data_9B8M
# 
_entry.id   9B8M 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9B8M         pdb_00009b8m 10.2210/pdb9b8m/pdb 
WWPDB D_1000282831 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'Structure model' 1 1 2025-03-26 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9B8M 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-31 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
4 melcher.karsten@yahoo.com Karsten Melcher   ? 'principal investigator/group leader' 0000-0002-9125-4027 
5 bachma26@msu.edu          Andre   Bachmann  S 'principal investigator/group leader' 0000-0002-6510-8560 
6 ellswo59@msu.edu          Edmund  Ellsworth ? 'principal investigator/group leader' 0000-0001-5158-928X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Schultz, C.R.'    1  ? 
'Aleiwi, B.'       2  ? 
'Zhou, X.E.'       3  ? 
'Suino-Powell, K.' 4  ? 
'Melcher, K.'      5  ? 
'Brunzelle, J.S.'  6  ? 
'Almeida, N.M.S.'  7  ? 
'Wilson, A.K.'     8  ? 
'Ellsworth, E.'    9  ? 
'Bachmann, A.S.'   10 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                5760 
_citation.page_last                 5773 
_citation.title                     'Design, Synthesis, and Biological Activity of Novel Ornithine Decarboxylase (ODC) Inhibitors.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c03120 
_citation.pdbx_database_id_PubMed   40035393 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Schultz, C.R.'    1 ? 
primary 'Aleiwi, B.'       2 ? 
primary 'Zhou, X.E.'       3 ? 
primary 'Suino-Powell, K.' 4 ? 
primary 'Melcher, K.'      5 ? 
primary 'Almeida, N.M.S.'  6 ? 
primary 'Wilson, A.K.'     7 ? 
primary 'Ellsworth, E.L.'  8 ? 
primary 'Bachmann, A.S.'   9 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Ornithine decarboxylase'                       47029.414 2  4.1.1.17 ? ? ? 
2 non-polymer nat 'O-{[(3R)-pyrrolidin-3-yl]methyl}hydroxylamine' 116.162   2  ?        ? ? ? 
3 non-polymer syn "PYRIDOXAL-5'-PHOSPHATE"                        247.142   2  ?        ? ? ? 
4 water       nat water                                           18.015    16 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        ODC 
# 
_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       
;MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTL
AATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDS
KAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPG
SEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQTGSDDEDESSEQTFMYYVND
GVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGF
QRPTIYYVMSGPAWQLMQQFQN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTL
AATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDS
KAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPG
SEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQTGSDDEDESSEQTFMYYVND
GVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGF
QRPTIYYVMSGPAWQLMQQFQN
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'O-{[(3R)-pyrrolidin-3-yl]methyl}hydroxylamine' A1AQO 
3 "PYRIDOXAL-5'-PHOSPHATE"                        PLP   
4 water                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASN n 
1 3   ASN n 
1 4   PHE n 
1 5   GLY n 
1 6   ASN n 
1 7   GLU n 
1 8   GLU n 
1 9   PHE n 
1 10  ASP n 
1 11  CYS n 
1 12  HIS n 
1 13  PHE n 
1 14  LEU n 
1 15  ASP n 
1 16  GLU n 
1 17  GLY n 
1 18  PHE n 
1 19  THR n 
1 20  ALA n 
1 21  LYS n 
1 22  ASP n 
1 23  ILE n 
1 24  LEU n 
1 25  ASP n 
1 26  GLN n 
1 27  LYS n 
1 28  ILE n 
1 29  ASN n 
1 30  GLU n 
1 31  VAL n 
1 32  SER n 
1 33  SER n 
1 34  SER n 
1 35  ASP n 
1 36  ASP n 
1 37  LYS n 
1 38  ASP n 
1 39  ALA n 
1 40  PHE n 
1 41  TYR n 
1 42  VAL n 
1 43  ALA n 
1 44  ASP n 
1 45  LEU n 
1 46  GLY n 
1 47  ASP n 
1 48  ILE n 
1 49  LEU n 
1 50  LYS n 
1 51  LYS n 
1 52  HIS n 
1 53  LEU n 
1 54  ARG n 
1 55  TRP n 
1 56  LEU n 
1 57  LYS n 
1 58  ALA n 
1 59  LEU n 
1 60  PRO n 
1 61  ARG n 
1 62  VAL n 
1 63  THR n 
1 64  PRO n 
1 65  PHE n 
1 66  TYR n 
1 67  ALA n 
1 68  VAL n 
1 69  LYS n 
1 70  CYS n 
1 71  ASN n 
1 72  ASP n 
1 73  SER n 
1 74  LYS n 
1 75  ALA n 
1 76  ILE n 
1 77  VAL n 
1 78  LYS n 
1 79  THR n 
1 80  LEU n 
1 81  ALA n 
1 82  ALA n 
1 83  THR n 
1 84  GLY n 
1 85  THR n 
1 86  GLY n 
1 87  PHE n 
1 88  ASP n 
1 89  CYS n 
1 90  ALA n 
1 91  SER n 
1 92  LYS n 
1 93  THR n 
1 94  GLU n 
1 95  ILE n 
1 96  GLN n 
1 97  LEU n 
1 98  VAL n 
1 99  GLN n 
1 100 SER n 
1 101 LEU n 
1 102 GLY n 
1 103 VAL n 
1 104 PRO n 
1 105 PRO n 
1 106 GLU n 
1 107 ARG n 
1 108 ILE n 
1 109 ILE n 
1 110 TYR n 
1 111 ALA n 
1 112 ASN n 
1 113 PRO n 
1 114 CYS n 
1 115 LYS n 
1 116 GLN n 
1 117 VAL n 
1 118 SER n 
1 119 GLN n 
1 120 ILE n 
1 121 LYS n 
1 122 TYR n 
1 123 ALA n 
1 124 ALA n 
1 125 ASN n 
1 126 ASN n 
1 127 GLY n 
1 128 VAL n 
1 129 GLN n 
1 130 MET n 
1 131 MET n 
1 132 THR n 
1 133 PHE n 
1 134 ASP n 
1 135 SER n 
1 136 GLU n 
1 137 VAL n 
1 138 GLU n 
1 139 LEU n 
1 140 MET n 
1 141 LYS n 
1 142 VAL n 
1 143 ALA n 
1 144 ARG n 
1 145 ALA n 
1 146 HIS n 
1 147 PRO n 
1 148 LYS n 
1 149 ALA n 
1 150 LYS n 
1 151 LEU n 
1 152 VAL n 
1 153 LEU n 
1 154 ARG n 
1 155 ILE n 
1 156 ALA n 
1 157 THR n 
1 158 ASP n 
1 159 ASP n 
1 160 SER n 
1 161 LYS n 
1 162 ALA n 
1 163 VAL n 
1 164 CYS n 
1 165 ARG n 
1 166 LEU n 
1 167 SER n 
1 168 VAL n 
1 169 LYS n 
1 170 PHE n 
1 171 GLY n 
1 172 ALA n 
1 173 THR n 
1 174 LEU n 
1 175 ARG n 
1 176 THR n 
1 177 SER n 
1 178 ARG n 
1 179 LEU n 
1 180 LEU n 
1 181 LEU n 
1 182 GLU n 
1 183 ARG n 
1 184 ALA n 
1 185 LYS n 
1 186 GLU n 
1 187 LEU n 
1 188 ASN n 
1 189 ILE n 
1 190 ASP n 
1 191 VAL n 
1 192 VAL n 
1 193 GLY n 
1 194 VAL n 
1 195 SER n 
1 196 PHE n 
1 197 HIS n 
1 198 VAL n 
1 199 GLY n 
1 200 SER n 
1 201 GLY n 
1 202 CYS n 
1 203 THR n 
1 204 ASP n 
1 205 PRO n 
1 206 GLU n 
1 207 THR n 
1 208 PHE n 
1 209 VAL n 
1 210 GLN n 
1 211 ALA n 
1 212 ILE n 
1 213 SER n 
1 214 ASP n 
1 215 ALA n 
1 216 ARG n 
1 217 CYS n 
1 218 VAL n 
1 219 PHE n 
1 220 ASP n 
1 221 MET n 
1 222 GLY n 
1 223 ALA n 
1 224 GLU n 
1 225 VAL n 
1 226 GLY n 
1 227 PHE n 
1 228 SER n 
1 229 MET n 
1 230 TYR n 
1 231 LEU n 
1 232 LEU n 
1 233 ASP n 
1 234 ILE n 
1 235 GLY n 
1 236 GLY n 
1 237 GLY n 
1 238 PHE n 
1 239 PRO n 
1 240 GLY n 
1 241 SER n 
1 242 GLU n 
1 243 ASP n 
1 244 VAL n 
1 245 LYS n 
1 246 LEU n 
1 247 LYS n 
1 248 PHE n 
1 249 GLU n 
1 250 GLU n 
1 251 ILE n 
1 252 THR n 
1 253 GLY n 
1 254 VAL n 
1 255 ILE n 
1 256 ASN n 
1 257 PRO n 
1 258 ALA n 
1 259 LEU n 
1 260 ASP n 
1 261 LYS n 
1 262 TYR n 
1 263 PHE n 
1 264 PRO n 
1 265 SER n 
1 266 ASP n 
1 267 SER n 
1 268 GLY n 
1 269 VAL n 
1 270 ARG n 
1 271 ILE n 
1 272 ILE n 
1 273 ALA n 
1 274 GLU n 
1 275 PRO n 
1 276 GLY n 
1 277 ARG n 
1 278 TYR n 
1 279 TYR n 
1 280 VAL n 
1 281 ALA n 
1 282 SER n 
1 283 ALA n 
1 284 PHE n 
1 285 THR n 
1 286 LEU n 
1 287 ALA n 
1 288 VAL n 
1 289 ASN n 
1 290 ILE n 
1 291 ILE n 
1 292 ALA n 
1 293 LYS n 
1 294 LYS n 
1 295 ILE n 
1 296 VAL n 
1 297 LEU n 
1 298 LYS n 
1 299 GLU n 
1 300 GLN n 
1 301 THR n 
1 302 GLY n 
1 303 SER n 
1 304 ASP n 
1 305 ASP n 
1 306 GLU n 
1 307 ASP n 
1 308 GLU n 
1 309 SER n 
1 310 SER n 
1 311 GLU n 
1 312 GLN n 
1 313 THR n 
1 314 PHE n 
1 315 MET n 
1 316 TYR n 
1 317 TYR n 
1 318 VAL n 
1 319 ASN n 
1 320 ASP n 
1 321 GLY n 
1 322 VAL n 
1 323 TYR n 
1 324 GLY n 
1 325 SER n 
1 326 PHE n 
1 327 ASN n 
1 328 CYS n 
1 329 ILE n 
1 330 LEU n 
1 331 TYR n 
1 332 ASP n 
1 333 HIS n 
1 334 ALA n 
1 335 HIS n 
1 336 VAL n 
1 337 LYS n 
1 338 PRO n 
1 339 LEU n 
1 340 LEU n 
1 341 GLN n 
1 342 LYS n 
1 343 ARG n 
1 344 PRO n 
1 345 LYS n 
1 346 PRO n 
1 347 ASP n 
1 348 GLU n 
1 349 LYS n 
1 350 TYR n 
1 351 TYR n 
1 352 SER n 
1 353 SER n 
1 354 SER n 
1 355 ILE n 
1 356 TRP n 
1 357 GLY n 
1 358 PRO n 
1 359 THR n 
1 360 CYS n 
1 361 ASP n 
1 362 GLY n 
1 363 LEU n 
1 364 ASP n 
1 365 ARG n 
1 366 ILE n 
1 367 VAL n 
1 368 GLU n 
1 369 ARG n 
1 370 CYS n 
1 371 ASP n 
1 372 LEU n 
1 373 PRO n 
1 374 GLU n 
1 375 MET n 
1 376 HIS n 
1 377 VAL n 
1 378 GLY n 
1 379 ASP n 
1 380 TRP n 
1 381 MET n 
1 382 LEU n 
1 383 PHE n 
1 384 GLU n 
1 385 ASN n 
1 386 MET n 
1 387 GLY n 
1 388 ALA n 
1 389 TYR n 
1 390 THR n 
1 391 VAL n 
1 392 ALA n 
1 393 ALA n 
1 394 ALA n 
1 395 SER n 
1 396 THR n 
1 397 PHE n 
1 398 ASN n 
1 399 GLY n 
1 400 PHE n 
1 401 GLN n 
1 402 ARG n 
1 403 PRO n 
1 404 THR n 
1 405 ILE n 
1 406 TYR n 
1 407 TYR n 
1 408 VAL n 
1 409 MET n 
1 410 SER n 
1 411 GLY n 
1 412 PRO n 
1 413 ALA n 
1 414 TRP n 
1 415 GLN n 
1 416 LEU n 
1 417 MET n 
1 418 GLN n 
1 419 GLN n 
1 420 PHE n 
1 421 GLN n 
1 422 ASN 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                   422 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ODC1 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 
A1AQO non-polymer         . 'O-{[(3R)-pyrrolidin-3-yl]methyl}hydroxylamine' ?                      'C5 H12 N2 O'    116.162 
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 
HOH   non-polymer         . WATER                                           ?                      'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                      ?                      'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                         ?                      'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                          ?                      'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                      ?                      'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                   ?                      'C9 H11 N O2'    165.189 
PLP   non-polymer         . "PYRIDOXAL-5'-PHOSPHATE"                        'VITAMIN B6 Phosphate' 'C8 H10 N O6 P'  247.142 
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   ASN 2   2   ?   ?   ?   A . n 
A 1 3   ASN 3   3   ?   ?   ?   A . n 
A 1 4   PHE 4   4   ?   ?   ?   A . n 
A 1 5   GLY 5   5   ?   ?   ?   A . n 
A 1 6   ASN 6   6   6   ASN ASN A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   GLU 8   8   8   GLU GLU A . n 
A 1 9   PHE 9   9   9   PHE PHE A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  CYS 11  11  11  CYS CYS A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  PHE 13  13  13  PHE PHE A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  ASP 15  15  15  ASP ASP A . n 
A 1 16  GLU 16  16  16  GLU GLU A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  PHE 18  18  18  PHE PHE A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  LYS 21  21  21  LYS LYS A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  GLN 26  26  26  GLN GLN A . n 
A 1 27  LYS 27  27  27  LYS LYS A . n 
A 1 28  ILE 28  28  28  ILE ILE A . n 
A 1 29  ASN 29  29  29  ASN ASN A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  ASP 36  36  36  ASP ASP A . n 
A 1 37  LYS 37  37  37  LYS LYS A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  PHE 40  40  40  PHE PHE A . n 
A 1 41  TYR 41  41  41  TYR TYR A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  ILE 48  48  48  ILE ILE A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  HIS 52  52  52  HIS HIS A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ARG 54  54  54  ARG ARG A . n 
A 1 55  TRP 55  55  55  TRP TRP A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  PRO 64  64  64  PRO PRO A . n 
A 1 65  PHE 65  65  65  PHE PHE A . n 
A 1 66  TYR 66  66  66  TYR TYR A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  CYS 70  70  70  CYS CYS A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  LYS 74  74  74  LYS LYS A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  ILE 76  76  76  ILE ILE A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  THR 83  83  83  THR THR A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  ASP 88  88  88  ASP ASP A . n 
A 1 89  CYS 89  89  89  CYS CYS A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 PRO 105 105 105 PRO PRO A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 TYR 110 110 110 TYR TYR A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 ASN 112 112 112 ASN ASN A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 CYS 114 114 114 CYS CYS A . n 
A 1 115 LYS 115 115 115 LYS LYS A . n 
A 1 116 GLN 116 116 116 GLN GLN A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 GLN 119 119 119 GLN GLN A . n 
A 1 120 ILE 120 120 120 ILE ILE A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 TYR 122 122 122 TYR TYR A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 ASN 125 125 125 ASN ASN A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 GLN 129 129 129 GLN GLN A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 MET 131 131 131 MET MET A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 ASP 134 134 134 ASP ASP A . n 
A 1 135 SER 135 135 135 SER SER A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 MET 140 140 140 MET MET A . n 
A 1 141 LYS 141 141 141 LYS LYS A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 HIS 146 146 146 HIS HIS A . n 
A 1 147 PRO 147 147 147 PRO PRO A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 LYS 150 150 150 LYS LYS 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 LEU 153 153 153 LEU LEU A . n 
A 1 154 ARG 154 154 154 ARG ARG A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 ALA 156 156 156 ALA ALA A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 ASP 159 159 159 ASP ASP A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 LYS 161 161 161 LYS LYS A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 CYS 164 164 164 CYS CYS A . n 
A 1 165 ARG 165 165 165 ARG ARG A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 THR 173 173 173 THR THR A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 SER 177 177 177 SER SER A . n 
A 1 178 ARG 178 178 178 ARG ARG A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 LYS 185 185 185 LYS LYS A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 ILE 189 189 189 ILE ILE A . n 
A 1 190 ASP 190 190 190 ASP ASP A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 VAL 192 192 192 VAL VAL A . n 
A 1 193 GLY 193 193 193 GLY GLY A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 PHE 196 196 196 PHE PHE A . n 
A 1 197 HIS 197 197 197 HIS HIS A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 SER 200 200 200 SER SER A . n 
A 1 201 GLY 201 201 201 GLY GLY A . n 
A 1 202 CYS 202 202 202 CYS CYS A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 ASP 204 204 204 ASP ASP A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 GLU 206 206 206 GLU GLU A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 PHE 208 208 208 PHE PHE A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 GLN 210 210 210 GLN GLN A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 ARG 216 216 216 ARG ARG A . n 
A 1 217 CYS 217 217 217 CYS CYS A . n 
A 1 218 VAL 218 218 218 VAL VAL A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 MET 221 221 221 MET MET A . n 
A 1 222 GLY 222 222 222 GLY GLY A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 GLY 226 226 226 GLY GLY A . n 
A 1 227 PHE 227 227 227 PHE PHE A . n 
A 1 228 SER 228 228 228 SER SER A . n 
A 1 229 MET 229 229 229 MET MET A . n 
A 1 230 TYR 230 230 230 TYR TYR A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 ASP 233 233 233 ASP ASP A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 PHE 238 238 238 PHE PHE A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 SER 241 241 241 SER SER A . n 
A 1 242 GLU 242 242 242 GLU GLU A . n 
A 1 243 ASP 243 243 243 ASP ASP A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 LYS 245 245 245 LYS LYS A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 LYS 247 247 247 LYS LYS A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 GLU 249 249 249 GLU GLU A . n 
A 1 250 GLU 250 250 250 GLU GLU A . n 
A 1 251 ILE 251 251 251 ILE ILE A . n 
A 1 252 THR 252 252 252 THR THR A . n 
A 1 253 GLY 253 253 253 GLY GLY A . n 
A 1 254 VAL 254 254 254 VAL VAL A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 ASN 256 256 256 ASN ASN A . n 
A 1 257 PRO 257 257 257 PRO PRO A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 LYS 261 261 261 LYS LYS A . n 
A 1 262 TYR 262 262 262 TYR TYR A . n 
A 1 263 PHE 263 263 263 PHE PHE A . n 
A 1 264 PRO 264 264 264 PRO PRO A . n 
A 1 265 SER 265 265 265 SER SER A . n 
A 1 266 ASP 266 266 266 ASP ASP A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 GLY 268 268 268 GLY GLY A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 ARG 270 270 270 ARG ARG A . n 
A 1 271 ILE 271 271 271 ILE ILE A . n 
A 1 272 ILE 272 272 272 ILE ILE A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 GLU 274 274 274 GLU GLU A . n 
A 1 275 PRO 275 275 275 PRO PRO A . n 
A 1 276 GLY 276 276 276 GLY GLY A . n 
A 1 277 ARG 277 277 277 ARG ARG A . n 
A 1 278 TYR 278 278 278 TYR TYR A . n 
A 1 279 TYR 279 279 279 TYR TYR A . n 
A 1 280 VAL 280 280 280 VAL VAL A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 SER 282 282 282 SER SER A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 PHE 284 284 284 PHE PHE A . n 
A 1 285 THR 285 285 285 THR THR A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 VAL 288 288 288 VAL VAL A . n 
A 1 289 ASN 289 289 289 ASN ASN A . n 
A 1 290 ILE 290 290 290 ILE ILE A . n 
A 1 291 ILE 291 291 291 ILE ILE A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 LYS 293 293 293 LYS LYS A . n 
A 1 294 LYS 294 294 294 LYS LYS A . n 
A 1 295 ILE 295 295 295 ILE ILE A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 LEU 297 297 297 LEU LEU A . n 
A 1 298 LYS 298 298 298 LYS LYS A . n 
A 1 299 GLU 299 299 ?   ?   ?   A . n 
A 1 300 GLN 300 300 ?   ?   ?   A . n 
A 1 301 THR 301 301 ?   ?   ?   A . n 
A 1 302 GLY 302 302 ?   ?   ?   A . n 
A 1 303 SER 303 303 ?   ?   ?   A . n 
A 1 304 ASP 304 304 ?   ?   ?   A . n 
A 1 305 ASP 305 305 ?   ?   ?   A . n 
A 1 306 GLU 306 306 ?   ?   ?   A . n 
A 1 307 ASP 307 307 ?   ?   ?   A . n 
A 1 308 GLU 308 308 ?   ?   ?   A . n 
A 1 309 SER 309 309 ?   ?   ?   A . n 
A 1 310 SER 310 310 ?   ?   ?   A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 GLN 312 312 312 GLN GLN A . n 
A 1 313 THR 313 313 313 THR THR A . n 
A 1 314 PHE 314 314 314 PHE PHE A . n 
A 1 315 MET 315 315 315 MET MET A . n 
A 1 316 TYR 316 316 316 TYR TYR A . n 
A 1 317 TYR 317 317 317 TYR TYR A . n 
A 1 318 VAL 318 318 318 VAL VAL A . n 
A 1 319 ASN 319 319 319 ASN ASN A . n 
A 1 320 ASP 320 320 320 ASP ASP A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 VAL 322 322 322 VAL VAL A . n 
A 1 323 TYR 323 323 323 TYR TYR A . n 
A 1 324 GLY 324 324 324 GLY GLY A . n 
A 1 325 SER 325 325 325 SER SER A . n 
A 1 326 PHE 326 326 326 PHE PHE A . n 
A 1 327 ASN 327 327 327 ASN ASN A . n 
A 1 328 CYS 328 328 328 CYS CYS A . n 
A 1 329 ILE 329 329 329 ILE ILE A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 TYR 331 331 331 TYR TYR A . n 
A 1 332 ASP 332 332 332 ASP ASP A . n 
A 1 333 HIS 333 333 333 HIS HIS A . n 
A 1 334 ALA 334 334 334 ALA ALA A . n 
A 1 335 HIS 335 335 335 HIS HIS A . n 
A 1 336 VAL 336 336 336 VAL VAL A . n 
A 1 337 LYS 337 337 337 LYS LYS A . n 
A 1 338 PRO 338 338 338 PRO PRO 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 GLN 341 341 341 GLN GLN A . n 
A 1 342 LYS 342 342 342 LYS LYS A . n 
A 1 343 ARG 343 343 343 ARG ARG A . n 
A 1 344 PRO 344 344 344 PRO PRO A . n 
A 1 345 LYS 345 345 345 LYS LYS 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 GLU 348 348 348 GLU GLU A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 TYR 350 350 350 TYR TYR A . n 
A 1 351 TYR 351 351 351 TYR TYR A . n 
A 1 352 SER 352 352 352 SER SER A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 SER 354 354 354 SER SER A . n 
A 1 355 ILE 355 355 355 ILE ILE A . n 
A 1 356 TRP 356 356 356 TRP TRP A . n 
A 1 357 GLY 357 357 357 GLY GLY A . n 
A 1 358 PRO 358 358 358 PRO PRO A . n 
A 1 359 THR 359 359 359 THR THR A . n 
A 1 360 CYS 360 360 360 CYS CYS A . n 
A 1 361 ASP 361 361 361 ASP ASP A . n 
A 1 362 GLY 362 362 362 GLY GLY A . n 
A 1 363 LEU 363 363 363 LEU LEU A . n 
A 1 364 ASP 364 364 364 ASP ASP A . n 
A 1 365 ARG 365 365 365 ARG ARG A . n 
A 1 366 ILE 366 366 366 ILE ILE A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 GLU 368 368 368 GLU GLU A . n 
A 1 369 ARG 369 369 369 ARG ARG A . n 
A 1 370 CYS 370 370 370 CYS CYS A . n 
A 1 371 ASP 371 371 371 ASP ASP A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 PRO 373 373 373 PRO PRO A . n 
A 1 374 GLU 374 374 374 GLU GLU A . n 
A 1 375 MET 375 375 375 MET MET A . n 
A 1 376 HIS 376 376 376 HIS HIS A . n 
A 1 377 VAL 377 377 377 VAL VAL A . n 
A 1 378 GLY 378 378 378 GLY GLY A . n 
A 1 379 ASP 379 379 379 ASP ASP A . n 
A 1 380 TRP 380 380 380 TRP TRP A . n 
A 1 381 MET 381 381 381 MET MET A . n 
A 1 382 LEU 382 382 382 LEU LEU A . n 
A 1 383 PHE 383 383 383 PHE PHE A . n 
A 1 384 GLU 384 384 384 GLU GLU A . n 
A 1 385 ASN 385 385 385 ASN ASN A . n 
A 1 386 MET 386 386 386 MET MET A . n 
A 1 387 GLY 387 387 387 GLY GLY A . n 
A 1 388 ALA 388 388 388 ALA ALA A . n 
A 1 389 TYR 389 389 389 TYR TYR A . n 
A 1 390 THR 390 390 390 THR THR A . n 
A 1 391 VAL 391 391 391 VAL VAL A . n 
A 1 392 ALA 392 392 392 ALA ALA A . n 
A 1 393 ALA 393 393 393 ALA ALA A . n 
A 1 394 ALA 394 394 394 ALA ALA A . n 
A 1 395 SER 395 395 395 SER SER A . n 
A 1 396 THR 396 396 396 THR THR A . n 
A 1 397 PHE 397 397 397 PHE PHE A . n 
A 1 398 ASN 398 398 398 ASN ASN A . n 
A 1 399 GLY 399 399 399 GLY GLY A . n 
A 1 400 PHE 400 400 400 PHE PHE A . n 
A 1 401 GLN 401 401 401 GLN GLN A . n 
A 1 402 ARG 402 402 402 ARG ARG A . n 
A 1 403 PRO 403 403 403 PRO PRO A . n 
A 1 404 THR 404 404 404 THR THR A . n 
A 1 405 ILE 405 405 405 ILE ILE A . n 
A 1 406 TYR 406 406 406 TYR TYR A . n 
A 1 407 TYR 407 407 407 TYR TYR A . n 
A 1 408 VAL 408 408 408 VAL VAL A . n 
A 1 409 MET 409 409 409 MET MET A . n 
A 1 410 SER 410 410 410 SER SER A . n 
A 1 411 GLY 411 411 411 GLY GLY A . n 
A 1 412 PRO 412 412 412 PRO PRO A . n 
A 1 413 ALA 413 413 413 ALA ALA A . n 
A 1 414 TRP 414 414 414 TRP TRP A . n 
A 1 415 GLN 415 415 415 GLN GLN A . n 
A 1 416 LEU 416 416 416 LEU LEU A . n 
A 1 417 MET 417 417 417 MET MET A . n 
A 1 418 GLN 418 418 418 GLN GLN A . n 
A 1 419 GLN 419 419 419 GLN GLN A . n 
A 1 420 PHE 420 420 420 PHE PHE A . n 
A 1 421 GLN 421 421 421 GLN GLN A . n 
A 1 422 ASN 422 422 422 ASN ASN A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   ASN 2   2   2   ASN ASN B . n 
B 1 3   ASN 3   3   3   ASN ASN B . n 
B 1 4   PHE 4   4   4   PHE PHE B . n 
B 1 5   GLY 5   5   5   GLY GLY B . n 
B 1 6   ASN 6   6   6   ASN ASN B . n 
B 1 7   GLU 7   7   7   GLU GLU B . n 
B 1 8   GLU 8   8   8   GLU GLU B . n 
B 1 9   PHE 9   9   9   PHE PHE B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  CYS 11  11  11  CYS CYS B . n 
B 1 12  HIS 12  12  12  HIS HIS B . n 
B 1 13  PHE 13  13  13  PHE PHE B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  ASP 15  15  15  ASP ASP B . n 
B 1 16  GLU 16  16  16  GLU GLU B . n 
B 1 17  GLY 17  17  17  GLY GLY B . n 
B 1 18  PHE 18  18  18  PHE PHE B . n 
B 1 19  THR 19  19  19  THR THR B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  LYS 21  21  21  LYS LYS B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  LEU 24  24  24  LEU LEU B . n 
B 1 25  ASP 25  25  25  ASP ASP B . n 
B 1 26  GLN 26  26  26  GLN GLN B . n 
B 1 27  LYS 27  27  27  LYS LYS B . n 
B 1 28  ILE 28  28  28  ILE ILE B . n 
B 1 29  ASN 29  29  29  ASN ASN B . n 
B 1 30  GLU 30  30  30  GLU GLU B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  SER 32  32  32  SER SER B . n 
B 1 33  SER 33  33  33  SER SER B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ASP 35  35  35  ASP ASP B . n 
B 1 36  ASP 36  36  36  ASP ASP B . n 
B 1 37  LYS 37  37  37  LYS LYS B . n 
B 1 38  ASP 38  38  38  ASP ASP B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  PHE 40  40  40  PHE PHE B . n 
B 1 41  TYR 41  41  41  TYR TYR B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  ASP 44  44  44  ASP ASP B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  ILE 48  48  48  ILE ILE B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  LYS 50  50  50  LYS LYS B . n 
B 1 51  LYS 51  51  51  LYS LYS B . n 
B 1 52  HIS 52  52  52  HIS HIS B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ARG 54  54  54  ARG ARG B . n 
B 1 55  TRP 55  55  55  TRP TRP B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  LYS 57  57  57  LYS LYS B . n 
B 1 58  ALA 58  58  58  ALA ALA B . n 
B 1 59  LEU 59  59  59  LEU LEU B . n 
B 1 60  PRO 60  60  60  PRO PRO B . n 
B 1 61  ARG 61  61  61  ARG ARG B . n 
B 1 62  VAL 62  62  62  VAL VAL B . n 
B 1 63  THR 63  63  63  THR THR B . n 
B 1 64  PRO 64  64  64  PRO PRO B . n 
B 1 65  PHE 65  65  65  PHE PHE B . n 
B 1 66  TYR 66  66  66  TYR TYR B . n 
B 1 67  ALA 67  67  67  ALA ALA B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  CYS 70  70  70  CYS CYS B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  LYS 74  74  74  LYS LYS B . n 
B 1 75  ALA 75  75  75  ALA ALA B . n 
B 1 76  ILE 76  76  76  ILE ILE B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  THR 79  79  79  THR THR B . n 
B 1 80  LEU 80  80  80  LEU LEU B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  THR 83  83  83  THR THR B . n 
B 1 84  GLY 84  84  84  GLY GLY B . n 
B 1 85  THR 85  85  85  THR THR B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  PHE 87  87  87  PHE PHE B . n 
B 1 88  ASP 88  88  88  ASP ASP B . n 
B 1 89  CYS 89  89  89  CYS CYS B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  SER 91  91  91  SER SER B . n 
B 1 92  LYS 92  92  92  LYS LYS B . n 
B 1 93  THR 93  93  93  THR THR B . n 
B 1 94  GLU 94  94  94  GLU GLU B . n 
B 1 95  ILE 95  95  95  ILE ILE B . n 
B 1 96  GLN 96  96  96  GLN GLN B . n 
B 1 97  LEU 97  97  97  LEU LEU B . n 
B 1 98  VAL 98  98  98  VAL VAL B . n 
B 1 99  GLN 99  99  99  GLN GLN B . n 
B 1 100 SER 100 100 100 SER SER B . n 
B 1 101 LEU 101 101 101 LEU LEU B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 PRO 104 104 104 PRO PRO B . n 
B 1 105 PRO 105 105 105 PRO PRO B . n 
B 1 106 GLU 106 106 106 GLU GLU B . n 
B 1 107 ARG 107 107 107 ARG ARG B . n 
B 1 108 ILE 108 108 108 ILE ILE B . n 
B 1 109 ILE 109 109 109 ILE ILE B . n 
B 1 110 TYR 110 110 110 TYR TYR B . n 
B 1 111 ALA 111 111 111 ALA ALA B . n 
B 1 112 ASN 112 112 112 ASN ASN B . n 
B 1 113 PRO 113 113 113 PRO PRO B . n 
B 1 114 CYS 114 114 114 CYS CYS B . n 
B 1 115 LYS 115 115 115 LYS LYS B . n 
B 1 116 GLN 116 116 116 GLN GLN B . n 
B 1 117 VAL 117 117 117 VAL VAL B . n 
B 1 118 SER 118 118 118 SER SER B . n 
B 1 119 GLN 119 119 119 GLN GLN B . n 
B 1 120 ILE 120 120 120 ILE ILE B . n 
B 1 121 LYS 121 121 121 LYS LYS B . n 
B 1 122 TYR 122 122 122 TYR TYR B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 ASN 125 125 125 ASN ASN B . n 
B 1 126 ASN 126 126 126 ASN ASN B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 VAL 128 128 128 VAL VAL B . n 
B 1 129 GLN 129 129 129 GLN GLN B . n 
B 1 130 MET 130 130 130 MET MET B . n 
B 1 131 MET 131 131 131 MET MET B . n 
B 1 132 THR 132 132 132 THR THR B . n 
B 1 133 PHE 133 133 133 PHE PHE B . n 
B 1 134 ASP 134 134 134 ASP ASP B . n 
B 1 135 SER 135 135 135 SER SER B . n 
B 1 136 GLU 136 136 136 GLU GLU B . n 
B 1 137 VAL 137 137 137 VAL VAL B . n 
B 1 138 GLU 138 138 138 GLU GLU B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 MET 140 140 140 MET MET B . n 
B 1 141 LYS 141 141 141 LYS LYS B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 ARG 144 144 144 ARG ARG B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 HIS 146 146 146 HIS HIS B . n 
B 1 147 PRO 147 147 147 PRO PRO B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 ALA 149 149 149 ALA ALA B . n 
B 1 150 LYS 150 150 150 LYS LYS 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 LEU 153 153 153 LEU LEU B . n 
B 1 154 ARG 154 154 154 ARG ARG B . n 
B 1 155 ILE 155 155 155 ILE ILE B . n 
B 1 156 ALA 156 156 156 ALA ALA B . n 
B 1 157 THR 157 157 157 THR THR B . n 
B 1 158 ASP 158 158 158 ASP ASP B . n 
B 1 159 ASP 159 159 ?   ?   ?   B . n 
B 1 160 SER 160 160 ?   ?   ?   B . n 
B 1 161 LYS 161 161 ?   ?   ?   B . n 
B 1 162 ALA 162 162 ?   ?   ?   B . n 
B 1 163 VAL 163 163 ?   ?   ?   B . n 
B 1 164 CYS 164 164 ?   ?   ?   B . n 
B 1 165 ARG 165 165 ?   ?   ?   B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 LYS 169 169 169 LYS LYS B . n 
B 1 170 PHE 170 170 170 PHE PHE B . n 
B 1 171 GLY 171 171 171 GLY GLY B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 THR 173 173 173 THR THR B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 ARG 175 175 175 ARG ARG B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 SER 177 177 177 SER SER B . n 
B 1 178 ARG 178 178 178 ARG ARG B . n 
B 1 179 LEU 179 179 179 LEU LEU B . n 
B 1 180 LEU 180 180 180 LEU LEU B . n 
B 1 181 LEU 181 181 181 LEU LEU B . n 
B 1 182 GLU 182 182 182 GLU GLU B . n 
B 1 183 ARG 183 183 183 ARG ARG B . n 
B 1 184 ALA 184 184 184 ALA ALA B . n 
B 1 185 LYS 185 185 185 LYS LYS B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 LEU 187 187 187 LEU LEU B . n 
B 1 188 ASN 188 188 188 ASN ASN B . n 
B 1 189 ILE 189 189 189 ILE ILE B . n 
B 1 190 ASP 190 190 190 ASP ASP B . n 
B 1 191 VAL 191 191 191 VAL VAL B . n 
B 1 192 VAL 192 192 192 VAL VAL B . n 
B 1 193 GLY 193 193 193 GLY GLY B . n 
B 1 194 VAL 194 194 194 VAL VAL B . n 
B 1 195 SER 195 195 195 SER SER B . n 
B 1 196 PHE 196 196 196 PHE PHE B . n 
B 1 197 HIS 197 197 197 HIS HIS B . n 
B 1 198 VAL 198 198 198 VAL VAL B . n 
B 1 199 GLY 199 199 199 GLY GLY B . n 
B 1 200 SER 200 200 200 SER SER B . n 
B 1 201 GLY 201 201 201 GLY GLY B . n 
B 1 202 CYS 202 202 202 CYS CYS B . n 
B 1 203 THR 203 203 203 THR THR B . n 
B 1 204 ASP 204 204 204 ASP ASP B . n 
B 1 205 PRO 205 205 205 PRO PRO B . n 
B 1 206 GLU 206 206 206 GLU GLU B . n 
B 1 207 THR 207 207 207 THR THR B . n 
B 1 208 PHE 208 208 208 PHE PHE B . n 
B 1 209 VAL 209 209 209 VAL VAL B . n 
B 1 210 GLN 210 210 210 GLN GLN B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 ILE 212 212 212 ILE ILE B . n 
B 1 213 SER 213 213 213 SER SER B . n 
B 1 214 ASP 214 214 214 ASP ASP B . n 
B 1 215 ALA 215 215 215 ALA ALA B . n 
B 1 216 ARG 216 216 216 ARG ARG B . n 
B 1 217 CYS 217 217 217 CYS CYS B . n 
B 1 218 VAL 218 218 218 VAL VAL B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 ASP 220 220 220 ASP ASP B . n 
B 1 221 MET 221 221 221 MET MET B . n 
B 1 222 GLY 222 222 222 GLY GLY B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 GLU 224 224 224 GLU GLU B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 GLY 226 226 226 GLY GLY B . n 
B 1 227 PHE 227 227 227 PHE PHE B . n 
B 1 228 SER 228 228 228 SER SER B . n 
B 1 229 MET 229 229 229 MET MET B . n 
B 1 230 TYR 230 230 230 TYR TYR B . n 
B 1 231 LEU 231 231 231 LEU LEU B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 ASP 233 233 233 ASP ASP B . n 
B 1 234 ILE 234 234 234 ILE ILE B . n 
B 1 235 GLY 235 235 235 GLY GLY B . n 
B 1 236 GLY 236 236 236 GLY GLY B . n 
B 1 237 GLY 237 237 237 GLY GLY B . n 
B 1 238 PHE 238 238 238 PHE PHE B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 GLY 240 240 240 GLY GLY B . n 
B 1 241 SER 241 241 241 SER SER B . n 
B 1 242 GLU 242 242 242 GLU GLU B . n 
B 1 243 ASP 243 243 243 ASP ASP B . n 
B 1 244 VAL 244 244 244 VAL VAL B . n 
B 1 245 LYS 245 245 245 LYS LYS B . n 
B 1 246 LEU 246 246 246 LEU LEU B . n 
B 1 247 LYS 247 247 247 LYS LYS B . n 
B 1 248 PHE 248 248 248 PHE PHE B . n 
B 1 249 GLU 249 249 249 GLU GLU B . n 
B 1 250 GLU 250 250 250 GLU GLU B . n 
B 1 251 ILE 251 251 251 ILE ILE B . n 
B 1 252 THR 252 252 252 THR THR B . n 
B 1 253 GLY 253 253 253 GLY GLY B . n 
B 1 254 VAL 254 254 254 VAL VAL B . n 
B 1 255 ILE 255 255 255 ILE ILE B . n 
B 1 256 ASN 256 256 256 ASN ASN B . n 
B 1 257 PRO 257 257 257 PRO PRO B . n 
B 1 258 ALA 258 258 258 ALA ALA B . n 
B 1 259 LEU 259 259 259 LEU LEU B . n 
B 1 260 ASP 260 260 260 ASP ASP B . n 
B 1 261 LYS 261 261 261 LYS LYS B . n 
B 1 262 TYR 262 262 262 TYR TYR B . n 
B 1 263 PHE 263 263 263 PHE PHE B . n 
B 1 264 PRO 264 264 264 PRO PRO B . n 
B 1 265 SER 265 265 265 SER SER B . n 
B 1 266 ASP 266 266 266 ASP ASP B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 GLY 268 268 268 GLY GLY B . n 
B 1 269 VAL 269 269 269 VAL VAL B . n 
B 1 270 ARG 270 270 270 ARG ARG B . n 
B 1 271 ILE 271 271 271 ILE ILE B . n 
B 1 272 ILE 272 272 272 ILE ILE B . n 
B 1 273 ALA 273 273 273 ALA ALA B . n 
B 1 274 GLU 274 274 274 GLU GLU B . n 
B 1 275 PRO 275 275 275 PRO PRO B . n 
B 1 276 GLY 276 276 276 GLY GLY B . n 
B 1 277 ARG 277 277 277 ARG ARG B . n 
B 1 278 TYR 278 278 278 TYR TYR B . n 
B 1 279 TYR 279 279 279 TYR TYR B . n 
B 1 280 VAL 280 280 280 VAL VAL B . n 
B 1 281 ALA 281 281 281 ALA ALA B . n 
B 1 282 SER 282 282 282 SER SER B . n 
B 1 283 ALA 283 283 283 ALA ALA B . n 
B 1 284 PHE 284 284 284 PHE PHE B . n 
B 1 285 THR 285 285 285 THR THR B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 ALA 287 287 287 ALA ALA B . n 
B 1 288 VAL 288 288 288 VAL VAL B . n 
B 1 289 ASN 289 289 289 ASN ASN B . n 
B 1 290 ILE 290 290 290 ILE ILE B . n 
B 1 291 ILE 291 291 291 ILE ILE B . n 
B 1 292 ALA 292 292 292 ALA ALA B . n 
B 1 293 LYS 293 293 293 LYS LYS B . n 
B 1 294 LYS 294 294 294 LYS LYS B . n 
B 1 295 ILE 295 295 295 ILE ILE B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 LEU 297 297 297 LEU LEU B . n 
B 1 298 LYS 298 298 298 LYS LYS B . n 
B 1 299 GLU 299 299 299 GLU GLU B . n 
B 1 300 GLN 300 300 ?   ?   ?   B . n 
B 1 301 THR 301 301 ?   ?   ?   B . n 
B 1 302 GLY 302 302 ?   ?   ?   B . n 
B 1 303 SER 303 303 ?   ?   ?   B . n 
B 1 304 ASP 304 304 ?   ?   ?   B . n 
B 1 305 ASP 305 305 ?   ?   ?   B . n 
B 1 306 GLU 306 306 ?   ?   ?   B . n 
B 1 307 ASP 307 307 ?   ?   ?   B . n 
B 1 308 GLU 308 308 ?   ?   ?   B . n 
B 1 309 SER 309 309 ?   ?   ?   B . n 
B 1 310 SER 310 310 310 SER SER B . n 
B 1 311 GLU 311 311 311 GLU GLU B . n 
B 1 312 GLN 312 312 312 GLN GLN B . n 
B 1 313 THR 313 313 313 THR THR B . n 
B 1 314 PHE 314 314 314 PHE PHE B . n 
B 1 315 MET 315 315 315 MET MET B . n 
B 1 316 TYR 316 316 316 TYR TYR B . n 
B 1 317 TYR 317 317 317 TYR TYR B . n 
B 1 318 VAL 318 318 318 VAL VAL B . n 
B 1 319 ASN 319 319 319 ASN ASN B . n 
B 1 320 ASP 320 320 320 ASP ASP B . n 
B 1 321 GLY 321 321 321 GLY GLY B . n 
B 1 322 VAL 322 322 322 VAL VAL B . n 
B 1 323 TYR 323 323 323 TYR TYR B . n 
B 1 324 GLY 324 324 324 GLY GLY B . n 
B 1 325 SER 325 325 325 SER SER B . n 
B 1 326 PHE 326 326 326 PHE PHE B . n 
B 1 327 ASN 327 327 327 ASN ASN B . n 
B 1 328 CYS 328 328 328 CYS CYS B . n 
B 1 329 ILE 329 329 329 ILE ILE B . n 
B 1 330 LEU 330 330 330 LEU LEU B . n 
B 1 331 TYR 331 331 331 TYR TYR B . n 
B 1 332 ASP 332 332 332 ASP ASP B . n 
B 1 333 HIS 333 333 333 HIS HIS B . n 
B 1 334 ALA 334 334 334 ALA ALA B . n 
B 1 335 HIS 335 335 335 HIS HIS B . n 
B 1 336 VAL 336 336 336 VAL VAL B . n 
B 1 337 LYS 337 337 337 LYS LYS B . n 
B 1 338 PRO 338 338 338 PRO PRO 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 GLN 341 341 341 GLN GLN B . n 
B 1 342 LYS 342 342 342 LYS LYS B . n 
B 1 343 ARG 343 343 343 ARG ARG B . n 
B 1 344 PRO 344 344 344 PRO PRO B . n 
B 1 345 LYS 345 345 345 LYS LYS 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 GLU 348 348 348 GLU GLU B . n 
B 1 349 LYS 349 349 349 LYS LYS B . n 
B 1 350 TYR 350 350 350 TYR TYR B . n 
B 1 351 TYR 351 351 351 TYR TYR B . n 
B 1 352 SER 352 352 352 SER SER B . n 
B 1 353 SER 353 353 353 SER SER B . n 
B 1 354 SER 354 354 354 SER SER B . n 
B 1 355 ILE 355 355 355 ILE ILE B . n 
B 1 356 TRP 356 356 356 TRP TRP B . n 
B 1 357 GLY 357 357 357 GLY GLY B . n 
B 1 358 PRO 358 358 358 PRO PRO B . n 
B 1 359 THR 359 359 359 THR THR B . n 
B 1 360 CYS 360 360 360 CYS CYS B . n 
B 1 361 ASP 361 361 361 ASP ASP B . n 
B 1 362 GLY 362 362 362 GLY GLY B . n 
B 1 363 LEU 363 363 363 LEU LEU B . n 
B 1 364 ASP 364 364 364 ASP ASP B . n 
B 1 365 ARG 365 365 365 ARG ARG B . n 
B 1 366 ILE 366 366 366 ILE ILE B . n 
B 1 367 VAL 367 367 367 VAL VAL B . n 
B 1 368 GLU 368 368 368 GLU GLU B . n 
B 1 369 ARG 369 369 369 ARG ARG B . n 
B 1 370 CYS 370 370 370 CYS CYS B . n 
B 1 371 ASP 371 371 371 ASP ASP B . n 
B 1 372 LEU 372 372 372 LEU LEU B . n 
B 1 373 PRO 373 373 373 PRO PRO B . n 
B 1 374 GLU 374 374 374 GLU GLU B . n 
B 1 375 MET 375 375 375 MET MET B . n 
B 1 376 HIS 376 376 376 HIS HIS B . n 
B 1 377 VAL 377 377 377 VAL VAL B . n 
B 1 378 GLY 378 378 378 GLY GLY B . n 
B 1 379 ASP 379 379 379 ASP ASP B . n 
B 1 380 TRP 380 380 380 TRP TRP B . n 
B 1 381 MET 381 381 381 MET MET B . n 
B 1 382 LEU 382 382 382 LEU LEU B . n 
B 1 383 PHE 383 383 383 PHE PHE B . n 
B 1 384 GLU 384 384 384 GLU GLU B . n 
B 1 385 ASN 385 385 385 ASN ASN B . n 
B 1 386 MET 386 386 386 MET MET B . n 
B 1 387 GLY 387 387 387 GLY GLY B . n 
B 1 388 ALA 388 388 388 ALA ALA B . n 
B 1 389 TYR 389 389 389 TYR TYR B . n 
B 1 390 THR 390 390 390 THR THR B . n 
B 1 391 VAL 391 391 391 VAL VAL B . n 
B 1 392 ALA 392 392 392 ALA ALA B . n 
B 1 393 ALA 393 393 393 ALA ALA B . n 
B 1 394 ALA 394 394 394 ALA ALA B . n 
B 1 395 SER 395 395 395 SER SER B . n 
B 1 396 THR 396 396 396 THR THR B . n 
B 1 397 PHE 397 397 397 PHE PHE B . n 
B 1 398 ASN 398 398 398 ASN ASN B . n 
B 1 399 GLY 399 399 399 GLY GLY B . n 
B 1 400 PHE 400 400 400 PHE PHE B . n 
B 1 401 GLN 401 401 401 GLN GLN B . n 
B 1 402 ARG 402 402 402 ARG ARG B . n 
B 1 403 PRO 403 403 403 PRO PRO B . n 
B 1 404 THR 404 404 404 THR THR B . n 
B 1 405 ILE 405 405 405 ILE ILE B . n 
B 1 406 TYR 406 406 406 TYR TYR B . n 
B 1 407 TYR 407 407 407 TYR TYR B . n 
B 1 408 VAL 408 408 408 VAL VAL B . n 
B 1 409 MET 409 409 409 MET MET B . n 
B 1 410 SER 410 410 410 SER SER B . n 
B 1 411 GLY 411 411 411 GLY GLY B . n 
B 1 412 PRO 412 412 412 PRO PRO B . n 
B 1 413 ALA 413 413 413 ALA ALA B . n 
B 1 414 TRP 414 414 414 TRP TRP B . n 
B 1 415 GLN 415 415 415 GLN GLN B . n 
B 1 416 LEU 416 416 416 LEU LEU B . n 
B 1 417 MET 417 417 417 MET MET B . n 
B 1 418 GLN 418 418 418 GLN GLN B . n 
B 1 419 GLN 419 419 419 GLN GLN B . n 
B 1 420 PHE 420 420 420 PHE PHE B . n 
B 1 421 GLN 421 421 421 GLN GLN B . n 
B 1 422 ASN 422 422 422 ASN ASN B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AQO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AQO 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1AQO 1 501 600 A1AQO M32 A . 
D 3 PLP   1 502 500 PLP   PLP A . 
E 2 A1AQO 1 501 600 A1AQO M32 B . 
F 3 PLP   1 502 500 PLP   PLP B . 
G 4 HOH   1 601 13  HOH   HOH A . 
G 4 HOH   2 602 4   HOH   HOH A . 
G 4 HOH   3 603 14  HOH   HOH A . 
G 4 HOH   4 604 10  HOH   HOH A . 
G 4 HOH   5 605 3   HOH   HOH A . 
G 4 HOH   6 606 7   HOH   HOH A . 
G 4 HOH   7 607 12  HOH   HOH A . 
H 4 HOH   1 601 1   HOH   HOH B . 
H 4 HOH   2 602 8   HOH   HOH B . 
H 4 HOH   3 603 5   HOH   HOH B . 
H 4 HOH   4 604 11  HOH   HOH B . 
H 4 HOH   5 605 2   HOH   HOH B . 
H 4 HOH   6 606 6   HOH   HOH B . 
H 4 HOH   7 607 15  HOH   HOH B . 
H 4 HOH   8 608 16  HOH   HOH B . 
H 4 HOH   9 609 9   HOH   HOH B . 
# 
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 ? ? ? '(1.13_2998: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9B8M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.650 
_cell.length_a_esd                 ? 
_cell.length_b                     86.430 
_cell.length_b_esd                 ? 
_cell.length_c                     153.220 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9B8M 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9B8M 
_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             2.72 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.79 
_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, SITTING 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    'Not available' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-02-14 
_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   1 
_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                        'APS BEAMLINE 21-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9B8M 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.9 
_reflns.d_resolution_low                               31.78 
_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                                     22613 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.9 
_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                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.9 
_reflns_shell.d_res_low                                     2.98 
_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                             1652 
_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                                  0.58 
_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                                 9B8M 
_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                            2.900 
_refine.ls_d_res_low                             31.78 
_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                     22546 
_refine.ls_number_reflns_R_free                  1108 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.66 
_refine.ls_percent_reflns_R_free                 4.91 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1951 
_refine.ls_R_factor_R_free                       0.2229 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1937 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.00 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 24.49 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.40 
_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                       2.900 
_refine_hist.d_res_low                        31.78 
_refine_hist.number_atoms_solvent             16 
_refine_hist.number_atoms_total               6408 
_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        6376 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         16 
_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' ? 0.003  ? 6534 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.618  ? 8843 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.363 ? 3896 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.043  ? 972  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 1133 ? 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' 2.9001 3.0320 . . 131 2647 100.00 . . . . 0.3143 . . . . . . . . . . . 0.3686 
'X-RAY DIFFRACTION' 3.0320 3.1917 . . 135 2648 100.00 . . . . 0.2603 . . . . . . . . . . . 0.3595 
'X-RAY DIFFRACTION' 3.1917 3.3915 . . 136 2624 99.00  . . . . 0.2375 . . . . . . . . . . . 0.3102 
'X-RAY DIFFRACTION' 3.3915 3.6530 . . 152 2630 100.00 . . . . 0.2210 . . . . . . . . . . . 0.2696 
'X-RAY DIFFRACTION' 3.6530 4.0199 . . 138 2653 100.00 . . . . 0.1850 . . . . . . . . . . . 0.2329 
'X-RAY DIFFRACTION' 4.0199 4.6001 . . 154 2691 100.00 . . . . 0.1579 . . . . . . . . . . . 0.1916 
'X-RAY DIFFRACTION' 4.6001 5.7899 . . 125 2736 100.00 . . . . 0.1726 . . . . . . . . . . . 0.1640 
'X-RAY DIFFRACTION' 5.7899 31.70  . . 137 2809 99.00  . . . . 0.1790 . . . . . . . . . . . 0.1846 
# 
_struct.entry_id                     9B8M 
_struct.title                        'Crystal structure of ornithine decarboxylase in complex with a novel inhibitor' 
_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        9B8M 
_struct_keywords.text            'analogs, drug inhibitors, DFMO, CARBOHYDRATE' 
_struct_keywords.pdbx_keywords   CARBOHYDRATE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DCOR_HUMAN 
_struct_ref.pdbx_db_accession          P11926 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTL
AATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDS
KAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPG
SEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQTGSDDEDESSEQTFMYYVND
GVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGF
QRPTIYYVMSGPAWQLMQQFQN
;
_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 9B8M A 1 ? 422 ? P11926 1 ? 422 ? 1 422 
2 1 9B8M B 1 ? 422 ? P11926 1 ? 422 ? 1 422 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6970  ? 
