? 64  LEU B C   1 
ATOM 2958 O O   . LEU B 1 64  ? 17.202 -2.324  55.161  1.00 54.19  ? 64  LEU B O   1 
ATOM 2959 C CB  . LEU B 1 64  ? 15.072 -2.247  57.375  1.00 52.07  ? 64  LEU B CB  1 
ATOM 2960 C CG  . LEU B 1 64  ? 15.344 -0.991  58.208  1.00 52.82  ? 64  LEU B CG  1 
ATOM 2961 C CD1 . LEU B 1 64  ? 14.121 -0.089  58.240  1.00 52.85  ? 64  LEU B CD1 1 
ATOM 2962 C CD2 . LEU B 1 64  ? 15.786 -1.353  59.619  1.00 53.11  ? 64  LEU B CD2 1 
ATOM 2963 N N   . PHE B 1 65  ? 16.310 -0.259  54.950  1.00 56.97  ? 65  PHE B N   1 
ATOM 2964 C CA  . PHE B 1 65  ? 17.535 0.414   54.537  1.00 54.90  ? 65  PHE B CA  1 
ATOM 2965 C C   . PHE B 1 65  ? 18.026 1.301   55.676  1.00 52.21  ? 65  PHE B C   1 
ATOM 2966 O O   . PHE B 1 65  ? 17.229 1.985   56.325  1.00 52.01  ? 65  PHE B O   1 
ATOM 2967 C CB  . PHE B 1 65  ? 17.288 1.258   53.282  1.00 50.56  ? 65  PHE B CB  1 
ATOM 2968 C CG  . PHE B 1 65  ? 18.425 1.262   52.298  1.00 45.11  ? 65  PHE B CG  1 
ATOM 2969 C CD1 . PHE B 1 65  ? 19.689 0.830   52.660  1.00 50.66  ? 65  PHE B CD1 1 
ATOM 2970 C CD2 . PHE B 1 65  ? 18.221 1.712   51.003  1.00 49.56  ? 65  PHE B CD2 1 
ATOM 2971 C CE1 . PHE B 1 65  ? 20.728 0.841   51.743  1.00 49.86  ? 65  PHE B CE1 1 
ATOM 2972 C CE2 . PHE B 1 65  ? 19.252 1.724   50.083  1.00 52.11  ? 65  PHE B CE2 1 
ATOM 2973 C CZ  . PHE B 1 65  ? 20.508 1.289   50.453  1.00 44.74  ? 65  PHE B CZ  1 
ATOM 2974 N N   . ILE B 1 66  ? 19.335 1.287   55.920  1.00 55.55  ? 66  ILE B N   1 
ATOM 2975 C CA  . ILE B 1 66  ? 19.938 2.046   57.014  1.00 50.19  ? 66  ILE B CA  1 
ATOM 2976 C C   . ILE B 1 66  ? 21.100 2.864   56.466  1.00 52.95  ? 66  ILE B C   1 
ATOM 2977 O O   . ILE B 1 66  ? 22.058 2.301   55.921  1.00 48.56  ? 66  ILE B O   1 
ATOM 2978 C CB  . ILE B 1 66  ? 20.418 1.133   58.155  1.00 45.89  ? 66  ILE B CB  1 
ATOM 2979 C CG1 . ILE B 1 66  ? 19.242 0.367   58.761  1.00 49.66  ? 66  ILE B CG1 1 
ATOM 2980 C CG2 . ILE B 1 66  ? 21.125 1.948   59.225  1.00 50.19  ? 66  ILE B CG2 1 
ATOM 2981 C CD1 . ILE B 1 66  ? 19.624 -0.979  59.334  1.00 44.65  ? 66  ILE B CD1 1 
ATOM 2982 N N   . HIS B 1 67  ? 21.016 4.187   56.611  1.00 54.92  ? 67  HIS B N   1 
ATOM 2983 C CA  . HIS B 1 67  ? 22.093 5.109   56.252  1.00 50.51  ? 67  HIS B CA  1 
ATOM 2984 C C   . HIS B 1 67  ? 22.593 5.785   57.526  1.00 58.09  ? 67  HIS B C   1 
ATOM 2985 O O   . HIS B 1 67  ? 21.962 6.719   58.029  1.00 64.64  ? 67  HIS B O   1 
ATOM 2986 C CB  . HIS B 1 67  ? 21.613 6.144   55.239  1.00 50.05  ? 67  HIS B CB  1 
ATOM 2987 C CG  . HIS B 1 67  ? 21.628 5.660   53.823  1.00 50.10  ? 67  HIS B CG  1 
ATOM 2988 N ND1 . HIS B 1 67  ? 20.740 4.720   53.347  1.00 45.40  ? 67  HIS B ND1 1 
ATOM 2989 C CD2 . HIS B 1 67  ? 22.421 5.993   52.776  1.00 48.99  ? 67  HIS B CD2 1 
ATOM 2990 C CE1 . HIS B 1 67  ? 20.987 4.492   52.070  1.00 46.85  ? 67  HIS B CE1 1 
ATOM 2991 N NE2 . HIS B 1 67  ? 22.002 5.250   51.699  1.00 52.28  ? 67  HIS B NE2 1 
ATOM 2992 N N   . TYR B 1 68  ? 23.733 5.328   58.038  1.00 58.87  ? 68  TYR B N   1 
ATOM 2993 C CA  . TYR B 1 68  ? 24.305 5.893   59.251  1.00 54.84  ? 68  TYR B CA  1 
ATOM 2994 C C   . TYR B 1 68  ? 25.809 6.039   59.079  1.00 47.43  ? 68  TYR B C   1 
ATOM 2995 O O   . TYR B 1 68  ? 26.473 5.130   58.574  1.00 54.12  ? 68  TYR B O   1 
ATOM 2996 C CB  . TYR B 1 68  ? 23.992 5.022   60.475  1.00 64.03  ? 68  TYR B CB  1 
ATOM 2997 C CG  . TYR B 1 68  ? 24.439 5.625   61.786  1.00 67.90  ? 68  TYR B CG  1 
ATOM 2998 C CD1 . TYR B 1 68  ? 24.342 6.993   62.015  1.00 64.16  ? 68  TYR B CD1 1 
ATOM 2999 C CD2 . TYR B 1 68  ? 24.959 4.828   62.796  1.00 68.36  ? 68  TYR B CD2 1 
ATOM 3000 C CE1 . TYR B 1 68  ? 24.752 7.547   63.211  1.00 66.23  ? 68  TYR B CE1 1 
ATOM 3001 C CE2 . TYR B 1 68  ? 25.371 5.372   63.995  1.00 71.09  ? 68  TYR B CE2 1 
ATOM 3002 C CZ  . TYR B 1 68  ? 25.266 6.731   64.197  1.00 68.42  ? 68  TYR B CZ  1 
ATOM 3003 O OH  . TYR B 1 68  ? 25.675 7.274   65.393  1.00 78.59  ? 68  TYR B OH  1 
ATOM 3004 N N   . GLY B 1 69  ? 26.339 7.179   59.510  1.00 55.76  ? 69  GLY B N   1 
ATOM 3005 C CA  . GLY B 1 69  ? 27.757 7.441   59.352  1.00 57.08  ? 69  GLY B CA  1 
ATOM 3006 C C   . GLY B 1 69  ? 28.088 8.872   59.729  1.00 62.49  ? 69  GLY B C   1 
ATOM 3007 O O   . GLY B 1 69  ? 27.293 9.557   60.376  1.00 60.17  ? 69  GLY B O   1 
ATOM 3008 N N   . LEU B 1 70  ? 29.282 9.306   59.313  1.00 61.87  ? 70  LEU B N   1 
ATOM 3009 C CA  . LEU B 1 70  ? 29.766 10.633  59.682  1.00 54.16  ? 70  LEU B CA  1 
ATOM 3010 C C   . LEU B 1 70  ? 28.810 11.724  59.216  1.00 55.82  ? 70  LEU B C   1 
ATOM 3011 O O   . LEU B 1 70  ? 28.635 12.739  59.901  1.00 60.21  ? 70  LEU B O   1 
ATOM 3012 C CB  . LEU B 1 70  ? 31.160 10.862  59.096  1.00 55.06  ? 70  LEU B CB  1 
ATOM 3013 C CG  . LEU B 1 70  ? 32.261 9.895   59.535  1.00 60.06  ? 70  LEU B CG  1 
ATOM 3014 C CD1 . LEU B 1 70  ? 33.626 10.407  59.103  1.00 61.22  ? 70  LEU B CD1 1 
ATOM 3015 C CD2 . LEU B 1 70  ? 32.221 9.672   61.039  1.00 55.92  ? 70  LEU B CD2 1 
ATOM 3016 N N   . TYR B 1 71  ? 28.193 11.538  58.046  1.00 60.25  ? 71  TYR B N   1 
ATOM 3017 C CA  . TYR B 1 71  ? 27.252 12.527  57.528  1.00 58.46  ? 71  TYR B CA  1 
ATOM 3018 C C   . TYR B 1 71  ? 26.081 12.752  58.477  1.00 57.05  ? 71  TYR B C   1 
ATOM 3019 O O   . TYR B 1 71  ? 25.516 13.852  58.515  1.00 54.16  ? 71  TYR B O   1 
ATOM 3020 C CB  . TYR B 1 71  ? 26.743 12.095  56.151  1.00 54.13  ? 71  TYR B CB  1 
ATOM 3021 C CG  . TYR B 1 71  ? 26.427 10.618  56.044  1.00 53.66  ? 71  TYR B CG  1 
ATOM 3022 C CD1 . TYR B 1 71  ? 25.187 10.123  56.427  1.00 50.80  ? 71  TYR B CD1 1 
ATOM 3023 C CD2 . TYR B 1 71  ? 27.368 9.719   55.555  1.00 56.48  ? 71  TYR B CD2 1 
ATOM 3024 C CE1 . TYR B 1 71  ? 24.893 8.774   56.330  1.00 53.50  ? 71  TYR B CE1 1 
ATOM 3025 C CE2 . TYR B 1 71  ? 27.083 8.369   55.454  1.00 57.95  ? 71  TYR B CE2 1 
ATOM 3026 C CZ  . TYR B 1 71  ? 25.845 7.901   55.843  1.00 55.61  ? 71  TYR B CZ  1 
ATOM 3027 O OH  . TYR B 1 71  ? 25.558 6.558   55.744  1.00 45.49  ? 71  TYR B OH  1 
ATOM 3028 N N   . SER B 1 72  ? 25.697 11.727  59.244  1.00 52.72  ? 72  SER B N   1 
ATOM 3029 C CA  . SER B 1 72  ? 24.570 11.867  60.159  1.00 60.12  ? 72  SER B CA  1 
ATOM 3030 C C   . SER B 1 72  ? 24.855 12.878  61.263  1.00 65.16  ? 72  SER B C   1 
ATOM 3031 O O   . SER B 1 72  ? 23.926 13.516  61.771  1.00 62.84  ? 72  SER B O   1 
ATOM 3032 C CB  . SER B 1 72  ? 24.213 10.511  60.767  1.00 62.63  ? 72  SER B CB  1 
ATOM 3033 O OG  . SER B 1 72  ? 24.462 9.462   59.849  1.00 64.74  ? 72  SER B OG  1 
ATOM 3034 N N   . LEU B 1 73  ? 26.126 13.039  61.642  1.00 63.87  ? 73  LEU B N   1 
ATOM 3035 C CA  . LEU B 1 73  ? 26.470 13.986  62.699  1.00 58.44  ? 73  LEU B CA  1 
ATOM 3036 C C   . LEU B 1 73  ? 26.175 15.417  62.268  1.00 62.99  ? 73  LEU B C   1 
ATOM 3037 O O   . LEU B 1 73  ? 25.729 16.237  63.080  1.00 64.49  ? 73  LEU B O   1 
ATOM 3038 C CB  . LEU B 1 73  ? 27.938 13.822  63.098  1.00 53.68  ? 73  LEU B CB  1 
ATOM 3039 C CG  . LEU B 1 73  ? 28.472 12.400  63.328  1.00 65.46  ? 73  LEU B CG  1 
ATOM 3040 C CD1 . LEU B 1 73  ? 29.756 12.444  64.140  1.00 63.82  ? 73  LEU B CD1 1 
ATOM 3041 C CD2 . LEU B 1 73  ? 27.451 11.496  64.014  1.00 60.79  ? 73  LEU B CD2 1 
ATOM 3042 N N   . LEU B 1 74  ? 26.417 15.737  60.997  1.00 62.99  ? 74  LEU B N   1 
ATOM 3043 C CA  . LEU B 1 74  ? 26.040 17.044  60.477  1.00 56.93  ? 74  LEU B CA  1 
ATOM 3044 C C   . LEU B 1 74  ? 24.541 17.145  60.246  1.00 60.58  ? 74  LEU B C   1 
ATOM 3045 O O   . LEU B 1 74  ? 24.008 18.258  60.192  1.00 67.16  ? 74  LEU B O   1 
ATOM 3046 C CB  . LEU B 1 74  ? 26.782 17.334  59.168  1.00 50.20  ? 74  LEU B CB  1 
ATOM 3047 C CG  . LEU B 1 74  ? 28.118 18.074  59.248  1.00 57.18  ? 74  LEU B CG  1 
ATOM 3048 C CD1 . LEU B 1 74  ? 28.960 17.535  60.376  1.00 56.07  ? 74  LEU B CD1 1 
ATOM 3049 C CD2 . LEU B 1 74  ? 28.870 17.966  57.932  1.00 53.39  ? 74  LEU B CD2 1 
ATOM 3050 N N   . GLY B 1 75  ? 23.860 16.006  60.140  1.00 56.94  ? 75  GLY B N   1 
ATOM 3051 C CA  . GLY B 1 75  ? 22.413 15.967  60.010  1.00 59.94  ? 75  GLY B CA  1 
ATOM 3052 C C   . GLY B 1 75  ? 21.848 16.763  58.856  1.00 62.66  ? 75  GLY B C   1 
ATOM 3053 O O   . GLY B 1 75  ? 20.753 17.319  58.978  1.00 69.33  ? 75  GLY B O   1 
ATOM 3054 N N   . ARG B 1 76  ? 22.565 16.837  57.731  1.00 61.48  ? 76  ARG B N   1 
ATOM 3055 C CA  . ARG B 1 76  ? 22.062 17.515  56.539  1.00 63.79  ? 76  ARG B CA  1 
ATOM 3056 C C   . ARG B 1 76  ? 22.068 16.621  55.301  1.00 59.65  ? 76  ARG B C   1 
ATOM 3057 O O   . ARG B 1 76  ? 22.105 17.132  54.177  1.00 55.85  ? 76  ARG B O   1 
ATOM 3058 C CB  . ARG B 1 76  ? 22.854 18.796  56.267  1.00 59.37  ? 76  ARG B CB  1 
ATOM 3059 C CG  . ARG B 1 76  ? 23.138 19.631  57.500  1.00 53.14  ? 76  ARG B CG  1 
ATOM 3060 C CD  . ARG B 1 76  ? 24.585 20.076  57.518  1.00 66.97  ? 76  ARG B CD  1 
ATOM 3061 N NE  . ARG B 1 76  ? 24.959 20.702  56.255  1.00 69.56  ? 76  ARG B NE  1 
ATOM 3062 C CZ  . ARG B 1 76  ? 26.092 21.358  56.049  1.00 73.78  ? 76  ARG B CZ  1 
ATOM 3063 N NH1 . ARG B 1 76  ? 26.999 21.488  57.004  1.00 74.75  ? 76  ARG B NH1 1 
ATOM 3064 N NH2 . ARG B 1 76  ? 26.321 21.899  54.856  1.00 65.92  ? 76  ARG B NH2 1 
ATOM 3065 N N   . GLY B 1 77  ? 22.025 15.306  55.474  1.00 57.85  ? 77  GLY B N   1 
ATOM 3066 C CA  . GLY B 1 77  ? 22.050 14.394  54.350  1.00 58.65  ? 77  GLY B CA  1 
ATOM 3067 C C   . GLY B 1 77  ? 23.418 13.764  54.125  1.00 56.01  ? 77  GLY B C   1 
ATOM 3068 O O   . GLY B 1 77  ? 24.453 14.249  54.590  1.00 50.47  ? 77  GLY B O   1 
ATOM 3069 N N   . GLU B 1 78  ? 23.407 12.659  53.374  1.00 54.54  ? 78  GLU B N   1 
ATOM 3070 C CA  . GLU B 1 78  ? 24.579 11.813  53.176  1.00 55.81  ? 78  GLU B CA  1 
ATOM 3071 C C   . GLU B 1 78  ? 25.558 12.349  52.138  1.00 52.85  ? 78  GLU B C   1 
ATOM 3072 O O   . GLU B 1 78  ? 26.678 11.834  52.051  1.00 49.53  ? 78  GLU B O   1 
ATOM 3073 C CB  . GLU B 1 78  ? 24.135 10.402  52.778  1.00 53.56  ? 78  GLU B CB  1 
ATOM 3074 C CG  . GLU B 1 78  ? 23.599 10.287  51.357  1.00 50.49  ? 78  GLU B CG  1 
ATOM 3075 C CD  . GLU B 1 78  ? 22.189 10.829  51.209  1.00 53.47  ? 78  GLU B CD  1 
ATOM 3076 O OE1 . GLU B 1 78  ? 21.487 10.962  52.234  1.00 50.43  ? 78  GLU B OE1 1 
ATOM 3077 O OE2 . GLU B 1 78  ? 21.784 11.125  50.065  1.00 59.63  ? 78  GLU B OE2 1 
ATOM 3078 N N   . TRP B 1 79  ? 25.176 13.357  51.354  1.00 52.78  ? 79  TRP B N   1 
ATOM 3079 C CA  . TRP B 1 79  ? 26.051 13.936  50.343  1.00 48.05  ? 79  TRP B CA  1 
ATOM 3080 C C   . TRP B 1 79  ? 26.697 15.228  50.827  1.00 53.93  ? 79  TRP B C   1 
ATOM 3081 O O   . TRP B 1 79  ? 27.172 16.023  50.008  1.00 60.03  ? 79  TRP B O   1 
ATOM 3082 C CB  . TRP B 1 79  ? 25.276 14.195  49.048  1.00 57.94  ? 79  TRP B CB  1 
ATOM 3083 C CG  . TRP B 1 79  ? 25.117 12.993  48.149  1.00 62.91  ? 79  TRP B CG  1 
ATOM 3084 C CD1 . TRP B 1 79  ? 24.546 11.797  48.473  1.00 53.42  ? 79  TRP B CD1 1 
ATOM 3085 C CD2 . TRP B 1 79  ? 25.517 12.886  46.774  1.00 59.18  ? 79  TRP B CD2 1 
ATOM 3086 N NE1 . TRP B 1 79  ? 24.572 10.950  47.392  1.00 61.57  ? 79  TRP B NE1 1 
ATOM 3087 C CE2 . TRP B 1 79  ? 25.163 11.594  46.336  1.00 53.33  ? 79  TRP B CE2 1 
ATOM 3088 C CE3 . TRP B 1 79  ? 26.142 13.754  45.874  1.00 55.90  ? 79  TRP B CE3 1 
ATOM 3089 C CZ2 . TRP B 1 79  ? 25.413 11.149  45.039  1.00 57.08  ? 79  TRP B CZ2 1 
ATOM 3090 C CZ3 . TRP B 1 79  ? 26.390 13.311  44.585  1.00 54.80  ? 79  TRP B CZ3 1 
ATOM 3091 C CH2 . TRP B 1 79  ? 26.026 12.020  44.181  1.00 58.61  ? 79  TRP B CH2 1 
ATOM 3092 N N   . VAL B 1 80  ? 26.721 15.449  52.146  1.00 54.77  ? 80  VAL B N   1 
ATOM 3093 C CA  . VAL B 1 80  ? 27.118 16.743  52.696  1.00 59.21  ? 80  VAL B CA  1 
ATOM 3094 C C   . VAL B 1 80  ? 28.572 17.076  52.376  1.00 59.77  ? 80  VAL B C   1 
ATOM 3095 O O   . VAL B 1 80  ? 28.920 18.252  52.215  1.00 58.57  ? 80  VAL B O   1 
ATOM 3096 C CB  . VAL B 1 80  ? 26.841 16.777  54.214  1.00 56.64  ? 80  VAL B CB  1 
ATOM 3097 C CG1 . VAL B 1 80  ? 27.665 15.726  54.945  1.00 52.32  ? 80  VAL B CG1 1 
ATOM 3098 C CG2 . VAL B 1 80  ? 27.094 18.168  54.777  1.00 51.60  ? 80  VAL B CG2 1 
ATOM 3099 N N   . GLN B 1 81  ? 29.443 16.067  52.276  1.00 53.31  ? 81  GLN B N   1 
ATOM 3100 C CA  . GLN B 1 81  ? 30.836 16.348  51.934  1.00 49.90  ? 81  GLN B CA  1 
ATOM 3101 C C   . GLN B 1 81  ? 30.940 16.983  50.554  1.00 56.27  ? 81  GLN B C   1 
ATOM 3102 O O   . GLN B 1 81  ? 31.699 17.938  50.354  1.00 58.76  ? 81  GLN B O   1 
ATOM 3103 C CB  . GLN B 1 81  ? 31.677 15.075  51.995  1.00 50.52  ? 81  GLN B CB  1 
ATOM 3104 C CG  . GLN B 1 81  ? 33.094 15.273  51.471  1.00 52.58  ? 81  GLN B CG  1 
ATOM 3105 C CD  . GLN B 1 81  ? 33.973 14.053  51.653  1.00 57.96  ? 81  GLN B CD  1 
ATOM 3106 O OE1 . GLN B 1 81  ? 33.547 13.041  52.210  1.00 60.21  ? 81  GLN B OE1 1 
ATOM 3107 N NE2 . GLN B 1 81  ? 35.213 14.144  51.183  1.00 56.20  ? 81  GLN B NE2 1 
ATOM 3108 N N   . LEU B 1 82  ? 30.176 16.467  49.590  1.00 52.34  ? 82  LEU B N   1 
ATOM 3109 C CA  . LEU B 1 82  ? 30.142 17.075  48.265  1.00 54.14  ? 82  LEU B CA  1 
ATOM 3110 C C   . LEU B 1 82  ? 29.380 18.393  48.290  1.00 57.57  ? 82  LEU B C   1 
ATOM 3111 O O   . LEU B 1 82  ? 29.883 19.424  47.829  1.00 60.09  ? 82  LEU B O   1 
ATOM 3112 C CB  . LEU B 1 82  ? 29.511 16.105  47.265  1.00 54.55  ? 82  LEU B CB  1 
ATOM 3113 C CG  . LEU B 1 82  ? 29.641 16.438  45.777  1.00 48.37  ? 82  LEU B CG  1 
ATOM 3114 C CD1 . LEU B 1 82  ? 30.225 15.263  45.011  1.00 56.21  ? 82  LEU B CD1 1 
ATOM 3115 C CD2 . LEU B 1 82  ? 28.295 16.838  45.199  1.00 46.86  ? 82  LEU B CD2 1 
ATOM 3116 N N   . GLN B 1 83  ? 28.158 18.376  48.828  1.00 54.49  ? 83  GLN B N   1 
ATOM 3117 C CA  . GLN B 1 83  ? 27.304 19.558  48.788  1.00 57.33  ? 83  GLN B CA  1 
ATOM 3118 C C   . GLN B 1 83  ? 27.847 20.686  49.657  1.00 57.59  ? 83  GLN B C   1 
ATOM 3119 O O   . GLN B 1 83  ? 27.560 21.859  49.395  1.00 56.12  ? 83  GLN B O   1 
ATOM 3120 C CB  . GLN B 1 83  ? 25.886 19.186  49.215  1.00 52.45  ? 83  GLN B CB  1 
ATOM 3121 C CG  . GLN B 1 83  ? 25.095 18.467  48.135  1.00 55.04  ? 83  GLN B CG  1 
ATOM 3122 C CD  . GLN B 1 83  ? 24.061 17.517  48.702  1.00 58.95  ? 83  GLN B CD  1 
ATOM 3123 O OE1 . GLN B 1 83  ? 23.949 17.356  49.917  1.00 58.34  ? 83  GLN B OE1 1 
ATOM 3124 N NE2 . GLN B 1 83  ? 23.301 16.876  47.822  1.00 66.42  ? 83  GLN B NE2 1 
ATOM 3125 N N   . GLY B 1 84  ? 28.617 20.357  50.691  1.00 61.16  ? 84  GLY B N   1 
ATOM 3126 C CA  . GLY B 1 84  ? 29.255 21.343  51.534  1.00 58.67  ? 84  GLY B CA  1 
ATOM 3127 C C   . GLY B 1 84  ? 30.680 21.679  51.163  1.00 63.96  ? 84  GLY B C   1 
ATOM 3128 O O   . GLY B 1 84  ? 31.307 22.493  51.849  1.00 58.42  ? 84  GLY B O   1 
ATOM 3129 N N   . LYS B 1 85  ? 31.208 21.081  50.091  1.00 59.43  ? 85  LYS B N   1 
ATOM 3130 C CA  . LYS B 1 85  ? 32.591 21.291  49.651  1.00 58.13  ? 85  LYS B CA  1 
ATOM 3131 C C   . LYS B 1 85  ? 33.597 21.072  50.780  1.00 57.33  ? 85  LYS B C   1 
ATOM 3132 O O   . LYS B 1 85  ? 34.690 21.643  50.769  1.00 62.28  ? 85  LYS B O   1 
ATOM 3133 C CB  . LYS B 1 85  ? 32.769 22.690  49.056  1.00 59.48  ? 85  LYS B CB  1 
ATOM 3134 C CG  . LYS B 1 85  ? 31.749 23.074  47.999  1.00 62.79  ? 85  LYS B CG  1 
ATOM 3135 C CD  . LYS B 1 85  ? 32.411 23.250  46.644  1.00 63.33  ? 85  LYS B CD  1 
ATOM 3136 C CE  . LYS B 1 85  ? 31.663 24.261  45.789  1.00 78.38  ? 85  LYS B CE  1 
ATOM 3137 N NZ  . LYS B 1 85  ? 32.359 25.581  45.755  1.00 82.08  ? 85  LYS B NZ  1 
ATOM 3138 N N   . ILE B 1 86  ? 33.248 20.237  51.755  1.00 57.08  ? 86  ILE B N   1 
ATOM 3139 C CA  . ILE B 1 86  ? 34.108 19.990  52.912  1.00 59.64  ? 86  ILE B CA  1 
ATOM 3140 C C   . ILE B 1 86  ? 35.404 19.319  52.471  1.00 62.85  ? 86  ILE B C   1 
ATOM 3141 O O   . ILE B 1 86  ? 35.370 18.213  51.911  1.00 63.72  ? 86  ILE B O   1 
ATOM 3142 C CB  . ILE B 1 86  ? 33.387 19.138  53.968  1.00 53.89  ? 86  ILE B CB  1 
ATOM 3143 C CG1 . ILE B 1 86  ? 31.921 19.561  54.084  1.00 53.43  ? 86  ILE B CG1 1 
ATOM 3144 C CG2 . ILE B 1 86  ? 34.101 19.241  55.307  1.00 57.83  ? 86  ILE B CG2 1 
ATOM 3145 C CD1 . ILE B 1 86  ? 31.224 19.025  55.317  1.00 41.89  ? 86  ILE B CD1 1 
ATOM 3146 N N   . PRO B 1 87  ? 36.559 19.947  52.696  1.00 62.07  ? 87  PRO B N   1 
ATOM 3147 C CA  . PRO B 1 87  ? 37.829 19.298  52.354  1.00 67.63  ? 87  PRO B CA  1 
ATOM 3148 C C   . PRO B 1 87  ? 38.014 17.990  53.110  1.00 68.01  ? 87  PRO B C   1 
ATOM 3149 O O   . PRO B 1 87  ? 37.517 17.815  54.225  1.00 72.35  ? 87  PRO B O   1 
ATOM 3150 C CB  . PRO B 1 87  ? 38.876 20.340  52.764  1.00 63.85  ? 87  PRO B CB  1 
ATOM 3151 C CG  . PRO B 1 87  ? 38.149 21.642  52.642  1.00 57.72  ? 87  PRO B CG  1 
ATOM 3152 C CD  . PRO B 1 87  ? 36.758 21.340  53.130  1.00 57.90  ? 87  PRO B CD  1 
ATOM 3153 N N   . VAL B 1 88  ? 38.735 17.065  52.470  1.00 64.28  ? 88  VAL B N   1 
ATOM 3154 C CA  . VAL B 1 88  ? 38.915 15.716  53.008  1.00 69.39  ? 88  VAL B CA  1 
ATOM 3155 C C   . VAL B 1 88  ? 39.462 15.749  54.432  1.00 71.26  ? 88  VAL B C   1 
ATOM 3156 O O   . VAL B 1 88  ? 39.033 14.966  55.290  1.00 60.25  ? 88  VAL B O   1 
ATOM 3157 C CB  . VAL B 1 88  ? 39.802 14.881  52.069  1.00 70.98  ? 88  VAL B CB  1 
ATOM 3158 C CG1 . VAL B 1 88  ? 39.860 13.443  52.543  1.00 65.90  ? 88  VAL B CG1 1 
ATOM 3159 C CG2 . VAL B 1 88  ? 39.242 14.929  50.660  1.00 65.11  ? 88  VAL B CG2 1 
ATOM 3160 N N   . ARG B 1 89  ? 40.427 16.632  54.709  1.00 77.15  ? 89  ARG B N   1 
ATOM 3161 C CA  . ARG B 1 89  ? 41.037 16.621  56.037  1.00 72.76  ? 89  ARG B CA  1 
ATOM 3162 C C   . ARG B 1 89  ? 40.082 17.181  57.084  1.00 67.83  ? 89  ARG B C   1 
ATOM 3163 O O   . ARG B 1 89  ? 40.006 16.663  58.205  1.00 62.02  ? 89  ARG B O   1 
ATOM 3164 C CB  . ARG B 1 89  ? 42.343 17.422  56.029  1.00 69.43  ? 89  ARG B CB  1 
ATOM 3165 C CG  . ARG B 1 89  ? 42.686 18.053  57.378  1.00 81.12  ? 89  ARG B CG  1 
ATOM 3166 C CD  . ARG B 1 89  ? 43.800 19.097  57.279  1.00 87.91  ? 89  ARG B CD  1 
ATOM 3167 N NE  . ARG B 1 89  ? 44.011 19.819  58.532  1.00 91.69  ? 89  ARG B NE  1 
ATOM 3168 C CZ  . ARG B 1 89  ? 43.110 20.587  59.133  1.00 89.21  ? 89  ARG B CZ  1 
ATOM 3169 N NH1 . ARG B 1 89  ? 41.908 20.783  58.615  1.00 82.61  ? 89  ARG B NH1 1 
ATOM 3170 N NH2 . ARG B 1 89  ? 43.423 21.172  60.286  1.00 85.92  ? 89  ARG B NH2 1 
ATOM 3171 N N   . GLU B 1 90  ? 39.333 18.225  56.729  1.00 64.11  ? 90  GLU B N   1 
ATOM 3172 C CA  . GLU B 1 90  ? 38.322 18.765  57.631  1.00 69.35  ? 90  GLU B CA  1 
ATOM 3173 C C   . GLU B 1 90  ? 37.225 17.739  57.902  1.00 69.02  ? 90  GLU B C   1 
ATOM 3174 O O   . GLU B 1 90  ? 36.836 17.520  59.056  1.00 63.97  ? 90  GLU B O   1 
ATOM 3175 C CB  . GLU B 1 90  ? 37.747 20.056  57.049  1.00 74.39  ? 90  GLU B CB  1 
ATOM 3176 C CG  . GLU B 1 90  ? 36.921 20.873  58.027  1.00 78.36  ? 90  GLU B CG  1 
ATOM 3177 C CD  . GLU B 1 90  ? 36.428 22.174  57.422  1.00 85.03  ? 90  GLU B CD  1 
ATOM 3178 O OE1 . GLU B 1 90  ? 37.182 22.781  56.631  1.00 85.10  ? 90  GLU B OE1 1 
ATOM 3179 O OE2 . GLU B 1 90  ? 35.296 22.594  57.739  1.00 77.48  ? 90  GLU B OE2 1 
ATOM 3180 N N   . TYR B 1 91  ? 36.705 17.111  56.843  1.00 65.84  ? 91  TYR B N   1 
ATOM 3181 C CA  . TYR B 1 91  ? 35.635 16.127  56.998  1.00 63.56  ? 91  TYR B CA  1 
ATOM 3182 C C   . TYR B 1 91  ? 36.071 14.967  57.886  1.00 63.73  ? 91  TYR B C   1 
ATOM 3183 O O   . TYR B 1 91  ? 35.281 14.465  58.693  1.00 56.97  ? 91  TYR B O   1 
ATOM 3184 C CB  . TYR B 1 91  ? 35.195 15.620  55.622  1.00 58.62  ? 91  TYR B CB  1 
ATOM 3185 C CG  . TYR B 1 91  ? 34.008 14.678  55.638  1.00 52.53  ? 91  TYR B CG  1 
ATOM 3186 C CD1 . TYR B 1 91  ? 34.181 13.311  55.822  1.00 54.46  ? 91  TYR B CD1 1 
ATOM 3187 C CD2 . TYR B 1 91  ? 32.715 15.153  55.452  1.00 50.40  ? 91  TYR B CD2 1 
ATOM 3188 C CE1 . TYR B 1 91  ? 33.103 12.446  55.832  1.00 51.08  ? 91  TYR B CE1 1 
ATOM 3189 C CE2 . TYR B 1 91  ? 31.628 14.294  55.460  1.00 53.87  ? 91  TYR B CE2 1 
ATOM 3190 C CZ  . TYR B 1 91  ? 31.829 12.940  55.649  1.00 55.56  ? 91  TYR B CZ  1 
ATOM 3191 O OH  . TYR B 1 91  ? 30.756 12.078  55.657  1.00 53.86  ? 91  TYR B OH  1 
ATOM 3192 N N   . ALA B 1 92  ? 37.323 14.523  57.745  1.00 65.00  ? 92  ALA B N   1 
ATOM 3193 C CA  . ALA B 1 92  ? 37.813 13.390  58.522  1.00 57.16  ? 92  ALA B CA  1 
ATOM 3194 C C   . ALA B 1 92  ? 37.790 13.651  60.023  1.00 63.22  ? 92  ALA B C   1 
ATOM 3195 O O   . ALA B 1 92  ? 37.853 12.697  60.805  1.00 67.83  ? 92  ALA B O   1 
ATOM 3196 C CB  . ALA B 1 92  ? 39.231 13.028  58.082  1.00 57.03  ? 92  ALA B CB  1 
ATOM 3197 N N   . LYS B 1 93  ? 37.703 14.917  60.443  1.00 63.52  ? 93  LYS B N   1 
ATOM 3198 C CA  . LYS B 1 93  ? 37.647 15.218  61.870  1.00 65.50  ? 93  LYS B CA  1 
ATOM 3199 C C   . LYS B 1 93  ? 36.375 14.683  62.511  1.00 67.51  ? 93  LYS B C   1 
ATOM 3200 O O   . LYS B 1 93  ? 36.352 14.437  63.723  1.00 71.95  ? 93  LYS B O   1 
ATOM 3201 C CB  . LYS B 1 93  ? 37.739 16.723  62.103  1.00 60.19  ? 93  LYS B CB  1 
ATOM 3202 C CG  . LYS B 1 93  ? 39.035 17.362  61.664  1.00 58.72  ? 93  LYS B CG  1 
ATOM 3203 C CD  . LYS B 1 93  ? 38.880 18.871  61.667  1.00 72.26  ? 93  LYS B CD  1 
ATOM 3204 C CE  . LYS B 1 93  ? 40.026 19.561  60.964  1.00 67.01  ? 93  LYS B CE  1 
ATOM 3205 N NZ  . LYS B 1 93  ? 39.534 20.778  60.264  1.00 70.78  ? 93  LYS B NZ  1 
ATOM 3206 N N   . LEU B 1 94  ? 35.312 14.505  61.721  1.00 66.85  ? 94  LEU B N   1 
ATOM 3207 C CA  . LEU B 1 94  ? 34.039 14.036  62.256  1.00 66.79  ? 94  LEU B CA  1 
ATOM 3208 C C   . LEU B 1 94  ? 34.159 12.696  62.964  1.00 68.53  ? 94  LEU B C   1 
ATOM 3209 O O   . LEU B 1 94  ? 33.272 12.339  63.747  1.00 71.33  ? 94  LEU B O   1 
ATOM 3210 C CB  . LEU B 1 94  ? 33.009 13.933  61.135  1.00 59.45  ? 94  LEU B CB  1 
ATOM 3211 C CG  . LEU B 1 94  ? 32.715 15.280  60.487  1.00 62.47  ? 94  LEU B CG  1 
ATOM 3212 C CD1 . LEU B 1 94  ? 32.044 15.113  59.129  1.00 61.05  ? 94  LEU B CD1 1 
ATOM 3213 C CD2 . LEU B 1 94  ? 31.880 16.105  61.435  1.00 61.17  ? 94  LEU B CD2 1 
ATOM 3214 N N   . GLU B 1 95  ? 35.232 11.949  62.704  1.00 70.41  ? 95  GLU B N   1 
ATOM 3215 C CA  . GLU B 1 95  ? 35.435 10.676  63.380  1.00 75.46  ? 95  GLU B CA  1 
ATOM 3216 C C   . GLU B 1 95  ? 35.651 10.865  64.876  1.00 78.05  ? 95  GLU B C   1 
ATOM 3217 O O   . GLU B 1 95  ? 35.277 9.994   65.669  1.00 79.52  ? 95  GLU B O   1 
ATOM 3218 C CB  . GLU B 1 95  ? 36.621 9.950   62.742  1.00 72.97  ? 95  GLU B CB  1 
ATOM 3219 C CG  . GLU B 1 95  ? 37.228 8.835   63.570  1.00 77.44  ? 95  GLU B CG  1 
ATOM 3220 C CD  . GLU B 1 95  ? 38.181 7.980   62.761  1.00 81.90  ? 95  GLU B CD  1 
ATOM 3221 O OE1 . GLU B 1 95  ? 38.882 8.538   61.888  1.00 72.54  ? 95  GLU B OE1 1 
ATOM 3222 O OE2 . GLU B 1 95  ? 38.228 6.753   62.993  1.00 77.47  ? 95  GLU B OE2 1 
ATOM 3223 N N   . ASN B 1 96  ? 36.212 12.008  65.283  1.00 82.22  ? 96  ASN B N   1 
ATOM 3224 C CA  . ASN B 1 96  ? 36.511 12.241  66.692  1.00 81.92  ? 96  ASN B CA  1 
ATOM 3225 C C   . ASN B 1 96  ? 35.259 12.336  67.555  1.00 85.44  ? 96  ASN B C   1 
ATOM 3226 O O   . ASN B 1 96  ? 35.350 12.156  68.774  1.00 91.52  ? 96  ASN B O   1 
ATOM 3227 C CB  . ASN B 1 96  ? 37.336 13.519  66.845  1.00 78.99  ? 96  ASN B CB  1 
ATOM 3228 C CG  . ASN B 1 96  ? 38.736 13.379  66.284  1.00 84.52  ? 96  ASN B CG  1 
ATOM 3229 O OD1 . ASN B 1 96  ? 38.930 12.825  65.202  1.00 88.95  ? 96  ASN B OD1 1 
ATOM 3230 N ND2 . ASN B 1 96  ? 39.721 13.887  67.016  1.00 91.68  ? 96  ASN B ND2 1 
ATOM 3231 N N   . ASP B 1 97  ? 34.099 12.616  66.962  1.00 83.69  ? 97  ASP B N   1 
ATOM 3232 C CA  . ASP B 1 97  ? 32.845 12.689  67.699  1.00 77.73  ? 97  ASP B CA  1 
ATOM 3233 C C   . ASP B 1 97  ? 31.894 11.544  67.381  1.00 77.56  ? 97  ASP B C   1 
ATOM 3234 O O   . ASP B 1 97  ? 30.764 11.541  67.879  1.00 85.00  ? 97  ASP B O   1 
ATOM 3235 C CB  . ASP B 1 97  ? 32.147 14.029  67.433  1.00 73.40  ? 97  ASP B CB  1 
ATOM 3236 C CG  . ASP B 1 97  ? 33.108 15.199  67.456  1.00 87.55  ? 97  ASP B CG  1 
ATOM 3237 O OD1 . ASP B 1 97  ? 33.546 15.588  68.559  1.00 89.63  ? 97  ASP B OD1 1 
ATOM 3238 O OD2 . ASP B 1 97  ? 33.430 15.727  66.371  1.00 90.66  ? 97  ASP B OD2 1 
ATOM 3239 N N   . PHE B 1 98  ? 32.339 10.576  66.581  1.00 69.19  ? 98  PHE B N   1 
ATOM 3240 C CA  . PHE B 1 98  ? 31.475 9.423   66.227  1.00 74.16  ? 98  PHE B CA  1 
ATOM 3241 C C   . PHE B 1 98  ? 31.501 8.398   67.358  1.00 76.46  ? 98  PHE B C   1 
ATOM 3242 O O   . PHE B 1 98  ? 32.491 7.664   67.467  1.00 76.11  ? 98  PHE B O   1 
ATOM 3243 C CB  . PHE B 1 98  ? 31.914 8.776   64.914  1.00 68.79  ? 98  PHE B CB  1 
ATOM 3244 C CG  . PHE B 1 98  ? 30.918 7.798   64.348  1.00 62.03  ? 98  PHE B CG  1 
ATOM 3245 C CD1 . PHE B 1 98  ? 29.721 8.238   63.810  1.00 61.63  ? 98  PHE B CD1 1 
ATOM 3246 C CD2 . PHE B 1 98  ? 31.171 6.438   64.365  1.00 67.54  ? 98  PHE B CD2 1 
ATOM 3247 C CE1 . PHE B 1 98  ? 28.803 7.339   63.295  1.00 66.99  ? 98  PHE B CE1 1 
ATOM 3248 C CE2 . PHE B 1 98  ? 30.250 5.540   63.851  1.00 68.86  ? 98  PHE B CE2 1 
ATOM 3249 C CZ  . PHE B 1 98  ? 29.068 5.992   63.317  1.00 67.81  ? 98  PHE B CZ  1 
ATOM 3250 N N   . THR B 1 99  ? 30.430 8.331   68.146  1.00 74.06  ? 99  THR B N   1 
ATOM 3251 C CA  . THR B 1 99  ? 30.400 7.416   69.315  1.00 73.93  ? 99  THR B CA  1 
ATOM 3252 C C   . THR B 1 99  ? 29.392 6.292   69.085  1.00 72.04  ? 99  THR B C   1 
ATOM 3253 O O   . THR B 1 99  ? 29.668 5.170   69.523  1.00 75.67  ? 99  THR B O   1 
ATOM 3254 C CB  . THR B 1 99  ? 30.034 8.182   70.587  1.00 71.89  ? 99  THR B CB  1 
ATOM 3255 O OG1 . THR B 1 99  ? 28.610 8.199   70.680  1.00 77.22  ? 99  THR B OG1 1 
ATOM 3256 C CG2 . THR B 1 99  ? 30.569 9.596   70.597  1.00 67.65  ? 99  THR B CG2 1 
ATOM 3257 N N   . ALA B 1 100 ? 28.260 6.600   68.457  1.00 76.94  ? 100 ALA B N   1 
ATOM 3258 C CA  . ALA B 1 100 ? 27.232 5.575   68.163  1.00 77.86  ? 100 ALA B CA  1 
ATOM 3259 C C   . ALA B 1 100 ? 26.726 4.977   69.472  1.00 82.55  ? 100 ALA B C   1 
ATOM 3260 O O   . ALA B 1 100 ? 26.443 3.769   69.499  1.00 76.17  ? 100 ALA B O   1 
ATOM 3261 C CB  . ALA B 1 100 ? 27.804 4.515   67.264  1.00 69.00  ? 100 ALA B CB  1 
ATOM 3262 N N   . LYS B 1 101 ? 26.594 5.807   70.504  1.00 86.85  ? 101 LYS B N   1 
ATOM 3263 C CA  . LYS B 1 101 ? 26.170 5.320   71.841  1.00 87.30  ? 101 LYS B CA  1 