1 MORE         -27   ? 
1 'SSA (A^2)'  33010 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_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 THR A 19  ? VAL A 31  ? THR A 19  VAL A 31  1 ? 13 
HELX_P HELX_P2  AA2 LEU A 45  ? LEU A 59  ? LEU A 45  LEU A 59  1 ? 15 
HELX_P HELX_P3  AA3 LYS A 69  ? ASN A 71  ? LYS A 69  ASN A 71  5 ? 3  
HELX_P HELX_P4  AA4 SER A 73  ? GLY A 84  ? SER A 73  GLY A 84  1 ? 12 
HELX_P HELX_P5  AA5 SER A 91  ? LEU A 101 ? SER A 91  LEU A 101 1 ? 11 
HELX_P HELX_P6  AA6 PRO A 104 ? GLU A 106 ? PRO A 104 GLU A 106 5 ? 3  
HELX_P HELX_P7  AA7 GLN A 116 ? ASN A 126 ? GLN A 116 ASN A 126 1 ? 11 
HELX_P HELX_P8  AA8 SER A 135 ? HIS A 146 ? SER A 135 HIS A 146 1 ? 12 
HELX_P HELX_P9  AA9 THR A 173 ? LEU A 187 ? THR A 173 LEU A 187 1 ? 15 
HELX_P HELX_P10 AB1 PRO A 205 ? GLY A 226 ? PRO A 205 GLY A 226 1 ? 22 
HELX_P HELX_P11 AB2 LYS A 247 ? PHE A 263 ? LYS A 247 PHE A 263 1 ? 17 
HELX_P HELX_P12 AB3 PRO A 264 ? GLY A 268 ? PRO A 264 GLY A 268 5 ? 5  
HELX_P HELX_P13 AB4 GLY A 276 ? ALA A 281 ? GLY A 276 ALA A 281 1 ? 6  
HELX_P HELX_P14 AB5 GLY A 324 ? LEU A 330 ? GLY A 324 LEU A 330 5 ? 7  
HELX_P HELX_P15 AB6 THR A 396 ? PHE A 400 ? THR A 396 PHE A 400 5 ? 5  
HELX_P HELX_P16 AB7 GLY A 411 ? ASN A 422 ? GLY A 411 ASN A 422 1 ? 12 
HELX_P HELX_P17 AB8 THR B 19  ? VAL B 31  ? THR B 19  VAL B 31  1 ? 13 
HELX_P HELX_P18 AB9 LEU B 45  ? LEU B 59  ? LEU B 45  LEU B 59  1 ? 15 
HELX_P HELX_P19 AC1 SER B 73  ? GLY B 84  ? SER B 73  GLY B 84  1 ? 12 
HELX_P HELX_P20 AC2 SER B 91  ? LEU B 101 ? SER B 91  LEU B 101 1 ? 11 
HELX_P HELX_P21 AC3 PRO B 104 ? GLU B 106 ? PRO B 104 GLU B 106 5 ? 3  
HELX_P HELX_P22 AC4 GLN B 116 ? ASN B 126 ? GLN B 116 ASN B 126 1 ? 11 
HELX_P HELX_P23 AC5 SER B 135 ? HIS B 146 ? SER B 135 HIS B 146 1 ? 12 
HELX_P HELX_P24 AC6 THR B 173 ? LEU B 187 ? THR B 173 LEU B 187 1 ? 15 
HELX_P HELX_P25 AC7 PRO B 205 ? GLY B 226 ? PRO B 205 GLY B 226 1 ? 22 
HELX_P HELX_P26 AC8 LYS B 247 ? PHE B 263 ? LYS B 247 PHE B 263 1 ? 17 
HELX_P HELX_P27 AC9 PRO B 264 ? GLY B 268 ? PRO B 264 GLY B 268 5 ? 5  
HELX_P HELX_P28 AD1 GLY B 276 ? ALA B 281 ? GLY B 276 ALA B 281 1 ? 6  
HELX_P HELX_P29 AD2 GLY B 324 ? PHE B 326 ? GLY B 324 PHE B 326 5 ? 3  
HELX_P HELX_P30 AD3 ASN B 327 ? ASP B 332 ? ASN B 327 ASP B 332 1 ? 6  
HELX_P HELX_P31 AD4 THR B 396 ? PHE B 400 ? THR B 396 PHE B 400 5 ? 5  
HELX_P HELX_P32 AD5 GLY B 411 ? ASN B 422 ? GLY B 411 ASN B 422 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale one ? C A1AQO . N02 ? ? ? 1_555 D PLP . C4A ? ? A A1AQO 501 A PLP 502 1_555 ? ? ? ? ? ? ? 1.285 ? ? 
covale2 covale one ? E A1AQO . N02 ? ? ? 1_555 F PLP . C4A ? ? B A1AQO 501 B PLP 502 1_555 ? ? ? ? ? ? ? 1.283 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 7 ? 
AA3 ? 9 ? 
AA4 ? 6 ? 
AA5 ? 7 ? 
AA6 ? 9 ? 
# 
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 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA3 7 8 ? parallel      
AA3 8 9 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? parallel      
AA5 6 7 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? parallel      
AA6 6 7 ? parallel      
AA6 7 8 ? parallel      
AA6 8 9 ? parallel      
# 
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 CYS A 11  ? LEU A 14  ? CYS A 11  LEU A 14  
AA1 2 THR A 404 ? SER A 410 ? THR A 404 SER A 410 
AA1 3 PHE A 40  ? ASP A 44  ? PHE A 40  ASP A 44  
AA1 4 PHE A 284 ? VAL A 296 ? PHE A 284 VAL A 296 
AA1 5 TRP A 380 ? PHE A 383 ? TRP A 380 PHE A 383 
AA1 6 LEU A 339 ? LEU A 340 ? LEU A 339 LEU A 340 
AA2 1 CYS A 11  ? LEU A 14  ? CYS A 11  LEU A 14  
AA2 2 THR A 404 ? SER A 410 ? THR A 404 SER A 410 
AA2 3 PHE A 40  ? ASP A 44  ? PHE A 40  ASP A 44  
AA2 4 PHE A 284 ? VAL A 296 ? PHE A 284 VAL A 296 
AA2 5 THR A 313 ? VAL A 318 ? THR A 313 VAL A 318 
AA2 6 TYR A 351 ? TRP A 356 ? TYR A 351 TRP A 356 
AA2 7 ARG A 365 ? LEU A 372 ? ARG A 365 LEU A 372 
AA3 1 VAL A 62  ? ALA A 67  ? VAL A 62  ALA A 67  
AA3 2 GLY A 86  ? CYS A 89  ? GLY A 86  CYS A 89  
AA3 3 ILE A 108 ? TYR A 110 ? ILE A 108 TYR A 110 
AA3 4 MET A 130 ? PHE A 133 ? MET A 130 PHE A 133 
AA3 5 LYS A 150 ? ARG A 154 ? LYS A 150 ARG A 154 
AA3 6 ASP A 190 ? SER A 195 ? ASP A 190 SER A 195 
AA3 7 LEU A 231 ? ASP A 233 ? LEU A 231 ASP A 233 
AA3 8 ARG A 270 ? ALA A 273 ? ARG A 270 ALA A 273 
AA3 9 VAL A 62  ? ALA A 67  ? VAL A 62  ALA A 67  
AA4 1 CYS B 11  ? LEU B 14  ? CYS B 11  LEU B 14  
AA4 2 THR B 404 ? SER B 410 ? THR B 404 SER B 410 
AA4 3 PHE B 40  ? ASP B 44  ? PHE B 40  ASP B 44  
AA4 4 PHE B 284 ? LYS B 298 ? PHE B 284 LYS B 298 
AA4 5 TRP B 380 ? PHE B 383 ? TRP B 380 PHE B 383 
AA4 6 LEU B 339 ? LEU B 340 ? LEU B 339 LEU B 340 
AA5 1 CYS B 11  ? LEU B 14  ? CYS B 11  LEU B 14  
AA5 2 THR B 404 ? SER B 410 ? THR B 404 SER B 410 
AA5 3 PHE B 40  ? ASP B 44  ? PHE B 40  ASP B 44  
AA5 4 PHE B 284 ? LYS B 298 ? PHE B 284 LYS B 298 
AA5 5 GLU B 311 ? VAL B 318 ? GLU B 311 VAL B 318 
AA5 6 TYR B 350 ? TRP B 356 ? TYR B 350 TRP B 356 
AA5 7 ARG B 365 ? PRO B 373 ? ARG B 365 PRO B 373 
AA6 1 VAL B 62  ? ALA B 67  ? VAL B 62  ALA B 67  
AA6 2 GLY B 86  ? CYS B 89  ? GLY B 86  CYS B 89  
AA6 3 ILE B 108 ? TYR B 110 ? ILE B 108 TYR B 110 
AA6 4 MET B 130 ? PHE B 133 ? MET B 130 PHE B 133 
AA6 5 LYS B 150 ? ARG B 154 ? LYS B 150 ARG B 154 
AA6 6 ASP B 190 ? SER B 195 ? ASP B 190 SER B 195 
AA6 7 LEU B 231 ? ASP B 233 ? LEU B 231 ASP B 233 
AA6 8 ARG B 270 ? ALA B 273 ? ARG B 270 ALA B 273 
AA6 9 VAL B 62  ? ALA B 67  ? VAL B 62  ALA B 67  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N HIS A 12  ? N HIS A 12  O TYR A 407 ? O TYR A 407 
AA1 2 3 O TYR A 406 ? O TYR A 406 N TYR A 41  ? N TYR A 41  
AA1 3 4 N PHE A 40  ? N PHE A 40  O ALA A 287 ? O ALA A 287 
AA1 4 5 N LEU A 286 ? N LEU A 286 O PHE A 383 ? O PHE A 383 
AA1 5 6 O LEU A 382 ? O LEU A 382 N LEU A 339 ? N LEU A 339 
AA2 1 2 N HIS A 12  ? N HIS A 12  O TYR A 407 ? O TYR A 407 
AA2 2 3 O TYR A 406 ? O TYR A 406 N TYR A 41  ? N TYR A 41  
AA2 3 4 N PHE A 40  ? N PHE A 40  O ALA A 287 ? O ALA A 287 
AA2 4 5 N LYS A 294 ? N LYS A 294 O MET A 315 ? O MET A 315 
AA2 5 6 N TYR A 316 ? N TYR A 316 O SER A 354 ? O SER A 354 
AA2 6 7 N TYR A 351 ? N TYR A 351 O LEU A 372 ? O LEU A 372 
AA3 1 2 N TYR A 66  ? N TYR A 66  O ASP A 88  ? O ASP A 88  
AA3 2 3 N CYS A 89  ? N CYS A 89  O ILE A 109 ? O ILE A 109 
AA3 3 4 N TYR A 110 ? N TYR A 110 O MET A 130 ? O MET A 130 
AA3 4 5 N PHE A 133 ? N PHE A 133 O ARG A 154 ? O ARG A 154 
AA3 5 6 N LEU A 151 ? N LEU A 151 O ASP A 190 ? O ASP A 190 
AA3 6 7 O VAL A 192 ? O VAL A 192 N LEU A 231 ? N LEU A 231 
AA3 7 8 N LEU A 232 ? N LEU A 232 O ILE A 272 ? O ILE A 272 
AA3 8 9 O ILE A 271 ? O ILE A 271 N THR A 63  ? N THR A 63  
AA4 1 2 N HIS B 12  ? N HIS B 12  O TYR B 407 ? O TYR B 407 
AA4 2 3 O VAL B 408 ? O VAL B 408 N ALA B 43  ? N ALA B 43  
AA4 3 4 N PHE B 40  ? N PHE B 40  O ALA B 287 ? O ALA B 287 
AA4 4 5 N LEU B 286 ? N LEU B 286 O PHE B 383 ? O PHE B 383 
AA4 5 6 O LEU B 382 ? O LEU B 382 N LEU B 339 ? N LEU B 339 
AA5 1 2 N HIS B 12  ? N HIS B 12  O TYR B 407 ? O TYR B 407 
AA5 2 3 O VAL B 408 ? O VAL B 408 N ALA B 43  ? N ALA B 43  
AA5 3 4 N PHE B 40  ? N PHE B 40  O ALA B 287 ? O ALA B 287 
AA5 4 5 N VAL B 296 ? N VAL B 296 O THR B 313 ? O THR B 313 
AA5 5 6 N TYR B 316 ? N TYR B 316 O SER B 354 ? O SER B 354 
AA5 6 7 N ILE B 355 ? N ILE B 355 O VAL B 367 ? O VAL B 367 
AA6 1 2 N TYR B 66  ? N TYR B 66  O ASP B 88  ? O ASP B 88  
AA6 2 3 N PHE B 87  ? N PHE B 87  O ILE B 109 ? O ILE B 109 
AA6 3 4 N TYR B 110 ? N TYR B 110 O MET B 130 ? O MET B 130 
AA6 4 5 N PHE B 133 ? N PHE B 133 O ARG B 154 ? O ARG B 154 
AA6 5 6 N LEU B 151 ? N LEU B 151 O ASP B 190 ? O ASP B 190 
AA6 6 7 N VAL B 194 ? N VAL B 194 O ASP B 233 ? O ASP B 233 
AA6 7 8 N LEU B 232 ? N LEU B 232 O ILE B 272 ? O ILE B 272 
AA6 8 9 O ILE B 271 ? O ILE B 271 N THR B 63  ? N THR B 63  
# 
_pdbx_entry_details.entry_id                   9B8M 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OG 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    352 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    601 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.11 
# 
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 ASP A 35  ? ? 79.38   -1.51 
2 1 ALA A 111 ? ? -91.41  52.51 
3 1 ASP A 134 ? ? -143.60 19.42 
4 1 HIS A 146 ? ? -152.16 62.98 
5 1 ASN A 319 ? ? -95.36  31.60 
6 1 ALA B 111 ? ? -85.24  48.63 
7 1 ASP B 134 ? ? -143.57 20.40 
8 1 HIS B 146 ? ? -153.10 70.19 
9 1 ASN B 319 ? ? -95.51  31.40 
# 
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 ASN 2   ? A ASN 2   
3  1 Y 1 A ASN 3   ? A ASN 3   
4  1 Y 1 A PHE 4   ? A PHE 4   
5  1 Y 1 A GLY 5   ? A GLY 5   
6  1 Y 1 A GLU 299 ? A GLU 299 
7  1 Y 1 A GLN 300 ? A GLN 300 
8  1 Y 1 A THR 301 ? A THR 301 
9  1 Y 1 A GLY 302 ? A GLY 302 
10 1 Y 1 A SER 303 ? A SER 303 
11 1 Y 1 A ASP 304 ? A ASP 304 
12 1 Y 1 A ASP 305 ? A ASP 305 
13 1 Y 1 A GLU 306 ? A GLU 306 
14 1 Y 1 A ASP 307 ? A ASP 307 
15 1 Y 1 A GLU 308 ? A GLU 308 
16 1 Y 1 A SER 309 ? A SER 309 
17 1 Y 1 A SER 310 ? A SER 310 
18 1 Y 1 B ASP 159 ? B ASP 159 
19 1 Y 1 B SER 160 ? B SER 160 
20 1 Y 1 B LYS 161 ? B LYS 161 
21 1 Y 1 B ALA 162 ? B ALA 162 
22 1 Y 1 B VAL 163 ? B VAL 163 
23 1 Y 1 B CYS 164 ? B CYS 164 
24 1 Y 1 B ARG 165 ? B ARG 165 
25 1 Y 1 B GLN 300 ? B GLN 300 
26 1 Y 1 B THR 301 ? B THR 301 
27 1 Y 1 B GLY 302 ? B GLY 302 
28 1 Y 1 B SER 303 ? B SER 303 
29 1 Y 1 B ASP 304 ? B ASP 304 
30 1 Y 1 B ASP 305 ? B ASP 305 
31 1 Y 1 B GLU 306 ? B GLU 306 
32 1 Y 1 B ASP 307 ? B ASP 307 
33 1 Y 1 B GLU 308 ? B GLU 308 
34 1 Y 1 B SER 309 ? B SER 309 
# 
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 
A1AQO C01  C N N 1   
A1AQO C02  C N N 2   
A1AQO C03  C N N 3   
A1AQO C04  C N R 4   
A1AQO C05  C N N 5   
A1AQO N01  N N N 6   
A1AQO N02  N N N 7   
A1AQO O01  O N N 8   
A1AQO H1   H N N 9   
A1AQO H2   H N N 10  
A1AQO H3   H N N 11  
A1AQO H4   H N N 12  
A1AQO H5   H N N 13  
A1AQO H6   H N N 14  
A1AQO H7   H N N 15  
A1AQO H8   H N N 16  
A1AQO H9   H N N 17  
A1AQO H10  H N N 18  
A1AQO H12  H N N 19  
A1AQO H13  H N N 20  
ALA   N    N N N 21  
ALA   CA   C N S 22  
ALA   C    C N N 23  
ALA   O    O N N 24  
ALA   CB   C N N 25  
ALA   OXT  O N N 26  
ALA   H    H N N 27  
ALA   H2   H N N 28  
ALA   HA   H N N 29  
ALA   HB1  H N N 30  
ALA   HB2  H N N 31  
ALA   HB3  H N N 32  
ALA   HXT  H N N 33  
ARG   N    N N N 34  
ARG   CA   C N S 35  
ARG   C    C N N 36  
ARG   O    O N N 37  
ARG   CB   C N N 38  
ARG   CG   C N N 39  
ARG   CD   C N N 40  
ARG   NE   N N N 41  
ARG   CZ   C N N 42  
ARG   NH1  N N N 43  
ARG   NH2  N N N 44  
ARG   OXT  O N N 45  
ARG   H    H N N 46  
ARG   H2   H N N 47  
ARG   HA   H N N 48  
ARG   HB2  H N N 49  
ARG   HB3  H N N 50  
ARG   HG2  H N N 51  
ARG   HG3  H N N 52  
ARG   HD2  H N N 53  
ARG   HD3  H N N 54  
ARG   HE   H N N 55  
ARG   HH11 H N N 56  
ARG   HH12 H N N 57  
ARG   HH21 H N N 58  
ARG   HH22 H N N 59  
ARG   HXT  H N N 60  
ASN   N    N N N 61  
ASN   CA   C N S 62  
ASN   C    C N N 63  
ASN   O    O N N 64  
ASN   CB   C N N 65  
ASN   CG   C N N 66  
ASN   OD1  O N N 67  
ASN   ND2  N N N 68  
ASN   OXT  O N N 69  
ASN   H    H N N 70  
ASN   H2   H N N 71  
ASN   HA   H N N 72  
ASN   HB2  H N N 73  
ASN   HB3  H N N 74  
ASN   HD21 H N N 75  
ASN   HD22 H N N 76  
ASN   HXT  H N N 77  
ASP   N    N N N 78  
ASP   CA   C N S 79  
ASP   C    C N N 80  
ASP   O    O N N 81  
ASP   CB   C N N 82  
ASP   CG   C N N 83  
ASP   OD1  O N N 84  
ASP   OD2  O N N 85  
ASP   OXT  O N N 86  
ASP   H    H N N 87  
ASP   H2   H N N 88  
ASP   HA   H N N 89  
ASP   HB2  H N N 90  
ASP   HB3  H N N 91  
ASP   HD2  H N N 92  
ASP   HXT  H N N 93  
CYS   N    N N N 94  
CYS   CA   C N R 95  
CYS   C    C N N 96  
CYS   O    O N N 97  
CYS   CB   C N N 98  
CYS   SG   S N N 99  
CYS   OXT  O N N 100 
CYS   H    H N N 101 
CYS   H2   H N N 102 
CYS   HA   H N N 103 
CYS   HB2  H N N 104 
CYS   HB3  H N N 105 
CYS   HG   H N N 106 
CYS   HXT  H N N 107 
GLN   N    N N N 108 
GLN   CA   C N S 109 
GLN   C    C N N 110 
GLN   O    O N N 111 
GLN   CB   C N N 112 
GLN   CG   C N N 113 
GLN   CD   C N N 114 
GLN   OE1  O N N 115 
GLN   NE2  N N N 116 
GLN   OXT  O N N 117 
GLN   H    H N N 118 
GLN   H2   H N N 119 
GLN   HA   H N N 120 
GLN   HB2  H N N 121 
GLN   HB3  H N N 122 
GLN   HG2  H N N 123 
GLN   HG3  H N N 124 
GLN   HE21 H N N 125 
GLN   HE22 H N N 126 
GLN   HXT  H N N 127 
GLU   N    N N N 128 
GLU   CA   C N S 129 
GLU   C    C N N 130 
GLU   O    O N N 131 
GLU   CB   C N N 132 
GLU   CG   C N N 133 
GLU   CD   C N N 134 
GLU   OE1  O N N 135 
GLU   OE2  O N N 136 
GLU   OXT  O N N 137 
GLU   H    H N N 138 
GLU   H2   H N N 139 
GLU   HA   H N N 140 
GLU   HB2  H N N 141 
GLU   HB3  H N N 142 
GLU   HG2  H N N 143 
GLU   HG3  H N N 144 
GLU   HE2  H N N 145 
GLU   HXT  H N N 146 
GLY   N    N N N 147 
GLY   CA   C N N 148 
GLY   C    C N N 149 
GLY   O    O N N 150 
GLY   OXT  O N N 151 
GLY   H    H N N 152 
GLY   H2   H N N 153 
GLY   HA2  H N N 154 
GLY   HA3  H N N 155 
GLY   HXT  H N N 156 
HIS   N    N N N 157 
HIS   CA   C N S 158 
HIS   C    C N N 159 
HIS   O    O N N 160 
HIS   CB   C N N 161 
HIS   CG   C Y N 162 
HIS   ND1  N Y N 163 
HIS   CD2  C Y N 164 
HIS   CE1  C Y N 165 
HIS   NE2  N Y N 166 
HIS   OXT  O N N 167 
HIS   H    H N N 168 
HIS   H2   H N N 169 
HIS   HA   H N N 170 
HIS   HB2  H N N 171 
HIS   HB3  H N N 172 
HIS   HD1  H N N 173 
HIS   HD2  H N N 174 
HIS   HE1  H N N 175 
HIS   HE2  H N N 176 
HIS   HXT  H N N 177 
HOH   O    O N N 178 
HOH   H1   H N N 179 
HOH   H2   H N N 180 
ILE   N    N N N 181 
ILE   CA   C N S 182 
ILE   C    C N N 183 
ILE   O    O N N 184 
ILE   CB   C N S 185 
ILE   CG1  C N N 186 
ILE   CG2  C N N 187 
ILE   CD1  C N N 188 
ILE   OXT  O N N 189 
ILE   H    H N N 190 
ILE   H2   H N N 191 
ILE   HA   H N N 192 
ILE   HB   H N N 193 
ILE   HG12 H N N 194 
ILE   HG13 H N N 195 
ILE   HG21 H N N 196 
ILE   HG22 H N N 197 
ILE   HG23 H N N 198 
ILE   HD11 H N N 199 
ILE   HD12 H N N 200 
ILE   HD13 H N N 201 
ILE   HXT  H N N 202 
LEU   N    N N N 203 
LEU   CA   C N S 204 
LEU   C    C N N 205 
LEU   O    O N N 206 
LEU   CB   C N N 207 
LEU   CG   C N N 208 
LEU   CD1  C N N 209 
LEU   CD2  C N N 210 
LEU   OXT  O N N 211 
LEU   H    H N N 212 
LEU   H2   H N N 213 
LEU   HA   H N N 214 
LEU   HB2  H N N 215 
LEU   HB3  H N N 216 
LEU   HG   H N N 217 
LEU   HD11 H N N 218 
LEU   HD12 H N N 219 
LEU   HD13 H N N 220 
LEU   HD21 H N N 221 
LEU   HD22 H N N 222 
LEU   HD23 H N N 223 
LEU   HXT  H N N 224 
LYS   N    N N N 225 
LYS   CA   C N S 226 
LYS   C    C N N 227 
LYS   O    O N N 228 
LYS   CB   C N N 229 
LYS   CG   C N N 230 
LYS   CD   C N N 231 
LYS   CE   C N N 232 
LYS   NZ   N N N 233 
LYS   OXT  O N N 234 
LYS   H    H N N 235 
LYS   H2   H N N 236 
LYS   HA   H N N 237 
LYS   HB2  H N N 238 
LYS   HB3  H N N 239 
LYS   HG2  H N N 240 
LYS   HG3  H N N 241 
LYS   HD2  H N N 242 
LYS   HD3  H N N 243 
LYS   HE2  H N N 244 
LYS   HE3  H N N 245 
LYS   HZ1  H N N 246 
LYS   HZ2  H N N 247 
LYS   HZ3  H N N 248 
LYS   HXT  H N N 249 
MET   N    N N N 250 
MET   CA   C N S 251 
MET   C    C N N 252 
MET   O    O N N 253 
MET   CB   C N N 254 
MET   CG   C N N 255 
MET   SD   S N N 256 
MET   CE   C N N 257 
MET   OXT  O N N 258 
MET   H    H N N 259 
MET   H2   H N N 260 
MET   HA   H N N 261 
MET   HB2  H N N 262 
MET   HB3  H N N 263 
MET   HG2  H N N 264 
MET   HG3  H N N 265 
MET   HE1  H N N 266 
MET   HE2  H N N 267 
MET   HE3  H N N 268 
MET   HXT  H N N 269 
PHE   N    N N N 270 
PHE   CA   C N S 271 
PHE   C    C N N 272 
PHE   O    O N N 273 
PHE   CB   C N N 274 
PHE   CG   C Y N 275 
PHE   CD1  C Y N 276 
PHE   CD2  C Y N 277 
PHE   CE1  C Y N 278 
PHE   CE2  C Y N 279 
PHE   CZ   C Y N 280 
PHE   OXT  O N N 281 
PHE   H    H N N 282 
PHE   H2   H N N 283 
PHE   HA   H N N 284 
PHE   HB2  H N N 285 
PHE   HB3  H N N 286 
PHE   HD1  H N N 287 
PHE   HD2  H N N 288 
PHE   HE1  H N N 289 
PHE   HE2  H N N 290 
PHE   HZ   H N N 291 
PHE   HXT  H N N 292 
PLP   N1   N Y N 293 
PLP   C2   C Y N 294 
PLP   C2A  C N N 295 
PLP   C3   C Y N 296 
PLP   O3   O N N 297 
PLP   C4   C Y N 298 
PLP   C4A  C N N 299 
PLP   O4A  O N N 300 
PLP   C5   C Y N 301 
PLP   C6   C Y N 302 
PLP   C5A  C N N 303 
PLP   O4P  O N N 304 
PLP   P    P N N 305 
PLP   O1P  O N N 306 
PLP   O2P  O N N 307 
PLP   O3P  O N N 308 
PLP   H2A1 H N N 309 
PLP   H2A2 H N N 310 
PLP   H2A3 H N N 311 
PLP   HO3  H N N 312 
PLP   H4A  H N N 313 
PLP   H6   H N N 314 
PLP   H5A1 H N N 315 
PLP   H5A2 H N N 316 
PLP   HOP2 H N N 317 
PLP   HOP3 H N N 318 
PRO   N    N N N 319 
PRO   CA   C N S 320 
PRO   C    C N N 321 
PRO   O    O N N 322 
PRO   CB   C N N 323 
PRO   CG   C N N 324 
PRO   CD   C N N 325 
PRO   OXT  O N N 326 
PRO   H    H N N 327 
PRO   HA   H N N 328 
PRO   HB2  H N N 329 
PRO   HB3  H N N 330 
PRO   HG2  H N N 331 
PRO   HG3  H N N 332 
PRO   HD2  H N N 333 
PRO   HD3  H N N 334 
PRO   HXT  H N N 335 
SER   N    N N N 336 
SER   CA   C N S 337 
SER   C    C N N 338 
SER   O    O N N 339 
SER   CB   C N N 340 
SER   OG   O N N 341 
SER   OXT  O N N 342 
SER   H    H N N 343 
SER   H2   H N N 344 
SER   HA   H N N 345 
SER   HB2  H N N 346 
SER   HB3  H N N 347 
SER   HG   H N N 348 
SER   HXT  H N N 349 
THR   N    N N N 350 
THR   CA   C N S 351 
THR   C    C N N 352 
THR   O    O N N 353 
THR   CB   C N R 354 
THR   OG1  O N N 355 
THR   CG2  C N N 356 
THR   OXT  O N N 357 
THR   H    H N N 358 
THR   H2   H N N 359 
THR   HA   H N N 360 
THR   HB   H N N 361 
THR   HG1  H N N 362 
THR   HG21 H N N 363 
THR   HG22 H N N 364 
THR   HG23 H N N 365 
THR   HXT  H N N 366 
TRP   N    N N N 367 
TRP   CA   C N S 368 
TRP   C    C N N 369 
TRP   O    O N N 370 
TRP   CB   C N N 371 
TRP   CG   C Y N 372 
TRP   CD1  C Y N 373 
TRP   CD2  C Y N 374 
TRP   NE1  N Y N 375 
TRP   CE2  C Y N 376 
TRP   CE3  C Y N 377 
TRP   CZ2  C Y N 378 
TRP   CZ3  C Y N 379 
TRP   CH2  C Y N 380 
TRP   OXT  O N N 381 
TRP   H    H N N 382 
TRP   H2   H N N 383 
TRP   HA   H N N 384 
TRP   HB2  H N N 385 
TRP   HB3  H N N 386 
TRP   HD1  H N N 387 
TRP   HE1  H N N 388 
TRP   HE3  H N N 389 
TRP   HZ2  H N N 390 
TRP   HZ3  H N N 391 
TRP   HH2  H N N 392 
TRP   HXT  H N N 393 
TYR   N    N N N 394 
TYR   CA   C N S 395 
TYR   C    C N N 396 
TYR   O    O N N 397 
TYR   CB   C N N 398 
TYR   CG   C Y N 399 
TYR   CD1  C Y N 400 
TYR   CD2  C Y N 401 
TYR   CE1  C Y N 402 
TYR   CE2  C Y N 403 
TYR   CZ   C Y N 404 
TYR   OH   O N N 405 
TYR   OXT  O N N 406 
TYR   H    H N N 407 
TYR   H2   H N N 408 
TYR   HA   H N N 409 
TYR   HB2  H N N 410 
TYR   HB3  H N N 411 
TYR   HD1  H N N 412 
TYR   HD2  H N N 413 
TYR   HE1  H N N 414 
TYR   HE2  H N N 415 
TYR   HH   H N N 416 
TYR   HXT  H N N 417 
VAL   N    N N N 418 
VAL   CA   C N S 419 
VAL   C    C N N 420 
VAL   O    O N N 421 
VAL   CB   C N N 422 
VAL   CG1  C N N 423 
VAL   CG2  C N N 424 
VAL   OXT  O N N 425 
VAL   H    H N N 426 
VAL   H2   H N N 427 
VAL   HA   H N N 428 
VAL   HB   H N N 429 
VAL   HG11 H N N 430 
VAL   HG12 H N N 431 
VAL   HG13 H N N 432 
VAL   HG21 H N N 433 
VAL   HG22 H N N 434 
VAL   HG23 H N N 435 
VAL   HXT  H N N 436 
# 
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 
A1AQO C02 N01  sing N N 1   
A1AQO C02 C04  sing N N 2   
A1AQO C01 N01  sing N N 3   
A1AQO C01 C03  sing N N 4   
A1AQO C04 C03  sing N N 5   
A1AQO C04 C05  sing N N 6   
A1AQO O01 C05  sing N N 7   
A1AQO O01 N02  sing N N 8   
A1AQO C01 H1   sing N N 9   
A1AQO C01 H2   sing N N 10  
A1AQO C02 H3   sing N N 11  
A1AQO C02 H4   sing N N 12  
A1AQO C03 H5   sing N N 13  
A1AQO C03 H6   sing N N 14  
A1AQO C04 H7   sing N N 15  
A1AQO C05 H8   sing N N 16  
A1AQO C05 H9   sing N N 17  
A1AQO N01 H10  sing N N 18  
A1AQO N02 H12  sing N N 19  
A1AQO N02 H13  sing N N 20  
ALA   N   CA   sing N N 21  
ALA   N   H    sing N N 22  
ALA   N   H2   sing N N 23  
ALA   CA  C    sing N N 24  
ALA   CA  CB   sing N N 25  
ALA   CA  HA   sing N N 26  
ALA   C   O    doub N N 27  
ALA   C   OXT  sing N N 28  
ALA   CB  HB1  sing N N 29  
ALA   CB  HB2  sing N N 30  
ALA   CB  HB3  sing N N 31  
ALA   OXT HXT  sing N N 32  
ARG   N   CA   sing N N 33  
ARG   N   H    sing N N 34  
ARG   N   H2   sing N N 35  
ARG   CA  C    sing N N 36  
ARG   CA  CB   sing N N 37  
ARG   CA  HA   sing N N 38  
ARG   C   O    doub N N 39  
ARG   C   OXT  sing N N 40  
ARG   CB  CG   sing N N 41  
ARG   CB  HB2  sing N N 42  
ARG   CB  HB3  sing N N 43  
ARG   CG  CD   sing N N 44  
ARG   CG  HG2  sing N N 45  
ARG   CG  HG3  sing N N 46  
ARG   CD  NE   sing N N 47  
ARG   CD  HD2  sing N N 48  
ARG   CD  HD3  sing N N 49  
ARG   NE  CZ   sing N N 50  
ARG   NE  HE   sing N N 51  
ARG   CZ  NH1  sing N N 52  
ARG   CZ  NH2  doub N N 53  
ARG   NH1 HH11 sing N N 54  
ARG   NH1 HH12 sing N N 55  
ARG   NH2 HH21 sing N N 56  
ARG   NH2 HH22 sing N N 57  
ARG   OXT HXT  sing N N 58  
ASN   N   CA   sing N N 59  
ASN   N   H    sing N N 60  
ASN   N   H2   sing N N 61  
ASN   CA  C    sing N N 62  
ASN   CA  CB   sing N N 63  
ASN   CA  HA   sing N N 64  
ASN   C   O    doub N N 65  
ASN   C   OXT  sing N N 66  
ASN   CB  CG   sing N N 67  
ASN   CB  HB2  sing N N 68  
ASN   CB  HB3  sing N N 69  
ASN   CG  OD1  doub N N 70  
ASN   CG  ND2  sing N N 71  
ASN   ND2 HD21 sing N N 72  
ASN   ND2 HD22 sing N N 73  
ASN   OXT HXT  sing N N 74  
ASP   N   CA   sing N N 75  
ASP   N   H    sing N N 76  
ASP   N   H2   sing N N 77  
ASP   CA  C    sing N N 78  
ASP   CA  CB   sing N N 79  
ASP   CA  HA   sing N N 80  
ASP   C   O    doub N N 81  
ASP   C   OXT  sing N N 82  
ASP   CB  CG   sing N N 83  
ASP   CB  HB2  sing N N 84  
ASP   CB  HB3  sing N N 85  
ASP   CG  OD1  doub N N 86  
ASP   CG  OD2  sing N N 87  
ASP   OD2 HD2  sing N N 88  
ASP   OXT HXT  sing N N 89  
CYS   N   CA   sing N N 90  
CYS   N   H    sing N N 91  
CYS   N   H2   sing N N 92  
CYS   CA  C    sing N N 93  
CYS   CA  CB   sing N N 94  
CYS   CA  HA   sing N N 95  
CYS   C   O    doub N N 96  
CYS   C   OXT  sing N N 97  
CYS   CB  SG   sing N N 98  
CYS   CB  HB2  sing N N 99  
CYS   CB  HB3  sing N N 100 
CYS   SG  HG   sing N N 101 
CYS   OXT HXT  sing N N 102 
GLN   N   CA   sing N N 103 
GLN   N   H    sing N N 104 
GLN   N   H2   sing N N 105 
GLN   CA  C    sing N N 106 
GLN   CA  CB   sing N N 107 
GLN   CA  HA   sing N N 108 
GLN   C   O    doub N N 109 
GLN   C   OXT  sing N N 110 
GLN   CB  CG   sing N N 111 
GLN   CB  HB2  sing N N 112 
GLN   CB  HB3  sing N N 113 
GLN   CG  CD   sing N N 114 
GLN   CG  HG2  sing N N 115 
GLN   CG  HG3  sing N N 116 
GLN   CD  OE1  doub N N 117 
GLN   CD  NE2  sing N N 118 
GLN   NE2 HE21 sing N N 119 
GLN   NE2 HE22 sing N N 120 
GLN   OXT HXT  sing N N 121 
GLU   N   CA   sing N N 122 
GLU   N   H    sing N N 123 
GLU   N   H2   sing N N 124 
GLU   CA  C    sing N N 125 
GLU   CA  CB   sing N N 126 
GLU   CA  HA   sing N N 127 
GLU   C   O    doub N N 128 
GLU   C   OXT  sing N N 129 
GLU   CB  CG   sing N N 130 
GLU   CB  HB2  sing N N 131 
GLU   CB  HB3  sing N N 132 
GLU   CG  CD   sing N N 133 
GLU   CG  HG2  sing N N 134 
GLU   CG  HG3  sing N N 135 
GLU   CD  OE1  doub N N 136 
GLU   CD  OE2  sing N N 137 
GLU   OE2 HE2  sing N N 138 
GLU   OXT HXT  sing N N 139 
GLY   N   CA   sing N N 140 
GLY   N   H    sing N N 141 
GLY   N   H2   sing N N 142 
GLY   CA  C    sing N N 143 
GLY   CA  HA2  sing N N 144 
GLY   CA  HA3  sing N N 145 
GLY   C   O    doub N N 146 
GLY   C   OXT  sing N N 147 
GLY   OXT HXT  sing N N 148 
HIS   N   CA   sing N N 149 
HIS   N   H    sing N N 150 
HIS   N   H2   sing N N 151 
HIS   CA  C    sing N N 152 
HIS   CA  CB   sing N N 153 
HIS   CA  HA   sing N N 154 
HIS   C   O    doub N N 155 
HIS   C   OXT  sing N N 156 
HIS   CB  CG   sing N N 157 
HIS   CB  HB2  sing N N 158 
HIS   CB  HB3  sing N N 159 
HIS   CG  ND1  sing Y N 160 
HIS   CG  CD2  doub Y N 161 
HIS   ND1 CE1  doub Y N 162 
HIS   ND1 HD1  sing N N 163 
HIS   CD2 NE2  sing Y N 164 
HIS   CD2 HD2  sing N N 165 
HIS   CE1 NE2  sing Y N 166 
HIS   CE1 HE1  sing N N 167 
HIS   NE2 HE2  sing N N 168 
HIS   OXT HXT  sing N N 169 
HOH   O   H1   sing N N 170 
HOH   O   H2   sing N N 171 
ILE   N   CA   sing N N 172 
ILE   N   H    sing N N 173 
ILE   N   H2   sing N N 174 
ILE   CA  C    sing N N 175 
ILE   CA  CB   sing N N 176 
ILE   CA  HA   sing N N 177 
ILE   C   O    doub N N 178 
ILE   C   OXT  sing N N 179 
ILE   CB  CG1  sing N N 180 
ILE   CB  CG2  sing N N 181 
ILE   CB  HB   sing N N 182 
ILE   CG1 CD1  sing N N 183 
ILE   CG1 HG12 sing N N 184 
ILE   CG1 HG13 sing N N 185 
ILE   CG2 HG21 sing N N 186 
ILE   CG2 HG22 sing N N 187 
ILE   CG2 HG23 sing N N 188 
ILE   CD1 HD11 sing N N 189 
ILE   CD1 HD12 sing N N 190 
ILE   CD1 HD13 sing N N 191 
ILE   OXT HXT  sing N N 192 
LEU   N   CA   sing N N 193 
LEU   N   H    sing N N 194 
LEU   N   H2   sing N N 195 
LEU   CA  C    sing N N 196 
LEU   CA  CB   sing N N 197 
LEU   CA  HA   sing N N 198 
LEU   C   O    doub N N 199 
LEU   C   OXT  sing N N 200 
LEU   CB  CG   sing N N 201 
LEU   CB  HB2  sing N N 202 
LEU   CB  HB3  sing N N 203 
LEU   CG  CD1  sing N N 204 
LEU   CG  CD2  sing N N 205 
LEU   CG  HG   sing N N 206 
LEU   CD1 HD11 sing N N 207 
LEU   CD1 HD12 sing N N 208 
LEU   CD1 HD13 sing N N 209 
LEU   CD2 HD21 sing N N 210 
LEU   CD2 HD22 sing N N 211 
LEU   CD2 HD23 sing N N 212 
LEU   OXT HXT  sing N N 213 
LYS   N   CA   sing N N 214 
LYS   N   H    sing N N 215 
LYS   N   H2   sing N N 216 
LYS   CA  C    sing N N 217 
LYS   CA  CB   sing N N 218 
LYS   CA  HA   sing N N 219 
LYS   C   O    doub N N 220 
LYS   C   OXT  sing N N 221 
LYS   CB  CG   sing N N 222 
LYS   CB  HB2  sing N N 223 
LYS   CB  HB3  sing N N 224 
LYS   CG  CD   sing N N 225 
LYS   CG  HG2  sing N N 226 
LYS   CG  HG3  sing N N 227 
LYS   CD  CE   sing N N 228 
LYS   CD  HD2  sing N N 229 
LYS   CD  HD3  sing N N 230 
LYS   CE  NZ   sing N N 231 
LYS   CE  HE2  sing N N 232 
LYS   CE  HE3  sing N N 233 
LYS   NZ  HZ1  sing N N 234 
LYS   NZ  HZ2  sing N N 235 
LYS   NZ  HZ3  sing N N 236 
LYS   OXT HXT  sing N N 237 
MET   N   CA   sing N N 238 
MET   N   H    sing N N 239 
MET   N   H2   sing N N 240 
MET   CA  C    sing N N 241 
MET   CA  CB   sing N N 242 
MET   CA  HA   sing N N 243 
MET   C   O    doub N N 244 
MET   C   OXT  sing N N 245 
MET   CB  CG   sing N N 246 
MET   CB  HB2  sing N N 247 
MET   CB  HB3  sing N N 248 
MET   CG  SD   sing N N 249 
MET   CG  HG2  sing N N 250 
MET   CG  HG3  sing N N 251 
MET   SD  CE   sing N N 252 
MET   CE  HE1  sing N N 253 
MET   CE  HE2  sing N N 254 
MET   CE  HE3  sing N N 255 
MET   OXT HXT  sing N N 256 
PHE   N   CA   sing N N 257 
PHE   N   H    sing N N 258 
PHE   N   H2   sing N N 259 
PHE   CA  C    sing N N 260 
PHE   CA  CB   sing N N 261 
PHE   CA  HA   sing N N 262 
PHE   C   O    doub N N 263 
PHE   C   OXT  sing N N 264 
PHE   CB  CG   sing N N 265 
PHE   CB  HB2  sing N N 266 
PHE   CB  HB3  sing N N 267 
PHE   CG  CD1  doub Y N 268 
PHE   CG  CD2  sing Y N 269 
PHE   CD1 CE1  sing Y N 270 
PHE   CD1 HD1  sing N N 271 
PHE   CD2 CE2  doub Y N 272 
PHE   CD2 HD2  sing N N 273 
PHE   CE1 CZ   doub Y N 274 
PHE   CE1 HE1  sing N N 275 
PHE   CE2 CZ   sing Y N 276 
PHE   CE2 HE2  sing N N 277 
PHE   CZ  HZ   sing N N 278 
PHE   OXT HXT  sing N N 279 
PLP   N1  C2   doub Y N 280 
PLP   N1  C6   sing Y N 281 
PLP   C2  C2A  sing N N 282 
PLP   C2  C3   sing Y N 283 
PLP   C2A H2A1 sing N N 284 
PLP   C2A H2A2 sing N N 285 
PLP   C2A H2A3 sing N N 286 
PLP   C3  O3   sing N N 287 
PLP   C3  C4   doub Y N 288 
PLP   O3  HO3  sing N N 289 
PLP   C4  C4A  sing N N 290 
PLP   C4  C5   sing Y N 291 
PLP   C4A O4A  doub N N 292 
PLP   C4A H4A  sing N N 293 
PLP   C5  C6   doub Y N 294 
PLP   C5  C5A  sing N N 295 
PLP   C6  H6   sing N N 296 
PLP   C5A O4P  sing N N 297 
PLP   C5A H5A1 sing N N 298 
PLP   C5A H5A2 sing N N 299 
PLP   O4P P    sing N N 300 
PLP   P   O1P  doub N N 301 
PLP   P   O2P  sing N N 302 
PLP   P   O3P  sing N N 303 
PLP   O2P HOP2 sing N N 304 
PLP   O3P HOP3 sing N N 305 
PRO   N   CA   sing N N 306 
PRO   N   CD   sing N N 307 
PRO   N   H    sing N N 308 
PRO   CA  C    sing N N 309 
PRO   CA  CB   sing N N 310 
PRO   CA  HA   sing N N 311 
PRO   C   O    doub N N 312 
PRO   C   OXT  sing N N 313 
PRO   CB  CG   sing N N 314 
PRO   CB  HB2  sing N N 315 
PRO   CB  HB3  sing N N 316 
PRO   CG  CD   sing N N 317 
PRO   CG  HG2  sing N N 318 
PRO   CG  HG3  sing N N 319 
PRO   CD  HD2  sing N N 320 
PRO   CD  HD3  sing N N 321 
PRO   OXT HXT  sing N N 322 
SER   N   CA   sing N N 323 
SER   N   H    sing N N 324 
SER   N   H2   sing N N 325 
SER   CA  C    sing N N 326 
SER   CA  CB   sing N N 327 
SER   CA  HA   sing N N 328 
SER   C   O    doub N N 329 
SER   C   OXT  sing N N 330 
SER   CB  OG   sing N N 331 
SER   CB  HB2  sing N N 332 
SER   CB  HB3  sing N N 333 
SER   OG  HG   sing N N 334 
SER   OXT HXT  sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TRP   N   CA   sing N N 352 
TRP   N   H    sing N N 353 
TRP   N   H2   sing N N 354 
TRP   CA  C    sing N N 355 
TRP   CA  CB   sing N N 356 
TRP   CA  HA   sing N N 357 
TRP   C   O    doub N N 358 
TRP   C   OXT  sing N N 359 
TRP   CB  CG   sing N N 360 
TRP   CB  HB2  sing N N 361 
TRP   CB  HB3  sing N N 362 
TRP   CG  CD1  doub Y N 363 
TRP   CG  CD2  sing Y N 364 
TRP   CD1 NE1  sing Y N 365 
TRP   CD1 HD1  sing N N 366 
TRP   CD2 CE2  doub Y N 367 
TRP   CD2 CE3  sing Y N 368 
TRP   NE1 CE2  sing Y N 369 
TRP   NE1 HE1  sing N N 370 
TRP   CE2 CZ2  sing Y N 371 
TRP   CE3 CZ3  doub Y N 372 
TRP   CE3 HE3  sing N N 373 
TRP   CZ2 CH2  doub Y N 374 
TRP   CZ2 HZ2  sing N N 375 
TRP   CZ3 CH2  sing Y N 376 
TRP   CZ3 HZ3  sing N N 377 
TRP   CH2 HH2  sing N N 378 
TRP   OXT HXT  sing N N 379 
TYR   N   CA   sing N N 380 
TYR   N   H    sing N N 381 
TYR   N   H2   sing N N 382 
TYR   CA  C    sing N N 383 
TYR   CA  CB   sing N N 384 
TYR   CA  HA   sing N N 385 
TYR   C   O    doub N N 386 
TYR   C   OXT  sing N N 387 
TYR   CB  CG   sing N N 388 
TYR   CB  HB2  sing N N 389 
TYR   CB  HB3  sing N N 390 
TYR   CG  CD1  doub Y N 391 
TYR   CG  CD2  sing Y N 392 
TYR   CD1 CE1  sing Y N 393 
TYR   CD1 HD1  sing N N 394 
TYR   CD2 CE2  doub Y N 395 
TYR   CD2 HD2  sing N N 396 
TYR   CE1 CZ   doub Y N 397 
TYR   CE1 HE1  sing N N 398 
TYR   CE2 CZ   sing Y N 399 
TYR   CE2 HE2  sing N N 400 
TYR   CZ  OH   sing N N 401 
TYR   OH  HH   sing N N 402 
TYR   OXT HXT  sing N N 403 
VAL   N   CA   sing N N 404 
VAL   N   H    sing N N 405 
VAL   N   H2   sing N N 406 
VAL   CA  C    sing N N 407 
VAL   CA  CB   sing N N 408 
VAL   CA  HA   sing N N 409 
VAL   C   O    doub N N 410 
VAL   C   OXT  sing N N 411 
VAL   CB  CG1  sing N N 412 
VAL   CB  CG2  sing N N 413 
VAL   CB  HB   sing N N 414 
VAL   CG1 HG11 sing N N 415 
VAL   CG1 HG12 sing N N 416 
VAL   CG1 HG13 sing N N 417 
VAL   CG2 HG21 sing N N 418 
VAL   CG2 HG22 sing N N 419 
VAL   CG2 HG23 sing N N 420 
VAL   OXT HXT  sing N N 421 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Cancer Institute (NIH/NCI)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           'R21 CA216867' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7u6u 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9B8M 
_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]   0.013396 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011570 
_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]   0.006527 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASN   A 1 6   ? -4.579  14.548  84.111 1.00 119.97 ? 6   ASN   A N   1 
ATOM   2    C CA  . ASN   A 1 6   ? -4.791  15.165  82.805 1.00 135.94 ? 6   ASN   A CA  1 
ATOM   3    C C   . ASN   A 1 6   ? -5.706  14.281  81.960 1.00 135.70 ? 6   ASN   A C   1 
ATOM   4    O O   . ASN   A 1 6   ? -6.125  13.213  82.410 1.00 140.04 ? 6   ASN   A O   1 
ATOM   5    C CB  . ASN   A 1 6   ? -3.451  15.404  82.103 1.00 140.09 ? 6   ASN   A CB  1 
ATOM   6    C CG  . ASN   A 1 6   ? -3.485  16.593  81.163 1.00 142.04 ? 6   ASN   A CG  1 
ATOM   7    O OD1 . ASN   A 1 6   ? -4.480  17.309  81.088 1.00 148.01 ? 6   ASN   A OD1 1 
ATOM   8    N ND2 . ASN   A 1 6   ? -2.382  16.826  80.461 1.00 126.79 ? 6   ASN   A ND2 1 
ATOM   9    N N   . GLU   A 1 7   ? -6.012  14.727  80.736 1.00 126.22 ? 7   GLU   A N   1 
ATOM   10   C CA  . GLU   A 1 7   ? -6.889  13.951  79.864 1.00 118.92 ? 7   GLU   A CA  1 
ATOM   11   C C   . GLU   A 1 7   ? -6.258  12.605  79.527 1.00 115.40 ? 7   GLU   A C   1 
ATOM   12   O O   . GLU   A 1 7   ? -6.958  11.592  79.413 1.00 108.77 ? 7   GLU   A O   1 
ATOM   13   C CB  . GLU   A 1 7   ? -7.205  14.738  78.589 1.00 118.76 ? 7   GLU   A CB  1 
ATOM   14   C CG  . GLU   A 1 7   ? -8.147  14.042  77.598 1.00 125.91 ? 7   GLU   A CG  1 
ATOM   15   C CD  . GLU   A 1 7   ? -9.555  13.770  78.148 1.00 109.84 ? 7   GLU   A CD  1 
ATOM   16   O OE1 . GLU   A 1 7   ? -9.798  13.908  79.365 1.00 115.96 ? 7   GLU   A OE1 1 
ATOM   17   O OE2 . GLU   A 1 7   ? -10.437 13.416  77.341 1.00 91.78  ? 7   GLU   A OE2 1 
ATOM   18   N N   . GLU   A 1 8   ? -4.933  12.586  79.344 1.00 117.49 ? 8   GLU   A N   1 
ATOM   19   C CA  . GLU   A 1 8   ? -4.230  11.346  79.023 1.00 115.24 ? 8   GLU   A CA  1 
ATOM   20   C C   . GLU   A 1 8   ? -4.408  10.319  80.132 1.00 109.92 ? 8   GLU   A C   1 
ATOM   21   O O   . GLU   A 1 8   ? -4.589  9.125   79.863 1.00 109.22 ? 8   GLU   A O   1 
ATOM   22   C CB  . GLU   A 1 8   ? -2.748  11.631  78.784 1.00 98.58  ? 8   GLU   A CB  1 
ATOM   23   C CG  . GLU   A 1 8   ? -2.488  12.528  77.592 1.00 119.01 ? 8   GLU   A CG  1 
ATOM   24   C CD  . GLU   A 1 8   ? -1.023  12.853  77.418 1.00 134.33 ? 8   GLU   A CD  1 
ATOM   25   O OE1 . GLU   A 1 8   ? -0.230  12.537  78.330 1.00 123.51 ? 8   GLU   A OE1 1 
ATOM   26   O OE2 . GLU   A 1 8   ? -0.667  13.435  76.373 1.00 130.44 ? 8   GLU   A OE2 1 
ATOM   27   N N   . PHE   A 1 9   ? -4.355  10.767  81.387 1.00 113.56 ? 9   PHE   A N   1 
ATOM   28   C CA  . PHE   A 1 9   ? -4.517  9.900   82.548 1.00 104.10 ? 9   PHE   A CA  1 
ATOM   29   C C   . PHE   A 1 9   ? -5.975  9.793   82.973 1.00 100.40 ? 9   PHE   A C   1 
ATOM   30   O O   . PHE   A 1 9   ? -6.280  9.077   83.933 1.00 103.42 ? 9   PHE   A O   1 
ATOM   31   C CB  . PHE   A 1 9   ? -3.680  10.424  83.723 1.00 100.95 ? 9   PHE   A CB  1 
ATOM   32   C CG  . PHE   A 1 9   ? -2.207  10.512  83.435 1.00 104.47 ? 9   PHE   A CG  1 
ATOM   33   C CD1 . PHE   A 1 9   ? -1.626  11.727  83.105 1.00 114.95 ? 9   PHE   A CD1 1 
ATOM   34   C CD2 . PHE   A 1 9   ? -1.408  9.381   83.467 1.00 93.05  ? 9   PHE   A CD2 1 
ATOM   35   C CE1 . PHE   A 1 9   ? -0.273  11.817  82.832 1.00 115.05 ? 9   PHE   A CE1 1 
ATOM   36   C CE2 . PHE   A 1 9   ? -0.051  9.463   83.194 1.00 97.70  ? 9   PHE   A CE2 1 
ATOM   37   C CZ  . PHE   A 1 9   ? 0.516   10.684  82.875 1.00 108.23 ? 9   PHE   A CZ  1 
ATOM   38   N N   . ASP   A 1 10  ? -6.874  10.492  82.279 1.00 103.68 ? 10  ASP   A N   1 
ATOM   39   C CA  . ASP   A 1 10  ? -8.301  10.469  82.581 1.00 90.92  ? 10  ASP   A CA  1 
ATOM   40   C C   . ASP   A 1 10  ? -8.946  9.241   81.946 1.00 90.42  ? 10  ASP   A C   1 
ATOM   41   O O   . ASP   A 1 10  ? -8.872  9.056   80.726 1.00 92.49  ? 10  ASP   A O   1 
ATOM   42   C CB  . ASP   A 1 10  ? -8.962  11.751  82.075 1.00 103.89 ? 10  ASP   A CB  1 
ATOM   43   C CG  . ASP   A 1 10  ? -10.421 11.859  82.476 1.00 93.58  ? 10  ASP   A CG  1 
ATOM   44   O OD1 . ASP   A 1 10  ? -10.854 11.109  83.375 1.00 89.68  ? 10  ASP   A OD1 1 
ATOM   45   O OD2 . ASP   A 1 10  ? -11.137 12.696  81.886 1.00 100.01 ? 10  ASP   A OD2 1 
ATOM   46   N N   . CYS   A 1 11  ? -9.584  8.411   82.769 1.00 79.64  ? 11  CYS   A N   1 
ATOM   47   C CA  . CYS   A 1 11  ? -10.264 7.205   82.315 1.00 72.46  ? 11  CYS   A CA  1 
ATOM   48   C C   . CYS   A 1 11  ? -11.729 7.258   82.720 1.00 66.66  ? 11  CYS   A C   1 
ATOM   49   O O   . CYS   A 1 11  ? -12.049 7.615   83.857 1.00 83.15  ? 11  CYS   A O   1 
ATOM   50   C CB  . CYS   A 1 11  ? -9.609  5.948   82.890 1.00 62.52  ? 11  CYS   A CB  1 
ATOM   51   S SG  . CYS   A 1 11  ? -10.229 4.417   82.173 1.00 76.03  ? 11  CYS   A SG  1 
ATOM   52   N N   . HIS   A 1 12  ? -12.612 6.912   81.789 1.00 64.26  ? 12  HIS   A N   1 
ATOM   53   C CA  . HIS   A 1 12  ? -14.048 6.937   82.016 1.00 60.51  ? 12  HIS   A CA  1 
ATOM   54   C C   . HIS   A 1 12  ? -14.591 5.525   82.213 1.00 66.33  ? 12  HIS   A C   1 
ATOM   55   O O   . HIS   A 1 12  ? -14.081 4.557   81.644 1.00 68.24  ? 12  HIS   A O   1 
ATOM   56   C CB  . HIS   A 1 12  ? -14.762 7.622   80.848 1.00 69.77  ? 12  HIS   A CB  1 
ATOM   57   C CG  . HIS   A 1 12  ? -14.219 8.980   80.527 1.00 66.39  ? 12  HIS   A CG  1 
ATOM   58   N ND1 . HIS   A 1 12  ? -14.838 10.146  80.925 1.00 69.06  ? 12  HIS   A ND1 1 
ATOM   59   C CD2 . HIS   A 1 12  ? -13.111 9.358   79.845 1.00 64.85  ? 12  HIS   A CD2 1 
ATOM   60   C CE1 . HIS   A 1 12  ? -14.135 11.182  80.502 1.00 72.29  ? 12  HIS   A CE1 1 
ATOM   61   N NE2 . HIS   A 1 12  ? -13.083 10.731  79.844 1.00 66.08  ? 12  HIS   A NE2 1 
ATOM   62   N N   . PHE   A 1 13  ? -15.635 5.419   83.033 1.00 56.69  ? 13  PHE   A N   1 
ATOM   63   C CA  . PHE   A 1 13  ? -16.272 4.132   83.285 1.00 56.49  ? 13  PHE   A CA  1 
ATOM   64   C C   . PHE   A 1 13  ? -17.095 3.671   82.088 1.00 67.92  ? 13  PHE   A C   1 
ATOM   65   O O   . PHE   A 1 13  ? -17.785 4.462   81.440 1.00 69.89  ? 13  PHE   A O   1 
ATOM   66   C CB  . PHE   A 1 13  ? -17.167 4.211   84.522 1.00 66.63  ? 13  PHE   A CB  1 
ATOM   67   C CG  . PHE   A 1 13  ? -16.529 3.669   85.769 1.00 72.29  ? 13  PHE   A CG  1 
ATOM   68   C CD1 . PHE   A 1 13  ? -16.618 2.321   86.074 1.00 68.24  ? 13  PHE   A CD1 1 
ATOM   69   C CD2 . PHE   A 1 13  ? -15.845 4.504   86.637 1.00 81.29  ? 13  PHE   A CD2 1 
ATOM   70   C CE1 . PHE   A 1 13  ? -16.036 1.814   87.220 1.00 73.38  ? 13  PHE   A CE1 1 
ATOM   71   C CE2 . PHE   A 1 13  ? -15.259 4.003   87.787 1.00 68.59  ? 13  PHE   A CE2 1 
ATOM   72   C CZ  . PHE   A 1 13  ? -15.355 2.656   88.078 1.00 72.21  ? 13  PHE   A CZ  1 
ATOM   73   N N   . LEU   A 1 14  ? -17.010 2.375   81.797 1.00 81.34  ? 14  LEU   A N   1 
ATOM   74   C CA  . LEU   A 1 14  ? -17.835 1.713   80.792 1.00 81.89  ? 14  LEU   A CA  1 
ATOM   75   C C   . LEU   A 1 14  ? -18.873 0.873   81.526 1.00 88.69  ? 14  LEU   A C   1 
ATOM   76   O O   . LEU   A 1 14  ? -18.531 -0.129  82.161 1.00 93.74  ? 14  LEU   A O   1 
ATOM   77   C CB  . LEU   A 1 14  ? -16.977 0.851   79.867 1.00 78.48  ? 14  LEU   A CB  1 
ATOM   78   C CG  . LEU   A 1 14  ? -17.689 0.063   78.766 1.00 91.26  ? 14  LEU   A CG  1 
ATOM   79   C CD1 . LEU   A 1 14  ? -18.392 1.003   77.799 1.00 82.45  ? 14  LEU   A CD1 1 
ATOM   80   C CD2 . LEU   A 1 14  ? -16.709 -0.839  78.032 1.00 91.73  ? 14  LEU   A CD2 1 
ATOM   81   N N   . ASP   A 1 15  ? -20.135 1.284   81.455 1.00 105.83 ? 15  ASP   A N   1 
ATOM   82   C CA  . ASP   A 1 15  ? -21.168 0.601   82.217 1.00 109.84 ? 15  ASP   A CA  1 
ATOM   83   C C   . ASP   A 1 15  ? -21.474 -0.768  81.613 1.00 110.35 ? 15  ASP   A C   1 
ATOM   84   O O   . ASP   A 1 15  ? -21.174 -1.049  80.448 1.00 104.86 ? 15  ASP   A O   1 
ATOM   85   C CB  . ASP   A 1 15  ? -22.436 1.452   82.280 1.00 99.99  ? 15  ASP   A CB  1 
ATOM   86   C CG  . ASP   A 1 15  ? -22.243 2.720   83.087 1.00 108.57 ? 15  ASP   A CG  1 
ATOM   87   O OD1 . ASP   A 1 15  ? -21.362 2.729   83.973 1.00 120.48 ? 15  ASP   A OD1 1 
ATOM   88   O OD2 . ASP   A 1 15  ? -22.967 3.705   82.837 1.00 111.05 ? 15  ASP   A OD2 1 
ATOM   89   N N   . GLU   A 1 16  ? -22.061 -1.634  82.440 1.00 105.25 ? 16  GLU   A N   1 
ATOM   90   C CA  . GLU   A 1 16  ? -22.397 -2.985  82.011 1.00 108.39 ? 16  GLU   A CA  1 
ATOM   91   C C   . GLU   A 1 16  ? -23.339 -2.955  80.814 1.00 110.93 ? 16  GLU   A C   1 
ATOM   92   O O   . GLU   A 1 16  ? -24.276 -2.155  80.757 1.00 112.92 ? 16  GLU   A O   1 
ATOM   93   C CB  . GLU   A 1 16  ? -23.035 -3.765  83.163 1.00 107.07 ? 16  GLU   A CB  1 
ATOM   94   C CG  . GLU   A 1 16  ? -23.342 -5.218  82.832 1.00 98.90  ? 16  GLU   A CG  1 
ATOM   95   C CD  . GLU   A 1 16  ? -23.928 -5.977  84.007 1.00 117.38 ? 16  GLU   A CD  1 
ATOM   96   O OE1 . GLU   A 1 16  ? -24.200 -5.347  85.051 1.00 119.78 ? 16  GLU   A OE1 1 
ATOM   97   O OE2 . GLU   A 1 16  ? -24.119 -7.205  83.885 1.00 111.04 ? 16  GLU   A OE2 1 
ATOM   98   N N   . GLY   A 1 17  ? -23.081 -3.839  79.851 1.00 105.85 ? 17  GLY   A N   1 
ATOM   99   C CA  . GLY   A 1 17  ? -23.876 -3.914  78.646 1.00 102.67 ? 17  GLY   A CA  1 
ATOM   100  C C   . GLY   A 1 17  ? -23.550 -2.872  77.602 1.00 110.76 ? 17  GLY   A C   1 
ATOM   101  O O   . GLY   A 1 17  ? -24.242 -2.808  76.578 1.00 118.67 ? 17  GLY   A O   1 
ATOM   102  N N   . PHE   A 1 18  ? -22.523 -2.058  77.824 1.00 113.63 ? 18  PHE   A N   1 
ATOM   103  C CA  . PHE   A 1 18  ? -22.120 -1.012  76.896 1.00 108.24 ? 18  PHE   A CA  1 
ATOM   104  C C   . PHE   A 1 18  ? -20.759 -1.347  76.306 1.00 101.70 ? 18  PHE   A C   1 
ATOM   105  O O   . PHE   A 1 18  ? -19.877 -1.860  77.002 1.00 100.48 ? 18  PHE   A O   1 
ATOM   106  C CB  . PHE   A 1 18  ? -22.066 0.352   77.589 1.00 107.40 ? 18  PHE   A CB  1 
ATOM   107  C CG  . PHE   A 1 18  ? -23.417 0.933   77.887 1.00 114.33 ? 18  PHE   A CG  1 
ATOM   108  C CD1 . PHE   A 1 18  ? -24.143 0.505   78.986 1.00 111.43 ? 18  PHE   A CD1 1 
ATOM   109  C CD2 . PHE   A 1 18  ? -23.964 1.905   77.067 1.00 103.83 ? 18  PHE   A CD2 1 
ATOM   110  C CE1 . PHE   A 1 18  ? -25.388 1.037   79.263 1.00 106.07 ? 18  PHE   A CE1 1 
ATOM   111  C CE2 . PHE   A 1 18  ? -25.210 2.439   77.338 1.00 88.29  ? 18  PHE   A CE2 1 
ATOM   112  C CZ  . PHE   A 1 18  ? -25.922 2.006   78.437 1.00 103.94 ? 18  PHE   A CZ  1 
ATOM   113  N N   . THR   A 1 19  ? -20.595 -1.056  75.022 1.00 99.11  ? 19  THR   A N   1 
ATOM   114  C CA  . THR   A 1 19  ? -19.329 -1.228  74.328 1.00 102.15 ? 19  THR   A CA  1 
ATOM   115  C C   . THR   A 1 19  ? -18.787 0.131   73.906 1.00 99.21  ? 19  THR   A C   1 
ATOM   116  O O   . THR   A 1 19  ? -19.469 1.156   74.001 1.00 98.71  ? 19  THR   A O   1 
ATOM   117  C CB  . THR   A 1 19  ? -19.495 -2.138  73.105 1.00 100.98 ? 19  THR   A CB  1 
ATOM   118  O OG1 . THR   A 1 19  ? -20.302 -1.477  72.121 1.00 94.29  ? 19  THR   A OG1 1 
ATOM   119  C CG2 . THR   A 1 19  ? -20.159 -3.448  73.500 1.00 93.47  ? 19  THR   A CG2 1 
ATOM   120  N N   . ALA   A 1 20  ? -17.528 0.129   73.458 1.00 90.29  ? 20  ALA   A N   1 
ATOM   121  C CA  . ALA   A 1 20  ? -16.923 1.349   72.932 1.00 89.59  ? 20  ALA   A CA  1 
ATOM   122  C C   . ALA   A 1 20  ? -17.762 1.950   71.812 1.00 85.12  ? 20  ALA   A C   1 
ATOM   123  O O   . ALA   A 1 20  ? -17.826 3.176   71.668 1.00 88.32  ? 20  ALA   A O   1 
ATOM   124  C CB  . ALA   A 1 20  ? -15.504 1.061   72.438 1.00 93.57  ? 20  ALA   A CB  1 
ATOM   125  N N   . LYS   A 1 21  ? -18.404 1.099   71.009 1.00 81.03  ? 21  LYS   A N   1 
ATOM   126  C CA  . LYS   A 1 21  ? -19.245 1.574   69.915 1.00 85.45  ? 21  LYS   A CA  1 
ATOM   127  C C   . LYS   A 1 21  ? -20.389 2.431   70.447 1.00 92.04  ? 21  LYS   A C   1 
ATOM   128  O O   . LYS   A 1 21  ? -20.684 3.511   69.914 1.00 94.57  ? 21  LYS   A O   1 
ATOM   129  C CB  . LYS   A 1 21  ? -19.788 0.375   69.137 1.00 88.45  ? 21  LYS   A CB  1 
ATOM   130  C CG  . LYS   A 1 21  ? -18.724 -0.609  68.649 1.00 79.71  ? 21  LYS   A CG  1 
ATOM   131  C CD  . LYS   A 1 21  ? -17.672 0.037   67.762 1.00 96.04  ? 21  LYS   A CD  1 
ATOM   132  C CE  . LYS   A 1 21  ? -18.288 0.658   66.520 1.00 103.95 ? 21  LYS   A CE  1 
ATOM   133  N NZ  . LYS   A 1 21  ? -17.254 1.283   65.648 1.00 74.72  ? 21  LYS   A NZ  1 
ATOM   134  N N   . ASP   A 1 22  ? -21.053 1.949   71.502 1.00 100.92 ? 22  ASP   A N   1 
ATOM   135  C CA  . ASP   A 1 22  ? -22.170 2.681   72.091 1.00 96.55  ? 22  ASP   A CA  1 
ATOM   136  C C   . ASP   A 1 22  ? -21.706 3.998   72.695 1.00 86.11  ? 22  ASP   A C   1 
ATOM   137  O O   . ASP   A 1 22  ? -22.409 5.009   72.611 1.00 83.82  ? 22  ASP   A O   1 
ATOM   138  C CB  . ASP   A 1 22  ? -22.854 1.820   73.153 1.00 101.08 ? 22  ASP   A CB  1 
ATOM   139  C CG  . ASP   A 1 22  ? -23.288 0.469   72.618 1.00 115.90 ? 22  ASP   A CG  1 
ATOM   140  O OD1 . ASP   A 1 22  ? -23.044 -0.551  73.299 1.00 107.82 ? 22  ASP   A OD1 1 
ATOM   141  O OD2 . ASP   A 1 22  ? -23.872 0.426   71.514 1.00 123.83 ? 22  ASP   A OD2 1 
ATOM   142  N N   . ILE   A 1 23  ? -20.529 3.999   73.322 1.00 90.78  ? 23  ILE   A N   1 
ATOM   143  C CA  . ILE   A 1 23  ? -19.959 5.230   73.863 1.00 93.34  ? 23  ILE   A CA  1 
ATOM   144  C C   . ILE   A 1 23  ? -19.692 6.233   72.747 1.00 83.62  ? 23  ILE   A C   1 
ATOM   145  O O   . ILE   A 1 23  ? -19.929 7.441   72.898 1.00 84.16  ? 23  ILE   A O   1 
ATOM   146  C CB  . ILE   A 1 23  ? -18.680 4.898   74.655 1.00 95.57  ? 23  ILE   A CB  1 
ATOM   147  C CG1 . ILE   A 1 23  ? -19.027 4.150   75.945 1.00 85.01  ? 23  ILE   A CG1 1 
ATOM   148  C CG2 . ILE   A 1 23  ? -17.877 6.143   74.936 1.00 86.59  ? 23  ILE   A CG2 1 
ATOM   149  C CD1 . ILE   A 1 23  ? -19.963 4.907   76.858 1.00 90.22  ? 23  ILE   A CD1 1 
ATOM   150  N N   . LEU   A 1 24  ? -19.190 5.745   71.611 1.00 81.84  ? 24  LEU   A N   1 
ATOM   151  C CA  . LEU   A 1 24  ? -19.003 6.596   70.441 1.00 82.11  ? 24  LEU   A CA  1 
ATOM   152  C C   . LEU   A 1 24  ? -20.323 7.219   70.004 1.00 93.77  ? 24  LEU   A C   1 
ATOM   153  O O   . LEU   A 1 24  ? -20.416 8.438   69.794 1.00 87.99  ? 24  LEU   A O   1 
ATOM   154  C CB  . LEU   A 1 24  ? -18.398 5.767   69.309 1.00 64.89  ? 24  LEU   A CB  1 
ATOM   155  C CG  . LEU   A 1 24  ? -17.611 6.445   68.196 1.00 73.70  ? 24  LEU   A CG  1 
ATOM   156  C CD1 . LEU   A 1 24  ? -16.722 7.527   68.754 1.00 63.78  ? 24  LEU   A CD1 1 
ATOM   157  C CD2 . LEU   A 1 24  ? -16.786 5.400   67.477 1.00 83.31  ? 24  LEU   A CD2 1 
ATOM   158  N N   . ASP   A 1 25  ? -21.356 6.383   69.860 1.00 92.62  ? 25  ASP   A N   1 
ATOM   159  C CA  . ASP   A 1 25  ? -22.679 6.877   69.490 1.00 90.06  ? 25  ASP   A CA  1 
ATOM   160  C C   . ASP   A 1 25  ? -23.164 7.937   70.471 1.00 89.88  ? 25  ASP   A C   1 
ATOM   161  O O   . ASP   A 1 25  ? -23.709 8.970   70.065 1.00 89.29  ? 25  ASP   A O   1 
ATOM   162  C CB  . ASP   A 1 25  ? -23.677 5.721   69.428 1.00 85.01  ? 25  ASP   A CB  1 
ATOM   163  C CG  . ASP   A 1 25  ? -23.407 4.775   68.276 1.00 103.32 ? 25  ASP   A CG  1 
ATOM   164  O OD1 . ASP   A 1 25  ? -22.365 4.927   67.604 1.00 100.69 ? 25  ASP   A OD1 1 
ATOM   165  O OD2 . ASP   A 1 25  ? -24.244 3.878   68.040 1.00 98.02  ? 25  ASP   A OD2 1 
ATOM   166  N N   . GLN   A 1 26  ? -22.975 7.690   71.768 1.00 89.00  ? 26  GLN   A N   1 
ATOM   167  C CA  . GLN   A 1 26  ? -23.429 8.630   72.786 1.00 83.71  ? 26  GLN   A CA  1 
ATOM   168  C C   . GLN   A 1 26  ? -22.742 9.978   72.640 1.00 91.22  ? 26  GLN   A C   1 
ATOM   169  O O   . GLN   A 1 26  ? -23.406 11.016  72.599 1.00 101.12 ? 26  GLN   A O   1 
ATOM   170  C CB  . GLN   A 1 26  ? -23.176 8.059   74.180 1.00 96.38  ? 26  GLN   A CB  1 
ATOM   171  C CG  . GLN   A 1 26  ? -24.074 6.906   74.565 1.00 105.01 ? 26  GLN   A CG  1 
ATOM   172  C CD  . GLN   A 1 26  ? -23.764 6.382   75.950 1.00 108.51 ? 26  GLN   A CD  1 
ATOM   173  O OE1 . GLN   A 1 26  ? -23.198 7.091   76.782 1.00 105.18 ? 26  GLN   A OE1 1 
ATOM   174  N NE2 . GLN   A 1 26  ? -24.130 5.134   76.204 1.00 112.05 ? 26  GLN   A NE2 1 
ATOM   175  N N   . LYS   A 1 27  ? -21.407 9.982   72.580 1.00 80.34  ? 27  LYS   A N   1 
ATOM   176  C CA  . LYS   A 1 27  ? -20.683 11.248  72.473 1.00 86.17  ? 27  LYS   A CA  1 
ATOM   177  C C   . LYS   A 1 27  ? -21.094 11.996  71.207 1.00 89.95  ? 27  LYS   A C   1 
ATOM   178  O O   . LYS   A 1 27  ? -21.295 13.223  71.230 1.00 93.89  ? 27  LYS   A O   1 
ATOM   179  C CB  . LYS   A 1 27  ? -19.173 10.979  72.511 1.00 80.31  ? 27  LYS   A CB  1 
ATOM   180  C CG  . LYS   A 1 27  ? -18.242 12.186  72.758 1.00 83.46  ? 27  LYS   A CG  1 
ATOM   181  C CD  . LYS   A 1 27  ? -18.146 13.194  71.622 1.00 78.48  ? 27  LYS   A CD  1 
ATOM   182  C CE  . LYS   A 1 27  ? -17.038 14.203  71.893 1.00 87.63  ? 27  LYS   A CE  1 
ATOM   183  N NZ  . LYS   A 1 27  ? -17.165 14.839  73.235 1.00 82.16  ? 27  LYS   A NZ  1 
ATOM   184  N N   . ILE   A 1 28  ? -21.272 11.264  70.102 1.00 77.83  ? 28  ILE   A N   1 
ATOM   185  C CA  . ILE   A 1 28  ? -21.662 11.893  68.843 1.00 84.23  ? 28  ILE   A CA  1 
ATOM   186  C C   . ILE   A 1 28  ? -23.034 12.542  68.974 1.00 92.10  ? 28  ILE   A C   1 
ATOM   187  O O   . ILE   A 1 28  ? -23.247 13.679  68.536 1.00 89.97  ? 28  ILE   A O   1 
ATOM   188  C CB  . ILE   A 1 28  ? -21.626 10.864  67.699 1.00 81.15  ? 28  ILE   A CB  1 
ATOM   189  C CG1 . ILE   A 1 28  ? -20.177 10.513  67.352 1.00 73.19  ? 28  ILE   A CG1 1 
ATOM   190  C CG2 . ILE   A 1 28  ? -22.375 11.384  66.483 1.00 74.43  ? 28  ILE   A CG2 1 
ATOM   191  C CD1 . ILE   A 1 28  ? -20.041 9.424   66.316 1.00 68.18  ? 28  ILE   A CD1 1 
ATOM   192  N N   . ASN   A 1 29  ? -23.990 11.827  69.576 1.00 96.98  ? 29  ASN   A N   1 
ATOM   193  C CA  . ASN   A 1 29  ? -25.311 12.409  69.791 1.00 97.63  ? 29  ASN   A CA  1 
ATOM   194  C C   . ASN   A 1 29  ? -25.243 13.609  70.728 1.00 102.48 ? 29  ASN   A C   1 
ATOM   195  O O   . ASN   A 1 29  ? -26.017 14.562  70.578 1.00 105.39 ? 29  ASN   A O   1 
ATOM   196  C CB  . ASN   A 1 29  ? -26.268 11.354  70.348 1.00 79.11  ? 29  ASN   A CB  1 
ATOM   197  C CG  . ASN   A 1 29  ? -26.425 10.161  69.423 1.00 99.75  ? 29  ASN   A CG  1 
ATOM   198  O OD1 . ASN   A 1 29  ? -26.162 10.250  68.224 1.00 82.08  ? 29  ASN   A OD1 1 
ATOM   199  N ND2 . ASN   A 1 29  ? -26.852 9.035   69.981 1.00 95.65  ? 29  ASN   A ND2 1 
ATOM   200  N N   . GLU   A 1 30  ? -24.328 13.578  71.701 1.00 101.34 ? 30  GLU   A N   1 
ATOM   201  C CA  . GLU   A 1 30  ? -24.214 14.672  72.659 1.00 100.00 ? 30  GLU   A CA  1 
ATOM   202  C C   . GLU   A 1 30  ? -23.706 15.945  72.000 1.00 106.68 ? 30  GLU   A C   1 
ATOM   203  O O   . GLU   A 1 30  ? -24.106 17.046  72.394 1.00 113.64 ? 30  GLU   A O   1 
ATOM   204  C CB  . GLU   A 1 30  ? -23.301 14.279  73.820 1.00 104.57 ? 30  GLU   A CB  1 
ATOM   205  C CG  . GLU   A 1 30  ? -23.838 13.147  74.676 1.00 113.64 ? 30  GLU   A CG  1 
ATOM   206  C CD  . GLU   A 1 30  ? -25.197 13.449  75.271 1.00 129.38 ? 30  GLU   A CD  1 
ATOM   207  O OE1 . GLU   A 1 30  ? -25.422 14.602  75.694 1.00 147.00 ? 30  GLU   A OE1 1 
ATOM   208  O OE2 . GLU   A 1 30  ? -26.042 12.531  75.313 1.00 124.26 ? 30  GLU   A OE2 1 
ATOM   209  N N   . VAL   A 1 31  ? -22.830 15.823  71.007 1.00 108.01 ? 31  VAL   A N   1 
ATOM   210  C CA  . VAL   A 1 31  ? -22.279 16.996  70.334 1.00 99.76  ? 31  VAL   A CA  1 
ATOM   211  C C   . VAL   A 1 31  ? -23.051 17.324  69.053 1.00 106.16 ? 31  VAL   A C   1 
ATOM   212  O O   . VAL   A 1 31  ? -22.523 18.003  68.173 1.00 111.76 ? 31  VAL   A O   1 
ATOM   213  C CB  . VAL   A 1 31  ? -20.778 16.833  70.048 1.00 92.62  ? 31  VAL   A CB  1 
ATOM   214  C CG1 . VAL   A 1 31  ? -19.990 16.789  71.349 1.00 101.70 ? 31  VAL   A CG1 1 
ATOM   215  C CG2 . VAL   A 1 31  ? -20.526 15.589  69.212 1.00 84.60  ? 31  VAL   A CG2 1 
ATOM   216  N N   . SER   A 1 32  ? -24.294 16.846  68.934 1.00 107.48 ? 32  SER   A N   1 
ATOM   217  C CA  . SER   A 1 32  ? -25.031 16.980  67.679 1.00 100.72 ? 32  SER   A CA  1 
ATOM   218  C C   . SER   A 1 32  ? -25.219 18.439  67.271 1.00 102.59 ? 32  SER   A C   1 
ATOM   219  O O   . SER   A 1 32  ? -25.099 18.775  66.087 1.00 98.89  ? 32  SER   A O   1 
ATOM   220  C CB  . SER   A 1 32  ? -26.385 16.282  67.799 1.00 100.17 ? 32  SER   A CB  1 
ATOM   221  O OG  . SER   A 1 32  ? -27.045 16.226  66.546 1.00 119.24 ? 32  SER   A OG  1 
ATOM   222  N N   . SER   A 1 33  ? -25.523 19.323  68.226 1.00 109.02 ? 33  SER   A N   1 
ATOM   223  C CA  . SER   A 1 33  ? -25.763 20.729  67.911 1.00 108.51 ? 33  SER   A CA  1 
ATOM   224  C C   . SER   A 1 33  ? -24.807 21.658  68.651 1.00 111.74 ? 33  SER   A C   1 
ATOM   225  O O   . SER   A 1 33  ? -25.121 22.836  68.849 1.00 106.26 ? 33  SER   A O   1 
ATOM   226  C CB  . SER   A 1 33  ? -27.214 21.109  68.219 1.00 110.39 ? 33  SER   A CB  1 
ATOM   227  O OG  . SER   A 1 33  ? -27.665 20.494  69.414 1.00 109.06 ? 33  SER   A OG  1 
ATOM   228  N N   . SER   A 1 34  ? -23.640 21.157  69.055 1.00 113.83 ? 34  SER   A N   1 
ATOM   229  C CA  . SER   A 1 34  ? -22.671 21.991  69.758 1.00 110.71 ? 34  SER   A CA  1 
ATOM   230  C C   . SER   A 1 34  ? -21.803 22.808  68.805 1.00 114.02 ? 34  SER   A C   1 
ATOM   231  O O   . SER   A 1 34  ? -21.392 23.920  69.157 1.00 122.00 ? 34  SER   A O   1 
ATOM   232  C CB  . SER   A 1 34  ? -21.812 21.119  70.668 1.00 109.58 ? 34  SER   A CB  1 
ATOM   233  O OG  . SER   A 1 34  ? -21.316 21.860  71.768 1.00 111.36 ? 34  SER   A OG  1 
ATOM   234  N N   . ASP   A 1 35  ? -21.500 22.262  67.626 1.00 109.86 ? 35  ASP   A N   1 
ATOM   235  C CA  . ASP   A 1 35  ? -20.658 22.789  66.542 1.00 98.36  ? 35  ASP   A CA  1 
ATOM   236  C C   . ASP   A 1 35  ? -19.165 22.592  66.843 1.00 97.50  ? 35  ASP   A C   1 
ATOM   237  O O   . ASP   A 1 35  ? -18.330 22.924  65.997 1.00 110.24 ? 35  ASP   A O   1 
ATOM   238  C CB  . ASP   A 1 35  ? -20.946 24.278  66.261 1.00 104.35 ? 35  ASP   A CB  1 
ATOM   239  C CG  . ASP   A 1 35  ? -20.250 24.817  65.010 1.00 115.16 ? 35  ASP   A CG  1 
ATOM   240  O OD1 . ASP   A 1 35  ? -19.582 24.050  64.284 1.00 118.76 ? 35  ASP   A OD1 1 
ATOM   241  O OD2 . ASP   A 1 35  ? -20.361 26.039  64.764 1.00 118.59 ? 35  ASP   A OD2 1 
ATOM   242  N N   . ASP   A 1 36  ? -18.790 22.030  67.993 1.00 98.24  ? 36  ASP   A N   1 
ATOM   243  C CA  . ASP   A 1 36  ? -17.402 21.625  68.225 1.00 92.11  ? 36  ASP   A CA  1 
ATOM   244  C C   . ASP   A 1 36  ? -17.320 20.136  67.898 1.00 89.66  ? 36  ASP   A C   1 
ATOM   245  O O   . ASP   A 1 36  ? -17.611 19.277  68.736 1.00 81.77  ? 36  ASP   A O   1 
ATOM   246  C CB  . ASP   A 1 36  ? -16.922 21.960  69.639 1.00 97.46  ? 36  ASP   A CB  1 
ATOM   247  C CG  . ASP   A 1 36  ? -17.802 21.380  70.733 1.00 111.90 ? 36  ASP   A CG  1 
ATOM   248  O OD1 . ASP   A 1 36  ? -18.866 20.820  70.422 1.00 120.01 ? 36  ASP   A OD1 1 
ATOM   249  O OD2 . ASP   A 1 36  ? -17.426 21.490  71.918 1.00 121.37 ? 36  ASP   A OD2 1 
ATOM   250  N N   . LYS   A 1 37  ? -16.898 19.831  66.675 1.00 71.98  ? 37  LYS   A N   1 
ATOM   251  C CA  . LYS   A 1 37  ? -16.947 18.459  66.196 1.00 65.34  ? 37  LYS   A CA  1 
ATOM   252  C C   . LYS   A 1 37  ? -15.571 17.997  65.744 1.00 63.79  ? 37  LYS   A C   1 
ATOM   253  O O   . LYS   A 1 37  ? -15.413 17.454  64.646 1.00 72.63  ? 37  LYS   A O   1 
ATOM   254  C CB  . LYS   A 1 37  ? -17.968 18.332  65.064 1.00 64.01  ? 37  LYS   A CB  1 
ATOM   255  C CG  . LYS   A 1 37  ? -19.383 18.686  65.492 1.00 65.01  ? 37  LYS   A CG  1 
ATOM   256  C CD  . LYS   A 1 37  ? -20.383 18.549  64.358 1.00 51.77  ? 37  LYS   A CD  1 
ATOM   257  C CE  . LYS   A 1 37  ? -21.795 18.798  64.868 1.00 63.98  ? 37  LYS   A CE  1 
ATOM   258  N NZ  . LYS   A 1 37  ? -22.830 18.163  64.005 1.00 75.07  ? 37  LYS   A NZ  1 
ATOM   259  N N   . ASP   A 1 38  ? -14.570 18.231  66.589 1.00 60.93  ? 38  ASP   A N   1 
ATOM   260  C CA  . ASP   A 1 38  ? -13.229 17.739  66.322 1.00 59.54  ? 38  ASP   A CA  1 
ATOM   261  C C   . ASP   A 1 38  ? -13.225 16.215  66.320 1.00 53.79  ? 38  ASP   A C   1 
ATOM   262  O O   . ASP   A 1 38  ? -14.033 15.568  66.990 1.00 56.79  ? 38  ASP   A O   1 
ATOM   263  C CB  . ASP   A 1 38  ? -12.250 18.264  67.374 1.00 76.11  ? 38  ASP   A CB  1 
ATOM   264  C CG  . ASP   A 1 38  ? -12.161 19.778  67.387 1.00 94.24  ? 38  ASP   A CG  1 
ATOM   265  O OD1 . ASP   A 1 38  ? -12.412 20.405  66.336 1.00 103.49 ? 38  ASP   A OD1 1 
ATOM   266  O OD2 . ASP   A 1 38  ? -11.838 20.342  68.455 1.00 87.82  ? 38  ASP   A OD2 1 
ATOM   267  N N   . ALA   A 1 39  ? -12.316 15.640  65.538 1.00 56.61  ? 39  ALA   A N   1 
ATOM   268  C CA  . ALA   A 1 39  ? -12.161 14.194  65.534 1.00 50.52  ? 39  ALA   A CA  1 
ATOM   269  C C   . ALA   A 1 39  ? -11.675 13.720  66.898 1.00 39.71  ? 39  ALA   A C   1 
ATOM   270  O O   . ALA   A 1 39  ? -10.983 14.442  67.620 1.00 42.78  ? 39  ALA   A O   1 
ATOM   271  C CB  . ALA   A 1 39  ? -11.179 13.768  64.442 1.00 45.98  ? 39  ALA   A CB  1 
ATOM   272  N N   . PHE   A 1 40  ? -12.060 12.502  67.271 1.00 34.48  ? 40  PHE   A N   1 
ATOM   273  C CA  . PHE   A 1 40  ? -11.635 11.992  68.565 1.00 42.84  ? 40  PHE   A CA  1 
ATOM   274  C C   . PHE   A 1 40  ? -11.561 10.472  68.526 1.00 54.65  ? 40  PHE   A C   1 
ATOM   275  O O   . PHE   A 1 40  ? -12.222 9.812   67.721 1.00 46.58  ? 40  PHE   A O   1 
ATOM   276  C CB  . PHE   A 1 40  ? -12.563 12.471  69.691 1.00 39.28  ? 40  PHE   A CB  1 
ATOM   277  C CG  . PHE   A 1 40  ? -13.963 11.953  69.583 1.00 42.77  ? 40  PHE   A CG  1 
ATOM   278  C CD1 . PHE   A 1 40  ? -14.887 12.585  68.769 1.00 59.17  ? 40  PHE   A CD1 1 
ATOM   279  C CD2 . PHE   A 1 40  ? -14.359 10.842  70.303 1.00 44.75  ? 40  PHE   A CD2 1 
ATOM   280  C CE1 . PHE   A 1 40  ? -16.177 12.110  68.666 1.00 54.27  ? 40  PHE   A CE1 1 
ATOM   281  C CE2 . PHE   A 1 40  ? -15.646 10.367  70.208 1.00 48.45  ? 40  PHE   A CE2 1 
ATOM   282  C CZ  . PHE   A 1 40  ? -16.557 10.999  69.386 1.00 52.79  ? 40  PHE   A CZ  1 
ATOM   283  N N   . TYR   A 1 41  ? -10.742 9.930   69.420 1.00 46.91  ? 41  TYR   A N   1 
ATOM   284  C CA  . TYR   A 1 41  ? -10.586 8.498   69.610 1.00 52.76  ? 41  TYR   A CA  1 
ATOM   285  C C   . TYR   A 1 41  ? -11.375 8.024   70.819 1.00 53.58  ? 41  TYR   A C   1 
ATOM   286  O O   . TYR   A 1 41  ? -11.489 8.731   71.822 1.00 55.36  ? 41  TYR   A O   1 
ATOM   287  C CB  . TYR   A 1 41  ? -9.118  8.127   69.818 1.00 57.11  ? 41  TYR   A CB  1 
ATOM   288  C CG  . TYR   A 1 41  ? -8.303  8.044   68.561 1.00 60.11  ? 41  TYR   A CG  1 
ATOM   289  C CD1 . TYR   A 1 41  ? -8.267  6.872   67.821 1.00 61.69  ? 41  TYR   A CD1 1 
ATOM   290  C CD2 . TYR   A 1 41  ? -7.553  9.124   68.122 1.00 54.80  ? 41  TYR   A CD2 1 
ATOM   291  C CE1 . TYR   A 1 41  ? -7.518  6.779   66.674 1.00 63.56  ? 41  TYR   A CE1 1 
ATOM   292  C CE2 . TYR   A 1 41  ? -6.800  9.041   66.972 1.00 49.44  ? 41  TYR   A CE2 1 
ATOM   293  C CZ  . TYR   A 1 41  ? -6.786  7.864   66.253 1.00 60.72  ? 41  TYR   A CZ  1 
ATOM   294  O OH  . TYR   A 1 41  ? -6.040  7.763   65.108 1.00 68.42  ? 41  TYR   A OH  1 
ATOM   295  N N   . VAL   A 1 42  ? -11.905 6.810   70.718 1.00 47.13  ? 42  VAL   A N   1 
ATOM   296  C CA  . VAL   A 1 42  ? -12.359 6.044   71.873 1.00 48.83  ? 42  VAL   A CA  1 
ATOM   297  C C   . VAL   A 1 42  ? -11.422 4.854   72.019 1.00 62.78  ? 42  VAL   A C   1 
ATOM   298  O O   . VAL   A 1 42  ? -11.296 4.038   71.095 1.00 68.83  ? 42  VAL   A O   1 
ATOM   299  C CB  . VAL   A 1 42  ? -13.818 5.589   71.725 1.00 57.14  ? 42  VAL   A CB  1 
ATOM   300  C CG1 . VAL   A 1 42  ? -14.189 4.652   72.861 1.00 62.82  ? 42  VAL   A CG1 1 
ATOM   301  C CG2 . VAL   A 1 42  ? -14.744 6.788   71.700 1.00 60.18  ? 42  VAL   A CG2 1 
ATOM   302  N N   . ALA   A 1 43  ? -10.754 4.763   73.170 1.00 56.33  ? 43  ALA   A N   1 
ATOM   303  C CA  . ALA   A 1 43  ? -9.759  3.727   73.435 1.00 49.00  ? 43  ALA   A CA  1 
ATOM   304  C C   . ALA   A 1 43  ? -10.249 2.845   74.577 1.00 56.90  ? 43  ALA   A C   1 
ATOM   305  O O   . ALA   A 1 43  ? -10.351 3.303   75.721 1.00 59.45  ? 43  ALA   A O   1 
ATOM   306  C CB  . ALA   A 1 43  ? -8.403  4.349   73.763 1.00 49.34  ? 43  ALA   A CB  1 
ATOM   307  N N   . ASP   A 1 44  ? -10.542 1.582   74.268 1.00 60.46  ? 44  ASP   A N   1 
ATOM   308  C CA  . ASP   A 1 44  ? -11.043 0.619   75.250 1.00 65.03  ? 44  ASP   A CA  1 
ATOM   309  C C   . ASP   A 1 44  ? -9.869  -0.175  75.812 1.00 60.98  ? 44  ASP   A C   1 
ATOM   310  O O   . ASP   A 1 44  ? -9.345  -1.078  75.157 1.00 78.17  ? 44  ASP   A O   1 
ATOM   311  C CB  . ASP   A 1 44  ? -12.082 -0.301  74.617 1.00 72.34  ? 44  ASP   A CB  1 
ATOM   312  C CG  . ASP   A 1 44  ? -12.745 -1.225  75.628 1.00 84.52  ? 44  ASP   A CG  1 
ATOM   313  O OD1 . ASP   A 1 44  ? -12.448 -1.116  76.838 1.00 78.77  ? 44  ASP   A OD1 1 
ATOM   314  O OD2 . ASP   A 1 44  ? -13.568 -2.066  75.210 1.00 80.92  ? 44  ASP   A OD2 1 
ATOM   315  N N   . LEU   A 1 45  ? -9.451  0.164   77.035 1.00 43.71  ? 45  LEU   A N   1 
ATOM   316  C CA  . LEU   A 1 45  ? -8.380  -0.583  77.688 1.00 48.31  ? 45  LEU   A CA  1 
ATOM   317  C C   . LEU   A 1 45  ? -8.796  -2.023  77.981 1.00 52.85  ? 45  LEU   A C   1 
ATOM   318  O O   . LEU   A 1 45  ? -7.946  -2.929  78.019 1.00 57.27  ? 45  LEU   A O   1 
ATOM   319  C CB  . LEU   A 1 45  ? -7.966  0.138   78.969 1.00 58.87  ? 45  LEU   A CB  1 
ATOM   320  C CG  . LEU   A 1 45  ? -7.581  1.609   78.768 1.00 57.18  ? 45  LEU   A CG  1 
ATOM   321  C CD1 . LEU   A 1 45  ? -7.299  2.303   80.093 1.00 39.81  ? 45  LEU   A CD1 1 
ATOM   322  C CD2 . LEU   A 1 45  ? -6.387  1.730   77.836 1.00 64.34  ? 45  LEU   A CD2 1 
ATOM   323  N N   . GLY   A 1 46  ? -10.094 -2.254  78.191 1.00 56.43  ? 46  GLY   A N   1 
ATOM   324  C CA  . GLY   A 1 46  ? -10.576 -3.613  78.362 1.00 62.62  ? 46  GLY   A CA  1 
ATOM   325  C C   . GLY   A 1 46  ? -10.270 -4.492  77.168 1.00 64.22  ? 46  GLY   A C   1 
ATOM   326  O O   . GLY   A 1 46  ? -10.049 -5.696  77.318 1.00 65.80  ? 46  GLY   A O   1 
ATOM   327  N N   . ASP   A 1 47  ? -10.238 -3.904  75.970 1.00 68.55  ? 47  ASP   A N   1 
ATOM   328  C CA  . ASP   A 1 47  ? -9.824  -4.660  74.794 1.00 72.28  ? 47  ASP   A CA  1 
ATOM   329  C C   . ASP   A 1 47  ? -8.369  -5.093  74.913 1.00 65.66  ? 47  ASP   A C   1 
ATOM   330  O O   . ASP   A 1 47  ? -8.004  -6.194  74.489 1.00 67.12  ? 47  ASP   A O   1 
ATOM   331  C CB  . ASP   A 1 47  ? -10.039 -3.829  73.529 1.00 72.88  ? 47  ASP   A CB  1 
ATOM   332  C CG  . ASP   A 1 47  ? -9.894  -4.650  72.263 1.00 78.41  ? 47  ASP   A CG  1 
ATOM   333  O OD1 . ASP   A 1 47  ? -10.670 -5.613  72.087 1.00 73.76  ? 47  ASP   A OD1 1 
ATOM   334  O OD2 . ASP   A 1 47  ? -9.005  -4.335  71.443 1.00 89.87  ? 47  ASP   A OD2 1 
ATOM   335  N N   . ILE   A 1 48  ? -7.526  -4.245  75.502 1.00 55.08  ? 48  ILE   A N   1 
ATOM   336  C CA  . ILE   A 1 48  ? -6.133  -4.617  75.723 1.00 47.95  ? 48  ILE   A CA  1 
ATOM   337  C C   . ILE   A 1 48  ? -6.036  -5.768  76.715 1.00 62.43  ? 48  ILE   A C   1 
ATOM   338  O O   . ILE   A 1 48  ? -5.236  -6.697  76.536 1.00 62.88  ? 48  ILE   A O   1 
ATOM   339  C CB  . ILE   A 1 48  ? -5.331  -3.395  76.196 1.00 51.55  ? 48  ILE   A CB  1 
ATOM   340  C CG1 . ILE   A 1 48  ? -5.370  -2.300  75.134 1.00 58.32  ? 48  ILE   A CG1 1 
ATOM   341  C CG2 . ILE   A 1 48  ? -3.905  -3.790  76.516 1.00 53.76  ? 48  ILE   A CG2 1 
ATOM   342  C CD1 . ILE   A 1 48  ? -4.814  -0.994  75.612 1.00 61.11  ? 48  ILE   A CD1 1 
ATOM   343  N N   . LEU   A 1 49  ? -6.841  -5.728  77.780 1.00 68.69  ? 49  LEU   A N   1 
ATOM   344  C CA  . LEU   A 1 49  ? -6.845  -6.846  78.720 1.00 57.79  ? 49  LEU   A CA  1 
ATOM   345  C C   . LEU   A 1 49  ? -7.325  -8.131  78.052 1.00 63.10  ? 49  LEU   A C   1 
ATOM   346  O O   . LEU   A 1 49  ? -6.785  -9.217  78.307 1.00 61.82  ? 49  LEU   A O   1 
ATOM   347  C CB  . LEU   A 1 49  ? -7.720  -6.520  79.924 1.00 61.69  ? 49  LEU   A CB  1 
ATOM   348  C CG  . LEU   A 1 49  ? -7.242  -5.396  80.836 1.00 70.82  ? 49  LEU   A CG  1 
ATOM   349  C CD1 . LEU   A 1 49  ? -8.332  -5.105  81.828 1.00 91.96  ? 49  LEU   A CD1 1 
ATOM   350  C CD2 . LEU   A 1 49  ? -5.953  -5.762  81.545 1.00 69.76  ? 49  LEU   A CD2 1 
ATOM   351  N N   . LYS   A 1 50  ? -8.340  -8.023  77.191 1.00 53.99  ? 50  LYS   A N   1 
ATOM   352  C CA  . LYS   A 1 50  ? -8.800  -9.178  76.427 1.00 55.19  ? 50  LYS   A CA  1 
ATOM   353  C C   . LYS   A 1 50  ? -7.680  -9.736  75.561 1.00 64.21  ? 50  LYS   A C   1 
ATOM   354  O O   . LYS   A 1 50  ? -7.479  -10.956 75.498 1.00 69.86  ? 50  LYS   A O   1 
ATOM   355  C CB  . LYS   A 1 50  ? -9.991  -8.787  75.553 1.00 64.67  ? 50  LYS   A CB  1 
ATOM   356  C CG  . LYS   A 1 50  ? -11.345 -8.803  76.240 1.00 73.28  ? 50  LYS   A CG  1 
ATOM   357  C CD  . LYS   A 1 50  ? -12.433 -8.386  75.257 1.00 78.53  ? 50  LYS   A CD  1 
ATOM   358  C CE  . LYS   A 1 50  ? -13.814 -8.406  75.891 1.00 89.22  ? 50  LYS   A CE  1 
ATOM   359  N NZ  . LYS   A 1 50  ? -14.312 -9.792  76.100 1.00 90.68  ? 50  LYS   A NZ  1 
ATOM   360  N N   . LYS   A 1 51  ? -6.945  -8.853  74.882 1.00 60.85  ? 51  LYS   A N   1 
ATOM   361  C CA  . LYS   A 1 51  ? -5.829  -9.290  74.051 1.00 56.17  ? 51  LYS   A CA  1 
ATOM   362  C C   . LYS   A 1 51  ? -4.767  -9.995  74.883 1.00 62.45  ? 51  LYS   A C   1 
ATOM   363  O O   . LYS   A 1 51  ? -4.189  -10.994 74.442 1.00 54.44  ? 51  LYS   A O   1 
ATOM   364  C CB  . LYS   A 1 51  ? -5.224  -8.099  73.307 1.00 52.09  ? 51  LYS   A CB  1 
ATOM   365  C CG  . LYS   A 1 51  ? -6.131  -7.497  72.247 1.00 54.96  ? 51  LYS   A CG  1 
ATOM   366  C CD  . LYS   A 1 51  ? -6.340  -8.450  71.082 1.00 55.20  ? 51  LYS   A CD  1 
ATOM   367  C CE  . LYS   A 1 51  ? -7.161  -7.798  69.982 1.00 48.47  ? 51  LYS   A CE  1 
ATOM   368  N NZ  . LYS   A 1 51  ? -6.465  -6.625  69.387 1.00 60.94  ? 51  LYS   A NZ  1 
ATOM   369  N N   . HIS   A 1 52  ? -4.490  -9.488  76.087 1.00 54.40  ? 52  HIS   A N   1 
ATOM   370  C CA  . HIS   A 1 52  ? -3.496  -10.147 76.931 1.00 61.06  ? 52  HIS   A CA  1 
ATOM   371  C C   . HIS   A 1 52  ? -3.962  -11.532 77.367 1.00 59.46  ? 52  HIS   A C   1 
ATOM   372  O O   . HIS   A 1 52  ? -3.162  -12.474 77.406 1.00 67.94  ? 52  HIS   A O   1 
ATOM   373  C CB  . HIS   A 1 52  ? -3.162  -9.307  78.158 1.00 53.53  ? 52  HIS   A CB  1 
ATOM   374  C CG  . HIS   A 1 52  ? -2.060  -9.893  78.985 1.00 62.22  ? 52  HIS   A CG  1 
ATOM   375  N ND1 . HIS   A 1 52  ? -0.731  -9.775  78.641 1.00 62.29  ? 52  HIS   A ND1 1 
ATOM   376  C CD2 . HIS   A 1 52  ? -2.093  -10.650 80.107 1.00 62.57  ? 52  HIS   A CD2 1 
ATOM   377  C CE1 . HIS   A 1 52  ? 0.011   -10.405 79.535 1.00 54.16  ? 52  HIS   A CE1 1 
ATOM   378  N NE2 . HIS   A 1 52  ? -0.791  -10.945 80.435 1.00 64.26  ? 52  HIS   A NE2 1 
ATOM   379  N N   . LEU   A 1 53  ? -5.231  -11.663 77.759 1.00 57.37  ? 53  LEU   A N   1 
ATOM   380  C CA  . LEU   A 1 53  ? -5.760  -12.987 78.083 1.00 63.70  ? 53  LEU   A CA  1 
ATOM   381  C C   . LEU   A 1 53  ? -5.614  -13.930 76.897 1.00 60.81  ? 53  LEU   A C   1 
ATOM   382  O O   . LEU   A 1 53  ? -5.179  -15.081 77.043 1.00 65.18  ? 53  LEU   A O   1 
ATOM   383  C CB  . LEU   A 1 53  ? -7.228  -12.893 78.495 1.00 68.98  ? 53  LEU   A CB  1 