ATOM 3264 C C   . LYS B 1 101 ? 24.802 4.641   71.777  1.00 90.87  ? 101 LYS B C   1 
ATOM 3265 O O   . LYS B 1 101 ? 24.575 3.737   72.595  1.00 89.55  ? 101 LYS B O   1 
ATOM 3266 C CB  . LYS B 1 101 ? 26.092 6.508   72.801  1.00 81.57  ? 101 LYS B CB  1 
ATOM 3267 C CG  . LYS B 1 101 ? 26.255 6.171   74.275  1.00 89.07  ? 101 LYS B CG  1 
ATOM 3268 C CD  . LYS B 1 101 ? 25.992 7.350   75.188  1.00 85.06  ? 101 LYS B CD  1 
ATOM 3269 C CE  . LYS B 1 101 ? 27.258 8.063   75.614  1.00 84.02  ? 101 LYS B CE  1 
ATOM 3270 N NZ  . LYS B 1 101 ? 27.351 9.416   75.017  1.00 89.14  ? 101 LYS B NZ  1 
ATOM 3271 N N   . ASN B 1 102 ? 23.935 5.034   70.839  1.00 93.21  ? 102 ASN B N   1 
ATOM 3272 C CA  . ASN B 1 102 ? 22.543 4.506   70.838  1.00 89.46  ? 102 ASN B CA  1 
ATOM 3273 C C   . ASN B 1 102 ? 22.252 3.636   69.610  1.00 84.84  ? 102 ASN B C   1 
ATOM 3274 O O   . ASN B 1 102 ? 21.076 3.559   69.221  1.00 86.52  ? 102 ASN B O   1 
ATOM 3275 C CB  . ASN B 1 102 ? 21.543 5.656   70.945  1.00 89.51  ? 102 ASN B CB  1 
ATOM 3276 C CG  . ASN B 1 102 ? 21.705 6.435   72.231  1.00 98.37  ? 102 ASN B CG  1 
ATOM 3277 O OD1 . ASN B 1 102 ? 21.261 5.995   73.287  1.00 108.14 ? 102 ASN B OD1 1 
ATOM 3278 N ND2 . ASN B 1 102 ? 22.352 7.585   72.154  1.00 97.82  ? 102 ASN B ND2 1 
ATOM 3279 N N   . PHE B 1 103 ? 23.266 2.987   69.044  1.00 78.30  ? 103 PHE B N   1 
ATOM 3280 C CA  . PHE B 1 103 ? 23.015 2.068   67.910  1.00 75.07  ? 103 PHE B CA  1 
ATOM 3281 C C   . PHE B 1 103 ? 22.762 0.665   68.461  1.00 79.96  ? 103 PHE B C   1 
ATOM 3282 O O   . PHE B 1 103 ? 23.731 -0.011  68.825  1.00 75.85  ? 103 PHE B O   1 
ATOM 3283 C CB  . PHE B 1 103 ? 24.187 2.099   66.931  1.00 71.59  ? 103 PHE B CB  1 
ATOM 3284 C CG  . PHE B 1 103 ? 23.946 1.348   65.647  1.00 75.38  ? 103 PHE B CG  1 
ATOM 3285 C CD1 . PHE B 1 103 ? 24.033 -0.033  65.604  1.00 67.78  ? 103 PHE B CD1 1 
ATOM 3286 C CD2 . PHE B 1 103 ? 23.630 2.023   64.480  1.00 66.68  ? 103 PHE B CD2 1 
ATOM 3287 C CE1 . PHE B 1 103 ? 23.810 -0.722  64.424  1.00 63.49  ? 103 PHE B CE1 1 
ATOM 3288 C CE2 . PHE B 1 103 ? 23.407 1.334   63.301  1.00 63.92  ? 103 PHE B CE2 1 
ATOM 3289 C CZ  . PHE B 1 103 ? 23.498 -0.037  63.275  1.00 67.61  ? 103 PHE B CZ  1 
ATOM 3290 N N   . ASP B 1 104 ? 21.493 0.248   68.513  1.00 82.09  ? 104 ASP B N   1 
ATOM 3291 C CA  . ASP B 1 104 ? 21.151 -1.087  69.067  1.00 77.18  ? 104 ASP B CA  1 
ATOM 3292 C C   . ASP B 1 104 ? 20.724 -2.042  67.961  1.00 79.22  ? 104 ASP B C   1 
ATOM 3293 O O   . ASP B 1 104 ? 19.535 -2.060  67.622  1.00 83.44  ? 104 ASP B O   1 
ATOM 3294 C CB  . ASP B 1 104 ? 20.040 -1.034  70.111  1.00 83.40  ? 104 ASP B CB  1 
ATOM 3295 C CG  . ASP B 1 104 ? 19.916 -2.346  70.865  1.00 91.38  ? 104 ASP B CG  1 
ATOM 3296 O OD1 . ASP B 1 104 ? 20.966 -2.914  71.227  1.00 87.05  ? 104 ASP B OD1 1 
ATOM 3297 O OD2 . ASP B 1 104 ? 18.776 -2.796  71.071  1.00 99.90  ? 104 ASP B OD2 1 
ATOM 3298 N N   . ALA B 1 105 ? 21.664 -2.827  67.453  1.00 74.14  ? 105 ALA B N   1 
ATOM 3299 C CA  . ALA B 1 105 ? 21.326 -3.828  66.445  1.00 75.02  ? 105 ALA B CA  1 
ATOM 3300 C C   . ALA B 1 105 ? 20.174 -4.713  66.901  1.00 82.57  ? 105 ALA B C   1 
ATOM 3301 O O   . ALA B 1 105 ? 19.429 -5.242  66.068  1.00 82.55  ? 105 ALA B O   1 
ATOM 3302 C CB  . ALA B 1 105 ? 22.554 -4.677  66.114  1.00 77.03  ? 105 ALA B CB  1 
ATOM 3303 N N   . ASP B 1 106 ? 19.999 -4.865  68.215  1.00 88.46  ? 106 ASP B N   1 
ATOM 3304 C CA  . ASP B 1 106 ? 18.884 -5.646  68.739  1.00 86.14  ? 106 ASP B CA  1 
ATOM 3305 C C   . ASP B 1 106 ? 17.561 -4.925  68.514  1.00 83.37  ? 106 ASP B C   1 
ATOM 3306 O O   . ASP B 1 106 ? 16.573 -5.533  68.086  1.00 81.24  ? 106 ASP B O   1 
ATOM 3307 C CB  . ASP B 1 106 ? 19.102 -5.927  70.227  1.00 91.54  ? 106 ASP B CB  1 
ATOM 3308 C CG  . ASP B 1 106 ? 18.522 -7.257  70.667  1.00 84.59  ? 106 ASP B CG  1 
ATOM 3309 O OD1 . ASP B 1 106 ? 18.493 -8.198  69.848  1.00 87.23  ? 106 ASP B OD1 1 
ATOM 3310 O OD2 . ASP B 1 106 ? 18.105 -7.362  71.839  1.00 80.53  ? 106 ASP B OD2 1 
ATOM 3311 N N   . PHE B 1 107 ? 17.527 -3.622  68.803  1.00 79.23  ? 107 PHE B N   1 
ATOM 3312 C CA  . PHE B 1 107 ? 16.314 -2.837  68.595  1.00 71.04  ? 107 PHE B CA  1 
ATOM 3313 C C   . PHE B 1 107 ? 15.982 -2.697  67.114  1.00 74.71  ? 107 PHE B C   1 
ATOM 3314 O O   . PHE B 1 107 ? 14.809 -2.777  66.729  1.00 73.81  ? 107 PHE B O   1 
ATOM 3315 C CB  . PHE B 1 107 ? 16.474 -1.464  69.246  1.00 67.91  ? 107 PHE B CB  1 
ATOM 3316 C CG  . PHE B 1 107 ? 15.378 -0.496  68.907  1.00 72.45  ? 107 PHE B CG  1 
ATOM 3317 C CD1 . PHE B 1 107 ? 14.120 -0.628  69.469  1.00 66.43  ? 107 PHE B CD1 1 
ATOM 3318 C CD2 . PHE B 1 107 ? 15.611 0.554   68.034  1.00 80.51  ? 107 PHE B CD2 1 
ATOM 3319 C CE1 . PHE B 1 107 ? 13.112 0.267   69.162  1.00 69.93  ? 107 PHE B CE1 1 
ATOM 3320 C CE2 . PHE B 1 107 ? 14.606 1.451   67.723  1.00 78.24  ? 107 PHE B CE2 1 
ATOM 3321 C CZ  . PHE B 1 107 ? 13.356 1.307   68.287  1.00 79.51  ? 107 PHE B CZ  1 
ATOM 3322 N N   . ILE B 1 108 ? 16.996 -2.471  66.270  1.00 81.00  ? 108 ILE B N   1 
ATOM 3323 C CA  . ILE B 1 108 ? 16.754 -2.284  64.838  1.00 72.26  ? 108 ILE B CA  1 
ATOM 3324 C C   . ILE B 1 108 ? 16.104 -3.524  64.235  1.00 78.19  ? 108 ILE B C   1 
ATOM 3325 O O   . ILE B 1 108 ? 15.057 -3.444  63.581  1.00 73.40  ? 108 ILE B O   1 
ATOM 3326 C CB  . ILE B 1 108 ? 18.060 -1.935  64.096  1.00 74.41  ? 108 ILE B CB  1 
ATOM 3327 C CG1 . ILE B 1 108 ? 18.525 -0.503  64.385  1.00 73.35  ? 108 ILE B CG1 1 
ATOM 3328 C CG2 . ILE B 1 108 ? 17.887 -2.125  62.598  1.00 70.66  ? 108 ILE B CG2 1 
ATOM 3329 C CD1 . ILE B 1 108 ? 19.945 -0.378  64.883  1.00 68.07  ? 108 ILE B CD1 1 
ATOM 3330 N N   . THR B 1 109 ? 16.722 -4.690  64.445  1.00 80.40  ? 109 THR B N   1 
ATOM 3331 C CA  . THR B 1 109 ? 16.233 -5.920  63.829  1.00 78.12  ? 109 THR B CA  1 
ATOM 3332 C C   . THR B 1 109 ? 14.841 -6.291  64.320  1.00 79.22  ? 109 THR B C   1 
ATOM 3333 O O   . THR B 1 109 ? 14.039 -6.839  63.554  1.00 79.82  ? 109 THR B O   1 
ATOM 3334 C CB  . THR B 1 109 ? 17.203 -7.060  64.118  1.00 77.37  ? 109 THR B CB  1 
ATOM 3335 O OG1 . THR B 1 109 ? 17.848 -6.811  65.370  1.00 79.96  ? 109 THR B OG1 1 
ATOM 3336 C CG2 . THR B 1 109 ? 18.261 -7.147  63.030  1.00 74.64  ? 109 THR B CG2 1 
ATOM 3337 N N   . ASP B 1 110 ? 14.534 -6.005  65.586  1.00 78.03  ? 110 ASP B N   1 
ATOM 3338 C CA  . ASP B 1 110 ? 13.186 -6.244  66.087  1.00 83.24  ? 110 ASP B CA  1 
ATOM 3339 C C   . ASP B 1 110 ? 12.178 -5.332  65.399  1.00 80.60  ? 110 ASP B C   1 
ATOM 3340 O O   . ASP B 1 110 ? 11.124 -5.792  64.946  1.00 77.13  ? 110 ASP B O   1 
ATOM 3341 C CB  . ASP B 1 110 ? 13.145 -6.068  67.605  1.00 80.80  ? 110 ASP B CB  1 
ATOM 3342 C CG  . ASP B 1 110 ? 13.342 -7.380  68.345  1.00 80.74  ? 110 ASP B CG  1 
ATOM 3343 O OD1 . ASP B 1 110 ? 13.521 -8.419  67.674  1.00 89.58  ? 110 ASP B OD1 1 
ATOM 3344 O OD2 . ASP B 1 110 ? 13.317 -7.376  69.593  1.00 83.94  ? 110 ASP B OD2 1 
ATOM 3345 N N   . MET B 1 111 ? 12.482 -4.032  65.322  1.00 79.09  ? 111 MET B N   1 
ATOM 3346 C CA  . MET B 1 111 ? 11.603 -3.096  64.626  1.00 75.14  ? 111 MET B CA  1 
ATOM 3347 C C   . MET B 1 111 ? 11.284 -3.587  63.218  1.00 83.58  ? 111 MET B C   1 
ATOM 3348 O O   . MET B 1 111 ? 10.130 -3.542  62.777  1.00 83.23  ? 111 MET B O   1 
ATOM 3349 C CB  . MET B 1 111 ? 12.242 -1.711  64.558  1.00 64.95  ? 111 MET B CB  1 
ATOM 3350 C CG  . MET B 1 111 ? 11.387 -0.707  63.801  1.00 67.94  ? 111 MET B CG  1 
ATOM 3351 S SD  . MET B 1 111 ? 12.139 0.921   63.710  1.00 73.17  ? 111 MET B SD  1 
ATOM 3352 C CE  . MET B 1 111 ? 13.630 0.491   62.818  1.00 68.90  ? 111 MET B CE  1 
ATOM 3353 N N   . ALA B 1 112 ? 12.308 -4.040  62.490  1.00 82.11  ? 112 ALA B N   1 
ATOM 3354 C CA  . ALA B 1 112 ? 12.092 -4.565  61.146  1.00 76.30  ? 112 ALA B CA  1 
ATOM 3355 C C   . ALA B 1 112 ? 11.112 -5.731  61.172  1.00 79.88  ? 112 ALA B C   1 
ATOM 3356 O O   . ALA B 1 112 ? 10.168 -5.782  60.375  1.00 84.06  ? 112 ALA B O   1 
ATOM 3357 C CB  . ALA B 1 112 ? 13.424 -4.987  60.525  1.00 75.95  ? 112 ALA B CB  1 
ATOM 3358 N N   . LEU B 1 113 ? 11.330 -6.684  62.082  1.00 82.56  ? 113 LEU B N   1 
ATOM 3359 C CA  . LEU B 1 113 ? 10.435 -7.831  62.198  1.00 77.91  ? 113 LEU B CA  1 
ATOM 3360 C C   . LEU B 1 113 ? 9.007  -7.385  62.500  1.00 80.09  ? 113 LEU B C   1 
ATOM 3361 O O   . LEU B 1 113 ? 8.060  -7.811  61.828  1.00 78.79  ? 113 LEU B O   1 
ATOM 3362 C CB  . LEU B 1 113 ? 10.947 -8.796  63.268  1.00 68.63  ? 113 LEU B CB  1 
ATOM 3363 C CG  . LEU B 1 113 ? 12.188 -9.603  62.877  1.00 68.31  ? 113 LEU B CG  1 
ATOM 3364 C CD1 . LEU B 1 113 ? 13.012 -9.961  64.103  1.00 72.51  ? 113 LEU B CD1 1 
ATOM 3365 C CD2 . LEU B 1 113 ? 11.804 -10.853 62.100  1.00 65.55  ? 113 LEU B CD2 1 
ATOM 3366 N N   . GLU B 1 114 ? 8.832  -6.544  63.527  1.00 76.82  ? 114 GLU B N   1 
ATOM 3367 C CA  . GLU B 1 114 ? 7.501  -6.031  63.847  1.00 75.06  ? 114 GLU B CA  1 
ATOM 3368 C C   . GLU B 1 114 ? 6.863  -5.361  62.638  1.00 73.77  ? 114 GLU B C   1 
ATOM 3369 O O   . GLU B 1 114 ? 5.674  -5.557  62.363  1.00 73.90  ? 114 GLU B O   1 
ATOM 3370 C CB  . GLU B 1 114 ? 7.567  -5.032  65.005  1.00 72.78  ? 114 GLU B CB  1 
ATOM 3371 C CG  . GLU B 1 114 ? 8.316  -5.488  66.242  1.00 81.50  ? 114 GLU B CG  1 
ATOM 3372 C CD  . GLU B 1 114 ? 8.299  -4.435  67.337  1.00 93.32  ? 114 GLU B CD  1 
ATOM 3373 O OE1 . GLU B 1 114 ? 7.209  -3.898  67.626  1.00 96.88  ? 114 GLU B OE1 1 
ATOM 3374 O OE2 . GLU B 1 114 ? 9.374  -4.134  67.899  1.00 91.99  ? 114 GLU B OE2 1 
ATOM 3375 N N   . ALA B 1 115 ? 7.641  -4.564  61.903  1.00 79.93  ? 115 ALA B N   1 
ATOM 3376 C CA  . ALA B 1 115 ? 7.125  -3.859  60.738  1.00 78.28  ? 115 ALA B CA  1 
ATOM 3377 C C   . ALA B 1 115 ? 6.784  -4.788  59.581  1.00 76.55  ? 115 ALA B C   1 
ATOM 3378 O O   . ALA B 1 115 ? 6.134  -4.346  58.628  1.00 75.66  ? 115 ALA B O   1 
ATOM 3379 C CB  . ALA B 1 115 ? 8.134  -2.808  60.272  1.00 74.46  ? 115 ALA B CB  1 
ATOM 3380 N N   . GLY B 1 116 ? 7.199  -6.049  59.637  1.00 74.78  ? 116 GLY B N   1 
ATOM 3381 C CA  . GLY B 1 116 ? 6.903  -6.996  58.585  1.00 78.38  ? 116 GLY B CA  1 
ATOM 3382 C C   . GLY B 1 116 ? 7.949  -7.092  57.499  1.00 79.57  ? 116 GLY B C   1 
ATOM 3383 O O   . GLY B 1 116 ? 7.680  -7.700  56.455  1.00 70.63  ? 116 GLY B O   1 
ATOM 3384 N N   . MET B 1 117 ? 9.130  -6.518  57.709  1.00 75.00  ? 117 MET B N   1 
ATOM 3385 C CA  . MET B 1 117 ? 10.218 -6.645  56.754  1.00 69.76  ? 117 MET B CA  1 
ATOM 3386 C C   . MET B 1 117 ? 10.928 -7.980  56.940  1.00 65.97  ? 117 MET B C   1 
ATOM 3387 O O   . MET B 1 117 ? 10.982 -8.530  58.044  1.00 67.92  ? 117 MET B O   1 
ATOM 3388 C CB  . MET B 1 117 ? 11.221 -5.503  56.919  1.00 70.68  ? 117 MET B CB  1 
ATOM 3389 C CG  . MET B 1 117 ? 10.769 -4.158  56.373  1.00 67.29  ? 117 MET B CG  1 
ATOM 3390 S SD  . MET B 1 117 ? 11.229 -2.815  57.488  1.00 71.97  ? 117 MET B SD  1 
ATOM 3391 C CE  . MET B 1 117 ? 10.706 -1.377  56.556  1.00 58.69  ? 117 MET B CE  1 
ATOM 3392 N N   . LYS B 1 118 ? 11.483 -8.498  55.845  1.00 64.65  ? 118 LYS B N   1 
ATOM 3393 C CA  . LYS B 1 118 ? 12.172 -9.778  55.875  1.00 67.16  ? 118 LYS B CA  1 
ATOM 3394 C C   . LYS B 1 118 ? 13.689 -9.659  55.805  1.00 66.07  ? 118 LYS B C   1 
ATOM 3395 O O   . LYS B 1 118 ? 14.377 -10.668 55.998  1.00 65.58  ? 118 LYS B O   1 
ATOM 3396 C CB  . LYS B 1 118 ? 11.693 -10.677 54.722  1.00 65.01  ? 118 LYS B CB  1 
ATOM 3397 C CG  . LYS B 1 118 ? 10.184 -10.735 54.517  1.00 60.52  ? 118 LYS B CG  1 
ATOM 3398 C CD  . LYS B 1 118 ? 9.440  -11.239 55.744  1.00 68.13  ? 118 LYS B CD  1 
ATOM 3399 C CE  . LYS B 1 118 ? 7.934  -11.208 55.508  1.00 71.50  ? 118 LYS B CE  1 
ATOM 3400 N NZ  . LYS B 1 118 ? 7.149  -11.304 56.770  1.00 82.93  ? 118 LYS B NZ  1 
ATOM 3401 N N   . TYR B 1 119 ? 14.234 -8.471  55.548  1.00 60.46  ? 119 TYR B N   1 
ATOM 3402 C CA  . TYR B 1 119 ? 15.682 -8.333  55.447  1.00 59.91  ? 119 TYR B CA  1 
ATOM 3403 C C   . TYR B 1 119 ? 16.091 -6.901  55.767  1.00 57.62  ? 119 TYR B C   1 
ATOM 3404 O O   . TYR B 1 119 ? 15.257 -5.997  55.868  1.00 55.05  ? 119 TYR B O   1 
ATOM 3405 C CB  . TYR B 1 119 ? 16.189 -8.767  54.065  1.00 53.04  ? 119 TYR B CB  1 
ATOM 3406 C CG  . TYR B 1 119 ? 15.718 -7.922  52.902  1.00 57.99  ? 119 TYR B CG  1 
ATOM 3407 C CD1 . TYR B 1 119 ? 14.466 -8.122  52.333  1.00 62.38  ? 119 TYR B CD1 1 
ATOM 3408 C CD2 . TYR B 1 119 ? 16.536 -6.943  52.356  1.00 59.07  ? 119 TYR B CD2 1 
ATOM 3409 C CE1 . TYR B 1 119 ? 14.038 -7.358  51.260  1.00 57.90  ? 119 TYR B CE1 1 
ATOM 3410 C CE2 . TYR B 1 119 ? 16.118 -6.176  51.285  1.00 57.33  ? 119 TYR B CE2 1 
ATOM 3411 C CZ  . TYR B 1 119 ? 14.870 -6.388  50.741  1.00 57.36  ? 119 TYR B CZ  1 
ATOM 3412 O OH  . TYR B 1 119 ? 14.454 -5.624  49.674  1.00 60.51  ? 119 TYR B OH  1 
ATOM 3413 N N   . VAL B 1 120 ? 17.402 -6.714  55.928  1.00 51.18  ? 120 VAL B N   1 
ATOM 3414 C CA  . VAL B 1 120 ? 17.992 -5.472  56.413  1.00 54.30  ? 120 VAL B CA  1 
ATOM 3415 C C   . VAL B 1 120 ? 19.180 -5.115  55.526  1.00 53.21  ? 120 VAL B C   1 
ATOM 3416 O O   . VAL B 1 120 ? 19.918 -5.999  55.078  1.00 55.27  ? 120 VAL B O   1 
ATOM 3417 C CB  . VAL B 1 120 ? 18.424 -5.606  57.892  1.00 55.89  ? 120 VAL B CB  1 
ATOM 3418 C CG1 . VAL B 1 120 ? 19.276 -4.427  58.333  1.00 54.55  ? 120 VAL B CG1 1 
ATOM 3419 C CG2 . VAL B 1 120 ? 17.203 -5.748  58.791  1.00 52.70  ? 120 VAL B CG2 1 
ATOM 3420 N N   . ASN B 1 121 ? 19.362 -3.817  55.274  1.00 50.69  ? 121 ASN B N   1 
ATOM 3421 C CA  . ASN B 1 121 ? 20.438 -3.307  54.432  1.00 54.49  ? 121 ASN B CA  1 
ATOM 3422 C C   . ASN B 1 121 ? 21.092 -2.124  55.132  1.00 47.74  ? 121 ASN B C   1 
ATOM 3423 O O   . ASN B 1 121 ? 20.402 -1.177  55.521  1.00 49.60  ? 121 ASN B O   1 
ATOM 3424 C CB  . ASN B 1 121 ? 19.898 -2.885  53.058  1.00 50.08  ? 121 ASN B CB  1 
ATOM 3425 C CG  . ASN B 1 121 ? 20.996 -2.645  52.037  1.00 48.14  ? 121 ASN B CG  1 
ATOM 3426 O OD1 . ASN B 1 121 ? 22.022 -2.033  52.334  1.00 54.41  ? 121 ASN B OD1 1 
ATOM 3427 N ND2 . ASN B 1 121 ? 20.776 -3.119  50.816  1.00 44.20  ? 121 ASN B ND2 1 
ATOM 3428 N N   . ILE B 1 122 ? 22.416 -2.172  55.291  1.00 44.06  ? 122 ILE B N   1 
ATOM 3429 C CA  . ILE B 1 122 ? 23.159 -1.101  55.948  1.00 53.38  ? 122 ILE B CA  1 
ATOM 3430 C C   . ILE B 1 122 ? 24.294 -0.626  55.050  1.00 48.53  ? 122 ILE B C   1 
ATOM 3431 O O   . ILE B 1 122 ? 24.939 -1.425  54.361  1.00 51.32  ? 122 ILE B O   1 
ATOM 3432 C CB  . ILE B 1 122 ? 23.710 -1.528  57.329  1.00 56.72  ? 122 ILE B CB  1 
ATOM 3433 C CG1 . ILE B 1 122 ? 24.318 -0.313  58.041  1.00 47.37  ? 122 ILE B CG1 1 
ATOM 3434 C CG2 . ILE B 1 122 ? 24.733 -2.653  57.194  1.00 43.27  ? 122 ILE B CG2 1 
ATOM 3435 C CD1 . ILE B 1 122 ? 24.070 -0.265  59.526  1.00 56.79  ? 122 ILE B CD1 1 
ATOM 3436 N N   . THR B 1 123 ? 24.516 0.685   55.046  1.00 44.16  ? 123 THR B N   1 
ATOM 3437 C CA  . THR B 1 123 ? 25.680 1.293   54.410  1.00 44.56  ? 123 THR B CA  1 
ATOM 3438 C C   . THR B 1 123 ? 26.931 0.901   55.182  1.00 44.95  ? 123 THR B C   1 
ATOM 3439 O O   . THR B 1 123 ? 27.226 1.465   56.238  1.00 46.48  ? 123 THR B O   1 
ATOM 3440 C CB  . THR B 1 123 ? 25.526 2.809   54.356  1.00 47.95  ? 123 THR B CB  1 
ATOM 3441 O OG1 . THR B 1 123 ? 25.176 3.302   55.656  1.00 42.66  ? 123 THR B OG1 1 
ATOM 3442 C CG2 . THR B 1 123 ? 24.441 3.196   53.366  1.00 44.74  ? 123 THR B CG2 1 
ATOM 3443 N N   . THR B 1 124 ? 27.677 -0.076  54.665  1.00 43.72  ? 124 THR B N   1 
ATOM 3444 C CA  . THR B 1 124 ? 28.956 -0.400  55.283  1.00 45.37  ? 124 THR B CA  1 
ATOM 3445 C C   . THR B 1 124 ? 29.964 0.715   55.056  1.00 44.25  ? 124 THR B C   1 
ATOM 3446 O O   . THR B 1 124 ? 30.817 0.967   55.915  1.00 49.07  ? 124 THR B O   1 
ATOM 3447 C CB  . THR B 1 124 ? 29.504 -1.716  54.727  1.00 44.16  ? 124 THR B CB  1 
ATOM 3448 O OG1 . THR B 1 124 ? 29.542 -1.653  53.296  1.00 42.91  ? 124 THR B OG1 1 
ATOM 3449 C CG2 . THR B 1 124 ? 28.622 -2.879  55.144  1.00 42.73  ? 124 THR B CG2 1 
ATOM 3450 N N   . ARG B 1 125 ? 29.869 1.397   53.918  1.00 43.81  ? 125 ARG B N   1 
ATOM 3451 C CA  . ARG B 1 125 ? 30.792 2.474   53.576  1.00 46.62  ? 125 ARG B CA  1 
ATOM 3452 C C   . ARG B 1 125 ? 30.188 3.264   52.427  1.00 52.98  ? 125 ARG B C   1 
ATOM 3453 O O   . ARG B 1 125 ? 29.959 2.703   51.350  1.00 48.06  ? 125 ARG B O   1 
ATOM 3454 C CB  . ARG B 1 125 ? 32.156 1.908   53.198  1.00 47.26  ? 125 ARG B CB  1 
ATOM 3455 C CG  . ARG B 1 125 ? 33.162 2.941   52.771  1.00 47.27  ? 125 ARG B CG  1 
ATOM 3456 C CD  . ARG B 1 125 ? 34.256 2.307   51.939  1.00 56.47  ? 125 ARG B CD  1 
ATOM 3457 N NE  . ARG B 1 125 ? 33.799 2.027   50.584  1.00 52.79  ? 125 ARG B NE  1 
ATOM 3458 C CZ  . ARG B 1 125 ? 34.361 2.522   49.491  1.00 49.00  ? 125 ARG B CZ  1 
ATOM 3459 N NH1 . ARG B 1 125 ? 35.416 3.317   49.555  1.00 50.26  ? 125 ARG B NH1 1 
ATOM 3460 N NH2 . ARG B 1 125 ? 33.852 2.212   48.303  1.00 52.42  ? 125 ARG B NH2 1 
ATOM 3461 N N   . HIS B 1 126 ? 29.925 4.550   52.650  1.00 46.35  ? 126 HIS B N   1 
ATOM 3462 C CA  . HIS B 1 126 ? 29.294 5.391   51.645  1.00 37.77  ? 126 HIS B CA  1 
ATOM 3463 C C   . HIS B 1 126 ? 30.369 6.097   50.816  1.00 48.59  ? 126 HIS B C   1 
ATOM 3464 O O   . HIS B 1 126 ? 31.546 5.727   50.838  1.00 45.75  ? 126 HIS B O   1 
ATOM 3465 C CB  . HIS B 1 126 ? 28.337 6.380   52.310  1.00 44.94  ? 126 HIS B CB  1 
ATOM 3466 C CG  . HIS B 1 126 ? 27.141 6.720   51.475  1.00 44.34  ? 126 HIS B CG  1 
ATOM 3467 N ND1 . HIS B 1 126 ? 27.143 7.744   50.551  1.00 50.43  ? 126 HIS B ND1 1 
ATOM 3468 C CD2 . HIS B 1 126 ? 25.902 6.176   51.428  1.00 42.83  ? 126 HIS B CD2 1 
ATOM 3469 C CE1 . HIS B 1 126 ? 25.959 7.814   49.970  1.00 45.58  ? 126 HIS B CE1 1 
ATOM 3470 N NE2 . HIS B 1 126 ? 25.187 6.873   50.484  1.00 45.87  ? 126 HIS B NE2 1 
ATOM 3471 N N   . HIS B 1 127 ? 29.963 7.125   50.065  1.00 50.99  ? 127 HIS B N   1 
ATOM 3472 C CA  . HIS B 1 127 ? 30.898 7.851   49.210  1.00 42.78  ? 127 HIS B CA  1 
ATOM 3473 C C   . HIS B 1 127 ? 32.030 8.493   50.007  1.00 46.60  ? 127 HIS B C   1 
ATOM 3474 O O   . HIS B 1 127 ? 33.131 8.677   49.474  1.00 48.93  ? 127 HIS B O   1 
ATOM 3475 C CB  . HIS B 1 127 ? 30.150 8.912   48.400  1.00 47.06  ? 127 HIS B CB  1 
ATOM 3476 C CG  . HIS B 1 127 ? 28.991 8.373   47.617  1.00 48.50  ? 127 HIS B CG  1 
ATOM 3477 N ND1 . HIS B 1 127 ? 28.911 7.058   47.214  1.00 45.10  ? 127 HIS B ND1 1 
ATOM 3478 C CD2 . HIS B 1 127 ? 27.866 8.975   47.162  1.00 50.60  ? 127 HIS B CD2 1 
ATOM 3479 C CE1 . HIS B 1 127 ? 27.786 6.872   46.545  1.00 50.15  ? 127 HIS B CE1 1 
ATOM 3480 N NE2 . HIS B 1 127 ? 27.134 8.020   46.499  1.00 45.88  ? 127 HIS B NE2 1 
ATOM 3481 N N   . ASP B 1 128 ? 31.789 8.842   51.274  1.00 52.27  ? 128 ASP B N   1 
ATOM 3482 C CA  . ASP B 1 128 ? 32.836 9.455   52.087  1.00 55.34  ? 128 ASP B CA  1 
ATOM 3483 C C   . ASP B 1 128 ? 33.910 8.465   52.524  1.00 58.73  ? 128 ASP B C   1 
ATOM 3484 O O   . ASP B 1 128 ? 34.923 8.893   53.090  1.00 63.58  ? 128 ASP B O   1 
ATOM 3485 C CB  . ASP B 1 128 ? 32.224 10.146  53.311  1.00 50.37  ? 128 ASP B CB  1 
ATOM 3486 C CG  . ASP B 1 128 ? 31.503 9.183   54.245  1.00 54.40  ? 128 ASP B CG  1 
ATOM 3487 O OD1 . ASP B 1 128 ? 31.535 7.955   54.015  1.00 49.70  ? 128 ASP B OD1 1 
ATOM 3488 O OD2 . ASP B 1 128 ? 30.895 9.667   55.224  1.00 54.65  ? 128 ASP B OD2 1 
ATOM 3489 N N   . SER B 1 129 ? 33.699 7.167   52.303  1.00 54.03  ? 129 SER B N   1 
ATOM 3490 C CA  . SER B 1 129 ? 34.654 6.084   52.532  1.00 53.93  ? 129 SER B CA  1 
ATOM 3491 C C   . SER B 1 129 ? 34.838 5.733   54.005  1.00 55.52  ? 129 SER B C   1 
ATOM 3492 O O   . SER B 1 129 ? 35.721 4.929   54.331  1.00 59.58  ? 129 SER B O   1 
ATOM 3493 C CB  . SER B 1 129 ? 36.022 6.377   51.903  1.00 57.62  ? 129 SER B CB  1 
ATOM 3494 O OG  . SER B 1 129 ? 36.420 5.318   51.048  1.00 59.79  ? 129 SER B OG  1 
ATOM 3495 N N   . PHE B 1 130 ? 34.034 6.296   54.903  1.00 55.65  ? 130 PHE B N   1 
ATOM 3496 C CA  . PHE B 1 130 ? 34.067 5.895   56.304  1.00 58.85  ? 130 PHE B CA  1 
ATOM 3497 C C   . PHE B 1 130 ? 33.369 4.548   56.450  1.00 49.03  ? 130 PHE B C   1 
ATOM 3498 O O   . PHE B 1 130 ? 32.279 4.346   55.908  1.00 50.02  ? 130 PHE B O   1 
ATOM 3499 C CB  . PHE B 1 130 ? 33.396 6.953   57.181  1.00 59.96  ? 130 PHE B CB  1 
ATOM 3500 C CG  . PHE B 1 130 ? 33.442 6.644   58.650  1.00 58.61  ? 130 PHE B CG  1 
ATOM 3501 C CD1 . PHE B 1 130 ? 34.643 6.662   59.340  1.00 59.68  ? 130 PHE B CD1 1 
ATOM 3502 C CD2 . PHE B 1 130 ? 32.281 6.341   59.344  1.00 62.64  ? 130 PHE B CD2 1 
ATOM 3503 C CE1 . PHE B 1 130 ? 34.687 6.378   60.693  1.00 63.61  ? 130 PHE B CE1 1 
ATOM 3504 C CE2 . PHE B 1 130 ? 32.318 6.058   60.698  1.00 61.70  ? 130 PHE B CE2 1 
ATOM 3505 C CZ  . PHE B 1 130 ? 33.523 6.076   61.373  1.00 65.57  ? 130 PHE B CZ  1 
ATOM 3506 N N   . CYS B 1 131 ? 33.995 3.627   57.180  1.00 52.03  ? 131 CYS B N   1 
ATOM 3507 C CA  . CYS B 1 131 ? 33.527 2.250   57.272  1.00 60.91  ? 131 CYS B CA  1 
ATOM 3508 C C   . CYS B 1 131 ? 32.896 1.962   58.628  1.00 63.37  ? 131 CYS B C   1 
ATOM 3509 O O   . CYS B 1 131 ? 33.399 2.401   59.668  1.00 64.51  ? 131 CYS B O   1 
ATOM 3510 C CB  . CYS B 1 131 ? 34.675 1.267   57.024  1.00 56.84  ? 131 CYS B CB  1 
ATOM 3511 S SG  . CYS B 1 131 ? 35.321 1.298   55.337  1.00 53.12  ? 131 CYS B SG  1 
ATOM 3512 N N   . LEU B 1 132 ? 31.793 1.212   58.605  1.00 55.05  ? 132 LEU B N   1 
ATOM 3513 C CA  . LEU B 1 132 ? 31.130 0.725   59.806  1.00 56.05  ? 132 LEU B CA  1 
ATOM 3514 C C   . LEU B 1 132 ? 31.617 -0.659  60.224  1.00 60.37  ? 132 LEU B C   1 
ATOM 3515 O O   . LEU B 1 132 ? 30.958 -1.320  61.034  1.00 58.02  ? 132 LEU B O   1 
ATOM 3516 C CB  . LEU B 1 132 ? 29.613 0.693   59.596  1.00 62.89  ? 132 LEU B CB  1 
ATOM 3517 C CG  . LEU B 1 132 ? 28.869 1.994   59.287  1.00 59.58  ? 132 LEU B CG  1 
ATOM 3518 C CD1 . LEU B 1 132 ? 27.381 1.823   59.555  1.00 54.69  ? 132 LEU B CD1 1 
ATOM 3519 C CD2 . LEU B 1 132 ? 29.429 3.151   60.095  1.00 53.01  ? 132 LEU B CD2 1 
ATOM 3520 N N   . PHE B 1 133 ? 32.750 -1.110  59.689  1.00 67.72  ? 133 PHE B N   1 
ATOM 3521 C CA  . PHE B 1 133 ? 33.284 -2.428  59.994  1.00 56.50  ? 133 PHE B CA  1 
ATOM 3522 C C   . PHE B 1 133 ? 34.795 -2.341  60.153  1.00 60.23  ? 133 PHE B C   1 
ATOM 3523 O O   . PHE B 1 133 ? 35.437 -1.405  59.672  1.00 69.23  ? 133 PHE B O   1 
ATOM 3524 C CB  . PHE B 1 133 ? 32.923 -3.445  58.901  1.00 55.89  ? 133 PHE B CB  1 
ATOM 3525 C CG  . PHE B 1 133 ? 33.524 -3.139  57.553  1.00 48.16  ? 133 PHE B CG  1 
ATOM 3526 C CD1 . PHE B 1 133 ? 32.967 -2.172  56.732  1.00 54.23  ? 133 PHE B CD1 1 
ATOM 3527 C CD2 . PHE B 1 133 ? 34.636 -3.831  57.103  1.00 50.55  ? 133 PHE B CD2 1 
ATOM 3528 C CE1 . PHE B 1 133 ? 33.515 -1.895  55.490  1.00 59.27  ? 133 PHE B CE1 1 
ATOM 3529 C CE2 . PHE B 1 133 ? 35.188 -3.559  55.863  1.00 51.81  ? 133 PHE B CE2 1 
ATOM 3530 C CZ  . PHE B 1 133 ? 34.627 -2.591  55.056  1.00 53.76  ? 133 PHE B CZ  1 
ATOM 3531 N N   . GLU B 1 134 ? 35.361 -3.333  60.838  1.00 56.56  ? 134 GLU B N   1 
ATOM 3532 C CA  . GLU B 1 134 ? 36.808 -3.384  60.994  1.00 57.52  ? 134 GLU B CA  1 
ATOM 3533 C C   . GLU B 1 134 ? 37.445 -3.778  59.670  1.00 64.21  ? 134 GLU B C   1 
ATOM 3534 O O   . GLU B 1 134 ? 37.037 -4.758  59.039  1.00 67.12  ? 134 GLU B O   1 
ATOM 3535 C CB  . GLU B 1 134 ? 37.207 -4.378  62.083  1.00 69.16  ? 134 GLU B CB  1 
ATOM 3536 C CG  . GLU B 1 134 ? 38.698 -4.694  62.087  1.00 73.04  ? 134 GLU B CG  1 
ATOM 3537 C CD  . GLU B 1 134 ? 39.134 -5.489  63.302  1.00 83.10  ? 134 GLU B CD  1 
ATOM 3538 O OE1 . GLU B 1 134 ? 38.259 -5.911  64.086  1.00 81.49  ? 134 GLU B OE1 1 
ATOM 3539 O OE2 . GLU B 1 134 ? 40.356 -5.689  63.471  1.00 88.59  ? 134 GLU B OE2 1 
ATOM 3540 N N   . SER B 1 135 ? 38.449 -3.016  59.248  1.00 65.21  ? 135 SER B N   1 
ATOM 3541 C CA  . SER B 1 135 ? 39.100 -3.258  57.971  1.00 65.12  ? 135 SER B CA  1 
ATOM 3542 C C   . SER B 1 135 ? 40.607 -3.180  58.140  1.00 74.66  ? 135 SER B C   1 
ATOM 3543 O O   . SER B 1 135 ? 41.122 -2.278  58.806  1.00 78.59  ? 135 SER B O   1 
ATOM 3544 C CB  . SER B 1 135 ? 38.640 -2.250  56.911  1.00 64.86  ? 135 SER B CB  1 
ATOM 3545 O OG  . SER B 1 135 ? 39.222 -2.537  55.652  1.00 75.92  ? 135 SER B OG  1 
ATOM 3546 N N   . LYS B 1 136 ? 41.306 -4.135  57.535  1.00 75.67  ? 136 LYS B N   1 
ATOM 3547 C CA  . LYS B 1 136 ? 42.760 -4.159  57.546  1.00 78.21  ? 136 LYS B CA  1 
ATOM 3548 C C   . LYS B 1 136 ? 43.357 -3.316  56.428  1.00 73.01  ? 136 LYS B C   1 
ATOM 3549 O O   . LYS B 1 136 ? 44.583 -3.180  56.356  1.00 70.65  ? 136 LYS B O   1 
ATOM 3550 C CB  . LYS B 1 136 ? 43.268 -5.603  57.447  1.00 72.97  ? 136 LYS B CB  1 
ATOM 3551 C CG  . LYS B 1 136 ? 43.443 -6.308  58.792  1.00 77.46  ? 136 LYS B CG  1 
ATOM 3552 C CD  . LYS B 1 136 ? 42.133 -6.389  59.570  1.00 80.38  ? 136 LYS B CD  1 
ATOM 3553 C CE  . LYS B 1 136 ? 41.958 -7.743  60.241  1.00 78.87  ? 136 LYS B CE  1 
ATOM 3554 N NZ  . LYS B 1 136 ? 40.527 -8.158  60.286  1.00 64.20  ? 136 LYS B NZ  1 
ATOM 3555 N N   . TYR B 1 137 ? 42.519 -2.743  55.564  1.00 74.36  ? 137 TYR B N   1 
ATOM 3556 C CA  . TYR B 1 137 ? 42.966 -1.918  54.452  1.00 67.49  ? 137 TYR B CA  1 
ATOM 3557 C C   . TYR B 1 137 ? 42.701 -0.440  54.684  1.00 71.04  ? 137 TYR B C   1 
ATOM 3558 O O   . TYR B 1 137 ? 43.060 0.382   53.834  1.00 74.16  ? 137 TYR B O   1 
ATOM 3559 C CB  . TYR B 1 137 ? 42.281 -2.355  53.151  1.00 70.26  ? 137 TYR B CB  1 
ATOM 3560 C CG  . TYR B 1 137 ? 42.557 -3.784  52.748  1.00 76.85  ? 137 TYR B CG  1 
ATOM 3561 C CD1 . TYR B 1 137 ? 43.693 -4.115  52.022  1.00 79.33  ? 137 TYR B CD1 1 
ATOM 3562 C CD2 . TYR B 1 137 ? 41.678 -4.802  53.089  1.00 77.92  ? 137 TYR B CD2 1 
ATOM 3563 C CE1 . TYR B 1 137 ? 43.947 -5.422  51.651  1.00 75.73  ? 137 TYR B CE1 1 
ATOM 3564 C CE2 . TYR B 1 137 ? 41.923 -6.111  52.725  1.00 72.46  ? 137 TYR B CE2 1 
ATOM 3565 C CZ  . TYR B 1 137 ? 43.060 -6.416  52.008  1.00 73.16  ? 137 TYR B CZ  1 
ATOM 3566 O OH  . TYR B 1 137 ? 43.305 -7.717  51.639  1.00 90.79  ? 137 TYR B OH  1 
ATOM 3567 N N   . THR B 1 138 ? 42.088 -0.082  55.809  1.00 75.51  ? 138 THR B N   1 
ATOM 3568 C CA  . THR B 1 138 ? 41.884 1.315   56.159  1.00 73.06  ? 138 THR B CA  1 
ATOM 3569 C C   . THR B 1 138 ? 41.714 1.423   57.667  1.00 64.01  ? 138 THR B C   1 