ATOM   384  C CG  . LEU   A 1 53  ? -7.591  -12.438 79.904 1.00 56.91  ? 53  LEU   A CG  1 
ATOM   385  C CD1 . LEU   A 1 53  ? -9.101  -12.401 80.020 1.00 57.95  ? 53  LEU   A CD1 1 
ATOM   386  C CD2 . LEU   A 1 53  ? -6.994  -13.376 80.930 1.00 57.52  ? 53  LEU   A CD2 1 
ATOM   387  N N   . ARG   A 1 54  ? -5.968  -13.445 75.706 1.00 61.10  ? 54  ARG   A N   1 
ATOM   388  C CA  . ARG   A 1 54  ? -5.871  -14.258 74.500 1.00 53.21  ? 54  ARG   A CA  1 
ATOM   389  C C   . ARG   A 1 54  ? -4.433  -14.685 74.236 1.00 56.13  ? 54  ARG   A C   1 
ATOM   390  O O   . ARG   A 1 54  ? -4.179  -15.829 73.841 1.00 53.77  ? 54  ARG   A O   1 
ATOM   391  C CB  . ARG   A 1 54  ? -6.439  -13.466 73.323 1.00 50.36  ? 54  ARG   A CB  1 
ATOM   392  C CG  . ARG   A 1 54  ? -6.604  -14.226 72.026 1.00 55.36  ? 54  ARG   A CG  1 
ATOM   393  C CD  . ARG   A 1 54  ? -7.368  -13.358 71.042 1.00 58.98  ? 54  ARG   A CD  1 
ATOM   394  N NE  . ARG   A 1 54  ? -7.362  -13.885 69.683 1.00 63.60  ? 54  ARG   A NE  1 
ATOM   395  C CZ  . ARG   A 1 54  ? -7.731  -13.182 68.619 1.00 67.22  ? 54  ARG   A CZ  1 
ATOM   396  N NH1 . ARG   A 1 54  ? -7.701  -13.729 67.412 1.00 77.62  ? 54  ARG   A NH1 1 
ATOM   397  N NH2 . ARG   A 1 54  ? -8.129  -11.925 68.763 1.00 73.47  ? 54  ARG   A NH2 1 
ATOM   398  N N   . TRP   A 1 55  ? -3.477  -13.779 74.459 1.00 61.72  ? 55  TRP   A N   1 
ATOM   399  C CA  . TRP   A 1 55  ? -2.067  -14.112 74.278 1.00 58.44  ? 55  TRP   A CA  1 
ATOM   400  C C   . TRP   A 1 55  ? -1.623  -15.171 75.277 1.00 53.05  ? 55  TRP   A C   1 
ATOM   401  O O   . TRP   A 1 55  ? -0.978  -16.158 74.906 1.00 59.83  ? 55  TRP   A O   1 
ATOM   402  C CB  . TRP   A 1 55  ? -1.208  -12.853 74.410 1.00 58.70  ? 55  TRP   A CB  1 
ATOM   403  C CG  . TRP   A 1 55  ? 0.271   -13.109 74.292 1.00 56.22  ? 55  TRP   A CG  1 
ATOM   404  C CD1 . TRP   A 1 55  ? 1.101   -13.606 75.257 1.00 65.20  ? 55  TRP   A CD1 1 
ATOM   405  C CD2 . TRP   A 1 55  ? 1.091   -12.886 73.137 1.00 57.88  ? 55  TRP   A CD2 1 
ATOM   406  N NE1 . TRP   A 1 55  ? 2.383   -13.704 74.775 1.00 60.63  ? 55  TRP   A NE1 1 
ATOM   407  C CE2 . TRP   A 1 55  ? 2.404   -13.268 73.477 1.00 54.74  ? 55  TRP   A CE2 1 
ATOM   408  C CE3 . TRP   A 1 55  ? 0.841   -12.399 71.850 1.00 67.84  ? 55  TRP   A CE3 1 
ATOM   409  C CZ2 . TRP   A 1 55  ? 3.464   -13.178 72.576 1.00 58.55  ? 55  TRP   A CZ2 1 
ATOM   410  C CZ3 . TRP   A 1 55  ? 1.896   -12.311 70.957 1.00 65.28  ? 55  TRP   A CZ3 1 
ATOM   411  C CH2 . TRP   A 1 55  ? 3.190   -12.698 71.325 1.00 63.90  ? 55  TRP   A CH2 1 
ATOM   412  N N   . LEU   A 1 56  ? -1.941  -14.971 76.559 1.00 63.17  ? 56  LEU   A N   1 
ATOM   413  C CA  . LEU   A 1 56  ? -1.608  -15.969 77.570 1.00 56.82  ? 56  LEU   A CA  1 
ATOM   414  C C   . LEU   A 1 56  ? -2.176  -17.333 77.210 1.00 64.22  ? 56  LEU   A C   1 
ATOM   415  O O   . LEU   A 1 56  ? -1.543  -18.362 77.478 1.00 72.98  ? 56  LEU   A O   1 
ATOM   416  C CB  . LEU   A 1 56  ? -2.125  -15.536 78.942 1.00 44.77  ? 56  LEU   A CB  1 
ATOM   417  C CG  . LEU   A 1 56  ? -1.492  -14.298 79.577 1.00 49.62  ? 56  LEU   A CG  1 
ATOM   418  C CD1 . LEU   A 1 56  ? -2.139  -14.020 80.919 1.00 58.65  ? 56  LEU   A CD1 1 
ATOM   419  C CD2 . LEU   A 1 56  ? 0.006   -14.479 79.733 1.00 53.32  ? 56  LEU   A CD2 1 
ATOM   420  N N   . LYS   A 1 57  ? -3.357  -17.362 76.590 1.00 59.17  ? 57  LYS   A N   1 
ATOM   421  C CA  . LYS   A 1 57  ? -3.954  -18.642 76.226 1.00 57.82  ? 57  LYS   A CA  1 
ATOM   422  C C   . LYS   A 1 57  ? -3.298  -19.252 74.991 1.00 63.59  ? 57  LYS   A C   1 
ATOM   423  O O   . LYS   A 1 57  ? -3.146  -20.475 74.914 1.00 79.34  ? 57  LYS   A O   1 
ATOM   424  C CB  . LYS   A 1 57  ? -5.454  -18.474 75.992 1.00 66.58  ? 57  LYS   A CB  1 
ATOM   425  C CG  . LYS   A 1 57  ? -6.176  -19.784 75.720 1.00 68.20  ? 57  LYS   A CG  1 
ATOM   426  C CD  . LYS   A 1 57  ? -7.639  -19.550 75.405 1.00 83.68  ? 57  LYS   A CD  1 
ATOM   427  C CE  . LYS   A 1 57  ? -8.333  -20.853 75.059 1.00 87.08  ? 57  LYS   A CE  1 
ATOM   428  N NZ  . LYS   A 1 57  ? -9.776  -20.651 74.753 1.00 94.47  ? 57  LYS   A NZ  1 
ATOM   429  N N   . ALA   A 1 58  ? -2.892  -18.425 74.026 1.00 68.12  ? 58  ALA   A N   1 
ATOM   430  C CA  . ALA   A 1 58  ? -2.402  -18.940 72.752 1.00 52.75  ? 58  ALA   A CA  1 
ATOM   431  C C   . ALA   A 1 58  ? -0.908  -19.240 72.747 1.00 58.81  ? 58  ALA   A C   1 
ATOM   432  O O   . ALA   A 1 58  ? -0.480  -20.182 72.071 1.00 56.35  ? 58  ALA   A O   1 
ATOM   433  C CB  . ALA   A 1 58  ? -2.718  -17.950 71.628 1.00 51.86  ? 58  ALA   A CB  1 
ATOM   434  N N   . LEU   A 1 59  ? -0.103  -18.471 73.477 1.00 64.95  ? 59  LEU   A N   1 
ATOM   435  C CA  . LEU   A 1 59  ? 1.351   -18.634 73.495 1.00 52.45  ? 59  LEU   A CA  1 
ATOM   436  C C   . LEU   A 1 59  ? 1.826   -18.720 74.940 1.00 57.62  ? 59  LEU   A C   1 
ATOM   437  O O   . LEU   A 1 59  ? 2.504   -17.815 75.442 1.00 64.02  ? 59  LEU   A O   1 
ATOM   438  C CB  . LEU   A 1 59  ? 2.039   -17.484 72.757 1.00 55.76  ? 59  LEU   A CB  1 
ATOM   439  C CG  . LEU   A 1 59  ? 1.827   -17.427 71.242 1.00 52.73  ? 59  LEU   A CG  1 
ATOM   440  C CD1 . LEU   A 1 59  ? 2.336   -16.113 70.678 1.00 61.96  ? 59  LEU   A CD1 1 
ATOM   441  C CD2 . LEU   A 1 59  ? 2.505   -18.600 70.554 1.00 55.45  ? 59  LEU   A CD2 1 
ATOM   442  N N   . PRO   A 1 60  ? 1.487   -19.806 75.641 1.00 63.79  ? 60  PRO   A N   1 
ATOM   443  C CA  . PRO   A 1 60  ? 1.810   -19.883 77.076 1.00 53.00  ? 60  PRO   A CA  1 
ATOM   444  C C   . PRO   A 1 60  ? 3.298   -19.869 77.375 1.00 57.18  ? 60  PRO   A C   1 
ATOM   445  O O   . PRO   A 1 60  ? 3.684   -19.515 78.495 1.00 62.18  ? 60  PRO   A O   1 
ATOM   446  C CB  . PRO   A 1 60  ? 1.167   -21.206 77.512 1.00 56.36  ? 60  PRO   A CB  1 
ATOM   447  C CG  . PRO   A 1 60  ? 1.065   -22.012 76.264 1.00 64.50  ? 60  PRO   A CG  1 
ATOM   448  C CD  . PRO   A 1 60  ? 0.847   -21.038 75.147 1.00 68.16  ? 60  PRO   A CD  1 
ATOM   449  N N   . ARG   A 1 61  ? 4.144   -20.233 76.416 1.00 56.42  ? 61  ARG   A N   1 
ATOM   450  C CA  . ARG   A 1 61  ? 5.584   -20.264 76.631 1.00 51.08  ? 61  ARG   A CA  1 
ATOM   451  C C   . ARG   A 1 61  ? 6.278   -18.958 76.269 1.00 64.64  ? 61  ARG   A C   1 
ATOM   452  O O   . ARG   A 1 61  ? 7.491   -18.845 76.476 1.00 63.47  ? 61  ARG   A O   1 
ATOM   453  C CB  . ARG   A 1 61  ? 6.211   -21.407 75.828 1.00 49.72  ? 61  ARG   A CB  1 
ATOM   454  C CG  . ARG   A 1 61  ? 5.735   -22.791 76.219 1.00 52.61  ? 61  ARG   A CG  1 
ATOM   455  C CD  . ARG   A 1 61  ? 6.517   -23.836 75.449 1.00 57.84  ? 61  ARG   A CD  1 
ATOM   456  N NE  . ARG   A 1 61  ? 7.947   -23.740 75.726 1.00 57.29  ? 61  ARG   A NE  1 
ATOM   457  C CZ  . ARG   A 1 61  ? 8.896   -24.219 74.929 1.00 71.53  ? 61  ARG   A CZ  1 
ATOM   458  N NH1 . ARG   A 1 61  ? 8.570   -24.826 73.795 1.00 71.43  ? 61  ARG   A NH1 1 
ATOM   459  N NH2 . ARG   A 1 61  ? 10.173  -24.087 75.261 1.00 64.15  ? 61  ARG   A NH2 1 
ATOM   460  N N   . VAL   A 1 62  ? 5.551   -17.974 75.747 1.00 62.94  ? 62  VAL   A N   1 
ATOM   461  C CA  . VAL   A 1 62  ? 6.144   -16.771 75.170 1.00 58.80  ? 62  VAL   A CA  1 
ATOM   462  C C   . VAL   A 1 62  ? 5.740   -15.572 76.016 1.00 58.47  ? 62  VAL   A C   1 
ATOM   463  O O   . VAL   A 1 62  ? 4.547   -15.267 76.146 1.00 62.12  ? 62  VAL   A O   1 
ATOM   464  C CB  . VAL   A 1 62  ? 5.716   -16.581 73.708 1.00 52.77  ? 62  VAL   A CB  1 
ATOM   465  C CG1 . VAL   A 1 62  ? 6.487   -15.436 73.074 1.00 51.08  ? 62  VAL   A CG1 1 
ATOM   466  C CG2 . VAL   A 1 62  ? 5.919   -17.868 72.926 1.00 49.87  ? 62  VAL   A CG2 1 
ATOM   467  N N   . THR   A 1 63  ? 6.732   -14.894 76.588 1.00 50.35  ? 63  THR   A N   1 
ATOM   468  C CA  . THR   A 1 63  ? 6.478   -13.686 77.363 1.00 59.56  ? 63  THR   A CA  1 
ATOM   469  C C   . THR   A 1 63  ? 6.380   -12.486 76.426 1.00 66.27  ? 63  THR   A C   1 
ATOM   470  O O   . THR   A 1 63  ? 7.324   -12.224 75.673 1.00 66.37  ? 63  THR   A O   1 
ATOM   471  C CB  . THR   A 1 63  ? 7.589   -13.458 78.381 1.00 62.29  ? 63  THR   A CB  1 
ATOM   472  O OG1 . THR   A 1 63  ? 7.712   -14.610 79.224 1.00 61.63  ? 63  THR   A OG1 1 
ATOM   473  C CG2 . THR   A 1 63  ? 7.276   -12.244 79.242 1.00 49.15  ? 63  THR   A CG2 1 
ATOM   474  N N   . PRO   A 1 64  ? 5.275   -11.739 76.438 1.00 61.84  ? 64  PRO   A N   1 
ATOM   475  C CA  . PRO   A 1 64  ? 5.134   -10.605 75.511 1.00 61.15  ? 64  PRO   A CA  1 
ATOM   476  C C   . PRO   A 1 64  ? 5.853   -9.362  76.023 1.00 58.24  ? 64  PRO   A C   1 
ATOM   477  O O   . PRO   A 1 64  ? 5.735   -8.998  77.196 1.00 60.21  ? 64  PRO   A O   1 
ATOM   478  C CB  . PRO   A 1 64  ? 3.618   -10.386 75.451 1.00 55.21  ? 64  PRO   A CB  1 
ATOM   479  C CG  . PRO   A 1 64  ? 3.131   -10.865 76.781 1.00 59.94  ? 64  PRO   A CG  1 
ATOM   480  C CD  . PRO   A 1 64  ? 4.033   -12.005 77.185 1.00 56.26  ? 64  PRO   A CD  1 
ATOM   481  N N   . PHE   A 1 65  ? 6.615   -8.722  75.135 1.00 51.82  ? 65  PHE   A N   1 
ATOM   482  C CA  . PHE   A 1 65  ? 7.228   -7.419  75.387 1.00 50.32  ? 65  PHE   A CA  1 
ATOM   483  C C   . PHE   A 1 65  ? 6.612   -6.411  74.423 1.00 50.98  ? 65  PHE   A C   1 
ATOM   484  O O   . PHE   A 1 65  ? 6.876   -6.460  73.218 1.00 64.96  ? 65  PHE   A O   1 
ATOM   485  C CB  . PHE   A 1 65  ? 8.746   -7.478  75.225 1.00 47.47  ? 65  PHE   A CB  1 
ATOM   486  C CG  . PHE   A 1 65  ? 9.462   -8.031  76.422 1.00 49.40  ? 65  PHE   A CG  1 
ATOM   487  C CD1 . PHE   A 1 65  ? 9.243   -9.334  76.835 1.00 48.15  ? 65  PHE   A CD1 1 
ATOM   488  C CD2 . PHE   A 1 65  ? 10.355  -7.249  77.134 1.00 62.38  ? 65  PHE   A CD2 1 
ATOM   489  C CE1 . PHE   A 1 65  ? 9.901   -9.845  77.936 1.00 52.03  ? 65  PHE   A CE1 1 
ATOM   490  C CE2 . PHE   A 1 65  ? 11.015  -7.754  78.239 1.00 49.25  ? 65  PHE   A CE2 1 
ATOM   491  C CZ  . PHE   A 1 65  ? 10.788  -9.055  78.638 1.00 48.97  ? 65  PHE   A CZ  1 
ATOM   492  N N   . TYR   A 1 66  ? 5.794   -5.502  74.947 1.00 48.55  ? 66  TYR   A N   1 
ATOM   493  C CA  . TYR   A 1 66  ? 5.069   -4.567  74.094 1.00 48.63  ? 66  TYR   A CA  1 
ATOM   494  C C   . TYR   A 1 66  ? 6.020   -3.620  73.370 1.00 53.26  ? 66  TYR   A C   1 
ATOM   495  O O   . TYR   A 1 66  ? 6.903   -3.013  73.985 1.00 50.09  ? 66  TYR   A O   1 
ATOM   496  C CB  . TYR   A 1 66  ? 4.066   -3.767  74.921 1.00 40.74  ? 66  TYR   A CB  1 
ATOM   497  C CG  . TYR   A 1 66  ? 3.384   -2.665  74.142 1.00 51.02  ? 66  TYR   A CG  1 
ATOM   498  C CD1 . TYR   A 1 66  ? 2.539   -2.958  73.078 1.00 56.06  ? 66  TYR   A CD1 1 
ATOM   499  C CD2 . TYR   A 1 66  ? 3.583   -1.332  74.472 1.00 55.29  ? 66  TYR   A CD2 1 
ATOM   500  C CE1 . TYR   A 1 66  ? 1.914   -1.953  72.365 1.00 52.19  ? 66  TYR   A CE1 1 
ATOM   501  C CE2 . TYR   A 1 66  ? 2.962   -0.321  73.765 1.00 55.70  ? 66  TYR   A CE2 1 
ATOM   502  C CZ  . TYR   A 1 66  ? 2.129   -0.636  72.714 1.00 54.98  ? 66  TYR   A CZ  1 
ATOM   503  O OH  . TYR   A 1 66  ? 1.511   0.371   72.010 1.00 59.83  ? 66  TYR   A OH  1 
ATOM   504  N N   . ALA   A 1 67  ? 5.834   -3.494  72.056 1.00 45.92  ? 67  ALA   A N   1 
ATOM   505  C CA  . ALA   A 1 67  ? 6.626   -2.578  71.236 1.00 47.92  ? 67  ALA   A CA  1 
ATOM   506  C C   . ALA   A 1 67  ? 6.065   -1.172  71.408 1.00 44.99  ? 67  ALA   A C   1 
ATOM   507  O O   . ALA   A 1 67  ? 5.046   -0.820  70.813 1.00 49.29  ? 67  ALA   A O   1 
ATOM   508  C CB  . ALA   A 1 67  ? 6.614   -3.010  69.776 1.00 41.02  ? 67  ALA   A CB  1 
ATOM   509  N N   . VAL   A 1 68  ? 6.731   -0.366  72.240 1.00 52.07  ? 68  VAL   A N   1 
ATOM   510  C CA  . VAL   A 1 68  ? 6.221   0.955   72.600 1.00 52.68  ? 68  VAL   A CA  1 
ATOM   511  C C   . VAL   A 1 68  ? 6.035   1.837   71.372 1.00 51.02  ? 68  VAL   A C   1 
ATOM   512  O O   . VAL   A 1 68  ? 5.092   2.637   71.308 1.00 49.99  ? 68  VAL   A O   1 
ATOM   513  C CB  . VAL   A 1 68  ? 7.164   1.614   73.627 1.00 43.38  ? 68  VAL   A CB  1 
ATOM   514  C CG1 . VAL   A 1 68  ? 6.732   3.046   73.921 1.00 47.48  ? 68  VAL   A CG1 1 
ATOM   515  C CG2 . VAL   A 1 68  ? 7.202   0.792   74.904 1.00 56.10  ? 68  VAL   A CG2 1 
ATOM   516  N N   . LYS   A 1 69  ? 6.907   1.698   70.370 1.00 59.97  ? 69  LYS   A N   1 
ATOM   517  C CA  . LYS   A 1 69  ? 6.836   2.567   69.198 1.00 58.32  ? 69  LYS   A CA  1 
ATOM   518  C C   . LYS   A 1 69  ? 5.516   2.434   68.454 1.00 44.83  ? 69  LYS   A C   1 
ATOM   519  O O   . LYS   A 1 69  ? 5.150   3.338   67.697 1.00 57.52  ? 69  LYS   A O   1 
ATOM   520  C CB  . LYS   A 1 69  ? 8.023   2.295   68.275 1.00 61.16  ? 69  LYS   A CB  1 
ATOM   521  C CG  . LYS   A 1 69  ? 8.028   0.975   67.536 1.00 55.64  ? 69  LYS   A CG  1 
ATOM   522  C CD  . LYS   A 1 69  ? 9.331   0.868   66.757 1.00 87.56  ? 69  LYS   A CD  1 
ATOM   523  C CE  . LYS   A 1 69  ? 9.276   -0.174  65.673 1.00 83.23  ? 69  LYS   A CE  1 
ATOM   524  N NZ  . LYS   A 1 69  ? 8.267   0.199   64.651 1.00 82.55  ? 69  LYS   A NZ  1 
ATOM   525  N N   . CYS   A 1 70  ? 4.786   1.339   68.664 1.00 49.51  ? 70  CYS   A N   1 
ATOM   526  C CA  . CYS   A 1 70  ? 3.498   1.177   68.000 1.00 47.82  ? 70  CYS   A CA  1 
ATOM   527  C C   . CYS   A 1 70  ? 2.488   2.200   68.502 1.00 51.71  ? 70  CYS   A C   1 
ATOM   528  O O   . CYS   A 1 70  ? 1.738   2.781   67.710 1.00 56.35  ? 70  CYS   A O   1 
ATOM   529  C CB  . CYS   A 1 70  ? 2.978   -0.241  68.220 1.00 52.28  ? 70  CYS   A CB  1 
ATOM   530  S SG  . CYS   A 1 70  ? 1.321   -0.523  67.577 1.00 78.39  ? 70  CYS   A SG  1 
ATOM   531  N N   . ASN   A 1 71  ? 2.449   2.428   69.814 1.00 53.59  ? 71  ASN   A N   1 
ATOM   532  C CA  . ASN   A 1 71  ? 1.558   3.428   70.398 1.00 46.85  ? 71  ASN   A CA  1 
ATOM   533  C C   . ASN   A 1 71  ? 2.128   3.782   71.765 1.00 57.94  ? 71  ASN   A C   1 
ATOM   534  O O   . ASN   A 1 71  ? 2.083   2.957   72.682 1.00 59.25  ? 71  ASN   A O   1 
ATOM   535  C CB  . ASN   A 1 71  ? 0.132   2.897   70.503 1.00 49.74  ? 71  ASN   A CB  1 
ATOM   536  C CG  . ASN   A 1 71  ? -0.868  3.969   70.903 1.00 61.09  ? 71  ASN   A CG  1 
ATOM   537  O OD1 . ASN   A 1 71  ? -0.554  4.879   71.669 1.00 68.12  ? 71  ASN   A OD1 1 
ATOM   538  N ND2 . ASN   A 1 71  ? -2.087  3.860   70.385 1.00 48.12  ? 71  ASN   A ND2 1 
ATOM   539  N N   . ASP   A 1 72  ? 2.654   4.998   71.900 1.00 59.32  ? 72  ASP   A N   1 
ATOM   540  C CA  . ASP   A 1 72  ? 3.332   5.424   73.117 1.00 63.70  ? 72  ASP   A CA  1 
ATOM   541  C C   . ASP   A 1 72  ? 2.403   6.121   74.107 1.00 69.74  ? 72  ASP   A C   1 
ATOM   542  O O   . ASP   A 1 72  ? 2.883   6.865   74.970 1.00 75.07  ? 72  ASP   A O   1 
ATOM   543  C CB  . ASP   A 1 72  ? 4.508   6.339   72.771 1.00 71.09  ? 72  ASP   A CB  1 
ATOM   544  C CG  . ASP   A 1 72  ? 4.085   7.556   71.969 1.00 88.66  ? 72  ASP   A CG  1 
ATOM   545  O OD1 . ASP   A 1 72  ? 2.991   7.524   71.363 1.00 82.77  ? 72  ASP   A OD1 1 
ATOM   546  O OD2 . ASP   A 1 72  ? 4.845   8.548   71.943 1.00 90.51  ? 72  ASP   A OD2 1 
ATOM   547  N N   . SER   A 1 73  ? 1.093   5.902   74.004 1.00 67.94  ? 73  SER   A N   1 
ATOM   548  C CA  . SER   A 1 73  ? 0.162   6.504   74.950 1.00 67.88  ? 73  SER   A CA  1 
ATOM   549  C C   . SER   A 1 73  ? 0.456   6.027   76.366 1.00 66.15  ? 73  SER   A C   1 
ATOM   550  O O   . SER   A 1 73  ? 0.589   4.826   76.616 1.00 63.73  ? 73  SER   A O   1 
ATOM   551  C CB  . SER   A 1 73  ? -1.277  6.166   74.567 1.00 71.16  ? 73  SER   A CB  1 
ATOM   552  O OG  . SER   A 1 73  ? -1.601  6.694   73.292 1.00 107.27 ? 73  SER   A OG  1 
ATOM   553  N N   . LYS   A 1 74  ? 0.555   6.984   77.293 1.00 82.34  ? 74  LYS   A N   1 
ATOM   554  C CA  . LYS   A 1 74  ? 0.935   6.661   78.665 1.00 60.17  ? 74  LYS   A CA  1 
ATOM   555  C C   . LYS   A 1 74  ? -0.087  5.758   79.342 1.00 58.63  ? 74  LYS   A C   1 
ATOM   556  O O   . LYS   A 1 74  ? 0.285   4.905   80.156 1.00 60.52  ? 74  LYS   A O   1 
ATOM   557  C CB  . LYS   A 1 74  ? 1.131   7.950   79.463 1.00 65.73  ? 74  LYS   A CB  1 
ATOM   558  C CG  . LYS   A 1 74  ? 2.325   8.761   78.987 1.00 95.97  ? 74  LYS   A CG  1 
ATOM   559  C CD  . LYS   A 1 74  ? 2.514   10.050  79.765 1.00 101.54 ? 74  LYS   A CD  1 
ATOM   560  C CE  . LYS   A 1 74  ? 3.636   10.881  79.156 1.00 88.50  ? 74  LYS   A CE  1 
ATOM   561  N NZ  . LYS   A 1 74  ? 3.913   12.116  79.938 1.00 102.52 ? 74  LYS   A NZ  1 
ATOM   562  N N   . ALA   A 1 75  ? -1.374  5.925   79.023 1.00 62.13  ? 75  ALA   A N   1 
ATOM   563  C CA  . ALA   A 1 75  ? -2.396  5.047   79.585 1.00 60.71  ? 75  ALA   A CA  1 
ATOM   564  C C   . ALA   A 1 75  ? -2.192  3.602   79.146 1.00 66.47  ? 75  ALA   A C   1 
ATOM   565  O O   . ALA   A 1 75  ? -2.321  2.674   79.954 1.00 70.26  ? 75  ALA   A O   1 
ATOM   566  C CB  . ALA   A 1 75  ? -3.786  5.538   79.183 1.00 56.56  ? 75  ALA   A CB  1 
ATOM   567  N N   . ILE   A 1 76  ? -1.875  3.393   77.866 1.00 73.18  ? 76  ILE   A N   1 
ATOM   568  C CA  . ILE   A 1 76  ? -1.650  2.042   77.358 1.00 54.24  ? 76  ILE   A CA  1 
ATOM   569  C C   . ILE   A 1 76  ? -0.476  1.395   78.079 1.00 68.78  ? 76  ILE   A C   1 
ATOM   570  O O   . ILE   A 1 76  ? -0.555  0.246   78.533 1.00 59.34  ? 76  ILE   A O   1 
ATOM   571  C CB  . ILE   A 1 76  ? -1.416  2.073   75.837 1.00 69.25  ? 76  ILE   A CB  1 
ATOM   572  C CG1 . ILE   A 1 76  ? -2.480  2.925   75.144 1.00 77.46  ? 76  ILE   A CG1 1 
ATOM   573  C CG2 . ILE   A 1 76  ? -1.395  0.659   75.278 1.00 54.78  ? 76  ILE   A CG2 1 
ATOM   574  C CD1 . ILE   A 1 76  ? -3.864  2.351   75.182 1.00 74.89  ? 76  ILE   A CD1 1 
ATOM   575  N N   . VAL   A 1 77  ? 0.640   2.121   78.174 1.00 56.56  ? 77  VAL   A N   1 
ATOM   576  C CA  . VAL   A 1 77  ? 1.836   1.569   78.797 1.00 55.83  ? 77  VAL   A CA  1 
ATOM   577  C C   . VAL   A 1 77  ? 1.589   1.298   80.274 1.00 63.06  ? 77  VAL   A C   1 
ATOM   578  O O   . VAL   A 1 77  ? 2.059   0.294   80.818 1.00 67.67  ? 77  VAL   A O   1 
ATOM   579  C CB  . VAL   A 1 77  ? 3.032   2.512   78.581 1.00 55.11  ? 77  VAL   A CB  1 
ATOM   580  C CG1 . VAL   A 1 77  ? 4.288   1.936   79.217 1.00 60.64  ? 77  VAL   A CG1 1 
ATOM   581  C CG2 . VAL   A 1 77  ? 3.251   2.757   77.097 1.00 56.04  ? 77  VAL   A CG2 1 
ATOM   582  N N   . LYS   A 1 78  ? 0.836   2.174   80.944 1.00 69.01  ? 78  LYS   A N   1 
ATOM   583  C CA  . LYS   A 1 78  ? 0.524   1.950   82.351 1.00 73.01  ? 78  LYS   A CA  1 
ATOM   584  C C   . LYS   A 1 78  ? -0.330  0.699   82.530 1.00 61.18  ? 78  LYS   A C   1 
ATOM   585  O O   . LYS   A 1 78  ? -0.071  -0.117  83.425 1.00 62.58  ? 78  LYS   A O   1 
ATOM   586  C CB  . LYS   A 1 78  ? -0.177  3.177   82.935 1.00 69.40  ? 78  LYS   A CB  1 
ATOM   587  C CG  . LYS   A 1 78  ? -0.443  3.083   84.430 1.00 83.79  ? 78  LYS   A CG  1 
ATOM   588  C CD  . LYS   A 1 78  ? -1.234  4.281   84.926 1.00 85.23  ? 78  LYS   A CD  1 
ATOM   589  C CE  . LYS   A 1 78  ? -1.463  4.213   86.428 1.00 83.62  ? 78  LYS   A CE  1 
ATOM   590  N NZ  . LYS   A 1 78  ? -2.159  5.428   86.940 1.00 85.67  ? 78  LYS   A NZ  1 
ATOM   591  N N   . THR   A 1 79  ? -1.354  0.534   81.689 1.00 65.63  ? 79  THR   A N   1 
ATOM   592  C CA  . THR   A 1 79  ? -2.197  -0.655  81.762 1.00 63.58  ? 79  THR   A CA  1 
ATOM   593  C C   . THR   A 1 79  ? -1.379  -1.920  81.540 1.00 65.14  ? 79  THR   A C   1 
ATOM   594  O O   . THR   A 1 79  ? -1.512  -2.901  82.282 1.00 74.56  ? 79  THR   A O   1 
ATOM   595  C CB  . THR   A 1 79  ? -3.323  -0.564  80.731 1.00 49.48  ? 79  THR   A CB  1 
ATOM   596  O OG1 . THR   A 1 79  ? -4.069  0.644   80.930 1.00 55.35  ? 79  THR   A OG1 1 
ATOM   597  C CG2 . THR   A 1 79  ? -4.256  -1.757  80.853 1.00 51.85  ? 79  THR   A CG2 1 
ATOM   598  N N   . LEU   A 1 80  ? -0.516  -1.912  80.522 1.00 73.14  ? 80  LEU   A N   1 
ATOM   599  C CA  . LEU   A 1 80  ? 0.282   -3.098  80.224 1.00 58.78  ? 80  LEU   A CA  1 
ATOM   600  C C   . LEU   A 1 80  ? 1.290   -3.386  81.330 1.00 67.80  ? 80  LEU   A C   1 
ATOM   601  O O   . LEU   A 1 80  ? 1.555   -4.553  81.642 1.00 66.81  ? 80  LEU   A O   1 
ATOM   602  C CB  . LEU   A 1 80  ? 0.983   -2.930  78.878 1.00 66.81  ? 80  LEU   A CB  1 
ATOM   603  C CG  . LEU   A 1 80  ? 0.061   -3.058  77.666 1.00 70.86  ? 80  LEU   A CG  1 
ATOM   604  C CD1 . LEU   A 1 80  ? 0.810   -2.783  76.376 1.00 58.44  ? 80  LEU   A CD1 1 
ATOM   605  C CD2 . LEU   A 1 80  ? -0.554  -4.445  77.640 1.00 56.30  ? 80  LEU   A CD2 1 
ATOM   606  N N   . ALA   A 1 81  ? 1.862   -2.341  81.933 1.00 70.23  ? 81  ALA   A N   1 
ATOM   607  C CA  . ALA   A 1 81  ? 2.773   -2.542  83.055 1.00 68.11  ? 81  ALA   A CA  1 
ATOM   608  C C   . ALA   A 1 81  ? 2.044   -3.145  84.247 1.00 71.59  ? 81  ALA   A C   1 
ATOM   609  O O   . ALA   A 1 81  ? 2.567   -4.049  84.911 1.00 73.91  ? 81  ALA   A O   1 
ATOM   610  C CB  . ALA   A 1 81  ? 3.432   -1.218  83.438 1.00 66.63  ? 81  ALA   A CB  1 
ATOM   611  N N   . ALA   A 1 82  ? 0.835   -2.654  84.535 1.00 73.45  ? 82  ALA   A N   1 
ATOM   612  C CA  . ALA   A 1 82  ? 0.016   -3.277  85.568 1.00 73.21  ? 82  ALA   A CA  1 
ATOM   613  C C   . ALA   A 1 82  ? -0.270  -4.733  85.234 1.00 65.46  ? 82  ALA   A C   1 
ATOM   614  O O   . ALA   A 1 82  ? -0.337  -5.580  86.133 1.00 68.85  ? 82  ALA   A O   1 
ATOM   615  C CB  . ALA   A 1 82  ? -1.291  -2.504  85.742 1.00 62.67  ? 82  ALA   A CB  1 
ATOM   616  N N   . THR   A 1 83  ? -0.426  -5.042  83.947 1.00 73.56  ? 83  THR   A N   1 
ATOM   617  C CA  . THR   A 1 83  ? -0.633  -6.418  83.515 1.00 68.87  ? 83  THR   A CA  1 
ATOM   618  C C   . THR   A 1 83  ? 0.618   -7.272  83.710 1.00 67.70  ? 83  THR   A C   1 
ATOM   619  O O   . THR   A 1 83  ? 0.509   -8.495  83.853 1.00 72.81  ? 83  THR   A O   1 
ATOM   620  C CB  . THR   A 1 83  ? -1.082  -6.416  82.050 1.00 72.82  ? 83  THR   A CB  1 
ATOM   621  O OG1 . THR   A 1 83  ? -2.392  -5.841  81.953 1.00 69.53  ? 83  THR   A OG1 1 
ATOM   622  C CG2 . THR   A 1 83  ? -1.131  -7.811  81.489 1.00 68.26  ? 83  THR   A CG2 1 
ATOM   623  N N   . GLY   A 1 84  ? 1.794   -6.654  83.768 1.00 75.35  ? 84  GLY   A N   1 
ATOM   624  C CA  . GLY   A 1 84  ? 3.028   -7.386  83.976 1.00 72.02  ? 84  GLY   A CA  1 
ATOM   625  C C   . GLY   A 1 84  ? 3.764   -7.798  82.722 1.00 77.03  ? 84  GLY   A C   1 
ATOM   626  O O   . GLY   A 1 84  ? 4.653   -8.654  82.799 1.00 69.72  ? 84  GLY   A O   1 
ATOM   627  N N   . THR   A 1 85  ? 3.431   -7.220  81.572 1.00 59.86  ? 85  THR   A N   1 
ATOM   628  C CA  . THR   A 1 85  ? 4.174   -7.502  80.354 1.00 60.98  ? 85  THR   A CA  1 
ATOM   629  C C   . THR   A 1 85  ? 5.532   -6.804  80.377 1.00 68.20  ? 85  THR   A C   1 
ATOM   630  O O   . THR   A 1 85  ? 5.789   -5.902  81.180 1.00 58.15  ? 85  THR   A O   1 
ATOM   631  C CB  . THR   A 1 85  ? 3.391   -7.048  79.122 1.00 60.80  ? 85  THR   A CB  1 
ATOM   632  O OG1 . THR   A 1 85  ? 3.417   -5.618  79.040 1.00 57.55  ? 85  THR   A OG1 1 
ATOM   633  C CG2 . THR   A 1 85  ? 1.947   -7.517  79.204 1.00 65.97  ? 85  THR   A CG2 1 
ATOM   634  N N   . GLY   A 1 86  ? 6.412   -7.242  79.476 1.00 57.43  ? 86  GLY   A N   1 
ATOM   635  C CA  . GLY   A 1 86  ? 7.649   -6.540  79.224 1.00 59.65  ? 86  GLY   A CA  1 
ATOM   636  C C   . GLY   A 1 86  ? 7.451   -5.398  78.247 1.00 58.36  ? 86  GLY   A C   1 
ATOM   637  O O   . GLY   A 1 86  ? 6.353   -5.137  77.755 1.00 57.36  ? 86  GLY   A O   1 
ATOM   638  N N   . PHE   A 1 87  ? 8.549   -4.705  77.953 1.00 64.22  ? 87  PHE   A N   1 
ATOM   639  C CA  . PHE   A 1 87  ? 8.491   -3.582  77.026 1.00 55.20  ? 87  PHE   A CA  1 
ATOM   640  C C   . PHE   A 1 87  ? 9.718   -3.561  76.130 1.00 56.88  ? 87  PHE   A C   1 
ATOM   641  O O   . PHE   A 1 87  ? 10.852  -3.641  76.613 1.00 52.07  ? 87  PHE   A O   1 
ATOM   642  C CB  . PHE   A 1 87  ? 8.362   -2.253  77.783 1.00 54.53  ? 87  PHE   A CB  1 
ATOM   643  C CG  . PHE   A 1 87  ? 7.072   -2.118  78.540 1.00 59.29  ? 87  PHE   A CG  1 
ATOM   644  C CD1 . PHE   A 1 87  ? 5.933   -1.641  77.913 1.00 62.42  ? 87  PHE   A CD1 1 
ATOM   645  C CD2 . PHE   A 1 87  ? 6.998   -2.473  79.877 1.00 59.44  ? 87  PHE   A CD2 1 
ATOM   646  C CE1 . PHE   A 1 87  ? 4.741   -1.524  78.604 1.00 55.66  ? 87  PHE   A CE1 1 
ATOM   647  C CE2 . PHE   A 1 87  ? 5.809   -2.355  80.575 1.00 71.88  ? 87  PHE   A CE2 1 
ATOM   648  C CZ  . PHE   A 1 87  ? 4.680   -1.879  79.937 1.00 68.12  ? 87  PHE   A CZ  1 
ATOM   649  N N   . ASP   A 1 88  ? 9.472   -3.442  74.828 1.00 68.31  ? 88  ASP   A N   1 
ATOM   650  C CA  . ASP   A 1 88  ? 10.512  -3.272  73.817 1.00 57.18  ? 88  ASP   A CA  1 
ATOM   651  C C   . ASP   A 1 88  ? 10.647  -1.782  73.525 1.00 61.72  ? 88  ASP   A C   1 
ATOM   652  O O   . ASP   A 1 88  ? 9.716   -1.159  73.007 1.00 66.38  ? 88  ASP   A O   1 
ATOM   653  C CB  . ASP   A 1 88  ? 10.159  -4.062  72.560 1.00 60.58  ? 88  ASP   A CB  1 
ATOM   654  C CG  . ASP   A 1 88  ? 10.893  -3.572  71.321 1.00 84.75  ? 88  ASP   A CG  1 
ATOM   655  O OD1 . ASP   A 1 88  ? 12.012  -3.030  71.446 1.00 87.78  ? 88  ASP   A OD1 1 
ATOM   656  O OD2 . ASP   A 1 88  ? 10.345  -3.733  70.209 1.00 97.67  ? 88  ASP   A OD2 1 
ATOM   657  N N   . CYS   A 1 89  ? 11.804  -1.216  73.855 1.00 57.25  ? 89  CYS   A N   1 
ATOM   658  C CA  . CYS   A 1 89  ? 12.077  0.198   73.656 1.00 63.03  ? 89  CYS   A CA  1 
ATOM   659  C C   . CYS   A 1 89  ? 13.172  0.373   72.613 1.00 64.15  ? 89  CYS   A C   1 
ATOM   660  O O   . CYS   A 1 89  ? 14.151  -0.380  72.592 1.00 64.32  ? 89  CYS   A O   1 
ATOM   661  C CB  . CYS   A 1 89  ? 12.492  0.863   74.969 1.00 60.86  ? 89  CYS   A CB  1 
ATOM   662  S SG  . CYS   A 1 89  ? 11.204  0.830   76.227 1.00 67.38  ? 89  CYS   A SG  1 
ATOM   663  N N   . ALA   A 1 90  ? 12.997  1.365   71.741 1.00 59.11  ? 90  ALA   A N   1 
ATOM   664  C CA  . ALA   A 1 90  ? 13.939  1.618   70.663 1.00 56.77  ? 90  ALA   A CA  1 
ATOM   665  C C   . ALA   A 1 90  ? 14.755  2.889   70.845 1.00 66.39  ? 90  ALA   A C   1 
ATOM   666  O O   . ALA   A 1 90  ? 15.656  3.140   70.037 1.00 70.89  ? 90  ALA   A O   1 
ATOM   667  C CB  . ALA   A 1 90  ? 13.205  1.676   69.316 1.00 76.91  ? 90  ALA   A CB  1 
ATOM   668  N N   . SER   A 1 91  ? 14.477  3.691   71.871 1.00 57.90  ? 91  SER   A N   1 
ATOM   669  C CA  . SER   A 1 91  ? 15.155  4.971   72.021 1.00 60.42  ? 91  SER   A CA  1 
ATOM   670  C C   . SER   A 1 91  ? 15.148  5.379   73.487 1.00 54.99  ? 91  SER   A C   1 
ATOM   671  O O   . SER   A 1 91  ? 14.481  4.767   74.325 1.00 59.77  ? 91  SER   A O   1 
ATOM   672  C CB  . SER   A 1 91  ? 14.504  6.057   71.158 1.00 63.60  ? 91  SER   A CB  1 
ATOM   673  O OG  . SER   A 1 91  ? 13.234  6.416   71.670 1.00 66.93  ? 91  SER   A OG  1 
ATOM   674  N N   . LYS   A 1 92  ? 15.910  6.435   73.777 1.00 62.86  ? 92  LYS   A N   1 
ATOM   675  C CA  . LYS   A 1 92  ? 15.999  6.962   75.135 1.00 54.98  ? 92  LYS   A CA  1 
ATOM   676  C C   . LYS   A 1 92  ? 14.642  7.429   75.646 1.00 56.45  ? 92  LYS   A C   1 
ATOM   677  O O   . LYS   A 1 92  ? 14.302  7.211   76.815 1.00 66.90  ? 92  LYS   A O   1 
ATOM   678  C CB  . LYS   A 1 92  ? 17.016  8.104   75.169 1.00 65.98  ? 92  LYS   A CB  1 
ATOM   679  C CG  . LYS   A 1 92  ? 16.889  9.053   76.347 1.00 72.76  ? 92  LYS   A CG  1 
ATOM   680  C CD  . LYS   A 1 92  ? 17.924  10.164  76.251 1.00 75.29  ? 92  LYS   A CD  1 
ATOM   681  C CE  . LYS   A 1 92  ? 17.762  11.181  77.368 1.00 87.11  ? 92  LYS   A CE  1 
ATOM   682  N NZ  . LYS   A 1 92  ? 18.804  12.243  77.296 1.00 97.89  ? 92  LYS   A NZ  1 
ATOM   683  N N   . THR   A 1 93  ? 13.851  8.072   74.784 1.00 60.46  ? 93  THR   A N   1 
ATOM   684  C CA  . THR   A 1 93  ? 12.562  8.605   75.214 1.00 55.26  ? 93  THR   A CA  1 
ATOM   685  C C   . THR   A 1 93  ? 11.615  7.491   75.644 1.00 65.88  ? 93  THR   A C   1 
ATOM   686  O O   . THR   A 1 93  ? 10.890  7.631   76.637 1.00 67.71  ? 93  THR   A O   1 
ATOM   687  C CB  . THR   A 1 93  ? 11.941  9.433   74.089 1.00 60.30  ? 93  THR   A CB  1 
ATOM   688  O OG1 . THR   A 1 93  ? 12.765  10.575  73.827 1.00 72.59  ? 93  THR   A OG1 1 
ATOM   689  C CG2 . THR   A 1 93  ? 10.544  9.901   74.471 1.00 49.32  ? 93  THR   A CG2 1 
ATOM   690  N N   . GLU   A 1 94  ? 11.607  6.375   74.914 1.00 69.52  ? 94  GLU   A N   1 
ATOM   691  C CA  . GLU   A 1 94  ? 10.722  5.272   75.272 1.00 63.03  ? 94  GLU   A CA  1 
ATOM   692  C C   . GLU   A 1 94  ? 11.153  4.620   76.581 1.00 67.09  ? 94  GLU   A C   1 
ATOM   693  O O   . GLU   A 1 94  ? 10.306  4.230   77.394 1.00 68.20  ? 94  GLU   A O   1 
ATOM   694  C CB  . GLU   A 1 94  ? 10.674  4.249   74.137 1.00 71.70  ? 94  GLU   A CB  1 
ATOM   695  C CG  . GLU   A 1 94  ? 10.000  4.781   72.877 1.00 78.44  ? 94  GLU   A CG  1 
ATOM   696  C CD  . GLU   A 1 94  ? 9.896   3.750   71.769 1.00 86.93  ? 94  GLU   A CD  1 
ATOM   697  O OE1 . GLU   A 1 94  ? 10.485  2.658   71.902 1.00 92.92  ? 94  GLU   A OE1 1 
ATOM   698  O OE2 . GLU   A 1 94  ? 9.224   4.041   70.757 1.00 70.73  ? 94  GLU   A OE2 1 
ATOM   699  N N   . ILE   A 1 95  ? 12.464  4.489   76.801 1.00 63.44  ? 95  ILE   A N   1 
ATOM   700  C CA  . ILE   A 1 95  ? 12.954  3.986   78.082 1.00 59.31  ? 95  ILE   A CA  1 
ATOM   701  C C   . ILE   A 1 95  ? 12.538  4.918   79.213 1.00 62.24  ? 95  ILE   A C   1 
ATOM   702  O O   . ILE   A 1 95  ? 12.117  4.466   80.286 1.00 63.69  ? 95  ILE   A O   1 
ATOM   703  C CB  . ILE   A 1 95  ? 14.482  3.797   78.036 1.00 61.94  ? 95  ILE   A CB  1 
ATOM   704  C CG1 . ILE   A 1 95  ? 14.856  2.728   77.009 1.00 70.03  ? 95  ILE   A CG1 1 
ATOM   705  C CG2 . ILE   A 1 95  ? 15.014  3.422   79.410 1.00 59.00  ? 95  ILE   A CG2 1 
ATOM   706  C CD1 . ILE   A 1 95  ? 16.346  2.563   76.816 1.00 63.51  ? 95  ILE   A CD1 1 
ATOM   707  N N   . GLN   A 1 96  ? 12.664  6.231   78.997 1.00 66.03  ? 96  GLN   A N   1 
ATOM   708  C CA  . GLN   A 1 96  ? 12.214  7.202   79.991 1.00 59.42  ? 96  GLN   A CA  1 
ATOM   709  C C   . GLN   A 1 96  ? 10.735  7.020   80.297 1.00 57.19  ? 96  GLN   A C   1 
ATOM   710  O O   . GLN   A 1 96  ? 10.323  7.019   81.461 1.00 61.11  ? 96  GLN   A O   1 
ATOM   711  C CB  . GLN   A 1 96  ? 12.477  8.626   79.496 1.00 63.46  ? 96  GLN   A CB  1 
ATOM   712  C CG  . GLN   A 1 96  ? 13.912  9.087   79.635 1.00 73.22  ? 96  GLN   A CG  1 
ATOM   713  C CD  . GLN   A 1 96  ? 14.141  10.484  79.095 1.00 84.96  ? 96  GLN   A CD  1 
ATOM   714  O OE1 . GLN   A 1 96  ? 13.451  10.930  78.179 1.00 81.65  ? 96  GLN   A OE1 1 
ATOM   715  N NE2 . GLN   A 1 96  ? 15.125  11.180  79.655 1.00 89.53  ? 96  GLN   A NE2 1 
ATOM   716  N N   . LEU   A 1 97  ? 9.920   6.875   79.252 1.00 65.43  ? 97  LEU   A N   1 
ATOM   717  C CA  . LEU   A 1 97  ? 8.483   6.699   79.432 1.00 62.34  ? 97  LEU   A CA  1 
ATOM   718  C C   . LEU   A 1 97  ? 8.179   5.445   80.241 1.00 62.58  ? 97  LEU   A C   1 
ATOM   719  O O   . LEU   A 1 97  ? 7.364   5.472   81.169 1.00 56.99  ? 97  LEU   A O   1 
ATOM   720  C CB  . LEU   A 1 97  ? 7.795   6.639   78.069 1.00 67.52  ? 97  LEU   A CB  1 
ATOM   721  C CG  . LEU   A 1 97  ? 6.325   6.217   78.072 1.00 67.38  ? 97  LEU   A CG  1 
ATOM   722  C CD1 . LEU   A 1 97  ? 5.497   7.210   78.859 1.00 67.28  ? 97  LEU   A CD1 1 
ATOM   723  C CD2 . LEU   A 1 97  ? 5.800   6.079   76.650 1.00 70.96  ? 97  LEU   A CD2 1 
ATOM   724  N N   . VAL   A 1 98  ? 8.824   4.332   79.894 1.00 70.56  ? 98  VAL   A N   1 
ATOM   725  C CA  . VAL   A 1 98  ? 8.530   3.067   80.559 1.00 65.58  ? 98  VAL   A CA  1 
ATOM   726  C C   . VAL   A 1 98  ? 8.975   3.104   82.018 1.00 70.33  ? 98  VAL   A C   1 
ATOM   727  O O   . VAL   A 1 98  ? 8.236   2.679   82.914 1.00 66.15  ? 98  VAL   A O   1 
ATOM   728  C CB  . VAL   A 1 98  ? 9.173   1.903   79.784 1.00 63.24  ? 98  VAL   A CB  1 
ATOM   729  C CG1 . VAL   A 1 98  ? 9.080   0.620   80.578 1.00 68.84  ? 98  VAL   A CG1 1 
ATOM   730  C CG2 . VAL   A 1 98  ? 8.486   1.738   78.439 1.00 58.30  ? 98  VAL   A CG2 1 
ATOM   731  N N   . GLN   A 1 99  ? 10.181  3.616   82.285 1.00 79.14  ? 99  GLN   A N   1 
ATOM   732  C CA  . GLN   A 1 99  ? 10.671  3.664   83.660 1.00 66.16  ? 99  GLN   A CA  1 
ATOM   733  C C   . GLN   A 1 99  ? 9.898   4.669   84.506 1.00 69.48  ? 99  GLN   A C   1 
ATOM   734  O O   . GLN   A 1 99  ? 9.727   4.456   85.712 1.00 67.73  ? 99  GLN   A O   1 
ATOM   735  C CB  . GLN   A 1 99  ? 12.162  3.999   83.682 1.00 53.22  ? 99  GLN   A CB  1 
ATOM   736  C CG  . GLN   A 1 99  ? 13.050  2.885   83.161 1.00 64.71  ? 99  GLN   A CG  1 
ATOM   737  C CD  . GLN   A 1 99  ? 14.511  3.093   83.505 1.00 82.27  ? 99  GLN   A CD  1 
ATOM   738  O OE1 . GLN   A 1 99  ? 15.072  4.162   83.265 1.00 78.85  ? 99  GLN   A OE1 1 
ATOM   739  N NE2 . GLN   A 1 99  ? 15.136  2.067   84.072 1.00 75.17  ? 99  GLN   A NE2 1 
ATOM   740  N N   . SER   A 1 100 ? 9.433   5.765   83.900 1.00 59.50  ? 100 SER   A N   1 
ATOM   741  C CA  . SER   A 1 100 ? 8.661   6.756   84.642 1.00 64.25  ? 100 SER   A CA  1 
ATOM   742  C C   . SER   A 1 100 ? 7.391   6.158   85.233 1.00 67.73  ? 100 SER   A C   1 
ATOM   743  O O   . SER   A 1 100 ? 6.926   6.609   86.286 1.00 81.16  ? 100 SER   A O   1 
ATOM   744  C CB  . SER   A 1 100 ? 8.326   7.941   83.735 1.00 55.56  ? 100 SER   A CB  1 
ATOM   745  O OG  . SER   A 1 100 ? 7.237   7.644   82.879 1.00 59.97  ? 100 SER   A OG  1 
ATOM   746  N N   . LEU   A 1 101 ? 6.814   5.154   84.575 1.00 70.17  ? 101 LEU   A N   1 
ATOM   747  C CA  . LEU   A 1 101 ? 5.623   4.484   85.081 1.00 62.37  ? 101 LEU   A CA  1 