ATOM 3570 O O   . THR B 1 138 ? 41.209 0.506   58.320  1.00 67.18  ? 138 THR B O   1 
ATOM 3571 C CB  . THR B 1 138 ? 40.675 1.918   55.425  1.00 66.99  ? 138 THR B CB  1 
ATOM 3572 O OG1 . THR B 1 138 ? 40.795 3.346   55.388  1.00 65.93  ? 138 THR B OG1 1 
ATOM 3573 C CG2 . THR B 1 138 ? 39.364 1.537   56.098  1.00 64.17  ? 138 THR B CG2 1 
ATOM 3574 N N   . ASP B 1 139 ? 42.174 2.545   58.210  1.00 66.52  ? 139 ASP B N   1 
ATOM 3575 C CA  . ASP B 1 139 ? 41.993 2.872   59.615  1.00 68.26  ? 139 ASP B CA  1 
ATOM 3576 C C   . ASP B 1 139 ? 40.811 3.802   59.840  1.00 73.28  ? 139 ASP B C   1 
ATOM 3577 O O   . ASP B 1 139 ? 40.495 4.125   60.990  1.00 74.10  ? 139 ASP B O   1 
ATOM 3578 C CB  . ASP B 1 139 ? 43.276 3.498   60.171  1.00 76.01  ? 139 ASP B CB  1 
ATOM 3579 C CG  . ASP B 1 139 ? 44.524 2.762   59.719  1.00 81.70  ? 139 ASP B CG  1 
ATOM 3580 O OD1 . ASP B 1 139 ? 44.460 1.525   59.555  1.00 85.67  ? 139 ASP B OD1 1 
ATOM 3581 O OD2 . ASP B 1 139 ? 45.568 3.420   59.525  1.00 87.49  ? 139 ASP B OD2 1 
ATOM 3582 N N   . PHE B 1 140 ? 40.159 4.237   58.762  1.00 68.66  ? 140 PHE B N   1 
ATOM 3583 C CA  . PHE B 1 140 ? 39.031 5.166   58.808  1.00 59.31  ? 140 PHE B CA  1 
ATOM 3584 C C   . PHE B 1 140 ? 37.720 4.428   59.094  1.00 69.41  ? 140 PHE B C   1 
ATOM 3585 O O   . PHE B 1 140 ? 36.757 4.487   58.329  1.00 74.23  ? 140 PHE B O   1 
ATOM 3586 C CB  . PHE B 1 140 ? 38.955 5.924   57.489  1.00 58.78  ? 140 PHE B CB  1 
ATOM 3587 C CG  . PHE B 1 140 ? 38.216 7.222   57.570  1.00 62.50  ? 140 PHE B CG  1 
ATOM 3588 C CD1 . PHE B 1 140 ? 38.113 7.910   58.766  1.00 68.70  ? 140 PHE B CD1 1 
ATOM 3589 C CD2 . PHE B 1 140 ? 37.614 7.753   56.443  1.00 58.83  ? 140 PHE B CD2 1 
ATOM 3590 C CE1 . PHE B 1 140 ? 37.430 9.110   58.833  1.00 62.55  ? 140 PHE B CE1 1 
ATOM 3591 C CE2 . PHE B 1 140 ? 36.929 8.949   56.502  1.00 59.26  ? 140 PHE B CE2 1 
ATOM 3592 C CZ  . PHE B 1 140 ? 36.837 9.630   57.699  1.00 58.13  ? 140 PHE B CZ  1 
ATOM 3593 N N   . THR B 1 141 ? 37.688 3.724   60.225  1.00 71.82  ? 141 THR B N   1 
ATOM 3594 C CA  . THR B 1 141 ? 36.587 2.820   60.530  1.00 67.94  ? 141 THR B CA  1 
ATOM 3595 C C   . THR B 1 141 ? 35.965 3.151   61.880  1.00 74.98  ? 141 THR B C   1 
ATOM 3596 O O   . THR B 1 141 ? 36.549 3.851   62.712  1.00 74.01  ? 141 THR B O   1 
ATOM 3597 C CB  . THR B 1 141 ? 37.038 1.351   60.535  1.00 67.19  ? 141 THR B CB  1 
ATOM 3598 O OG1 . THR B 1 141 ? 37.718 1.061   61.763  1.00 76.97  ? 141 THR B OG1 1 
ATOM 3599 C CG2 . THR B 1 141 ? 37.965 1.066   59.369  1.00 61.85  ? 141 THR B CG2 1 
ATOM 3600 N N   . SER B 1 142 ? 34.749 2.631   62.075  1.00 69.62  ? 142 SER B N   1 
ATOM 3601 C CA  . SER B 1 142 ? 34.044 2.812   63.338  1.00 70.54  ? 142 SER B CA  1 
ATOM 3602 C C   . SER B 1 142 ? 34.722 2.062   64.478  1.00 73.32  ? 142 SER B C   1 
ATOM 3603 O O   . SER B 1 142 ? 34.592 2.459   65.642  1.00 74.88  ? 142 SER B O   1 
ATOM 3604 C CB  . SER B 1 142 ? 32.592 2.354   63.194  1.00 72.64  ? 142 SER B CB  1 
ATOM 3605 O OG  . SER B 1 142 ? 32.526 0.977   62.860  1.00 72.26  ? 142 SER B OG  1 
ATOM 3606 N N   . THR B 1 143 ? 35.434 0.975   64.169  1.00 70.87  ? 143 THR B N   1 
ATOM 3607 C CA  . THR B 1 143 ? 36.166 0.250   65.204  1.00 75.65  ? 143 THR B CA  1 
ATOM 3608 C C   . THR B 1 143 ? 37.298 1.095   65.773  1.00 77.14  ? 143 THR B C   1 
ATOM 3609 O O   . THR B 1 143 ? 37.584 1.034   66.974  1.00 80.20  ? 143 THR B O   1 
ATOM 3610 C CB  . THR B 1 143 ? 36.719 -1.062  64.646  1.00 78.24  ? 143 THR B CB  1 
ATOM 3611 O OG1 . THR B 1 143 ? 37.501 -0.794  63.475  1.00 70.56  ? 143 THR B OG1 1 
ATOM 3612 C CG2 . THR B 1 143 ? 35.589 -2.012  64.290  1.00 70.60  ? 143 THR B CG2 1 
ATOM 3613 N N   . ASN B 1 144 ? 37.961 1.881   64.926  1.00 74.14  ? 144 ASN B N   1 
ATOM 3614 C CA  . ASN B 1 144 ? 39.029 2.749   65.398  1.00 76.66  ? 144 ASN B CA  1 
ATOM 3615 C C   . ASN B 1 144 ? 38.506 4.066   65.952  1.00 78.16  ? 144 ASN B C   1 
ATOM 3616 O O   . ASN B 1 144 ? 39.183 4.688   66.777  1.00 80.01  ? 144 ASN B O   1 
ATOM 3617 C CB  . ASN B 1 144 ? 40.024 3.011   64.267  1.00 76.56  ? 144 ASN B CB  1 
ATOM 3618 C CG  . ASN B 1 144 ? 40.681 1.738   63.769  1.00 83.12  ? 144 ASN B CG  1 
ATOM 3619 O OD1 . ASN B 1 144 ? 40.667 0.712   64.449  1.00 78.33  ? 144 ASN B OD1 1 
ATOM 3620 N ND2 . ASN B 1 144 ? 41.258 1.797   62.576  1.00 83.96  ? 144 ASN B ND2 1 
ATOM 3621 N N   . SER B 1 145 ? 37.318 4.495   65.527  1.00 80.07  ? 145 SER B N   1 
ATOM 3622 C CA  . SER B 1 145 ? 36.705 5.707   66.038  1.00 77.15  ? 145 SER B CA  1 
ATOM 3623 C C   . SER B 1 145 ? 36.360 5.530   67.516  1.00 75.47  ? 145 SER B C   1 
ATOM 3624 O O   . SER B 1 145 ? 36.429 4.422   68.052  1.00 76.59  ? 145 SER B O   1 
ATOM 3625 C CB  . SER B 1 145 ? 35.461 6.044   65.216  1.00 77.34  ? 145 SER B CB  1 
ATOM 3626 O OG  . SER B 1 145 ? 34.278 5.682   65.907  1.00 77.69  ? 145 SER B OG  1 
ATOM 3627 N N   . PRO B 1 146 ? 35.993 6.625   68.212  1.00 72.40  ? 146 PRO B N   1 
ATOM 3628 C CA  . PRO B 1 146 ? 35.532 6.506   69.605  1.00 72.07  ? 146 PRO B CA  1 
ATOM 3629 C C   . PRO B 1 146 ? 34.456 5.452   69.821  1.00 76.54  ? 146 PRO B C   1 
ATOM 3630 O O   . PRO B 1 146 ? 34.287 4.960   70.942  1.00 82.32  ? 146 PRO B O   1 
ATOM 3631 C CB  . PRO B 1 146 ? 34.997 7.909   69.908  1.00 76.47  ? 146 PRO B CB  1 
ATOM 3632 C CG  . PRO B 1 146 ? 35.832 8.810   69.068  1.00 76.73  ? 146 PRO B CG  1 
ATOM 3633 C CD  . PRO B 1 146 ? 36.284 8.026   67.856  1.00 78.50  ? 146 PRO B CD  1 
ATOM 3634 N N   . ALA B 1 147 ? 33.722 5.096   68.763  1.00 81.29  ? 147 ALA B N   1 
ATOM 3635 C CA  . ALA B 1 147 ? 32.696 4.069   68.899  1.00 77.65  ? 147 ALA B CA  1 
ATOM 3636 C C   . ALA B 1 147 ? 33.312 2.722   69.246  1.00 72.66  ? 147 ALA B C   1 
ATOM 3637 O O   . ALA B 1 147 ? 32.719 1.945   70.003  1.00 76.33  ? 147 ALA B O   1 
ATOM 3638 C CB  . ALA B 1 147 ? 31.877 3.965   67.613  1.00 72.39  ? 147 ALA B CB  1 
ATOM 3639 N N   . LYS B 1 148 ? 34.499 2.433   68.707  1.00 72.90  ? 148 LYS B N   1 
ATOM 3640 C CA  . LYS B 1 148 ? 35.239 1.206   69.000  1.00 76.77  ? 148 LYS B CA  1 
ATOM 3641 C C   . LYS B 1 148 ? 34.405 -0.040  68.721  1.00 78.12  ? 148 LYS B C   1 
ATOM 3642 O O   . LYS B 1 148 ? 34.594 -1.082  69.354  1.00 76.14  ? 148 LYS B O   1 
ATOM 3643 C CB  . LYS B 1 148 ? 35.743 1.199   70.447  1.00 82.46  ? 148 LYS B CB  1 
ATOM 3644 C CG  . LYS B 1 148 ? 36.669 2.358   70.784  1.00 78.28  ? 148 LYS B CG  1 
ATOM 3645 C CD  . LYS B 1 148 ? 37.989 2.237   70.042  1.00 77.06  ? 148 LYS B CD  1 
ATOM 3646 C CE  . LYS B 1 148 ? 38.860 3.462   70.257  1.00 69.54  ? 148 LYS B CE  1 
ATOM 3647 N NZ  . LYS B 1 148 ? 40.110 3.393   69.450  1.00 64.38  ? 148 LYS B NZ  1 
ATOM 3648 N N   . ARG B 1 149 ? 33.482 0.056   67.768  1.00 81.10  ? 149 ARG B N   1 
ATOM 3649 C CA  . ARG B 1 149 ? 32.550 -1.020  67.479  1.00 76.39  ? 149 ARG B CA  1 
ATOM 3650 C C   . ARG B 1 149 ? 32.585 -1.390  66.003  1.00 76.75  ? 149 ARG B C   1 
ATOM 3651 O O   . ARG B 1 149 ? 32.872 -0.556  65.139  1.00 73.63  ? 149 ARG B O   1 
ATOM 3652 C CB  . ARG B 1 149 ? 31.130 -0.625  67.889  1.00 68.17  ? 149 ARG B CB  1 
ATOM 3653 C CG  . ARG B 1 149 ? 30.903 -0.664  69.389  1.00 65.81  ? 149 ARG B CG  1 
ATOM 3654 C CD  . ARG B 1 149 ? 29.671 0.126   69.779  1.00 71.89  ? 149 ARG B CD  1 
ATOM 3655 N NE  . ARG B 1 149 ? 28.445 -0.610  69.496  1.00 65.02  ? 149 ARG B NE  1 
ATOM 3656 C CZ  . ARG B 1 149 ? 27.243 -0.058  69.415  1.00 63.05  ? 149 ARG B CZ  1 
ATOM 3657 N NH1 . ARG B 1 149 ? 27.064 1.240   69.602  1.00 66.01  ? 149 ARG B NH1 1 
ATOM 3658 N NH2 . ARG B 1 149 ? 26.193 -0.826  69.139  1.00 70.22  ? 149 ARG B NH2 1 
ATOM 3659 N N   . ASP B 1 150 ? 32.284 -2.659  65.730  1.00 72.52  ? 150 ASP B N   1 
ATOM 3660 C CA  . ASP B 1 150 ? 32.092 -3.173  64.374  1.00 63.23  ? 150 ASP B CA  1 
ATOM 3661 C C   . ASP B 1 150 ? 30.587 -3.259  64.143  1.00 64.19  ? 150 ASP B C   1 
ATOM 3662 O O   . ASP B 1 150 ? 29.950 -4.265  64.455  1.00 67.38  ? 150 ASP B O   1 
ATOM 3663 C CB  . ASP B 1 150 ? 32.775 -4.526  64.206  1.00 63.35  ? 150 ASP B CB  1 
ATOM 3664 C CG  . ASP B 1 150 ? 32.933 -4.930  62.752  1.00 66.08  ? 150 ASP B CG  1 
ATOM 3665 O OD1 . ASP B 1 150 ? 31.963 -4.785  61.978  1.00 65.43  ? 150 ASP B OD1 1 
ATOM 3666 O OD2 . ASP B 1 150 ? 34.030 -5.402  62.384  1.00 66.25  ? 150 ASP B OD2 1 
ATOM 3667 N N   . LEU B 1 151 ? 30.016 -2.186  63.588  1.00 62.67  ? 151 LEU B N   1 
ATOM 3668 C CA  . LEU B 1 151 ? 28.565 -2.110  63.447  1.00 62.09  ? 151 LEU B CA  1 
ATOM 3669 C C   . LEU B 1 151 ? 28.029 -3.145  62.467  1.00 62.32  ? 151 LEU B C   1 
ATOM 3670 O O   . LEU B 1 151 ? 26.871 -3.564  62.583  1.00 52.05  ? 151 LEU B O   1 
ATOM 3671 C CB  . LEU B 1 151 ? 28.155 -0.704  63.012  1.00 56.88  ? 151 LEU B CB  1 
ATOM 3672 C CG  . LEU B 1 151 ? 28.332 0.387   64.069  1.00 66.52  ? 151 LEU B CG  1 
ATOM 3673 C CD1 . LEU B 1 151 ? 27.523 1.622   63.708  1.00 68.50  ? 151 LEU B CD1 1 
ATOM 3674 C CD2 . LEU B 1 151 ? 27.944 -0.131  65.448  1.00 67.22  ? 151 LEU B CD2 1 
ATOM 3675 N N   . VAL B 1 152 ? 28.844 -3.567  61.498  1.00 63.10  ? 152 VAL B N   1 
ATOM 3676 C CA  . VAL B 1 152 ? 28.418 -4.624  60.588  1.00 59.87  ? 152 VAL B CA  1 
ATOM 3677 C C   . VAL B 1 152 ? 28.332 -5.959  61.316  1.00 67.57  ? 152 VAL B C   1 
ATOM 3678 O O   . VAL B 1 152 ? 27.378 -6.723  61.127  1.00 72.84  ? 152 VAL B O   1 
ATOM 3679 C CB  . VAL B 1 152 ? 29.365 -4.696  59.377  1.00 55.98  ? 152 VAL B CB  1 
ATOM 3680 C CG1 . VAL B 1 152 ? 28.972 -5.845  58.462  1.00 53.87  ? 152 VAL B CG1 1 
ATOM 3681 C CG2 . VAL B 1 152 ? 29.349 -3.379  58.625  1.00 58.79  ? 152 VAL B CG2 1 
ATOM 3682 N N   . ALA B 1 153 ? 29.319 -6.260  62.164  1.00 67.60  ? 153 ALA B N   1 
ATOM 3683 C CA  . ALA B 1 153 ? 29.278 -7.491  62.949  1.00 62.37  ? 153 ALA B CA  1 
ATOM 3684 C C   . ALA B 1 153 ? 28.079 -7.510  63.889  1.00 64.35  ? 153 ALA B C   1 
ATOM 3685 O O   . ALA B 1 153 ? 27.364 -8.515  63.983  1.00 62.66  ? 153 ALA B O   1 
ATOM 3686 C CB  . ALA B 1 153 ? 30.580 -7.653  63.732  1.00 61.00  ? 153 ALA B CB  1 
ATOM 3687 N N   . GLU B 1 154 ? 27.849 -6.404  64.599  1.00 59.08  ? 154 GLU B N   1 
ATOM 3688 C CA  . GLU B 1 154 ? 26.716 -6.322  65.517  1.00 63.65  ? 154 GLU B CA  1 
ATOM 3689 C C   . GLU B 1 154 ? 25.399 -6.571  64.792  1.00 66.18  ? 154 GLU B C   1 
ATOM 3690 O O   . GLU B 1 154 ? 24.572 -7.373  65.240  1.00 69.39  ? 154 GLU B O   1 
ATOM 3691 C CB  . GLU B 1 154 ? 26.717 -4.963  66.216  1.00 67.74  ? 154 GLU B CB  1 
ATOM 3692 C CG  . GLU B 1 154 ? 27.983 -4.715  67.025  1.00 68.48  ? 154 GLU B CG  1 
ATOM 3693 C CD  . GLU B 1 154 ? 27.958 -3.410  67.791  1.00 75.70  ? 154 GLU B CD  1 
ATOM 3694 O OE1 . GLU B 1 154 ? 26.859 -2.854  68.000  1.00 76.50  ? 154 GLU B OE1 1 
ATOM 3695 O OE2 . GLU B 1 154 ? 29.045 -2.944  68.191  1.00 70.06  ? 154 GLU B OE2 1 
ATOM 3696 N N   . LEU B 1 155 ? 25.180 -5.880  63.672  1.00 74.96  ? 155 LEU B N   1 
ATOM 3697 C CA  . LEU B 1 155 ? 23.938 -6.058  62.925  1.00 68.81  ? 155 LEU B CA  1 
ATOM 3698 C C   . LEU B 1 155 ? 23.852 -7.444  62.293  1.00 64.02  ? 155 LEU B C   1 
ATOM 3699 O O   . LEU B 1 155 ? 22.767 -8.034  62.233  1.00 63.33  ? 155 LEU B O   1 
ATOM 3700 C CB  . LEU B 1 155 ? 23.806 -4.974  61.857  1.00 63.54  ? 155 LEU B CB  1 
ATOM 3701 C CG  . LEU B 1 155 ? 22.607 -4.042  62.033  1.00 61.95  ? 155 LEU B CG  1 
ATOM 3702 C CD1 . LEU B 1 155 ? 22.473 -3.119  60.841  1.00 64.65  ? 155 LEU B CD1 1 
ATOM 3703 C CD2 . LEU B 1 155 ? 21.333 -4.844  62.236  1.00 66.91  ? 155 LEU B CD2 1 
ATOM 3704 N N   . ALA B 1 156 ? 24.977 -7.971  61.798  1.00 64.72  ? 156 ALA B N   1 
ATOM 3705 C CA  . ALA B 1 156 ? 24.962 -9.276  61.138  1.00 71.20  ? 156 ALA B CA  1 
ATOM 3706 C C   . ALA B 1 156 ? 24.513 -10.377 62.090  1.00 74.75  ? 156 ALA B C   1 
ATOM 3707 O O   . ALA B 1 156 ? 23.642 -11.188 61.753  1.00 70.70  ? 156 ALA B O   1 
ATOM 3708 C CB  . ALA B 1 156 ? 26.344 -9.597  60.568  1.00 65.53  ? 156 ALA B CB  1 
ATOM 3709 N N   . GLU B 1 157 ? 25.106 -10.426 63.286  1.00 79.85  ? 157 GLU B N   1 
ATOM 3710 C CA  . GLU B 1 157 ? 24.738 -11.454 64.254  1.00 79.48  ? 157 GLU B CA  1 
ATOM 3711 C C   . GLU B 1 157 ? 23.268 -11.346 64.632  1.00 78.11  ? 157 GLU B C   1 
ATOM 3712 O O   . GLU B 1 157 ? 22.572 -12.362 64.754  1.00 75.38  ? 157 GLU B O   1 
ATOM 3713 C CB  . GLU B 1 157 ? 25.622 -11.345 65.497  1.00 80.30  ? 157 GLU B CB  1 
ATOM 3714 C CG  . GLU B 1 157 ? 25.443 -12.479 66.497  1.00 87.28  ? 157 GLU B CG  1 
ATOM 3715 C CD  . GLU B 1 157 ? 25.751 -13.840 65.903  1.00 90.09  ? 157 GLU B CD  1 
ATOM 3716 O OE1 . GLU B 1 157 ? 26.898 -14.047 65.452  1.00 88.52  ? 157 GLU B OE1 1 
ATOM 3717 O OE2 . GLU B 1 157 ? 24.849 -14.705 65.892  1.00 88.85  ? 157 GLU B OE2 1 
ATOM 3718 N N   . GLU B 1 158 ? 22.781 -10.120 64.826  1.00 68.55  ? 158 GLU B N   1 
ATOM 3719 C CA  . GLU B 1 158 ? 21.377 -9.925  65.164  1.00 69.91  ? 158 GLU B CA  1 
ATOM 3720 C C   . GLU B 1 158 ? 20.452 -10.396 64.048  1.00 73.05  ? 158 GLU B C   1 
ATOM 3721 O O   . GLU B 1 158 ? 19.322 -10.815 64.317  1.00 75.66  ? 158 GLU B O   1 
ATOM 3722 C CB  . GLU B 1 158 ? 21.124 -8.455  65.490  1.00 74.00  ? 158 GLU B CB  1 
ATOM 3723 C CG  . GLU B 1 158 ? 20.190 -8.238  66.663  1.00 86.06  ? 158 GLU B CG  1 
ATOM 3724 C CD  . GLU B 1 158 ? 20.781 -8.683  67.985  1.00 93.60  ? 158 GLU B CD  1 
ATOM 3725 O OE1 . GLU B 1 158 ? 20.672 -9.882  68.319  1.00 91.50  ? 158 GLU B OE1 1 
ATOM 3726 O OE2 . GLU B 1 158 ? 21.356 -7.830  68.695  1.00 90.07  ? 158 GLU B OE2 1 
ATOM 3727 N N   . CYS B 1 159 ? 20.905 -10.335 62.794  1.00 78.04  ? 159 CYS B N   1 
ATOM 3728 C CA  . CYS B 1 159 ? 20.093 -10.839 61.691  1.00 69.16  ? 159 CYS B CA  1 
ATOM 3729 C C   . CYS B 1 159 ? 20.132 -12.361 61.628  1.00 71.83  ? 159 CYS B C   1 
ATOM 3730 O O   . CYS B 1 159 ? 19.085 -13.015 61.557  1.00 73.32  ? 159 CYS B O   1 
ATOM 3731 C CB  . CYS B 1 159 ? 20.569 -10.239 60.367  1.00 64.65  ? 159 CYS B CB  1 
ATOM 3732 S SG  . CYS B 1 159 ? 20.174 -8.489  60.154  1.00 76.92  ? 159 CYS B SG  1 
ATOM 3733 N N   . ARG B 1 160 ? 21.339 -12.935 61.647  1.00 74.91  ? 160 ARG B N   1 
ATOM 3734 C CA  . ARG B 1 160 ? 21.495 -14.386 61.599  1.00 70.45  ? 160 ARG B CA  1 
ATOM 3735 C C   . ARG B 1 160 ? 20.710 -15.068 62.712  1.00 73.68  ? 160 ARG B C   1 
ATOM 3736 O O   . ARG B 1 160 ? 20.107 -16.128 62.502  1.00 78.27  ? 160 ARG B O   1 
ATOM 3737 C CB  . ARG B 1 160 ? 22.982 -14.739 61.683  1.00 71.59  ? 160 ARG B CB  1 
ATOM 3738 C CG  . ARG B 1 160 ? 23.312 -15.984 62.489  1.00 72.44  ? 160 ARG B CG  1 
ATOM 3739 C CD  . ARG B 1 160 ? 24.719 -16.486 62.183  1.00 77.18  ? 160 ARG B CD  1 
ATOM 3740 N NE  . ARG B 1 160 ? 25.751 -15.545 62.607  1.00 87.57  ? 160 ARG B NE  1 
ATOM 3741 C CZ  . ARG B 1 160 ? 26.381 -14.703 61.798  1.00 87.40  ? 160 ARG B CZ  1 
ATOM 3742 N NH1 . ARG B 1 160 ? 26.106 -14.651 60.504  1.00 82.65  ? 160 ARG B NH1 1 
ATOM 3743 N NH2 . ARG B 1 160 ? 27.311 -13.893 62.299  1.00 75.32  ? 160 ARG B NH2 1 
ATOM 3744 N N   . LYS B 1 161 ? 20.694 -14.463 63.901  1.00 75.93  ? 161 LYS B N   1 
ATOM 3745 C CA  . LYS B 1 161 ? 19.932 -15.019 65.014  1.00 75.39  ? 161 LYS B CA  1 
ATOM 3746 C C   . LYS B 1 161 ? 18.434 -14.998 64.729  1.00 72.88  ? 161 LYS B C   1 
ATOM 3747 O O   . LYS B 1 161 ? 17.706 -15.914 65.128  1.00 81.71  ? 161 LYS B O   1 
ATOM 3748 C CB  . LYS B 1 161 ? 20.238 -14.243 66.293  1.00 77.52  ? 161 LYS B CB  1 
ATOM 3749 C CG  . LYS B 1 161 ? 21.104 -14.985 67.297  1.00 74.49  ? 161 LYS B CG  1 
ATOM 3750 C CD  . LYS B 1 161 ? 21.309 -14.159 68.564  1.00 86.19  ? 161 LYS B CD  1 
ATOM 3751 C CE  . LYS B 1 161 ? 20.138 -13.213 68.817  1.00 80.22  ? 161 LYS B CE  1 
ATOM 3752 N NZ  . LYS B 1 161 ? 20.357 -12.345 70.006  1.00 75.90  ? 161 LYS B NZ  1 
ATOM 3753 N N   . LYS B 1 162 ? 17.957 -13.964 64.037  1.00 70.81  ? 162 LYS B N   1 
ATOM 3754 C CA  . LYS B 1 162 ? 16.530 -13.710 63.886  1.00 63.30  ? 162 LYS B CA  1 
ATOM 3755 C C   . LYS B 1 162 ? 16.004 -14.070 62.502  1.00 66.50  ? 162 LYS B C   1 
ATOM 3756 O O   . LYS B 1 162 ? 14.865 -13.720 62.174  1.00 69.36  ? 162 LYS B O   1 
ATOM 3757 C CB  . LYS B 1 162 ? 16.224 -12.244 64.203  1.00 63.60  ? 162 LYS B CB  1 
ATOM 3758 C CG  . LYS B 1 162 ? 16.684 -11.804 65.586  1.00 66.06  ? 162 LYS B CG  1 
ATOM 3759 C CD  . LYS B 1 162 ? 16.146 -10.428 65.946  1.00 58.90  ? 162 LYS B CD  1 
ATOM 3760 C CE  . LYS B 1 162 ? 16.832 -9.880  67.187  1.00 67.12  ? 162 LYS B CE  1 
ATOM 3761 N NZ  . LYS B 1 162 ? 16.220 -8.601  67.640  1.00 79.65  ? 162 LYS B NZ  1 
ATOM 3762 N N   . GLY B 1 163 ? 16.800 -14.756 61.683  1.00 60.98  ? 163 GLY B N   1 
ATOM 3763 C CA  . GLY B 1 163 ? 16.333 -15.190 60.380  1.00 69.74  ? 163 GLY B CA  1 
ATOM 3764 C C   . GLY B 1 163 ? 16.158 -14.098 59.348  1.00 73.46  ? 163 GLY B C   1 
ATOM 3765 O O   . GLY B 1 163 ? 15.484 -14.319 58.338  1.00 65.72  ? 163 GLY B O   1 
ATOM 3766 N N   . LEU B 1 164 ? 16.740 -12.924 59.570  1.00 67.54  ? 164 LEU B N   1 
ATOM 3767 C CA  . LEU B 1 164 ? 16.628 -11.820 58.628  1.00 58.66  ? 164 LEU B CA  1 
ATOM 3768 C C   . LEU B 1 164 ? 17.731 -11.892 57.579  1.00 59.10  ? 164 LEU B C   1 
ATOM 3769 O O   . LEU B 1 164 ? 18.886 -12.196 57.892  1.00 52.80  ? 164 LEU B O   1 
ATOM 3770 C CB  . LEU B 1 164 ? 16.696 -10.480 59.362  1.00 56.50  ? 164 LEU B CB  1 
ATOM 3771 C CG  . LEU B 1 164 ? 15.436 -10.053 60.117  1.00 65.72  ? 164 LEU B CG  1 
ATOM 3772 C CD1 . LEU B 1 164 ? 15.790 -9.142  61.280  1.00 67.51  ? 164 LEU B CD1 1 
ATOM 3773 C CD2 . LEU B 1 164 ? 14.452 -9.367  59.181  1.00 54.91  ? 164 LEU B CD2 1 
ATOM 3774 N N   . GLY B 1 165 ? 17.360 -11.627 56.329  1.00 59.71  ? 165 GLY B N   1 
ATOM 3775 C CA  . GLY B 1 165 ? 18.354 -11.489 55.279  1.00 44.68  ? 165 GLY B CA  1 
ATOM 3776 C C   . GLY B 1 165 ? 19.192 -10.241 55.493  1.00 48.72  ? 165 GLY B C   1 
ATOM 3777 O O   . GLY B 1 165 ? 18.702 -9.208  55.952  1.00 52.09  ? 165 GLY B O   1 
ATOM 3778 N N   . PHE B 1 166 ? 20.479 -10.341 55.173  1.00 46.34  ? 166 PHE B N   1 
ATOM 3779 C CA  . PHE B 1 166 ? 21.420 -9.257  55.427  1.00 51.31  ? 166 PHE B CA  1 
ATOM 3780 C C   . PHE B 1 166 ? 22.121 -8.861  54.138  1.00 55.19  ? 166 PHE B C   1 
ATOM 3781 O O   . PHE B 1 166 ? 22.818 -9.680  53.530  1.00 48.38  ? 166 PHE B O   1 
ATOM 3782 C CB  . PHE B 1 166 ? 22.449 -9.658  56.483  1.00 48.47  ? 166 PHE B CB  1 
ATOM 3783 C CG  . PHE B 1 166 ? 23.128 -8.489  57.125  1.00 56.47  ? 166 PHE B CG  1 
ATOM 3784 C CD1 . PHE B 1 166 ? 22.445 -7.299  57.312  1.00 56.21  ? 166 PHE B CD1 1 
ATOM 3785 C CD2 . PHE B 1 166 ? 24.449 -8.569  57.528  1.00 58.03  ? 166 PHE B CD2 1 
ATOM 3786 C CE1 . PHE B 1 166 ? 23.062 -6.215  57.900  1.00 65.09  ? 166 PHE B CE1 1 
ATOM 3787 C CE2 . PHE B 1 166 ? 25.073 -7.486  58.115  1.00 57.85  ? 166 PHE B CE2 1 
ATOM 3788 C CZ  . PHE B 1 166 ? 24.378 -6.308  58.302  1.00 62.23  ? 166 PHE B CZ  1 
ATOM 3789 N N   . TYR B 1 167 ? 21.961 -7.601  53.741  1.00 54.05  ? 167 TYR B N   1 
ATOM 3790 C CA  . TYR B 1 167 ? 22.574 -7.077  52.531  1.00 48.45  ? 167 TYR B CA  1 
ATOM 3791 C C   . TYR B 1 167 ? 23.433 -5.871  52.886  1.00 49.01  ? 167 TYR B C   1 
ATOM 3792 O O   . TYR B 1 167 ? 23.103 -5.096  53.789  1.00 57.40  ? 167 TYR B O   1 
ATOM 3793 C CB  . TYR B 1 167 ? 21.509 -6.706  51.490  1.00 40.97  ? 167 TYR B CB  1 
ATOM 3794 C CG  . TYR B 1 167 ? 20.688 -7.896  51.041  1.00 49.77  ? 167 TYR B CG  1 
ATOM 3795 C CD1 . TYR B 1 167 ? 19.649 -8.384  51.824  1.00 37.74  ? 167 TYR B CD1 1 
ATOM 3796 C CD2 . TYR B 1 167 ? 20.964 -8.543  49.843  1.00 53.14  ? 167 TYR B CD2 1 
ATOM 3797 C CE1 . TYR B 1 167 ? 18.904 -9.474  51.424  1.00 45.56  ? 167 TYR B CE1 1 
ATOM 3798 C CE2 . TYR B 1 167 ? 20.222 -9.637  49.433  1.00 46.31  ? 167 TYR B CE2 1 
ATOM 3799 C CZ  . TYR B 1 167 ? 19.193 -10.098 50.229  1.00 52.58  ? 167 TYR B CZ  1 
ATOM 3800 O OH  . TYR B 1 167 ? 18.450 -11.188 49.832  1.00 54.68  ? 167 TYR B OH  1 
ATOM 3801 N N   . LEU B 1 168 ? 24.541 -5.720  52.166  1.00 46.08  ? 168 LEU B N   1 
ATOM 3802 C CA  . LEU B 1 168 ? 25.595 -4.775  52.522  1.00 43.20  ? 168 LEU B CA  1 
ATOM 3803 C C   . LEU B 1 168 ? 25.741 -3.730  51.424  1.00 46.73  ? 168 LEU B C   1 
ATOM 3804 O O   . LEU B 1 168 ? 26.198 -4.042  50.319  1.00 45.05  ? 168 LEU B O   1 
ATOM 3805 C CB  . LEU B 1 168 ? 26.918 -5.503  52.754  1.00 40.31  ? 168 LEU B CB  1 
ATOM 3806 C CG  . LEU B 1 168 ? 26.848 -6.723  53.672  1.00 47.28  ? 168 LEU B CG  1 
ATOM 3807 C CD1 . LEU B 1 168 ? 28.202 -7.413  53.762  1.00 43.88  ? 168 LEU B CD1 1 
ATOM 3808 C CD2 . LEU B 1 168 ? 26.357 -6.311  55.048  1.00 44.45  ? 168 LEU B CD2 1 
ATOM 3809 N N   . TYR B 1 169 ? 25.363 -2.492  51.731  1.00 41.68  ? 169 TYR B N   1 
ATOM 3810 C CA  . TYR B 1 169 ? 25.681 -1.375  50.855  1.00 42.89  ? 169 TYR B CA  1 
ATOM 3811 C C   . TYR B 1 169 ? 27.187 -1.142  50.863  1.00 43.47  ? 169 TYR B C   1 
ATOM 3812 O O   . TYR B 1 169 ? 27.814 -1.106  51.926  1.00 45.56  ? 169 TYR B O   1 
ATOM 3813 C CB  . TYR B 1 169 ? 24.931 -0.119  51.311  1.00 46.62  ? 169 TYR B CB  1 
ATOM 3814 C CG  . TYR B 1 169 ? 25.204 1.148   50.516  1.00 42.11  ? 169 TYR B CG  1 
ATOM 3815 C CD1 . TYR B 1 169 ? 26.413 1.828   50.628  1.00 42.97  ? 169 TYR B CD1 1 
ATOM 3816 C CD2 . TYR B 1 169 ? 24.238 1.677   49.671  1.00 42.16  ? 169 TYR B CD2 1 
ATOM 3817 C CE1 . TYR B 1 169 ? 26.659 2.980   49.908  1.00 41.34  ? 169 TYR B CE1 1 
ATOM 3818 C CE2 . TYR B 1 169 ? 24.474 2.832   48.950  1.00 45.61  ? 169 TYR B CE2 1 
ATOM 3819 C CZ  . TYR B 1 169 ? 25.686 3.479   49.073  1.00 40.16  ? 169 TYR B CZ  1 
ATOM 3820 O OH  . TYR B 1 169 ? 25.925 4.628   48.356  1.00 40.93  ? 169 TYR B OH  1 
ATOM 3821 N N   . TYR B 1 170 ? 27.770 -0.996  49.674  1.00 39.87  ? 170 TYR B N   1 
ATOM 3822 C CA  . TYR B 1 170 ? 29.187 -0.677  49.536  1.00 40.43  ? 170 TYR B CA  1 
ATOM 3823 C C   . TYR B 1 170 ? 29.361 0.269   48.357  1.00 49.90  ? 170 TYR B C   1 
ATOM 3824 O O   . TYR B 1 170 ? 28.946 -0.050  47.239  1.00 50.88  ? 170 TYR B O   1 
ATOM 3825 C CB  . TYR B 1 170 ? 30.028 -1.945  49.349  1.00 35.93  ? 170 TYR B CB  1 
ATOM 3826 C CG  . TYR B 1 170 ? 31.516 -1.681  49.298  1.00 48.77  ? 170 TYR B CG  1 
ATOM 3827 C CD1 . TYR B 1 170 ? 32.155 -1.417  48.092  1.00 54.48  ? 170 TYR B CD1 1 
ATOM 3828 C CD2 . TYR B 1 170 ? 32.280 -1.678  50.458  1.00 53.32  ? 170 TYR B CD2 1 
ATOM 3829 C CE1 . TYR B 1 170 ? 33.515 -1.166  48.043  1.00 53.35  ? 170 TYR B CE1 1 
ATOM 3830 C CE2 . TYR B 1 170 ? 33.639 -1.428  50.419  1.00 51.37  ? 170 TYR B CE2 1 
ATOM 3831 C CZ  . TYR B 1 170 ? 34.250 -1.173  49.210  1.00 54.18  ? 170 TYR B CZ  1 
ATOM 3832 O OH  . TYR B 1 170 ? 35.601 -0.924  49.169  1.00 54.08  ? 170 TYR B OH  1 
ATOM 3833 N N   . SER B 1 171 ? 29.974 1.424   48.610  1.00 45.21  ? 171 SER B N   1 
ATOM 3834 C CA  . SER B 1 171 ? 30.166 2.430   47.572  1.00 45.83  ? 171 SER B CA  1 
ATOM 3835 C C   . SER B 1 171 ? 31.193 1.955   46.552  1.00 47.60  ? 171 SER B C   1 
ATOM 3836 O O   . SER B 1 171 ? 32.296 1.539   46.917  1.00 49.93  ? 171 SER B O   1 
ATOM 3837 C CB  . SER B 1 171 ? 30.611 3.751   48.197  1.00 49.11  ? 171 SER B CB  1 
ATOM 3838 O OG  . SER B 1 171 ? 31.000 4.684   47.204  1.00 49.32  ? 171 SER B OG  1 
ATOM 3839 N N   . HIS B 1 172 ? 30.832 2.010   45.268  1.00 53.54  ? 172 HIS B N   1 
ATOM 3840 C CA  . HIS B 1 172 ? 31.681 1.454   44.217  1.00 58.49  ? 172 HIS B CA  1 
ATOM 3841 C C   . HIS B 1 172 ? 32.161 2.499   43.218  1.00 55.86  ? 172 HIS B C   1 
ATOM 3842 O O   . HIS B 1 172 ? 33.370 2.736   43.119  1.00 51.53  ? 172 HIS B O   1 
ATOM 3843 C CB  . HIS B 1 172 ? 30.941 0.331   43.483  1.00 49.55  ? 172 HIS B CB  1 
ATOM 3844 C CG  . HIS B 1 172 ? 31.744 -0.296  42.389  1.00 54.48  ? 172 HIS B CG  1 
ATOM 3845 N ND1 . HIS B 1 172 ? 31.659 0.113   41.075  1.00 54.78  ? 172 HIS B ND1 1 
ATOM 3846 C CD2 . HIS B 1 172 ? 32.655 -1.297  42.412  1.00 58.34  ? 172 HIS B CD2 1 
ATOM 3847 C CE1 . HIS B 1 172 ? 32.478 -0.613  40.336  1.00 55.41  ? 172 HIS B CE1 1 
ATOM 3848 N NE2 . HIS B 1 172 ? 33.095 -1.475  41.123  1.00 58.95  ? 172 HIS B NE2 1 
ATOM 3849 N N   . GLY B 1 173 ? 31.255 3.131   42.465  1.00 57.05  ? 173 GLY B N   1 
ATOM 3850 C CA  . GLY B 1 173 ? 31.675 4.009   41.385  1.00 55.78  ? 173 GLY B CA  1 
ATOM 3851 C C   . GLY B 1 173 ? 32.135 5.382   41.818  1.00 60.57  ? 173 GLY B C   1 
ATOM 3852 O O   . GLY B 1 173 ? 32.794 6.076   41.036  1.00 63.95  ? 173 GLY B O   1 
ATOM 3853 N N   . ARG B 1 174 ? 31.818 5.783   43.045  1.00 62.83  ? 174 ARG B N   1 
ATOM 3854 C CA  . ARG B 1 174 ? 32.195 7.081   43.584  1.00 41.34  ? 174 ARG B CA  1 
ATOM 3855 C C   . ARG B 1 174 ? 32.953 6.883   44.886  1.00 49.70  ? 174 ARG B C   1 
ATOM 3856 O O   . ARG B 1 174 ? 32.558 6.069   45.726  1.00 52.57  ? 174 ARG B O   1 
ATOM 3857 C CB  . ARG B 1 174 ? 30.969 7.959   43.851  1.00 48.26  ? 174 ARG B CB  1 
ATOM 3858 C CG  . ARG B 1 174 ? 30.529 8.832   42.694  1.00 56.21  ? 174 ARG B CG  1 
ATOM 3859 C CD  . ARG B 1 174 ? 29.416 9.765   43.145  1.00 54.31  ? 174 ARG B CD  1 
ATOM 3860 N NE  . ARG B 1 174 ? 28.175 9.045   43.406  1.00 50.71  ? 174 ARG B NE  1 
ATOM 3861 C CZ  . ARG B 1 174 ? 27.310 8.680   42.471  1.00 54.60  ? 174 ARG B CZ  1 
ATOM 3862 N NH1 . ARG B 1 174 ? 27.518 8.951   41.193  1.00 52.01  ? 174 ARG B NH1 1 
ATOM 3863 N NH2 . ARG B 1 174 ? 26.210 8.021   42.827  1.00 60.63  ? 174 ARG B NH2 1 
ATOM 3864 N N   . ASP B 1 175 ? 34.039 7.630   45.050  1.00 57.57  ? 175 ASP B N   1 
ATOM 3865 C CA  . ASP B 1 175 ? 34.716 7.719   46.336  1.00 53.62  ? 175 ASP B CA  1 
ATOM 3866 C C   . ASP B 1 175 ? 35.279 9.123   46.470  1.00 57.41  ? 175 ASP B C   1 
ATOM 3867 O O   . ASP B 1 175 ? 35.888 9.641   45.529  1.00 58.41  ? 175 ASP B O   1 
ATOM 3868 C CB  . ASP B 1 175 ? 35.823 6.667   46.461  1.00 50.72  ? 175 ASP B CB  1 
ATOM 3869 C CG  . ASP B 1 175 ? 36.247 6.430   47.898  1.00 56.67  ? 175 ASP B CG  1 
ATOM 3870 O OD1 . ASP B 1 175 ? 36.319 7.408   48.673  1.00 61.97  ? 175 ASP B OD1 1 
ATOM 3871 O OD2 . ASP B 1 175 ? 36.508 5.263   48.255  1.00 53.36  ? 175 ASP B OD2 1 
ATOM 3872 N N   . TRP B 1 176 ? 35.069 9.734   47.633  1.00 58.85  ? 176 TRP B N   1 
ATOM 3873 C CA  . TRP B 1 176 ? 35.448 11.120  47.868  1.00 54.92  ? 176 TRP B CA  1 
ATOM 3874 C C   . TRP B 1 176 ? 36.672 11.249  48.766  1.00 59.01  ? 176 TRP B C   1 
ATOM 3875 O O   . TRP B 1 176 ? 37.014 12.364  49.174  1.00 56.18  ? 176 TRP B O   1 
ATOM 3876 C CB  . TRP B 1 176 ? 34.267 11.886  48.467  1.00 43.90  ? 176 TRP B CB  1 
ATOM 3877 C CG  . TRP B 1 176 ? 33.078 11.936  47.556  1.00 50.17  ? 176 TRP B CG  1 
ATOM 3878 C CD1 . TRP B 1 176 ? 33.078 11.765  46.203  1.00 52.47  ? 176 TRP B CD1 1 
ATOM 3879 C CD2 . TRP B 1 176 ? 31.713 12.164  47.930  1.00 49.01  ? 176 TRP B CD2 1 
ATOM 3880 N NE1 . TRP B 1 176 ? 31.801 11.877  45.710  1.00 52.57  ? 176 TRP B NE1 1 
ATOM 3881 C CE2 . TRP B 1 176 ? 30.944 12.122  46.750  1.00 48.05  ? 176 TRP B CE2 1 
ATOM 3882 C CE3 . TRP B 1 176 ? 31.067 12.403  49.147  1.00 44.86  ? 176 TRP B CE3 1 
ATOM 3883 C CZ2 . TRP B 1 176 ? 29.563 12.308  46.751  1.00 47.28  ? 176 TRP B CZ2 1 
ATOM 3884 C CZ3 . TRP B 1 176 ? 29.696 12.588  49.145  1.00 43.21  ? 176 TRP B CZ3 1 
ATOM 3885 C CH2 . TRP B 1 176 ? 28.960 12.540  47.956  1.00 49.99  ? 176 TRP B CH2 1 
ATOM 3886 N N   . ARG B 1 177 ? 37.338 10.140  49.086  1.00 58.80  ? 177 ARG B N   1 
ATOM 3887 C CA  . ARG B 1 177 ? 38.531 10.189  49.922  1.00 56.55  ? 177 ARG B CA  1 
ATOM 3888 C C   . ARG B 1 177 ? 39.709 9.484   49.262  1.00 65.26  ? 177 ARG B C   1 
ATOM 3889 O O   . ARG B 1 177 ? 40.790 10.067  49.139  1.00 72.43  ? 177 ARG B O   1 
ATOM 3890 C CB  . ARG B 1 177 ? 38.252 9.569   51.292  1.00 53.37  ? 177 ARG B CB  1 
ATOM 3891 C CG  . ARG B 1 177 ? 39.455 9.566   52.221  1.00 51.57  ? 177 ARG B CG  1 
ATOM 3892 C CD  . ARG B 1 177 ? 39.098 8.956   53.561  1.00 48.18  ? 177 ARG B CD  1 
ATOM 3893 N NE  . ARG B 1 177 ? 40.244 8.861   54.458  1.00 52.47  ? 177 ARG B NE  1 
ATOM 3894 C CZ  . ARG B 1 177 ? 40.433 9.635   55.518  1.00 58.29  ? 177 ARG B CZ  1 
ATOM 3895 N NH1 . ARG B 1 177 ? 39.575 10.590  55.839  1.00 53.42  ? 177 ARG B NH1 1 
ATOM 3896 N NH2 . ARG B 1 177 ? 41.507 9.443   56.279  1.00 56.30  ? 177 ARG B NH2 1 
ATOM 3897 N N   . HIS B 1 178 ? 39.509 8.231   48.857  1.00 68.06  ? 178 HIS B N   1 
ATOM 3898 C CA  . HIS B 1 178 ? 40.576 7.431   48.272  1.00 66.89  ? 178 HIS B CA  1 
ATOM 3899 C C   . HIS B 1 178 ? 41.262 8.197   47.142  1.00 69.74  ? 178 HIS B C   1 
ATOM 3900 O O   . HIS B 1 178 ? 40.587 8.653   46.208  1.00 66.18  ? 178 HIS B O   1 
ATOM 3901 C CB  . HIS B 1 178 ? 40.027 6.103   47.750  1.00 71.56  ? 178 HIS B CB  1 
ATOM 3902 C CG  . HIS B 1 178 ? 41.075 5.051   47.567  1.00 70.12  ? 178 HIS B CG  1 
ATOM 3903 N ND1 . HIS B 1 178 ? 42.042 5.125   46.587  1.00 69.40  ? 178 HIS B ND1 1 
ATOM 3904 C CD2 . HIS B 1 178 ? 41.317 3.905   48.247  1.00 58.40  ? 178 HIS B CD2 1 
ATOM 3905 C CE1 . HIS B 1 178 ? 42.828 4.067   46.666  1.00 73.70  ? 178 HIS B CE1 1 
ATOM 3906 N NE2 . HIS B 1 178 ? 42.410 3.311   47.665  1.00 69.01  ? 178 HIS B NE2 1 
ATOM 3907 N N   . PRO B 1 179 ? 42.588 8.362   47.190  1.00 76.31  ? 179 PRO B N   1 
ATOM 3908 C CA  . PRO B 1 179 ? 43.258 9.239   46.214  1.00 77.25  ? 179 PRO B CA  1 
ATOM 3909 C C   . PRO B 1 179 ? 43.179 8.745   44.780  1.00 79.74  ? 179 PRO B C   1 
ATOM 3910 O O   . PRO B 1 179 ? 43.305 9.561   43.858  1.00 78.57  ? 179 PRO B O   1 
ATOM 3911 C CB  . PRO B 1 179 ? 44.715 9.287   46.701  1.00 74.43  ? 179 PRO B CB  1 
ATOM 3912 C CG  . PRO B 1 179 ? 44.843 8.285   47.791  1.00 82.04  ? 179 PRO B CG  1 
ATOM 3913 C CD  . PRO B 1 179 ? 43.521 7.672   48.097  1.00 74.96  ? 179 PRO B CD  1 
ATOM 3914 N N   . HIS B 1 180 ? 42.974 7.450   44.556  1.00 80.08  ? 180 HIS B N   1 
ATOM 3915 C CA  . HIS B 1 180 ? 43.019 6.882   43.216  1.00 79.48  ? 180 HIS B CA  1 
ATOM 3916 C C   . HIS B 1 180 ? 41.637 6.676   42.607  1.00 76.00  ? 180 HIS B C   1 
ATOM 3917 O O   . HIS B 1 180 ? 41.538 6.221   41.464  1.00 78.18  ? 180 HIS B O   1 
ATOM 3918 C CB  . HIS B 1 180 ? 43.805 5.568   43.236  1.00 79.23  ? 180 HIS B CB  1 
ATOM 3919 C CG  . HIS B 1 180 ? 45.254 5.748   43.571  1.00 87.33  ? 180 HIS B CG  1 
ATOM 3920 N ND1 . HIS B 1 180 ? 46.158 6.305   42.692  1.00 89.86  ? 180 HIS B ND1 1 
ATOM 3921 C CD2 . HIS B 1 180 ? 45.951 5.466   44.697  1.00 85.55  ? 180 HIS B CD2 1 
ATOM 3922 C CE1 . HIS B 1 180 ? 47.351 6.348   43.257  1.00 85.77  ? 180 HIS B CE1 1 
ATOM 3923 N NE2 . HIS B 1 180 ? 47.253 5.844   44.474  1.00 85.23  ? 180 HIS B NE2 1 
ATOM 3924 N N   . ALA B 1 181 ? 40.576 7.004   43.341  1.00 68.71  ? 181 ALA B N   1 
ATOM 3925 C CA  . ALA B 1 181 ? 39.218 6.854   42.850  1.00 63.10  ? 181 ALA B CA  1 
ATOM 3926 C C   . ALA B 1 181 ? 38.916 7.882   41.756  1.00 68.66  ? 181 ALA B C   1 
ATOM 3927 O O   . ALA B 1 181 ? 39.612 8.893   41.636  1.00 71.95  ? 181 ALA B O   1 
ATOM 3928 C CB  . ALA B 1 181 ? 38.237 7.002   44.009  1.00 64.95  ? 181 ALA B CB  1 
ATOM 3929 N N   . PRO B 1 182 ? 37.890 7.630   40.937  1.00 69.89  ? 182 PRO B N   1 
ATOM 3930 C CA  . PRO B 1 182 ? 37.587 8.513   39.797  1.00 67.74  ? 182 PRO B CA  1 
ATOM 3931 C C   . PRO B 1 182 ? 37.546 9.999   40.139  1.00 72.65  ? 182 PRO B C   1 
ATOM 3932 O O   . PRO B 1 182 ? 36.923 10.417  41.118  1.00 69.17  ? 182 PRO B O   1 
ATOM 3933 C CB  . PRO B 1 182 ? 36.215 8.012   39.340  1.00 67.30  ? 182 PRO B CB  1 
ATOM 3934 C CG  . PRO B 1 182 ? 36.260 6.561   39.633  1.00 67.93  ? 182 PRO B CG  1 
ATOM 3935 C CD  . PRO B 1 182 ? 37.049 6.417   40.912  1.00 63.39  ? 182 PRO B CD  1 
ATOM 3936 N N   . ASN B 1 183 ? 38.222 10.798  39.312  1.00 72.18  ? 183 ASN B N   1 
ATOM 3937 C CA  . ASN B 1 183 ? 38.275 12.249  39.436  1.00 61.86  ? 183 ASN B CA  1 
ATOM 3938 C C   . ASN B 1 183 ? 37.315 12.914  38.447  1.00 72.15  ? 183 ASN B C   1 
ATOM 3939 O O   . ASN B 1 183 ? 36.820 12.291  37.505  1.00 75.01  ? 183 ASN B O   1 
ATOM 3940 C CB  . ASN B 1 183 ? 39.706 12.751  39.223  1.00 62.52  ? 183 ASN B CB  1 
ATOM 3941 C CG  . ASN B 1 183 ? 40.568 12.590  40.460  1.00 65.00  ? 183 ASN B CG  1 
ATOM 3942 O OD1 . ASN B 1 183 ? 40.443 11.609  41.193  1.00 63.35  ? 183 ASN B OD1 1 
ATOM 3943 N ND2 . ASN B 1 183 ? 41.451 13.553  40.698  1.00 68.06  ? 183 ASN B ND2 1 
ATOM 3944 N N   . ASN B 1 184 ? 37.066 14.210  38.670  1.00 69.76  ? 184 ASN B N   1 
ATOM 3945 C CA  . ASN B 1 184 ? 36.004 14.927  37.964  1.00 74.31  ? 184 ASN B CA  1 
ATOM 3946 C C   . ASN B 1 184 ? 36.322 15.234  36.508  1.00 71.01  ? 184 ASN B C   1 
ATOM 3947 O O   . ASN B 1 184 ? 35.414 15.629  35.769  1.00 71.15  ? 184 ASN B O   1 
ATOM 3948 C CB  . ASN B 1 184 ? 35.680 16.240  38.671  1.00 68.29  ? 184 ASN B CB  1 
ATOM 3949 C CG  . ASN B 1 184 ? 35.149 16.029  40.058  1.00 70.89  ? 184 ASN B CG  1 
ATOM 3950 O OD1 . ASN B 1 184 ? 35.900 15.696  40.968  1.00 68.96  ? 184 ASN B OD1 1 
ATOM 3951 N ND2 . ASN B 1 184 ? 33.845 16.207  40.231  1.00 71.70  ? 184 ASN B ND2 1 
ATOM 3952 N N   . GLY B 1 185 ? 37.563 15.086  36.076  1.00 64.92  ? 185 GLY B N   1 
ATOM 3953 C CA  . GLY B 1 185 ? 37.843 15.267  34.670  1.00 80.87  ? 185 GLY B CA  1 
ATOM 3954 C C   . GLY B 1 185 ? 37.446 14.030  33.898  1.00 76.59  ? 185 GLY B C   1 
ATOM 3955 O O   . GLY B 1 185 ? 36.584 14.067  33.014  1.00 73.53  ? 185 GLY B O   1 
ATOM 3956 N N   . ASP B 1 186 ? 38.089 12.919  34.250  1.00 73.59  ? 186 ASP B N   1 
ATOM 3957 C CA  . ASP B 1 186 ? 37.922 11.672  33.514  1.00 82.73  ? 186 ASP B CA  1 
ATOM 3958 C C   . ASP B 1 186 ? 36.484 11.156  33.550  1.00 82.90  ? 186 ASP B C   1 
ATOM 3959 O O   . ASP B 1 186 ? 35.969 10.684  32.531  1.00 76.72  ? 186 ASP B O   1 
ATOM 3960 C CB  . ASP B 1 186 ? 38.892 10.633  34.073  1.00 90.16  ? 186 ASP B CB  1 
ATOM 3961 C CG  . ASP B 1 186 ? 40.315 11.157  34.149  1.00 96.67  ? 186 ASP B CG  1 
ATOM 3962 O OD1 . ASP B 1 186 ? 40.595 11.994  35.035  1.00 72.50  ? 186 ASP B OD1 1 
ATOM 3963 O OD2 . ASP B 1 186 ? 41.151 10.737  33.321  1.00 105.79 ? 186 ASP B OD2 1 
ATOM 3964 N N   . TRP B 1 187 ? 35.818 11.231  34.706  1.00 85.64  ? 187 TRP B N   1 
ATOM 3965 C CA  . TRP B 1 187 ? 34.513 10.586  34.847  1.00 79.41  ? 187 TRP B CA  1 
ATOM 3966 C C   . TRP B 1 187 ? 33.359 11.528  35.171  1.00 72.93  ? 187 TRP B C   1 
ATOM 3967 O O   . TRP B 1 187 ? 32.614 11.286  36.127  1.00 73.08  ? 187 TRP B O   1 
ATOM 3968 C CB  . TRP B 1 187 ? 34.576 9.516   35.936  1.00 74.89  ? 187 TRP B CB  1 
ATOM 3969 C CG  . TRP B 1 187 ? 35.685 8.547   35.765  1.00 69.96  ? 187 TRP B CG  1 
ATOM 3970 C CD1 . TRP B 1 187 ? 36.979 8.704   36.161  1.00 73.93  ? 187 TRP B CD1 1 
ATOM 3971 C CD2 . TRP B 1 187 ? 35.604 7.256   35.155  1.00 71.72  ? 187 TRP B CD2 1 
ATOM 3972 N NE1 . TRP B 1 187 ? 37.712 7.590   35.835  1.00 80.73  ? 187 TRP B NE1 1 
ATOM 3973 C CE2 . TRP B 1 187 ? 36.890 6.686   35.216  1.00 76.05  ? 187 TRP B CE2 1 
ATOM 3974 C CE3 . TRP B 1 187 ? 34.569 6.527   34.563  1.00 75.21  ? 187 TRP B CE3 1 
ATOM 3975 C CZ2 . TRP B 1 187 ? 37.169 5.421   34.708  1.00 72.22  ? 187 TRP B CZ2 1 
ATOM 3976 C CZ3 . TRP B 1 187 ? 34.848 5.272   34.057  1.00 73.05  ? 187 TRP B CZ3 1 
ATOM 3977 C CH2 . TRP B 1 187 ? 36.138 4.731   34.136  1.00 73.61  ? 187 TRP B CH2 1 
ATOM 3978 N N   . GLY B 1 188 ? 33.176 12.578  34.383  1.00 84.81  ? 188 GLY B N   1 
ATOM 3979 C CA  . GLY B 1 188 ? 32.096 13.513  34.636  1.00 97.51  ? 188 GLY B CA  1 
ATOM 3980 C C   . GLY B 1 188 ? 32.296 14.273  35.938  1.00 99.95  ? 188 GLY B C   1 
ATOM 3981 O O   . GLY B 1 188 ? 33.260 14.079  36.675  1.00 88.55  ? 188 GLY B O   1 
ATOM 3982 N N   . GLY B 1 189 ? 31.334 15.147  36.228  1.00 101.99 ? 189 GLY B N   1 
ATOM 3983 C CA  . GLY B 1 189 ? 31.491 16.092  37.314  1.00 94.43  ? 189 GLY B CA  1 
ATOM 3984 C C   . GLY B 1 189 ? 31.091 15.635  38.700  1.00 97.03  ? 189 GLY B C   1 
ATOM 3985 O O   . GLY B 1 189 ? 31.357 16.355  39.667  1.00 95.67  ? 189 GLY B O   1 
ATOM 3986 N N   . ASN B 1 190 ? 30.469 14.465  38.843  1.00 84.26  ? 190 ASN B N   1 
ATOM 3987 C CA  . ASN B 1 190 ? 29.926 14.046  40.130  1.00 66.33  ? 190 ASN B CA  1 
ATOM 3988 C C   . ASN B 1 190 ? 30.795 13.030  40.858  1.00 61.03  ? 190 ASN B C   1 
ATOM 3989 O O   . ASN B 1 190 ? 30.417 12.586  41.947  1.00 56.40  ? 190 ASN B O   1 
ATOM 3990 C CB  . ASN B 1 190 ? 28.512 13.490  39.950  1.00 55.00  ? 190 ASN B CB  1 
ATOM 3991 C CG  . ASN B 1 190 ? 27.447 14.481  40.376  1.00 65.50  ? 190 ASN B CG  1 
ATOM 3992 O OD1 . ASN B 1 190 ? 27.599 15.176  41.381  1.00 61.50  ? 190 ASN B OD1 1 
ATOM 3993 N ND2 . ASN B 1 190 ? 26.367 14.561  39.607  1.00 66.10  ? 190 ASN B ND2 1 
ATOM 3994 N N   . ALA B 1 191 ? 31.943 12.653  40.292  1.00 61.98  ? 191 ALA B N   1 
ATOM 3995 C CA  . ALA B 1 191 ? 32.792 11.652  40.931  1.00 48.55  ? 191 ALA B CA  1 
ATOM 3996 C C   . ALA B 1 191 ? 33.290 12.136  42.288  1.00 56.13  ? 191 ALA B C   1 
ATOM 3997 O O   . ALA B 1 191 ? 33.290 11.378  43.264  1.00 60.24  ? 191 ALA B O   1 
ATOM 3998 C CB  . ALA B 1 191 ? 33.966 11.297  40.021  1.00 55.68  ? 191 ALA B CB  1 
ATOM 3999 N N   . ARG B 1 192 ? 33.723 13.388  42.368  1.00 60.41  ? 192 ARG B N   1 
ATOM 4000 C CA  . ARG B 1 192 ? 34.247 13.994  43.579  1.00 55.22  ? 192 ARG B CA  1 
ATOM 4001 C C   . ARG B 1 192 ? 33.614 15.365  43.774  1.00 48.92  ? 192 ARG B C   1 
ATOM 4002 O O   . ARG B 1 192 ? 33.050 15.932  42.835  1.00 50.00  ? 192 ARG B O   1 
ATOM 4003 C CB  . ARG B 1 192 ? 35.774 14.149  43.517  1.00 53.44  ? 192 ARG B CB  1 
ATOM 4004 C CG  . ARG B 1 192 ? 36.522 12.947  42.997  1.00 58.82  ? 192 ARG B CG  1 
ATOM 4005 C CD  . ARG B 1 192 ? 37.125 12.182  44.148  1.00 61.58  ? 192 ARG B CD  1 
ATOM 4006 N NE  . ARG B 1 192 ? 38.433 11.629  43.825  1.00 62.09  ? 192 ARG B NE  1 
ATOM 4007 C CZ  . ARG B 1 192 ? 39.088 10.771  44.595  1.00 65.32  ? 192 ARG B CZ  1 
ATOM 4008 N NH1 . ARG B 1 192 ? 38.552 10.293  45.706  1.00 59.76  ? 192 ARG B NH1 1 
ATOM 4009 N NH2 . ARG B 1 192 ? 40.301 10.367  44.231  1.00 66.74  ? 192 ARG B NH2 1 
ATOM 4010 N N   . PRO B 1 193 ? 33.678 15.910  44.989  1.00 50.29  ? 193 PRO B N   1 
ATOM 4011 C CA  . PRO B 1 193 ? 33.181 17.277  45.196  1.00 57.24  ? 193 PRO B CA  1 
ATOM 4012 C C   . PRO B 1 193 ? 33.996 18.277  44.394  1.00 54.22  ? 193 PRO B C   1 
ATOM 4013 O O   . PRO B 1 193 ? 35.219 18.169  44.286  1.00 55.49  ? 193 PRO B O   1 
ATOM 4014 C CB  . PRO B 1 193 ? 33.345 17.496  46.706  1.00 57.65  ? 193 PRO B CB  1 
ATOM 4015 C CG  . PRO B 1 193 ? 34.254 16.409  47.180  1.00 52.87  ? 193 PRO B CG  1 
ATOM 4016 C CD  . PRO B 1 193 ? 34.058 15.260  46.254  1.00 52.81  ? 193 PRO B CD  1 
ATOM 4017 N N   . LYS B 1 194 ? 33.302 19.263  43.827  1.00 43.56  ? 194 LYS B N   1 
ATOM 4018 C CA  . LYS B 1 194 ? 33.937 20.238  42.944  1.00 57.82  ? 194 LYS B CA  1 
ATOM 4019 C C   . LYS B 1 194 ? 34.598 21.302  43.814  1.00 61.91  ? 194 LYS B C   1 
ATOM 4020 O O   . LYS B 1 194 ? 34.071 22.394  44.040  1.00 66.12  ? 194 LYS B O   1 
ATOM 4021 C CB  . LYS B 1 194 ? 32.921 20.840  41.982  1.00 59.85  ? 194 LYS B CB  1 
ATOM 4022 C CG  . LYS B 1 194 ? 33.435 21.003  40.561  1.00 66.52  ? 194 LYS B CG  1 
ATOM 4023 C CD  . LYS B 1 194 ? 32.900 19.908  39.651  1.00 68.80  ? 194 LYS B CD  1 
ATOM 4024 C CE  . LYS B 1 194 ? 31.401 20.057  39.438  1.00 81.00  ? 194 LYS B CE  1 
ATOM 4025 N NZ  . LYS B 1 194 ? 30.811 18.876  38.752  1.00 68.64  ? 194 LYS B NZ  1 
ATOM 4026 N N   . TYR B 1 195 ? 35.787 20.964  44.308  1.00 56.59  ? 195 TYR B N   1 
ATOM 4027 C CA  . TYR B 1 195 ? 36.527 21.868  45.171  1.00 60.16  ? 195 TYR B CA  1 
ATOM 4028 C C   . TYR B 1 195 ? 37.002 23.083  44.379  1.00 71.79  ? 195 TYR B C   1 
ATOM 4029 O O   . TYR B 1 195 ? 37.095 23.061  43.148  1.00 75.67  ? 195 TYR B O   1 
ATOM 4030 C CB  . TYR B 1 195 ? 37.727 21.153  45.796  1.00 62.43  ? 195 TYR B CB  1 
ATOM 4031 C CG  . TYR B 1 195 ? 37.381 20.108  46.839  1.00 65.85  ? 195 TYR B CG  1 
ATOM 4032 C CD1 . TYR B 1 195 ? 36.598 20.424  47.943  1.00 62.63  ? 195 TYR B CD1 1 
ATOM 4033 C CD2 . TYR B 1 195 ? 37.852 18.806  46.723  1.00 65.30  ? 195 TYR B CD2 1 
ATOM 4034 C CE1 . TYR B 1 195 ? 36.290 19.468  48.900  1.00 60.50  ? 195 TYR B CE1 1 
ATOM 4035 C CE2 . TYR B 1 195 ? 37.549 17.845  47.672  1.00 60.68  ? 195 TYR B CE2 1 
ATOM 4036 C CZ  . TYR B 1 195 ? 36.769 18.180  48.758  1.00 63.71  ? 195 TYR B CZ  1 
ATOM 4037 O OH  . TYR B 1 195 ? 36.468 17.223  49.701  1.00 62.05  ? 195 TYR B OH  1 
ATOM 4038 N N   . ASP B 1 196 ? 37.310 24.157  45.105  1.00 70.91  ? 196 ASP B N   1 
ATOM 4039 C CA  . ASP B 1 196 ? 37.766 25.384  44.465  1.00 69.20  ? 196 ASP B CA  1 
ATOM 4040 C C   . ASP B 1 196 ? 39.267 25.385  44.215  1.00 73.08  ? 196 ASP B C   1 
ATOM 4041 O O   . ASP B 1 196 ? 39.727 26.005  43.248  1.00 76.03  ? 196 ASP B O   1 
ATOM 4042 C CB  . ASP B 1 196 ? 37.375 26.594  45.317  1.00 70.28  ? 196 ASP B CB  1 
ATOM 4043 C CG  . ASP B 1 196 ? 35.900 26.599  45.677  1.00 84.64  ? 196 ASP B CG  1 
ATOM 4044 O OD1 . ASP B 1 196 ? 35.358 25.516  45.984  1.00 75.45  ? 196 ASP B OD1 1 
ATOM 4045 O OD2 . ASP B 1 196 ? 35.282 27.684  45.649  1.00 92.86  ? 196 ASP B OD2 1 
ATOM 4046 N N   . SER B 1 197 ? 40.037 24.704  45.061  1.00 77.13  ? 197 SER B N   1 
ATOM 4047 C CA  . SER B 1 197 ? 41.445 24.425  44.833  1.00 77.62  ? 197 SER B CA  1 
ATOM 4048 C C   . SER B 1 197 ? 41.671 22.926  44.930  1.00 73.26  ? 197 SER B C   1 
ATOM 4049 O O   . SER B 1 197 ? 41.045 22.258  45.765  1.00 74.96  ? 197 SER B O   1 
ATOM 4050 C CB  . SER B 1 197 ? 42.336 25.168  45.838  1.00 77.74  ? 197 SER B CB  1 
ATOM 4051 O OG  . SER B 1 197 ? 42.405 26.550  45.524  1.00 80.79  ? 197 SER B OG  1 
ATOM 4052 N N   . PRO B 1 198 ? 42.531 22.364  44.078  1.00 63.75  ? 198 PRO B N   1 
ATOM 4053 C CA  . PRO B 1 198 ? 42.739 20.908  44.053  1.00 71.18  ? 198 PRO B CA  1 
ATOM 4054 C C   . PRO B 1 198 ? 42.934 20.308  45.440  1.00 79.62  ? 198 PRO B C   1 
ATOM 4055 O O   . PRO B 1 198 ? 43.717 20.809  46.250  1.00 82.71  ? 198 PRO B O   1 
ATOM 4056 C CB  . PRO B 1 198 ? 43.993 20.734  43.188  1.00 70.49  ? 198 PRO B CB  1 
ATOM 4057 C CG  . PRO B 1 198 ? 44.192 22.013  42.471  1.00 81.46  ? 198 PRO B CG  1 
ATOM 4058 C CD  . PRO B 1 198 ? 43.355 23.082  43.090  1.00 70.08  ? 198 PRO B CD  1 
ATOM 4059 N N   . GLU B 1 199 ? 42.204 19.232  45.708  1.00 71.27  ? 199 GLU B N   1 
ATOM 4060 C CA  . GLU B 1 199 ? 42.250 18.592  47.017  1.00 77.81  ? 199 GLU B CA  1 
ATOM 4061 C C   . GLU B 1 199 ? 43.600 17.922  47.233  1.00 82.14  ? 199 GLU B C   1 
ATOM 4062 O O   . GLU B 1 199 ? 43.980 17.044  46.446  1.00 76.00  ? 199 GLU B O   1 
ATOM 4063 C CB  . GLU B 1 199 ? 41.129 17.568  47.145  1.00 75.09  ? 199 GLU B CB  1 
ATOM 4064 C CG  . GLU B 1 199 ? 41.276 16.646  48.341  1.00 72.44  ? 199 GLU B CG  1 
ATOM 4065 C CD  . GLU B 1 199 ? 41.344 17.398  49.658  1.00 74.67  ? 199 GLU B CD  1 
ATOM 4066 O OE1 . GLU B 1 199 ? 40.687 18.453  49.780  1.00 75.68  ? 199 GLU B OE1 1 
ATOM 4067 O OE2 . GLU B 1 199 ? 42.054 16.932  50.574  1.00 78.80  ? 199 GLU B OE2 1 
ATOM 4068 N N   . PRO B 1 200 ? 44.351 18.296  48.273  1.00 83.92  ? 200 PRO B N   1 
ATOM 4069 C CA  . PRO B 1 200 ? 45.684 17.700  48.470  1.00 82.45  ? 200 PRO B CA  1 
ATOM 4070 C C   . PRO B 1 200 ? 45.661 16.204  48.729  1.00 74.25  ? 200 PRO B C   1 
ATOM 4071 O O   . PRO B 1 200 ? 46.654 15.525  48.441  1.00 80.52  ? 200 PRO B O   1 
ATOM 4072 C CB  . PRO B 1 200 ? 46.235 18.470  49.680  1.00 83.22  ? 200 PRO B CB  1 
ATOM 4073 C CG  . PRO B 1 200 ? 45.034 19.083  50.339  1.00 72.84  ? 200 PRO B CG  1 
ATOM 4074 C CD  . PRO B 1 200 ? 44.076 19.377  49.233  1.00 75.16  ? 200 PRO B CD  1 
ATOM 4075 N N   . PHE B 1 201 ? 44.560 15.665  49.260  1.00 71.26  ? 201 PHE B N   1 
ATOM 4076 C CA  . PHE B 1 201 ? 44.519 14.238  49.564  1.00 74.69  ? 201 PHE B CA  1 
ATOM 4077 C C   . PHE B 1 201 ? 44.471 13.403  48.291  1.00 73.58  ? 201 PHE B C   1 
ATOM 4078 O O   . PHE B 1 201 ? 44.936 12.257  48.282  1.00 71.09  ? 201 PHE B O   1 
ATOM 4079 C CB  . PHE B 1 201 ? 43.316 13.929  50.459  1.00 76.12  ? 201 PHE B CB  1 
ATOM 4080 C CG  . PHE B 1 201 ? 43.415 12.617  51.194  1.00 77.76  ? 201 PHE B CG  1 
ATOM 4081 C CD1 . PHE B 1 201 ? 43.118 11.422  50.559  1.00 73.77  ? 201 PHE B CD1 1 
ATOM 4082 C CD2 . PHE B 1 201 ? 43.793 12.582  52.527  1.00 70.89  ? 201 PHE B CD2 1 
ATOM 4083 C CE1 . PHE B 1 201 ? 43.204 10.219  51.233  1.00 67.96  ? 201 PHE B CE1 1 
ATOM 4084 C CE2 . PHE B 1 201 ? 43.881 11.381  53.207  1.00 63.44  ? 201 PHE B CE2 1 
ATOM 4085 C CZ  . PHE B 1 201 ? 43.585 10.198  52.559  1.00 68.25  ? 201 PHE B CZ  1 
ATOM 4086 N N   . TYR B 1 202 ? 43.941 13.964  47.209  1.00 79.02  ? 202 TYR B N   1 
ATOM 4087 C CA  . TYR B 1 202 ? 43.846 13.247  45.948  1.00 79.23  ? 202 TYR B CA  1 
ATOM 4088 C C   . TYR B 1 202 ? 45.165 13.292  45.189  1.00 81.34  ? 202 TYR B C   1 
ATOM 4089 O O   . TYR B 1 202 ? 45.843 14.323  45.149  1.00 84.75  ? 202 TYR B O   1 
ATOM 4090 C CB  . TYR B 1 202 ? 42.754 13.847  45.059  1.00 74.21  ? 202 TYR B CB  1 
ATOM 4091 C CG  . TYR B 1 202 ? 41.355 13.857  45.633  1.00 69.75  ? 202 TYR B CG  1 
ATOM 4092 C CD1 . TYR B 1 202 ? 40.996 13.020  46.682  1.00 66.50  ? 202 TYR B CD1 1 
ATOM 4093 C CD2 . TYR B 1 202 ? 40.388 14.704  45.111  1.00 62.58  ? 202 TYR B CD2 1 
ATOM 4094 C CE1 . TYR B 1 202 ? 39.712 13.035  47.197  1.00 59.85  ? 202 TYR B CE1 1 
ATOM 4095 C CE2 . TYR B 1 202 ? 39.107 14.727  45.616  1.00 62.39  ? 202 TYR B CE2 1 
ATOM 4096 C CZ  . TYR B 1 202 ? 38.772 13.891  46.659  1.00 62.96  ? 202 TYR B CZ  1 
ATOM 4097 O OH  . TYR B 1 202 ? 37.490 13.917  47.160  1.00 62.13  ? 202 TYR B OH  1 
ATOM 4098 N N   . LYS B 1 203 ? 45.527 12.162  44.592  1.00 72.06  ? 203 LYS B N   1 
ATOM 4099 C CA  . LYS B 1 203 ? 46.480 12.187  43.498  1.00 79.19  ? 203 LYS B CA  1 
ATOM 4100 C C   . LYS B 1 203 ? 45.730 12.524  42.212  1.00 78.83  ? 203 LYS B C   1 
ATOM 4101 O O   . LYS B 1 203 ? 44.509 12.368  42.123  1.00 74.79  ? 203 LYS B O   1 
ATOM 4102 C CB  . LYS B 1 203 ? 47.202 10.844  43.373  1.00 84.11  ? 203 LYS B CB  1 
ATOM 4103 C CG  . LYS B 1 203 ? 48.595 10.819  43.992  1.00 82.34  ? 203 LYS B CG  1 
ATOM 4104 C CD  . LYS B 1 203 ? 48.604 10.066  45.316  1.00 70.99  ? 203 LYS B CD  1 
ATOM 4105 C CE  . LYS B 1 203 ? 49.759 10.511  46.200  1.00 62.62  ? 203 LYS B CE  1 
ATOM 4106 N NZ  . LYS B 1 203 ? 49.715 9.868   47.543  1.00 72.54  ? 203 LYS B NZ  1 
ATOM 4107 N N   . TYR B 1 204 ? 46.461 13.005  41.210  1.00 80.11  ? 204 TYR B N   1 
ATOM 4108 C CA  . TYR B 1 204 ? 45.824 13.448  39.980  1.00 81.70  ? 204 TYR B CA  1 
ATOM 4109 C C   . TYR B 1 204 ? 46.566 12.924  38.758  1.00 85.02  ? 204 TYR B C   1 
ATOM 4110 O O   . TYR B 1 204 ? 47.727 12.514  38.831  1.00 86.53  ? 204 TYR B O   1 
ATOM 4111 C CB  . TYR B 1 204 ? 45.747 14.984  39.900  1.00 76.99  ? 204 TYR B CB  1 
ATOM 4112 C CG  . TYR B 1 204 ? 44.867 15.638  40.946  1.00 75.24  ? 204 TYR B CG  1 
ATOM 4113 C CD1 . TYR B 1 204 ? 45.297 15.775  42.261  1.00 74.41  ? 204 TYR B CD1 1 
ATOM 4114 C CD2 . TYR B 1 204 ? 43.608 16.123  40.616  1.00 68.00  ? 204 TYR B CD2 1 
ATOM 4115 C CE1 . TYR B 1 204 ? 44.497 16.375  43.216  1.00 69.06  ? 204 TYR B CE1 1 
ATOM 4116 C CE2 . TYR B 1 204 ? 42.800 16.723  41.566  1.00 61.59  ? 204 TYR B CE2 1 
ATOM 4117 C CZ  . TYR B 1 204 ? 43.250 16.846  42.864  1.00 65.11  ? 204 TYR B CZ  1 
ATOM 4118 O OH  . TYR B 1 204 ? 42.453 17.442  43.815  1.00 71.22  ? 204 TYR B OH  1 
ATOM 4119 N N   . GLY B 1 205 ? 45.866 12.975  37.627  1.00 80.58  ? 205 GLY B N   1 
ATOM 4120 C CA  . GLY B 1 205 ? 46.431 12.619  36.334  1.00 74.52  ? 205 GLY B CA  1 
ATOM 4121 C C   . GLY B 1 205 ? 47.208 11.317  36.308  1.00 90.19  ? 205 GLY B C   1 
ATOM 4122 O O   . GLY B 1 205 ? 46.746 10.271  36.783  1.00 89.82  ? 205 GLY B O   1 
ATOM 4123 N N   . GLU B 1 206 ? 48.406 11.389  35.724  1.00 96.81  ? 206 GLU B N   1 
ATOM 4124 C CA  . GLU B 1 206 ? 49.354 10.279  35.698  1.00 92.61  ? 206 GLU B CA  1 
ATOM 4125 C C   . GLU B 1 206 ? 49.751 9.773   37.080  1.00 88.03  ? 206 GLU B C   1 
ATOM 4126 O O   . GLU B 1 206 ? 50.185 8.622   37.200  1.00 87.76  ? 206 GLU B O   1 
ATOM 4127 C CB  . GLU B 1 206 ? 50.622 10.703  34.948  1.00 98.24  ? 206 GLU B CB  1 
ATOM 4128 C CG  . GLU B 1 206 ? 51.377 11.890  35.570  1.00 100.63 ? 206 GLU B CG  1 
ATOM 4129 C CD  . GLU B 1 206 ? 50.608 13.203  35.514  1.00 101.80 ? 206 GLU B CD  1 
ATOM 4130 O OE1 . GLU B 1 206 ? 49.782 13.372  34.592  1.00 101.72 ? 206 GLU B OE1 1 
ATOM 4131 O OE2 . GLU B 1 206 ? 50.822 14.059  36.400  1.00 100.82 ? 206 GLU B OE2 1 
ATOM 4132 N N   . ASP B 1 207 ? 49.598 10.583  38.128  1.00 86.66  ? 207 ASP B N   1 
ATOM 4133 C CA  . ASP B 1 207 ? 49.886 10.101  39.475  1.00 91.84  ? 207 ASP B CA  1 
ATOM 4134 C C   . ASP B 1 207 ? 48.793 9.188   40.006  1.00 92.85  ? 207 ASP B C   1 
ATOM 4135 O O   . ASP B 1 207 ? 49.004 8.516   41.022  1.00 86.12  ? 207 ASP B O   1 
ATOM 4136 C CB  . ASP B 1 207 ? 50.093 11.281  40.425  1.00 91.34  ? 207 ASP B CB  1 
ATOM 4137 C CG  . ASP B 1 207 ? 51.092 12.290  39.891  1.00 95.36  ? 207 ASP B CG  1 
ATOM 4138 O OD1 . ASP B 1 207 ? 52.281 11.935  39.747  1.00 102.42 ? 207 ASP B OD1 1 
ATOM 4139 O OD2 . ASP B 1 207 ? 50.686 13.437  39.608  1.00 93.07  ? 207 ASP B OD2 1 
ATOM 4140 N N   . GLN B 1 208 ? 47.641 9.152   39.346  1.00 93.55  ? 208 GLN B N   1 
ATOM 4141 C CA  . GLN B 1 208 ? 46.493 8.372   39.779  1.00 90.17  ? 208 GLN B CA  1 
ATOM 4142 C C   . GLN B 1 208 ? 46.433 7.090   38.957  1.00 86.52  ? 208 GLN B C   1 
ATOM 4143 O O   . GLN B 1 208 ? 46.390 7.143   37.723  1.00 80.42  ? 208 GLN B O   1 
ATOM 4144 C CB  . GLN B 1 208 ? 45.207 9.182   39.619  1.00 84.60  ? 208 GLN B CB  1 
ATOM 4145 C CG  . GLN B 1 208 ? 44.187 8.932   40.699  1.00 79.94  ? 208 GLN B CG  1 
ATOM 4146 C CD  . GLN B 1 208 ? 42.922 9.739   40.506  1.00 76.78  ? 208 GLN B CD  1 
ATOM 4147 O OE1 . GLN B 1 208 ? 42.329 9.738   39.427  1.00 71.60  ? 208 GLN B OE1 1 
ATOM 4148 N NE2 . GLN B 1 208 ? 42.497 10.430  41.557  1.00 70.87  ? 208 GLN B NE2 1 
ATOM 4149 N N   . ASP B 1 209 ? 46.432 5.947   39.637  1.00 85.76  ? 209 ASP B N   1 
ATOM 4150 C CA  . ASP B 1 209 ? 46.273 4.641   39.000  1.00 82.48  ? 209 ASP B CA  1 
ATOM 4151 C C   . ASP B 1 209 ? 45.013 3.999   39.572  1.00 82.33  ? 209 ASP B C   1 
ATOM 4152 O O   . ASP B 1 209 ? 45.019 3.504   40.704  1.00 82.65  ? 209 ASP B O   1 
ATOM 4153 C CB  . ASP B 1 209 ? 47.505 3.767   39.221  1.00 89.48  ? 209 ASP B CB  1 
ATOM 4154 C CG  . ASP B 1 209 ? 47.334 2.362   38.669  1.00 85.94  ? 209 ASP B CG  1 
ATOM 4155 O OD1 . ASP B 1 209 ? 46.903 2.226   37.504  1.00 79.66  ? 209 ASP B OD1 1 
ATOM 4156 O OD2 . ASP B 1 209 ? 47.638 1.395   39.400  1.00 80.08  ? 209 ASP B OD2 1 
ATOM 4157 N N   . LEU B 1 210 ? 43.934 4.026   38.781  1.00 77.79  ? 210 LEU B N   1 
ATOM 4158 C CA  . LEU B 1 210 ? 42.638 3.512   39.219  1.00 73.95  ? 210 LEU B CA  1 
ATOM 4159 C C   . LEU B 1 210 ? 42.724 2.103   39.791  1.00 74.73  ? 210 LEU B C   1 
ATOM 4160 O O   . LEU B 1 210 ? 41.938 1.745   40.676  1.00 74.65  ? 210 LEU B O   1 
ATOM 4161 C CB  . LEU B 1 210 ? 41.646 3.538   38.054  1.00 67.40  ? 210 LEU B CB  1 
ATOM 4162 C CG  . LEU B 1 210 ? 40.218 3.099   38.389  1.00 65.22  ? 210 LEU B CG  1 
ATOM 4163 C CD1 . LEU B 1 210 ? 39.627 3.992   39.470  1.00 66.66  ? 210 LEU B CD1 1 
ATOM 4164 C CD2 . LEU B 1 210 ? 39.342 3.094   37.147  1.00 67.19  ? 210 LEU B CD2 1 
ATOM 4165 N N   . GLN B 1 211 ? 43.667 1.291   39.304  1.00 73.75  ? 211 GLN B N   1 
ATOM 4166 C CA  . GLN B 1 211 ? 43.761 -0.093  39.760  1.00 84.58  ? 211 GLN B CA  1 
ATOM 4167 C C   . GLN B 1 211 ? 43.977 -0.182  41.265  1.00 80.02  ? 211 GLN B C   1 
ATOM 4168 O O   . GLN B 1 211 ? 43.616 -1.191  41.882  1.00 76.28  ? 211 GLN B O   1 
ATOM 4169 C CB  . GLN B 1 211 ? 44.885 -0.819  39.019  1.00 84.51  ? 211 GLN B CB  1 
ATOM 4170 C CG  . GLN B 1 211 ? 44.466 -1.412  37.681  1.00 83.11  ? 211 GLN B CG  1 
ATOM 4171 C CD  . GLN B 1 211 ? 43.172 -2.203  37.766  1.00 81.93  ? 211 GLN B CD  1 
ATOM 4172 O OE1 . GLN B 1 211 ? 42.969 -2.988  38.694  1.00 79.12  ? 211 GLN B OE1 1 
ATOM 4173 N NE2 . GLN B 1 211 ? 42.290 -2.000  36.794  1.00 89.56  ? 211 GLN B NE2 1 
ATOM 4174 N N   . ILE B 1 212 ? 44.564 0.853   41.872  1.00 74.95  ? 212 ILE B N   1 
ATOM 4175 C CA  . ILE B 1 212 ? 44.701 0.880   43.325  1.00 75.54  ? 212 ILE B CA  1 
ATOM 4176 C C   . ILE B 1 212 ? 43.330 0.902   43.988  1.00 72.42  ? 212 ILE B C   1 
ATOM 4177 O O   . ILE B 1 212 ? 43.095 0.207   44.984  1.00 73.02  ? 212 ILE B O   1 
ATOM 4178 C CB  . ILE B 1 212 ? 45.557 2.083   43.763  1.00 83.12  ? 212 ILE B CB  1 
ATOM 4179 C CG1 . ILE B 1 212 ? 46.880 2.111   42.992  1.00 84.37  ? 212 ILE B CG1 1 
ATOM 4180 C CG2 . ILE B 1 212 ? 45.788 2.050   45.270  1.00 79.99  ? 212 ILE B CG2 1 
ATOM 4181 C CD1 . ILE B 1 212 ? 47.996 1.321   43.645  1.00 87.12  ? 212 ILE B CD1 1 
ATOM 4182 N N   . TYR B 1 213 ? 42.403 1.695   43.447  1.00 66.80  ? 213 TYR B N   1 