ATOM   748  C C   . LEU   A 1 101 ? 5.937   3.417   86.123 1.00 67.79  ? 101 LEU   A C   1 
ATOM   749  O O   . LEU   A 1 101 ? 5.014   2.730   86.579 1.00 62.27  ? 101 LEU   A O   1 
ATOM   750  C CB  . LEU   A 1 101 ? 4.837   3.870   83.921 1.00 57.47  ? 101 LEU   A CB  1 
ATOM   751  C CG  . LEU   A 1 101 ? 4.188   4.892   82.985 1.00 69.17  ? 101 LEU   A CG  1 
ATOM   752  C CD1 . LEU   A 1 101 ? 3.415   4.202   81.878 1.00 75.98  ? 101 LEU   A CD1 1 
ATOM   753  C CD2 . LEU   A 1 101 ? 3.283   5.836   83.762 1.00 69.64  ? 101 LEU   A CD2 1 
ATOM   754  N N   . GLY   A 1 102 ? 7.201   3.255   86.503 1.00 63.20  ? 102 GLY   A N   1 
ATOM   755  C CA  . GLY   A 1 102 ? 7.577   2.342   87.561 1.00 57.67  ? 102 GLY   A CA  1 
ATOM   756  C C   . GLY   A 1 102 ? 8.062   0.980   87.122 1.00 61.30  ? 102 GLY   A C   1 
ATOM   757  O O   . GLY   A 1 102 ? 8.157   0.080   87.963 1.00 72.35  ? 102 GLY   A O   1 
ATOM   758  N N   . VAL   A 1 103 ? 8.374   0.798   85.848 1.00 67.71  ? 103 VAL   A N   1 
ATOM   759  C CA  . VAL   A 1 103 ? 8.798   -0.514  85.354 1.00 62.87  ? 103 VAL   A CA  1 
ATOM   760  C C   . VAL   A 1 103 ? 10.288  -0.690  85.635 1.00 65.68  ? 103 VAL   A C   1 
ATOM   761  O O   . VAL   A 1 103 ? 11.085  0.196   85.286 1.00 69.74  ? 103 VAL   A O   1 
ATOM   762  C CB  . VAL   A 1 103 ? 8.500   -0.648  83.865 1.00 63.31  ? 103 VAL   A CB  1 
ATOM   763  C CG1 . VAL   A 1 103 ? 9.017   -1.978  83.337 1.00 62.37  ? 103 VAL   A CG1 1 
ATOM   764  C CG2 . VAL   A 1 103 ? 7.008   -0.505  83.608 1.00 56.38  ? 103 VAL   A CG2 1 
ATOM   765  N N   . PRO   A 1 104 ? 10.698  -1.793  86.254 1.00 63.77  ? 104 PRO   A N   1 
ATOM   766  C CA  . PRO   A 1 104 ? 12.124  -2.021  86.512 1.00 71.33  ? 104 PRO   A CA  1 
ATOM   767  C C   . PRO   A 1 104 ? 12.868  -2.322  85.223 1.00 71.17  ? 104 PRO   A C   1 
ATOM   768  O O   . PRO   A 1 104 ? 12.255  -2.722  84.222 1.00 67.90  ? 104 PRO   A O   1 
ATOM   769  C CB  . PRO   A 1 104 ? 12.118  -3.234  87.454 1.00 63.18  ? 104 PRO   A CB  1 
ATOM   770  C CG  . PRO   A 1 104 ? 10.850  -3.950  87.128 1.00 64.30  ? 104 PRO   A CG  1 
ATOM   771  C CD  . PRO   A 1 104 ? 9.855   -2.872  86.798 1.00 60.36  ? 104 PRO   A CD  1 
ATOM   772  N N   . PRO   A 1 105 ? 14.191  -2.135  85.205 1.00 73.66  ? 105 PRO   A N   1 
ATOM   773  C CA  . PRO   A 1 105 ? 14.932  -2.300  83.943 1.00 73.34  ? 105 PRO   A CA  1 
ATOM   774  C C   . PRO   A 1 105 ? 14.923  -3.720  83.403 1.00 74.57  ? 105 PRO   A C   1 
ATOM   775  O O   . PRO   A 1 105 ? 15.055  -3.902  82.186 1.00 74.08  ? 105 PRO   A O   1 
ATOM   776  C CB  . PRO   A 1 105 ? 16.354  -1.847  84.307 1.00 71.59  ? 105 PRO   A CB  1 
ATOM   777  C CG  . PRO   A 1 105 ? 16.195  -1.017  85.539 1.00 76.04  ? 105 PRO   A CG  1 
ATOM   778  C CD  . PRO   A 1 105 ? 15.048  -1.619  86.285 1.00 81.42  ? 105 PRO   A CD  1 
ATOM   779  N N   . GLU   A 1 106 ? 14.780  -4.734  84.259 1.00 76.64  ? 106 GLU   A N   1 
ATOM   780  C CA  . GLU   A 1 106 ? 14.800  -6.112  83.779 1.00 69.13  ? 106 GLU   A CA  1 
ATOM   781  C C   . GLU   A 1 106 ? 13.553  -6.483  82.986 1.00 76.89  ? 106 GLU   A C   1 
ATOM   782  O O   . GLU   A 1 106 ? 13.505  -7.582  82.423 1.00 66.67  ? 106 GLU   A O   1 
ATOM   783  C CB  . GLU   A 1 106 ? 14.976  -7.080  84.951 1.00 73.54  ? 106 GLU   A CB  1 
ATOM   784  C CG  . GLU   A 1 106 ? 13.846  -7.053  85.964 1.00 88.67  ? 106 GLU   A CG  1 
ATOM   785  C CD  . GLU   A 1 106 ? 14.089  -6.060  87.084 1.00 102.19 ? 106 GLU   A CD  1 
ATOM   786  O OE1 . GLU   A 1 106 ? 13.461  -6.207  88.153 1.00 109.22 ? 106 GLU   A OE1 1 
ATOM   787  O OE2 . GLU   A 1 106 ? 14.912  -5.137  86.902 1.00 86.39  ? 106 GLU   A OE2 1 
ATOM   788  N N   . ARG   A 1 107 ? 12.547  -5.610  82.939 1.00 73.73  ? 107 ARG   A N   1 
ATOM   789  C CA  . ARG   A 1 107 ? 11.385  -5.788  82.078 1.00 66.19  ? 107 ARG   A CA  1 
ATOM   790  C C   . ARG   A 1 107 ? 11.457  -4.918  80.828 1.00 68.52  ? 107 ARG   A C   1 
ATOM   791  O O   . ARG   A 1 107 ? 10.431  -4.691  80.177 1.00 61.11  ? 107 ARG   A O   1 
ATOM   792  C CB  . ARG   A 1 107 ? 10.102  -5.491  82.854 1.00 67.56  ? 107 ARG   A CB  1 
ATOM   793  C CG  . ARG   A 1 107 ? 9.730   -6.549  83.876 1.00 64.71  ? 107 ARG   A CG  1 
ATOM   794  C CD  . ARG   A 1 107 ? 8.603   -6.070  84.777 1.00 63.67  ? 107 ARG   A CD  1 
ATOM   795  N NE  . ARG   A 1 107 ? 7.382   -5.789  84.028 1.00 73.85  ? 107 ARG   A NE  1 
ATOM   796  C CZ  . ARG   A 1 107 ? 6.326   -5.157  84.531 1.00 82.22  ? 107 ARG   A CZ  1 
ATOM   797  N NH1 . ARG   A 1 107 ? 6.341   -4.735  85.788 1.00 74.41  ? 107 ARG   A NH1 1 
ATOM   798  N NH2 . ARG   A 1 107 ? 5.256   -4.945  83.777 1.00 70.84  ? 107 ARG   A NH2 1 
ATOM   799  N N   . ILE   A 1 108 ? 12.647  -4.428  80.483 1.00 65.40  ? 108 ILE   A N   1 
ATOM   800  C CA  . ILE   A 1 108 ? 12.859  -3.563  79.329 1.00 64.60  ? 108 ILE   A CA  1 
ATOM   801  C C   . ILE   A 1 108 ? 13.929  -4.192  78.451 1.00 68.81  ? 108 ILE   A C   1 
ATOM   802  O O   . ILE   A 1 108 ? 14.991  -4.586  78.947 1.00 74.08  ? 108 ILE   A O   1 
ATOM   803  C CB  . ILE   A 1 108 ? 13.286  -2.145  79.753 1.00 68.64  ? 108 ILE   A CB  1 
ATOM   804  C CG1 . ILE   A 1 108 ? 12.184  -1.466  80.566 1.00 66.97  ? 108 ILE   A CG1 1 
ATOM   805  C CG2 . ILE   A 1 108 ? 13.658  -1.314  78.532 1.00 60.25  ? 108 ILE   A CG2 1 
ATOM   806  C CD1 . ILE   A 1 108 ? 12.601  -0.135  81.148 1.00 67.99  ? 108 ILE   A CD1 1 
ATOM   807  N N   . ILE   A 1 109 ? 13.653  -4.284  77.153 1.00 76.06  ? 109 ILE   A N   1 
ATOM   808  C CA  . ILE   A 1 109 ? 14.643  -4.706  76.170 1.00 63.65  ? 109 ILE   A CA  1 
ATOM   809  C C   . ILE   A 1 109 ? 14.867  -3.576  75.178 1.00 63.74  ? 109 ILE   A C   1 
ATOM   810  O O   . ILE   A 1 109 ? 13.912  -3.070  74.578 1.00 70.81  ? 109 ILE   A O   1 
ATOM   811  C CB  . ILE   A 1 109 ? 14.214  -5.991  75.445 1.00 63.08  ? 109 ILE   A CB  1 
ATOM   812  C CG1 . ILE   A 1 109 ? 14.090  -7.128  76.453 1.00 87.54  ? 109 ILE   A CG1 1 
ATOM   813  C CG2 . ILE   A 1 109 ? 15.211  -6.344  74.358 1.00 70.88  ? 109 ILE   A CG2 1 
ATOM   814  C CD1 . ILE   A 1 109 ? 13.460  -8.341  75.887 1.00 78.71  ? 109 ILE   A CD1 1 
ATOM   815  N N   . TYR   A 1 110 ? 16.134  -3.204  74.987 1.00 58.78  ? 110 TYR   A N   1 
ATOM   816  C CA  . TYR   A 1 110 ? 16.515  -2.153  74.046 1.00 60.04  ? 110 TYR   A CA  1 
ATOM   817  C C   . TYR   A 1 110 ? 16.744  -2.811  72.688 1.00 66.50  ? 110 TYR   A C   1 
ATOM   818  O O   . TYR   A 1 110 ? 17.871  -3.057  72.254 1.00 67.30  ? 110 TYR   A O   1 
ATOM   819  C CB  . TYR   A 1 110 ? 17.748  -1.418  74.553 1.00 61.95  ? 110 TYR   A CB  1 
ATOM   820  C CG  . TYR   A 1 110 ? 18.051  -0.104  73.866 1.00 71.34  ? 110 TYR   A CG  1 
ATOM   821  C CD1 . TYR   A 1 110 ? 17.277  0.350   72.805 1.00 71.51  ? 110 TYR   A CD1 1 
ATOM   822  C CD2 . TYR   A 1 110 ? 19.124  0.676   74.274 1.00 74.02  ? 110 TYR   A CD2 1 
ATOM   823  C CE1 . TYR   A 1 110 ? 17.562  1.547   72.176 1.00 70.49  ? 110 TYR   A CE1 1 
ATOM   824  C CE2 . TYR   A 1 110 ? 19.415  1.875   73.652 1.00 76.07  ? 110 TYR   A CE2 1 
ATOM   825  C CZ  . TYR   A 1 110 ? 18.631  2.305   72.603 1.00 75.83  ? 110 TYR   A CZ  1 
ATOM   826  O OH  . TYR   A 1 110 ? 18.917  3.496   71.978 1.00 85.09  ? 110 TYR   A OH  1 
ATOM   827  N N   . ALA   A 1 111 ? 15.639  -3.103  72.008 1.00 65.66  ? 111 ALA   A N   1 
ATOM   828  C CA  . ALA   A 1 111 ? 15.679  -3.894  70.776 1.00 68.63  ? 111 ALA   A CA  1 
ATOM   829  C C   . ALA   A 1 111 ? 15.812  -3.020  69.532 1.00 74.86  ? 111 ALA   A C   1 
ATOM   830  O O   . ALA   A 1 111 ? 15.037  -3.131  68.584 1.00 81.48  ? 111 ALA   A O   1 
ATOM   831  C CB  . ALA   A 1 111 ? 14.445  -4.783  70.692 1.00 67.84  ? 111 ALA   A CB  1 
ATOM   832  N N   . ASN   A 1 112 ? 16.809  -2.139  69.528 1.00 65.05  ? 112 ASN   A N   1 
ATOM   833  C CA  . ASN   A 1 112 ? 17.154  -1.374  68.341 1.00 60.64  ? 112 ASN   A CA  1 
ATOM   834  C C   . ASN   A 1 112 ? 18.520  -1.844  67.869 1.00 67.62  ? 112 ASN   A C   1 
ATOM   835  O O   . ASN   A 1 112 ? 19.502  -1.710  68.614 1.00 68.90  ? 112 ASN   A O   1 
ATOM   836  C CB  . ASN   A 1 112 ? 17.169  0.127   68.637 1.00 75.47  ? 112 ASN   A CB  1 
ATOM   837  C CG  . ASN   A 1 112 ? 17.448  0.977   67.404 1.00 77.64  ? 112 ASN   A CG  1 
ATOM   838  O OD1 . ASN   A 1 112 ? 17.820  0.470   66.344 1.00 76.99  ? 112 ASN   A OD1 1 
ATOM   839  N ND2 . ASN   A 1 112 ? 17.269  2.283   67.544 1.00 75.59  ? 112 ASN   A ND2 1 
ATOM   840  N N   . PRO   A 1 113 ? 18.634  -2.424  66.673 1.00 72.09  ? 113 PRO   A N   1 
ATOM   841  C CA  . PRO   A 1 113 ? 19.928  -2.985  66.256 1.00 56.02  ? 113 PRO   A CA  1 
ATOM   842  C C   . PRO   A 1 113 ? 20.979  -1.934  65.938 1.00 70.17  ? 113 PRO   A C   1 
ATOM   843  O O   . PRO   A 1 113 ? 22.169  -2.269  65.913 1.00 79.19  ? 113 PRO   A O   1 
ATOM   844  C CB  . PRO   A 1 113 ? 19.571  -3.815  65.015 1.00 57.00  ? 113 PRO   A CB  1 
ATOM   845  C CG  . PRO   A 1 113 ? 18.079  -4.018  65.097 1.00 65.54  ? 113 PRO   A CG  1 
ATOM   846  C CD  . PRO   A 1 113 ? 17.553  -2.776  65.739 1.00 66.51  ? 113 PRO   A CD  1 
ATOM   847  N N   . CYS   A 1 114 ? 20.586  -0.684  65.690 1.00 72.47  ? 114 CYS   A N   1 
ATOM   848  C CA  . CYS   A 1 114 ? 21.512  0.386   65.310 1.00 71.73  ? 114 CYS   A CA  1 
ATOM   849  C C   . CYS   A 1 114 ? 21.233  1.592   66.205 1.00 67.27  ? 114 CYS   A C   1 
ATOM   850  O O   . CYS   A 1 114 ? 20.403  2.443   65.876 1.00 79.07  ? 114 CYS   A O   1 
ATOM   851  C CB  . CYS   A 1 114 ? 21.375  0.730   63.830 1.00 75.53  ? 114 CYS   A CB  1 
ATOM   852  S SG  . CYS   A 1 114 ? 21.868  -0.601  62.711 1.00 77.01  ? 114 CYS   A SG  1 
ATOM   853  N N   . LYS   A 1 115 ? 21.931  1.658   67.337 1.00 61.94  ? 115 LYS   A N   1 
ATOM   854  C CA  . LYS   A 1 115 ? 21.675  2.638   68.382 1.00 58.89  ? 115 LYS   A CA  1 
ATOM   855  C C   . LYS   A 1 115 ? 22.773  3.692   68.412 1.00 52.95  ? 115 LYS   A C   1 
ATOM   856  O O   . LYS   A 1 115 ? 23.954  3.375   68.242 1.00 51.30  ? 115 LYS   A O   1 
ATOM   857  C CB  . LYS   A 1 115 ? 21.580  1.962   69.752 1.00 68.85  ? 115 LYS   A CB  1 
ATOM   858  C CG  . LYS   A 1 115 ? 20.480  0.930   69.858 1.00 68.27  ? 115 LYS   A CG  1 
ATOM   859  C CD  . LYS   A 1 115 ? 20.718  -0.011  71.025 1.00 63.07  ? 115 LYS   A CD  1 
ATOM   860  C CE  . LYS   A 1 115 ? 21.922  -0.906  70.772 1.00 78.41  ? 115 LYS   A CE  1 
ATOM   861  N NZ  . LYS   A 1 115 ? 21.804  -1.656  69.490 1.00 68.84  ? 115 LYS   A NZ  1 
ATOM   862  N N   . GLN   A 1 116 ? 22.374  4.946   68.617 1.00 71.61  ? 116 GLN   A N   1 
ATOM   863  C CA  . GLN   A 1 116 ? 23.340  6.017   68.829 1.00 56.39  ? 116 GLN   A CA  1 
ATOM   864  C C   . GLN   A 1 116 ? 24.117  5.777   70.118 1.00 56.35  ? 116 GLN   A C   1 
ATOM   865  O O   . GLN   A 1 116 ? 23.571  5.282   71.107 1.00 62.38  ? 116 GLN   A O   1 
ATOM   866  C CB  . GLN   A 1 116 ? 22.630  7.370   68.882 1.00 56.43  ? 116 GLN   A CB  1 
ATOM   867  C CG  . GLN   A 1 116 ? 23.564  8.567   68.962 1.00 59.76  ? 116 GLN   A CG  1 
ATOM   868  C CD  . GLN   A 1 116 ? 22.825  9.885   68.854 1.00 54.97  ? 116 GLN   A CD  1 
ATOM   869  O OE1 . GLN   A 1 116 ? 21.905  10.028  68.051 1.00 75.25  ? 116 GLN   A OE1 1 
ATOM   870  N NE2 . GLN   A 1 116 ? 23.227  10.858  69.664 1.00 71.92  ? 116 GLN   A NE2 1 
ATOM   871  N N   . VAL   A 1 117 ? 25.407  6.123   70.093 1.00 63.97  ? 117 VAL   A N   1 
ATOM   872  C CA  . VAL   A 1 117 ? 26.290  5.832   71.222 1.00 57.34  ? 117 VAL   A CA  1 
ATOM   873  C C   . VAL   A 1 117 ? 25.762  6.461   72.506 1.00 58.29  ? 117 VAL   A C   1 
ATOM   874  O O   . VAL   A 1 117 ? 25.753  5.822   73.567 1.00 65.58  ? 117 VAL   A O   1 
ATOM   875  C CB  . VAL   A 1 117 ? 27.722  6.302   70.910 1.00 55.55  ? 117 VAL   A CB  1 
ATOM   876  C CG1 . VAL   A 1 117 ? 28.600  6.185   72.146 1.00 65.56  ? 117 VAL   A CG1 1 
ATOM   877  C CG2 . VAL   A 1 117 ? 28.296  5.502   69.752 1.00 71.14  ? 117 VAL   A CG2 1 
ATOM   878  N N   . SER   A 1 118 ? 25.326  7.723   72.438 1.00 54.61  ? 118 SER   A N   1 
ATOM   879  C CA  . SER   A 1 118 ? 24.824  8.391   73.635 1.00 56.68  ? 118 SER   A CA  1 
ATOM   880  C C   . SER   A 1 118 ? 23.598  7.684   74.199 1.00 59.30  ? 118 SER   A C   1 
ATOM   881  O O   . SER   A 1 118 ? 23.422  7.622   75.422 1.00 64.22  ? 118 SER   A O   1 
ATOM   882  C CB  . SER   A 1 118 ? 24.497  9.851   73.326 1.00 61.08  ? 118 SER   A CB  1 
ATOM   883  O OG  . SER   A 1 118 ? 23.501  9.947   72.326 1.00 72.12  ? 118 SER   A OG  1 
ATOM   884  N N   . GLN   A 1 119 ? 22.761  7.113   73.331 1.00 72.58  ? 119 GLN   A N   1 
ATOM   885  C CA  . GLN   A 1 119 ? 21.591  6.390   73.816 1.00 68.78  ? 119 GLN   A CA  1 
ATOM   886  C C   . GLN   A 1 119 ? 21.980  5.054   74.436 1.00 69.43  ? 119 GLN   A C   1 
ATOM   887  O O   . GLN   A 1 119 ? 21.351  4.615   75.406 1.00 71.91  ? 119 GLN   A O   1 
ATOM   888  C CB  . GLN   A 1 119 ? 20.591  6.194   72.677 1.00 54.95  ? 119 GLN   A CB  1 
ATOM   889  C CG  . GLN   A 1 119 ? 20.264  7.480   71.937 1.00 54.81  ? 119 GLN   A CG  1 
ATOM   890  C CD  . GLN   A 1 119 ? 18.781  7.652   71.688 1.00 62.27  ? 119 GLN   A CD  1 
ATOM   891  O OE1 . GLN   A 1 119 ? 17.980  6.775   72.010 1.00 76.20  ? 119 GLN   A OE1 1 
ATOM   892  N NE2 . GLN   A 1 119 ? 18.405  8.790   71.116 1.00 73.30  ? 119 GLN   A NE2 1 
ATOM   893  N N   . ILE   A 1 120 ? 23.016  4.402   73.903 1.00 62.23  ? 120 ILE   A N   1 
ATOM   894  C CA  . ILE   A 1 120 ? 23.561  3.215   74.555 1.00 70.23  ? 120 ILE   A CA  1 
ATOM   895  C C   . ILE   A 1 120 ? 24.071  3.564   75.948 1.00 69.09  ? 120 ILE   A C   1 
ATOM   896  O O   . ILE   A 1 120 ? 23.842  2.825   76.915 1.00 63.12  ? 120 ILE   A O   1 
ATOM   897  C CB  . ILE   A 1 120 ? 24.669  2.590   73.687 1.00 64.59  ? 120 ILE   A CB  1 
ATOM   898  C CG1 . ILE   A 1 120 ? 24.094  2.111   72.353 1.00 73.51  ? 120 ILE   A CG1 1 
ATOM   899  C CG2 . ILE   A 1 120 ? 25.337  1.438   74.419 1.00 58.69  ? 120 ILE   A CG2 1 
ATOM   900  C CD1 . ILE   A 1 120 ? 25.138  1.616   71.372 1.00 58.16  ? 120 ILE   A CD1 1 
ATOM   901  N N   . LYS   A 1 121 ? 24.777  4.692   76.071 1.00 65.79  ? 121 LYS   A N   1 
ATOM   902  C CA  . LYS   A 1 121 ? 25.258  5.113   77.382 1.00 73.10  ? 121 LYS   A CA  1 
ATOM   903  C C   . LYS   A 1 121 ? 24.099  5.390   78.331 1.00 64.21  ? 121 LYS   A C   1 
ATOM   904  O O   . LYS   A 1 121 ? 24.161  5.035   79.513 1.00 68.94  ? 121 LYS   A O   1 
ATOM   905  C CB  . LYS   A 1 121 ? 26.160  6.341   77.259 1.00 69.53  ? 121 LYS   A CB  1 
ATOM   906  C CG  . LYS   A 1 121 ? 26.876  6.679   78.562 1.00 88.36  ? 121 LYS   A CG  1 
ATOM   907  C CD  . LYS   A 1 121 ? 27.932  7.758   78.388 1.00 103.82 ? 121 LYS   A CD  1 
ATOM   908  C CE  . LYS   A 1 121 ? 27.306  9.127   78.182 1.00 108.69 ? 121 LYS   A CE  1 
ATOM   909  N NZ  . LYS   A 1 121 ? 28.329  10.211  78.215 1.00 89.11  ? 121 LYS   A NZ  1 
ATOM   910  N N   . TYR   A 1 122 ? 23.037  6.036   77.838 1.00 65.98  ? 122 TYR   A N   1 
ATOM   911  C CA  . TYR   A 1 122 ? 21.861  6.249   78.679 1.00 60.47  ? 122 TYR   A CA  1 
ATOM   912  C C   . TYR   A 1 122 ? 21.266  4.925   79.140 1.00 71.52  ? 122 TYR   A C   1 
ATOM   913  O O   . TYR   A 1 122 ? 20.892  4.780   80.310 1.00 75.50  ? 122 TYR   A O   1 
ATOM   914  C CB  . TYR   A 1 122 ? 20.798  7.069   77.946 1.00 63.32  ? 122 TYR   A CB  1 
ATOM   915  C CG  . TYR   A 1 122 ? 19.554  7.274   78.789 1.00 66.85  ? 122 TYR   A CG  1 
ATOM   916  C CD1 . TYR   A 1 122 ? 19.439  8.365   79.638 1.00 71.78  ? 122 TYR   A CD1 1 
ATOM   917  C CD2 . TYR   A 1 122 ? 18.503  6.362   78.750 1.00 77.23  ? 122 TYR   A CD2 1 
ATOM   918  C CE1 . TYR   A 1 122 ? 18.313  8.547   80.419 1.00 77.57  ? 122 TYR   A CE1 1 
ATOM   919  C CE2 . TYR   A 1 122 ? 17.377  6.533   79.529 1.00 71.22  ? 122 TYR   A CE2 1 
ATOM   920  C CZ  . TYR   A 1 122 ? 17.286  7.628   80.359 1.00 72.95  ? 122 TYR   A CZ  1 
ATOM   921  O OH  . TYR   A 1 122 ? 16.166  7.798   81.136 1.00 62.64  ? 122 TYR   A OH  1 
ATOM   922  N N   . ALA   A 1 123 ? 21.142  3.959   78.227 1.00 75.49  ? 123 ALA   A N   1 
ATOM   923  C CA  . ALA   A 1 123 ? 20.609  2.652   78.602 1.00 69.29  ? 123 ALA   A CA  1 
ATOM   924  C C   . ALA   A 1 123 ? 21.472  2.001   79.673 1.00 70.07  ? 123 ALA   A C   1 
ATOM   925  O O   . ALA   A 1 123 ? 20.955  1.370   80.601 1.00 72.93  ? 123 ALA   A O   1 
ATOM   926  C CB  . ALA   A 1 123 ? 20.506  1.749   77.373 1.00 76.81  ? 123 ALA   A CB  1 
ATOM   927  N N   . ALA   A 1 124 ? 22.793  2.132   79.549 1.00 72.71  ? 124 ALA   A N   1 
ATOM   928  C CA  . ALA   A 1 124 ? 23.683  1.598   80.573 1.00 66.50  ? 124 ALA   A CA  1 
ATOM   929  C C   . ALA   A 1 124 ? 23.472  2.304   81.909 1.00 70.76  ? 124 ALA   A C   1 
ATOM   930  O O   . ALA   A 1 124 ? 23.450  1.659   82.964 1.00 61.72  ? 124 ALA   A O   1 
ATOM   931  C CB  . ALA   A 1 124 ? 25.136  1.720   80.118 1.00 59.92  ? 124 ALA   A CB  1 
ATOM   932  N N   . ASN   A 1 125 ? 23.307  3.630   81.882 1.00 66.14  ? 125 ASN   A N   1 
ATOM   933  C CA  . ASN   A 1 125 ? 23.164  4.399   83.115 1.00 56.00  ? 125 ASN   A CA  1 
ATOM   934  C C   . ASN   A 1 125 ? 21.903  4.027   83.888 1.00 58.51  ? 125 ASN   A C   1 
ATOM   935  O O   . ASN   A 1 125 ? 21.861  4.183   85.114 1.00 76.61  ? 125 ASN   A O   1 
ATOM   936  C CB  . ASN   A 1 125 ? 23.170  5.896   82.798 1.00 54.20  ? 125 ASN   A CB  1 
ATOM   937  C CG  . ASN   A 1 125 ? 24.540  6.397   82.376 1.00 69.61  ? 125 ASN   A CG  1 
ATOM   938  O OD1 . ASN   A 1 125 ? 25.549  5.718   82.569 1.00 73.56  ? 125 ASN   A OD1 1 
ATOM   939  N ND2 . ASN   A 1 125 ? 24.581  7.587   81.788 1.00 62.58  ? 125 ASN   A ND2 1 
ATOM   940  N N   . ASN   A 1 126 ? 20.867  3.539   83.202 1.00 64.56  ? 126 ASN   A N   1 
ATOM   941  C CA  . ASN   A 1 126 ? 19.587  3.238   83.835 1.00 66.96  ? 126 ASN   A CA  1 
ATOM   942  C C   . ASN   A 1 126 ? 19.353  1.740   84.000 1.00 61.88  ? 126 ASN   A C   1 
ATOM   943  O O   . ASN   A 1 126 ? 18.222  1.316   84.258 1.00 60.42  ? 126 ASN   A O   1 
ATOM   944  C CB  . ASN   A 1 126 ? 18.444  3.872   83.041 1.00 55.42  ? 126 ASN   A CB  1 
ATOM   945  C CG  . ASN   A 1 126 ? 18.412  5.382   83.173 1.00 66.28  ? 126 ASN   A CG  1 
ATOM   946  O OD1 . ASN   A 1 126 ? 17.684  5.930   84.001 1.00 63.57  ? 126 ASN   A OD1 1 
ATOM   947  N ND2 . ASN   A 1 126 ? 19.218  6.063   82.367 1.00 63.71  ? 126 ASN   A ND2 1 
ATOM   948  N N   . GLY   A 1 127 ? 20.400  0.931   83.866 1.00 73.26  ? 127 GLY   A N   1 
ATOM   949  C CA  . GLY   A 1 127 ? 20.320  -0.476  84.198 1.00 73.65  ? 127 GLY   A CA  1 
ATOM   950  C C   . GLY   A 1 127 ? 19.657  -1.360  83.168 1.00 64.84  ? 127 GLY   A C   1 
ATOM   951  O O   . GLY   A 1 127 ? 19.358  -2.519  83.477 1.00 72.88  ? 127 GLY   A O   1 
ATOM   952  N N   . VAL   A 1 128 ? 19.420  -0.863  81.958 1.00 65.46  ? 128 VAL   A N   1 
ATOM   953  C CA  . VAL   A 1 128 ? 18.861  -1.685  80.890 1.00 61.44  ? 128 VAL   A CA  1 
ATOM   954  C C   . VAL   A 1 128 ? 20.007  -2.483  80.280 1.00 59.38  ? 128 VAL   A C   1 
ATOM   955  O O   . VAL   A 1 128 ? 20.850  -1.934  79.567 1.00 71.84  ? 128 VAL   A O   1 
ATOM   956  C CB  . VAL   A 1 128 ? 18.144  -0.835  79.837 1.00 63.04  ? 128 VAL   A CB  1 
ATOM   957  C CG1 . VAL   A 1 128 ? 17.653  -1.710  78.695 1.00 61.35  ? 128 VAL   A CG1 1 
ATOM   958  C CG2 . VAL   A 1 128 ? 16.987  -0.074  80.472 1.00 62.27  ? 128 VAL   A CG2 1 
ATOM   959  N N   . GLN   A 1 129 ? 20.042  -3.783  80.561 1.00 64.18  ? 129 GLN   A N   1 
ATOM   960  C CA  . GLN   A 1 129 ? 21.195  -4.605  80.221 1.00 73.30  ? 129 GLN   A CA  1 
ATOM   961  C C   . GLN   A 1 129 ? 21.090  -5.256  78.851 1.00 67.37  ? 129 GLN   A C   1 
ATOM   962  O O   . GLN   A 1 129 ? 22.115  -5.457  78.190 1.00 68.73  ? 129 GLN   A O   1 
ATOM   963  C CB  . GLN   A 1 129 ? 21.387  -5.696  81.278 1.00 74.95  ? 129 GLN   A CB  1 
ATOM   964  C CG  . GLN   A 1 129 ? 21.564  -5.168  82.690 1.00 79.91  ? 129 GLN   A CG  1 
ATOM   965  C CD  . GLN   A 1 129 ? 22.726  -4.204  82.805 1.00 94.36  ? 129 GLN   A CD  1 
ATOM   966  O OE1 . GLN   A 1 129 ? 22.536  -2.990  82.881 1.00 89.43  ? 129 GLN   A OE1 1 
ATOM   967  N NE2 . GLN   A 1 129 ? 23.940  -4.740  82.808 1.00 93.96  ? 129 GLN   A NE2 1 
ATOM   968  N N   . MET   A 1 130 ? 19.883  -5.581  78.405 1.00 74.95  ? 130 MET   A N   1 
ATOM   969  C CA  . MET   A 1 130 ? 19.676  -6.404  77.220 1.00 70.09  ? 130 MET   A CA  1 
ATOM   970  C C   . MET   A 1 130 ? 19.450  -5.528  75.993 1.00 66.81  ? 130 MET   A C   1 
ATOM   971  O O   . MET   A 1 130 ? 18.540  -4.692  75.980 1.00 68.87  ? 130 MET   A O   1 
ATOM   972  C CB  . MET   A 1 130 ? 18.492  -7.339  77.449 1.00 68.43  ? 130 MET   A CB  1 
ATOM   973  C CG  . MET   A 1 130 ? 18.388  -8.481  76.477 1.00 78.73  ? 130 MET   A CG  1 
ATOM   974  S SD  . MET   A 1 130 ? 17.241  -9.696  77.134 1.00 100.48 ? 130 MET   A SD  1 
ATOM   975  C CE  . MET   A 1 130 ? 18.220  -10.376 78.472 1.00 85.89  ? 130 MET   A CE  1 
ATOM   976  N N   . MET   A 1 131 ? 20.271  -5.733  74.962 1.00 57.48  ? 131 MET   A N   1 
ATOM   977  C CA  . MET   A 1 131 ? 20.165  -4.984  73.714 1.00 63.95  ? 131 MET   A CA  1 
ATOM   978  C C   . MET   A 1 131 ? 20.372  -5.916  72.529 1.00 51.03  ? 131 MET   A C   1 
ATOM   979  O O   . MET   A 1 131 ? 21.079  -6.917  72.631 1.00 54.56  ? 131 MET   A O   1 
ATOM   980  C CB  . MET   A 1 131 ? 21.187  -3.841  73.637 1.00 65.66  ? 131 MET   A CB  1 
ATOM   981  C CG  . MET   A 1 131 ? 21.228  -2.932  74.850 1.00 76.06  ? 131 MET   A CG  1 
ATOM   982  S SD  . MET   A 1 131 ? 22.389  -1.577  74.613 1.00 86.94  ? 131 MET   A SD  1 
ATOM   983  C CE  . MET   A 1 131 ? 23.906  -2.491  74.362 1.00 79.98  ? 131 MET   A CE  1 
ATOM   984  N N   . THR   A 1 132 ? 19.757  -5.575  71.400 1.00 57.79  ? 132 THR   A N   1 
ATOM   985  C CA  . THR   A 1 132 ? 19.935  -6.347  70.178 1.00 61.07  ? 132 THR   A CA  1 
ATOM   986  C C   . THR   A 1 132 ? 21.042  -5.749  69.312 1.00 54.93  ? 132 THR   A C   1 
ATOM   987  O O   . THR   A 1 132 ? 21.423  -4.585  69.458 1.00 51.38  ? 132 THR   A O   1 
ATOM   988  C CB  . THR   A 1 132 ? 18.634  -6.420  69.374 1.00 43.20  ? 132 THR   A CB  1 
ATOM   989  O OG1 . THR   A 1 132 ? 18.216  -5.099  69.010 1.00 60.94  ? 132 THR   A OG1 1 
ATOM   990  C CG2 . THR   A 1 132 ? 17.540  -7.089  70.188 1.00 50.07  ? 132 THR   A CG2 1 
ATOM   991  N N   . PHE   A 1 133 ? 21.546  -6.565  68.390 1.00 52.02  ? 133 PHE   A N   1 
ATOM   992  C CA  . PHE   A 1 133 ? 22.592  -6.106  67.484 1.00 62.35  ? 133 PHE   A CA  1 
ATOM   993  C C   . PHE   A 1 133 ? 22.647  -7.016  66.265 1.00 52.28  ? 133 PHE   A C   1 
ATOM   994  O O   . PHE   A 1 133 ? 22.233  -8.178  66.323 1.00 58.77  ? 133 PHE   A O   1 
ATOM   995  C CB  . PHE   A 1 133 ? 23.960  -6.076  68.175 1.00 53.66  ? 133 PHE   A CB  1 
ATOM   996  C CG  . PHE   A 1 133 ? 24.624  -7.420  68.251 1.00 58.24  ? 133 PHE   A CG  1 
ATOM   997  C CD1 . PHE   A 1 133 ? 24.151  -8.393  69.115 1.00 50.55  ? 133 PHE   A CD1 1 
ATOM   998  C CD2 . PHE   A 1 133 ? 25.711  -7.715  67.445 1.00 46.02  ? 133 PHE   A CD2 1 
ATOM   999  C CE1 . PHE   A 1 133 ? 24.756  -9.634  69.180 1.00 52.40  ? 133 PHE   A CE1 1 
ATOM   1000 C CE2 . PHE   A 1 133 ? 26.319  -8.955  67.504 1.00 43.88  ? 133 PHE   A CE2 1 
ATOM   1001 C CZ  . PHE   A 1 133 ? 25.841  -9.915  68.373 1.00 57.91  ? 133 PHE   A CZ  1 
ATOM   1002 N N   . ASP   A 1 134 ? 23.143  -6.463  65.148 1.00 48.78  ? 134 ASP   A N   1 
ATOM   1003 C CA  . ASP   A 1 134 ? 23.363  -7.272  63.954 1.00 65.20  ? 134 ASP   A CA  1 
ATOM   1004 C C   . ASP   A 1 134 ? 24.611  -6.875  63.163 1.00 61.58  ? 134 ASP   A C   1 
ATOM   1005 O O   . ASP   A 1 134 ? 24.710  -7.222  61.980 1.00 69.37  ? 134 ASP   A O   1 
ATOM   1006 C CB  . ASP   A 1 134 ? 22.135  -7.225  63.031 1.00 64.51  ? 134 ASP   A CB  1 
ATOM   1007 C CG  . ASP   A 1 134 ? 21.828  -5.825  62.526 1.00 69.83  ? 134 ASP   A CG  1 
ATOM   1008 O OD1 . ASP   A 1 134 ? 22.535  -4.872  62.917 1.00 73.93  ? 134 ASP   A OD1 1 
ATOM   1009 O OD2 . ASP   A 1 134 ? 20.872  -5.676  61.737 1.00 63.60  ? 134 ASP   A OD2 1 
ATOM   1010 N N   . SER   A 1 135 ? 25.566  -6.165  63.766 1.00 60.04  ? 135 SER   A N   1 
ATOM   1011 C CA  . SER   A 1 135 ? 26.735  -5.716  63.019 1.00 54.89  ? 135 SER   A CA  1 
ATOM   1012 C C   . SER   A 1 135 ? 27.933  -5.563  63.949 1.00 69.05  ? 135 SER   A C   1 
ATOM   1013 O O   . SER   A 1 135 ? 27.790  -5.444  65.169 1.00 73.04  ? 135 SER   A O   1 
ATOM   1014 C CB  . SER   A 1 135 ? 26.458  -4.397  62.285 1.00 55.62  ? 135 SER   A CB  1 
ATOM   1015 O OG  . SER   A 1 135 ? 26.336  -3.319  63.193 1.00 70.03  ? 135 SER   A OG  1 
ATOM   1016 N N   . GLU   A 1 136 ? 29.127  -5.571  63.343 1.00 69.17  ? 136 GLU   A N   1 
ATOM   1017 C CA  . GLU   A 1 136 ? 30.373  -5.474  64.103 1.00 62.99  ? 136 GLU   A CA  1 
ATOM   1018 C C   . GLU   A 1 136 ? 30.573  -4.080  64.690 1.00 69.38  ? 136 GLU   A C   1 
ATOM   1019 O O   . GLU   A 1 136 ? 31.083  -3.939  65.810 1.00 73.06  ? 136 GLU   A O   1 
ATOM   1020 C CB  . GLU   A 1 136 ? 31.558  -5.848  63.214 1.00 60.05  ? 136 GLU   A CB  1 
ATOM   1021 C CG  . GLU   A 1 136 ? 31.585  -7.307  62.792 1.00 92.69  ? 136 GLU   A CG  1 
ATOM   1022 C CD  . GLU   A 1 136 ? 32.820  -7.662  61.988 1.00 108.42 ? 136 GLU   A CD  1 
ATOM   1023 O OE1 . GLU   A 1 136 ? 33.599  -6.745  61.655 1.00 96.23  ? 136 GLU   A OE1 1 
ATOM   1024 O OE2 . GLU   A 1 136 ? 33.008  -8.859  61.686 1.00 102.65 ? 136 GLU   A OE2 1 
ATOM   1025 N N   . VAL   A 1 137 ? 30.226  -3.039  63.930 1.00 71.17  ? 137 VAL   A N   1 
ATOM   1026 C CA  . VAL   A 1 137 ? 30.341  -1.674  64.439 1.00 65.17  ? 137 VAL   A CA  1 
ATOM   1027 C C   . VAL   A 1 137 ? 29.505  -1.512  65.702 1.00 67.43  ? 137 VAL   A C   1 
ATOM   1028 O O   . VAL   A 1 137 ? 29.902  -0.818  66.650 1.00 74.67  ? 137 VAL   A O   1 
ATOM   1029 C CB  . VAL   A 1 137 ? 29.930  -0.667  63.349 1.00 67.18  ? 137 VAL   A CB  1 
ATOM   1030 C CG1 . VAL   A 1 137 ? 29.819  0.734   63.931 1.00 67.53  ? 137 VAL   A CG1 1 
ATOM   1031 C CG2 . VAL   A 1 137 ? 30.919  -0.704  62.189 1.00 42.08  ? 137 VAL   A CG2 1 
ATOM   1032 N N   . GLU   A 1 138 ? 28.339  -2.160  65.740 1.00 64.69  ? 138 GLU   A N   1 
ATOM   1033 C CA  . GLU   A 1 138 ? 27.531  -2.150  66.952 1.00 63.98  ? 138 GLU   A CA  1 
ATOM   1034 C C   . GLU   A 1 138 ? 28.268  -2.821  68.103 1.00 69.99  ? 138 GLU   A C   1 
ATOM   1035 O O   . GLU   A 1 138 ? 28.183  -2.369  69.249 1.00 72.47  ? 138 GLU   A O   1 
ATOM   1036 C CB  . GLU   A 1 138 ? 26.190  -2.837  66.692 1.00 69.71  ? 138 GLU   A CB  1 
ATOM   1037 C CG  . GLU   A 1 138 ? 25.049  -2.353  67.579 1.00 76.21  ? 138 GLU   A CG  1 
ATOM   1038 C CD  . GLU   A 1 138 ? 24.572  -0.954  67.226 1.00 86.87  ? 138 GLU   A CD  1 
ATOM   1039 O OE1 . GLU   A 1 138 ? 24.997  -0.414  66.182 1.00 79.61  ? 138 GLU   A OE1 1 
ATOM   1040 O OE2 . GLU   A 1 138 ? 23.763  -0.394  67.996 1.00 81.62  ? 138 GLU   A OE2 1 
ATOM   1041 N N   . LEU   A 1 139 ? 29.006  -3.897  67.814 1.00 72.17  ? 139 LEU   A N   1 
ATOM   1042 C CA  . LEU   A 1 139 ? 29.795  -4.556  68.852 1.00 65.18  ? 139 LEU   A CA  1 
ATOM   1043 C C   . LEU   A 1 139 ? 30.877  -3.633  69.397 1.00 64.71  ? 139 LEU   A C   1 
ATOM   1044 O O   . LEU   A 1 139 ? 31.109  -3.587  70.611 1.00 68.75  ? 139 LEU   A O   1 
ATOM   1045 C CB  . LEU   A 1 139 ? 30.416  -5.839  68.302 1.00 66.04  ? 139 LEU   A CB  1 
ATOM   1046 C CG  . LEU   A 1 139 ? 29.486  -7.040  68.146 1.00 53.23  ? 139 LEU   A CG  1 
ATOM   1047 C CD1 . LEU   A 1 139 ? 30.215  -8.195  67.483 1.00 62.25  ? 139 LEU   A CD1 1 
ATOM   1048 C CD2 . LEU   A 1 139 ? 28.946  -7.456  69.496 1.00 57.87  ? 139 LEU   A CD2 1 
ATOM   1049 N N   . MET   A 1 140 ? 31.558  -2.899  68.514 1.00 70.12  ? 140 MET   A N   1 
ATOM   1050 C CA  . MET   A 1 140 ? 32.545  -1.919  68.962 1.00 75.63  ? 140 MET   A CA  1 
ATOM   1051 C C   . MET   A 1 140 ? 31.905  -0.867  69.860 1.00 74.02  ? 140 MET   A C   1 
ATOM   1052 O O   . MET   A 1 140 ? 32.423  -0.554  70.941 1.00 73.50  ? 140 MET   A O   1 
ATOM   1053 C CB  . MET   A 1 140 ? 33.214  -1.258  67.757 1.00 73.50  ? 140 MET   A CB  1 
ATOM   1054 C CG  . MET   A 1 140 ? 34.049  -2.191  66.900 1.00 67.88  ? 140 MET   A CG  1 
ATOM   1055 S SD  . MET   A 1 140 ? 35.790  -2.200  67.384 1.00 125.20 ? 140 MET   A SD  1 
ATOM   1056 C CE  . MET   A 1 140 ? 35.782  -3.315  68.785 1.00 83.22  ? 140 MET   A CE  1 
ATOM   1057 N N   . LYS   A 1 141 ? 30.776  -0.308  69.419 1.00 69.15  ? 141 LYS   A N   1 
ATOM   1058 C CA  . LYS   A 1 141 ? 30.102  0.722   70.203 1.00 69.40  ? 141 LYS   A CA  1 
ATOM   1059 C C   . LYS   A 1 141 ? 29.669  0.192   71.565 1.00 72.24  ? 141 LYS   A C   1 
ATOM   1060 O O   . LYS   A 1 141 ? 29.770  0.899   72.574 1.00 78.58  ? 141 LYS   A O   1 
ATOM   1061 C CB  . LYS   A 1 141 ? 28.902  1.268   69.428 1.00 64.28  ? 141 LYS   A CB  1 
ATOM   1062 C CG  . LYS   A 1 141 ? 29.279  2.129   68.232 1.00 69.34  ? 141 LYS   A CG  1 
ATOM   1063 C CD  . LYS   A 1 141 ? 28.238  2.030   67.135 1.00 59.59  ? 141 LYS   A CD  1 
ATOM   1064 C CE  . LYS   A 1 141 ? 26.864  2.378   67.665 1.00 59.82  ? 141 LYS   A CE  1 
ATOM   1065 N NZ  . LYS   A 1 141 ? 25.811  2.189   66.633 1.00 63.27  ? 141 LYS   A NZ  1 
ATOM   1066 N N   . VAL   A 1 142 ? 29.176  -1.047  71.613 1.00 73.61  ? 142 VAL   A N   1 
ATOM   1067 C CA  . VAL   A 1 142 ? 28.743  -1.628  72.881 1.00 78.72  ? 142 VAL   A CA  1 
ATOM   1068 C C   . VAL   A 1 142 ? 29.937  -1.857  73.799 1.00 85.41  ? 142 VAL   A C   1 
ATOM   1069 O O   . VAL   A 1 142 ? 29.891  -1.537  74.993 1.00 84.06  ? 142 VAL   A O   1 
ATOM   1070 C CB  . VAL   A 1 142 ? 27.961  -2.931  72.633 1.00 78.45  ? 142 VAL   A CB  1 
ATOM   1071 C CG1 . VAL   A 1 142 ? 27.744  -3.679  73.939 1.00 75.85  ? 142 VAL   A CG1 1 
ATOM   1072 C CG2 . VAL   A 1 142 ? 26.629  -2.627  71.971 1.00 74.21  ? 142 VAL   A CG2 1 
ATOM   1073 N N   . ALA   A 1 143 ? 31.023  -2.421  73.258 1.00 73.80  ? 143 ALA   A N   1 
ATOM   1074 C CA  . ALA   A 1 143 ? 32.227  -2.623  74.055 1.00 63.49  ? 143 ALA   A CA  1 
ATOM   1075 C C   . ALA   A 1 143 ? 32.762  -1.307  74.597 1.00 73.45  ? 143 ALA   A C   1 
ATOM   1076 O O   . ALA   A 1 143 ? 33.349  -1.273  75.685 1.00 81.88  ? 143 ALA   A O   1 
ATOM   1077 C CB  . ALA   A 1 143 ? 33.296  -3.330  73.222 1.00 57.30  ? 143 ALA   A CB  1 
ATOM   1078 N N   . ARG   A 1 144 ? 32.561  -0.216  73.865 1.00 76.83  ? 144 ARG   A N   1 
ATOM   1079 C CA  . ARG   A 1 144 ? 33.102  1.076   74.262 1.00 70.95  ? 144 ARG   A CA  1 
ATOM   1080 C C   . ARG   A 1 144 ? 32.131  1.906   75.100 1.00 73.44  ? 144 ARG   A C   1 
ATOM   1081 O O   . ARG   A 1 144 ? 32.562  2.867   75.750 1.00 80.32  ? 144 ARG   A O   1 
ATOM   1082 C CB  . ARG   A 1 144 ? 33.547  1.834   72.996 1.00 71.76  ? 144 ARG   A CB  1 
ATOM   1083 C CG  . ARG   A 1 144 ? 33.631  3.356   73.084 1.00 77.99  ? 144 ARG   A CG  1 
ATOM   1084 C CD  . ARG   A 1 144 ? 33.528  4.000   71.704 1.00 95.09  ? 144 ARG   A CD  1 
ATOM   1085 N NE  . ARG   A 1 144 ? 33.615  5.456   71.770 1.00 106.91 ? 144 ARG   A NE  1 
ATOM   1086 C CZ  . ARG   A 1 144 ? 34.700  6.162   71.468 1.00 109.23 ? 144 ARG   A CZ  1 
ATOM   1087 N NH1 . ARG   A 1 144 ? 35.809  5.553   71.071 1.00 97.40  ? 144 ARG   A NH1 1 
ATOM   1088 N NH2 . ARG   A 1 144 ? 34.673  7.483   71.562 1.00 111.13 ? 144 ARG   A NH2 1 
ATOM   1089 N N   . ALA   A 1 145 ? 30.854  1.517   75.175 1.00 78.07  ? 145 ALA   A N   1 
ATOM   1090 C CA  . ALA   A 1 145 ? 29.865  2.305   75.904 1.00 71.48  ? 145 ALA   A CA  1 
ATOM   1091 C C   . ALA   A 1 145 ? 29.004  1.527   76.892 1.00 70.84  ? 145 ALA   A C   1 
ATOM   1092 O O   . ALA   A 1 145 ? 28.425  2.159   77.785 1.00 77.18  ? 145 ALA   A O   1 
ATOM   1093 C CB  . ALA   A 1 145 ? 28.929  3.025   74.919 1.00 74.00  ? 145 ALA   A CB  1 
ATOM   1094 N N   . HIS   A 1 146 ? 28.881  0.201   76.773 1.00 70.52  ? 146 HIS   A N   1 
ATOM   1095 C CA  . HIS   A 1 146 ? 28.071  -0.539  77.737 1.00 76.02  ? 146 HIS   A CA  1 
ATOM   1096 C C   . HIS   A 1 146 ? 28.634  -1.955  77.818 1.00 88.06  ? 146 HIS   A C   1 
ATOM   1097 O O   . HIS   A 1 146 ? 27.933  -2.914  77.470 1.00 76.88  ? 146 HIS   A O   1 
ATOM   1098 C CB  . HIS   A 1 146 ? 26.597  -0.548  77.314 1.00 69.14  ? 146 HIS   A CB  1 
ATOM   1099 C CG  . HIS   A 1 146 ? 25.664  -1.128  78.334 1.00 72.02  ? 146 HIS   A CG  1 
ATOM   1100 N ND1 . HIS   A 1 146 ? 26.035  -1.368  79.640 1.00 86.33  ? 146 HIS   A ND1 1 
ATOM   1101 C CD2 . HIS   A 1 146 ? 24.365  -1.498  78.240 1.00 74.45  ? 146 HIS   A CD2 1 
ATOM   1102 C CE1 . HIS   A 1 146 ? 25.014  -1.884  80.301 1.00 84.30  ? 146 HIS   A CE1 1 
ATOM   1103 N NE2 . HIS   A 1 146 ? 23.987  -1.967  79.476 1.00 76.59  ? 146 HIS   A NE2 1 
ATOM   1104 N N   . PRO   A 1 147 ? 29.889  -2.121  78.263 1.00 82.87  ? 147 PRO   A N   1 
ATOM   1105 C CA  . PRO   A 1 147 ? 30.584  -3.419  78.108 1.00 68.47  ? 147 PRO   A CA  1 
ATOM   1106 C C   . PRO   A 1 147 ? 29.910  -4.599  78.786 1.00 78.20  ? 147 PRO   A C   1 
ATOM   1107 O O   . PRO   A 1 147 ? 30.106  -5.738  78.343 1.00 69.00  ? 147 PRO   A O   1 
ATOM   1108 C CB  . PRO   A 1 147 ? 31.965  -3.143  78.716 1.00 68.35  ? 147 PRO   A CB  1 
ATOM   1109 C CG  . PRO   A 1 147 ? 31.724  -2.008  79.680 1.00 82.41  ? 147 PRO   A CG  1 
ATOM   1110 C CD  . PRO   A 1 147 ? 30.683  -1.157  79.041 1.00 68.94  ? 147 PRO   A CD  1 