ATOM 4183 C CA  . TYR B 1 213 ? 41.056 1.741   44.005  1.00 60.65  ? 213 TYR B CA  1 
ATOM 4184 C C   . TYR B 1 213 ? 40.290 0.463   43.692  1.00 68.77  ? 213 TYR B C   1 
ATOM 4185 O O   . TYR B 1 213 ? 39.656 -0.122  44.578  1.00 68.17  ? 213 TYR B O   1 
ATOM 4186 C CB  . TYR B 1 213 ? 40.303 2.961   43.474  1.00 65.04  ? 213 TYR B CB  1 
ATOM 4187 C CG  . TYR B 1 213 ? 38.900 3.082   44.025  1.00 56.86  ? 213 TYR B CG  1 
ATOM 4188 C CD1 . TYR B 1 213 ? 38.662 2.998   45.390  1.00 55.55  ? 213 TYR B CD1 1 
ATOM 4189 C CD2 . TYR B 1 213 ? 37.815 3.270   43.181  1.00 52.06  ? 213 TYR B CD2 1 
ATOM 4190 C CE1 . TYR B 1 213 ? 37.383 3.104   45.900  1.00 53.20  ? 213 TYR B CE1 1 
ATOM 4191 C CE2 . TYR B 1 213 ? 36.532 3.377   43.681  1.00 55.83  ? 213 TYR B CE2 1 
ATOM 4192 C CZ  . TYR B 1 213 ? 36.321 3.293   45.041  1.00 56.89  ? 213 TYR B CZ  1 
ATOM 4193 O OH  . TYR B 1 213 ? 35.044 3.399   45.544  1.00 54.47  ? 213 TYR B OH  1 
ATOM 4194 N N   . VAL B 1 214 ? 40.323 0.029   42.427  1.00 72.47  ? 214 VAL B N   1 
ATOM 4195 C CA  . VAL B 1 214 ? 39.657 -1.211  42.026  1.00 66.52  ? 214 VAL B CA  1 
ATOM 4196 C C   . VAL B 1 214 ? 40.062 -2.353  42.948  1.00 65.23  ? 214 VAL B C   1 
ATOM 4197 O O   . VAL B 1 214 ? 39.215 -3.080  43.482  1.00 71.33  ? 214 VAL B O   1 
ATOM 4198 C CB  . VAL B 1 214 ? 39.977 -1.539  40.557  1.00 69.42  ? 214 VAL B CB  1 
ATOM 4199 C CG1 . VAL B 1 214 ? 39.292 -2.830  40.143  1.00 65.75  ? 214 VAL B CG1 1 
ATOM 4200 C CG2 . VAL B 1 214 ? 39.559 -0.390  39.652  1.00 69.43  ? 214 VAL B CG2 1 
ATOM 4201 N N   . GLU B 1 215 ? 41.370 -2.526  43.146  1.00 69.99  ? 215 GLU B N   1 
ATOM 4202 C CA  . GLU B 1 215 ? 41.853 -3.580  44.030  1.00 71.08  ? 215 GLU B CA  1 
ATOM 4203 C C   . GLU B 1 215 ? 41.474 -3.313  45.483  1.00 71.78  ? 215 GLU B C   1 
ATOM 4204 O O   . GLU B 1 215 ? 41.218 -4.259  46.237  1.00 69.69  ? 215 GLU B O   1 
ATOM 4205 C CB  . GLU B 1 215 ? 43.369 -3.720  43.884  1.00 69.84  ? 215 GLU B CB  1 
ATOM 4206 C CG  . GLU B 1 215 ? 44.023 -4.668  44.874  1.00 78.07  ? 215 GLU B CG  1 
ATOM 4207 C CD  . GLU B 1 215 ? 44.154 -6.079  44.332  1.00 89.79  ? 215 GLU B CD  1 
ATOM 4208 O OE1 . GLU B 1 215 ? 43.163 -6.604  43.781  1.00 89.12  ? 215 GLU B OE1 1 
ATOM 4209 O OE2 . GLU B 1 215 ? 45.252 -6.661  44.456  1.00 88.62  ? 215 GLU B OE2 1 
ATOM 4210 N N   . PHE B 1 216 ? 41.416 -2.039  45.888  1.00 70.56  ? 216 PHE B N   1 
ATOM 4211 C CA  . PHE B 1 216 ? 41.094 -1.720  47.276  1.00 69.24  ? 216 PHE B CA  1 
ATOM 4212 C C   . PHE B 1 216 ? 39.686 -2.174  47.641  1.00 67.39  ? 216 PHE B C   1 
ATOM 4213 O O   . PHE B 1 216 ? 39.469 -2.729  48.725  1.00 61.84  ? 216 PHE B O   1 
ATOM 4214 C CB  . PHE B 1 216 ? 41.246 -0.220  47.527  1.00 63.12  ? 216 PHE B CB  1 
ATOM 4215 C CG  . PHE B 1 216 ? 40.490 0.270   48.729  1.00 61.60  ? 216 PHE B CG  1 
ATOM 4216 C CD1 . PHE B 1 216 ? 40.812 -0.181  50.000  1.00 61.94  ? 216 PHE B CD1 1 
ATOM 4217 C CD2 . PHE B 1 216 ? 39.448 1.170   48.587  1.00 60.78  ? 216 PHE B CD2 1 
ATOM 4218 C CE1 . PHE B 1 216 ? 40.113 0.266   51.106  1.00 66.31  ? 216 PHE B CE1 1 
ATOM 4219 C CE2 . PHE B 1 216 ? 38.746 1.621   49.690  1.00 55.10  ? 216 PHE B CE2 1 
ATOM 4220 C CZ  . PHE B 1 216 ? 39.079 1.168   50.951  1.00 53.87  ? 216 PHE B CZ  1 
ATOM 4221 N N   . MET B 1 217 ? 38.714 -1.942  46.756  1.00 64.16  ? 217 MET B N   1 
ATOM 4222 C CA  . MET B 1 217 ? 37.369 -2.446  47.011  1.00 63.47  ? 217 MET B CA  1 
ATOM 4223 C C   . MET B 1 217 ? 37.362 -3.966  47.041  1.00 67.77  ? 217 MET B C   1 
ATOM 4224 O O   . MET B 1 217 ? 36.945 -4.575  48.032  1.00 63.90  ? 217 MET B O   1 
ATOM 4225 C CB  . MET B 1 217 ? 36.387 -1.938  45.955  1.00 66.35  ? 217 MET B CB  1 
ATOM 4226 C CG  . MET B 1 217 ? 36.671 -0.561  45.402  1.00 53.76  ? 217 MET B CG  1 
ATOM 4227 S SD  . MET B 1 217 ? 35.245 0.046   44.483  1.00 54.90  ? 217 MET B SD  1 
ATOM 4228 C CE  . MET B 1 217 ? 35.874 -0.013  42.807  1.00 53.27  ? 217 MET B CE  1 
ATOM 4229 N N   . LYS B 1 218 ? 37.872 -4.593  45.976  1.00 72.57  ? 218 LYS B N   1 
ATOM 4230 C CA  . LYS B 1 218 ? 37.882 -6.050  45.889  1.00 68.09  ? 218 LYS B CA  1 
ATOM 4231 C C   . LYS B 1 218 ? 38.526 -6.673  47.117  1.00 65.47  ? 218 LYS B C   1 
ATOM 4232 O O   . LYS B 1 218 ? 38.157 -7.781  47.524  1.00 74.36  ? 218 LYS B O   1 
ATOM 4233 C CB  . LYS B 1 218 ? 38.609 -6.481  44.616  1.00 63.37  ? 218 LYS B CB  1 
ATOM 4234 C CG  . LYS B 1 218 ? 38.481 -7.952  44.285  1.00 71.56  ? 218 LYS B CG  1 
ATOM 4235 C CD  . LYS B 1 218 ? 39.743 -8.467  43.619  1.00 81.64  ? 218 LYS B CD  1 
ATOM 4236 C CE  . LYS B 1 218 ? 40.298 -9.678  44.346  1.00 75.39  ? 218 LYS B CE  1 
ATOM 4237 N NZ  . LYS B 1 218 ? 41.084 -10.549 43.431  1.00 77.18  ? 218 LYS B NZ  1 
ATOM 4238 N N   . ASN B 1 219 ? 39.485 -5.974  47.723  1.00 62.05  ? 219 ASN B N   1 
ATOM 4239 C CA  . ASN B 1 219 ? 40.032 -6.416  48.998  1.00 66.46  ? 219 ASN B CA  1 
ATOM 4240 C C   . ASN B 1 219 ? 39.015 -6.234  50.121  1.00 70.39  ? 219 ASN B C   1 
ATOM 4241 O O   . ASN B 1 219 ? 38.884 -7.100  50.994  1.00 61.85  ? 219 ASN B O   1 
ATOM 4242 C CB  . ASN B 1 219 ? 41.317 -5.648  49.300  1.00 68.99  ? 219 ASN B CB  1 
ATOM 4243 C CG  . ASN B 1 219 ? 42.465 -6.055  48.397  1.00 77.36  ? 219 ASN B CG  1 
ATOM 4244 O OD1 . ASN B 1 219 ? 42.509 -7.178  47.895  1.00 74.29  ? 219 ASN B OD1 1 
ATOM 4245 N ND2 . ASN B 1 219 ? 43.401 -5.138  48.182  1.00 82.57  ? 219 ASN B ND2 1 
ATOM 4246 N N   . GLN B 1 220 ? 38.289 -5.111  50.115  1.00 74.56  ? 220 GLN B N   1 
ATOM 4247 C CA  . GLN B 1 220 ? 37.316 -4.844  51.172  1.00 67.21  ? 220 GLN B CA  1 
ATOM 4248 C C   . GLN B 1 220 ? 36.107 -5.770  51.079  1.00 60.00  ? 220 GLN B C   1 
ATOM 4249 O O   . GLN B 1 220 ? 35.623 -6.259  52.107  1.00 54.04  ? 220 GLN B O   1 
ATOM 4250 C CB  . GLN B 1 220 ? 36.876 -3.380  51.129  1.00 63.85  ? 220 GLN B CB  1 
ATOM 4251 C CG  . GLN B 1 220 ? 37.856 -2.420  51.786  1.00 65.44  ? 220 GLN B CG  1 
ATOM 4252 C CD  . GLN B 1 220 ? 37.163 -1.264  52.485  1.00 59.34  ? 220 GLN B CD  1 
ATOM 4253 O OE1 . GLN B 1 220 ? 36.373 -0.540  51.879  1.00 57.31  ? 220 GLN B OE1 1 
ATOM 4254 N NE2 . GLN B 1 220 ? 37.459 -1.084  53.768  1.00 56.99  ? 220 GLN B NE2 1 
ATOM 4255 N N   . ILE B 1 221 ? 35.587 -6.008  49.869  1.00 62.48  ? 221 ILE B N   1 
ATOM 4256 C CA  . ILE B 1 221 ? 34.462 -6.934  49.743  1.00 66.32  ? 221 ILE B CA  1 
ATOM 4257 C C   . ILE B 1 221 ? 34.876 -8.332  50.192  1.00 61.45  ? 221 ILE B C   1 
ATOM 4258 O O   . ILE B 1 221 ? 34.061 -9.082  50.744  1.00 59.77  ? 221 ILE B O   1 
ATOM 4259 C CB  . ILE B 1 221 ? 33.873 -6.938  48.312  1.00 62.58  ? 221 ILE B CB  1 
ATOM 4260 C CG1 . ILE B 1 221 ? 33.233 -5.592  47.952  1.00 61.15  ? 221 ILE B CG1 1 
ATOM 4261 C CG2 . ILE B 1 221 ? 32.807 -7.996  48.162  1.00 52.98  ? 221 ILE B CG2 1 
ATOM 4262 C CD1 . ILE B 1 221 ? 34.108 -4.641  47.211  1.00 59.66  ? 221 ILE B CD1 1 
ATOM 4263 N N   . THR B 1 222 ? 36.145 -8.700  49.987  1.00 60.01  ? 222 THR B N   1 
ATOM 4264 C CA  . THR B 1 222 ? 36.637 -9.966  50.525  1.00 62.59  ? 222 THR B CA  1 
ATOM 4265 C C   . THR B 1 222 ? 36.514 -9.996  52.046  1.00 56.52  ? 222 THR B C   1 
ATOM 4266 O O   . THR B 1 222 ? 36.208 -11.041 52.632  1.00 59.05  ? 222 THR B O   1 
ATOM 4267 C CB  . THR B 1 222 ? 38.088 -10.197 50.101  1.00 57.74  ? 222 THR B CB  1 
ATOM 4268 O OG1 . THR B 1 222 ? 38.197 -10.088 48.677  1.00 67.50  ? 222 THR B OG1 1 
ATOM 4269 C CG2 . THR B 1 222 ? 38.558 -11.577 50.531  1.00 45.70  ? 222 THR B CG2 1 
ATOM 4270 N N   . GLU B 1 223 ? 36.742 -8.855  52.700  1.00 63.06  ? 223 GLU B N   1 
ATOM 4271 C CA  . GLU B 1 223 ? 36.592 -8.791  54.151  1.00 59.61  ? 223 GLU B CA  1 
ATOM 4272 C C   . GLU B 1 223 ? 35.136 -8.965  54.560  1.00 62.91  ? 223 GLU B C   1 
ATOM 4273 O O   . GLU B 1 223 ? 34.827 -9.713  55.494  1.00 63.30  ? 223 GLU B O   1 
ATOM 4274 C CB  . GLU B 1 223 ? 37.117 -7.455  54.678  1.00 64.89  ? 223 GLU B CB  1 
ATOM 4275 C CG  . GLU B 1 223 ? 38.565 -7.144  54.370  1.00 64.68  ? 223 GLU B CG  1 
ATOM 4276 C CD  . GLU B 1 223 ? 39.172 -6.221  55.409  1.00 79.01  ? 223 GLU B CD  1 
ATOM 4277 O OE1 . GLU B 1 223 ? 39.369 -6.667  56.560  1.00 81.33  ? 223 GLU B OE1 1 
ATOM 4278 O OE2 . GLU B 1 223 ? 39.428 -5.042  55.085  1.00 77.09  ? 223 GLU B OE2 1 
ATOM 4279 N N   . LEU B 1 224 ? 34.228 -8.278  53.863  1.00 65.92  ? 224 LEU B N   1 
ATOM 4280 C CA  . LEU B 1 224 ? 32.820 -8.289  54.246  1.00 61.60  ? 224 LEU B CA  1 
ATOM 4281 C C   . LEU B 1 224 ? 32.203 -9.671  54.070  1.00 58.57  ? 224 LEU B C   1 
ATOM 4282 O O   . LEU B 1 224 ? 31.370 -10.094 54.880  1.00 58.42  ? 224 LEU B O   1 
ATOM 4283 C CB  . LEU B 1 224 ? 32.053 -7.246  53.433  1.00 55.88  ? 224 LEU B CB  1 
ATOM 4284 C CG  . LEU B 1 224 ? 32.264 -5.789  53.855  1.00 56.08  ? 224 LEU B CG  1 
ATOM 4285 C CD1 . LEU B 1 224 ? 31.504 -4.842  52.939  1.00 43.63  ? 224 LEU B CD1 1 
ATOM 4286 C CD2 . LEU B 1 224 ? 31.853 -5.581  55.305  1.00 49.56  ? 224 LEU B CD2 1 
ATOM 4287 N N   . LEU B 1 225 ? 32.597 -10.388 53.018  1.00 53.57  ? 225 LEU B N   1 
ATOM 4288 C CA  . LEU B 1 225 ? 32.014 -11.694 52.740  1.00 62.10  ? 225 LEU B CA  1 
ATOM 4289 C C   . LEU B 1 225 ? 32.555 -12.797 53.639  1.00 63.24  ? 225 LEU B C   1 
ATOM 4290 O O   . LEU B 1 225 ? 31.917 -13.849 53.753  1.00 63.21  ? 225 LEU B O   1 
ATOM 4291 C CB  . LEU B 1 225 ? 32.254 -12.071 51.276  1.00 55.90  ? 225 LEU B CB  1 
ATOM 4292 C CG  . LEU B 1 225 ? 31.381 -11.345 50.252  1.00 58.95  ? 225 LEU B CG  1 
ATOM 4293 C CD1 . LEU B 1 225 ? 32.025 -11.360 48.876  1.00 54.32  ? 225 LEU B CD1 1 
ATOM 4294 C CD2 . LEU B 1 225 ? 30.000 -11.966 50.207  1.00 58.27  ? 225 LEU B CD2 1 
ATOM 4295 N N   . THR B 1 226 ? 33.698 -12.584 54.288  1.00 56.38  ? 226 THR B N   1 
ATOM 4296 C CA  . THR B 1 226 ? 34.375 -13.643 55.026  1.00 59.52  ? 226 THR B CA  1 
ATOM 4297 C C   . THR B 1 226 ? 34.201 -13.547 56.536  1.00 61.70  ? 226 THR B C   1 
ATOM 4298 O O   . THR B 1 226 ? 33.981 -14.569 57.193  1.00 59.20  ? 226 THR B O   1 
ATOM 4299 C CB  . THR B 1 226 ? 35.870 -13.633 54.695  1.00 55.75  ? 226 THR B CB  1 
ATOM 4300 O OG1 . THR B 1 226 ? 36.344 -12.281 54.680  1.00 60.43  ? 226 THR B OG1 1 
ATOM 4301 C CG2 . THR B 1 226 ? 36.116 -14.261 53.333  1.00 60.71  ? 226 THR B CG2 1 
ATOM 4302 N N   . ASN B 1 227 ? 34.290 -12.349 57.103  1.00 64.07  ? 227 ASN B N   1 
ATOM 4303 C CA  . ASN B 1 227 ? 34.337 -12.181 58.549  1.00 60.09  ? 227 ASN B CA  1 
ATOM 4304 C C   . ASN B 1 227 ? 32.963 -12.016 59.184  1.00 64.77  ? 227 ASN B C   1 
ATOM 4305 O O   . ASN B 1 227 ? 32.884 -11.787 60.395  1.00 68.25  ? 227 ASN B O   1 
ATOM 4306 C CB  . ASN B 1 227 ? 35.216 -10.979 58.908  1.00 60.44  ? 227 ASN B CB  1 
ATOM 4307 C CG  . ASN B 1 227 ? 36.595 -11.060 58.283  1.00 67.67  ? 227 ASN B CG  1 
ATOM 4308 O OD1 . ASN B 1 227 ? 36.816 -11.815 57.337  1.00 63.31  ? 227 ASN B OD1 1 
ATOM 4309 N ND2 . ASN B 1 227 ? 37.531 -10.280 58.811  1.00 79.18  ? 227 ASN B ND2 1 
ATOM 4310 N N   . TYR B 1 228 ? 31.880 -12.127 58.409  1.00 61.48  ? 228 TYR B N   1 
ATOM 4311 C CA  . TYR B 1 228 ? 30.545 -11.853 58.928  1.00 62.04  ? 228 TYR B CA  1 
ATOM 4312 C C   . TYR B 1 228 ? 29.552 -12.959 58.587  1.00 72.57  ? 228 TYR B C   1 
ATOM 4313 O O   . TYR B 1 228 ? 28.339 -12.725 58.613  1.00 74.39  ? 228 TYR B O   1 
ATOM 4314 C CB  . TYR B 1 228 ? 30.048 -10.497 58.418  1.00 58.85  ? 228 TYR B CB  1 
ATOM 4315 C CG  . TYR B 1 228 ? 30.996 -9.371  58.772  1.00 62.22  ? 228 TYR B CG  1 
ATOM 4316 C CD1 . TYR B 1 228 ? 30.906 -8.723  59.997  1.00 56.57  ? 228 TYR B CD1 1 
ATOM 4317 C CD2 . TYR B 1 228 ? 31.998 -8.978  57.894  1.00 61.26  ? 228 TYR B CD2 1 
ATOM 4318 C CE1 . TYR B 1 228 ? 31.777 -7.706  60.332  1.00 56.94  ? 228 TYR B CE1 1 
ATOM 4319 C CE2 . TYR B 1 228 ? 32.876 -7.961  58.221  1.00 60.46  ? 228 TYR B CE2 1 
ATOM 4320 C CZ  . TYR B 1 228 ? 32.759 -7.328  59.441  1.00 62.52  ? 228 TYR B CZ  1 
ATOM 4321 O OH  . TYR B 1 228 ? 33.630 -6.318  59.772  1.00 59.42  ? 228 TYR B OH  1 
ATOM 4322 N N   . GLY B 1 229 ? 30.039 -14.156 58.270  1.00 71.50  ? 229 GLY B N   1 
ATOM 4323 C CA  . GLY B 1 229 ? 29.180 -15.285 58.007  1.00 69.43  ? 229 GLY B CA  1 
ATOM 4324 C C   . GLY B 1 229 ? 28.466 -15.200 56.675  1.00 68.39  ? 229 GLY B C   1 
ATOM 4325 O O   . GLY B 1 229 ? 28.837 -14.424 55.788  1.00 62.80  ? 229 GLY B O   1 
ATOM 4326 N N   . PRO B 1 230 ? 27.429 -16.018 56.505  1.00 71.99  ? 230 PRO B N   1 
ATOM 4327 C CA  . PRO B 1 230 ? 26.662 -15.985 55.254  1.00 69.37  ? 230 PRO B CA  1 
ATOM 4328 C C   . PRO B 1 230 ? 25.960 -14.644 55.096  1.00 66.60  ? 230 PRO B C   1 
ATOM 4329 O O   . PRO B 1 230 ? 25.280 -14.168 56.008  1.00 65.89  ? 230 PRO B O   1 
ATOM 4330 C CB  . PRO B 1 230 ? 25.664 -17.141 55.412  1.00 66.33  ? 230 PRO B CB  1 
ATOM 4331 C CG  . PRO B 1 230 ? 26.075 -17.878 56.671  1.00 70.70  ? 230 PRO B CG  1 
ATOM 4332 C CD  . PRO B 1 230 ? 26.805 -16.889 57.512  1.00 72.95  ? 230 PRO B CD  1 
ATOM 4333 N N   . VAL B 1 231 ? 26.136 -14.032 53.929  1.00 62.22  ? 231 VAL B N   1 
ATOM 4334 C CA  . VAL B 1 231 ? 25.615 -12.698 53.667  1.00 53.95  ? 231 VAL B CA  1 
ATOM 4335 C C   . VAL B 1 231 ? 24.646 -12.760 52.494  1.00 54.61  ? 231 VAL B C   1 
ATOM 4336 O O   . VAL B 1 231 ? 24.815 -13.554 51.562  1.00 60.69  ? 231 VAL B O   1 
ATOM 4337 C CB  . VAL B 1 231 ? 26.769 -11.699 53.410  1.00 49.92  ? 231 VAL B CB  1 
ATOM 4338 C CG1 . VAL B 1 231 ? 26.492 -10.810 52.206  1.00 50.43  ? 231 VAL B CG1 1 
ATOM 4339 C CG2 . VAL B 1 231 ? 27.024 -10.862 54.658  1.00 49.56  ? 231 VAL B CG2 1 
ATOM 4340 N N   . GLY B 1 232 ? 23.614 -11.915 52.552  1.00 53.96  ? 232 GLY B N   1 
ATOM 4341 C CA  . GLY B 1 232 ? 22.604 -11.923 51.506  1.00 46.43  ? 232 GLY B CA  1 
ATOM 4342 C C   . GLY B 1 232 ? 23.127 -11.386 50.188  1.00 49.49  ? 232 GLY B C   1 
ATOM 4343 O O   . GLY B 1 232 ? 23.008 -12.039 49.147  1.00 56.59  ? 232 GLY B O   1 
ATOM 4344 N N   . GLY B 1 233 ? 23.706 -10.188 50.207  1.00 48.51  ? 233 GLY B N   1 
ATOM 4345 C CA  . GLY B 1 233 ? 24.223 -9.620  48.978  1.00 48.57  ? 233 GLY B CA  1 
ATOM 4346 C C   . GLY B 1 233 ? 25.169 -8.466  49.210  1.00 46.41  ? 233 GLY B C   1 
ATOM 4347 O O   . GLY B 1 233 ? 25.211 -7.869  50.291  1.00 46.77  ? 233 GLY B O   1 
ATOM 4348 N N   . ILE B 1 234 ? 25.941 -8.166  48.170  1.00 49.72  ? 234 ILE B N   1 
ATOM 4349 C CA  . ILE B 1 234 ? 26.786 -6.980  48.113  1.00 41.06  ? 234 ILE B CA  1 
ATOM 4350 C C   . ILE B 1 234 ? 26.056 -5.945  47.269  1.00 51.21  ? 234 ILE B C   1 
ATOM 4351 O O   . ILE B 1 234 ? 25.809 -6.166  46.077  1.00 50.99  ? 234 ILE B O   1 
ATOM 4352 C CB  . ILE B 1 234 ? 28.173 -7.302  47.537  1.00 41.41  ? 234 ILE B CB  1 
ATOM 4353 C CG1 . ILE B 1 234 ? 28.865 -8.373  48.382  1.00 42.47  ? 234 ILE B CG1 1 
ATOM 4354 C CG2 . ILE B 1 234 ? 29.028 -6.045  47.467  1.00 55.30  ? 234 ILE B CG2 1 
ATOM 4355 C CD1 . ILE B 1 234 ? 28.971 -8.024  49.851  1.00 40.54  ? 234 ILE B CD1 1 
ATOM 4356 N N   . TRP B 1 235 ? 25.709 -4.819  47.889  1.00 47.50  ? 235 TRP B N   1 
ATOM 4357 C CA  . TRP B 1 235 ? 24.814 -3.817  47.309  1.00 44.73  ? 235 TRP B CA  1 
ATOM 4358 C C   . TRP B 1 235 ? 25.665 -2.637  46.850  1.00 43.95  ? 235 TRP B C   1 
ATOM 4359 O O   . TRP B 1 235 ? 25.951 -1.719  47.618  1.00 51.29  ? 235 TRP B O   1 
ATOM 4360 C CB  . TRP B 1 235 ? 23.771 -3.407  48.345  1.00 51.94  ? 235 TRP B CB  1 
ATOM 4361 C CG  . TRP B 1 235 ? 22.450 -2.918  47.822  1.00 49.06  ? 235 TRP B CG  1 
ATOM 4362 C CD1 . TRP B 1 235 ? 21.294 -3.637  47.725  1.00 46.62  ? 235 TRP B CD1 1 
ATOM 4363 C CD2 . TRP B 1 235 ? 22.132 -1.589  47.392  1.00 45.91  ? 235 TRP B CD2 1 
ATOM 4364 N NE1 . TRP B 1 235 ? 20.283 -2.847  47.233  1.00 44.55  ? 235 TRP B NE1 1 
ATOM 4365 C CE2 . TRP B 1 235 ? 20.771 -1.584  47.021  1.00 49.75  ? 235 TRP B CE2 1 
ATOM 4366 C CE3 . TRP B 1 235 ? 22.867 -0.407  47.270  1.00 46.19  ? 235 TRP B CE3 1 
ATOM 4367 C CZ2 . TRP B 1 235 ? 20.133 -0.444  46.538  1.00 43.34  ? 235 TRP B CZ2 1 
ATOM 4368 C CZ3 . TRP B 1 235 ? 22.230 0.725   46.788  1.00 50.51  ? 235 TRP B CZ3 1 
ATOM 4369 C CH2 . TRP B 1 235 ? 20.876 0.697   46.430  1.00 41.47  ? 235 TRP B CH2 1 
ATOM 4370 N N   . LEU B 1 236 ? 26.067 -2.659  45.582  1.00 47.41  ? 236 LEU B N   1 
ATOM 4371 C CA  . LEU B 1 236 ? 26.965 -1.640  45.057  1.00 39.66  ? 236 LEU B CA  1 
ATOM 4372 C C   . LEU B 1 236 ? 26.183 -0.408  44.618  1.00 42.41  ? 236 LEU B C   1 
ATOM 4373 O O   . LEU B 1 236 ? 25.049 -0.502  44.140  1.00 45.61  ? 236 LEU B O   1 
ATOM 4374 C CB  . LEU B 1 236 ? 27.777 -2.184  43.880  1.00 48.35  ? 236 LEU B CB  1 
ATOM 4375 C CG  . LEU B 1 236 ? 28.611 -3.450  44.099  1.00 56.87  ? 236 LEU B CG  1 
ATOM 4376 C CD1 . LEU B 1 236 ? 29.114 -3.994  42.769  1.00 55.87  ? 236 LEU B CD1 1 
ATOM 4377 C CD2 . LEU B 1 236 ? 29.772 -3.187  45.047  1.00 57.77  ? 236 LEU B CD2 1 
ATOM 4378 N N   . ASP B 1 237 ? 26.805 0.757   44.782  1.00 46.42  ? 237 ASP B N   1 
ATOM 4379 C CA  . ASP B 1 237 ? 26.195 2.032   44.434  1.00 42.48  ? 237 ASP B CA  1 
ATOM 4380 C C   . ASP B 1 237 ? 27.203 2.897   43.688  1.00 42.68  ? 237 ASP B C   1 
ATOM 4381 O O   . ASP B 1 237 ? 28.398 2.592   43.628  1.00 48.67  ? 237 ASP B O   1 
ATOM 4382 C CB  . ASP B 1 237 ? 25.686 2.763   45.685  1.00 46.36  ? 237 ASP B CB  1 
ATOM 4383 C CG  . ASP B 1 237 ? 24.751 3.911   45.354  1.00 48.01  ? 237 ASP B CG  1 
ATOM 4384 O OD1 . ASP B 1 237 ? 24.214 3.933   44.226  1.00 46.81  ? 237 ASP B OD1 1 
ATOM 4385 O OD2 . ASP B 1 237 ? 24.555 4.792   46.218  1.00 42.58  ? 237 ASP B OD2 1 
ATOM 4386 N N   . GLY B 1 238 ? 26.705 3.985   43.113  1.00 46.68  ? 238 GLY B N   1 
ATOM 4387 C CA  . GLY B 1 238 ? 27.532 4.915   42.376  1.00 55.43  ? 238 GLY B CA  1 
ATOM 4388 C C   . GLY B 1 238 ? 27.548 4.713   40.879  1.00 55.78  ? 238 GLY B C   1 
ATOM 4389 O O   . GLY B 1 238 ? 28.513 5.131   40.232  1.00 57.89  ? 238 GLY B O   1 
ATOM 4390 N N   . VAL B 1 239 ? 26.506 4.099   40.312  1.00 58.33  ? 239 VAL B N   1 
ATOM 4391 C CA  . VAL B 1 239 ? 26.542 3.623   38.931  1.00 56.27  ? 239 VAL B CA  1 
ATOM 4392 C C   . VAL B 1 239 ? 26.716 4.766   37.936  1.00 51.19  ? 239 VAL B C   1 
ATOM 4393 O O   . VAL B 1 239 ? 27.234 4.559   36.832  1.00 55.54  ? 239 VAL B O   1 
ATOM 4394 C CB  . VAL B 1 239 ? 25.274 2.794   38.634  1.00 58.31  ? 239 VAL B CB  1 
ATOM 4395 C CG1 . VAL B 1 239 ? 24.190 3.653   37.994  1.00 53.04  ? 239 VAL B CG1 1 
ATOM 4396 C CG2 . VAL B 1 239 ? 25.612 1.608   37.749  1.00 57.08  ? 239 VAL B CG2 1 
ATOM 4397 N N   . ALA B 1 240 ? 26.287 5.979   38.296  1.00 58.57  ? 240 ALA B N   1 
ATOM 4398 C CA  . ALA B 1 240 ? 26.280 7.077   37.334  1.00 52.65  ? 240 ALA B CA  1 
ATOM 4399 C C   . ALA B 1 240 ? 27.684 7.471   36.891  1.00 56.61  ? 240 ALA B C   1 
ATOM 4400 O O   . ALA B 1 240 ? 27.863 7.957   35.768  1.00 60.96  ? 240 ALA B O   1 
ATOM 4401 C CB  . ALA B 1 240 ? 25.555 8.286   37.925  1.00 61.46  ? 240 ALA B CB  1 
ATOM 4402 N N   . THR B 1 241 ? 28.686 7.281   37.746  1.00 51.69  ? 241 THR B N   1 
ATOM 4403 C CA  . THR B 1 241 ? 30.036 7.712   37.399  1.00 53.66  ? 241 THR B CA  1 
ATOM 4404 C C   . THR B 1 241 ? 30.697 6.760   36.399  1.00 55.99  ? 241 THR B C   1 
ATOM 4405 O O   . THR B 1 241 ? 31.152 7.222   35.345  1.00 60.22  ? 241 THR B O   1 
ATOM 4406 C CB  . THR B 1 241 ? 30.893 7.879   38.661  1.00 53.67  ? 241 THR B CB  1 
ATOM 4407 O OG1 . THR B 1 241 ? 30.602 9.143   39.271  1.00 58.30  ? 241 THR B OG1 1 
ATOM 4408 C CG2 . THR B 1 241 ? 32.375 7.822   38.319  1.00 56.77  ? 241 THR B CG2 1 
ATOM 4409 N N   . PRO B 1 242 ? 30.789 5.447   36.667  1.00 59.96  ? 242 PRO B N   1 
ATOM 4410 C CA  . PRO B 1 242 ? 31.393 4.559   35.657  1.00 64.82  ? 242 PRO B CA  1 
ATOM 4411 C C   . PRO B 1 242 ? 30.641 4.534   34.338  1.00 64.13  ? 242 PRO B C   1 
ATOM 4412 O O   . PRO B 1 242 ? 31.268 4.390   33.281  1.00 63.38  ? 242 PRO B O   1 
ATOM 4413 C CB  . PRO B 1 242 ? 31.373 3.186   36.343  1.00 61.30  ? 242 PRO B CB  1 
ATOM 4414 C CG  . PRO B 1 242 ? 30.282 3.282   37.334  1.00 55.92  ? 242 PRO B CG  1 
ATOM 4415 C CD  . PRO B 1 242 ? 30.369 4.678   37.852  1.00 55.19  ? 242 PRO B CD  1 
ATOM 4416 N N   . ALA B 1 243 ? 29.315 4.682   34.364  1.00 63.22  ? 243 ALA B N   1 
ATOM 4417 C CA  . ALA B 1 243 ? 28.519 4.645   33.144  1.00 65.73  ? 243 ALA B CA  1 
ATOM 4418 C C   . ALA B 1 243 ? 28.566 5.949   32.360  1.00 70.25  ? 243 ALA B C   1 
ATOM 4419 O O   . ALA B 1 243 ? 28.079 5.988   31.225  1.00 74.48  ? 243 ALA B O   1 
ATOM 4420 C CB  . ALA B 1 243 ? 27.065 4.299   33.476  1.00 57.08  ? 243 ALA B CB  1 
ATOM 4421 N N   . SER B 1 244 ? 29.142 7.008   32.928  1.00 69.60  ? 244 SER B N   1 
ATOM 4422 C CA  . SER B 1 244 ? 29.253 8.276   32.220  1.00 75.91  ? 244 SER B CA  1 
ATOM 4423 C C   . SER B 1 244 ? 30.337 8.248   31.151  1.00 76.83  ? 244 SER B C   1 
ATOM 4424 O O   . SER B 1 244 ? 30.355 9.126   30.281  1.00 77.90  ? 244 SER B O   1 
ATOM 4425 C CB  . SER B 1 244 ? 29.519 9.412   33.212  1.00 65.60  ? 244 SER B CB  1 
ATOM 4426 O OG  . SER B 1 244 ? 30.904 9.685   33.331  1.00 71.25  ? 244 SER B OG  1 
ATOM 4427 N N   . ARG B 1 245 ? 31.229 7.257   31.194  1.00 71.87  ? 245 ARG B N   1 
ATOM 4428 C CA  . ARG B 1 245 ? 32.306 7.073   30.219  1.00 73.82  ? 245 ARG B CA  1 
ATOM 4429 C C   . ARG B 1 245 ? 32.278 5.620   29.750  1.00 79.17  ? 245 ARG B C   1 
ATOM 4430 O O   . ARG B 1 245 ? 32.996 4.775   30.290  1.00 80.93  ? 245 ARG B O   1 
ATOM 4431 C CB  . ARG B 1 245 ? 33.661 7.439   30.820  1.00 72.32  ? 245 ARG B CB  1 
ATOM 4432 C CG  . ARG B 1 245 ? 34.123 8.851   30.504  1.00 84.27  ? 245 ARG B CG  1 
ATOM 4433 C CD  . ARG B 1 245 ? 33.252 9.876   31.195  1.00 77.70  ? 245 ARG B CD  1 
ATOM 4434 N NE  . ARG B 1 245 ? 33.861 11.199  31.226  1.00 72.48  ? 245 ARG B NE  1 
ATOM 4435 C CZ  . ARG B 1 245 ? 33.173 12.333  31.214  1.00 79.68  ? 245 ARG B CZ  1 
ATOM 4436 N NH1 . ARG B 1 245 ? 31.850 12.337  31.182  1.00 77.46  ? 245 ARG B NH1 1 
ATOM 4437 N NH2 . ARG B 1 245 ? 33.828 13.490  31.238  1.00 78.22  ? 245 ARG B NH2 1 
ATOM 4438 N N   . LYS B 1 246 ? 31.446 5.327   28.746  1.00 80.30  ? 246 LYS B N   1 
ATOM 4439 C CA  . LYS B 1 246 ? 31.165 3.940   28.399  1.00 75.93  ? 246 LYS B CA  1 
ATOM 4440 C C   . LYS B 1 246 ? 32.279 3.290   27.593  1.00 69.04  ? 246 LYS B C   1 
ATOM 4441 O O   . LYS B 1 246 ? 32.263 2.067   27.422  1.00 74.86  ? 246 LYS B O   1 
ATOM 4442 C CB  . LYS B 1 246 ? 29.870 3.859   27.586  1.00 68.12  ? 246 LYS B CB  1 
ATOM 4443 C CG  . LYS B 1 246 ? 28.605 4.145   28.366  1.00 67.87  ? 246 LYS B CG  1 
ATOM 4444 C CD  . LYS B 1 246 ? 28.173 2.953   29.193  1.00 65.23  ? 246 LYS B CD  1 
ATOM 4445 C CE  . LYS B 1 246 ? 26.827 3.214   29.846  1.00 68.64  ? 246 LYS B CE  1 
ATOM 4446 N NZ  . LYS B 1 246 ? 26.208 1.964   30.365  1.00 76.41  ? 246 LYS B NZ  1 
ATOM 4447 N N   . GLY B 1 247 ? 33.258 4.067   27.123  1.00 74.74  ? 247 GLY B N   1 
ATOM 4448 C CA  . GLY B 1 247 ? 34.486 3.484   26.618  1.00 74.43  ? 247 GLY B CA  1 
ATOM 4449 C C   . GLY B 1 247 ? 35.498 3.190   27.698  1.00 77.80  ? 247 GLY B C   1 
ATOM 4450 O O   . GLY B 1 247 ? 36.458 2.454   27.454  1.00 75.64  ? 247 GLY B O   1 
ATOM 4451 N N   . LYS B 1 248 ? 35.304 3.766   28.883  1.00 76.66  ? 248 LYS B N   1 
ATOM 4452 C CA  . LYS B 1 248 ? 36.146 3.538   30.046  1.00 74.76  ? 248 LYS B CA  1 
ATOM 4453 C C   . LYS B 1 248 ? 35.568 2.521   31.024  1.00 71.00  ? 248 LYS B C   1 
ATOM 4454 O O   . LYS B 1 248 ? 36.235 2.195   32.013  1.00 70.09  ? 248 LYS B O   1 
ATOM 4455 C CB  . LYS B 1 248 ? 36.381 4.862   30.781  1.00 85.04  ? 248 LYS B CB  1 
ATOM 4456 C CG  . LYS B 1 248 ? 37.096 5.919   29.964  1.00 82.78  ? 248 LYS B CG  1 
ATOM 4457 C CD  . LYS B 1 248 ? 38.046 6.724   30.831  1.00 82.68  ? 248 LYS B CD  1 
ATOM 4458 C CE  . LYS B 1 248 ? 37.495 8.115   31.087  1.00 83.23  ? 248 LYS B CE  1 
ATOM 4459 N NZ  . LYS B 1 248 ? 38.572 9.115   31.290  1.00 89.25  ? 248 LYS B NZ  1 
ATOM 4460 N N   . LEU B 1 249 ? 34.336 2.053   30.798  1.00 69.81  ? 249 LEU B N   1 
ATOM 4461 C CA  . LEU B 1 249 ? 33.679 1.139   31.732  1.00 78.73  ? 249 LEU B CA  1 
ATOM 4462 C C   . LEU B 1 249 ? 34.558 -0.048  32.118  1.00 72.83  ? 249 LEU B C   1 
ATOM 4463 O O   . LEU B 1 249 ? 34.528 -0.499  33.269  1.00 75.61  ? 249 LEU B O   1 
ATOM 4464 C CB  . LEU B 1 249 ? 32.359 0.647   31.134  1.00 78.93  ? 249 LEU B CB  1 
ATOM 4465 C CG  . LEU B 1 249 ? 31.236 0.336   32.127  1.00 61.82  ? 249 LEU B CG  1 
ATOM 4466 C CD1 . LEU B 1 249 ? 31.400 1.145   33.400  1.00 68.66  ? 249 LEU B CD1 1 
ATOM 4467 C CD2 . LEU B 1 249 ? 29.877 0.599   31.498  1.00 69.20  ? 249 LEU B CD2 1 
ATOM 4468 N N   . HIS B 1 250 ? 35.346 -0.571  31.176  1.00 70.55  ? 250 HIS B N   1 
ATOM 4469 C CA  . HIS B 1 250 ? 36.093 -1.797  31.441  1.00 68.83  ? 250 HIS B CA  1 
ATOM 4470 C C   . HIS B 1 250 ? 37.235 -1.593  32.429  1.00 67.67  ? 250 HIS B C   1 
ATOM 4471 O O   . HIS B 1 250 ? 37.722 -2.577  32.999  1.00 56.90  ? 250 HIS B O   1 
ATOM 4472 C CB  . HIS B 1 250 ? 36.637 -2.389  30.139  1.00 70.00  ? 250 HIS B CB  1 
ATOM 4473 C CG  . HIS B 1 250 ? 37.580 -1.488  29.405  1.00 64.39  ? 250 HIS B CG  1 
ATOM 4474 N ND1 . HIS B 1 250 ? 37.176 -0.315  28.804  1.00 66.56  ? 250 HIS B ND1 1 
ATOM 4475 C CD2 . HIS B 1 250 ? 38.912 -1.587  29.178  1.00 71.71  ? 250 HIS B CD2 1 
ATOM 4476 C CE1 . HIS B 1 250 ? 38.216 0.264   28.232  1.00 71.79  ? 250 HIS B CE1 1 
ATOM 4477 N NE2 . HIS B 1 250 ? 39.282 -0.484  28.449  1.00 73.23  ? 250 HIS B NE2 1 
ATOM 4478 N N   . LEU B 1 251 ? 37.675 -0.351  32.644  1.00 63.41  ? 251 LEU B N   1 
ATOM 4479 C CA  . LEU B 1 251 ? 38.771 -0.099  33.575  1.00 68.26  ? 251 LEU B CA  1 
ATOM 4480 C C   . LEU B 1 251 ? 38.411 -0.454  35.013  1.00 71.16  ? 251 LEU B C   1 
ATOM 4481 O O   . LEU B 1 251 ? 39.314 -0.661  35.832  1.00 66.12  ? 251 LEU B O   1 
ATOM 4482 C CB  . LEU B 1 251 ? 39.201 1.374   33.505  1.00 67.19  ? 251 LEU B CB  1 
ATOM 4483 C CG  . LEU B 1 251 ? 39.968 1.919   32.291  1.00 74.70  ? 251 LEU B CG  1 
ATOM 4484 C CD1 . LEU B 1 251 ? 39.180 1.834   30.999  1.00 76.90  ? 251 LEU B CD1 1 
ATOM 4485 C CD2 . LEU B 1 251 ? 40.399 3.359   32.540  1.00 61.95  ? 251 LEU B CD2 1 
ATOM 4486 N N   . PHE B 1 252 ? 37.119 -0.533  35.336  1.00 69.33  ? 252 PHE B N   1 
ATOM 4487 C CA  . PHE B 1 252 ? 36.687 -0.829  36.696  1.00 74.57  ? 252 PHE B CA  1 
ATOM 4488 C C   . PHE B 1 252 ? 36.811 -2.300  37.074  1.00 73.56  ? 252 PHE B C   1 