ATOM   1111 N N   . LYS   A 1 148 ? 29.131  -4.379  79.845 1.00 71.10  ? 148 LYS   A N   1 
ATOM   1112 C CA  . LYS   A 1 148 ? 28.507  -5.466  80.589 1.00 61.03  ? 148 LYS   A CA  1 
ATOM   1113 C C   . LYS   A 1 148 ? 27.068  -5.714  80.146 1.00 78.32  ? 148 LYS   A C   1 
ATOM   1114 O O   . LYS   A 1 148 ? 26.239  -6.161  80.946 1.00 84.04  ? 148 LYS   A O   1 
ATOM   1115 C CB  . LYS   A 1 148 ? 28.558  -5.166  82.088 1.00 70.81  ? 148 LYS   A CB  1 
ATOM   1116 C CG  . LYS   A 1 148 ? 29.967  -4.930  82.628 1.00 88.67  ? 148 LYS   A CG  1 
ATOM   1117 C CD  . LYS   A 1 148 ? 29.943  -4.513  84.087 1.00 109.68 ? 148 LYS   A CD  1 
ATOM   1118 C CE  . LYS   A 1 148 ? 31.340  -4.212  84.602 1.00 106.19 ? 148 LYS   A CE  1 
ATOM   1119 N NZ  . LYS   A 1 148 ? 31.310  -3.749  86.016 1.00 93.64  ? 148 LYS   A NZ  1 
ATOM   1120 N N   . ALA   A 1 149 ? 26.767  -5.433  78.878 1.00 75.48  ? 149 ALA   A N   1 
ATOM   1121 C CA  . ALA   A 1 149 ? 25.436  -5.650  78.339 1.00 66.87  ? 149 ALA   A CA  1 
ATOM   1122 C C   . ALA   A 1 149 ? 25.238  -7.099  77.906 1.00 71.97  ? 149 ALA   A C   1 
ATOM   1123 O O   . ALA   A 1 149 ? 26.193  -7.817  77.590 1.00 80.32  ? 149 ALA   A O   1 
ATOM   1124 C CB  . ALA   A 1 149 ? 25.178  -4.722  77.151 1.00 73.12  ? 149 ALA   A CB  1 
ATOM   1125 N N   . LYS   A 1 150 ? 23.975  -7.526  77.898 1.00 69.73  ? 150 LYS   A N   1 
ATOM   1126 C CA  . LYS   A 1 150 ? 23.573  -8.828  77.372 1.00 65.52  ? 150 LYS   A CA  1 
ATOM   1127 C C   . LYS   A 1 150 ? 23.036  -8.613  75.957 1.00 67.91  ? 150 LYS   A C   1 
ATOM   1128 O O   . LYS   A 1 150 ? 21.998  -7.966  75.772 1.00 67.65  ? 150 LYS   A O   1 
ATOM   1129 C CB  . LYS   A 1 150 ? 22.517  -9.476  78.267 1.00 70.80  ? 150 LYS   A CB  1 
ATOM   1130 C CG  . LYS   A 1 150 ? 22.926  -9.624  79.727 1.00 71.80  ? 150 LYS   A CG  1 
ATOM   1131 C CD  . LYS   A 1 150 ? 24.305  -10.245 79.874 1.00 89.39  ? 150 LYS   A CD  1 
ATOM   1132 C CE  . LYS   A 1 150 ? 24.621  -10.542 81.334 1.00 80.44  ? 150 LYS   A CE  1 
ATOM   1133 N NZ  . LYS   A 1 150 ? 25.988  -11.107 81.514 1.00 67.76  ? 150 LYS   A NZ  1 
ATOM   1134 N N   . LEU   A 1 151 ? 23.741  -9.143  74.957 1.00 64.96  ? 151 LEU   A N   1 
ATOM   1135 C CA  . LEU   A 1 151 ? 23.407  -8.879  73.563 1.00 60.10  ? 151 LEU   A CA  1 
ATOM   1136 C C   . LEU   A 1 151 ? 22.606  -10.020 72.951 1.00 59.33  ? 151 LEU   A C   1 
ATOM   1137 O O   . LEU   A 1 151 ? 22.869  -11.197 73.209 1.00 57.96  ? 151 LEU   A O   1 
ATOM   1138 C CB  . LEU   A 1 151 ? 24.665  -8.632  72.732 1.00 51.46  ? 151 LEU   A CB  1 
ATOM   1139 C CG  . LEU   A 1 151 ? 25.394  -7.326  73.046 1.00 63.21  ? 151 LEU   A CG  1 
ATOM   1140 C CD1 . LEU   A 1 151 ? 26.367  -6.989  71.935 1.00 57.98  ? 151 LEU   A CD1 1 
ATOM   1141 C CD2 . LEU   A 1 151 ? 24.398  -6.193  73.256 1.00 69.72  ? 151 LEU   A CD2 1 
ATOM   1142 N N   . VAL   A 1 152 ? 21.630  -9.653  72.130 1.00 55.10  ? 152 VAL   A N   1 
ATOM   1143 C CA  . VAL   A 1 152 ? 20.804  -10.595 71.390 1.00 57.11  ? 152 VAL   A CA  1 
ATOM   1144 C C   . VAL   A 1 152 ? 21.047  -10.347 69.909 1.00 52.35  ? 152 VAL   A C   1 
ATOM   1145 O O   . VAL   A 1 152 ? 20.867  -9.223  69.421 1.00 52.97  ? 152 VAL   A O   1 
ATOM   1146 C CB  . VAL   A 1 152 ? 19.318  -10.447 71.744 1.00 49.71  ? 152 VAL   A CB  1 
ATOM   1147 C CG1 . VAL   A 1 152 ? 18.490  -11.425 70.938 1.00 60.08  ? 152 VAL   A CG1 1 
ATOM   1148 C CG2 . VAL   A 1 152 ? 19.115  -10.654 73.232 1.00 53.18  ? 152 VAL   A CG2 1 
ATOM   1149 N N   . LEU   A 1 153 ? 21.475  -11.384 69.202 1.00 46.79  ? 153 LEU   A N   1 
ATOM   1150 C CA  . LEU   A 1 153 ? 21.787  -11.258 67.786 1.00 51.51  ? 153 LEU   A CA  1 
ATOM   1151 C C   . LEU   A 1 153 ? 20.491  -11.318 66.989 1.00 54.44  ? 153 LEU   A C   1 
ATOM   1152 O O   . LEU   A 1 153 ? 19.754  -12.308 67.065 1.00 59.29  ? 153 LEU   A O   1 
ATOM   1153 C CB  . LEU   A 1 153 ? 22.749  -12.368 67.363 1.00 48.99  ? 153 LEU   A CB  1 
ATOM   1154 C CG  . LEU   A 1 153 ? 23.555  -12.270 66.061 1.00 61.50  ? 153 LEU   A CG  1 
ATOM   1155 C CD1 . LEU   A 1 153 ? 24.602  -13.368 66.030 1.00 68.18  ? 153 LEU   A CD1 1 
ATOM   1156 C CD2 . LEU   A 1 153 ? 22.687  -12.358 64.815 1.00 49.95  ? 153 LEU   A CD2 1 
ATOM   1157 N N   . ARG   A 1 154 ? 20.203  -10.262 66.232 1.00 45.14  ? 154 ARG   A N   1 
ATOM   1158 C CA  . ARG   A 1 154 ? 19.024  -10.244 65.379 1.00 55.05  ? 154 ARG   A CA  1 
ATOM   1159 C C   . ARG   A 1 154 ? 19.384  -10.815 64.014 1.00 49.33  ? 154 ARG   A C   1 
ATOM   1160 O O   . ARG   A 1 154 ? 20.285  -10.303 63.341 1.00 53.09  ? 154 ARG   A O   1 
ATOM   1161 C CB  . ARG   A 1 154 ? 18.451  -8.835  65.235 1.00 49.71  ? 154 ARG   A CB  1 
ATOM   1162 C CG  . ARG   A 1 154 ? 17.227  -8.802  64.328 1.00 51.77  ? 154 ARG   A CG  1 
ATOM   1163 C CD  . ARG   A 1 154 ? 16.420  -7.525  64.471 1.00 51.07  ? 154 ARG   A CD  1 
ATOM   1164 N NE  . ARG   A 1 154 ? 15.407  -7.417  63.425 1.00 48.08  ? 154 ARG   A NE  1 
ATOM   1165 C CZ  . ARG   A 1 154 ? 14.640  -6.349  63.231 1.00 55.01  ? 154 ARG   A CZ  1 
ATOM   1166 N NH1 . ARG   A 1 154 ? 14.765  -5.289  64.018 1.00 68.76  ? 154 ARG   A NH1 1 
ATOM   1167 N NH2 . ARG   A 1 154 ? 13.744  -6.342  62.254 1.00 65.24  ? 154 ARG   A NH2 1 
ATOM   1168 N N   . ILE   A 1 155 ? 18.680  -11.870 63.607 1.00 50.65  ? 155 ILE   A N   1 
ATOM   1169 C CA  . ILE   A 1 155 ? 18.961  -12.548 62.353 1.00 54.75  ? 155 ILE   A CA  1 
ATOM   1170 C C   . ILE   A 1 155 ? 17.945  -12.099 61.313 1.00 58.10  ? 155 ILE   A C   1 
ATOM   1171 O O   . ILE   A 1 155 ? 16.832  -11.665 61.628 1.00 57.24  ? 155 ILE   A O   1 
ATOM   1172 C CB  . ILE   A 1 155 ? 18.957  -14.089 62.504 1.00 57.44  ? 155 ILE   A CB  1 
ATOM   1173 C CG1 . ILE   A 1 155 ? 17.579  -14.585 62.943 1.00 49.12  ? 155 ILE   A CG1 1 
ATOM   1174 C CG2 . ILE   A 1 155 ? 20.045  -14.540 63.468 1.00 52.31  ? 155 ILE   A CG2 1 
ATOM   1175 C CD1 . ILE   A 1 155 ? 17.430  -16.086 62.889 1.00 48.35  ? 155 ILE   A CD1 1 
ATOM   1176 N N   . ALA   A 1 156 ? 18.335  -12.214 60.049 1.00 57.65  ? 156 ALA   A N   1 
ATOM   1177 C CA  . ALA   A 1 156 ? 17.497  -11.774 58.945 1.00 58.08  ? 156 ALA   A CA  1 
ATOM   1178 C C   . ALA   A 1 156 ? 16.383  -12.765 58.630 1.00 54.54  ? 156 ALA   A C   1 
ATOM   1179 O O   . ALA   A 1 156 ? 16.485  -13.966 58.896 1.00 58.78  ? 156 ALA   A O   1 
ATOM   1180 C CB  . ALA   A 1 156 ? 18.345  -11.551 57.692 1.00 56.94  ? 156 ALA   A CB  1 
ATOM   1181 N N   . THR   A 1 157 ? 15.305  -12.231 58.058 1.00 68.98  ? 157 THR   A N   1 
ATOM   1182 C CA  . THR   A 1 157 ? 14.165  -13.000 57.581 1.00 79.57  ? 157 THR   A CA  1 
ATOM   1183 C C   . THR   A 1 157 ? 13.793  -12.409 56.231 1.00 101.80 ? 157 THR   A C   1 
ATOM   1184 O O   . THR   A 1 157 ? 13.904  -11.195 56.041 1.00 115.88 ? 157 THR   A O   1 
ATOM   1185 C CB  . THR   A 1 157 ? 12.959  -12.918 58.534 1.00 78.59  ? 157 THR   A CB  1 
ATOM   1186 O OG1 . THR   A 1 157 ? 12.410  -11.595 58.492 1.00 90.03  ? 157 THR   A OG1 1 
ATOM   1187 C CG2 . THR   A 1 157 ? 13.357  -13.247 59.969 1.00 70.54  ? 157 THR   A CG2 1 
ATOM   1188 N N   . ASP   A 1 158 ? 13.361  -13.246 55.290 1.00 103.10 ? 158 ASP   A N   1 
ATOM   1189 C CA  . ASP   A 1 158 ? 12.980  -12.755 53.971 1.00 124.61 ? 158 ASP   A CA  1 
ATOM   1190 C C   . ASP   A 1 158 ? 11.463  -12.726 53.850 1.00 129.41 ? 158 ASP   A C   1 
ATOM   1191 O O   . ASP   A 1 158 ? 10.803  -13.749 54.062 1.00 129.34 ? 158 ASP   A O   1 
ATOM   1192 C CB  . ASP   A 1 158 ? 13.592  -13.606 52.858 1.00 125.97 ? 158 ASP   A CB  1 
ATOM   1193 C CG  . ASP   A 1 158 ? 13.324  -13.031 51.482 1.00 133.26 ? 158 ASP   A CG  1 
ATOM   1194 O OD1 . ASP   A 1 158 ? 13.605  -11.829 51.286 1.00 132.82 ? 158 ASP   A OD1 1 
ATOM   1195 O OD2 . ASP   A 1 158 ? 12.838  -13.770 50.602 1.00 133.78 ? 158 ASP   A OD2 1 
ATOM   1196 N N   . ASP   A 1 159 ? 10.916  -11.559 53.511 1.00 130.49 ? 159 ASP   A N   1 
ATOM   1197 C CA  . ASP   A 1 159 ? 9.479   -11.390 53.333 1.00 141.82 ? 159 ASP   A CA  1 
ATOM   1198 C C   . ASP   A 1 159 ? 9.195   -11.052 51.876 1.00 142.80 ? 159 ASP   A C   1 
ATOM   1199 O O   . ASP   A 1 159 ? 9.693   -10.046 51.359 1.00 141.42 ? 159 ASP   A O   1 
ATOM   1200 C CB  . ASP   A 1 159 ? 8.933   -10.304 54.265 1.00 150.19 ? 159 ASP   A CB  1 
ATOM   1201 C CG  . ASP   A 1 159 ? 7.420   -10.190 54.207 1.00 149.07 ? 159 ASP   A CG  1 
ATOM   1202 O OD1 . ASP   A 1 159 ? 6.902   -9.052  54.216 1.00 134.81 ? 159 ASP   A OD1 1 
ATOM   1203 O OD2 . ASP   A 1 159 ? 6.749   -11.240 54.135 1.00 153.03 ? 159 ASP   A OD2 1 
ATOM   1204 N N   . SER   A 1 160 ? 8.391   -11.893 51.218 1.00 142.43 ? 160 SER   A N   1 
ATOM   1205 C CA  . SER   A 1 160 ? 8.083   -11.679 49.808 1.00 134.59 ? 160 SER   A CA  1 
ATOM   1206 C C   . SER   A 1 160 ? 7.206   -10.449 49.605 1.00 137.78 ? 160 SER   A C   1 
ATOM   1207 O O   . SER   A 1 160 ? 7.405   -9.691  48.647 1.00 139.48 ? 160 SER   A O   1 
ATOM   1208 C CB  . SER   A 1 160 ? 7.409   -12.922 49.234 1.00 117.58 ? 160 SER   A CB  1 
ATOM   1209 O OG  . SER   A 1 160 ? 6.188   -13.197 49.901 1.00 125.89 ? 160 SER   A OG  1 
ATOM   1210 N N   . LYS   A 1 161 ? 6.224   -10.242 50.486 1.00 126.15 ? 161 LYS   A N   1 
ATOM   1211 C CA  . LYS   A 1 161 ? 5.313   -9.111  50.351 1.00 125.36 ? 161 LYS   A CA  1 
ATOM   1212 C C   . LYS   A 1 161 ? 6.005   -7.769  50.557 1.00 129.48 ? 161 LYS   A C   1 
ATOM   1213 O O   . LYS   A 1 161 ? 5.453   -6.735  50.163 1.00 120.50 ? 161 LYS   A O   1 
ATOM   1214 C CB  . LYS   A 1 161 ? 4.152   -9.264  51.332 1.00 132.81 ? 161 LYS   A CB  1 
ATOM   1215 C CG  . LYS   A 1 161 ? 3.304   -10.496 51.073 1.00 126.26 ? 161 LYS   A CG  1 
ATOM   1216 C CD  . LYS   A 1 161 ? 2.670   -10.456 49.686 1.00 100.79 ? 161 LYS   A CD  1 
ATOM   1217 C CE  . LYS   A 1 161 ? 1.834   -11.700 49.397 1.00 87.69  ? 161 LYS   A CE  1 
ATOM   1218 N NZ  . LYS   A 1 161 ? 2.598   -12.958 49.630 1.00 88.72  ? 161 LYS   A NZ  1 
ATOM   1219 N N   . ALA   A 1 162 ? 7.185   -7.757  51.173 1.00 143.61 ? 162 ALA   A N   1 
ATOM   1220 C CA  . ALA   A 1 162 ? 7.916   -6.511  51.361 1.00 146.92 ? 162 ALA   A CA  1 
ATOM   1221 C C   . ALA   A 1 162 ? 8.428   -5.979  50.025 1.00 141.01 ? 162 ALA   A C   1 
ATOM   1222 O O   . ALA   A 1 162 ? 8.877   -6.742  49.165 1.00 144.83 ? 162 ALA   A O   1 
ATOM   1223 C CB  . ALA   A 1 162 ? 9.076   -6.722  52.330 1.00 147.86 ? 162 ALA   A CB  1 
ATOM   1224 N N   . VAL   A 1 163 ? 8.362   -4.654  49.859 1.00 126.00 ? 163 VAL   A N   1 
ATOM   1225 C CA  . VAL   A 1 163 ? 8.716   -4.031  48.585 1.00 127.17 ? 163 VAL   A CA  1 
ATOM   1226 C C   . VAL   A 1 163 ? 10.193  -4.236  48.265 1.00 140.70 ? 163 VAL   A C   1 
ATOM   1227 O O   . VAL   A 1 163 ? 10.555  -4.543  47.121 1.00 127.14 ? 163 VAL   A O   1 
ATOM   1228 C CB  . VAL   A 1 163 ? 8.340   -2.536  48.602 1.00 105.58 ? 163 VAL   A CB  1 
ATOM   1229 C CG1 . VAL   A 1 163 ? 8.843   -1.837  47.349 1.00 107.50 ? 163 VAL   A CG1 1 
ATOM   1230 C CG2 . VAL   A 1 163 ? 6.836   -2.367  48.745 1.00 95.67  ? 163 VAL   A CG2 1 
ATOM   1231 N N   . CYS   A 1 164 ? 11.067  -4.087  49.261 1.00 142.32 ? 164 CYS   A N   1 
ATOM   1232 C CA  . CYS   A 1 164 ? 12.511  -4.179  49.064 1.00 131.81 ? 164 CYS   A CA  1 
ATOM   1233 C C   . CYS   A 1 164 ? 13.044  -5.420  49.765 1.00 131.46 ? 164 CYS   A C   1 
ATOM   1234 O O   . CYS   A 1 164 ? 12.969  -5.523  50.996 1.00 132.90 ? 164 CYS   A O   1 
ATOM   1235 C CB  . CYS   A 1 164 ? 13.214  -2.924  49.585 1.00 119.59 ? 164 CYS   A CB  1 
ATOM   1236 S SG  . CYS   A 1 164 ? 12.667  -1.390  48.793 1.00 129.73 ? 164 CYS   A SG  1 
ATOM   1237 N N   . ARG   A 1 165 ? 13.583  -6.356  48.979 1.00 123.96 ? 165 ARG   A N   1 
ATOM   1238 C CA  . ARG   A 1 165 ? 14.219  -7.551  49.518 1.00 126.61 ? 165 ARG   A CA  1 
ATOM   1239 C C   . ARG   A 1 165 ? 15.718  -7.593  49.285 1.00 122.30 ? 165 ARG   A C   1 
ATOM   1240 O O   . ARG   A 1 165 ? 16.420  -8.298  50.016 1.00 126.87 ? 165 ARG   A O   1 
ATOM   1241 C CB  . ARG   A 1 165 ? 13.599  -8.817  48.911 1.00 132.93 ? 165 ARG   A CB  1 
ATOM   1242 C CG  . ARG   A 1 165 ? 12.309  -9.265  49.575 1.00 148.73 ? 165 ARG   A CG  1 
ATOM   1243 C CD  . ARG   A 1 165 ? 11.793  -10.555 48.965 1.00 135.92 ? 165 ARG   A CD  1 
ATOM   1244 N NE  . ARG   A 1 165 ? 10.917  -10.309 47.826 1.00 120.25 ? 165 ARG   A NE  1 
ATOM   1245 C CZ  . ARG   A 1 165 ? 10.352  -11.269 47.104 1.00 107.86 ? 165 ARG   A CZ  1 
ATOM   1246 N NH1 . ARG   A 1 165 ? 9.563   -10.959 46.085 1.00 106.39 ? 165 ARG   A NH1 1 
ATOM   1247 N NH2 . ARG   A 1 165 ? 10.578  -12.541 47.400 1.00 110.22 ? 165 ARG   A NH2 1 
ATOM   1248 N N   . LEU   A 1 166 ? 16.220  -6.871  48.280 1.00 108.42 ? 166 LEU   A N   1 
ATOM   1249 C CA  . LEU   A 1 166 ? 17.654  -6.867  48.017 1.00 95.84  ? 166 LEU   A CA  1 
ATOM   1250 C C   . LEU   A 1 166 ? 18.420  -6.210  49.154 1.00 104.90 ? 166 LEU   A C   1 
ATOM   1251 O O   . LEU   A 1 166 ? 19.510  -6.663  49.528 1.00 80.83  ? 166 LEU   A O   1 
ATOM   1252 C CB  . LEU   A 1 166 ? 17.933  -6.128  46.714 1.00 83.88  ? 166 LEU   A CB  1 
ATOM   1253 C CG  . LEU   A 1 166 ? 17.385  -6.713  45.420 1.00 94.25  ? 166 LEU   A CG  1 
ATOM   1254 C CD1 . LEU   A 1 166 ? 18.378  -6.379  44.324 1.00 100.60 ? 166 LEU   A CD1 1 
ATOM   1255 C CD2 . LEU   A 1 166 ? 17.186  -8.233  45.549 1.00 85.63  ? 166 LEU   A CD2 1 
ATOM   1256 N N   . SER   A 1 167 ? 17.873  -5.125  49.692 1.00 111.85 ? 167 SER   A N   1 
ATOM   1257 C CA  . SER   A 1 167 ? 18.473  -4.386  50.791 1.00 92.58  ? 167 SER   A CA  1 
ATOM   1258 C C   . SER   A 1 167 ? 17.548  -4.505  51.989 1.00 96.71  ? 167 SER   A C   1 
ATOM   1259 O O   . SER   A 1 167 ? 16.395  -4.062  51.931 1.00 101.95 ? 167 SER   A O   1 
ATOM   1260 C CB  . SER   A 1 167 ? 18.684  -2.920  50.414 1.00 98.06  ? 167 SER   A CB  1 
ATOM   1261 O OG  . SER   A 1 167 ? 17.443  -2.291  50.133 1.00 78.22  ? 167 SER   A OG  1 
ATOM   1262 N N   . VAL   A 1 168 ? 18.043  -5.107  53.066 1.00 91.62  ? 168 VAL   A N   1 
ATOM   1263 C CA  . VAL   A 1 168 ? 17.278  -5.282  54.295 1.00 79.18  ? 168 VAL   A CA  1 
ATOM   1264 C C   . VAL   A 1 168 ? 17.945  -4.431  55.365 1.00 73.51  ? 168 VAL   A C   1 
ATOM   1265 O O   . VAL   A 1 168 ? 19.170  -4.484  55.531 1.00 78.71  ? 168 VAL   A O   1 
ATOM   1266 C CB  . VAL   A 1 168 ? 17.194  -6.763  54.708 1.00 78.67  ? 168 VAL   A CB  1 
ATOM   1267 C CG1 . VAL   A 1 168 ? 16.379  -6.917  55.974 1.00 70.95  ? 168 VAL   A CG1 1 
ATOM   1268 C CG2 . VAL   A 1 168 ? 16.589  -7.592  53.582 1.00 79.23  ? 168 VAL   A CG2 1 
ATOM   1269 N N   . LYS   A 1 169 ? 17.142  -3.651  56.092 1.00 65.13  ? 169 LYS   A N   1 
ATOM   1270 C CA  . LYS   A 1 169 ? 17.704  -2.712  57.056 1.00 68.00  ? 169 LYS   A CA  1 
ATOM   1271 C C   . LYS   A 1 169 ? 18.309  -3.429  58.255 1.00 66.53  ? 169 LYS   A C   1 
ATOM   1272 O O   . LYS   A 1 169 ? 19.360  -3.019  58.760 1.00 56.08  ? 169 LYS   A O   1 
ATOM   1273 C CB  . LYS   A 1 169 ? 16.625  -1.729  57.511 1.00 72.07  ? 169 LYS   A CB  1 
ATOM   1274 C CG  . LYS   A 1 169 ? 17.127  -0.639  58.441 1.00 54.58  ? 169 LYS   A CG  1 
ATOM   1275 C CD  . LYS   A 1 169 ? 16.063  0.419   58.677 1.00 54.22  ? 169 LYS   A CD  1 
ATOM   1276 C CE  . LYS   A 1 169 ? 16.621  1.584   59.475 1.00 55.16  ? 169 LYS   A CE  1 
ATOM   1277 N NZ  . LYS   A 1 169 ? 15.618  2.668   59.650 1.00 65.69  ? 169 LYS   A NZ  1 
ATOM   1278 N N   . PHE   A 1 170 ? 17.664  -4.489  58.733 1.00 63.11  ? 170 PHE   A N   1 
ATOM   1279 C CA  . PHE   A 1 170 ? 18.128  -5.189  59.920 1.00 61.11  ? 170 PHE   A CA  1 
ATOM   1280 C C   . PHE   A 1 170 ? 18.160  -6.688  59.663 1.00 59.28  ? 170 PHE   A C   1 
ATOM   1281 O O   . PHE   A 1 170 ? 17.462  -7.209  58.792 1.00 58.74  ? 170 PHE   A O   1 
ATOM   1282 C CB  . PHE   A 1 170 ? 17.245  -4.887  61.138 1.00 72.87  ? 170 PHE   A CB  1 
ATOM   1283 C CG  . PHE   A 1 170 ? 17.186  -3.430  61.496 1.00 68.42  ? 170 PHE   A CG  1 
ATOM   1284 C CD1 . PHE   A 1 170 ? 18.322  -2.763  61.924 1.00 73.80  ? 170 PHE   A CD1 1 
ATOM   1285 C CD2 . PHE   A 1 170 ? 15.992  -2.732  61.428 1.00 60.66  ? 170 PHE   A CD2 1 
ATOM   1286 C CE1 . PHE   A 1 170 ? 18.272  -1.426  62.264 1.00 77.16  ? 170 PHE   A CE1 1 
ATOM   1287 C CE2 . PHE   A 1 170 ? 15.936  -1.394  61.767 1.00 62.54  ? 170 PHE   A CE2 1 
ATOM   1288 C CZ  . PHE   A 1 170 ? 17.077  -0.740  62.186 1.00 69.38  ? 170 PHE   A CZ  1 
ATOM   1289 N N   . GLY   A 1 171 ? 18.986  -7.379  60.441 1.00 60.09  ? 171 GLY   A N   1 
ATOM   1290 C CA  . GLY   A 1 171 ? 19.036  -8.824  60.384 1.00 55.11  ? 171 GLY   A CA  1 
ATOM   1291 C C   . GLY   A 1 171 ? 20.302  -9.343  59.741 1.00 58.20  ? 171 GLY   A C   1 
ATOM   1292 O O   . GLY   A 1 171 ? 20.593  -9.036  58.582 1.00 72.89  ? 171 GLY   A O   1 
ATOM   1293 N N   . ALA   A 1 172 ? 21.061  -10.136 60.488 1.00 69.00  ? 172 ALA   A N   1 
ATOM   1294 C CA  . ALA   A 1 172 ? 22.277  -10.748 59.979 1.00 63.18  ? 172 ALA   A CA  1 
ATOM   1295 C C   . ALA   A 1 172 ? 21.967  -12.107 59.370 1.00 59.37  ? 172 ALA   A C   1 
ATOM   1296 O O   . ALA   A 1 172 ? 21.115  -12.847 59.871 1.00 66.42  ? 172 ALA   A O   1 
ATOM   1297 C CB  . ALA   A 1 172 ? 23.312  -10.900 61.096 1.00 65.68  ? 172 ALA   A CB  1 
ATOM   1298 N N   . THR   A 1 173 ? 22.654  -12.429 58.278 1.00 68.38  ? 173 THR   A N   1 
ATOM   1299 C CA  . THR   A 1 173 ? 22.594  -13.780 57.745 1.00 60.99  ? 173 THR   A CA  1 
ATOM   1300 C C   . THR   A 1 173 ? 23.319  -14.741 58.686 1.00 62.78  ? 173 THR   A C   1 
ATOM   1301 O O   . THR   A 1 173 ? 24.068  -14.333 59.579 1.00 70.50  ? 173 THR   A O   1 
ATOM   1302 C CB  . THR   A 1 173 ? 23.209  -13.838 56.349 1.00 57.67  ? 173 THR   A CB  1 
ATOM   1303 O OG1 . THR   A 1 173 ? 24.585  -13.445 56.417 1.00 66.13  ? 173 THR   A OG1 1 
ATOM   1304 C CG2 . THR   A 1 173 ? 22.468  -12.906 55.407 1.00 49.10  ? 173 THR   A CG2 1 
ATOM   1305 N N   . LEU   A 1 174 ? 23.092  -16.039 58.474 1.00 56.48  ? 174 LEU   A N   1 
ATOM   1306 C CA  . LEU   A 1 174 ? 23.756  -17.049 59.294 1.00 63.24  ? 174 LEU   A CA  1 
ATOM   1307 C C   . LEU   A 1 174 ? 25.272  -16.956 59.159 1.00 67.40  ? 174 LEU   A C   1 
ATOM   1308 O O   . LEU   A 1 174 ? 26.005  -17.033 60.157 1.00 81.37  ? 174 LEU   A O   1 
ATOM   1309 C CB  . LEU   A 1 174 ? 23.274  -18.443 58.894 1.00 53.05  ? 174 LEU   A CB  1 
ATOM   1310 C CG  . LEU   A 1 174 ? 21.780  -18.735 59.052 1.00 58.79  ? 174 LEU   A CG  1 
ATOM   1311 C CD1 . LEU   A 1 174 ? 21.461  -20.163 58.637 1.00 52.15  ? 174 LEU   A CD1 1 
ATOM   1312 C CD2 . LEU   A 1 174 ? 21.320  -18.476 60.472 1.00 77.58  ? 174 LEU   A CD2 1 
ATOM   1313 N N   . ARG   A 1 175 ? 25.755  -16.789 57.927 1.00 67.62  ? 175 ARG   A N   1 
ATOM   1314 C CA  . ARG   A 1 175 ? 27.183  -16.627 57.686 1.00 63.98  ? 175 ARG   A CA  1 
ATOM   1315 C C   . ARG   A 1 175 ? 27.732  -15.422 58.444 1.00 70.85  ? 175 ARG   A C   1 
ATOM   1316 O O   . ARG   A 1 175 ? 28.759  -15.517 59.126 1.00 74.89  ? 175 ARG   A O   1 
ATOM   1317 C CB  . ARG   A 1 175 ? 27.431  -16.504 56.182 1.00 66.70  ? 175 ARG   A CB  1 
ATOM   1318 C CG  . ARG   A 1 175 ? 28.875  -16.661 55.753 1.00 87.33  ? 175 ARG   A CG  1 
ATOM   1319 C CD  . ARG   A 1 175 ? 29.004  -16.460 54.250 1.00 110.49 ? 175 ARG   A CD  1 
ATOM   1320 N NE  . ARG   A 1 175 ? 30.318  -16.854 53.747 1.00 123.03 ? 175 ARG   A NE  1 
ATOM   1321 C CZ  . ARG   A 1 175 ? 30.653  -16.863 52.460 1.00 122.29 ? 175 ARG   A CZ  1 
ATOM   1322 N NH1 . ARG   A 1 175 ? 31.871  -17.238 52.094 1.00 119.34 ? 175 ARG   A NH1 1 
ATOM   1323 N NH2 . ARG   A 1 175 ? 29.772  -16.498 51.539 1.00 127.22 ? 175 ARG   A NH2 1 
ATOM   1324 N N   . THR   A 1 176 ? 27.061  -14.273 58.325 1.00 65.52  ? 176 THR   A N   1 
ATOM   1325 C CA  . THR   A 1 176 ? 27.466  -13.097 59.089 1.00 66.59  ? 176 THR   A CA  1 
ATOM   1326 C C   . THR   A 1 176 ? 27.290  -13.317 60.587 1.00 72.58  ? 176 THR   A C   1 
ATOM   1327 O O   . THR   A 1 176 ? 28.087  -12.811 61.386 1.00 68.43  ? 176 THR   A O   1 
ATOM   1328 C CB  . THR   A 1 176 ? 26.664  -11.876 58.631 1.00 61.34  ? 176 THR   A CB  1 
ATOM   1329 O OG1 . THR   A 1 176 ? 26.988  -11.580 57.267 1.00 68.89  ? 176 THR   A OG1 1 
ATOM   1330 C CG2 . THR   A 1 176 ? 26.973  -10.655 59.493 1.00 63.74  ? 176 THR   A CG2 1 
ATOM   1331 N N   . SER   A 1 177 ? 26.265  -14.077 60.985 1.00 67.61  ? 177 SER   A N   1 
ATOM   1332 C CA  . SER   A 1 177 ? 26.024  -14.321 62.403 1.00 66.06  ? 177 SER   A CA  1 
ATOM   1333 C C   . SER   A 1 177 ? 27.184  -15.071 63.045 1.00 68.41  ? 177 SER   A C   1 
ATOM   1334 O O   . SER   A 1 177 ? 27.553  -14.795 64.193 1.00 88.31  ? 177 SER   A O   1 
ATOM   1335 C CB  . SER   A 1 177 ? 24.721  -15.096 62.588 1.00 63.94  ? 177 SER   A CB  1 
ATOM   1336 O OG  . SER   A 1 177 ? 23.603  -14.301 62.242 1.00 72.45  ? 177 SER   A OG  1 
ATOM   1337 N N   . ARG   A 1 178 ? 27.756  -16.040 62.328 1.00 64.14  ? 178 ARG   A N   1 
ATOM   1338 C CA  . ARG   A 1 178 ? 28.894  -16.783 62.865 1.00 70.01  ? 178 ARG   A CA  1 
ATOM   1339 C C   . ARG   A 1 178 ? 30.073  -15.854 63.148 1.00 66.00  ? 178 ARG   A C   1 
ATOM   1340 O O   . ARG   A 1 178 ? 30.687  -15.909 64.226 1.00 77.72  ? 178 ARG   A O   1 
ATOM   1341 C CB  . ARG   A 1 178 ? 29.275  -17.898 61.891 1.00 88.22  ? 178 ARG   A CB  1 
ATOM   1342 C CG  . ARG   A 1 178 ? 30.191  -18.960 62.461 1.00 92.27  ? 178 ARG   A CG  1 
ATOM   1343 C CD  . ARG   A 1 178 ? 30.275  -20.138 61.505 1.00 93.28  ? 178 ARG   A CD  1 
ATOM   1344 N NE  . ARG   A 1 178 ? 30.047  -21.402 62.199 1.00 112.83 ? 178 ARG   A NE  1 
ATOM   1345 C CZ  . ARG   A 1 178 ? 29.414  -22.443 61.667 1.00 103.76 ? 178 ARG   A CZ  1 
ATOM   1346 N NH1 . ARG   A 1 178 ? 29.251  -23.554 62.373 1.00 103.74 ? 178 ARG   A NH1 1 
ATOM   1347 N NH2 . ARG   A 1 178 ? 28.933  -22.369 60.434 1.00 80.50  ? 178 ARG   A NH2 1 
ATOM   1348 N N   . LEU   A 1 179 ? 30.400  -14.985 62.188 1.00 66.75  ? 179 LEU   A N   1 
ATOM   1349 C CA  . LEU   A 1 179 ? 31.492  -14.039 62.385 1.00 69.71  ? 179 LEU   A CA  1 
ATOM   1350 C C   . LEU   A 1 179 ? 31.174  -13.066 63.512 1.00 70.48  ? 179 LEU   A C   1 
ATOM   1351 O O   . LEU   A 1 179 ? 32.065  -12.676 64.274 1.00 77.34  ? 179 LEU   A O   1 
ATOM   1352 C CB  . LEU   A 1 179 ? 31.778  -13.279 61.089 1.00 74.25  ? 179 LEU   A CB  1 
ATOM   1353 C CG  . LEU   A 1 179 ? 32.179  -14.110 59.870 1.00 66.28  ? 179 LEU   A CG  1 
ATOM   1354 C CD1 . LEU   A 1 179 ? 32.359  -13.216 58.654 1.00 59.60  ? 179 LEU   A CD1 1 
ATOM   1355 C CD2 . LEU   A 1 179 ? 33.446  -14.894 60.157 1.00 77.43  ? 179 LEU   A CD2 1 
ATOM   1356 N N   . LEU   A 1 180 ? 29.907  -12.661 63.631 1.00 69.98  ? 180 LEU   A N   1 
ATOM   1357 C CA  . LEU   A 1 180 ? 29.518  -11.767 64.716 1.00 78.73  ? 180 LEU   A CA  1 
ATOM   1358 C C   . LEU   A 1 180 ? 29.716  -12.430 66.073 1.00 78.87  ? 180 LEU   A C   1 
ATOM   1359 O O   . LEU   A 1 180 ? 30.187  -11.793 67.021 1.00 79.02  ? 180 LEU   A O   1 
ATOM   1360 C CB  . LEU   A 1 180 ? 28.063  -11.329 64.545 1.00 72.29  ? 180 LEU   A CB  1 
ATOM   1361 C CG  . LEU   A 1 180 ? 27.755  -10.342 63.420 1.00 66.06  ? 180 LEU   A CG  1 
ATOM   1362 C CD1 . LEU   A 1 180 ? 26.270  -10.030 63.383 1.00 73.75  ? 180 LEU   A CD1 1 
ATOM   1363 C CD2 . LEU   A 1 180 ? 28.563  -9.072  63.598 1.00 68.26  ? 180 LEU   A CD2 1 
ATOM   1364 N N   . LEU   A 1 181 ? 29.367  -13.714 66.182 1.00 75.97  ? 181 LEU   A N   1 
ATOM   1365 C CA  . LEU   A 1 181 ? 29.559  -14.428 67.441 1.00 72.12  ? 181 LEU   A CA  1 
ATOM   1366 C C   . LEU   A 1 181 ? 31.039  -14.554 67.784 1.00 80.20  ? 181 LEU   A C   1 
ATOM   1367 O O   . LEU   A 1 181 ? 31.437  -14.350 68.940 1.00 81.26  ? 181 LEU   A O   1 
ATOM   1368 C CB  . LEU   A 1 181 ? 28.904  -15.807 67.370 1.00 70.39  ? 181 LEU   A CB  1 
ATOM   1369 C CG  . LEU   A 1 181 ? 27.377  -15.819 67.376 1.00 63.77  ? 181 LEU   A CG  1 
ATOM   1370 C CD1 . LEU   A 1 181 ? 26.854  -17.215 67.089 1.00 69.45  ? 181 LEU   A CD1 1 
ATOM   1371 C CD2 . LEU   A 1 181 ? 26.847  -15.308 68.707 1.00 67.33  ? 181 LEU   A CD2 1 
ATOM   1372 N N   . GLU   A 1 182 ? 31.873  -14.887 66.794 1.00 74.15  ? 182 GLU   A N   1 
ATOM   1373 C CA  . GLU   A 1 182 ? 33.305  -14.988 67.069 1.00 72.81  ? 182 GLU   A CA  1 
ATOM   1374 C C   . GLU   A 1 182 ? 33.890  -13.635 67.467 1.00 71.26  ? 182 GLU   A C   1 
ATOM   1375 O O   . GLU   A 1 182 ? 34.716  -13.551 68.386 1.00 68.79  ? 182 GLU   A O   1 
ATOM   1376 C CB  . GLU   A 1 182 ? 34.041  -15.565 65.862 1.00 74.71  ? 182 GLU   A CB  1 
ATOM   1377 C CG  . GLU   A 1 182 ? 33.769  -17.043 65.628 1.00 81.59  ? 182 GLU   A CG  1 
ATOM   1378 C CD  . GLU   A 1 182 ? 34.339  -17.541 64.317 1.00 108.11 ? 182 GLU   A CD  1 
ATOM   1379 O OE1 . GLU   A 1 182 ? 34.569  -18.763 64.196 1.00 116.22 ? 182 GLU   A OE1 1 
ATOM   1380 O OE2 . GLU   A 1 182 ? 34.566  -16.712 63.412 1.00 104.21 ? 182 GLU   A OE2 1 
ATOM   1381 N N   . ARG   A 1 183 ? 33.462  -12.563 66.795 1.00 70.44  ? 183 ARG   A N   1 
ATOM   1382 C CA  . ARG   A 1 183 ? 33.928  -11.224 67.141 1.00 74.81  ? 183 ARG   A CA  1 
ATOM   1383 C C   . ARG   A 1 183 ? 33.494  -10.828 68.548 1.00 70.98  ? 183 ARG   A C   1 
ATOM   1384 O O   . ARG   A 1 183 ? 34.263  -10.207 69.291 1.00 69.07  ? 183 ARG   A O   1 
ATOM   1385 C CB  . ARG   A 1 183 ? 33.412  -10.219 66.110 1.00 78.30  ? 183 ARG   A CB  1 
ATOM   1386 C CG  . ARG   A 1 183 ? 33.911  -8.799  66.298 1.00 77.27  ? 183 ARG   A CG  1 
ATOM   1387 C CD  . ARG   A 1 183 ? 35.426  -8.734  66.312 1.00 83.23  ? 183 ARG   A CD  1 
ATOM   1388 N NE  . ARG   A 1 183 ? 35.902  -7.356  66.254 1.00 81.55  ? 183 ARG   A NE  1 
ATOM   1389 C CZ  . ARG   A 1 183 ? 37.060  -6.946  66.759 1.00 85.50  ? 183 ARG   A CZ  1 
ATOM   1390 N NH1 . ARG   A 1 183 ? 37.414  -5.672  66.661 1.00 89.24  ? 183 ARG   A NH1 1 
ATOM   1391 N NH2 . ARG   A 1 183 ? 37.863  -7.809  67.366 1.00 90.37  ? 183 ARG   A NH2 1 
ATOM   1392 N N   . ALA   A 1 184 ? 32.257  -11.165 68.926 1.00 85.16  ? 184 ALA   A N   1 
ATOM   1393 C CA  . ALA   A 1 184 ? 31.793  -10.886 70.281 1.00 78.13  ? 184 ALA   A CA  1 
ATOM   1394 C C   . ALA   A 1 184 ? 32.607  -11.655 71.312 1.00 78.19  ? 184 ALA   A C   1 
ATOM   1395 O O   . ALA   A 1 184 ? 32.913  -11.131 72.390 1.00 74.66  ? 184 ALA   A O   1 
ATOM   1396 C CB  . ALA   A 1 184 ? 30.308  -11.223 70.410 1.00 71.62  ? 184 ALA   A CB  1 
ATOM   1397 N N   . LYS   A 1 185 ? 32.962  -12.905 71.002 1.00 80.31  ? 185 LYS   A N   1 
ATOM   1398 C CA  . LYS   A 1 185 ? 33.827  -13.662 71.902 1.00 79.52  ? 185 LYS   A CA  1 
ATOM   1399 C C   . LYS   A 1 185 ? 35.190  -12.998 72.041 1.00 73.71  ? 185 LYS   A C   1 
ATOM   1400 O O   . LYS   A 1 185 ? 35.752  -12.943 73.142 1.00 79.96  ? 185 LYS   A O   1 
ATOM   1401 C CB  . LYS   A 1 185 ? 33.983  -15.100 71.407 1.00 77.23  ? 185 LYS   A CB  1 
ATOM   1402 C CG  . LYS   A 1 185 ? 34.411  -16.077 72.492 1.00 71.48  ? 185 LYS   A CG  1 
ATOM   1403 C CD  . LYS   A 1 185 ? 33.382  -16.140 73.608 1.00 76.24  ? 185 LYS   A CD  1 
ATOM   1404 C CE  . LYS   A 1 185 ? 33.847  -17.035 74.745 1.00 85.48  ? 185 LYS   A CE  1 
ATOM   1405 N NZ  . LYS   A 1 185 ? 33.028  -16.836 75.972 1.00 77.85  ? 185 LYS   A NZ  1 
ATOM   1406 N N   . GLU   A 1 186 ? 35.741  -12.497 70.932 1.00 73.43  ? 186 GLU   A N   1 
ATOM   1407 C CA  . GLU   A 1 186 ? 37.017  -11.789 70.991 1.00 73.76  ? 186 GLU   A CA  1 
ATOM   1408 C C   . GLU   A 1 186 ? 36.953  -10.590 71.932 1.00 71.18  ? 186 GLU   A C   1 
ATOM   1409 O O   . GLU   A 1 186 ? 37.880  -10.355 72.715 1.00 84.11  ? 186 GLU   A O   1 
ATOM   1410 C CB  . GLU   A 1 186 ? 37.435  -11.343 69.590 1.00 75.43  ? 186 GLU   A CB  1 
ATOM   1411 C CG  . GLU   A 1 186 ? 37.899  -12.473 68.688 1.00 74.69  ? 186 GLU   A CG  1 
ATOM   1412 C CD  . GLU   A 1 186 ? 38.204  -12.001 67.280 1.00 98.46  ? 186 GLU   A CD  1 
ATOM   1413 O OE1 . GLU   A 1 186 ? 38.661  -10.849 67.125 1.00 100.97 ? 186 GLU   A OE1 1 
ATOM   1414 O OE2 . GLU   A 1 186 ? 37.985  -12.779 66.328 1.00 102.41 ? 186 GLU   A OE2 1 
ATOM   1415 N N   . LEU   A 1 187 ? 35.869  -9.820  71.874 1.00 73.82  ? 187 LEU   A N   1 
ATOM   1416 C CA  . LEU   A 1 187 ? 35.748  -8.584  72.635 1.00 78.86  ? 187 LEU   A CA  1 
ATOM   1417 C C   . LEU   A 1 187 ? 35.216  -8.794  74.047 1.00 81.58  ? 187 LEU   A C   1 
ATOM   1418 O O   . LEU   A 1 187 ? 34.966  -7.808  74.749 1.00 73.75  ? 187 LEU   A O   1 
ATOM   1419 C CB  . LEU   A 1 187 ? 34.851  -7.592  71.891 1.00 77.41  ? 187 LEU   A CB  1 
ATOM   1420 C CG  . LEU   A 1 187 ? 35.293  -7.224  70.475 1.00 72.97  ? 187 LEU   A CG  1 
ATOM   1421 C CD1 . LEU   A 1 187 ? 34.189  -6.471  69.752 1.00 76.03  ? 187 LEU   A CD1 1 
ATOM   1422 C CD2 . LEU   A 1 187 ? 36.571  -6.406  70.513 1.00 72.04  ? 187 LEU   A CD2 1 
ATOM   1423 N N   . ASN   A 1 188 ? 35.023  -10.046 74.470 1.00 82.82  ? 188 ASN   A N   1 
ATOM   1424 C CA  . ASN   A 1 188 ? 34.549  -10.364 75.820 1.00 79.58  ? 188 ASN   A CA  1 
ATOM   1425 C C   . ASN   A 1 188 ? 33.172  -9.753  76.083 1.00 76.73  ? 188 ASN   A C   1 
ATOM   1426 O O   . ASN   A 1 188 ? 32.905  -9.204  77.154 1.00 80.36  ? 188 ASN   A O   1 
ATOM   1427 C CB  . ASN   A 1 188 ? 35.563  -9.918  76.880 1.00 81.71  ? 188 ASN   A CB  1 
ATOM   1428 C CG  . ASN   A 1 188 ? 35.300  -10.537 78.239 1.00 112.00 ? 188 ASN   A CG  1 
ATOM   1429 O OD1 . ASN   A 1 188 ? 34.794  -11.655 78.337 1.00 120.33 ? 188 ASN   A OD1 1 
ATOM   1430 N ND2 . ASN   A 1 188 ? 35.643  -9.811  79.296 1.00 118.95 ? 188 ASN   A ND2 1 
ATOM   1431 N N   . ILE   A 1 189 ? 32.293  -9.839  75.089 1.00 78.59  ? 189 ILE   A N   1 
ATOM   1432 C CA  . ILE   A 1 189 ? 30.919  -9.362  75.195 1.00 68.38  ? 189 ILE   A CA  1 
ATOM   1433 C C   . ILE   A 1 189 ? 29.994  -10.569 75.255 1.00 67.94  ? 189 ILE   A C   1 
ATOM   1434 O O   . ILE   A 1 189 ? 30.155  -11.527 74.490 1.00 74.96  ? 189 ILE   A O   1 
ATOM   1435 C CB  . ILE   A 1 189 ? 30.549  -8.437  74.020 1.00 74.07  ? 189 ILE   A CB  1 
ATOM   1436 C CG1 . ILE   A 1 189 ? 31.388  -7.161  74.063 1.00 74.76  ? 189 ILE   A CG1 1 
ATOM   1437 C CG2 . ILE   A 1 189 ? 29.077  -8.088  74.062 1.00 83.12  ? 189 ILE   A CG2 1 
ATOM   1438 C CD1 . ILE   A 1 189 ? 31.119  -6.229  72.906 1.00 75.83  ? 189 ILE   A CD1 1 
ATOM   1439 N N   . ASP   A 1 190 ? 29.025  -10.522 76.165 1.00 74.87  ? 190 ASP   A N   1 
ATOM   1440 C CA  . ASP   A 1 190 ? 28.137  -11.651 76.418 1.00 73.83  ? 190 ASP   A CA  1 
ATOM   1441 C C   . ASP   A 1 190 ? 26.959  -11.631 75.448 1.00 75.50  ? 190 ASP   A C   1 
ATOM   1442 O O   . ASP   A 1 190 ? 26.167  -10.681 75.444 1.00 77.15  ? 190 ASP   A O   1 
ATOM   1443 C CB  . ASP   A 1 190 ? 27.643  -11.620 77.863 1.00 78.82  ? 190 ASP   A CB  1 
ATOM   1444 C CG  . ASP   A 1 190 ? 27.032  -12.931 78.293 1.00 86.75  ? 190 ASP   A CG  1 
ATOM   1445 O OD1 . ASP   A 1 190 ? 27.245  -13.943 77.592 1.00 95.66  ? 190 ASP   A OD1 1 
ATOM   1446 O OD2 . ASP   A 1 190 ? 26.339  -12.950 79.331 1.00 95.36  ? 190 ASP   A OD2 1 
ATOM   1447 N N   . VAL   A 1 191 ? 26.841  -12.684 74.642 1.00 70.72  ? 191 VAL   A N   1 
ATOM   1448 C CA  . VAL   A 1 191 ? 25.699  -12.892 73.755 1.00 71.32  ? 191 VAL   A CA  1 
ATOM   1449 C C   . VAL   A 1 191 ? 24.807  -13.958 74.377 1.00 63.28  ? 191 VAL   A C   1 
ATOM   1450 O O   . VAL   A 1 191 ? 25.255  -15.082 74.630 1.00 66.21  ? 191 VAL   A O   1 
ATOM   1451 C CB  . VAL   A 1 191 ? 26.148  -13.302 72.343 1.00 58.44  ? 191 VAL   A CB  1 
ATOM   1452 C CG1 . VAL   A 1 191 ? 24.938  -13.597 71.472 1.00 53.56  ? 191 VAL   A CG1 1 
ATOM   1453 C CG2 . VAL   A 1 191 ? 26.989  -12.205 71.723 1.00 66.03  ? 191 VAL   A CG2 1 
ATOM   1454 N N   . VAL   A 1 192 ? 23.547  -13.608 74.634 1.00 73.96  ? 192 VAL   A N   1 
ATOM   1455 C CA  . VAL   A 1 192 ? 22.651  -14.469 75.403 1.00 72.57  ? 192 VAL   A CA  1 
ATOM   1456 C C   . VAL   A 1 192 ? 21.507  -15.051 74.588 1.00 64.11  ? 192 VAL   A C   1 
ATOM   1457 O O   . VAL   A 1 192 ? 20.736  -15.863 75.132 1.00 59.70  ? 192 VAL   A O   1 
ATOM   1458 C CB  . VAL   A 1 192 ? 22.082  -13.730 76.632 1.00 61.79  ? 192 VAL   A CB  1 
ATOM   1459 C CG1 . VAL   A 1 192 ? 23.209  -13.242 77.524 1.00 65.55  ? 192 VAL   A CG1 1 
ATOM   1460 C CG2 . VAL   A 1 192 ? 21.194  -12.569 76.193 1.00 55.89  ? 192 VAL   A CG2 1 
ATOM   1461 N N   . GLY   A 1 193 ? 21.352  -14.674 73.326 1.00 63.41  ? 193 GLY   A N   1 
ATOM   1462 C CA  . GLY   A 1 193 ? 20.246  -15.221 72.565 1.00 67.41  ? 193 GLY   A CA  1 
ATOM   1463 C C   . GLY   A 1 193 ? 20.186  -14.685 71.153 1.00 51.10  ? 193 GLY   A C   1 
ATOM   1464 O O   . GLY   A 1 193 ? 21.084  -13.979 70.693 1.00 46.90  ? 193 GLY   A O   1 
ATOM   1465 N N   . VAL   A 1 194 ? 19.091  -15.044 70.478 1.00 51.95  ? 194 VAL   A N   1 
ATOM   1466 C CA  . VAL   A 1 194 ? 18.835  -14.682 69.087 1.00 52.11  ? 194 VAL   A CA  1 
ATOM   1467 C C   . VAL   A 1 194 ? 17.430  -14.106 68.964 1.00 61.95  ? 194 VAL   A C   1 
ATOM   1468 O O   . VAL   A 1 194 ? 16.490  -14.605 69.595 1.00 69.39  ? 194 VAL   A O   1 
ATOM   1469 C CB  . VAL   A 1 194 ? 19.000  -15.899 68.148 1.00 63.58  ? 194 VAL   A CB  1 
ATOM   1470 C CG1 . VAL   A 1 194 ? 18.863  -15.484 66.695 1.00 68.14  ? 194 VAL   A CG1 1 
ATOM   1471 C CG2 . VAL   A 1 194 ? 20.335  -16.570 68.380 1.00 57.67  ? 194 VAL   A CG2 1 
ATOM   1472 N N   . SER   A 1 195 ? 17.288  -13.051 68.154 1.00 63.67  ? 195 SER   A N   1 
ATOM   1473 C CA  . SER   A 1 195 ? 15.996  -12.421 67.900 1.00 59.57  ? 195 SER   A CA  1 
ATOM   1474 C C   . SER   A 1 195 ? 15.743  -12.269 66.405 1.00 55.37  ? 195 SER   A C   1 
ATOM   1475 O O   . SER   A 1 195 ? 16.678  -12.155 65.611 1.00 60.13  ? 195 SER   A O   1 
ATOM   1476 C CB  . SER   A 1 195 ? 15.909  -11.047 68.552 1.00 65.99  ? 195 SER   A CB  1 
ATOM   1477 O OG  . SER   A 1 195 ? 14.665  -10.437 68.259 1.00 75.27  ? 195 SER   A OG  1 
ATOM   1478 N N   . PHE   A 1 196 ? 14.465  -12.281 66.025 1.00 60.39  ? 196 PHE   A N   1 
ATOM   1479 C CA  . PHE   A 1 196 ? 14.081  -12.073 64.633 1.00 50.54  ? 196 PHE   A CA  1 
ATOM   1480 C C   . PHE   A 1 196 ? 12.734  -11.362 64.575 1.00 42.23  ? 196 PHE   A C   1 
ATOM   1481 O O   . PHE   A 1 196 ? 11.965  -11.369 65.538 1.00 53.37  ? 196 PHE   A O   1 
ATOM   1482 C CB  . PHE   A 1 196 ? 14.046  -13.391 63.846 1.00 51.85  ? 196 PHE   A CB  1 
ATOM   1483 C CG  . PHE   A 1 196 ? 13.034  -14.379 64.345 1.00 52.95  ? 196 PHE   A CG  1 
ATOM   1484 C CD1 . PHE   A 1 196 ? 11.696  -14.264 64.003 1.00 48.76  ? 196 PHE   A CD1 1 
ATOM   1485 C CD2 . PHE   A 1 196 ? 13.428  -15.435 65.146 1.00 46.78  ? 196 PHE   A CD2 1 
ATOM   1486 C CE1 . PHE   A 1 196 ? 10.770  -15.176 64.463 1.00 45.73  ? 196 PHE   A CE1 1 
ATOM   1487 C CE2 . PHE   A 1 196 ? 12.507  -16.353 65.606 1.00 49.34  ? 196 PHE   A CE2 1 
ATOM   1488 C CZ  . PHE   A 1 196 ? 11.176  -16.226 65.262 1.00 50.06  ? 196 PHE   A CZ  1 
ATOM   1489 N N   . HIS   A 1 197 ? 12.453  -10.752 63.421 1.00 50.59  ? 197 HIS   A N   1 
ATOM   1490 C CA  . HIS   A 1 197 ? 11.184  -10.070 63.170 1.00 63.62  ? 197 HIS   A CA  1 
ATOM   1491 C C   . HIS   A 1 197 ? 10.641  -10.523 61.820 1.00 58.94  ? 197 HIS   A C   1 
ATOM   1492 O O   . HIS   A 1 197 ? 11.204  -10.181 60.776 1.00 62.32  ? 197 HIS   A O   1 
ATOM   1493 C CB  . HIS   A 1 197 ? 11.359  -8.550  63.213 1.00 48.62  ? 197 HIS   A CB  1 
ATOM   1494 C CG  . HIS   A 1 197 ? 10.074  -7.789  63.119 1.00 58.08  ? 197 HIS   A CG  1 
ATOM   1495 N ND1 . HIS   A 1 197 ? 8.988   -8.055  63.925 1.00 56.51  ? 197 HIS   A ND1 1 
ATOM   1496 C CD2 . HIS   A 1 197 ? 9.704   -6.764  62.315 1.00 68.78  ? 197 HIS   A CD2 1 
ATOM   1497 C CE1 . HIS   A 1 197 ? 8.003   -7.229  63.620 1.00 59.26  ? 197 HIS   A CE1 1 
ATOM   1498 N NE2 . HIS   A 1 197 ? 8.412   -6.435  62.646 1.00 60.55  ? 197 HIS   A NE2 1 
ATOM   1499 N N   . VAL   A 1 198 ? 9.549   -11.295 61.841 1.00 62.92  ? 198 VAL   A N   1 
ATOM   1500 C CA  . VAL   A 1 198 ? 8.981   -11.819 60.602 1.00 64.42  ? 198 VAL   A CA  1 
ATOM   1501 C C   . VAL   A 1 198 ? 8.306   -10.717 59.787 1.00 68.37  ? 198 VAL   A C   1 
ATOM   1502 O O   . VAL   A 1 198 ? 8.243   -10.798 58.553 1.00 78.54  ? 198 VAL   A O   1 
ATOM   1503 C CB  . VAL   A 1 198 ? 8.011   -12.972 60.931 1.00 58.65  ? 198 VAL   A CB  1 
ATOM   1504 C CG1 . VAL   A 1 198 ? 7.134   -13.323 59.742 1.00 65.94  ? 198 VAL   A CG1 1 
ATOM   1505 C CG2 . VAL   A 1 198 ? 8.783   -14.199 61.388 1.00 58.93  ? 198 VAL   A CG2 1 
ATOM   1506 N N   . GLY   A 1 199 ? 7.844   -9.659  60.433 1.00 58.52  ? 199 GLY   A N   1 
ATOM   1507 C CA  . GLY   A 1 199 ? 7.184   -8.610  59.682 1.00 63.15  ? 199 GLY   A CA  1 
ATOM   1508 C C   . GLY   A 1 199 ? 5.677   -8.636  59.863 1.00 81.68  ? 199 GLY   A C   1 
ATOM   1509 O O   . GLY   A 1 199 ? 5.061   -9.690  60.059 1.00 80.35  ? 199 GLY   A O   1 
ATOM   1510 N N   . SER   A 1 200 ? 5.068   -7.449  59.804 1.00 86.81  ? 200 SER   A N   1 
ATOM   1511 C CA  . SER   A 1 200 ? 3.620   -7.352  59.963 1.00 84.00  ? 200 SER   A CA  1 
ATOM   1512 C C   . SER   A 1 200 ? 2.877   -7.976  58.786 1.00 81.43  ? 200 SER   A C   1 
ATOM   1513 O O   . SER   A 1 200 ? 1.835   -8.615  58.974 1.00 84.02  ? 200 SER   A O   1 
ATOM   1514 C CB  . SER   A 1 200 ? 3.209   -5.890  60.135 1.00 84.37  ? 200 SER   A CB  1 
ATOM   1515 O OG  . SER   A 1 200 ? 3.762   -5.084  59.108 1.00 95.95  ? 200 SER   A OG  1 
ATOM   1516 N N   . GLY   A 1 201 ? 3.384   -7.798  57.568 1.00 81.93  ? 201 GLY   A N   1 
ATOM   1517 C CA  . GLY   A 1 201 ? 2.703   -8.323  56.399 1.00 98.84  ? 201 GLY   A CA  1 
ATOM   1518 C C   . GLY   A 1 201 ? 2.980   -9.784  56.105 1.00 122.50 ? 201 GLY   A C   1 
ATOM   1519 O O   . GLY   A 1 201 ? 3.274   -10.147 54.962 1.00 112.98 ? 201 GLY   A O   1 
ATOM   1520 N N   . CYS   A 1 202 ? 2.903   -10.632 57.130 1.00 126.38 ? 202 CYS   A N   1 
ATOM   1521 C CA  . CYS   A 1 202 ? 3.117   -12.060 56.949 1.00 111.66 ? 202 CYS   A CA  1 
ATOM   1522 C C   . CYS   A 1 202 ? 1.895   -12.706 56.308 1.00 114.22 ? 202 CYS   A C   1 
ATOM   1523 O O   . CYS   A 1 202 ? 0.772   -12.546 56.796 1.00 104.85 ? 202 CYS   A O   1 
ATOM   1524 C CB  . CYS   A 1 202 ? 3.417   -12.720 58.295 1.00 99.07  ? 202 CYS   A CB  1 
ATOM   1525 S SG  . CYS   A 1 202 ? 3.677   -14.507 58.226 1.00 114.71 ? 202 CYS   A SG  1 
ATOM   1526 N N   . THR   A 1 203 ? 2.112   -13.416 55.202 1.00 109.72 ? 203 THR   A N   1 
ATOM   1527 C CA  . THR   A 1 203 ? 1.055   -14.143 54.507 1.00 99.08  ? 203 THR   A CA  1 
ATOM   1528 C C   . THR   A 1 203 ? 1.008   -15.620 54.869 1.00 99.13  ? 203 THR   A C   1 
ATOM   1529 O O   . THR   A 1 203 ? -0.078  -16.197 54.966 1.00 105.27 ? 203 THR   A O   1 
ATOM   1530 C CB  . THR   A 1 203 ? 1.206   -13.990 52.995 1.00 100.81 ? 203 THR   A CB  1 
ATOM   1531 O OG1 . THR   A 1 203 ? 2.486   -14.490 52.583 1.00 107.32 ? 203 THR   A OG1 1 
ATOM   1532 C CG2 . THR   A 1 203 ? 1.066   -12.533 52.620 1.00 94.37  ? 203 THR   A CG2 1 
ATOM   1533 N N   . ASP   A 1 204 ? 2.167   -16.242 55.062 1.00 104.31 ? 204 ASP   A N   1 
ATOM   1534 C CA  . ASP   A 1 204 ? 2.265   -17.668 55.337 1.00 106.88 ? 204 ASP   A CA  1 
ATOM   1535 C C   . ASP   A 1 204 ? 2.915   -17.836 56.702 1.00 102.12 ? 204 ASP   A C   1 
ATOM   1536 O O   . ASP   A 1 204 ? 4.052   -17.372 56.899 1.00 96.65  ? 204 ASP   A O   1 
ATOM   1537 C CB  . ASP   A 1 204 ? 3.082   -18.373 54.247 1.00 93.89  ? 204 ASP   A CB  1 
ATOM   1538 C CG  . ASP   A 1 204 ? 3.169   -19.879 54.446 1.00 104.38 ? 204 ASP   A CG  1 
ATOM   1539 O OD1 . ASP   A 1 204 ? 2.453   -20.424 55.312 1.00 100.78 ? 204 ASP   A OD1 1 
ATOM   1540 O OD2 . ASP   A 1 204 ? 3.953   -20.524 53.719 1.00 108.41 ? 204 ASP   A OD2 1 
ATOM   1541 N N   . PRO   A 1 205 ? 2.254   -18.475 57.669 1.00 97.32  ? 205 PRO   A N   1 
ATOM   1542 C CA  . PRO   A 1 205 ? 2.867   -18.619 59.000 1.00 95.12  ? 205 PRO   A CA  1 
ATOM   1543 C C   . PRO   A 1 205 ? 4.131   -19.456 58.991 1.00 87.35  ? 205 PRO   A C   1 
ATOM   1544 O O   . PRO   A 1 205 ? 4.950   -19.322 59.911 1.00 88.69  ? 205 PRO   A O   1 
ATOM   1545 C CB  . PRO   A 1 205 ? 1.757   -19.275 59.834 1.00 92.31  ? 205 PRO   A CB  1 
ATOM   1546 C CG  . PRO   A 1 205 ? 0.847   -19.916 58.837 1.00 87.32  ? 205 PRO   A CG  1 
ATOM   1547 C CD  . PRO   A 1 205 ? 0.905   -19.065 57.606 1.00 86.25  ? 205 PRO   A CD  1 
ATOM   1548 N N   . GLU   A 1 206 ? 4.318   -20.304 57.971 1.00 86.64  ? 206 GLU   A N   1 
ATOM   1549 C CA  . GLU   A 1 206 ? 5.504   -21.151 57.886 1.00 90.39  ? 206 GLU   A CA  1 
ATOM   1550 C C   . GLU   A 1 206 ? 6.787   -20.341 58.032 1.00 79.46  ? 206 GLU   A C   1 
ATOM   1551 O O   . GLU   A 1 206 ? 7.798   -20.861 58.521 1.00 80.11  ? 206 GLU   A O   1 
ATOM   1552 C CB  . GLU   A 1 206 ? 5.507   -21.912 56.558 1.00 86.86  ? 206 GLU   A CB  1 
ATOM   1553 C CG  . GLU   A 1 206 ? 4.358   -22.905 56.400 1.00 104.90 ? 206 GLU   A CG  1 
ATOM   1554 C CD  . GLU   A 1 206 ? 4.319   -23.950 57.498 1.00 111.48 ? 206 GLU   A CD  1 
ATOM   1555 O OE1 . GLU   A 1 206 ? 5.394   -24.451 57.890 1.00 108.87 ? 206 GLU   A OE1 1 
ATOM   1556 O OE2 . GLU   A 1 206 ? 3.209   -24.270 57.971 1.00 108.56 ? 206 GLU   A OE2 1 
ATOM   1557 N N   . THR   A 1 207 ? 6.760   -19.070 57.617 1.00 78.52  ? 207 THR   A N   1 
ATOM   1558 C CA  . THR   A 1 207 ? 7.921   -18.196 57.754 1.00 66.52  ? 207 THR   A CA  1 
ATOM   1559 C C   . THR   A 1 207 ? 8.459   -18.215 59.178 1.00 71.93  ? 207 THR   A C   1 
ATOM   1560 O O   . THR   A 1 207 ? 9.663   -18.401 59.398 1.00 64.18  ? 207 THR   A O   1 
ATOM   1561 C CB  . THR   A 1 207 ? 7.547   -16.770 57.348 1.00 65.95  ? 207 THR   A CB  1 
ATOM   1562 O OG1 . THR   A 1 207 ? 7.117   -16.756 55.980 1.00 76.44  ? 207 THR   A OG1 1 
ATOM   1563 C CG2 . THR   A 1 207 ? 8.735   -15.840 57.520 1.00 60.54  ? 207 THR   A CG2 1 
ATOM   1564 N N   . PHE   A 1 208 ? 7.569   -18.049 60.162 1.00 76.15  ? 208 PHE   A N   1 
ATOM   1565 C CA  . PHE   A 1 208 ? 7.980   -18.105 61.560 1.00 74.10  ? 208 PHE   A CA  1 
ATOM   1566 C C   . PHE   A 1 208 ? 8.788   -19.364 61.832 1.00 64.31  ? 208 PHE   A C   1 
ATOM   1567 O O   . PHE   A 1 208 ? 9.895   -19.301 62.382 1.00 69.28  ? 208 PHE   A O   1 
ATOM   1568 C CB  . PHE   A 1 208 ? 6.754   -18.051 62.473 1.00 72.45  ? 208 PHE   A CB  1 
ATOM   1569 C CG  . PHE   A 1 208 ? 6.284   -16.661 62.786 1.00 70.93  ? 208 PHE   A CG  1 
ATOM   1570 C CD1 . PHE   A 1 208 ? 5.284   -16.066 62.035 1.00 63.22  ? 208 PHE   A CD1 1 
ATOM   1571 C CD2 . PHE   A 1 208 ? 6.840   -15.949 63.837 1.00 60.80  ? 208 PHE   A CD2 1 
ATOM   1572 C CE1 . PHE   A 1 208 ? 4.849   -14.786 62.322 1.00 69.58  ? 208 PHE   A CE1 1 
ATOM   1573 C CE2 . PHE   A 1 208 ? 6.410   -14.672 64.132 1.00 88.30  ? 208 PHE   A CE2 1 
ATOM   1574 C CZ  . PHE   A 1 208 ? 5.412   -14.088 63.373 1.00 87.22  ? 208 PHE   A CZ  1 
ATOM   1575 N N   . VAL   A 1 209 ? 8.267   -20.515 61.394 1.00 63.86  ? 209 VAL   A N   1 
ATOM   1576 C CA  . VAL   A 1 209 ? 8.968   -21.782 61.586 1.00 73.28  ? 209 VAL   A CA  1 
ATOM   1577 C C   . VAL   A 1 209 ? 10.384  -21.680 61.047 1.00 60.08  ? 209 VAL   A C   1 
ATOM   1578 O O   . VAL   A 1 209 ? 11.360  -21.977 61.749 1.00 72.23  ? 209 VAL   A O   1 
ATOM   1579 C CB  . VAL   A 1 209 ? 8.198   -22.934 60.917 1.00 66.95  ? 209 VAL   A CB  1 
ATOM   1580 C CG1 . VAL   A 1 209 ? 8.931   -24.248 61.132 1.00 73.98  ? 209 VAL   A CG1 1 
ATOM   1581 C CG2 . VAL   A 1 209 ? 6.786   -23.013 61.463 1.00 75.68  ? 209 VAL   A CG2 1 
ATOM   1582 N N   . GLN   A 1 210 ? 10.515  -21.213 59.802 1.00 57.08  ? 210 GLN   A N   1 
ATOM   1583 C CA  . GLN   A 1 210 ? 11.838  -21.062 59.211 1.00 65.22  ? 210 GLN   A CA  1 
ATOM   1584 C C   . GLN   A 1 210 ? 12.721  -20.218 60.115 1.00 63.70  ? 210 GLN   A C   1 
ATOM   1585 O O   . GLN   A 1 210 ? 13.821  -20.637 60.500 1.00 61.39  ? 210 GLN   A O   1 
ATOM   1586 C CB  . GLN   A 1 210 ? 11.718  -20.436 57.821 1.00 63.41  ? 210 GLN   A CB  1 
ATOM   1587 C CG  . GLN   A 1 210 ? 13.034  -20.274 57.087 1.00 65.81  ? 210 GLN   A CG  1 
ATOM   1588 C CD  . GLN   A 1 210 ? 13.710  -21.600 56.814 1.00 80.30  ? 210 GLN   A CD  1 
ATOM   1589 O OE1 . GLN   A 1 210 ? 13.125  -22.491 56.198 1.00 78.02  ? 210 GLN   A OE1 1 
ATOM   1590 N NE2 . GLN   A 1 210 ? 14.954  -21.735 57.260 1.00 82.34  ? 210 GLN   A NE2 1 
ATOM   1591 N N   . ALA   A 1 211 ? 12.208  -19.059 60.539 1.00 60.00  ? 211 ALA   A N   1 
ATOM   1592 C CA  . ALA   A 1 211 ? 12.977  -18.197 61.424 1.00 52.19  ? 211 ALA   A CA  1 
ATOM   1593 C C   . ALA   A 1 211 ? 13.364  -18.947 62.685 1.00 56.61  ? 211 ALA   A C   1 
ATOM   1594 O O   . ALA   A 1 211 ? 14.537  -18.953 63.085 1.00 58.55  ? 211 ALA   A O   1 
ATOM   1595 C CB  . ALA   A 1 211 ? 12.178  -16.939 61.761 1.00 52.50  ? 211 ALA   A CB  1 
ATOM   1596 N N   . ILE   A 1 212 ? 12.400  -19.651 63.286 1.00 54.02  ? 212 ILE   A N   1 
ATOM   1597 C CA  . ILE   A 1 212 ? 12.693  -20.408 64.496 1.00 52.41  ? 212 ILE   A CA  1 
ATOM   1598 C C   . ILE   A 1 212 ? 13.812  -21.397 64.218 1.00 61.99  ? 212 ILE   A C   1 
ATOM   1599 O O   . ILE   A 1 212 ? 14.804  -21.465 64.956 1.00 61.42  ? 212 ILE   A O   1 
ATOM   1600 C CB  . ILE   A 1 212 ? 11.426  -21.110 65.014 1.00 45.86  ? 212 ILE   A CB  1 
ATOM   1601 C CG1 . ILE   A 1 212 ? 10.402  -20.074 65.485 1.00 61.77  ? 212 ILE   A CG1 1 
ATOM   1602 C CG2 . ILE   A 1 212 ? 11.775  -22.074 66.135 1.00 56.20  ? 212 ILE   A CG2 1 
ATOM   1603 C CD1 . ILE   A 1 212 ? 9.028   -20.646 65.761 1.00 59.96  ? 212 ILE   A CD1 1 
ATOM   1604 N N   . SER   A 1 213 ? 13.709  -22.111 63.093 1.00 63.30  ? 213 SER   A N   1 
ATOM   1605 C CA  . SER   A 1 213 ? 14.763  -23.045 62.722 1.00 63.65  ? 213 SER   A CA  1 
ATOM   1606 C C   . SER   A 1 213 ? 16.095  -22.321 62.628 1.00 59.19  ? 213 SER   A C   1 
ATOM   1607 O O   . SER   A 1 213 ? 17.082  -22.721 63.262 1.00 61.35  ? 213 SER   A O   1 
ATOM   1608 C CB  . SER   A 1 213 ? 14.415  -23.726 61.398 1.00 54.48  ? 213 SER   A CB  1 
ATOM   1609 O OG  . SER   A 1 213 ? 15.462  -24.579 60.970 1.00 64.90  ? 213 SER   A OG  1 
ATOM   1610 N N   . ASP   A 1 214 ? 16.116  -21.195 61.908 1.00 57.06  ? 214 ASP   A N   1 
ATOM   1611 C CA  . ASP   A 1 214 ? 17.350  -20.432 61.788 1.00 61.42  ? 214 ASP   A CA  1 
ATOM   1612 C C   . ASP   A 1 214 ? 17.859  -20.030 63.161 1.00 61.49  ? 214 ASP   A C   1 
ATOM   1613 O O   . ASP   A 1 214 ? 19.055  -20.166 63.451 1.00 60.66  ? 214 ASP   A O   1 
ATOM   1614 C CB  . ASP   A 1 214 ? 17.128  -19.202 60.910 1.00 64.94  ? 214 ASP   A CB  1 
ATOM   1615 C CG  . ASP   A 1 214 ? 16.875  -19.561 59.460 1.00 82.28  ? 214 ASP   A CG  1 
ATOM   1616 O OD1 . ASP   A 1 214 ? 17.187  -20.705 59.068 1.00 89.91  ? 214 ASP   A OD1 1 
ATOM   1617 O OD2 . ASP   A 1 214 ? 16.361  -18.702 58.714 1.00 92.14  ? 214 ASP   A OD2 1 
ATOM   1618 N N   . ALA   A 1 215 ? 16.951  -19.603 64.044 1.00 63.95  ? 215 ALA   A N   1 
ATOM   1619 C CA  . ALA   A 1 215 ? 17.371  -19.213 65.382 1.00 67.41  ? 215 ALA   A CA  1 
ATOM   1620 C C   . ALA   A 1 215 ? 18.081  -20.367 66.069 1.00 65.18  ? 215 ALA   A C   1 
ATOM   1621 O O   . ALA   A 1 215 ? 19.180  -20.199 66.615 1.00 61.50  ? 215 ALA   A O   1 
ATOM   1622 C CB  . ALA   A 1 215 ? 16.167  -18.746 66.197 1.00 66.63  ? 215 ALA   A CB  1 
ATOM   1623 N N   . ARG   A 1 216 ? 17.499  -21.570 65.981 1.00 65.21  ? 216 ARG   A N   1 
ATOM   1624 C CA  . ARG   A 1 216 ? 18.139  -22.737 66.574 1.00 66.49  ? 216 ARG   A CA  1 
ATOM   1625 C C   . ARG   A 1 216 ? 19.552  -22.892 66.041 1.00 72.79  ? 216 ARG   A C   1 
ATOM   1626 O O   . ARG   A 1 216 ? 20.502  -23.086 66.812 1.00 74.26  ? 216 ARG   A O   1 
ATOM   1627 C CB  . ARG   A 1 216 ? 17.315  -23.996 66.305 1.00 57.17  ? 216 ARG   A CB  1 
ATOM   1628 C CG  . ARG   A 1 216 ? 17.983  -25.267 66.808 1.00 63.46  ? 216 ARG   A CG  1 
ATOM   1629 C CD  . ARG   A 1 216 ? 17.978  -25.333 68.330 1.00 65.99  ? 216 ARG   A CD  1 
ATOM   1630 N NE  . ARG   A 1 216 ? 18.844  -26.395 68.834 1.00 73.61  ? 216 ARG   A NE  1 
ATOM   1631 C CZ  . ARG   A 1 216 ? 18.442  -27.638 69.082 1.00 87.39  ? 216 ARG   A CZ  1 
ATOM   1632 N NH1 . ARG   A 1 216 ? 17.178  -27.984 68.876 1.00 83.05  ? 216 ARG   A NH1 1 
ATOM   1633 N NH2 . ARG   A 1 216 ? 19.305  -28.536 69.537 1.00 84.82  ? 216 ARG   A NH2 1 
ATOM   1634 N N   . CYS   A 1 217 ? 19.714  -22.751 64.723 1.00 63.36  ? 217 CYS   A N   1 
ATOM   1635 C CA  . CYS   A 1 217 ? 21.038  -22.864 64.127 1.00 62.93  ? 217 CYS   A CA  1 
ATOM   1636 C C   . CYS   A 1 217 ? 22.009  -21.910 64.806 1.00 68.13  ? 217 CYS   A C   1 
ATOM   1637 O O   . CYS   A 1 217 ? 23.078  -22.322 65.273 1.00 75.00  ? 217 CYS   A O   1 
ATOM   1638 C CB  . CYS   A 1 217 ? 20.959  -22.588 62.626 1.00 65.56  ? 217 CYS   A CB  1 
ATOM   1639 S SG  . CYS   A 1 217 ? 22.544  -22.675 61.771 1.00 97.43  ? 217 CYS   A SG  1 
ATOM   1640 N N   . VAL   A 1 218 ? 21.615  -20.641 64.944 1.00 69.04  ? 218 VAL   A N   1 
ATOM   1641 C CA  . VAL   A 1 218 ? 22.524  -19.670 65.541 1.00 71.22  ? 218 VAL   A CA  1 
ATOM   1642 C C   . VAL   A 1 218 ? 22.804  -20.050 66.986 1.00 63.28  ? 218 VAL   A C   1 
ATOM   1643 O O   . VAL   A 1 218 ? 23.941  -19.942 67.464 1.00 70.74  ? 218 VAL   A O   1 
ATOM   1644 C CB  . VAL   A 1 218 ? 21.958  -18.243 65.423 1.00 74.63  ? 218 VAL   A CB  1 
ATOM   1645 C CG1 . VAL   A 1 218 ? 22.901  -17.244 66.081 1.00 61.63  ? 218 VAL   A CG1 1 
ATOM   1646 C CG2 . VAL   A 1 218 ? 21.729  -17.883 63.969 1.00 65.10  ? 218 VAL   A CG2 1 
ATOM   1647 N N   . PHE   A 1 219 ? 21.781  -20.547 67.690 1.00 59.97  ? 219 PHE   A N   1 
ATOM   1648 C CA  . PHE   A 1 219 ? 21.990  -21.037 69.046 1.00 65.14  ? 219 PHE   A CA  1 
ATOM   1649 C C   . PHE   A 1 219 ? 23.123  -22.052 69.075 1.00 70.81  ? 219 PHE   A C   1 
ATOM   1650 O O   . PHE   A 1 219 ? 24.062  -21.932 69.872 1.00 71.47  ? 219 PHE   A O   1 
ATOM   1651 C CB  . PHE   A 1 219 ? 20.697  -21.648 69.591 1.00 62.76  ? 219 PHE   A CB  1 
ATOM   1652 C CG  . PHE   A 1 219 ? 19.898  -20.713 70.453 1.00 68.05  ? 219 PHE   A CG  1 
ATOM   1653 C CD1 . PHE   A 1 219 ? 19.320  -19.574 69.917 1.00 76.42  ? 219 PHE   A CD1 1 
ATOM   1654 C CD2 . PHE   A 1 219 ? 19.721  -20.976 71.802 1.00 53.48  ? 219 PHE   A CD2 1 
ATOM   1655 C CE1 . PHE   A 1 219 ? 18.581  -18.712 70.711 1.00 71.33  ? 219 PHE   A CE1 1 
ATOM   1656 C CE2 . PHE   A 1 219 ? 18.985  -20.119 72.601 1.00 63.45  ? 219 PHE   A CE2 1 
ATOM   1657 C CZ  . PHE   A 1 219 ? 18.414  -18.985 72.054 1.00 66.63  ? 219 PHE   A CZ  1 
ATOM   1658 N N   . ASP   A 1 220 ? 23.081  -23.026 68.159 1.00 67.64  ? 220 ASP   A N   1 
ATOM   1659 C CA  . ASP   A 1 220 ? 24.146  -24.019 68.104 1.00 66.57  ? 220 ASP   A CA  1 
ATOM   1660 C C   . ASP   A 1 220 ? 25.489  -23.355 67.844 1.00 73.26  ? 220 ASP   A C   1 
ATOM   1661 O O   . ASP   A 1 220 ? 26.486  -23.672 68.507 1.00 83.25  ? 220 ASP   A O   1 
ATOM   1662 C CB  . ASP   A 1 220 ? 23.837  -25.065 67.032 1.00 61.68  ? 220 ASP   A CB  1 
ATOM   1663 C CG  . ASP   A 1 220 ? 22.572  -25.849 67.330 1.00 83.19  ? 220 ASP   A CG  1 
ATOM   1664 O OD1 . ASP   A 1 220 ? 22.117  -25.828 68.494 1.00 79.34  ? 220 ASP   A OD1 1 
ATOM   1665 O OD2 . ASP   A 1 220 ? 22.030  -26.486 66.401 1.00 70.36  ? 220 ASP   A OD2 1 
ATOM   1666 N N   . MET   A 1 221 ? 25.522  -22.392 66.917 1.00 72.81  ? 221 MET   A N   1 
ATOM   1667 C CA  . MET   A 1 221 ? 26.747  -21.638 66.675 1.00 68.70  ? 221 MET   A CA  1 
ATOM   1668 C C   . MET   A 1 221 ? 27.265  -21.033 67.972 1.00 74.36  ? 221 MET   A C   1 
ATOM   1669 O O   . MET   A 1 221 ? 28.457  -21.134 68.287 1.00 78.03  ? 221 MET   A O   1 
ATOM   1670 C CB  . MET   A 1 221 ? 26.503  -20.554 65.624 1.00 63.55  ? 221 MET   A CB  1 
ATOM   1671 C CG  . MET   A 1 221 ? 26.302  -21.086 64.211 1.00 78.73  ? 221 MET   A CG  1 
ATOM   1672 S SD  . MET   A 1 221 ? 25.954  -19.779 63.014 1.00 98.22  ? 221 MET   A SD  1 
ATOM   1673 C CE  . MET   A 1 221 ? 25.692  -20.735 61.522 1.00 96.50  ? 221 MET   A CE  1 
ATOM   1674 N N   . GLY   A 1 222 ? 26.366  -20.431 68.757 1.00 73.07  ? 222 GLY   A N   1 
ATOM   1675 C CA  . GLY   A 1 222 ? 26.780  -19.870 70.031 1.00 81.59  ? 222 GLY   A CA  1 
ATOM   1676 C C   . GLY   A 1 222 ? 27.399  -20.916 70.934 1.00 84.27  ? 222 GLY   A C   1 
ATOM   1677 O O   . GLY   A 1 222 ? 28.451  -20.686 71.540 1.00 85.24  ? 222 GLY   A O   1 
ATOM   1678 N N   . ALA   A 1 223 ? 26.776  -22.098 71.001 1.00 79.90  ? 223 ALA   A N   1 
ATOM   1679 C CA  . ALA   A 1 223 ? 27.329  -23.176 71.810 1.00 82.88  ? 223 ALA   A CA  1 
ATOM   1680 C C   . ALA   A 1 223 ? 28.735  -23.537 71.354 1.00 91.85  ? 223 ALA   A C   1 
ATOM   1681 O O   . ALA   A 1 223 ? 29.583  -23.896 72.178 1.00 93.47  ? 223 ALA   A O   1 
ATOM   1682 C CB  . ALA   A 1 223 ? 26.412  -24.397 71.757 1.00 72.07  ? 223 ALA   A CB  1 
ATOM   1683 N N   . GLU   A 1 224 ? 29.002  -23.435 70.049 1.00 85.35  ? 224 GLU   A N   1 
ATOM   1684 C CA  . GLU   A 1 224 ? 30.335  -23.739 69.545 1.00 83.67  ? 224 GLU   A CA  1 
ATOM   1685 C C   . GLU   A 1 224 ? 31.359  -22.704 69.995 1.00 77.48  ? 224 GLU   A C   1 
ATOM   1686 O O   . GLU   A 1 224 ? 32.527  -23.046 70.212 1.00 88.18  ? 224 GLU   A O   1 
ATOM   1687 C CB  . GLU   A 1 224 ? 30.306  -23.843 68.020 1.00 76.35  ? 224 GLU   A CB  1 
ATOM   1688 C CG  . GLU   A 1 224 ? 29.649  -25.118 67.513 1.00 88.17  ? 224 GLU   A CG  1 
ATOM   1689 C CD  . GLU   A 1 224 ? 29.782  -25.290 66.015 1.00 100.68 ? 224 GLU   A CD  1 
ATOM   1690 O OE1 . GLU   A 1 224 ? 30.552  -24.527 65.395 1.00 103.88 ? 224 GLU   A OE1 1 
ATOM   1691 O OE2 . GLU   A 1 224 ? 29.116  -26.188 65.458 1.00 107.50 ? 224 GLU   A OE2 1 
ATOM   1692 N N   . VAL   A 1 225 ? 30.948  -21.439 70.137 1.00 75.39  ? 225 VAL   A N   1 
ATOM   1693 C CA  . VAL   A 1 225 ? 31.898  -20.378 70.465 1.00 76.01  ? 225 VAL   A CA  1 
ATOM   1694 C C   . VAL   A 1 225 ? 32.044  -20.185 71.970 1.00 80.71  ? 225 VAL   A C   1 
ATOM   1695 O O   . VAL   A 1 225 ? 32.931  -19.435 72.412 1.00 71.45  ? 225 VAL   A O   1 
ATOM   1696 C CB  . VAL   A 1 225 ? 31.457  -19.080 69.753 1.00 72.59  ? 225 VAL   A CB  1 
ATOM   1697 C CG1 . VAL   A 1 225 ? 32.507  -17.982 69.870 1.00 71.43  ? 225 VAL   A CG1 1 
ATOM   1698 C CG2 . VAL   A 1 225 ? 31.148  -19.364 68.292 1.00 58.17  ? 225 VAL   A CG2 1 
ATOM   1699 N N   . GLY   A 1 226 ? 31.243  -20.874 72.776 1.00 76.24  ? 226 GLY   A N   1 
ATOM   1700 C CA  . GLY   A 1 226 ? 31.348  -20.790 74.216 1.00 71.39  ? 226 GLY   A CA  1 
ATOM   1701 C C   . GLY   A 1 226 ? 30.287  -19.960 74.901 1.00 72.81  ? 226 GLY   A C   1 
ATOM   1702 O O   . GLY   A 1 226 ? 30.376  -19.761 76.118 1.00 82.89  ? 226 GLY   A O   1 
ATOM   1703 N N   . PHE   A 1 227 ? 29.290  -19.475 74.169 1.00 82.68  ? 227 PHE   A N   1 
ATOM   1704 C CA  . PHE   A 1 227 ? 28.222  -18.686 74.763 1.00 82.15  ? 227 PHE   A CA  1 
ATOM   1705 C C   . PHE   A 1 227 ? 27.154  -19.583 75.377 1.00 82.35  ? 227 PHE   A C   1 
ATOM   1706 O O   . PHE   A 1 227 ? 26.894  -20.693 74.904 1.00 81.08  ? 227 PHE   A O   1 
ATOM   1707 C CB  . PHE   A 1 227 ? 27.587  -17.772 73.715 1.00 74.39  ? 227 PHE   A CB  1 
ATOM   1708 C CG  . PHE   A 1 227 ? 28.460  -16.622 73.304 1.00 77.52  ? 227 PHE   A CG  1 
ATOM   1709 C CD1 . PHE   A 1 227 ? 28.830  -15.653 74.221 1.00 76.84  ? 227 PHE   A CD1 1 
ATOM   1710 C CD2 . PHE   A 1 227 ? 28.908  -16.508 71.998 1.00 76.70  ? 227 PHE   A CD2 1 
ATOM   1711 C CE1 . PHE   A 1 227 ? 29.633  -14.592 73.845 1.00 74.90  ? 227 PHE   A CE1 1 
ATOM   1712 C CE2 . PHE   A 1 227 ? 29.710  -15.450 71.616 1.00 73.78  ? 227 PHE   A CE2 1 
ATOM   1713 C CZ  . PHE   A 1 227 ? 30.073  -14.491 72.540 1.00 71.21  ? 227 PHE   A CZ  1 
ATOM   1714 N N   . SER   A 1 228 ? 26.525  -19.082 76.440 1.00 77.79  ? 228 SER   A N   1 
ATOM   1715 C CA  . SER   A 1 228 ? 25.390  -19.751 77.074 1.00 73.02  ? 228 SER   A CA  1 
ATOM   1716 C C   . SER   A 1 228 ? 24.129  -19.049 76.587 1.00 74.41  ? 228 SER   A C   1 
ATOM   1717 O O   . SER   A 1 228 ? 23.665  -18.077 77.183 1.00 85.33  ? 228 SER   A O   1 
ATOM   1718 C CB  . SER   A 1 228 ? 25.505  -19.711 78.592 1.00 83.69  ? 228 SER   A CB  1 
ATOM   1719 O OG  . SER   A 1 228 ? 26.576  -20.513 79.048 1.00 88.23  ? 228 SER   A OG  1 
ATOM   1720 N N   . MET   A 1 229 ? 23.569  -19.558 75.495 1.00 70.08  ? 229 MET   A N   1 
ATOM   1721 C CA  . MET   A 1 229 ? 22.409  -18.937 74.874 1.00 65.90  ? 229 MET   A CA  1 
ATOM   1722 C C   . MET   A 1 229 ? 21.135  -19.416 75.556 1.00 69.18  ? 229 MET   A C   1 
ATOM   1723 O O   . MET   A 1 229 ? 20.921  -20.622 75.712 1.00 69.52  ? 229 MET   A O   1 
ATOM   1724 C CB  . MET   A 1 229 ? 22.373  -19.271 73.386 1.00 74.60  ? 229 MET   A CB  1 
ATOM   1725 C CG  . MET   A 1 229 ? 23.713  -19.088 72.698 1.00 84.24  ? 229 MET   A CG  1 
ATOM   1726 S SD  . MET   A 1 229 ? 23.952  -17.421 72.066 1.00 82.59  ? 229 MET   A SD  1 
ATOM   1727 C CE  . MET   A 1 229 ? 22.919  -17.478 70.610 1.00 61.87  ? 229 MET   A CE  1 
ATOM   1728 N N   . TYR   A 1 230 ? 20.296  -18.471 75.976 1.00 56.79  ? 230 TYR   A N   1 
ATOM   1729 C CA  . TYR   A 1 230 ? 19.034  -18.833 76.606 1.00 56.41  ? 230 TYR   A CA  1 
ATOM   1730 C C   . TYR   A 1 230 ? 17.838  -18.025 76.128 1.00 66.30  ? 230 TYR   A C   1 
ATOM   1731 O O   . TYR   A 1 230 ? 16.709  -18.427 76.419 1.00 78.46  ? 230 TYR   A O   1 
ATOM   1732 C CB  . TYR   A 1 230 ? 19.136  -18.707 78.136 1.00 54.19  ? 230 TYR   A CB  1 
ATOM   1733 C CG  . TYR   A 1 230 ? 19.277  -17.289 78.650 1.00 57.75  ? 230 TYR   A CG  1 
ATOM   1734 C CD1 . TYR   A 1 230 ? 18.160  -16.543 79.006 1.00 53.13  ? 230 TYR   A CD1 1 
ATOM   1735 C CD2 . TYR   A 1 230 ? 20.528  -16.706 78.801 1.00 55.58  ? 230 TYR   A CD2 1 
ATOM   1736 C CE1 . TYR   A 1 230 ? 18.284  -15.250 79.483 1.00 63.62  ? 230 TYR   A CE1 1 
ATOM   1737 C CE2 . TYR   A 1 230 ? 20.662  -15.415 79.281 1.00 53.47  ? 230 TYR   A CE2 1 
ATOM   1738 C CZ  . TYR   A 1 230 ? 19.536  -14.691 79.619 1.00 69.35  ? 230 TYR   A CZ  1 
ATOM   1739 O OH  . TYR   A 1 230 ? 19.664  -13.405 80.094 1.00 74.96  ? 230 TYR   A OH  1 
ATOM   1740 N N   . LEU   A 1 231 ? 18.025  -16.914 75.425 1.00 58.93  ? 231 LEU   A N   1 
ATOM   1741 C CA  . LEU   A 1 231 ? 16.921  -16.028 75.081 1.00 61.81  ? 231 LEU   A CA  1 
ATOM   1742 C C   . LEU   A 1 231 ? 16.577  -16.161 73.601 1.00 55.92  ? 231 LEU   A C   1 
ATOM   1743 O O   . LEU   A 1 231 ? 17.438  -15.958 72.734 1.00 53.45  ? 231 LEU   A O   1 
ATOM   1744 C CB  . LEU   A 1 231 ? 17.260  -14.579 75.416 1.00 56.04  ? 231 LEU   A CB  1 
ATOM   1745 C CG  . LEU   A 1 231 ? 16.123  -13.645 75.008 1.00 62.92  ? 231 LEU   A CG  1 
ATOM   1746 C CD1 . LEU   A 1 231 ? 14.863  -13.950 75.809 1.00 71.00  ? 231 LEU   A CD1 1 
ATOM   1747 C CD2 . LEU   A 1 231 ? 16.522  -12.208 75.153 1.00 72.59  ? 231 LEU   A CD2 1 
ATOM   1748 N N   . LEU   A 1 232 ? 15.323  -16.510 73.319 1.00 58.53  ? 232 LEU   A N   1 
ATOM   1749 C CA  . LEU   A 1 232 ? 14.790  -16.562 71.962 1.00 66.64  ? 232 LEU   A CA  1 
ATOM   1750 C C   . LEU   A 1 232 ? 13.693  -15.517 71.823 1.00 60.99  ? 232 LEU   A C   1 
ATOM   1751 O O   . LEU   A 1 232 ? 12.696  -15.567 72.551 1.00 57.93  ? 232 LEU   A O   1 
ATOM   1752 C CB  . LEU   A 1 232 ? 14.239  -17.950 71.637 1.00 47.44  ? 232 LEU   A CB  1 
ATOM   1753 C CG  . LEU   A 1 232 ? 13.511  -18.001 70.293 1.00 49.59  ? 232 LEU   A CG  1 
ATOM   1754 C CD1 . LEU   A 1 232 ? 14.476  -17.713 69.152 1.00 45.54  ? 232 LEU   A CD1 1 
ATOM   1755 C CD2 . LEU   A 1 232 ? 12.803  -19.334 70.099 1.00 43.06  ? 232 LEU   A CD2 1 
ATOM   1756 N N   . ASP   A 1 233 ? 13.860  -14.594 70.878 1.00 56.46  ? 233 ASP   A N   1 
ATOM   1757 C CA  . ASP   A 1 233 ? 12.912  -13.502 70.673 1.00 62.44  ? 233 ASP   A CA  1 
ATOM   1758 C C   . ASP   A 1 233 ? 12.312  -13.658 69.280 1.00 62.20  ? 233 ASP   A C   1 
ATOM   1759 O O   . ASP   A 1 233 ? 13.018  -13.513 68.275 1.00 56.84  ? 233 ASP   A O   1 
ATOM   1760 C CB  . ASP   A 1 233 ? 13.599  -12.148 70.843 1.00 60.10  ? 233 ASP   A CB  1 
ATOM   1761 C CG  . ASP   A 1 233 ? 12.625  -10.979 70.817 1.00 76.66  ? 233 ASP   A CG  1 
ATOM   1762 O OD1 . ASP   A 1 233 ? 11.498  -11.118 70.296 1.00 79.40  ? 233 ASP   A OD1 1 
ATOM   1763 O OD2 . ASP   A 1 233 ? 12.993  -9.908  71.342 1.00 77.93  ? 233 ASP   A OD2 1 
ATOM   1764 N N   . ILE   A 1 234 ? 11.010  -13.943 69.222 1.00 47.31  ? 234 ILE   A N   1 
ATOM   1765 C CA  . ILE   A 1 234 ? 10.350  -14.247 67.959 1.00 48.41  ? 234 ILE   A CA  1 
ATOM   1766 C C   . ILE   A 1 234 ? 9.714   -12.994 67.367 1.00 54.69  ? 234 ILE   A C   1 
ATOM   1767 O O   . ILE   A 1 234 ? 8.968   -13.071 66.384 1.00 71.93  ? 234 ILE   A O   1 
ATOM   1768 C CB  . ILE   A 1 234 ? 9.301   -15.362 68.140 1.00 46.90  ? 234 ILE   A CB  1 
ATOM   1769 C CG1 . ILE   A 1 234 ? 8.127   -14.870 68.986 1.00 56.57  ? 234 ILE   A CG1 1 
ATOM   1770 C CG2 . ILE   A 1 234 ? 9.929   -16.587 68.786 1.00 42.08  ? 234 ILE   A CG2 1 
ATOM   1771 C CD1 . ILE   A 1 234 ? 6.974   -15.852 69.056 1.00 39.28  ? 234 ILE   A CD1 1 
ATOM   1772 N N   . GLY   A 1 235 ? 10.012  -11.833 67.951 1.00 60.83  ? 235 GLY   A N   1 
ATOM   1773 C CA  . GLY   A 1 235 ? 9.591   -10.572 67.364 1.00 62.06  ? 235 GLY   A CA  1 
ATOM   1774 C C   . GLY   A 1 235 ? 8.087   -10.357 67.415 1.00 58.85  ? 235 GLY   A C   1 
ATOM   1775 O O   . GLY   A 1 235 ? 7.383   -10.858 68.297 1.00 58.32  ? 235 GLY   A O   1 
ATOM   1776 N N   . GLY   A 1 236 ? 7.588   -9.594  66.443 1.00 61.03  ? 236 GLY   A N   1 
ATOM   1777 C CA  . GLY   A 1 236 ? 6.191   -9.237  66.361 1.00 56.63  ? 236 GLY   A CA  1 
ATOM   1778 C C   . GLY   A 1 236 ? 5.608   -9.580  65.002 1.00 63.03  ? 236 GLY   A C   1 
ATOM   1779 O O   . GLY   A 1 236 ? 6.006   -10.548 64.351 1.00 78.60  ? 236 GLY   A O   1 
ATOM   1780 N N   . GLY   A 1 237 ? 4.648   -8.758  64.578 1.00 56.98  ? 237 GLY   A N   1 
ATOM   1781 C CA  . GLY   A 1 237 ? 3.957   -8.955  63.322 1.00 53.42  ? 237 GLY   A CA  1 
ATOM   1782 C C   . GLY   A 1 237 ? 2.603   -9.620  63.430 1.00 54.52  ? 237 GLY   A C   1 
ATOM   1783 O O   . GLY   A 1 237 ? 1.930   -9.784  62.406 1.00 74.48  ? 237 GLY   A O   1 
ATOM   1784 N N   . PHE   A 1 238 ? 2.181   -10.004 64.630 1.00 57.80  ? 238 PHE   A N   1 
ATOM   1785 C CA  . PHE   A 1 238 ? 0.893   -10.660 64.794 1.00 60.92  ? 238 PHE   A CA  1 
ATOM   1786 C C   . PHE   A 1 238 ? -0.240  -9.666  64.544 1.00 65.37  ? 238 PHE   A C   1 
ATOM   1787 O O   . PHE   A 1 238 ? -0.118  -8.487  64.887 1.00 61.26  ? 238 PHE   A O   1 
ATOM   1788 C CB  . PHE   A 1 238 ? 0.774   -11.250 66.198 1.00 48.38  ? 238 PHE   A CB  1 
ATOM   1789 C CG  . PHE   A 1 238 ? 1.953   -12.086 66.603 1.00 54.09  ? 238 PHE   A CG  1 
ATOM   1790 C CD1 . PHE   A 1 238 ? 2.014   -13.429 66.272 1.00 62.98  ? 238 PHE   A CD1 1 
ATOM   1791 C CD2 . PHE   A 1 238 ? 3.005   -11.526 67.311 1.00 48.67  ? 238 PHE   A CD2 1 
ATOM   1792 C CE1 . PHE   A 1 238 ? 3.101   -14.199 66.643 1.00 70.40  ? 238 PHE   A CE1 1 
ATOM   1793 C CE2 . PHE   A 1 238 ? 4.094   -12.291 67.683 1.00 52.73  ? 238 PHE   A CE2 1 
ATOM   1794 C CZ  . PHE   A 1 238 ? 4.142   -13.629 67.349 1.00 56.36  ? 238 PHE   A CZ  1 
ATOM   1795 N N   . PRO   A 1 239 ? -1.351  -10.108 63.956 1.00 59.97  ? 239 PRO   A N   1 
ATOM   1796 C CA  . PRO   A 1 239 ? -2.446  -9.179  63.657 1.00 49.37  ? 239 PRO   A CA  1 
ATOM   1797 C C   . PRO   A 1 239 ? -3.122  -8.668  64.918 1.00 64.20  ? 239 PRO   A C   1 
ATOM   1798 O O   . PRO   A 1 239 ? -3.200  -9.356  65.939 1.00 64.24  ? 239 PRO   A O   1 
ATOM   1799 C CB  . PRO   A 1 239 ? -3.411  -10.027 62.823 1.00 50.18  ? 239 PRO   A CB  1 
ATOM   1800 C CG  . PRO   A 1 239 ? -3.159  -11.420 63.279 1.00 53.11  ? 239 PRO   A CG  1 
ATOM   1801 C CD  . PRO   A 1 239 ? -1.680  -11.489 63.560 1.00 56.36  ? 239 PRO   A CD  1 
ATOM   1802 N N   . GLY   A 1 240 ? -3.621  -7.439  64.831 1.00 77.45  ? 240 GLY   A N   1 
ATOM   1803 C CA  . GLY   A 1 240 ? -4.302  -6.791  65.927 1.00 67.92  ? 240 GLY   A CA  1 
ATOM   1804 C C   . GLY   A 1 240 ? -5.805  -6.739  65.813 1.00 68.40  ? 240 GLY   A C   1 
ATOM   1805 O O   . GLY   A 1 240 ? -6.461  -6.174  66.694 1.00 69.94  ? 240 GLY   A O   1 
ATOM   1806 N N   . SER   A 1 241 ? -6.376  -7.296  64.749 1.00 71.90  ? 241 SER   A N   1 
ATOM   1807 C CA  . SER   A 1 241 ? -7.819  -7.344  64.587 1.00 67.76  ? 241 SER   A CA  1 
ATOM   1808 C C   . SER   A 1 241 ? -8.177  -8.606  63.819 1.00 66.71  ? 241 SER   A C   1 
ATOM   1809 O O   . SER   A 1 241 ? -7.320  -9.260  63.221 1.00 65.19  ? 241 SER   A O   1 
ATOM   1810 C CB  . SER   A 1 241 ? -8.344  -6.098  63.869 1.00 68.80  ? 241 SER   A CB  1 
ATOM   1811 O OG  . SER   A 1 241 ? -8.093  -6.174  62.479 1.00 68.71  ? 241 SER   A OG  1 
ATOM   1812 N N   . GLU   A 1 242 ? -9.464  -8.946  63.845 1.00 93.16  ? 242 GLU   A N   1 
ATOM   1813 C CA  . GLU   A 1 242 ? -9.965  -10.092 63.099 1.00 89.26  ? 242 GLU   A CA  1 
ATOM   1814 C C   . GLU   A 1 242 ? -10.210 -9.779  61.630 1.00 87.27  ? 242 GLU   A C   1 
ATOM   1815 O O   . GLU   A 1 242 ? -10.544 -10.692 60.867 1.00 87.64  ? 242 GLU   A O   1 
ATOM   1816 C CB  . GLU   A 1 242 ? -11.252 -10.615 63.741 1.00 80.50  ? 242 GLU   A CB  1 
ATOM   1817 C CG  . GLU   A 1 242 ? -11.044 -11.225 65.117 1.00 91.15  ? 242 GLU   A CG  1 
ATOM   1818 C CD  . GLU   A 1 242 ? -9.893  -12.212 65.146 1.00 96.27  ? 242 GLU   A CD  1 
ATOM   1819 O OE1 . GLU   A 1 242 ? -10.010 -13.283 64.513 1.00 102.65 ? 242 GLU   A OE1 1 
ATOM   1820 O OE2 . GLU   A 1 242 ? -8.870  -11.919 65.802 1.00 88.51  ? 242 GLU   A OE2 1 
ATOM   1821 N N   . ASP   A 1 243 ? -10.044 -8.524  61.213 1.00 90.43  ? 243 ASP   A N   1 
ATOM   1822 C CA  . ASP   A 1 243 ? -10.295 -8.139  59.831 1.00 81.82  ? 243 ASP   A CA  1 
ATOM   1823 C C   . ASP   A 1 243 ? -9.067  -8.415  58.972 1.00 81.84  ? 243 ASP   A C   1 
ATOM   1824 O O   . ASP   A 1 243 ? -8.570  -7.527  58.272 1.00 80.20  ? 243 ASP   A O   1 
ATOM   1825 C CB  . ASP   A 1 243 ? -10.694 -6.663  59.752 1.00 87.95  ? 243 ASP   A CB  1 
ATOM   1826 C CG  . ASP   A 1 243 ? -11.249 -6.279  58.394 1.00 111.30 ? 243 ASP   A CG  1 
ATOM   1827 O OD1 . ASP   A 1 243 ? -11.684 -7.185  57.650 1.00 107.05 ? 243 ASP   A OD1 1 
ATOM   1828 O OD2 . ASP   A 1 243 ? -11.256 -5.072  58.074 1.00 119.30 ? 243 ASP   A OD2 1 
ATOM   1829 N N   . VAL   A 1 244 ? -8.568  -9.648  59.029 1.00 89.33  ? 244 VAL   A N   1 
ATOM   1830 C CA  . VAL   A 1 244 ? -7.402  -10.071 58.265 1.00 77.91  ? 244 VAL   A CA  1 
ATOM   1831 C C   . VAL   A 1 244 ? -7.622  -11.508 57.824 1.00 92.12  ? 244 VAL   A C   1 
ATOM   1832 O O   . VAL   A 1 244 ? -8.379  -12.262 58.445 1.00 92.15  ? 244 VAL   A O   1 
ATOM   1833 C CB  . VAL   A 1 244 ? -6.086  -9.957  59.065 1.00 68.96  ? 244 VAL   A CB  1 
ATOM   1834 C CG1 . VAL   A 1 244 ? -5.753  -8.505  59.361 1.00 61.63  ? 244 VAL   A CG1 1 
ATOM   1835 C CG2 . VAL   A 1 244 ? -6.177  -10.764 60.347 1.00 76.61  ? 244 VAL   A CG2 1 
ATOM   1836 N N   . LYS   A 1 245 ? -6.950  -11.885 56.736 1.00 81.46  ? 245 LYS   A N   1 