ATOM 4489 O O   . PHE B 1 252 ? 36.770 -2.616  38.269  1.00 73.01  ? 252 PHE B O   1 
ATOM 4490 C CB  . PHE B 1 252 ? 35.239 -0.377  36.892  1.00 70.33  ? 252 PHE B CB  1 
ATOM 4491 C CG  . PHE B 1 252 ? 35.108 1.040   37.361  1.00 60.40  ? 252 PHE B CG  1 
ATOM 4492 C CD1 . PHE B 1 252 ? 35.138 1.342   38.711  1.00 61.44  ? 252 PHE B CD1 1 
ATOM 4493 C CD2 . PHE B 1 252 ? 34.957 2.073   36.452  1.00 68.36  ? 252 PHE B CD2 1 
ATOM 4494 C CE1 . PHE B 1 252 ? 35.018 2.647   39.147  1.00 66.79  ? 252 PHE B CE1 1 
ATOM 4495 C CE2 . PHE B 1 252 ? 34.836 3.379   36.882  1.00 67.24  ? 252 PHE B CE2 1 
ATOM 4496 C CZ  . PHE B 1 252 ? 34.866 3.667   38.229  1.00 69.20  ? 252 PHE B CZ  1 
ATOM 4497 N N   . GLU B 1 253 ? 36.954 -3.198  36.099  1.00 73.40  ? 253 GLU B N   1 
ATOM 4498 C CA  . GLU B 1 253 ? 36.993 -4.642  36.345  1.00 75.26  ? 253 GLU B CA  1 
ATOM 4499 C C   . GLU B 1 253 ? 35.790 -5.094  37.175  1.00 67.68  ? 253 GLU B C   1 
ATOM 4500 O O   . GLU B 1 253 ? 35.920 -5.805  38.174  1.00 65.06  ? 253 GLU B O   1 
ATOM 4501 C CB  . GLU B 1 253 ? 38.304 -5.052  37.021  1.00 75.22  ? 253 GLU B CB  1 
ATOM 4502 C CG  . GLU B 1 253 ? 39.552 -4.801  36.189  1.00 79.66  ? 253 GLU B CG  1 
ATOM 4503 C CD  . GLU B 1 253 ? 40.818 -5.271  36.884  1.00 88.51  ? 253 GLU B CD  1 
ATOM 4504 O OE1 . GLU B 1 253 ? 40.712 -5.887  37.967  1.00 83.34  ? 253 GLU B OE1 1 
ATOM 4505 O OE2 . GLU B 1 253 ? 41.919 -5.025  36.348  1.00 84.39  ? 253 GLU B OE2 1 
ATOM 4506 N N   . THR B 1 254 ? 34.599 -4.668  36.745  1.00 64.12  ? 254 THR B N   1 
ATOM 4507 C CA  . THR B 1 254 ? 33.391 -4.946  37.518  1.00 61.73  ? 254 THR B CA  1 
ATOM 4508 C C   . THR B 1 254 ? 32.953 -6.398  37.374  1.00 67.16  ? 254 THR B C   1 
ATOM 4509 O O   . THR B 1 254 ? 32.538 -7.024  38.356  1.00 70.33  ? 254 THR B O   1 
ATOM 4510 C CB  . THR B 1 254 ? 32.264 -4.006  37.094  1.00 71.92  ? 254 THR B CB  1 
ATOM 4511 O OG1 . THR B 1 254 ? 32.771 -2.671  36.979  1.00 67.78  ? 254 THR B OG1 1 
ATOM 4512 C CG2 . THR B 1 254 ? 31.136 -4.034  38.119  1.00 56.88  ? 254 THR B CG2 1 
ATOM 4513 N N   . GLN B 1 255 ? 33.014 -6.947  36.156  1.00 65.22  ? 255 GLN B N   1 
ATOM 4514 C CA  . GLN B 1 255 ? 32.616 -8.338  35.960  1.00 63.20  ? 255 GLN B CA  1 
ATOM 4515 C C   . GLN B 1 255 ? 33.506 -9.277  36.763  1.00 65.28  ? 255 GLN B C   1 
ATOM 4516 O O   . GLN B 1 255 ? 33.032 -10.280 37.313  1.00 66.16  ? 255 GLN B O   1 
ATOM 4517 C CB  . GLN B 1 255 ? 32.660 -8.696  34.475  1.00 62.92  ? 255 GLN B CB  1 
ATOM 4518 C CG  . GLN B 1 255 ? 32.160 -10.099 34.160  1.00 59.49  ? 255 GLN B CG  1 
ATOM 4519 C CD  . GLN B 1 255 ? 30.750 -10.346 34.666  1.00 64.17  ? 255 GLN B CD  1 
ATOM 4520 O OE1 . GLN B 1 255 ? 29.773 -9.923  34.048  1.00 52.31  ? 255 GLN B OE1 1 
ATOM 4521 N NE2 . GLN B 1 255 ? 30.638 -11.038 35.796  1.00 62.45  ? 255 GLN B NE2 1 
ATOM 4522 N N   . GLU B 1 256 ? 34.800 -8.965  36.844  1.00 61.48  ? 256 GLU B N   1 
ATOM 4523 C CA  . GLU B 1 256 ? 35.698 -9.734  37.695  1.00 62.30  ? 256 GLU B CA  1 
ATOM 4524 C C   . GLU B 1 256 ? 35.318 -9.598  39.162  1.00 65.91  ? 256 GLU B C   1 
ATOM 4525 O O   . GLU B 1 256 ? 35.548 -10.521 39.952  1.00 67.63  ? 256 GLU B O   1 
ATOM 4526 C CB  . GLU B 1 256 ? 37.142 -9.285  37.469  1.00 70.33  ? 256 GLU B CB  1 
ATOM 4527 C CG  . GLU B 1 256 ? 37.632 -9.470  36.038  1.00 73.70  ? 256 GLU B CG  1 
ATOM 4528 C CD  . GLU B 1 256 ? 37.260 -8.308  35.131  1.00 75.98  ? 256 GLU B CD  1 
ATOM 4529 O OE1 . GLU B 1 256 ? 36.084 -7.884  35.152  1.00 64.58  ? 256 GLU B OE1 1 
ATOM 4530 O OE2 . GLU B 1 256 ? 38.143 -7.819  34.396  1.00 91.84  ? 256 GLU B OE2 1 
ATOM 4531 N N   . LEU B 1 257 ? 34.744 -8.454  39.545  1.00 63.75  ? 257 LEU B N   1 
ATOM 4532 C CA  . LEU B 1 257 ? 34.286 -8.275  40.919  1.00 56.70  ? 257 LEU B CA  1 
ATOM 4533 C C   . LEU B 1 257 ? 33.106 -9.187  41.231  1.00 62.44  ? 257 LEU B C   1 
ATOM 4534 O O   . LEU B 1 257 ? 33.105 -9.885  42.252  1.00 63.68  ? 257 LEU B O   1 
ATOM 4535 C CB  . LEU B 1 257 ? 33.919 -6.811  41.163  1.00 56.50  ? 257 LEU B CB  1 
ATOM 4536 C CG  . LEU B 1 257 ? 33.553 -6.429  42.597  1.00 48.74  ? 257 LEU B CG  1 
ATOM 4537 C CD1 . LEU B 1 257 ? 34.663 -6.825  43.555  1.00 51.85  ? 257 LEU B CD1 1 
ATOM 4538 C CD2 . LEU B 1 257 ? 33.261 -4.940  42.696  1.00 56.55  ? 257 LEU B CD2 1 
ATOM 4539 N N   . TYR B 1 258 ? 32.085 -9.192  40.365  1.00 59.00  ? 258 TYR B N   1 
ATOM 4540 C CA  . TYR B 1 258 ? 30.954 -10.097 40.562  1.00 60.86  ? 258 TYR B CA  1 
ATOM 4541 C C   . TYR B 1 258 ? 31.420 -11.544 40.637  1.00 65.83  ? 258 TYR B C   1 
ATOM 4542 O O   . TYR B 1 258 ? 30.976 -12.306 41.505  1.00 64.23  ? 258 TYR B O   1 
ATOM 4543 C CB  . TYR B 1 258 ? 29.931 -9.951  39.435  1.00 63.74  ? 258 TYR B CB  1 
ATOM 4544 C CG  . TYR B 1 258 ? 29.305 -8.584  39.260  1.00 65.50  ? 258 TYR B CG  1 
ATOM 4545 C CD1 . TYR B 1 258 ? 29.554 -7.548  40.151  1.00 59.47  ? 258 TYR B CD1 1 
ATOM 4546 C CD2 . TYR B 1 258 ? 28.449 -8.338  38.195  1.00 63.97  ? 258 TYR B CD2 1 
ATOM 4547 C CE1 . TYR B 1 258 ? 28.975 -6.304  39.977  1.00 60.67  ? 258 TYR B CE1 1 
ATOM 4548 C CE2 . TYR B 1 258 ? 27.867 -7.105  38.017  1.00 66.15  ? 258 TYR B CE2 1 
ATOM 4549 C CZ  . TYR B 1 258 ? 28.132 -6.090  38.907  1.00 58.54  ? 258 TYR B CZ  1 
ATOM 4550 O OH  . TYR B 1 258 ? 27.549 -4.859  38.722  1.00 55.76  ? 258 TYR B OH  1 
ATOM 4551 N N   . ASP B 1 259 ? 32.311 -11.941 39.726  1.00 65.58  ? 259 ASP B N   1 
ATOM 4552 C CA  . ASP B 1 259 ? 32.811 -13.311 39.717  1.00 64.46  ? 259 ASP B CA  1 
ATOM 4553 C C   . ASP B 1 259 ? 33.572 -13.619 40.999  1.00 59.77  ? 259 ASP B C   1 
ATOM 4554 O O   . ASP B 1 259 ? 33.415 -14.699 41.581  1.00 60.24  ? 259 ASP B O   1 
ATOM 4555 C CB  . ASP B 1 259 ? 33.697 -13.528 38.492  1.00 67.14  ? 259 ASP B CB  1 
ATOM 4556 C CG  . ASP B 1 259 ? 32.922 -13.439 37.189  1.00 74.16  ? 259 ASP B CG  1 
ATOM 4557 O OD1 . ASP B 1 259 ? 31.682 -13.594 37.221  1.00 71.38  ? 259 ASP B OD1 1 
ATOM 4558 O OD2 . ASP B 1 259 ? 33.550 -13.200 36.136  1.00 71.12  ? 259 ASP B OD2 1 
ATOM 4559 N N   . HIS B 1 260 ? 34.403 -12.679 41.452  1.00 60.32  ? 260 HIS B N   1 
ATOM 4560 C CA  . HIS B 1 260 ? 35.102 -12.849 42.721  1.00 58.64  ? 260 HIS B CA  1 
ATOM 4561 C C   . HIS B 1 260 ? 34.117 -12.963 43.879  1.00 64.08  ? 260 HIS B C   1 
ATOM 4562 O O   . HIS B 1 260 ? 34.332 -13.746 44.811  1.00 58.08  ? 260 HIS B O   1 
ATOM 4563 C CB  . HIS B 1 260 ? 36.068 -11.685 42.936  1.00 62.73  ? 260 HIS B CB  1 
ATOM 4564 C CG  . HIS B 1 260 ? 36.720 -11.678 44.282  1.00 69.73  ? 260 HIS B CG  1 
ATOM 4565 N ND1 . HIS B 1 260 ? 37.418 -12.758 44.777  1.00 70.39  ? 260 HIS B ND1 1 
ATOM 4566 C CD2 . HIS B 1 260 ? 36.786 -10.719 45.236  1.00 76.08  ? 260 HIS B CD2 1 
ATOM 4567 C CE1 . HIS B 1 260 ? 37.883 -12.466 45.979  1.00 73.94  ? 260 HIS B CE1 1 
ATOM 4568 N NE2 . HIS B 1 260 ? 37.515 -11.234 46.280  1.00 76.71  ? 260 HIS B NE2 1 
ATOM 4569 N N   . ILE B 1 261 ? 33.025 -12.195 43.831  1.00 69.41  ? 261 ILE B N   1 
ATOM 4570 C CA  . ILE B 1 261 ? 32.025 -12.238 44.896  1.00 60.01  ? 261 ILE B CA  1 
ATOM 4571 C C   . ILE B 1 261 ? 31.329 -13.592 44.915  1.00 61.11  ? 261 ILE B C   1 
ATOM 4572 O O   . ILE B 1 261 ? 31.135 -14.197 45.977  1.00 60.29  ? 261 ILE B O   1 
ATOM 4573 C CB  . ILE B 1 261 ? 31.013 -11.088 44.732  1.00 58.03  ? 261 ILE B CB  1 
ATOM 4574 C CG1 . ILE B 1 261 ? 31.672 -9.740  45.029  1.00 63.47  ? 261 ILE B CG1 1 
ATOM 4575 C CG2 . ILE B 1 261 ? 29.810 -11.300 45.640  1.00 51.84  ? 261 ILE B CG2 1 
ATOM 4576 C CD1 . ILE B 1 261 ? 30.705 -8.572  45.015  1.00 52.16  ? 261 ILE B CD1 1 
ATOM 4577 N N   . HIS B 1 262 ? 30.938 -14.086 43.737  1.00 63.37  ? 262 HIS B N   1 
ATOM 4578 C CA  . HIS B 1 262 ? 30.249 -15.369 43.654  1.00 65.59  ? 262 HIS B CA  1 
ATOM 4579 C C   . HIS B 1 262 ? 31.124 -16.515 44.147  1.00 66.29  ? 262 HIS B C   1 
ATOM 4580 O O   . HIS B 1 262 ? 30.612 -17.491 44.708  1.00 57.33  ? 262 HIS B O   1 
ATOM 4581 C CB  . HIS B 1 262 ? 29.806 -15.634 42.215  1.00 57.82  ? 262 HIS B CB  1 
ATOM 4582 C CG  . HIS B 1 262 ? 28.677 -14.765 41.755  1.00 64.51  ? 262 HIS B CG  1 
ATOM 4583 N ND1 . HIS B 1 262 ? 28.653 -14.173 40.511  1.00 68.78  ? 262 HIS B ND1 1 
ATOM 4584 C CD2 . HIS B 1 262 ? 27.531 -14.389 42.372  1.00 62.45  ? 262 HIS B CD2 1 
ATOM 4585 C CE1 . HIS B 1 262 ? 27.542 -13.470 40.380  1.00 62.03  ? 262 HIS B CE1 1 
ATOM 4586 N NE2 . HIS B 1 262 ? 26.844 -13.584 41.495  1.00 61.43  ? 262 HIS B NE2 1 
ATOM 4587 N N   . SER B 1 263 ? 32.440 -16.416 43.951  1.00 69.38  ? 263 SER B N   1 
ATOM 4588 C CA  . SER B 1 263 ? 33.344 -17.467 44.400  1.00 58.97  ? 263 SER B CA  1 
ATOM 4589 C C   . SER B 1 263 ? 33.479 -17.525 45.916  1.00 55.05  ? 263 SER B C   1 
ATOM 4590 O O   . SER B 1 263 ? 33.827 -18.582 46.451  1.00 72.29  ? 263 SER B O   1 
ATOM 4591 C CB  . SER B 1 263 ? 34.725 -17.272 43.774  1.00 52.73  ? 263 SER B CB  1 
ATOM 4592 O OG  . SER B 1 263 ? 34.691 -16.274 42.770  1.00 61.32  ? 263 SER B OG  1 
ATOM 4593 N N   . LEU B 1 264 ? 33.212 -16.425 46.622  1.00 53.28  ? 264 LEU B N   1 
ATOM 4594 C CA  . LEU B 1 264 ? 33.473 -16.411 48.057  1.00 59.75  ? 264 LEU B CA  1 
ATOM 4595 C C   . LEU B 1 264 ? 32.394 -17.136 48.853  1.00 55.34  ? 264 LEU B C   1 
ATOM 4596 O O   . LEU B 1 264 ? 32.698 -17.725 49.895  1.00 56.21  ? 264 LEU B O   1 
ATOM 4597 C CB  . LEU B 1 264 ? 33.636 -14.971 48.549  1.00 57.96  ? 264 LEU B CB  1 
ATOM 4598 C CG  . LEU B 1 264 ? 34.814 -14.206 47.933  1.00 61.86  ? 264 LEU B CG  1 
ATOM 4599 C CD1 . LEU B 1 264 ? 35.196 -12.996 48.774  1.00 63.13  ? 264 LEU B CD1 1 
ATOM 4600 C CD2 . LEU B 1 264 ? 36.019 -15.116 47.732  1.00 60.64  ? 264 LEU B CD2 1 
ATOM 4601 N N   . GLN B 1 265 ? 31.143 -17.109 48.395  1.00 58.44  ? 265 GLN B N   1 
ATOM 4602 C CA  . GLN B 1 265 ? 30.073 -17.890 49.006  1.00 59.20  ? 265 GLN B CA  1 
ATOM 4603 C C   . GLN B 1 265 ? 29.079 -18.269 47.922  1.00 62.03  ? 265 GLN B C   1 
ATOM 4604 O O   . GLN B 1 265 ? 28.860 -17.495 46.982  1.00 57.44  ? 265 GLN B O   1 
ATOM 4605 C CB  . GLN B 1 265 ? 29.339 -17.138 50.131  1.00 59.53  ? 265 GLN B CB  1 
ATOM 4606 C CG  . GLN B 1 265 ? 30.183 -16.330 51.104  1.00 53.52  ? 265 GLN B CG  1 
ATOM 4607 C CD  . GLN B 1 265 ? 29.331 -15.513 52.059  1.00 55.26  ? 265 GLN B CD  1 
ATOM 4608 O OE1 . GLN B 1 265 ? 28.134 -15.763 52.208  1.00 57.44  ? 265 GLN B OE1 1 
ATOM 4609 N NE2 . GLN B 1 265 ? 29.942 -14.529 52.707  1.00 51.83  ? 265 GLN B NE2 1 
ATOM 4610 N N   . PRO B 1 266 ? 28.462 -19.452 48.020  1.00 68.48  ? 266 PRO B N   1 
ATOM 4611 C CA  . PRO B 1 266 ? 27.552 -19.903 46.951  1.00 67.72  ? 266 PRO B CA  1 
ATOM 4612 C C   . PRO B 1 266 ? 26.321 -19.032 46.754  1.00 71.86  ? 266 PRO B C   1 
ATOM 4613 O O   . PRO B 1 266 ? 25.847 -18.899 45.620  1.00 70.88  ? 266 PRO B O   1 
ATOM 4614 C CB  . PRO B 1 266 ? 27.168 -21.323 47.393  1.00 64.67  ? 266 PRO B CB  1 
ATOM 4615 C CG  . PRO B 1 266 ? 27.430 -21.360 48.857  1.00 53.84  ? 266 PRO B CG  1 
ATOM 4616 C CD  . PRO B 1 266 ? 28.580 -20.440 49.107  1.00 58.91  ? 266 PRO B CD  1 
ATOM 4617 N N   . GLN B 1 267 ? 25.739 -18.494 47.823  1.00 70.93  ? 267 GLN B N   1 
ATOM 4618 C CA  . GLN B 1 267 ? 24.409 -17.904 47.739  1.00 66.65  ? 267 GLN B CA  1 
ATOM 4619 C C   . GLN B 1 267 ? 24.397 -16.378 47.716  1.00 61.36  ? 267 GLN B C   1 
ATOM 4620 O O   . GLN B 1 267 ? 23.319 -15.792 47.573  1.00 62.79  ? 267 GLN B O   1 
ATOM 4621 C CB  . GLN B 1 267 ? 23.546 -18.408 48.901  1.00 59.89  ? 267 GLN B CB  1 
ATOM 4622 C CG  . GLN B 1 267 ? 23.590 -17.536 50.143  1.00 65.03  ? 267 GLN B CG  1 
ATOM 4623 C CD  . GLN B 1 267 ? 24.952 -17.524 50.810  1.00 64.74  ? 267 GLN B CD  1 
ATOM 4624 O OE1 . GLN B 1 267 ? 25.846 -18.290 50.447  1.00 65.57  ? 267 GLN B OE1 1 
ATOM 4625 N NE2 . GLN B 1 267 ? 25.117 -16.644 51.791  1.00 64.21  ? 267 GLN B NE2 1 
ATOM 4626 N N   . VAL B 1 268 ? 25.546 -15.711 47.842  1.00 63.69  ? 268 VAL B N   1 
ATOM 4627 C CA  . VAL B 1 268 ? 25.527 -14.253 47.866  1.00 62.59  ? 268 VAL B CA  1 
ATOM 4628 C C   . VAL B 1 268 ? 25.105 -13.721 46.507  1.00 59.02  ? 268 VAL B C   1 
ATOM 4629 O O   . VAL B 1 268 ? 25.525 -14.227 45.457  1.00 63.21  ? 268 VAL B O   1 
ATOM 4630 C CB  . VAL B 1 268 ? 26.889 -13.669 48.271  1.00 60.21  ? 268 VAL B CB  1 
ATOM 4631 C CG1 . VAL B 1 268 ? 26.714 -12.240 48.762  1.00 55.17  ? 268 VAL B CG1 1 
ATOM 4632 C CG2 . VAL B 1 268 ? 27.490 -14.487 49.353  1.00 65.94  ? 268 VAL B CG2 1 
ATOM 4633 N N   . LEU B 1 269 ? 24.272 -12.692 46.526  1.00 58.36  ? 269 LEU B N   1 
ATOM 4634 C CA  . LEU B 1 269 ? 23.884 -11.971 45.328  1.00 55.35  ? 269 LEU B CA  1 
ATOM 4635 C C   . LEU B 1 269 ? 24.745 -10.724 45.184  1.00 49.21  ? 269 LEU B C   1 
ATOM 4636 O O   . LEU B 1 269 ? 25.423 -10.297 46.121  1.00 45.73  ? 269 LEU B O   1 
ATOM 4637 C CB  . LEU B 1 269 ? 22.401 -11.598 45.385  1.00 51.05  ? 269 LEU B CB  1 
ATOM 4638 C CG  . LEU B 1 269 ? 21.482 -12.777 45.717  1.00 53.08  ? 269 LEU B CG  1 
ATOM 4639 C CD1 . LEU B 1 269 ? 20.019 -12.364 45.688  1.00 60.46  ? 269 LEU B CD1 1 
ATOM 4640 C CD2 . LEU B 1 269 ? 21.734 -13.940 44.767  1.00 52.94  ? 269 LEU B CD2 1 
ATOM 4641 N N   . VAL B 1 270 ? 24.730 -10.152 43.985  1.00 53.67  ? 270 VAL B N   1 
ATOM 4642 C CA  . VAL B 1 270 ? 25.351 -8.855  43.747  1.00 50.06  ? 270 VAL B CA  1 
ATOM 4643 C C   . VAL B 1 270 ? 24.410 -8.019  42.893  1.00 52.99  ? 270 VAL B C   1 
ATOM 4644 O O   . VAL B 1 270 ? 23.938 -8.469  41.843  1.00 53.16  ? 270 VAL B O   1 
ATOM 4645 C CB  . VAL B 1 270 ? 26.744 -8.981  43.093  1.00 54.00  ? 270 VAL B CB  1 
ATOM 4646 C CG1 . VAL B 1 270 ? 26.675 -9.729  41.765  1.00 62.51  ? 270 VAL B CG1 1 
ATOM 4647 C CG2 . VAL B 1 270 ? 27.369 -7.603  42.917  1.00 56.49  ? 270 VAL B CG2 1 
ATOM 4648 N N   . SER B 1 271 ? 24.112 -6.814  43.362  1.00 54.54  ? 271 SER B N   1 
ATOM 4649 C CA  . SER B 1 271 ? 23.328 -5.846  42.618  1.00 47.44  ? 271 SER B CA  1 
ATOM 4650 C C   . SER B 1 271 ? 24.127 -4.561  42.477  1.00 47.97  ? 271 SER B C   1 
ATOM 4651 O O   . SER B 1 271 ? 25.063 -4.298  43.237  1.00 52.09  ? 271 SER B O   1 
ATOM 4652 C CB  . SER B 1 271 ? 21.991 -5.556  43.300  1.00 44.22  ? 271 SER B CB  1 
ATOM 4653 O OG  . SER B 1 271 ? 22.191 -4.963  44.570  1.00 53.91  ? 271 SER B OG  1 
ATOM 4654 N N   . TYR B 1 272 ? 23.740 -3.755  41.491  1.00 47.70  ? 272 TYR B N   1 
ATOM 4655 C CA  . TYR B 1 272 ? 24.422 -2.505  41.216  1.00 48.76  ? 272 TYR B CA  1 
ATOM 4656 C C   . TYR B 1 272 ? 23.376 -1.511  40.708  1.00 50.16  ? 272 TYR B C   1 
ATOM 4657 O O   . TYR B 1 272 ? 23.401 -1.064  39.561  1.00 55.80  ? 272 TYR B O   1 
ATOM 4658 C CB  . TYR B 1 272 ? 25.560 -2.699  40.212  1.00 51.47  ? 272 TYR B CB  1 
ATOM 4659 C CG  . TYR B 1 272 ? 26.642 -1.651  40.302  1.00 55.46  ? 272 TYR B CG  1 
ATOM 4660 C CD1 . TYR B 1 272 ? 26.348 -0.354  40.701  1.00 47.64  ? 272 TYR B CD1 1 
ATOM 4661 C CD2 . TYR B 1 272 ? 27.958 -1.958  39.989  1.00 52.99  ? 272 TYR B CD2 1 
ATOM 4662 C CE1 . TYR B 1 272 ? 27.331 0.607   40.784  1.00 57.57  ? 272 TYR B CE1 1 
ATOM 4663 C CE2 . TYR B 1 272 ? 28.948 -1.004  40.068  1.00 49.61  ? 272 TYR B CE2 1 
ATOM 4664 C CZ  . TYR B 1 272 ? 28.630 0.278   40.467  1.00 56.44  ? 272 TYR B CZ  1 
ATOM 4665 O OH  . TYR B 1 272 ? 29.612 1.238   40.551  1.00 56.48  ? 272 TYR B OH  1 
ATOM 4666 N N   . LYS B 1 273 ? 22.452 -1.156  41.599  1.00 50.89  ? 273 LYS B N   1 
ATOM 4667 C CA  . LYS B 1 273 ? 21.339 -0.243  41.305  1.00 63.46  ? 273 LYS B CA  1 
ATOM 4668 C C   . LYS B 1 273 ? 20.557 -0.824  40.129  1.00 59.55  ? 273 LYS B C   1 
ATOM 4669 O O   . LYS B 1 273 ? 20.195 -2.011  40.170  1.00 56.18  ? 273 LYS B O   1 
ATOM 4670 C CB  . LYS B 1 273 ? 21.885 1.164   41.101  1.00 59.45  ? 273 LYS B CB  1 
ATOM 4671 C CG  . LYS B 1 273 ? 22.683 1.690   42.274  1.00 51.98  ? 273 LYS B CG  1 
ATOM 4672 C CD  . LYS B 1 273 ? 21.763 2.054   43.420  1.00 42.03  ? 273 LYS B CD  1 
ATOM 4673 C CE  . LYS B 1 273 ? 21.054 3.366   43.154  1.00 51.15  ? 273 LYS B CE  1 
ATOM 4674 N NZ  . LYS B 1 273 ? 21.340 4.369   44.213  1.00 53.59  ? 273 LYS B NZ  1 
ATOM 4675 N N   . GLN B 1 274 ? 20.288 -0.057  39.077  1.00 65.45  ? 274 GLN B N   1 
ATOM 4676 C CA  . GLN B 1 274 ? 19.547 -0.552  37.926  1.00 64.58  ? 274 GLN B CA  1 
ATOM 4677 C C   . GLN B 1 274 ? 20.396 -1.440  37.033  1.00 54.92  ? 274 GLN B C   1 
ATOM 4678 O O   . GLN B 1 274 ? 19.886 -1.968  36.039  1.00 51.99  ? 274 GLN B O   1 
ATOM 4679 C CB  . GLN B 1 274 ? 19.005 0.623   37.109  1.00 61.97  ? 274 GLN B CB  1 
ATOM 4680 C CG  . GLN B 1 274 ? 20.092 1.437   36.421  1.00 62.63  ? 274 GLN B CG  1 
ATOM 4681 C CD  . GLN B 1 274 ? 20.554 2.618   37.253  1.00 68.55  ? 274 GLN B CD  1 
ATOM 4682 O OE1 . GLN B 1 274 ? 20.489 2.588   38.483  1.00 66.64  ? 274 GLN B OE1 1 
ATOM 4683 N NE2 . GLN B 1 274 ? 21.028 3.665   36.586  1.00 61.88  ? 274 GLN B NE2 1 
ATOM 4684 N N   . GLY B 1 275 ? 21.674 -1.601  37.356  1.00 55.24  ? 275 GLY B N   1 
ATOM 4685 C CA  . GLY B 1 275 ? 22.562 -2.438  36.582  1.00 48.88  ? 275 GLY B CA  1 
ATOM 4686 C C   . GLY B 1 275 ? 23.642 -1.591  35.951  1.00 57.32  ? 275 GLY B C   1 
ATOM 4687 O O   . GLY B 1 275 ? 23.361 -0.494  35.460  1.00 72.57  ? 275 GLY B O   1 
ATOM 4688 N N   . LEU B 1 276 ? 24.880 -2.072  35.967  1.00 59.79  ? 276 LEU B N   1 
ATOM 4689 C CA  . LEU B 1 276 ? 25.974 -1.390  35.292  1.00 60.50  ? 276 LEU B CA  1 
ATOM 4690 C C   . LEU B 1 276 ? 26.425 -2.136  34.048  1.00 67.85  ? 276 LEU B C   1 
ATOM 4691 O O   . LEU B 1 276 ? 26.612 -1.528  32.990  1.00 80.04  ? 276 LEU B O   1 
ATOM 4692 C CB  . LEU B 1 276 ? 27.167 -1.206  36.241  1.00 57.81  ? 276 LEU B CB  1 
ATOM 4693 C CG  . LEU B 1 276 ? 28.387 -0.562  35.576  1.00 58.58  ? 276 LEU B CG  1 
ATOM 4694 C CD1 . LEU B 1 276 ? 28.027 0.804   35.001  1.00 53.14  ? 276 LEU B CD1 1 
ATOM 4695 C CD2 . LEU B 1 276 ? 29.554 -0.452  36.543  1.00 56.77  ? 276 LEU B CD2 1 
ATOM 4696 N N   . ILE B 1 277 ? 26.590 -3.453  34.150  1.00 67.07  ? 277 ILE B N   1 
ATOM 4697 C CA  . ILE B 1 277 ? 27.036 -4.279  33.041  1.00 67.51  ? 277 ILE B CA  1 
ATOM 4698 C C   . ILE B 1 277 ? 25.998 -5.326  32.659  1.00 68.29  ? 277 ILE B C   1 
ATOM 4699 O O   . ILE B 1 277 ? 26.262 -6.174  31.807  1.00 80.79  ? 277 ILE B O   1 
ATOM 4700 C CB  . ILE B 1 277 ? 28.396 -4.934  33.353  1.00 65.68  ? 277 ILE B CB  1 
ATOM 4701 C CG1 . ILE B 1 277 ? 28.256 -5.954  34.483  1.00 62.92  ? 277 ILE B CG1 1 
ATOM 4702 C CG2 . ILE B 1 277 ? 29.419 -3.868  33.729  1.00 59.55  ? 277 ILE B CG2 1 
ATOM 4703 C CD1 . ILE B 1 277 ? 29.578 -6.344  35.113  1.00 65.30  ? 277 ILE B CD1 1 
ATOM 4704 N N   . GLY B 1 278 ? 24.814 -5.280  33.274  1.00 65.48  ? 278 GLY B N   1 
ATOM 4705 C CA  . GLY B 1 278 ? 23.696 -6.111  32.880  1.00 59.12  ? 278 GLY B CA  1 
ATOM 4706 C C   . GLY B 1 278 ? 23.689 -7.520  33.431  1.00 63.48  ? 278 GLY B C   1 
ATOM 4707 O O   . GLY B 1 278 ? 22.705 -8.240  33.221  1.00 70.01  ? 278 GLY B O   1 
ATOM 4708 N N   . THR B 1 279 ? 24.741 -7.942  34.133  1.00 58.77  ? 279 THR B N   1 
ATOM 4709 C CA  . THR B 1 279 ? 24.864 -9.318  34.599  1.00 59.06  ? 279 THR B CA  1 
ATOM 4710 C C   . THR B 1 279 ? 24.682 -9.443  36.109  1.00 68.82  ? 279 THR B C   1 
ATOM 4711 O O   . THR B 1 279 ? 25.132 -10.427 36.704  1.00 70.06  ? 279 THR B O   1 
ATOM 4712 C CB  . THR B 1 279 ? 26.213 -9.904  34.180  1.00 65.60  ? 279 THR B CB  1 
ATOM 4713 O OG1 . THR B 1 279 ? 27.123 -9.858  35.286  1.00 72.12  ? 279 THR B OG1 1 
ATOM 4714 C CG2 . THR B 1 279 ? 26.797 -9.121  33.013  1.00 59.88  ? 279 THR B CG2 1 
ATOM 4715 N N   . GLU B 1 280 ? 24.030 -8.469  36.738  1.00 65.14  ? 280 GLU B N   1 
ATOM 4716 C CA  . GLU B 1 280 ? 23.800 -8.517  38.173  1.00 62.83  ? 280 GLU B CA  1 
ATOM 4717 C C   . GLU B 1 280 ? 22.665 -9.484  38.497  1.00 59.67  ? 280 GLU B C   1 
ATOM 4718 O O   . GLU B 1 280 ? 21.853 -9.842  37.639  1.00 58.39  ? 280 GLU B O   1 
ATOM 4719 C CB  . GLU B 1 280 ? 23.477 -7.123  38.716  1.00 62.31  ? 280 GLU B CB  1 
ATOM 4720 C CG  . GLU B 1 280 ? 24.587 -6.097  38.525  1.00 63.13  ? 280 GLU B CG  1 
ATOM 4721 C CD  . GLU B 1 280 ? 24.644 -5.534  37.115  1.00 67.95  ? 280 GLU B CD  1 
ATOM 4722 O OE1 . GLU B 1 280 ? 23.827 -5.956  36.269  1.00 62.41  ? 280 GLU B OE1 1 
ATOM 4723 O OE2 . GLU B 1 280 ? 25.511 -4.672  36.852  1.00 65.57  ? 280 GLU B OE2 1 
ATOM 4724 N N   . ASP B 1 281 ? 22.610 -9.904  39.763  1.00 56.85  ? 281 ASP B N   1 
ATOM 4725 C CA  . ASP B 1 281 ? 21.592 -10.869 40.167  1.00 59.65  ? 281 ASP B CA  1 
ATOM 4726 C C   . ASP B 1 281 ? 20.233 -10.219 40.386  1.00 61.05  ? 281 ASP B C   1 
ATOM 4727 O O   . ASP B 1 281 ? 19.204 -10.889 40.236  1.00 64.60  ? 281 ASP B O   1 
ATOM 4728 C CB  . ASP B 1 281 ? 22.040 -11.612 41.425  1.00 49.74  ? 281 ASP B CB  1 
ATOM 4729 C CG  . ASP B 1 281 ? 23.390 -12.274 41.251  1.00 61.93  ? 281 ASP B CG  1 
ATOM 4730 O OD1 . ASP B 1 281 ? 23.844 -12.396 40.094  1.00 69.24  ? 281 ASP B OD1 1 
ATOM 4731 O OD2 . ASP B 1 281 ? 23.994 -12.680 42.265  1.00 62.12  ? 281 ASP B OD2 1 
ATOM 4732 N N   . PHE B 1 282 ? 20.196 -8.937  40.737  1.00 54.52  ? 282 PHE B N   1 
ATOM 4733 C CA  . PHE B 1 282 ? 18.944 -8.197  40.704  1.00 60.82  ? 282 PHE B CA  1 
ATOM 4734 C C   . PHE B 1 282 ? 19.245 -6.728  40.454  1.00 60.72  ? 282 PHE B C   1 
ATOM 4735 O O   . PHE B 1 282 ? 20.395 -6.285  40.509  1.00 55.67  ? 282 PHE B O   1 
ATOM 4736 C CB  . PHE B 1 282 ? 18.117 -8.395  41.985  1.00 54.50  ? 282 PHE B CB  1 
ATOM 4737 C CG  . PHE B 1 282 ? 18.765 -7.872  43.238  1.00 50.93  ? 282 PHE B CG  1 
ATOM 4738 C CD1 . PHE B 1 282 ? 19.689 -8.637  43.931  1.00 53.90  ? 282 PHE B CD1 1 
ATOM 4739 C CD2 . PHE B 1 282 ? 18.418 -6.629  43.745  1.00 58.58  ? 282 PHE B CD2 1 
ATOM 4740 C CE1 . PHE B 1 282 ? 20.270 -8.164  45.096  1.00 58.38  ? 282 PHE B CE1 1 
ATOM 4741 C CE2 . PHE B 1 282 ? 18.992 -6.151  44.912  1.00 56.73  ? 282 PHE B CE2 1 
ATOM 4742 C CZ  . PHE B 1 282 ? 19.918 -6.921  45.588  1.00 53.58  ? 282 PHE B CZ  1 
ATOM 4743 N N   . LYS B 1 283 ? 18.188 -5.977  40.166  1.00 55.29  ? 283 LYS B N   1 
ATOM 4744 C CA  . LYS B 1 283 ? 18.281 -4.557  39.865  1.00 56.15  ? 283 LYS B CA  1 
ATOM 4745 C C   . LYS B 1 283 ? 17.620 -3.768  40.983  1.00 62.59  ? 283 LYS B C   1 
ATOM 4746 O O   . LYS B 1 283 ? 16.485 -4.065  41.372  1.00 57.00  ? 283 LYS B O   1 
ATOM 4747 C CB  . LYS B 1 283 ? 17.623 -4.239  38.521  1.00 52.01  ? 283 LYS B CB  1 
ATOM 4748 C CG  . LYS B 1 283 ? 18.321 -4.886  37.341  1.00 59.17  ? 283 LYS B CG  1 
ATOM 4749 C CD  . LYS B 1 283 ? 17.813 -4.335  36.026  1.00 58.35  ? 283 LYS B CD  1 
ATOM 4750 C CE  . LYS B 1 283 ? 18.650 -4.838  34.867  1.00 54.41  ? 283 LYS B CE  1 
ATOM 4751 N NZ  . LYS B 1 283 ? 18.455 -3.986  33.666  1.00 72.37  ? 283 LYS B NZ  1 
ATOM 4752 N N   . ALA B 1 284 ? 18.333 -2.768  41.502  1.00 62.41  ? 284 ALA B N   1 
ATOM 4753 C CA  . ALA B 1 284 ? 17.862 -1.949  42.616  1.00 63.81  ? 284 ALA B CA  1 
ATOM 4754 C C   . ALA B 1 284 ? 17.762 -0.487  42.191  1.00 61.22  ? 284 ALA B C   1 
ATOM 4755 O O   . ALA B 1 284 ? 18.561 0.352   42.631  1.00 61.65  ? 284 ALA B O   1 
ATOM 4756 C CB  . ALA B 1 284 ? 18.781 -2.099  43.826  1.00 53.53  ? 284 ALA B CB  1 
ATOM 4757 N N   . PRO B 1 285 ? 16.788 -0.142  41.352  1.00 61.85  ? 285 PRO B N   1 
ATOM 4758 C CA  . PRO B 1 285 ? 16.587 1.269   41.015  1.00 65.16  ? 285 PRO B CA  1 
ATOM 4759 C C   . PRO B 1 285 ? 16.064 2.036   42.217  1.00 68.50  ? 285 PRO B C   1 
ATOM 4760 O O   . PRO B 1 285 ? 15.437 1.474   43.118  1.00 64.69  ? 285 PRO B O   1 
ATOM 4761 C CB  . PRO B 1 285 ? 15.548 1.226   39.890  1.00 73.00  ? 285 PRO B CB  1 
ATOM 4762 C CG  . PRO B 1 285 ? 14.804 -0.038  40.127  1.00 72.19  ? 285 PRO B CG  1 
ATOM 4763 C CD  . PRO B 1 285 ? 15.794 -1.010  40.696  1.00 62.15  ? 285 PRO B CD  1 
ATOM 4764 N N   . GLU B 1 286 ? 16.339 3.337   42.229  1.00 73.18  ? 286 GLU B N   1 
ATOM 4765 C CA  . GLU B 1 286 ? 15.780 4.203   43.257  1.00 68.64  ? 286 GLU B CA  1 
ATOM 4766 C C   . GLU B 1 286 ? 14.336 4.536   42.906  1.00 69.66  ? 286 GLU B C   1 
ATOM 4767 O O   . GLU B 1 286 ? 14.063 5.089   41.835  1.00 68.28  ? 286 GLU B O   1 
ATOM 4768 C CB  . GLU B 1 286 ? 16.607 5.478   43.408  1.00 70.35  ? 286 GLU B CB  1 
ATOM 4769 C CG  . GLU B 1 286 ? 18.050 5.359   42.953  1.00 75.80  ? 286 GLU B CG  1 
ATOM 4770 C CD  . GLU B 1 286 ? 18.906 6.516   43.435  1.00 68.08  ? 286 GLU B CD  1 
ATOM 4771 O OE1 . GLU B 1 286 ? 18.427 7.296   44.286  1.00 66.65  ? 286 GLU B OE1 1 
ATOM 4772 O OE2 . GLU B 1 286 ? 20.056 6.646   42.965  1.00 53.21  ? 286 GLU B OE2 1 
ATOM 4773 N N   . ARG B 1 287 ? 13.416 4.165   43.799  1.00 73.32  ? 287 ARG B N   1 
ATOM 4774 C CA  . ARG B 1 287 ? 12.024 4.603   43.766  1.00 79.69  ? 287 ARG B CA  1 
ATOM 4775 C C   . ARG B 1 287 ? 11.207 3.976   42.637  1.00 80.82  ? 287 ARG B C   1 
ATOM 4776 O O   . ARG B 1 287 ? 10.126 3.435   42.896  1.00 69.70  ? 287 ARG B O   1 
ATOM 4777 C CB  . ARG B 1 287 ? 11.971 6.133   43.710  1.00 74.67  ? 287 ARG B CB  1 
ATOM 4778 C CG  . ARG B 1 287 ? 12.665 6.759   44.914  1.00 70.05  ? 287 ARG B CG  1 
ATOM 4779 C CD  . ARG B 1 287 ? 12.876 8.253   44.789  1.00 66.52  ? 287 ARG B CD  1 
ATOM 4780 N NE  . ARG B 1 287 ? 13.345 8.817   46.050  1.00 70.92  ? 287 ARG B NE  1 
ATOM 4781 C CZ  . ARG B 1 287 ? 14.610 9.108   46.319  1.00 62.35  ? 287 ARG B CZ  1 
ATOM 4782 N NH1 . ARG B 1 287 ? 15.568 8.917   45.427  1.00 67.01  ? 287 ARG B NH1 1 
ATOM 4783 N NH2 . ARG B 1 287 ? 14.923 9.602   47.514  1.00 62.83  ? 287 ARG B NH2 1 
ATOM 4784 N N   . HIS B 1 288 ? 11.687 4.027   41.394  1.00 82.83  ? 288 HIS B N   1 
ATOM 4785 C CA  . HIS B 1 288 ? 10.872 3.547   40.285  1.00 81.98  ? 288 HIS B CA  1 
ATOM 4786 C C   . HIS B 1 288 ? 11.751 3.017   39.160  1.00 90.31  ? 288 HIS B C   1 
ATOM 4787 O O   . HIS B 1 288 ? 12.930 3.362   39.045  1.00 93.80  ? 288 HIS B O   1 
ATOM 4788 C CB  . HIS B 1 288 ? 9.955  4.655   39.753  1.00 85.69  ? 288 HIS B CB  1 
ATOM 4789 C CG  . HIS B 1 288 ? 10.631 5.589   38.798  1.00 91.47  ? 288 HIS B CG  1 
ATOM 4790 N ND1 . HIS B 1 288 ? 11.243 6.755   39.207  1.00 93.26  ? 288 HIS B ND1 1 
ATOM 4791 C CD2 . HIS B 1 288 ? 10.790 5.532   37.454  1.00 96.84  ? 288 HIS B CD2 1 
ATOM 4792 C CE1 . HIS B 1 288 ? 11.752 7.374   38.157  1.00 96.09  ? 288 HIS B CE1 1 
ATOM 4793 N NE2 . HIS B 1 288 ? 11.492 6.652   37.082  1.00 99.12  ? 288 HIS B NE2 1 
ATOM 4794 N N   . PHE B 1 289 ? 11.149 2.165   38.328  1.00 94.69  ? 289 PHE B N   1 
ATOM 4795 C CA  . PHE B 1 289 ? 11.806 1.613   37.149  1.00 99.66  ? 289 PHE B CA  1 
ATOM 4796 C C   . PHE B 1 289 ? 10.785 1.461   36.030  1.00 103.41 ? 289 PHE B C   1 
ATOM 4797 O O   . PHE B 1 289 ? 9.736  0.841   36.227  1.00 96.20  ? 289 PHE B O   1 
ATOM 4798 C CB  . PHE B 1 289 ? 12.457 0.260   37.458  1.00 88.77  ? 289 PHE B CB  1 
ATOM 4799 C CG  . PHE B 1 289 ? 13.206 -0.334  36.297  1.00 92.05  ? 289 PHE B CG  1 
ATOM 4800 C CD1 . PHE B 1 289 ? 14.367 0.257   35.826  1.00 94.02  ? 289 PHE B CD1 1 
ATOM 4801 C CD2 . PHE B 1 289 ? 12.750 -1.488  35.679  1.00 94.37  ? 289 PHE B CD2 1 
ATOM 4802 C CE1 . PHE B 1 289 ? 15.059 -0.289  34.759  1.00 96.22  ? 289 PHE B CE1 1 
ATOM 4803 C CE2 . PHE B 1 289 ? 13.437 -2.039  34.612  1.00 98.34  ? 289 PHE B CE2 1 
ATOM 4804 C CZ  . PHE B 1 289 ? 14.593 -1.438  34.152  1.00 95.51  ? 289 PHE B CZ  1 
ATOM 4805 N N   . LYS B 1 290 ? 11.099 2.016   34.863  1.00 104.49 ? 290 LYS B N   1 
ATOM 4806 C CA  . LYS B 1 290 ? 10.241 1.920   33.690  1.00 108.56 ? 290 LYS B CA  1 
ATOM 4807 C C   . LYS B 1 290 ? 10.773 0.843   32.752  1.00 109.72 ? 290 LYS B C   1 
ATOM 4808 O O   . LYS B 1 290 ? 11.983 0.747   32.523  1.00 105.52 ? 290 LYS B O   1 
ATOM 4809 C CB  . LYS B 1 290 ? 10.144 3.261   32.961  1.00 102.20 ? 290 LYS B CB  1 
ATOM 4810 C CG  . LYS B 1 290 ? 9.795  4.432   33.865  1.00 101.56 ? 290 LYS B CG  1 
ATOM 4811 C CD  . LYS B 1 290 ? 10.682 5.629   33.576  1.00 91.70  ? 290 LYS B CD  1 
ATOM 4812 C CE  . LYS B 1 290 ? 10.048 6.920   34.061  1.00 96.73  ? 290 LYS B CE  1 
ATOM 4813 N NZ  . LYS B 1 290 ? 11.075 7.912   34.481  1.00 110.28 ? 290 LYS B NZ  1 
ATOM 4814 N N   . GLY B 1 291 ? 9.865  0.045   32.205  1.00 111.00 ? 291 GLY B N   1 
ATOM 4815 C CA  . GLY B 1 291 ? 10.247 -1.156  31.492  1.00 107.69 ? 291 GLY B CA  1 
ATOM 4816 C C   . GLY B 1 291 ? 10.252 -2.370  32.399  1.00 111.55 ? 291 GLY B C   1 
ATOM 4817 O O   . GLY B 1 291 ? 9.811  -2.335  33.551  1.00 108.63 ? 291 GLY B O   1 
ATOM 4818 N N   . THR B 1 292 ? 10.768 -3.471  31.860  1.00 113.71 ? 292 THR B N   1 
ATOM 4819 C CA  . THR B 1 292 ? 10.840 -4.731  32.583  1.00 113.41 ? 292 THR B CA  1 
ATOM 4820 C C   . THR B 1 292 ? 12.284 -5.220  32.632  1.00 105.03 ? 292 THR B C   1 
ATOM 4821 O O   . THR B 1 292 ? 13.160 -4.725  31.917  1.00 95.42  ? 292 THR B O   1 
ATOM 4822 C CB  . THR B 1 292 ? 9.931  -5.788  31.937  1.00 106.00 ? 292 THR B CB  1 
ATOM 4823 O OG1 . THR B 1 292 ? 8.768  -5.148  31.398  1.00 115.11 ? 292 THR B OG1 1 
ATOM 4824 C CG2 . THR B 1 292 ? 9.482  -6.820  32.967  1.00 88.82  ? 292 THR B CG2 1 
ATOM 4825 N N   . SER B 1 293 ? 12.524 -6.206  33.496  1.00 104.45 ? 293 SER B N   1 
ATOM 4826 C CA  . SER B 1 293 ? 13.867 -6.651  33.831  1.00 92.86  ? 293 SER B CA  1 
ATOM 4827 C C   . SER B 1 293 ? 13.960 -8.169  33.774  1.00 86.43  ? 293 SER B C   1 
ATOM 4828 O O   . SER B 1 293 ? 13.000 -8.883  34.079  1.00 83.61  ? 293 SER B O   1 
ATOM 4829 C CB  . SER B 1 293 ? 14.279 -6.169  35.227  1.00 81.76  ? 293 SER B CB  1 
ATOM 4830 O OG  . SER B 1 293 ? 15.627 -6.503  35.499  1.00 82.74  ? 293 SER B OG  1 
ATOM 4831 N N   . ASP B 1 294 ? 15.139 -8.650  33.369  1.00 83.67  ? 294 ASP B N   1 
ATOM 4832 C CA  . ASP B 1 294 ? 15.420 -10.082 33.384  1.00 74.54  ? 294 ASP B CA  1 
ATOM 4833 C C   . ASP B 1 294 ? 15.353 -10.658 34.791  1.00 75.11  ? 294 ASP B C   1 
ATOM 4834 O O   . ASP B 1 294 ? 15.067 -11.848 34.964  1.00 79.74  ? 294 ASP B O   1 
ATOM 4835 C CB  . ASP B 1 294 ? 16.814 -10.338 32.804  1.00 75.21  ? 294 ASP B CB  1 
ATOM 4836 C CG  . ASP B 1 294 ? 16.778 -10.955 31.424  1.00 83.99  ? 294 ASP B CG  1 
ATOM 4837 O OD1 . ASP B 1 294 ? 15.741 -11.542 31.053  1.00 93.19  ? 294 ASP B OD1 1 
ATOM 4838 O OD2 . ASP B 1 294 ? 17.799 -10.856 30.710  1.00 87.25  ? 294 ASP B OD2 1 
ATOM 4839 N N   . VAL B 1 295 ? 15.597 -9.830  35.802  1.00 79.62  ? 295 VAL B N   1 
ATOM 4840 C CA  . VAL B 1 295 ? 15.948 -10.295 37.142  1.00 70.00  ? 295 VAL B CA  1 
ATOM 4841 C C   . VAL B 1 295 ? 14.970 -9.753  38.183  1.00 65.18  ? 295 VAL B C   1 
ATOM 4842 O O   . VAL B 1 295 ? 14.061 -8.987  37.831  1.00 67.00  ? 295 VAL B O   1 
ATOM 4843 C CB  . VAL B 1 295 ? 17.395 -9.888  37.463  1.00 68.73  ? 295 VAL B CB  1 
ATOM 4844 C CG1 . VAL B 1 295 ? 18.362 -10.590 36.521  1.00 57.40  ? 295 VAL B CG1 1 
ATOM 4845 C CG2 . VAL B 1 295 ? 17.546 -8.383  37.353  1.00 60.57  ? 295 VAL B CG2 1 
ATOM 4846 N N   . PRO B 1 296 ? 15.093 -10.139 39.459  1.00 50.28  ? 296 PRO B N   1 
ATOM 4847 C CA  . PRO B 1 296 ? 14.272 -9.508  40.501  1.00 55.78  ? 296 PRO B CA  1 
ATOM 4848 C C   . PRO B 1 296 ? 14.486 -8.001  40.571  1.00 60.42  ? 296 PRO B C   1 
ATOM 4849 O O   . PRO B 1 296 ? 15.557 -7.484  40.246  1.00 57.75  ? 296 PRO B O   1 
ATOM 4850 C CB  . PRO B 1 296 ? 14.745 -10.194 41.787  1.00 55.30  ? 296 PRO B CB  1 
ATOM 4851 C CG  . PRO B 1 296 ? 15.222 -11.521 41.340  1.00 57.84  ? 296 PRO B CG  1 
ATOM 4852 C CD  . PRO B 1 296 ? 15.791 -11.337 39.967  1.00 48.60  ? 296 PRO B CD  1 
ATOM 4853 N N   . LEU B 1 297 ? 13.440 -7.298  41.001  1.00 61.88  ? 297 LEU B N   1 
ATOM 4854 C CA  . LEU B 1 297 ? 13.450 -5.848  41.152  1.00 64.93  ? 297 LEU B CA  1 
ATOM 4855 C C   . LEU B 1 297 ? 13.337 -5.454  42.620  1.00 61.12  ? 297 LEU B C   1 
ATOM 4856 O O   . LEU B 1 297 ? 12.626 -6.103  43.394  1.00 56.71  ? 297 LEU B O   1 
ATOM 4857 C CB  . LEU B 1 297 ? 12.307 -5.212  40.359  1.00 64.85  ? 297 LEU B CB  1 
ATOM 4858 C CG  . LEU B 1 297 ? 12.581 -4.944  38.880  1.00 61.15  ? 297 LEU B CG  1 
ATOM 4859 C CD1 . LEU B 1 297 ? 11.315 -4.475  38.187  1.00 63.58  ? 297 LEU B CD1 1 
ATOM 4860 C CD2 . LEU B 1 297 ? 13.696 -3.922  38.726  1.00 64.64  ? 297 LEU B CD2 1 
ATOM 4861 N N   . GLU B 1 298 ? 14.040 -4.385  42.998  1.00 67.64  ? 298 GLU B N   1 
ATOM 4862 C CA  . GLU B 1 298 ? 13.930 -3.812  44.336  1.00 64.31  ? 298 GLU B CA  1 
ATOM 4863 C C   . GLU B 1 298 ? 13.944 -2.293  44.242  1.00 61.51  ? 298 GLU B C   1 
ATOM 4864 O O   . GLU B 1 298 ? 14.951 -1.707  43.835  1.00 57.36  ? 298 GLU B O   1 
ATOM 4865 C CB  . GLU B 1 298 ? 15.066 -4.301  45.241  1.00 60.43  ? 298 GLU B CB  1 
ATOM 4866 C CG  . GLU B 1 298 ? 15.093 -3.648  46.613  1.00 58.65  ? 298 GLU B CG  1 
ATOM 4867 C CD  . GLU B 1 298 ? 16.405 -3.875  47.339  1.00 59.60  ? 298 GLU B CD  1 
ATOM 4868 O OE1 . GLU B 1 298 ? 17.442 -3.359  46.868  1.00 59.21  ? 298 GLU B OE1 1 
ATOM 4869 O OE2 . GLU B 1 298 ? 16.397 -4.567  48.380  1.00 48.71  ? 298 GLU B OE2 1 
ATOM 4870 N N   . PHE B 1 299 ? 12.832 -1.660  44.614  1.00 64.60  ? 299 PHE B N   1 
ATOM 4871 C CA  . PHE B 1 299 ? 12.750 -0.207  44.706  1.00 61.84  ? 299 PHE B CA  1 
ATOM 4872 C C   . PHE B 1 299 ? 13.174 0.241   46.098  1.00 58.80  ? 299 PHE B C   1 
ATOM 4873 O O   . PHE B 1 299 ? 12.670 -0.277  47.100  1.00 56.29  ? 299 PHE B O   1 
ATOM 4874 C CB  . PHE B 1 299 ? 11.329 0.292   44.432  1.00 59.94  ? 299 PHE B CB  1 
ATOM 4875 C CG  . PHE B 1 299 ? 10.830 0.011   43.045  1.00 64.88  ? 299 PHE B CG  1 
ATOM 4876 C CD1 . PHE B 1 299 ? 11.707 -0.253  42.006  1.00 74.32  ? 299 PHE B CD1 1 
ATOM 4877 C CD2 . PHE B 1 299 ? 9.471  0.028   42.781  1.00 65.92  ? 299 PHE B CD2 1 
ATOM 4878 C CE1 . PHE B 1 299 ? 11.234 -0.506  40.732  1.00 74.64  ? 299 PHE B CE1 1 
ATOM 4879 C CE2 . PHE B 1 299 ? 8.995  -0.221  41.514  1.00 70.32  ? 299 PHE B CE2 1 
ATOM 4880 C CZ  . PHE B 1 299 ? 9.877  -0.489  40.487  1.00 73.40  ? 299 PHE B CZ  1 
ATOM 4881 N N   . CYS B 1 300 ? 14.099 1.196   46.165  1.00 58.30  ? 300 CYS B N   1 
ATOM 4882 C CA  . CYS B 1 300 ? 14.506 1.795   47.430  1.00 58.12  ? 300 CYS B CA  1 
ATOM 4883 C C   . CYS B 1 300 ? 13.951 3.210   47.535  1.00 61.85  ? 300 CYS B C   1 
ATOM 4884 O O   . CYS B 1 300 ? 14.076 4.003   46.595  1.00 62.81  ? 300 CYS B O   1 
ATOM 4885 C CB  . CYS B 1 300 ? 16.030 1.805   47.576  1.00 53.19  ? 300 CYS B CB  1 
ATOM 4886 S SG  . CYS B 1 300 ? 16.940 2.447   46.156  1.00 63.32  ? 300 CYS B SG  1 
ATOM 4887 N N   . ASP B 1 301 ? 13.337 3.523   48.677  1.00 61.67  ? 301 ASP B N   1 
ATOM 4888 C CA  . ASP B 1 301 ? 12.745 4.833   48.910  1.00 68.46  ? 301 ASP B CA  1 
ATOM 4889 C C   . ASP B 1 301 ? 12.940 5.217   50.371  1.00 65.38  ? 301 ASP B C   1 
ATOM 4890 O O   . ASP B 1 301 ? 13.335 4.397   51.205  1.00 67.49  ? 301 ASP B O   1 
ATOM 4891 C CB  . ASP B 1 301 ? 11.261 4.861   48.521  1.00 80.31  ? 301 ASP B CB  1 
ATOM 4892 C CG  . ASP B 1 301 ? 10.865 6.159   47.841  1.00 80.40  ? 301 ASP B CG  1 
ATOM 4893 O OD1 . ASP B 1 301 ? 11.654 7.126   47.903  1.00 71.24  ? 301 ASP B OD1 1 
ATOM 4894 O OD2 . ASP B 1 301 ? 9.777  6.208   47.230  1.00 84.91  ? 301 ASP B OD2 1 
ATOM 4895 N N   . THR B 1 302 ? 12.690 6.494   50.674  1.00 66.46  ? 302 THR B N   1 
ATOM 4896 C CA  . THR B 1 302 ? 13.010 7.025   52.021  1.00 64.36  ? 302 THR B CA  1 
ATOM 4897 C C   . THR B 1 302 ? 11.783 7.389   52.854  1.00 63.94  ? 302 THR B C   1 
ATOM 4898 O O   . THR B 1 302 ? 10.734 7.672   52.263  1.00 67.75  ? 302 THR B O   1 
ATOM 4899 C CB  . THR B 1 302 ? 13.829 8.307   51.856  1.00 62.10  ? 302 THR B CB  1 
ATOM 4900 O OG1 . THR B 1 302 ? 13.144 9.128   50.912  1.00 67.35  ? 302 THR B OG1 1 
ATOM 4901 C CG2 . THR B 1 302 ? 15.237 8.056   51.374  1.00 62.45  ? 302 THR B CG2 1 
ATOM 4902 N N   . LEU B 1 303 ? 11.933 7.394   54.181  1.00 60.45  ? 303 LEU B N   1 
ATOM 4903 C CA  . LEU B 1 303 ? 10.836 7.835   55.079  1.00 61.19  ? 303 LEU B CA  1 
ATOM 4904 C C   . LEU B 1 303 ? 10.990 9.341   55.236  1.00 66.01  ? 303 LEU B C   1 
ATOM 4905 O O   . LEU B 1 303 ? 10.064 9.984   55.742  1.00 74.55  ? 303 LEU B O   1 
ATOM 4906 C CB  . LEU B 1 303 ? 10.952 7.118   56.425  1.00 64.92  ? 303 LEU B CB  1 
ATOM 4907 C CG  . LEU B 1 303 ? 10.211 5.787   56.521  1.00 66.59  ? 303 LEU B CG  1 
ATOM 4908 C CD1 . LEU B 1 303 ? 10.215 5.265   57.948  1.00 70.31  ? 303 LEU B CD1 1 
ATOM 4909 C CD2 . LEU B 1 303 ? 8.788  5.928   56.009  1.00 64.15  ? 303 LEU B CD2 1 
ATOM 4910 N N   . GLN B 1 304 ? 12.137 9.866   54.824  1.00 64.66  ? 304 GLN B N   1 
ATOM 4911 C CA  . GLN B 1 304 ? 12.339 11.328  54.817  1.00 64.57  ? 304 GLN B CA  1 
ATOM 4912 C C   . GLN B 1 304 ? 12.119 11.784  53.385  1.00 65.77  ? 304 GLN B C   1 
ATOM 4913 O O   . GLN B 1 304 ? 12.376 10.991  52.476  1.00 72.48  ? 304 GLN B O   1 
ATOM 4914 C CB  . GLN B 1 304 ? 13.775 11.674  55.193  1.00 67.76  ? 304 GLN B CB  1 
ATOM 4915 C CG  . GLN B 1 304 ? 14.115 11.421  56.653  1.00 69.76  ? 304 GLN B CG  1 
ATOM 4916 C CD  . GLN B 1 304 ? 15.424 12.067  57.032  1.00 69.99  ? 304 GLN B CD  1 
ATOM 4917 O OE1 . GLN B 1 304 ? 16.042 12.772  56.238  1.00 67.27  ? 304 GLN B OE1 1 
ATOM 4918 N NE2 . GLN B 1 304 ? 15.859 11.829  58.258  1.00 71.76  ? 304 GLN B NE2 1 
ATOM 4919 N N   . PRO B 1 305 ? 11.657 13.016  53.130  1.00 68.11  ? 305 PRO B N   1 
ATOM 4920 C CA  . PRO B 1 305 ? 11.546 13.487  51.757  1.00 69.25  ? 305 PRO B CA  1 
ATOM 4921 C C   . PRO B 1 305 ? 12.896 13.638  51.035  1.00 65.33  ? 305 PRO B C   1 
ATOM 4922 O O   . PRO B 1 305 ? 13.605 14.560  51.361  1.00 63.49  ? 305 PRO B O   1 
ATOM 4923 C CB  . PRO B 1 305 ? 10.863 14.852  51.908  1.00 63.69  ? 305 PRO B CB  1 
ATOM 4924 C CG  . PRO B 1 305 ? 11.105 15.258  53.342  1.00 70.51  ? 305 PRO B CG  1 
ATOM 4925 C CD  . PRO B 1 305 ? 11.180 13.967  54.126  1.00 71.82  ? 305 PRO B CD  1 
ATOM 4926 N N   . TRP B 1 306 ? 13.237 12.710  50.137  1.00 62.07  ? 306 TRP B N   1 
ATOM 4927 C CA  . TRP B 1 306 ? 14.449 12.840  49.275  1.00 65.61  ? 306 TRP B CA  1 
ATOM 4928 C C   . TRP B 1 306 ? 15.766 12.489  49.982  1.00 67.74  ? 306 TRP B C   1 
ATOM 4929 O O   . TRP B 1 306 ? 16.665 11.971  49.303  1.00 59.17  ? 306 TRP B O   1 
ATOM 4930 C CB  . TRP B 1 306 ? 14.507 14.242  48.656  1.00 60.68  ? 306 TRP B CB  1 
ATOM 4931 C CG  . TRP B 1 306 ? 13.368 14.567  47.745  1.00 60.28  ? 306 TRP B CG  1 
ATOM 4932 C CD1 . TRP B 1 306 ? 12.298 15.368  48.017  1.00 62.27  ? 306 TRP B CD1 1 
ATOM 4933 C CD2 . TRP B 1 306 ? 13.191 14.106  46.396  1.00 64.40  ? 306 TRP B CD2 1 
ATOM 4934 N NE1 . TRP B 1 306 ? 11.466 15.433  46.933  1.00 63.04  ? 306 TRP B NE1 1 
ATOM 4935 C CE2 . TRP B 1 306 ? 11.989 14.670  45.924  1.00 59.10  ? 306 TRP B CE2 1 
ATOM 4936 C CE3 . TRP B 1 306 ? 13.926 13.275  45.547  1.00 68.74  ? 306 TRP B CE3 1 
ATOM 4937 C CZ2 . TRP B 1 306 ? 11.508 14.424  44.640  1.00 61.98  ? 306 TRP B CZ2 1 
ATOM 4938 C CZ3 . TRP B 1 306 ? 13.451 13.035  44.278  1.00 65.28  ? 306 TRP B CZ3 1 
ATOM 4939 C CH2 . TRP B 1 306 ? 12.258 13.602  43.833  1.00 63.10  ? 306 TRP B CH2 1 
ATOM 4940 N N   . LYS B 1 307 ? 15.890 12.752  51.281  1.00 72.78  ? 307 LYS B N   1 
ATOM 4941 C CA  . LYS B 1 307 ? 17.205 12.545  51.948  1.00 66.33  ? 307 LYS B CA  1 
ATOM 4942 C C   . LYS B 1 307 ? 17.282 11.153  52.583  1.00 64.11  ? 307 LYS B C   1 
ATOM 4943 O O   . LYS B 1 307 ? 16.322 10.763  53.261  1.00 63.68  ? 307 LYS B O   1 
ATOM 4944 C CB  . LYS B 1 307 ? 17.477 13.680  52.940  1.00 66.70  ? 307 LYS B CB  1 
ATOM 4945 C CG  . LYS B 1 307 ? 18.415 14.771  52.443  1.00 56.70  ? 307 LYS B CG  1 
ATOM 4946 C CD  . LYS B 1 307 ? 18.034 15.310  51.084  1.00 66.21  ? 307 LYS B CD  1 
ATOM 4947 C CE  . LYS B 1 307 ? 19.182 15.294  50.097  1.00 58.50  ? 307 LYS B CE  1 
ATOM 4948 N NZ  . LYS B 1 307 ? 19.449 13.931  49.579  1.00 78.80  ? 307 LYS B NZ  1 
ATOM 4949 N N   . TRP B 1 308 ? 18.404 10.456  52.382  1.00 59.73  ? 308 TRP B N   1 
ATOM 4950 C CA  . TRP B 1 308 ? 18.585 9.076   52.897  1.00 51.90  ? 308 TRP B CA  1 
ATOM 4951 C C   . TRP B 1 308 ? 19.278 9.147   54.250  1.00 55.31  ? 308 TRP B C   1 
ATOM 4952 O O   . TRP B 1 308 ? 18.944 8.340   55.127  1.00 63.30  ? 308 TRP B O   1 
ATOM 4953 C CB  . TRP B 1 308 ? 19.391 8.259   51.887  1.00 53.52  ? 308 TRP B CB  1 
ATOM 4954 C CG  . TRP B 1 308 ? 18.700 8.096   50.571  1.00 55.66  ? 308 TRP B CG  1 
ATOM 4955 C CD1 . TRP B 1 308 ? 18.645 9.001   49.552  1.00 53.80  ? 308 TRP B CD1 1 
ATOM 4956 C CD2 . TRP B 1 308 ? 17.952 6.951   50.131  1.00 60.38  ? 308 TRP B CD2 1 
ATOM 4957 N NE1 . TRP B 1 308 ? 17.914 8.499   48.511  1.00 58.21  ? 308 TRP B NE1 1 
ATOM 4958 C CE2 . TRP B 1 308 ? 17.475 7.244   48.837  1.00 59.82  ? 308 TRP B CE2 1 
ATOM 4959 C CE3 . TRP B 1 308 ? 17.636 5.716   50.704  1.00 57.66  ? 308 TRP B CE3 1 
ATOM 4960 C CZ2 . TRP B 1 308 ? 16.703 6.343   48.109  1.00 56.85  ? 308 TRP B CZ2 1 
ATOM 4961 C CZ3 . TRP B 1 308 ? 16.871 4.827   49.985  1.00 61.83  ? 308 TRP B CZ3 1 
ATOM 4962 C CH2 . TRP B 1 308 ? 16.414 5.139   48.706  1.00 59.76  ? 308 TRP B CH2 1 
ATOM 4963 N N   . GLY B 1 309 ? 20.211 10.080  54.402  1.00 54.56  ? 309 GLY B N   1 
ATOM 4964 C CA  . GLY B 1 309 ? 20.863 10.285  55.703  1.00 58.23  ? 309 GLY B CA  1 
ATOM 4965 C C   . GLY B 1 309 ? 20.051 11.240  56.552  1.00 62.52  ? 309 GLY B C   1 
ATOM 4966 O O   . GLY B 1 309 ? 19.132 11.866  56.011  1.00 53.01  ? 309 GLY B O   1 
ATOM 4967 N N   . TYR B 1 310 ? 20.388 11.369  57.832  1.00 62.67  ? 310 TYR B N   1 
ATOM 4968 C CA  . TYR B 1 310 ? 19.563 12.201  58.741  1.00 63.83  ? 310 TYR B CA  1 
ATOM 4969 C C   . TYR B 1 310 ? 19.584 13.663  58.328  1.00 59.78  ? 310 TYR B C   1 
ATOM 4970 O O   . TYR B 1 310 ? 20.670 14.231  58.231  1.00 63.23  ? 310 TYR B O   1 
ATOM 4971 C CB  . TYR B 1 310 ? 20.062 12.092  60.178  1.00 70.08  ? 310 TYR B CB  1 
ATOM 4972 C CG  . TYR B 1 310 ? 19.345 12.965  61.174  1.00 74.80  ? 310 TYR B CG  1 
ATOM 4973 C CD1 . TYR B 1 310 ? 17.988 13.209  61.069  1.00 76.98  ? 310 TYR B CD1 1 
ATOM 4974 C CD2 . TYR B 1 310 ? 20.025 13.537  62.234  1.00 74.40  ? 310 TYR B CD2 1 
ATOM 4975 C CE1 . TYR B 1 310 ? 17.325 14.007  61.985  1.00 78.95  ? 310 TYR B CE1 1 
ATOM 4976 C CE2 . TYR B 1 310 ? 19.379 14.336  63.160  1.00 77.71  ? 310 TYR B CE2 1 
ATOM 4977 C CZ  . TYR B 1 310 ? 18.023 14.572  63.036  1.00 84.65  ? 310 TYR B CZ  1 
ATOM 4978 O OH  . TYR B 1 310 ? 17.379 15.358  63.946  1.00 86.44  ? 310 TYR B OH  1 
ATOM 4979 N N   . ASP B 1 311 ? 18.417 14.229  58.055  1.00 62.81  ? 311 ASP B N   1 
ATOM 4980 C CA  . ASP B 1 311 ? 18.303 15.659  57.791  1.00 68.17  ? 311 ASP B CA  1 
ATOM 4981 C C   . ASP B 1 311 ? 17.414 16.236  58.886  1.00 68.98  ? 311 ASP B C   1 
ATOM 4982 O O   . ASP B 1 311 ? 16.199 16.013  58.885  1.00 68.63  ? 311 ASP B O   1 
ATOM 4983 C CB  . ASP B 1 311 ? 17.726 15.925  56.399  1.00 62.49  ? 311 ASP B CB  1 
ATOM 4984 C CG  . ASP B 1 311 ? 17.714 17.403  56.035  1.00 70.02  ? 311 ASP B CG  1 
ATOM 4985 O OD1 . ASP B 1 311 ? 17.133 18.211  56.790  1.00 71.91  ? 311 ASP B OD1 1 
ATOM 4986 O OD2 . ASP B 1 311 ? 18.290 17.760  54.985  1.00 69.60  ? 311 ASP B OD2 1 
ATOM 4987 N N   . LYS B 1 312 ? 18.018 16.981  59.817  1.00 70.73  ? 312 LYS B N   1 
ATOM 4988 C CA  . LYS B 1 312 ? 17.253 17.502  60.946  1.00 77.11  ? 312 LYS B CA  1 
ATOM 4989 C C   . LYS B 1 312 ? 16.252 18.552  60.485  1.00 80.09  ? 312 LYS B C   1 
ATOM 4990 O O   . LYS B 1 312 ? 15.137 18.619  61.017  1.00 75.40  ? 312 LYS B O   1 
ATOM 4991 C CB  . LYS B 1 312 ? 18.212 18.064  62.005  1.00 73.00  ? 312 LYS B CB  1 
ATOM 4992 C CG  . LYS B 1 312 ? 17.847 19.417  62.644  1.00 82.05  ? 312 LYS B CG  1 
ATOM 4993 C CD  . LYS B 1 312 ? 16.607 19.388  63.543  1.00 81.79  ? 312 LYS B CD  1 
ATOM 4994 C CE  . LYS B 1 312 ? 16.535 20.639  64.404  1.00 71.37  ? 312 LYS B CE  1 
ATOM 4995 N NZ  . LYS B 1 312 ? 16.631 21.877  63.578  1.00 66.28  ? 312 LYS B NZ  1 
ATOM 4996 N N   . SER B 1 313 ? 16.594 19.321  59.447  1.00 73.05  ? 313 SER B N   1 
ATOM 4997 C CA  . SER B 1 313 ? 15.677 20.328  58.925  1.00 59.31  ? 313 SER B CA  1 
ATOM 4998 C C   . SER B 1 313 ? 14.394 19.715  58.382  1.00 73.50  ? 313 SER B C   1 
ATOM 4999 O O   . SER B 1 313 ? 13.485 20.458  57.997  1.00 77.66  ? 313 SER B O   1 
ATOM 5000 C CB  . SER B 1 313 ? 16.365 21.148  57.834  1.00 63.85  ? 313 SER B CB  1 
ATOM 5001 O OG  . SER B 1 313 ? 16.193 20.546  56.564  1.00 59.71  ? 313 SER B OG  1 
ATOM 5002 N N   . LEU B 1 314 ? 14.302 18.386  58.347  1.00 79.06  ? 314 LEU B N   1 
ATOM 5003 C CA  . LEU B 1 314 ? 13.130 17.668  57.874  1.00 75.01  ? 314 LEU B CA  1 
ATOM 5004 C C   . LEU B 1 314 ? 12.313 17.092  59.023  1.00 78.70  ? 314 LEU B C   1 
ATOM 5005 O O   . LEU B 1 314 ? 11.396 16.301  58.781  1.00 83.39  ? 314 LEU B O   1 
ATOM 5006 C CB  . LEU B 1 314 ? 13.543 16.550  56.916  1.00 75.23  ? 314 LEU B CB  1 
ATOM 5007 C CG  . LEU B 1 314 ? 14.027 16.958  55.524  1.00 70.70  ? 314 LEU B CG  1 
ATOM 5008 C CD1 . LEU B 1 314 ? 14.435 15.729  54.727  1.00 72.15  ? 314 LEU B CD1 1 
ATOM 5009 C CD2 . LEU B 1 314 ? 12.956 17.746  54.789  1.00 64.06  ? 314 LEU B CD2 1 
ATOM 5010 N N   . ASP B 1 315 ? 12.646 17.444  60.265  1.00 75.49  ? 315 ASP B N   1 
ATOM 5011 C CA  . ASP B 1 315 ? 11.891 16.957  61.411  1.00 85.59  ? 315 ASP B CA  1 
ATOM 5012 C C   . ASP B 1 315 ? 10.445 17.426  61.315  1.00 90.75  ? 315 ASP B C   1 
ATOM 5013 O O   . ASP B 1 315 ? 10.167 18.555  60.901  1.00 87.80  ? 315 ASP B O   1 
ATOM 5014 C CB  . ASP B 1 315 ? 12.522 17.450  62.715  1.00 81.48  ? 315 ASP B CB  1 
ATOM 5015 C CG  . ASP B 1 315 ? 13.453 16.427  63.337  1.00 90.64  ? 315 ASP B CG  1 
ATOM 5016 O OD1 . ASP B 1 315 ? 13.728 15.398  62.685  1.00 90.29  ? 315 ASP B OD1 1 
ATOM 5017 O OD2 . ASP B 1 315 ? 13.910 16.652  64.478  1.00 89.59  ? 315 ASP B OD2 1 
ATOM 5018 N N   . GLY B 1 316 ? 9.518  16.555  61.704  1.00 94.92  ? 316 GLY B N   1 
ATOM 5019 C CA  . GLY B 1 316 ? 8.114  16.857  61.521  1.00 96.80  ? 316 GLY B CA  1 
ATOM 5020 C C   . GLY B 1 316 ? 7.616  16.677  60.106  1.00 93.54  ? 316 GLY B C   1 
ATOM 5021 O O   . GLY B 1 316 ? 6.490  17.089  59.805  1.00 91.20  ? 316 GLY B O   1 
ATOM 5022 N N   . LYS B 1 317 ? 8.422  16.077  59.225  1.00 93.23  ? 317 LYS B N   1 
ATOM 5023 C CA  . LYS B 1 317 ? 8.075  15.928  57.818  1.00 87.75  ? 317 LYS B CA  1 
ATOM 5024 C C   . LYS B 1 317 ? 8.280  14.509  57.298  1.00 87.21  ? 317 LYS B C   1 
ATOM 5025 O O   . LYS B 1 317 ? 8.298  14.309  56.078  1.00 83.13  ? 317 LYS B O   1 
ATOM 5026 C CB  . LYS B 1 317 ? 8.899  16.901  56.968  1.00 86.79  ? 317 LYS B CB  1 
ATOM 5027 C CG  . LYS B 1 317 ? 8.401  18.332  56.972  1.00 83.44  ? 317 LYS B CG  1 
ATOM 5028 C CD  . LYS B 1 317 ? 8.815  19.080  55.704  1.00 83.25  ? 317 LYS B CD  1 
ATOM 5029 C CE  . LYS B 1 317 ? 8.010  18.664  54.470  1.00 79.23  ? 317 LYS B CE  1 
ATOM 5030 N NZ  . LYS B 1 317 ? 8.260  17.275  53.982  1.00 81.80  ? 317 LYS B NZ  1 
ATOM 5031 N N   . HIS B 1 318 ? 8.440  13.526  58.179  1.00 82.54  ? 318 HIS B N   1 
ATOM 5032 C CA  . HIS B 1 318 ? 8.628  12.151  57.742  1.00 85.44  ? 318 HIS B CA  1 
ATOM 5033 C C   . HIS B 1 318 ? 7.332  11.562  57.186  1.00 87.01  ? 318 HIS B C   1 
ATOM 5034 O O   . HIS B 1 318 ? 6.225  12.007  57.502  1.00 94.85  ? 318 HIS B O   1 
ATOM 5035 C CB  . HIS B 1 318 ? 9.153  11.294  58.893  1.00 82.75  ? 318 HIS B CB  1 
ATOM 5036 C CG  . HIS B 1 318 ? 10.544 11.647  59.317  1.00 78.72  ? 318 HIS B CG  1 
ATOM 5037 N ND1 . HIS B 1 318 ? 11.349 10.783  60.027  1.00 76.92  ? 318 HIS B ND1 1 
ATOM 5038 C CD2 . HIS B 1 318 ? 11.274 12.772  59.129  1.00 76.32  ? 318 HIS B CD2 1 
ATOM 5039 C CE1 . HIS B 1 318 ? 12.515 11.359  60.256  1.00 73.89  ? 318 HIS B CE1 1 
ATOM 5040 N NE2 . HIS B 1 318 ? 12.495 12.568  59.724  1.00 74.58  ? 318 HIS B NE2 1 
ATOM 5041 N N   . LYS B 1 319 ? 7.489  10.547  56.339  1.00 82.48  ? 319 LYS B N   1 
ATOM 5042 C CA  . LYS B 1 319 ? 6.351  9.875   55.732  1.00 83.16  ? 319 LYS B CA  1 
ATOM 5043 C C   . LYS B 1 319 ? 5.528  9.133   56.783  1.00 84.15  ? 319 LYS B C   1 
ATOM 5044 O O   . LYS B 1 319 ? 6.008  8.792   57.868  1.00 81.39  ? 319 LYS B O   1 
ATOM 5045 C CB  . LYS B 1 319 ? 6.819  8.899   54.650  1.00 79.04  ? 319 LYS B CB  1 
ATOM 5046 C CG  . LYS B 1 319 ? 7.484  9.562   53.454  1.00 72.53  ? 319 LYS B CG  1 
ATOM 5047 C CD  . LYS B 1 319 ? 6.624  9.435   52.206  1.00 72.77  ? 319 LYS B CD  1 
ATOM 5048 C CE  . LYS B 1 319 ? 7.192  10.252  51.057  1.00 73.10  ? 319 LYS B CE  1 
ATOM 5049 N NZ  . LYS B 1 319 ? 8.668  10.095  50.938  1.00 68.97  ? 319 LYS B NZ  1 
ATOM 5050 N N   . THR B 1 320 ? 4.267  8.886   56.441  1.00 85.89  ? 320 THR B N   1 
ATOM 5051 C CA  . THR B 1 320 ? 3.304  8.234   57.316  1.00 83.46  ? 320 THR B CA  1 
ATOM 5052 C C   . THR B 1 320 ? 3.003  6.832   56.793  1.00 84.49  ? 320 THR B C   1 
ATOM 5053 O O   . THR B 1 320 ? 3.191  6.536   55.609  1.00 82.56  ? 320 THR B O   1 
ATOM 5054 C CB  . THR B 1 320 ? 2.030  9.094   57.420  1.00 74.04  ? 320 THR B CB  1 
ATOM 5055 O OG1 . THR B 1 320 ? 2.314  10.259  58.204  1.00 85.09  ? 320 THR B OG1 1 
ATOM 5056 C CG2 . THR B 1 320 ? 0.863  8.353   58.068  1.00 79.16  ? 320 THR B CG2 1 
ATOM 5057 N N   . ALA B 1 321 ? 2.547  5.961   57.703  1.00 88.98  ? 321 ALA B N   1 
ATOM 5058 C CA  . ALA B 1 321 ? 2.209  4.584   57.352  1.00 82.21  ? 321 ALA B CA  1 
ATOM 5059 C C   . ALA B 1 321 ? 1.280  4.508   56.148  1.00 86.04  ? 321 ALA B C   1 
ATOM 5060 O O   . ALA B 1 321 ? 1.364  3.560   55.358  1.00 91.27  ? 321 ALA B O   1 
ATOM 5061 C CB  . ALA B 1 321 ? 1.571  3.881   58.551  1.00 84.76  ? 321 ALA B CB  1 
ATOM 5062 N N   . ASP B 1 322 ? 0.388  5.488   55.991  1.00 85.77  ? 322 ASP B N   1 
ATOM 5063 C CA  . ASP B 1 322 ? -0.506 5.481   54.839  1.00 90.36  ? 322 ASP B CA  1 
ATOM 5064 C C   . ASP B 1 322 ? 0.261  5.738   53.548  1.00 83.06  ? 322 ASP B C   1 
ATOM 5065 O O   . ASP B 1 322 ? -0.130 5.243   52.485  1.00 85.40  ? 322 ASP B O   1 
ATOM 5066 C CB  . ASP B 1 322 ? -1.609 6.521   55.028  1.00 92.50  ? 322 ASP B CB  1 
ATOM 5067 C CG  . ASP B 1 322 ? -2.854 5.941   55.675  1.00 95.25  ? 322 ASP B CG  1 
ATOM 5068 O OD1 . ASP B 1 322 ? -2.891 4.714   55.907  1.00 97.59  ? 322 ASP B OD1 1 
ATOM 5069 O OD2 . ASP B 1 322 ? -3.792 6.715   55.960  1.00 92.80  ? 322 ASP B OD2 1 
ATOM 5070 N N   . GLN B 1 323 ? 1.348  6.509   53.621  1.00 76.98  ? 323 GLN B N   1 
ATOM 5071 C CA  . GLN B 1 323 ? 2.230  6.674   52.472  1.00 80.94  ? 323 GLN B CA  1 
ATOM 5072 C C   . GLN B 1 323 ? 3.099  5.441   52.257  1.00 80.99  ? 323 GLN B C   1 
ATOM 5073 O O   . GLN B 1 323 ? 3.388  5.074   51.113  1.00 78.37  ? 323 GLN B O   1 
ATOM 5074 C CB  . GLN B 1 323 ? 3.111  7.907   52.657  1.00 77.97  ? 323 GLN B CB  1 
ATOM 5075 C CG  . GLN B 1 323 ? 2.479  9.205   52.205  1.00 78.98  ? 323 GLN B CG  1 
ATOM 5076 C CD  . GLN B 1 323 ? 3.224  10.410  52.734  1.00 81.67  ? 323 GLN B CD  1 
ATOM 5077 O OE1 . GLN B 1 323 ? 3.530  10.490  53.924  1.00 83.81  ? 323 GLN B OE1 1 
ATOM 5078 N NE2 . GLN B 1 323 ? 3.533  11.350  51.849  1.00 75.47  ? 323 GLN B NE2 1 
ATOM 5079 N N   . VAL B 1 324 ? 3.541  4.804   53.344  1.00 78.06  ? 324 VAL B N   1 
ATOM 5080 C CA  . VAL B 1 324 ? 4.310  3.570   53.218  1.00 82.83  ? 324 VAL B CA  1 
ATOM 5081 C C   . VAL B 1 324 ? 3.461  2.482   52.573  1.00 84.84  ? 324 VAL B C   1 
ATOM 5082 O O   . VAL B 1 324 ? 3.933  1.737   51.705  1.00 83.95  ? 324 VAL B O   1 
ATOM 5083 C CB  . VAL B 1 324 ? 4.851  3.132   54.590  1.00 77.40  ? 324 VAL B CB  1 
ATOM 5084 C CG1 . VAL B 1 324 ? 5.490  1.756   54.489  1.00 71.91  ? 324 VAL B CG1 1 
ATOM 5085 C CG2 . VAL B 1 324 ? 5.847  4.152   55.116  1.00 75.17  ? 324 VAL B CG2 1 
ATOM 5086 N N   . MET B 1 325 ? 2.201  2.364   53.000  1.00 83.66  ? 325 MET B N   1 
ATOM 5087 C CA  . MET B 1 325 ? 1.270  1.460   52.333  1.00 78.84  ? 325 MET B CA  1 
ATOM 5088 C C   . MET B 1 325 ? 1.171  1.775   50.846  1.00 79.90  ? 325 MET B C   1 
ATOM 5089 O O   . MET B 1 325 ? 1.097  0.863   50.013  1.00 74.32  ? 325 MET B O   1 
ATOM 5090 C CB  . MET B 1 325 ? -0.103 1.540   52.998  1.00 83.26  ? 325 MET B CB  1 
ATOM 5091 C CG  . MET B 1 325 ? -0.163 0.828   54.332  1.00 86.91  ? 325 MET B CG  1 
ATOM 5092 S SD  . MET B 1 325 ? 0.605  -0.798  54.233  1.00 94.52  ? 325 MET B SD  1 
ATOM 5093 C CE  . MET B 1 325 ? 0.901  -1.131  55.962  1.00 83.42  ? 325 MET B CE  1 
ATOM 5094 N N   . GLU B 1 326 ? 1.155  3.065   50.496  1.00 82.73  ? 326 GLU B N   1 
ATOM 5095 C CA  . GLU B 1 326 ? 1.203  3.462   49.092  1.00 80.55  ? 326 GLU B CA  1 
ATOM 5096 C C   . GLU B 1 326 ? 2.464  2.930   48.423  1.00 79.02  ? 326 GLU B C   1 
ATOM 5097 O O   . GLU B 1 326 ? 2.403  2.316   47.352  1.00 82.23  ? 326 GLU B O   1 
ATOM 5098 C CB  . GLU B 1 326 ? 1.143  4.987   48.976  1.00 82.65  ? 326 GLU B CB  1 
ATOM 5099 C CG  . GLU B 1 326 ? -0.228 5.609   49.190  1.00 83.90  ? 326 GLU B CG  1 
ATOM 5100 C CD  . GLU B 1 326 ? -1.200 5.296   48.071  1.00 99.50  ? 326 GLU B CD  1 
ATOM 5101 O OE1 . GLU B 1 326 ? -2.423 5.294   48.328  1.00 93.28  ? 326 GLU B OE1 1 
ATOM 5102 O OE2 . GLU B 1 326 ? -0.743 5.048   46.935  1.00 108.82 ? 326 GLU B OE2 1 
ATOM 5103 N N   . MET B 1 327 ? 3.623  3.171   49.046  1.00 78.20  ? 327 MET B N   1 
ATOM 5104 C CA  . MET B 1 327 ? 4.895  2.718   48.488  1.00 78.48  ? 327 MET B CA  1 
ATOM 5105 C C   . MET B 1 327 ? 4.891  1.214   48.251  1.00 77.08  ? 327 MET B C   1 
ATOM 5106 O O   . MET B 1 327 ? 5.345  0.739   47.203  1.00 61.59  ? 327 MET B O   1 
ATOM 5107 C CB  . MET B 1 327 ? 6.038  3.098   49.430  1.00 70.51  ? 327 MET B CB  1 
ATOM 5108 C CG  . MET B 1 327 ? 6.740  4.402   49.098  1.00 85.93  ? 327 MET B CG  1 
ATOM 5109 S SD  . MET B 1 327 ? 7.392  5.183   50.589  1.00 96.89  ? 327 MET B SD  1 
ATOM 5110 C CE  . MET B 1 327 ? 8.140  6.662   49.914  1.00 73.31  ? 327 MET B CE  1 
ATOM 5111 N N   . LEU B 1 328 ? 4.388  0.449   49.223  1.00 75.16  ? 328 LEU B N   1 
ATOM 5112 C CA  . LEU B 1 328 ? 4.297  -0.999  49.072  1.00 70.67  ? 328 LEU B CA  1 
ATOM 5113 C C   . LEU B 1 328 ? 3.377  -1.379  47.918  1.00 78.25  ? 328 LEU B C   1 
ATOM 5114 O O   . LEU B 1 328 ? 3.731  -2.215  47.078  1.00 83.76  ? 328 LEU B O   1 
ATOM 5115 C CB  . LEU B 1 328 ? 3.818  -1.627  50.379  1.00 67.92  ? 328 LEU B CB  1 
ATOM 5116 C CG  . LEU B 1 328 ? 4.954  -2.020  51.323  1.00 67.39  ? 328 LEU B CG  1 
ATOM 5117 C CD1 . LEU B 1 328 ? 4.497  -2.000  52.774  1.00 69.01  ? 328 LEU B CD1 1 
ATOM 5118 C CD2 . LEU B 1 328 ? 5.511  -3.383  50.942  1.00 74.49  ? 328 LEU B CD2 1 
ATOM 5119 N N   . SER B 1 329 ? 2.179  -0.790  47.877  1.00 73.69  ? 329 SER B N   1 
ATOM 5120 C CA  . SER B 1 329 ? 1.231  -1.060  46.798  1.00 76.63  ? 329 SER B CA  1 
ATOM 5121 C C   . SER B 1 329 ? 1.871  -0.849  45.431  1.00 82.10  ? 329 SER B C   1 
ATOM 5122 O O   . SER B 1 329 ? 1.849  -1.743  44.575  1.00 79.79  ? 329 SER B O   1 
ATOM 5123 C CB  . SER B 1 329 ? -0.008 -0.177  46.955  1.00 79.41  ? 329 SER B CB  1 
ATOM 5124 O OG  . SER B 1 329 ? -0.753 -0.138  45.748  1.00 82.18  ? 329 SER B OG  1 
ATOM 5125 N N   . LYS B 1 330 ? 2.417  0.350   45.202  1.00 80.02  ? 330 LYS B N   1 
ATOM 5126 C CA  . LYS B 1 330 ? 3.114  0.635   43.951  1.00 75.19  ? 330 LYS B CA  1 
ATOM 5127 C C   . LYS B 1 330 ? 4.127  -0.457  43.619  1.00 78.54  ? 330 LYS B C   1 
ATOM 5128 O O   . LYS B 1 330 ? 4.208  -0.919  42.475  1.00 73.83  ? 330 LYS B O   1 
ATOM 5129 C CB  . LYS B 1 330 ? 3.799  2.003   44.034  1.00 69.23  ? 330 LYS B CB  1 
ATOM 5130 C CG  . LYS B 1 330 ? 2.905  3.179   43.664  1.00 77.68  ? 330 LYS B CG  1 
ATOM 5131 C CD  . LYS B 1 330 ? 3.687  4.279   42.952  1.00 79.87  ? 330 LYS B CD  1 
ATOM 5132 C CE  . LYS B 1 330 ? 3.530  5.627   43.646  1.00 90.27  ? 330 LYS B CE  1 
ATOM 5133 N NZ  . LYS B 1 330 ? 4.413  6.671   43.049  1.00 85.71  ? 330 LYS B NZ  1 
ATOM 5134 N N   . ALA B 1 331 ? 4.886  -0.909  44.621  1.00 79.82  ? 331 ALA B N   1 
ATOM 5135 C CA  . ALA B 1 331 ? 5.941  -1.884  44.358  1.00 72.35  ? 331 ALA B CA  1 
ATOM 5136 C C   . ALA B 1 331 ? 5.379  -3.227  43.894  1.00 77.68  ? 331 ALA B C   1 
ATOM 5137 O O   . ALA B 1 331 ? 5.927  -3.857  42.985  1.00 79.89  ? 331 ALA B O   1 
ATOM 5138 C CB  . ALA B 1 331 ? 6.796  -2.067  45.599  1.00 72.01  ? 331 ALA B CB  1 
ATOM 5139 N N   . ASN B 1 332 ? 4.293  -3.687  44.513  1.00 78.78  ? 332 ASN B N   1 
ATOM 5140 C CA  . ASN B 1 332 ? 3.700  -4.978  44.159  1.00 85.76  ? 332 ASN B CA  1 
ATOM 5141 C C   . ASN B 1 332 ? 3.241  -4.985  42.699  1.00 90.87  ? 332 ASN B C   1 
ATOM 5142 O O   . ASN B 1 332 ? 3.464  -5.940  41.951  1.00 91.32  ? 332 ASN B O   1 
ATOM 5143 C CB  . ASN B 1 332 ? 2.522  -5.248  45.082  1.00 93.41  ? 332 ASN B CB  1 
ATOM 5144 C CG  . ASN B 1 332 ? 2.253  -6.729  45.264  1.00 96.35  ? 332 ASN B CG  1 
ATOM 5145 O OD1 . ASN B 1 332 ? 3.129  -7.481  45.685  1.00 95.23  ? 332 ASN B OD1 1 
ATOM 5146 N ND2 . ASN B 1 332 ? 1.031  -7.153  44.966  1.00 92.48  ? 332 ASN B ND2 1 
ATOM 5147 N N   . LYS B 1 333 ? 2.668  -3.863  42.280  1.00 87.61  ? 333 LYS B N   1 
ATOM 5148 C CA  . LYS B 1 333 ? 2.328  -3.749  40.847  1.00 80.37  ? 333 LYS B CA  1 
ATOM 5149 C C   . LYS B 1 333 ? 3.601  -4.026  40.047  1.00 86.34  ? 333 LYS B C   1 
ATOM 5150 O O   . LYS B 1 333 ? 3.507  -4.734  39.034  1.00 93.12  ? 333 LYS B O   1 
ATOM 5151 C CB  . LYS B 1 333 ? 1.794  -2.347  40.557  1.00 89.85  ? 333 LYS B CB  1 
ATOM 5152 C CG  . LYS B 1 333 ? 1.569  -2.024  39.087  1.00 91.21  ? 333 LYS B CG  1 
ATOM 5153 C CD  . LYS B 1 333 ? 0.334  -1.186  38.849  1.00 87.96  ? 333 LYS B CD  1 
ATOM 5154 C CE  . LYS B 1 333 ? 0.025  -0.255  40.002  1.00 101.51 ? 333 LYS B CE  1 
ATOM 5155 N NZ  . LYS B 1 333 ? -0.240 1.126   39.533  1.00 117.16 ? 333 LYS B NZ  1 
ATOM 5156 N N   . MET B 1 334 ? 4.750  -3.505  40.490  1.00 83.20  ? 334 MET B N   1 
ATOM 5157 C CA  . MET B 1 334 ? 5.965  -3.683  39.685  1.00 79.86  ? 334 MET B CA  1 
ATOM 5158 C C   . MET B 1 334 ? 6.639  -5.037  39.868  1.00 79.34  ? 334 MET B C   1 
ATOM 5159 O O   . MET B 1 334 ? 7.700  -5.233  39.288  1.00 80.44  ? 334 MET B O   1 
ATOM 5160 C CB  . MET B 1 334 ? 6.973  -2.574  39.971  1.00 83.20  ? 334 MET B CB  1 
ATOM 5161 C CG  . MET B 1 334 ? 6.955  -1.428  38.968  1.00 82.70  ? 334 MET B CG  1 
ATOM 5162 S SD  . MET B 1 334 ? 5.304  -1.035  38.375  1.00 100.77 ? 334 MET B SD  1 
ATOM 5163 C CE  . MET B 1 334 ? 4.759  0.044   39.685  1.00 93.30  ? 334 MET B CE  1 
ATOM 5164 N N   . ASP B 1 335 ? 6.059  -5.962  40.642  1.00 79.40  ? 335 ASP B N   1 
ATOM 5165 C CA  . ASP B 1 335 ? 6.719  -7.227  41.021  1.00 83.05  ? 335 ASP B CA  1 
ATOM 5166 C C   . ASP B 1 335 ? 8.092  -6.955  41.637  1.00 78.46  ? 335 ASP B C   1 
ATOM 5167 O O   . ASP B 1 335 ? 9.099  -7.586  41.301  1.00 74.18  ? 335 ASP B O   1 
ATOM 5168 C CB  . ASP B 1 335 ? 6.842  -8.195  39.833  1.00 83.99  ? 335 ASP B CB  1 
ATOM 5169 C CG  . ASP B 1 335 ? 7.177  -9.624  40.269  1.00 83.98  ? 335 ASP B CG  1 
ATOM 5170 O OD1 . ASP B 1 335 ? 6.763  -10.026 41.378  1.00 77.79  ? 335 ASP B OD1 1 
ATOM 5171 O OD2 . ASP B 1 335 ? 7.862  -10.345 39.510  1.00 87.79  ? 335 ASP B OD2 1 
ATOM 5172 N N   . ALA B 1 336 ? 8.119  -6.004  42.566  1.00 65.57  ? 336 ALA B N   1 
ATOM 5173 C CA  . ALA B 1 336 ? 9.352  -5.556  43.191  1.00 59.51  ? 336 ALA B CA  1 
ATOM 5174 C C   . ALA B 1 336 ? 9.208  -5.529  44.704  1.00 58.22  ? 336 ALA B C   1 
ATOM 5175 O O   . ALA B 1 336 ? 8.105  -5.394  45.242  1.00 53.75  ? 336 ALA B O   1 
ATOM 5176 C CB  . ALA B 1 336 ? 9.753  -4.165  42.690  1.00 68.29  ? 336 ALA B CB  1 
ATOM 5177 N N   . ASN B 1 337 ? 10.341 -5.679  45.383  1.00 59.52  ? 337 ASN B N   1 
ATOM 5178 C CA  . ASN B 1 337 ? 10.421 -5.453  46.814  1.00 49.86  ? 337 ASN B CA  1 
ATOM 5179 C C   . ASN B 1 337 ? 10.415 -3.957  47.115  1.00 62.60  ? 337 ASN B C   1 
ATOM 5180 O O   . ASN B 1 337 ? 10.651 -3.117  46.241  1.00 62.77  ? 337 ASN B O   1 
ATOM 5181 C CB  . ASN B 1 337 ? 11.682 -6.092  47.394  1.00 56.23  ? 337 ASN B CB  1 
ATOM 5182 C CG  . ASN B 1 337 ? 11.725 -7.591  47.186  1.00 61.14  ? 337 ASN B CG  1 
ATOM 5183 O OD1 . ASN B 1 337 ? 10.805 -8.178  46.615  1.00 58.61  ? 337 ASN B OD1 1 
ATOM 5184 N ND2 . ASN B 1 337 ? 12.798 -8.221  47.651  1.00 64.04  ? 337 ASN B ND2 1 
ATOM 5185 N N   . LEU B 1 338 ? 10.137 -3.626  48.373  1.00 60.30  ? 338 LEU B N   1 
ATOM 5186 C CA  . LEU B 1 338 ? 10.306 -2.272  48.883  1.00 54.09  ? 338 LEU B CA  1 
ATOM 5187 C C   . LEU B 1 338 ? 11.455 -2.257  49.882  1.00 55.11  ? 338 LEU B C   1 
ATOM 5188 O O   . LEU B 1 338 ? 11.385 -2.919  50.923  1.00 57.11  ? 338 LEU B O   1 
ATOM 5189 C CB  . LEU B 1 338 ? 9.023  -1.755  49.533  1.00 59.19  ? 338 LEU B CB  1 
ATOM 5190 C CG  . LEU B 1 338 ? 9.180  -0.402  50.233  1.00 59.80  ? 338 LEU B CG  1 
ATOM 5191 C CD1 . LEU B 1 338 ? 9.504  0.684   49.220  1.00 57.69  ? 338 LEU B CD1 1 
ATOM 5192 C CD2 . LEU B 1 338 ? 7.934  -0.037  51.017  1.00 56.13  ? 338 LEU B CD2 1 
ATOM 5193 N N   . LEU B 1 339 ? 12.508 -1.511  49.560  1.00 60.47  ? 339 LEU B N   1 
ATOM 5194 C CA  . LEU B 1 339 ? 13.621 -1.274  50.477  1.00 56.11  ? 339 LEU B CA  1 
ATOM 5195 C C   . LEU B 1 339 ? 13.446 0.126   51.054  1.00 57.04  ? 339 LEU B C   1 
ATOM 5196 O O   . LEU B 1 339 ? 13.761 1.124   50.400  1.00 57.83  ? 339 LEU B O   1 
ATOM 5197 C CB  . LEU B 1 339 ? 14.961 -1.431  49.765  1.00 50.18  ? 339 LEU B CB  1 
ATOM 5198 C CG  . LEU B 1 339 ? 16.194 -1.442  50.670  1.00 49.75  ? 339 LEU B CG  1 
ATOM 5199 C CD1 . LEU B 1 339 ? 16.126 -2.606  51.643  1.00 54.26  ? 339 LEU B CD1 1 
ATOM 5200 C CD2 . LEU B 1 339 ? 17.470 -1.506  49.846  1.00 45.85  ? 339 LEU B CD2 1 
ATOM 5201 N N   . LEU B 1 340 ? 12.945 0.199   52.283  1.00 52.75  ? 340 LEU B N   1 
ATOM 5202 C CA  . LEU B 1 340 ? 12.546 1.459   52.895  1.00 56.53  ? 340 LEU B CA  1 
ATOM 5203 C C   . LEU B 1 340 ? 13.629 1.926   53.859  1.00 57.82  ? 340 LEU B C   1 
ATOM 5204 O O   . LEU B 1 340 ? 14.106 1.146   54.690  1.00 63.15  ? 340 LEU B O   1 
ATOM 5205 C CB  . LEU B 1 340 ? 11.211 1.308   53.624  1.00 58.89  ? 340 LEU B CB  1 
ATOM 5206 C CG  . LEU B 1 340 ? 10.491 2.601   54.003  1.00 58.41  ? 340 LEU B CG  1 
ATOM 5207 C CD1 . LEU B 1 340 ? 10.281 3.478   52.778  1.00 60.94  ? 340 LEU B CD1 1 
ATOM 5208 C CD2 . LEU B 1 340 ? 9.163  2.287   54.669  1.00 69.08  ? 340 LEU B CD2 1 
ATOM 5209 N N   . ASN B 1 341 ? 14.009 3.196   53.748  1.00 57.03  ? 341 ASN B N   1 
ATOM 5210 C CA  . ASN B 1 341 ? 15.190 3.720   54.418  1.00 53.79  ? 341 ASN B CA  1 
ATOM 5211 C C   . ASN B 1 341 ? 14.835 4.430   55.714  1.00 58.05  ? 341 ASN B C   1 
ATOM 5212 O O   . ASN B 1 341 ? 13.860 5.184   55.780  1.00 62.26  ? 341 ASN B O   1 
ATOM 5213 C CB  . ASN B 1 341 ? 15.950 4.687   53.507  1.00 55.06  ? 341 ASN B CB  1 
ATOM 5214 C CG  . ASN B 1 341 ? 17.227 5.208   54.146  1.00 56.88  ? 341 ASN B CG  1 
ATOM 5215 O OD1 . ASN B 1 341 ? 18.293 4.608   54.009  1.00 60.70  ? 341 ASN B OD1 1 
ATOM 5216 N ND2 . ASN B 1 341 ? 17.124 6.331   54.849  1.00 53.28  ? 341 ASN B ND2 1 
ATOM 5217 N N   . VAL B 1 342 ? 15.642 4.186   56.743  1.00 54.99  ? 342 VAL B N   1 
ATOM 5218 C CA  . VAL B 1 342 ? 15.718 5.048   57.914  1.00 51.47  ? 342 VAL B CA  1 
ATOM 5219 C C   . VAL B 1 342 ? 17.125 5.630   57.959  1.00 59.71  ? 342 VAL B C   1 
ATOM 5220 O O   . VAL B 1 342 ? 18.106 4.925   57.692  1.00 56.59  ? 342 VAL B O   1 
ATOM 5221 C CB  . VAL B 1 342 ? 15.360 4.300   59.216  1.00 63.18  ? 342 VAL B CB  1 
ATOM 5222 C CG1 . VAL B 1 342 ? 14.126 3.438   59.008  1.00 67.43  ? 342 VAL B CG1 1 
ATOM 5223 C CG2 . VAL B 1 342 ? 16.520 3.444   59.722  1.00 60.88  ? 342 VAL B CG2 1 
ATOM 5224 N N   . GLY B 1 343 ? 17.216 6.928   58.230  1.00 70.65  ? 343 GLY B N   1 
ATOM 5225 C CA  . GLY B 1 343 ? 18.492 7.564   58.440  1.00 56.97  ? 343 GLY B CA  1 
ATOM 5226 C C   . GLY B 1 343 ? 18.639 7.967   59.890  1.00 70.10  ? 343 GLY B C   1 
ATOM 5227 O O   . GLY B 1 343 ? 18.097 8.983   60.337  1.00 71.94  ? 343 GLY B O   1 
ATOM 5228 N N   . PRO B 1 344 ? 19.378 7.165   60.655  1.00 63.90  ? 344 PRO B N   1 
ATOM 5229 C CA  . PRO B 1 344 ? 19.451 7.383   62.102  1.00 67.15  ? 344 PRO B CA  1 
ATOM 5230 C C   . PRO B 1 344 ? 20.041 8.738   62.467  1.00 70.07  ? 344 PRO B C   1 
ATOM 5231 O O   . PRO B 1 344 ? 20.694 9.410   61.665  1.00 68.84  ? 344 PRO B O   1 
ATOM 5232 C CB  . PRO B 1 344 ? 20.351 6.239   62.580  1.00 63.33  ? 344 PRO B CB  1 
ATOM 5233 C CG  . PRO B 1 344 ? 20.081 5.152   61.598  1.00 61.40  ? 344 PRO B CG  1 
ATOM 5234 C CD  . PRO B 1 344 ? 19.949 5.862   60.273  1.00 63.12  ? 344 PRO B CD  1 
ATOM 5235 N N   . LEU B 1 345 ? 19.794 9.124   63.714  1.00 72.90  ? 345 LEU B N   1 
ATOM 5236 C CA  . LEU B 1 345 ? 20.301 10.345  64.314  1.00 78.54  ? 345 LEU B CA  1 
ATOM 5237 C C   . LEU B 1 345 ? 21.762 10.161  64.732  1.00 71.59  ? 345 LEU B C   1 
ATOM 5238 O O   . LEU B 1 345 ? 22.234 9.030   64.869  1.00 72.79  ? 345 LEU B O   1 
ATOM 5239 C CB  . LEU B 1 345 ? 19.411 10.735  65.495  1.00 81.92  ? 345 LEU B CB  1 
ATOM 5240 C CG  . LEU B 1 345 ? 18.078 11.391  65.100  1.00 75.72  ? 345 LEU B CG  1 
ATOM 5241 C CD1 . LEU B 1 345 ? 17.098 10.382  64.537  1.00 76.98  ? 345 LEU B CD1 1 
ATOM 5242 C CD2 . LEU B 1 345 ? 17.454 12.132  66.270  1.00 81.49  ? 345 LEU B CD2 1 
ATOM 5243 N N   . PRO B 1 346 ? 22.505 11.265  64.926  1.00 66.26  ? 346 PRO B N   1 
ATOM 5244 C CA  . PRO B 1 346 ? 23.968 11.165  65.120  1.00 67.49  ? 346 PRO B CA  1 
ATOM 5245 C C   . PRO B 1 346 ? 24.427 10.136  66.137  1.00 66.58  ? 346 PRO B C   1 
ATOM 5246 O O   . PRO B 1 346 ? 25.535 9.597   66.015  1.00 63.29  ? 346 PRO B O   1 
ATOM 5247 C CB  . PRO B 1 346 ? 24.348 12.583  65.569  1.00 62.10  ? 346 PRO B CB  1 
ATOM 5248 C CG  . PRO B 1 346 ? 23.326 13.455  64.954  1.00 67.23  ? 346 PRO B CG  1 
ATOM 5249 C CD  . PRO B 1 346 ? 22.051 12.669  64.938  1.00 69.06  ? 346 PRO B CD  1 
ATOM 5250 N N   . ASP B 1 347 ? 23.608 9.854   67.141  1.00 71.75  ? 347 ASP B N   1 
ATOM 5251 C CA  . ASP B 1 347 ? 23.955 8.927   68.204  1.00 75.18  ? 347 ASP B CA  1 
ATOM 5252 C C   . ASP B 1 347 ? 23.747 7.465   67.826  1.00 81.61  ? 347 ASP B C   1 
ATOM 5253 O O   . ASP B 1 347 ? 24.269 6.582   68.513  1.00 81.11  ? 347 ASP B O   1 
ATOM 5254 C CB  . ASP B 1 347 ? 23.140 9.333   69.438  1.00 91.00  ? 347 ASP B CB  1 
ATOM 5255 C CG  . ASP B 1 347 ? 21.669 8.953   69.332  1.00 96.48  ? 347 ASP B CG  1 
ATOM 5256 O OD1 . ASP B 1 347 ? 21.226 8.441   68.281  1.00 96.83  ? 347 ASP B OD1 1 
ATOM 5257 O OD2 . ASP B 1 347 ? 20.943 9.134   70.328  1.00 95.72  ? 347 ASP B OD2 1 
ATOM 5258 N N   . GLY B 1 348 ? 23.069 7.198   66.714  1.00 80.77  ? 348 GLY B N   1 
ATOM 5259 C CA  . GLY B 1 348 ? 22.757 5.852   66.294  1.00 74.45  ? 348 GLY B CA  1 
ATOM 5260 C C   . GLY B 1 348 ? 21.334 5.423   66.561  1.00 80.30  ? 348 GLY B C   1 
ATOM 5261 O O   . GLY B 1 348 ? 20.994 4.264   66.290  1.00 82.10  ? 348 GLY B O   1 
ATOM 5262 N N   . SER B 1 349 ? 20.494 6.309   67.085  1.00 82.96  ? 349 SER B N   1 
ATOM 5263 C CA  . SER B 1 349 ? 19.106 5.968   67.350  1.00 83.15  ? 349 SER B CA  1 
ATOM 5264 C C   . SER B 1 349 ? 18.244 6.295   66.140  1.00 76.36  ? 349 SER B C   1 
ATOM 5265 O O   . SER B 1 349 ? 18.525 7.221   65.374  1.00 74.76  ? 349 SER B O   1 
ATOM 5266 C CB  . SER B 1 349 ? 18.567 6.710   68.573  1.00 88.83  ? 349 SER B CB  1 
ATOM 5267 O OG  . SER B 1 349 ? 19.006 8.054   68.593  1.00 94.77  ? 349 SER B OG  1 
ATOM 5268 N N   . ILE B 1 350 ? 17.189 5.519   65.983  1.00 74.49  ? 350 ILE B N   1 
ATOM 5269 C CA  . ILE B 1 350 ? 16.243 5.686   64.890  1.00 80.75  ? 350 ILE B CA  1 
ATOM 5270 C C   . ILE B 1 350 ? 15.263 6.795   65.240  1.00 79.97  ? 350 ILE B C   1 
ATOM 5271 O O   . ILE B 1 350 ? 14.813 6.907   66.386  1.00 79.61  ? 350 ILE B O   1 
ATOM 5272 C CB  . ILE B 1 350 ? 15.543 4.349   64.619  1.00 75.03  ? 350 ILE B CB  1 
ATOM 5273 C CG1 . ILE B 1 350 ? 16.626 3.282   64.480  1.00 71.70  ? 350 ILE B CG1 1 
ATOM 5274 C CG2 . ILE B 1 350 ? 14.670 4.435   63.374  1.00 67.50  ? 350 ILE B CG2 1 
ATOM 5275 C CD1 . ILE B 1 350 ? 16.132 1.906   64.626  1.00 72.03  ? 350 ILE B CD1 1 
ATOM 5276 N N   . HIS B 1 351 ? 14.960 7.634   64.254  1.00 81.20  ? 351 HIS B N   1 
ATOM 5277 C CA  . HIS B 1 351 ? 14.057 8.758   64.453  1.00 84.79  ? 351 HIS B CA  1 
ATOM 5278 C C   . HIS B 1 351 ? 12.765 8.308   65.131  1.00 88.59  ? 351 HIS B C   1 
ATOM 5279 O O   . HIS B 1 351 ? 12.239 7.232   64.815  1.00 87.94  ? 351 HIS B O   1 
ATOM 5280 C CB  . HIS B 1 351 ? 13.739 9.428   63.115  1.00 84.08  ? 351 HIS B CB  1 
ATOM 5281 C CG  . HIS B 1 351 ? 13.520 10.904  63.222  1.00 86.85  ? 351 HIS B CG  1 
ATOM 5282 N ND1 . HIS B 1 351 ? 12.274 11.458  63.419  1.00 82.73  ? 351 HIS B ND1 1 
ATOM 5283 C CD2 . HIS B 1 351 ? 14.387 11.943  63.156  1.00 74.05  ? 351 HIS B CD2 1 
ATOM 5284 C CE1 . HIS B 1 351 ? 12.382 12.773  63.473  1.00 80.19  ? 351 HIS B CE1 1 
ATOM 5285 N NE2 . HIS B 1 351 ? 13.654 13.093  63.316  1.00 78.76  ? 351 HIS B NE2 1 
ATOM 5286 N N   . PRO B 1 352 ? 12.232 9.095   66.069  1.00 90.07  ? 352 PRO B N   1 
ATOM 5287 C CA  . PRO B 1 352 ? 10.954 8.719   66.691  1.00 86.51  ? 352 PRO B CA  1 
ATOM 5288 C C   . PRO B 1 352 ? 9.815  8.703   65.692  1.00 91.46  ? 352 PRO B C   1 
ATOM 5289 O O   . PRO B 1 352 ? 8.862  7.930   65.858  1.00 88.89  ? 352 PRO B O   1 
ATOM 5290 C CB  . PRO B 1 352 ? 10.745 9.783   67.779  1.00 78.43  ? 352 PRO B CB  1 
ATOM 5291 C CG  . PRO B 1 352 ? 11.956 10.660  67.767  1.00 86.21  ? 352 PRO B CG  1 
ATOM 5292 C CD  . PRO B 1 352 ? 12.740 10.397  66.531  1.00 80.17  ? 352 PRO B CD  1 
ATOM 5293 N N   . GLU B 1 353 ? 9.888  9.541   64.654  1.00 90.65  ? 353 GLU B N   1 
ATOM 5294 C CA  . GLU B 1 353 ? 8.879  9.515   63.601  1.00 87.31  ? 353 GLU B CA  1 
ATOM 5295 C C   . GLU B 1 353 ? 8.930  8.208   62.825  1.00 88.47  ? 353 GLU B C   1 
ATOM 5296 O O   . GLU B 1 353 ? 7.886  7.619   62.519  1.00 89.42  ? 353 GLU B O   1 
ATOM 5297 C CB  . GLU B 1 353 ? 9.079  10.690  62.653  1.00 86.69  ? 353 GLU B CB  1 
ATOM 5298 C CG  . GLU B 1 353 ? 8.937  12.044  63.294  1.00 84.53  ? 353 GLU B CG  1 
ATOM 5299 C CD  . GLU B 1 353 ? 8.332  13.044  62.343  1.00 90.12  ? 353 GLU B CD  1 
ATOM 5300 O OE1 . GLU B 1 353 ? 7.152  12.875  61.971  1.00 96.56  ? 353 GLU B OE1 1 
ATOM 5301 O OE2 . GLU B 1 353 ? 9.052  13.980  61.942  1.00 79.80  ? 353 GLU B OE2 1 
ATOM 5302 N N   . ASP B 1 354 ? 10.136 7.741   62.494  1.00 89.12  ? 354 ASP B N   1 
ATOM 5303 C CA  . ASP B 1 354 ? 10.256 6.491   61.756  1.00 84.09  ? 354 ASP B CA  1 
ATOM 5304 C C   . ASP B 1 354 ? 9.817  5.318   62.619  1.00 84.00  ? 354 ASP B C   1 
ATOM 5305 O O   . ASP B 1 354 ? 9.259  4.343   62.105  1.00 90.72  ? 354 ASP B O   1 
ATOM 5306 C CB  . ASP B 1 354 ? 11.695 6.293   61.275  1.00 85.30  ? 354 ASP B CB  1 
ATOM 5307 C CG  . ASP B 1 354 ? 12.205 7.462   60.448  1.00 85.97  ? 354 ASP B CG  1 
ATOM 5308 O OD1 . ASP B 1 354 ? 11.378 8.174   59.838  1.00 77.66  ? 354 ASP B OD1 1 
ATOM 5309 O OD2 . ASP B 1 354 ? 13.437 7.668   60.407  1.00 81.45  ? 354 ASP B OD2 1 
ATOM 5310 N N   . VAL B 1 355 ? 10.065 5.401   63.928  1.00 85.86  ? 355 VAL B N   1 
ATOM 5311 C CA  . VAL B 1 355 ? 9.594  4.376   64.854  1.00 82.81  ? 355 VAL B CA  1 
ATOM 5312 C C   . VAL B 1 355 ? 8.072  4.299   64.821  1.00 89.31  ? 355 VAL B C   1 
ATOM 5313 O O   . VAL B 1 355 ? 7.487  3.210   64.762  1.00 91.94  ? 355 VAL B O   1 
ATOM 5314 C CB  . VAL B 1 355 ? 10.120 4.661   66.273  1.00 79.50  ? 355 VAL B CB  1 
ATOM 5315 C CG1 . VAL B 1 355 ? 9.175  4.100   67.327  1.00 86.79  ? 355 VAL B CG1 1 
ATOM 5316 C CG2 . VAL B 1 355 ? 11.523 4.098   66.445  1.00 72.04  ? 355 VAL B CG2 1 
ATOM 5317 N N   . LYS B 1 356 ? 7.408  5.459   64.848  1.00 89.88  ? 356 LYS B N   1 
ATOM 5318 C CA  . LYS B 1 356 ? 5.948  5.492   64.819  1.00 87.16  ? 356 LYS B CA  1 
ATOM 5319 C C   . LYS B 1 356 ? 5.410  4.915   63.517  1.00 92.18  ? 356 LYS B C   1 
ATOM 5320 O O   . LYS B 1 356 ? 4.517  4.060   63.523  1.00 99.65  ? 356 LYS B O   1 
ATOM 5321 C CB  . LYS B 1 356 ? 5.448  6.926   64.992  1.00 92.50  ? 356 LYS B CB  1 
ATOM 5322 C CG  . LYS B 1 356 ? 5.651  7.539   66.365  1.00 84.86  ? 356 LYS B CG  1 
ATOM 5323 C CD  . LYS B 1 356 ? 5.628  9.067   66.283  1.00 92.01  ? 356 LYS B CD  1 
ATOM 5324 C CE  . LYS B 1 356 ? 5.162  9.557   64.911  1.00 93.55  ? 356 LYS B CE  1 
ATOM 5325 N NZ  . LYS B 1 356 ? 5.212  11.038  64.771  1.00 86.50  ? 356 LYS B NZ  1 
ATOM 5326 N N   . THR B 1 357 ? 5.933  5.392   62.385  1.00 83.44  ? 357 THR B N   1 
ATOM 5327 C CA  . THR B 1 357 ? 5.455  4.928   61.087  1.00 82.44  ? 357 THR B CA  1 
ATOM 5328 C C   . THR B 1 357 ? 5.692  3.434   60.921  1.00 90.35  ? 357 THR B C   1 
ATOM 5329 O O   . THR B 1 357 ? 4.786  2.687   60.531  1.00 90.74  ? 357 THR B O   1 
ATOM 5330 C CB  . THR B 1 357 ? 6.143  5.708   59.967  1.00 84.83  ? 357 THR B CB  1 
ATOM 5331 O OG1 . THR B 1 357 ? 5.802  7.096   60.067  1.00 99.43  ? 357 THR B OG1 1 
ATOM 5332 C CG2 . THR B 1 357 ? 5.713  5.182   58.609  1.00 76.09  ? 357 THR B CG2 1 
ATOM 5333 N N   . LEU B 1 358 ? 6.901  2.973   61.248  1.00 90.91  ? 358 LEU B N   1 
ATOM 5334 C CA  . LEU B 1 358 ? 7.235  1.567   61.046  1.00 89.09  ? 358 LEU B CA  1 
ATOM 5335 C C   . LEU B 1 358 ? 6.450  0.669   61.984  1.00 90.83  ? 358 LEU B C   1 
ATOM 5336 O O   . LEU B 1 358 ? 6.078  -0.447  61.605  1.00 87.76  ? 358 LEU B O   1 
ATOM 5337 C CB  . LEU B 1 358 ? 8.732  1.347   61.247  1.00 86.57  ? 358 LEU B CB  1 
ATOM 5338 C CG  . LEU B 1 358 ? 9.635  1.688   60.058  1.00 86.49  ? 358 LEU B CG  1 
ATOM 5339 C CD1 . LEU B 1 358 ? 11.015 1.085   60.250  1.00 80.27  ? 358 LEU B CD1 1 
ATOM 5340 C CD2 . LEU B 1 358 ? 9.018  1.222   58.746  1.00 78.67  ? 358 LEU B CD2 1 
ATOM 5341 N N   . ALA B 1 359 ? 6.186  1.133   63.204  1.00 88.91  ? 359 ALA B N   1 
ATOM 5342 C CA  . ALA B 1 359 ? 5.406  0.312   64.114  1.00 91.11  ? 359 ALA B CA  1 
ATOM 5343 C C   . ALA B 1 359 ? 4.022  0.060   63.545  1.00 92.67  ? 359 ALA B C   1 
ATOM 5344 O O   . ALA B 1 359 ? 3.456  -1.029  63.734  1.00 84.31  ? 359 ALA B O   1 
ATOM 5345 C CB  . ALA B 1 359 ? 5.327  0.958   65.499  1.00 88.62  ? 359 ALA B CB  1 
ATOM 5346 N N   . GLU B 1 360 ? 3.466  1.044   62.853  1.00 87.17  ? 360 GLU B N   1 
ATOM 5347 C CA  . GLU B 1 360 ? 2.084  0.853   62.364  1.00 93.27  ? 360 GLU B CA  1 
ATOM 5348 C C   . GLU B 1 360 ? 2.133  0.047   61.067  1.00 95.46  ? 360 GLU B C   1 
ATOM 5349 O O   . GLU B 1 360 ? 1.314  -0.872  60.919  1.00 97.25  ? 360 GLU B O   1 
ATOM 5350 C CB  . GLU B 1 360 ? 1.408  2.207   62.170  1.00 95.84  ? 360 GLU B CB  1 
ATOM 5351 C CG  . GLU B 1 360 ? -0.082 2.101   61.905  1.00 104.45 ? 360 GLU B CG  1 
ATOM 5352 C CD  . GLU B 1 360 ? -0.935 1.813   63.129  1.00 103.39 ? 360 GLU B CD  1 
ATOM 5353 O OE1 . GLU B 1 360 ? -0.470 2.088   64.251  1.00 99.43  ? 360 GLU B OE1 1 
ATOM 5354 O OE2 . GLU B 1 360 ? -2.065 1.317   62.957  1.00 101.79 ? 360 GLU B OE2 1 
ATOM 5355 N N   . VAL B 1 361 ? 3.067  0.368   60.172  1.00 91.02  ? 361 VAL B N   1 
ATOM 5356 C CA  . VAL B 1 361 ? 3.071  -0.324  58.892  1.00 87.53  ? 361 VAL B CA  1 
ATOM 5357 C C   . VAL B 1 361 ? 2.971  -1.832  59.134  1.00 86.95  ? 361 VAL B C   1 
ATOM 5358 O O   . VAL B 1 361 ? 2.236  -2.542  58.441  1.00 83.59  ? 361 VAL B O   1 
ATOM 5359 C CB  . VAL B 1 361 ? 4.319  0.054   58.069  1.00 77.45  ? 361 VAL B CB  1 
ATOM 5360 C CG1 . VAL B 1 361 ? 4.415  -0.834  56.866  1.00 87.20  ? 361 VAL B CG1 1 
ATOM 5361 C CG2 . VAL B 1 361 ? 4.200  1.510   57.676  1.00 85.27  ? 361 VAL B CG2 1 
ATOM 5362 N N   . GLY B 1 362 ? 3.605  -2.320  60.204  1.00 81.01  ? 362 GLY B N   1 
ATOM 5363 C CA  . GLY B 1 362 ? 3.538  -3.745  60.513  1.00 85.75  ? 362 GLY B CA  1 
ATOM 5364 C C   . GLY B 1 362 ? 2.158  -4.243  60.915  1.00 90.80  ? 362 GLY B C   1 
ATOM 5365 O O   . GLY B 1 362 ? 1.712  -5.296  60.449  1.00 91.75  ? 362 GLY B O   1 
ATOM 5366 N N   . ARG B 1 363 ? 1.471  -3.512  61.796  1.00 92.43  ? 363 ARG B N   1 
ATOM 5367 C CA  . ARG B 1 363 ? 0.166  -3.962  62.277  1.00 93.18  ? 363 ARG B CA  1 
ATOM 5368 C C   . ARG B 1 363 ? -0.909 -3.788  61.210  1.00 87.83  ? 363 ARG B C   1 
ATOM 5369 O O   . ARG B 1 363 ? -1.812 -4.625  61.089  1.00 85.90  ? 363 ARG B O   1 
ATOM 5370 C CB  . ARG B 1 363 ? -0.173 -3.241  63.581  1.00 91.07  ? 363 ARG B CB  1 
ATOM 5371 C CG  . ARG B 1 363 ? 0.754  -3.715  64.698  1.00 101.68 ? 363 ARG B CG  1 
ATOM 5372 C CD  . ARG B 1 363 ? 0.528  -3.057  66.045  1.00 102.54 ? 363 ARG B CD  1 
ATOM 5373 N NE  . ARG B 1 363 ? 1.130  -1.732  66.122  1.00 99.41  ? 363 ARG B NE  1 
ATOM 5374 C CZ  . ARG B 1 363 ? 1.521  -1.157  67.252  1.00 98.47  ? 363 ARG B CZ  1 
ATOM 5375 N NH1 . ARG B 1 363 ? 1.555  -1.828  68.392  1.00 94.26  ? 363 ARG B NH1 1 
ATOM 5376 N NH2 . ARG B 1 363 ? 1.939  0.106   67.228  1.00 101.83 ? 363 ARG B NH2 1 
ATOM 5377 N N   . LYS B 1 364 ? -0.840 -2.699  60.440  1.00 86.29  ? 364 LYS B N   1 
ATOM 5378 C CA  . LYS B 1 364 ? -1.708 -2.580  59.274  1.00 85.87  ? 364 LYS B CA  1 
ATOM 5379 C C   . LYS B 1 364 ? -1.465 -3.721  58.294  1.00 88.47  ? 364 LYS B C   1 
ATOM 5380 O O   . LYS B 1 364 ? -2.397 -4.170  57.616  1.00 96.01  ? 364 LYS B O   1 
ATOM 5381 C CB  . LYS B 1 364 ? -1.492 -1.236  58.577  1.00 82.97  ? 364 LYS B CB  1 
ATOM 5382 C CG  . LYS B 1 364 ? -1.883 -0.012  59.389  1.00 82.96  ? 364 LYS B CG  1 
ATOM 5383 C CD  . LYS B 1 364 ? -1.669 1.264   58.581  1.00 90.42  ? 364 LYS B CD  1 
ATOM 5384 C CE  . LYS B 1 364 ? -2.987 1.885   58.140  1.00 89.15  ? 364 LYS B CE  1 
ATOM 5385 N NZ  . LYS B 1 364 ? -3.303 3.121   58.909  1.00 89.49  ? 364 LYS B NZ  1 
ATOM 5386 N N   . LEU B 1 365 ? -0.221 -4.201  58.205  1.00 91.30  ? 365 LEU B N   1 
ATOM 5387 C CA  . LEU B 1 365 ? 0.107  -5.263  57.259  1.00 92.45  ? 365 LEU B CA  1 
ATOM 5388 C C   . LEU B 1 365 ? -0.416 -6.610  57.742  1.00 89.41  ? 365 LEU B C   1 
ATOM 5389 O O   . LEU B 1 365 ? -1.036 -7.357  56.976  1.00 88.66  ? 365 LEU B O   1 
ATOM 5390 C CB  . LEU B 1 365 ? 1.620  -5.323  57.045  1.00 86.53  ? 365 LEU B CB  1 
ATOM 5391 C CG  . LEU B 1 365 ? 2.187  -4.616  55.813  1.00 82.03  ? 365 LEU B CG  1 
ATOM 5392 C CD1 . LEU B 1 365 ? 3.499  -5.258  55.394  1.00 77.31  ? 365 LEU B CD1 1 
ATOM 5393 C CD2 . LEU B 1 365 ? 1.187  -4.638  54.667  1.00 86.37  ? 365 LEU B CD2 1 
ATOM 5394 N N   . LYS B 1 366 ? -0.180 -6.937  59.014  1.00 86.74  ? 366 LYS B N   1 
ATOM 5395 C CA  . LYS B 1 366 ? -0.646 -8.209  59.554  1.00 95.20  ? 366 LYS B CA  1 
ATOM 5396 C C   . LYS B 1 366 ? -2.155 -8.250  59.745  1.00 101.92 ? 366 LYS B C   1 
ATOM 5397 O O   . LYS B 1 366 ? -2.674 -9.267  60.220  1.00 102.60 ? 366 LYS B O   1 
ATOM 5398 C CB  . LYS B 1 366 ? 0.052  -8.501  60.885  1.00 94.76  ? 366 LYS B CB  1 
ATOM 5399 C CG  . LYS B 1 366 ? 1.547  -8.749  60.763  1.00 91.64  ? 366 LYS B CG  1 
ATOM 5400 C CD  . LYS B 1 366 ? 2.248  -8.552  62.096  1.00 89.30  ? 366 LYS B CD  1 
ATOM 5401 C CE  . LYS B 1 366 ? 3.673  -8.066  61.905  1.00 83.95  ? 366 LYS B CE  1 
ATOM 5402 N NZ  . LYS B 1 366 ? 4.164  -7.319  63.097  1.00 84.79  ? 366 LYS B NZ  1 
ATOM 5403 N N   . ALA B 1 367 ? -2.863 -7.184  59.386  1.00 103.65 ? 367 ALA B N   1 
ATOM 5404 C CA  . ALA B 1 367 ? -4.317 -7.169  59.412  1.00 100.95 ? 367 ALA B CA  1 
ATOM 5405 C C   . ALA B 1 367 ? -4.866 -7.495  58.028  1.00 101.23 ? 367 ALA B C   1 
ATOM 5406 O O   . ALA B 1 367 ? -4.150 -7.397  57.029  1.00 100.19 ? 367 ALA B O   1 
ATOM 5407 C CB  . ALA B 1 367 ? -4.829 -5.818  59.890  1.00 92.74  ? 367 ALA B CB  1 
# 