ATOM   1837 C CA  . LYS   A 1 245 ? -7.060  -13.253 56.246 1.00 92.09  ? 245 LYS   A CA  1 
ATOM   1838 C C   . LYS   A 1 245 ? -6.295  -14.220 57.140 1.00 92.61  ? 245 LYS   A C   1 
ATOM   1839 O O   . LYS   A 1 245 ? -6.783  -15.317 57.442 1.00 98.89  ? 245 LYS   A O   1 
ATOM   1840 C CB  . LYS   A 1 245 ? -6.565  -13.337 54.804 1.00 90.69  ? 245 LYS   A CB  1 
ATOM   1841 C CG  . LYS   A 1 245 ? -6.696  -14.734 54.190 1.00 91.42  ? 245 LYS   A CG  1 
ATOM   1842 C CD  . LYS   A 1 245 ? -6.015  -14.811 52.830 1.00 101.95 ? 245 LYS   A CD  1 
ATOM   1843 C CE  . LYS   A 1 245 ? -6.208  -16.156 52.142 1.00 98.84  ? 245 LYS   A CE  1 
ATOM   1844 N NZ  . LYS   A 1 245 ? -5.661  -16.137 50.754 1.00 98.76  ? 245 LYS   A NZ  1 
ATOM   1845 N N   . LEU   A 1 246 ? -5.100  -13.830 57.575 1.00 81.89  ? 246 LEU   A N   1 
ATOM   1846 C CA  . LEU   A 1 246 ? -4.248  -14.664 58.418 1.00 87.86  ? 246 LEU   A CA  1 
ATOM   1847 C C   . LEU   A 1 246 ? -4.450  -14.212 59.859 1.00 86.76  ? 246 LEU   A C   1 
ATOM   1848 O O   . LEU   A 1 246 ? -3.930  -13.174 60.275 1.00 80.40  ? 246 LEU   A O   1 
ATOM   1849 C CB  . LEU   A 1 246 ? -2.789  -14.552 57.996 1.00 82.43  ? 246 LEU   A CB  1 
ATOM   1850 C CG  . LEU   A 1 246 ? -1.820  -15.403 58.816 1.00 74.19  ? 246 LEU   A CG  1 
ATOM   1851 C CD1 . LEU   A 1 246 ? -2.137  -16.881 58.660 1.00 82.44  ? 246 LEU   A CD1 1 
ATOM   1852 C CD2 . LEU   A 1 246 ? -0.379  -15.107 58.435 1.00 82.79  ? 246 LEU   A CD2 1 
ATOM   1853 N N   . LYS   A 1 247 ? -5.207  -14.997 60.615 1.00 85.73  ? 247 LYS   A N   1 
ATOM   1854 C CA  . LYS   A 1 247 ? -5.601  -14.640 61.968 1.00 88.14  ? 247 LYS   A CA  1 
ATOM   1855 C C   . LYS   A 1 247 ? -4.570  -15.112 62.990 1.00 75.76  ? 247 LYS   A C   1 
ATOM   1856 O O   . LYS   A 1 247 ? -3.748  -15.994 62.726 1.00 76.85  ? 247 LYS   A O   1 
ATOM   1857 C CB  . LYS   A 1 247 ? -6.982  -15.212 62.290 1.00 92.54  ? 247 LYS   A CB  1 
ATOM   1858 C CG  . LYS   A 1 247 ? -8.117  -14.365 61.733 1.00 95.97  ? 247 LYS   A CG  1 
ATOM   1859 C CD  . LYS   A 1 247 ? -9.382  -15.173 61.513 1.00 99.03  ? 247 LYS   A CD  1 
ATOM   1860 C CE  . LYS   A 1 247 ? -10.441 -14.339 60.808 1.00 92.75  ? 247 LYS   A CE  1 
ATOM   1861 N NZ  . LYS   A 1 247 ? -9.994  -13.896 59.457 1.00 81.42  ? 247 LYS   A NZ  1 
ATOM   1862 N N   . PHE   A 1 248 ? -4.622  -14.485 64.169 1.00 73.51  ? 248 PHE   A N   1 
ATOM   1863 C CA  . PHE   A 1 248 ? -3.646  -14.734 65.229 1.00 77.39  ? 248 PHE   A CA  1 
ATOM   1864 C C   . PHE   A 1 248 ? -3.528  -16.218 65.564 1.00 72.72  ? 248 PHE   A C   1 
ATOM   1865 O O   . PHE   A 1 248 ? -2.420  -16.756 65.685 1.00 74.31  ? 248 PHE   A O   1 
ATOM   1866 C CB  . PHE   A 1 248 ? -4.037  -13.926 66.470 1.00 68.58  ? 248 PHE   A CB  1 
ATOM   1867 C CG  . PHE   A 1 248 ? -3.095  -14.085 67.628 1.00 60.26  ? 248 PHE   A CG  1 
ATOM   1868 C CD1 . PHE   A 1 248 ? -1.765  -13.714 67.516 1.00 62.52  ? 248 PHE   A CD1 1 
ATOM   1869 C CD2 . PHE   A 1 248 ? -3.545  -14.589 68.838 1.00 66.72  ? 248 PHE   A CD2 1 
ATOM   1870 C CE1 . PHE   A 1 248 ? -0.899  -13.853 68.587 1.00 75.00  ? 248 PHE   A CE1 1 
ATOM   1871 C CE2 . PHE   A 1 248 ? -2.685  -14.731 69.911 1.00 63.35  ? 248 PHE   A CE2 1 
ATOM   1872 C CZ  . PHE   A 1 248 ? -1.361  -14.361 69.787 1.00 59.76  ? 248 PHE   A CZ  1 
ATOM   1873 N N   . GLU   A 1 249 ? -4.667  -16.897 65.716 1.00 70.99  ? 249 GLU   A N   1 
ATOM   1874 C CA  . GLU   A 1 249 ? -4.645  -18.272 66.204 1.00 76.59  ? 249 GLU   A CA  1 
ATOM   1875 C C   . GLU   A 1 249 ? -4.011  -19.230 65.202 1.00 77.22  ? 249 GLU   A C   1 
ATOM   1876 O O   . GLU   A 1 249 ? -3.378  -20.207 65.611 1.00 74.64  ? 249 GLU   A O   1 
ATOM   1877 C CB  . GLU   A 1 249 ? -6.061  -18.725 66.561 1.00 71.82  ? 249 GLU   A CB  1 
ATOM   1878 C CG  . GLU   A 1 249 ? -6.484  -18.361 67.978 1.00 79.93  ? 249 GLU   A CG  1 
ATOM   1879 C CD  . GLU   A 1 249 ? -6.761  -16.879 68.156 1.00 96.70  ? 249 GLU   A CD  1 
ATOM   1880 O OE1 . GLU   A 1 249 ? -6.837  -16.153 67.143 1.00 87.77  ? 249 GLU   A OE1 1 
ATOM   1881 O OE2 . GLU   A 1 249 ? -6.903  -16.440 69.318 1.00 83.90  ? 249 GLU   A OE2 1 
ATOM   1882 N N   . GLU   A 1 250 ? -4.150  -18.969 63.900 1.00 77.66  ? 250 GLU   A N   1 
ATOM   1883 C CA  . GLU   A 1 250 ? -3.446  -19.779 62.909 1.00 71.23  ? 250 GLU   A CA  1 
ATOM   1884 C C   . GLU   A 1 250 ? -1.936  -19.650 63.082 1.00 74.30  ? 250 GLU   A C   1 
ATOM   1885 O O   . GLU   A 1 250 ? -1.203  -20.651 63.083 1.00 81.09  ? 250 GLU   A O   1 
ATOM   1886 C CB  . GLU   A 1 250 ? -3.861  -19.359 61.499 1.00 84.83  ? 250 GLU   A CB  1 
ATOM   1887 C CG  . GLU   A 1 250 ? -5.363  -19.230 61.294 1.00 99.12  ? 250 GLU   A CG  1 
ATOM   1888 C CD  . GLU   A 1 250 ? -5.721  -18.683 59.924 1.00 114.65 ? 250 GLU   A CD  1 
ATOM   1889 O OE1 . GLU   A 1 250 ? -5.166  -19.177 58.920 1.00 111.05 ? 250 GLU   A OE1 1 
ATOM   1890 O OE2 . GLU   A 1 250 ? -6.557  -17.758 59.850 1.00 109.18 ? 250 GLU   A OE2 1 
ATOM   1891 N N   . ILE   A 1 251 ? -1.457  -18.414 63.231 1.00 68.86  ? 251 ILE   A N   1 
ATOM   1892 C CA  . ILE   A 1 251 ? -0.033  -18.173 63.433 1.00 72.31  ? 251 ILE   A CA  1 
ATOM   1893 C C   . ILE   A 1 251 ? 0.456   -18.885 64.687 1.00 70.01  ? 251 ILE   A C   1 
ATOM   1894 O O   . ILE   A 1 251 ? 1.518   -19.515 64.683 1.00 72.90  ? 251 ILE   A O   1 
ATOM   1895 C CB  . ILE   A 1 251 ? 0.249   -16.660 63.490 1.00 73.12  ? 251 ILE   A CB  1 
ATOM   1896 C CG1 . ILE   A 1 251 ? -0.175  -15.993 62.182 1.00 70.87  ? 251 ILE   A CG1 1 
ATOM   1897 C CG2 . ILE   A 1 251 ? 1.719   -16.400 63.763 1.00 75.67  ? 251 ILE   A CG2 1 
ATOM   1898 C CD1 . ILE   A 1 251 ? -0.078  -14.486 62.208 1.00 64.43  ? 251 ILE   A CD1 1 
ATOM   1899 N N   . THR   A 1 252 ? -0.307  -18.800 65.779 1.00 68.97  ? 252 THR   A N   1 
ATOM   1900 C CA  . THR   A 1 252 ? 0.130   -19.438 67.018 1.00 66.30  ? 252 THR   A CA  1 
ATOM   1901 C C   . THR   A 1 252 ? 0.099   -20.960 66.910 1.00 68.66  ? 252 THR   A C   1 
ATOM   1902 O O   . THR   A 1 252 ? 0.979   -21.645 67.451 1.00 69.97  ? 252 THR   A O   1 
ATOM   1903 C CB  . THR   A 1 252 ? -0.738  -18.969 68.183 1.00 75.03  ? 252 THR   A CB  1 
ATOM   1904 O OG1 . THR   A 1 252 ? -2.100  -19.341 67.942 1.00 69.16  ? 252 THR   A OG1 1 
ATOM   1905 C CG2 . THR   A 1 252 ? -0.643  -17.461 68.337 1.00 66.23  ? 252 THR   A CG2 1 
ATOM   1906 N N   . GLY   A 1 253 ? -0.908  -21.508 66.224 1.00 72.08  ? 253 GLY   A N   1 
ATOM   1907 C CA  . GLY   A 1 253 ? -0.967  -22.942 66.010 1.00 65.29  ? 253 GLY   A CA  1 
ATOM   1908 C C   . GLY   A 1 253 ? 0.160   -23.459 65.145 1.00 64.60  ? 253 GLY   A C   1 
ATOM   1909 O O   . GLY   A 1 253 ? 0.524   -24.635 65.231 1.00 65.71  ? 253 GLY   A O   1 
ATOM   1910 N N   . VAL   A 1 254 ? 0.702   -22.606 64.277 1.00 63.53  ? 254 VAL   A N   1 
ATOM   1911 C CA  . VAL   A 1 254 ? 1.885   -23.004 63.522 1.00 60.24  ? 254 VAL   A CA  1 
ATOM   1912 C C   . VAL   A 1 254 ? 3.160   -22.799 64.347 1.00 67.00  ? 254 VAL   A C   1 
ATOM   1913 O O   . VAL   A 1 254 ? 4.126   -23.560 64.208 1.00 54.23  ? 254 VAL   A O   1 
ATOM   1914 C CB  . VAL   A 1 254 ? 1.930   -22.238 62.188 1.00 64.99  ? 254 VAL   A CB  1 
ATOM   1915 C CG1 . VAL   A 1 254 ? 3.244   -22.465 61.471 1.00 65.07  ? 254 VAL   A CG1 1 
ATOM   1916 C CG2 . VAL   A 1 254 ? 0.764   -22.658 61.304 1.00 74.80  ? 254 VAL   A CG2 1 
ATOM   1917 N N   . ILE   A 1 255 ? 3.175   -21.803 65.235 1.00 68.38  ? 255 ILE   A N   1 
ATOM   1918 C CA  . ILE   A 1 255 ? 4.388   -21.464 65.975 1.00 54.21  ? 255 ILE   A CA  1 
ATOM   1919 C C   . ILE   A 1 255 ? 4.660   -22.476 67.082 1.00 70.35  ? 255 ILE   A C   1 
ATOM   1920 O O   . ILE   A 1 255 ? 5.799   -22.923 67.263 1.00 67.72  ? 255 ILE   A O   1 
ATOM   1921 C CB  . ILE   A 1 255 ? 4.287   -20.033 66.537 1.00 55.76  ? 255 ILE   A CB  1 
ATOM   1922 C CG1 . ILE   A 1 255 ? 4.522   -18.999 65.437 1.00 60.44  ? 255 ILE   A CG1 1 
ATOM   1923 C CG2 . ILE   A 1 255 ? 5.273   -19.823 67.676 1.00 53.28  ? 255 ILE   A CG2 1 
ATOM   1924 C CD1 . ILE   A 1 255 ? 4.372   -17.574 65.916 1.00 68.14  ? 255 ILE   A CD1 1 
ATOM   1925 N N   . ASN   A 1 256 ? 3.629   -22.846 67.843 1.00 67.65  ? 256 ASN   A N   1 
ATOM   1926 C CA  . ASN   A 1 256 ? 3.852   -23.668 69.032 1.00 60.19  ? 256 ASN   A CA  1 
ATOM   1927 C C   . ASN   A 1 256 ? 4.520   -25.010 68.741 1.00 75.69  ? 256 ASN   A C   1 
ATOM   1928 O O   . ASN   A 1 256 ? 5.444   -25.377 69.489 1.00 65.93  ? 256 ASN   A O   1 
ATOM   1929 C CB  . ASN   A 1 256 ? 2.528   -23.868 69.780 1.00 53.13  ? 256 ASN   A CB  1 
ATOM   1930 C CG  . ASN   A 1 256 ? 2.115   -22.641 70.562 1.00 64.55  ? 256 ASN   A CG  1 
ATOM   1931 O OD1 . ASN   A 1 256 ? 2.955   -21.944 71.131 1.00 67.02  ? 256 ASN   A OD1 1 
ATOM   1932 N ND2 . ASN   A 1 256 ? 0.817   -22.365 70.592 1.00 68.21  ? 256 ASN   A ND2 1 
ATOM   1933 N N   . PRO   A 1 257 ? 4.124   -25.780 67.718 1.00 67.83  ? 257 PRO   A N   1 
ATOM   1934 C CA  . PRO   A 1 257 ? 4.887   -27.003 67.415 1.00 60.98  ? 257 PRO   A CA  1 
ATOM   1935 C C   . PRO   A 1 257 ? 6.337   -26.727 67.064 1.00 64.19  ? 257 PRO   A C   1 
ATOM   1936 O O   . PRO   A 1 257 ? 7.221   -27.492 67.465 1.00 69.11  ? 257 PRO   A O   1 
ATOM   1937 C CB  . PRO   A 1 257 ? 4.117   -27.613 66.237 1.00 60.12  ? 257 PRO   A CB  1 
ATOM   1938 C CG  . PRO   A 1 257 ? 2.744   -27.073 66.367 1.00 63.12  ? 257 PRO   A CG  1 
ATOM   1939 C CD  . PRO   A 1 257 ? 2.911   -25.682 66.888 1.00 55.85  ? 257 PRO   A CD  1 
ATOM   1940 N N   . ALA   A 1 258 ? 6.610   -25.648 66.326 1.00 60.38  ? 258 ALA   A N   1 
ATOM   1941 C CA  . ALA   A 1 258 ? 7.992   -25.311 66.001 1.00 65.31  ? 258 ALA   A CA  1 
ATOM   1942 C C   . ALA   A 1 258 ? 8.790   -24.987 67.258 1.00 61.74  ? 258 ALA   A C   1 
ATOM   1943 O O   . ALA   A 1 258 ? 9.949   -25.400 67.391 1.00 65.72  ? 258 ALA   A O   1 
ATOM   1944 C CB  . ALA   A 1 258 ? 8.033   -24.142 65.018 1.00 60.29  ? 258 ALA   A CB  1 
ATOM   1945 N N   . LEU   A 1 259 ? 8.189   -24.243 68.190 1.00 72.94  ? 259 LEU   A N   1 
ATOM   1946 C CA  . LEU   A 1 259 ? 8.862   -23.954 69.453 1.00 68.60  ? 259 LEU   A CA  1 
ATOM   1947 C C   . LEU   A 1 259 ? 9.138   -25.231 70.233 1.00 69.08  ? 259 LEU   A C   1 
ATOM   1948 O O   . LEU   A 1 259 ? 10.228  -25.404 70.791 1.00 70.40  ? 259 LEU   A O   1 
ATOM   1949 C CB  . LEU   A 1 259 ? 8.027   -22.988 70.293 1.00 60.74  ? 259 LEU   A CB  1 
ATOM   1950 C CG  . LEU   A 1 259 ? 7.911   -21.547 69.792 1.00 68.69  ? 259 LEU   A CG  1 
ATOM   1951 C CD1 . LEU   A 1 259 ? 7.077   -20.715 70.754 1.00 55.19  ? 259 LEU   A CD1 1 
ATOM   1952 C CD2 . LEU   A 1 259 ? 9.288   -20.931 69.596 1.00 50.42  ? 259 LEU   A CD2 1 
ATOM   1953 N N   . ASP   A 1 260 ? 8.161   -26.140 70.287 1.00 76.41  ? 260 ASP   A N   1 
ATOM   1954 C CA  . ASP   A 1 260 ? 8.370   -27.394 71.003 1.00 80.01  ? 260 ASP   A CA  1 
ATOM   1955 C C   . ASP   A 1 260 ? 9.449   -28.246 70.344 1.00 76.69  ? 260 ASP   A C   1 
ATOM   1956 O O   . ASP   A 1 260 ? 10.200  -28.943 71.036 1.00 75.29  ? 260 ASP   A O   1 
ATOM   1957 C CB  . ASP   A 1 260 ? 7.056   -28.170 71.092 1.00 67.60  ? 260 ASP   A CB  1 
ATOM   1958 C CG  . ASP   A 1 260 ? 6.019   -27.462 71.944 1.00 86.83  ? 260 ASP   A CG  1 
ATOM   1959 O OD1 . ASP   A 1 260 ? 6.381   -26.486 72.635 1.00 85.63  ? 260 ASP   A OD1 1 
ATOM   1960 O OD2 . ASP   A 1 260 ? 4.843   -27.883 71.925 1.00 100.65 ? 260 ASP   A OD2 1 
ATOM   1961 N N   . LYS   A 1 261 ? 9.547   -28.197 69.016 1.00 65.17  ? 261 LYS   A N   1 
ATOM   1962 C CA  . LYS   A 1 261 ? 10.521  -29.017 68.304 1.00 61.84  ? 261 LYS   A CA  1 
ATOM   1963 C C   . LYS   A 1 261 ? 11.936  -28.468 68.443 1.00 74.87  ? 261 LYS   A C   1 
ATOM   1964 O O   . LYS   A 1 261 ? 12.868  -29.211 68.769 1.00 83.00  ? 261 LYS   A O   1 
ATOM   1965 C CB  . LYS   A 1 261 ? 10.132  -29.119 66.828 1.00 64.58  ? 261 LYS   A CB  1 
ATOM   1966 C CG  . LYS   A 1 261 ? 11.202  -29.735 65.946 1.00 67.44  ? 261 LYS   A CG  1 
ATOM   1967 C CD  . LYS   A 1 261 ? 10.723  -29.858 64.509 1.00 76.56  ? 261 LYS   A CD  1 
ATOM   1968 C CE  . LYS   A 1 261 ? 11.810  -30.423 63.608 1.00 85.98  ? 261 LYS   A CE  1 
ATOM   1969 N NZ  . LYS   A 1 261 ? 11.346  -30.589 62.202 1.00 91.10  ? 261 LYS   A NZ  1 
ATOM   1970 N N   . TYR   A 1 262 ? 12.119  -27.169 68.206 1.00 76.58  ? 262 TYR   A N   1 
ATOM   1971 C CA  . TYR   A 1 262 ? 13.463  -26.604 68.173 1.00 60.70  ? 262 TYR   A CA  1 
ATOM   1972 C C   . TYR   A 1 262 ? 13.921  -26.055 69.515 1.00 63.64  ? 262 TYR   A C   1 
ATOM   1973 O O   . TYR   A 1 262 ? 15.129  -26.022 69.776 1.00 71.77  ? 262 TYR   A O   1 
ATOM   1974 C CB  . TYR   A 1 262 ? 13.546  -25.498 67.118 1.00 64.36  ? 262 TYR   A CB  1 
ATOM   1975 C CG  . TYR   A 1 262 ? 13.348  -25.986 65.702 1.00 66.00  ? 262 TYR   A CG  1 
ATOM   1976 C CD1 . TYR   A 1 262 ? 14.399  -26.547 64.989 1.00 64.43  ? 262 TYR   A CD1 1 
ATOM   1977 C CD2 . TYR   A 1 262 ? 12.113  -25.888 65.077 1.00 68.38  ? 262 TYR   A CD2 1 
ATOM   1978 C CE1 . TYR   A 1 262 ? 14.227  -26.994 63.692 1.00 66.18  ? 262 TYR   A CE1 1 
ATOM   1979 C CE2 . TYR   A 1 262 ? 11.929  -26.333 63.781 1.00 76.05  ? 262 TYR   A CE2 1 
ATOM   1980 C CZ  . TYR   A 1 262 ? 12.991  -26.885 63.094 1.00 71.04  ? 262 TYR   A CZ  1 
ATOM   1981 O OH  . TYR   A 1 262 ? 12.815  -27.331 61.804 1.00 69.76  ? 262 TYR   A OH  1 
ATOM   1982 N N   . PHE   A 1 263 ? 13.000  -25.625 70.373 1.00 58.44  ? 263 PHE   A N   1 
ATOM   1983 C CA  . PHE   A 1 263 ? 13.341  -25.061 71.679 1.00 62.58  ? 263 PHE   A CA  1 
ATOM   1984 C C   . PHE   A 1 263 ? 12.465  -25.693 72.752 1.00 72.39  ? 263 PHE   A C   1 
ATOM   1985 O O   . PHE   A 1 263 ? 11.567  -25.043 73.303 1.00 71.10  ? 263 PHE   A O   1 
ATOM   1986 C CB  . PHE   A 1 263 ? 13.189  -23.540 71.674 1.00 62.94  ? 263 PHE   A CB  1 
ATOM   1987 C CG  . PHE   A 1 263 ? 14.171  -22.835 70.785 1.00 61.16  ? 263 PHE   A CG  1 
ATOM   1988 C CD1 . PHE   A 1 263 ? 15.377  -22.379 71.290 1.00 56.81  ? 263 PHE   A CD1 1 
ATOM   1989 C CD2 . PHE   A 1 263 ? 13.890  -22.631 69.443 1.00 54.43  ? 263 PHE   A CD2 1 
ATOM   1990 C CE1 . PHE   A 1 263 ? 16.285  -21.727 70.476 1.00 56.50  ? 263 PHE   A CE1 1 
ATOM   1991 C CE2 . PHE   A 1 263 ? 14.795  -21.980 68.623 1.00 60.54  ? 263 PHE   A CE2 1 
ATOM   1992 C CZ  . PHE   A 1 263 ? 15.994  -21.527 69.141 1.00 56.71  ? 263 PHE   A CZ  1 
ATOM   1993 N N   . PRO   A 1 264 ? 12.696  -26.967 73.071 1.00 82.92  ? 264 PRO   A N   1 
ATOM   1994 C CA  . PRO   A 1 264 ? 11.905  -27.614 74.124 1.00 77.20  ? 264 PRO   A CA  1 
ATOM   1995 C C   . PRO   A 1 264 ? 12.131  -26.945 75.472 1.00 72.23  ? 264 PRO   A C   1 
ATOM   1996 O O   . PRO   A 1 264 ? 13.181  -26.351 75.729 1.00 76.44  ? 264 PRO   A O   1 
ATOM   1997 C CB  . PRO   A 1 264 ? 12.413  -29.060 74.116 1.00 87.57  ? 264 PRO   A CB  1 
ATOM   1998 C CG  . PRO   A 1 264 ? 13.763  -28.993 73.486 1.00 76.51  ? 264 PRO   A CG  1 
ATOM   1999 C CD  . PRO   A 1 264 ? 13.717  -27.865 72.505 1.00 73.11  ? 264 PRO   A CD  1 
ATOM   2000 N N   . SER   A 1 265 ? 11.116  -27.041 76.336 1.00 70.62  ? 265 SER   A N   1 
ATOM   2001 C CA  . SER   A 1 265 ? 11.160  -26.346 77.621 1.00 87.93  ? 265 SER   A CA  1 
ATOM   2002 C C   . SER   A 1 265 ? 12.297  -26.844 78.507 1.00 92.05  ? 265 SER   A C   1 
ATOM   2003 O O   . SER   A 1 265 ? 12.879  -26.058 79.263 1.00 96.97  ? 265 SER   A O   1 
ATOM   2004 C CB  . SER   A 1 265 ? 9.818   -26.492 78.342 1.00 74.06  ? 265 SER   A CB  1 
ATOM   2005 O OG  . SER   A 1 265 ? 9.411   -27.847 78.405 1.00 89.76  ? 265 SER   A OG  1 
ATOM   2006 N N   . ASP   A 1 266 ? 12.626  -28.137 78.434 1.00 92.72  ? 266 ASP   A N   1 
ATOM   2007 C CA  . ASP   A 1 266 ? 13.687  -28.685 79.274 1.00 94.72  ? 266 ASP   A CA  1 
ATOM   2008 C C   . ASP   A 1 266 ? 15.058  -28.106 78.945 1.00 96.27  ? 266 ASP   A C   1 
ATOM   2009 O O   . ASP   A 1 266 ? 15.968  -28.197 79.776 1.00 108.12 ? 266 ASP   A O   1 
ATOM   2010 C CB  . ASP   A 1 266 ? 13.725  -30.209 79.147 1.00 98.32  ? 266 ASP   A CB  1 
ATOM   2011 C CG  . ASP   A 1 266 ? 14.258  -30.670 77.804 1.00 103.90 ? 266 ASP   A CG  1 
ATOM   2012 O OD1 . ASP   A 1 266 ? 15.135  -31.558 77.782 1.00 124.60 ? 266 ASP   A OD1 1 
ATOM   2013 O OD2 . ASP   A 1 266 ? 13.807  -30.137 76.769 1.00 98.76  ? 266 ASP   A OD2 1 
ATOM   2014 N N   . SER   A 1 267 ? 15.232  -27.520 77.758 1.00 94.98  ? 267 SER   A N   1 
ATOM   2015 C CA  . SER   A 1 267 ? 16.518  -26.937 77.388 1.00 86.14  ? 267 SER   A CA  1 
ATOM   2016 C C   . SER   A 1 267 ? 16.869  -25.712 78.224 1.00 77.02  ? 267 SER   A C   1 
ATOM   2017 O O   . SER   A 1 267 ? 18.032  -25.298 78.232 1.00 73.41  ? 267 SER   A O   1 
ATOM   2018 C CB  . SER   A 1 267 ? 16.526  -26.571 75.902 1.00 80.69  ? 267 SER   A CB  1 
ATOM   2019 O OG  . SER   A 1 267 ? 15.573  -25.564 75.617 1.00 87.02  ? 267 SER   A OG  1 
ATOM   2020 N N   . GLY   A 1 268 ? 15.896  -25.116 78.908 1.00 84.02  ? 268 GLY   A N   1 
ATOM   2021 C CA  . GLY   A 1 268 ? 16.139  -23.928 79.698 1.00 86.15  ? 268 GLY   A CA  1 
ATOM   2022 C C   . GLY   A 1 268 ? 15.998  -22.624 78.950 1.00 76.11  ? 268 GLY   A C   1 
ATOM   2023 O O   . GLY   A 1 268 ? 16.300  -21.567 79.518 1.00 63.67  ? 268 GLY   A O   1 
ATOM   2024 N N   . VAL   A 1 269 ? 15.558  -22.664 77.691 1.00 84.67  ? 269 VAL   A N   1 
ATOM   2025 C CA  . VAL   A 1 269 ? 15.405  -21.452 76.900 1.00 71.78  ? 269 VAL   A CA  1 
ATOM   2026 C C   . VAL   A 1 269 ? 14.268  -20.600 77.458 1.00 76.24  ? 269 VAL   A C   1 
ATOM   2027 O O   . VAL   A 1 269 ? 13.279  -21.110 78.004 1.00 74.73  ? 269 VAL   A O   1 
ATOM   2028 C CB  . VAL   A 1 269 ? 15.166  -21.815 75.422 1.00 71.33  ? 269 VAL   A CB  1 
ATOM   2029 C CG1 . VAL   A 1 269 ? 13.857  -22.577 75.260 1.00 74.02  ? 269 VAL   A CG1 1 
ATOM   2030 C CG2 . VAL   A 1 269 ? 15.193  -20.576 74.536 1.00 84.91  ? 269 VAL   A CG2 1 
ATOM   2031 N N   . ARG   A 1 270 ? 14.413  -19.286 77.326 1.00 74.31  ? 270 ARG   A N   1 
ATOM   2032 C CA  . ARG   A 1 270 ? 13.374  -18.326 77.674 1.00 67.68  ? 270 ARG   A CA  1 
ATOM   2033 C C   . ARG   A 1 270 ? 12.898  -17.661 76.389 1.00 65.18  ? 270 ARG   A C   1 
ATOM   2034 O O   . ARG   A 1 270 ? 13.695  -17.042 75.675 1.00 60.67  ? 270 ARG   A O   1 
ATOM   2035 C CB  . ARG   A 1 270 ? 13.898  -17.289 78.667 1.00 68.35  ? 270 ARG   A CB  1 
ATOM   2036 C CG  . ARG   A 1 270 ? 12.813  -16.569 79.445 1.00 88.72  ? 270 ARG   A CG  1 
ATOM   2037 C CD  . ARG   A 1 270 ? 13.295  -15.216 79.944 1.00 84.56  ? 270 ARG   A CD  1 
ATOM   2038 N NE  . ARG   A 1 270 ? 12.185  -14.367 80.369 1.00 88.98  ? 270 ARG   A NE  1 
ATOM   2039 C CZ  . ARG   A 1 270 ? 12.314  -13.099 80.746 1.00 87.32  ? 270 ARG   A CZ  1 
ATOM   2040 N NH1 . ARG   A 1 270 ? 13.510  -12.525 80.755 1.00 83.91  ? 270 ARG   A NH1 1 
ATOM   2041 N NH2 . ARG   A 1 270 ? 11.247  -12.404 81.114 1.00 87.56  ? 270 ARG   A NH2 1 
ATOM   2042 N N   . ILE   A 1 271 ? 11.606  -17.792 76.096 1.00 63.13  ? 271 ILE   A N   1 
ATOM   2043 C CA  . ILE   A 1 271 ? 11.027  -17.341 74.836 1.00 49.81  ? 271 ILE   A CA  1 
ATOM   2044 C C   . ILE   A 1 271 ? 10.207  -16.085 75.093 1.00 56.31  ? 271 ILE   A C   1 
ATOM   2045 O O   . ILE   A 1 271 ? 9.382   -16.045 76.013 1.00 65.72  ? 271 ILE   A O   1 
ATOM   2046 C CB  . ILE   A 1 271 ? 10.167  -18.435 74.182 1.00 52.92  ? 271 ILE   A CB  1 
ATOM   2047 C CG1 . ILE   A 1 271 ? 10.976  -19.724 74.024 1.00 60.66  ? 271 ILE   A CG1 1 
ATOM   2048 C CG2 . ILE   A 1 271 ? 9.645   -17.964 72.838 1.00 50.65  ? 271 ILE   A CG2 1 
ATOM   2049 C CD1 . ILE   A 1 271 ? 10.181  -20.876 73.455 1.00 52.00  ? 271 ILE   A CD1 1 
ATOM   2050 N N   . ILE   A 1 272 ? 10.444  -15.060 74.276 1.00 63.46  ? 272 ILE   A N   1 
ATOM   2051 C CA  . ILE   A 1 272 ? 9.767   -13.776 74.365 1.00 57.73  ? 272 ILE   A CA  1 
ATOM   2052 C C   . ILE   A 1 272 ? 9.331   -13.357 72.966 1.00 57.16  ? 272 ILE   A C   1 
ATOM   2053 O O   . ILE   A 1 272 ? 9.741   -13.936 71.960 1.00 52.02  ? 272 ILE   A O   1 
ATOM   2054 C CB  . ILE   A 1 272 ? 10.667  -12.693 74.986 1.00 56.77  ? 272 ILE   A CB  1 
ATOM   2055 C CG1 . ILE   A 1 272 ? 11.823  -12.415 74.031 1.00 62.11  ? 272 ILE   A CG1 1 
ATOM   2056 C CG2 . ILE   A 1 272 ? 11.175  -13.121 76.355 1.00 52.88  ? 272 ILE   A CG2 1 
ATOM   2057 C CD1 . ILE   A 1 272 ? 12.700  -11.305 74.450 1.00 51.08  ? 272 ILE   A CD1 1 
ATOM   2058 N N   . ALA   A 1 273 ? 8.490   -12.326 72.918 1.00 62.75  ? 273 ALA   A N   1 
ATOM   2059 C CA  . ALA   A 1 273 ? 8.038   -11.740 71.665 1.00 48.45  ? 273 ALA   A CA  1 
ATOM   2060 C C   . ALA   A 1 273 ? 7.956   -10.229 71.823 1.00 52.34  ? 273 ALA   A C   1 
ATOM   2061 O O   . ALA   A 1 273 ? 8.043   -9.692  72.930 1.00 58.08  ? 273 ALA   A O   1 
ATOM   2062 C CB  . ALA   A 1 273 ? 6.684   -12.311 71.231 1.00 48.01  ? 273 ALA   A CB  1 
ATOM   2063 N N   . GLU   A 1 274 ? 7.785   -9.541  70.695 1.00 59.70  ? 274 GLU   A N   1 
ATOM   2064 C CA  . GLU   A 1 274 ? 7.676   -8.080  70.662 1.00 50.66  ? 274 GLU   A CA  1 
ATOM   2065 C C   . GLU   A 1 274 ? 6.420   -7.645  69.909 1.00 55.62  ? 274 GLU   A C   1 
ATOM   2066 O O   . GLU   A 1 274 ? 6.502   -6.918  68.915 1.00 58.83  ? 274 GLU   A O   1 
ATOM   2067 C CB  . GLU   A 1 274 ? 8.921   -7.462  70.028 1.00 66.04  ? 274 GLU   A CB  1 
ATOM   2068 C CG  . GLU   A 1 274 ? 10.233  -7.808  70.710 1.00 65.03  ? 274 GLU   A CG  1 
ATOM   2069 C CD  . GLU   A 1 274 ? 11.436  -7.542  69.819 1.00 90.01  ? 274 GLU   A CD  1 
ATOM   2070 O OE1 . GLU   A 1 274 ? 11.259  -7.438  68.587 1.00 92.39  ? 274 GLU   A OE1 1 
ATOM   2071 O OE2 . GLU   A 1 274 ? 12.558  -7.423  70.350 1.00 77.13  ? 274 GLU   A OE2 1 
ATOM   2072 N N   . PRO   A 1 275 ? 5.234   -8.075  70.347 1.00 60.18  ? 275 PRO   A N   1 
ATOM   2073 C CA  . PRO   A 1 275 ? 4.010   -7.697  69.622 1.00 58.78  ? 275 PRO   A CA  1 
ATOM   2074 C C   . PRO   A 1 275 ? 3.679   -6.229  69.854 1.00 54.24  ? 275 PRO   A C   1 
ATOM   2075 O O   . PRO   A 1 275 ? 3.514   -5.791  70.995 1.00 61.64  ? 275 PRO   A O   1 
ATOM   2076 C CB  . PRO   A 1 275 ? 2.946   -8.618  70.227 1.00 61.45  ? 275 PRO   A CB  1 
ATOM   2077 C CG  . PRO   A 1 275 ? 3.417   -8.821  71.632 1.00 46.37  ? 275 PRO   A CG  1 
ATOM   2078 C CD  . PRO   A 1 275 ? 4.926   -8.835  71.574 1.00 45.40  ? 275 PRO   A CD  1 
ATOM   2079 N N   . GLY   A 1 276 ? 3.601   -5.461  68.769 1.00 54.60  ? 276 GLY   A N   1 
ATOM   2080 C CA  . GLY   A 1 276 ? 3.126   -4.096  68.878 1.00 47.76  ? 276 GLY   A CA  1 
ATOM   2081 C C   . GLY   A 1 276 ? 1.660   -3.891  68.545 1.00 50.84  ? 276 GLY   A C   1 
ATOM   2082 O O   . GLY   A 1 276 ? 0.882   -3.433  69.385 1.00 61.69  ? 276 GLY   A O   1 
ATOM   2083 N N   . ARG   A 1 277 ? 1.262   -4.257  67.325 1.00 57.60  ? 277 ARG   A N   1 
ATOM   2084 C CA  . ARG   A 1 277 ? -0.086  -3.950  66.858 1.00 55.02  ? 277 ARG   A CA  1 
ATOM   2085 C C   . ARG   A 1 277 ? -1.134  -4.895  67.435 1.00 57.29  ? 277 ARG   A C   1 
ATOM   2086 O O   . ARG   A 1 277 ? -2.305  -4.515  67.546 1.00 59.65  ? 277 ARG   A O   1 
ATOM   2087 C CB  . ARG   A 1 277 ? -0.123  -3.969  65.327 1.00 44.38  ? 277 ARG   A CB  1 
ATOM   2088 C CG  . ARG   A 1 277 ? -0.057  -5.347  64.703 1.00 50.22  ? 277 ARG   A CG  1 
ATOM   2089 C CD  . ARG   A 1 277 ? -0.182  -5.281  63.187 1.00 50.61  ? 277 ARG   A CD  1 
ATOM   2090 N NE  . ARG   A 1 277 ? 0.998   -4.677  62.571 1.00 56.55  ? 277 ARG   A NE  1 
ATOM   2091 C CZ  . ARG   A 1 277 ? 0.986   -3.536  61.889 1.00 63.64  ? 277 ARG   A CZ  1 
ATOM   2092 N NH1 . ARG   A 1 277 ? 2.109   -3.062  61.368 1.00 65.94  ? 277 ARG   A NH1 1 
ATOM   2093 N NH2 . ARG   A 1 277 ? -0.149  -2.872  61.723 1.00 53.42  ? 277 ARG   A NH2 1 
ATOM   2094 N N   . TYR   A 1 278 ? -0.734  -6.117  67.799 1.00 55.52  ? 278 TYR   A N   1 
ATOM   2095 C CA  . TYR   A 1 278 ? -1.683  -7.095  68.322 1.00 53.27  ? 278 TYR   A CA  1 
ATOM   2096 C C   . TYR   A 1 278 ? -2.420  -6.565  69.548 1.00 57.72  ? 278 TYR   A C   1 
ATOM   2097 O O   . TYR   A 1 278 ? -3.620  -6.811  69.716 1.00 48.27  ? 278 TYR   A O   1 
ATOM   2098 C CB  . TYR   A 1 278 ? -0.955  -8.400  68.649 1.00 48.85  ? 278 TYR   A CB  1 
ATOM   2099 C CG  . TYR   A 1 278 ? -1.750  -9.342  69.520 1.00 52.32  ? 278 TYR   A CG  1 
ATOM   2100 C CD1 . TYR   A 1 278 ? -2.722  -10.168 68.975 1.00 50.71  ? 278 TYR   A CD1 1 
ATOM   2101 C CD2 . TYR   A 1 278 ? -1.520  -9.411  70.888 1.00 57.11  ? 278 TYR   A CD2 1 
ATOM   2102 C CE1 . TYR   A 1 278 ? -3.449  -11.029 69.767 1.00 49.75  ? 278 TYR   A CE1 1 
ATOM   2103 C CE2 . TYR   A 1 278 ? -2.242  -10.268 71.688 1.00 52.56  ? 278 TYR   A CE2 1 
ATOM   2104 C CZ  . TYR   A 1 278 ? -3.204  -11.075 71.122 1.00 55.64  ? 278 TYR   A CZ  1 
ATOM   2105 O OH  . TYR   A 1 278 ? -3.927  -11.933 71.916 1.00 73.49  ? 278 TYR   A OH  1 
ATOM   2106 N N   . TYR   A 1 279 ? -1.722  -5.825  70.409 1.00 59.95  ? 279 TYR   A N   1 
ATOM   2107 C CA  . TYR   A 1 279 ? -2.314  -5.402  71.671 1.00 51.81  ? 279 TYR   A CA  1 
ATOM   2108 C C   . TYR   A 1 279 ? -3.263  -4.220  71.515 1.00 54.13  ? 279 TYR   A C   1 
ATOM   2109 O O   . TYR   A 1 279 ? -4.230  -4.108  72.276 1.00 68.56  ? 279 TYR   A O   1 
ATOM   2110 C CB  . TYR   A 1 279 ? -1.216  -5.040  72.670 1.00 47.37  ? 279 TYR   A CB  1 
ATOM   2111 C CG  . TYR   A 1 279 ? -0.792  -6.184  73.559 1.00 46.77  ? 279 TYR   A CG  1 
ATOM   2112 C CD1 . TYR   A 1 279 ? -1.609  -6.623  74.591 1.00 64.18  ? 279 TYR   A CD1 1 
ATOM   2113 C CD2 . TYR   A 1 279 ? 0.428   -6.818  73.372 1.00 49.98  ? 279 TYR   A CD2 1 
ATOM   2114 C CE1 . TYR   A 1 279 ? -1.228  -7.665  75.409 1.00 58.71  ? 279 TYR   A CE1 1 
ATOM   2115 C CE2 . TYR   A 1 279 ? 0.819   -7.862  74.187 1.00 61.95  ? 279 TYR   A CE2 1 
ATOM   2116 C CZ  . TYR   A 1 279 ? -0.014  -8.281  75.203 1.00 47.83  ? 279 TYR   A CZ  1 
ATOM   2117 O OH  . TYR   A 1 279 ? 0.366   -9.320  76.020 1.00 68.59  ? 279 TYR   A OH  1 
ATOM   2118 N N   . VAL   A 1 280 ? -3.025  -3.344  70.544 1.00 45.01  ? 280 VAL   A N   1 
ATOM   2119 C CA  . VAL   A 1 280 ? -3.657  -2.032  70.545 1.00 46.71  ? 280 VAL   A CA  1 
ATOM   2120 C C   . VAL   A 1 280 ? -4.482  -1.746  69.299 1.00 43.96  ? 280 VAL   A C   1 
ATOM   2121 O O   . VAL   A 1 280 ? -5.274  -0.790  69.319 1.00 53.55  ? 280 VAL   A O   1 
ATOM   2122 C CB  . VAL   A 1 280 ? -2.608  -0.918  70.745 1.00 47.83  ? 280 VAL   A CB  1 
ATOM   2123 C CG1 . VAL   A 1 280 ? -1.869  -1.112  72.062 1.00 42.29  ? 280 VAL   A CG1 1 
ATOM   2124 C CG2 . VAL   A 1 280 ? -1.641  -0.893  69.576 1.00 44.16  ? 280 VAL   A CG2 1 
ATOM   2125 N N   . ALA   A 1 281 ? -4.330  -2.512  68.214 1.00 50.08  ? 281 ALA   A N   1 
ATOM   2126 C CA  . ALA   A 1 281 ? -4.967  -2.156  66.949 1.00 48.29  ? 281 ALA   A CA  1 
ATOM   2127 C C   . ALA   A 1 281 ? -6.469  -1.944  67.110 1.00 46.89  ? 281 ALA   A C   1 
ATOM   2128 O O   . ALA   A 1 281 ? -6.992  -0.865  66.815 1.00 48.15  ? 281 ALA   A O   1 
ATOM   2129 C CB  . ALA   A 1 281 ? -4.685  -3.237  65.906 1.00 43.19  ? 281 ALA   A CB  1 
ATOM   2130 N N   . SER   A 1 282 ? -7.173  -2.952  67.619 1.00 52.62  ? 282 SER   A N   1 
ATOM   2131 C CA  . SER   A 1 282 ? -8.625  -2.886  67.712 1.00 53.05  ? 282 SER   A CA  1 
ATOM   2132 C C   . SER   A 1 282 ? -9.117  -2.091  68.914 1.00 53.95  ? 282 SER   A C   1 
ATOM   2133 O O   . SER   A 1 282 ? -10.325 -1.853  69.022 1.00 59.15  ? 282 SER   A O   1 
ATOM   2134 C CB  . SER   A 1 282 ? -9.213  -4.299  67.763 1.00 64.42  ? 282 SER   A CB  1 
ATOM   2135 O OG  . SER   A 1 282 ? -8.695  -5.026  68.864 1.00 65.15  ? 282 SER   A OG  1 
ATOM   2136 N N   . ALA   A 1 283 ? -8.224  -1.679  69.817 1.00 63.40  ? 283 ALA   A N   1 
ATOM   2137 C CA  . ALA   A 1 283 ? -8.647  -0.960  71.013 1.00 49.58  ? 283 ALA   A CA  1 
ATOM   2138 C C   . ALA   A 1 283 ? -9.098  0.464   70.718 1.00 56.01  ? 283 ALA   A C   1 
ATOM   2139 O O   . ALA   A 1 283 ? -9.842  1.041   71.517 1.00 63.08  ? 283 ALA   A O   1 
ATOM   2140 C CB  . ALA   A 1 283 ? -7.513  -0.935  72.041 1.00 42.61  ? 283 ALA   A CB  1 
ATOM   2141 N N   . PHE   A 1 284 ? -8.663  1.044   69.604 1.00 52.40  ? 284 PHE   A N   1 
ATOM   2142 C CA  . PHE   A 1 284 ? -8.951  2.431   69.268 1.00 46.90  ? 284 PHE   A CA  1 
ATOM   2143 C C   . PHE   A 1 284 ? -9.935  2.492   68.110 1.00 56.37  ? 284 PHE   A C   1 
ATOM   2144 O O   . PHE   A 1 284 ? -9.754  1.806   67.098 1.00 54.90  ? 284 PHE   A O   1 
ATOM   2145 C CB  . PHE   A 1 284 ? -7.672  3.183   68.898 1.00 52.30  ? 284 PHE   A CB  1 
ATOM   2146 C CG  . PHE   A 1 284 ? -6.799  3.516   70.072 1.00 50.90  ? 284 PHE   A CG  1 
ATOM   2147 C CD1 . PHE   A 1 284 ? -6.177  2.516   70.801 1.00 54.30  ? 284 PHE   A CD1 1 
ATOM   2148 C CD2 . PHE   A 1 284 ? -6.587  4.836   70.436 1.00 46.76  ? 284 PHE   A CD2 1 
ATOM   2149 C CE1 . PHE   A 1 284 ? -5.368  2.825   71.879 1.00 52.59  ? 284 PHE   A CE1 1 
ATOM   2150 C CE2 . PHE   A 1 284 ? -5.778  5.150   71.510 1.00 61.56  ? 284 PHE   A CE2 1 
ATOM   2151 C CZ  . PHE   A 1 284 ? -5.168  4.143   72.234 1.00 51.59  ? 284 PHE   A CZ  1 
ATOM   2152 N N   . THR   A 1 285 ? -10.977 3.303   68.265 1.00 65.16  ? 285 THR   A N   1 
ATOM   2153 C CA  . THR   A 1 285 ? -11.872 3.639   67.167 1.00 39.38  ? 285 THR   A CA  1 
ATOM   2154 C C   . THR   A 1 285 ? -11.885 5.150   66.989 1.00 60.99  ? 285 THR   A C   1 
ATOM   2155 O O   . THR   A 1 285 ? -12.045 5.893   67.965 1.00 58.90  ? 285 THR   A O   1 
ATOM   2156 C CB  . THR   A 1 285 ? -13.284 3.111   67.412 1.00 49.37  ? 285 THR   A CB  1 
ATOM   2157 O OG1 . THR   A 1 285 ? -13.224 1.696   67.626 1.00 68.22  ? 285 THR   A OG1 1 
ATOM   2158 C CG2 . THR   A 1 285 ? -14.160 3.387   66.205 1.00 43.82  ? 285 THR   A CG2 1 
ATOM   2159 N N   . LEU   A 1 286 ? -11.717 5.598   65.748 1.00 53.41  ? 286 LEU   A N   1 
ATOM   2160 C CA  . LEU   A 1 286 ? -11.589 7.014   65.432 1.00 55.16  ? 286 LEU   A CA  1 
ATOM   2161 C C   . LEU   A 1 286 ? -12.891 7.536   64.839 1.00 55.08  ? 286 LEU   A C   1 
ATOM   2162 O O   . LEU   A 1 286 ? -13.491 6.886   63.977 1.00 54.94  ? 286 LEU   A O   1 
ATOM   2163 C CB  . LEU   A 1 286 ? -10.435 7.242   64.454 1.00 51.87  ? 286 LEU   A CB  1 
ATOM   2164 C CG  . LEU   A 1 286 ? -10.289 8.652   63.880 1.00 51.60  ? 286 LEU   A CG  1 
ATOM   2165 C CD1 . LEU   A 1 286 ? -9.968  9.651   64.984 1.00 50.15  ? 286 LEU   A CD1 1 
ATOM   2166 C CD2 . LEU   A 1 286 ? -9.228  8.683   62.791 1.00 47.55  ? 286 LEU   A CD2 1 
ATOM   2167 N N   . ALA   A 1 287 ? -13.330 8.700   65.310 1.00 46.18  ? 287 ALA   A N   1 
ATOM   2168 C CA  . ALA   A 1 287 ? -14.496 9.386   64.775 1.00 44.82  ? 287 ALA   A CA  1 
ATOM   2169 C C   . ALA   A 1 287 ? -14.036 10.705  64.175 1.00 56.67  ? 287 ALA   A C   1 
ATOM   2170 O O   . ALA   A 1 287 ? -13.431 11.529  64.872 1.00 54.14  ? 287 ALA   A O   1 
ATOM   2171 C CB  . ALA   A 1 287 ? -15.542 9.624   65.865 1.00 58.82  ? 287 ALA   A CB  1 
ATOM   2172 N N   . VAL   A 1 288 ? -14.318 10.900  62.888 1.00 47.76  ? 288 VAL   A N   1 
ATOM   2173 C CA  . VAL   A 1 288 ? -13.998 12.140  62.197 1.00 55.38  ? 288 VAL   A CA  1 
ATOM   2174 C C   . VAL   A 1 288 ? -15.299 12.769  61.724 1.00 59.85  ? 288 VAL   A C   1 
ATOM   2175 O O   . VAL   A 1 288 ? -16.294 12.079  61.489 1.00 59.02  ? 288 VAL   A O   1 
ATOM   2176 C CB  . VAL   A 1 288 ? -13.032 11.922  61.010 1.00 53.58  ? 288 VAL   A CB  1 
ATOM   2177 C CG1 . VAL   A 1 288 ? -11.722 11.331  61.497 1.00 54.19  ? 288 VAL   A CG1 1 
ATOM   2178 C CG2 . VAL   A 1 288 ? -13.667 11.021  59.961 1.00 54.82  ? 288 VAL   A CG2 1 
ATOM   2179 N N   . ASN   A 1 289 ? -15.294 14.092  61.604 1.00 58.45  ? 289 ASN   A N   1 
ATOM   2180 C CA  . ASN   A 1 289 ? -16.454 14.840  61.146 1.00 55.14  ? 289 ASN   A CA  1 
ATOM   2181 C C   . ASN   A 1 289 ? -16.243 15.302  59.712 1.00 60.91  ? 289 ASN   A C   1 
ATOM   2182 O O   . ASN   A 1 289 ? -15.149 15.743  59.347 1.00 62.45  ? 289 ASN   A O   1 
ATOM   2183 C CB  . ASN   A 1 289 ? -16.720 16.049  62.045 1.00 54.09  ? 289 ASN   A CB  1 
ATOM   2184 C CG  . ASN   A 1 289 ? -18.110 16.616  61.856 1.00 55.50  ? 289 ASN   A CG  1 
ATOM   2185 O OD1 . ASN   A 1 289 ? -18.287 17.667  61.239 1.00 68.20  ? 289 ASN   A OD1 1 
ATOM   2186 N ND2 . ASN   A 1 289 ? -19.109 15.918  62.381 1.00 60.05  ? 289 ASN   A ND2 1 
ATOM   2187 N N   . ILE   A 1 290 ? -17.297 15.212  58.905 1.00 52.69  ? 290 ILE   A N   1 
ATOM   2188 C CA  . ILE   A 1 290 ? -17.249 15.730  57.541 1.00 53.35  ? 290 ILE   A CA  1 
ATOM   2189 C C   . ILE   A 1 290 ? -17.310 17.252  57.619 1.00 54.05  ? 290 ILE   A C   1 
ATOM   2190 O O   . ILE   A 1 290 ? -18.345 17.819  57.977 1.00 58.22  ? 290 ILE   A O   1 
ATOM   2191 C CB  . ILE   A 1 290 ? -18.388 15.173  56.682 1.00 50.97  ? 290 ILE   A CB  1 
ATOM   2192 C CG1 . ILE   A 1 290 ? -18.251 13.662  56.530 1.00 45.78  ? 290 ILE   A CG1 1 
ATOM   2193 C CG2 . ILE   A 1 290 ? -18.401 15.843  55.313 1.00 50.31  ? 290 ILE   A CG2 1 
ATOM   2194 C CD1 . ILE   A 1 290 ? -19.414 13.041  55.815 1.00 60.44  ? 290 ILE   A CD1 1 
ATOM   2195 N N   . ILE   A 1 291 ? -16.198 17.916  57.307 1.00 53.05  ? 291 ILE   A N   1 
ATOM   2196 C CA  . ILE   A 1 291 ? -16.138 19.368  57.416 1.00 52.42  ? 291 ILE   A CA  1 
ATOM   2197 C C   . ILE   A 1 291 ? -16.414 20.073  56.092 1.00 51.20  ? 291 ILE   A C   1 
ATOM   2198 O O   . ILE   A 1 291 ? -16.728 21.273  56.102 1.00 57.81  ? 291 ILE   A O   1 
ATOM   2199 C CB  . ILE   A 1 291 ? -14.778 19.829  57.984 1.00 60.12  ? 291 ILE   A CB  1 
ATOM   2200 C CG1 . ILE   A 1 291 ? -13.633 19.398  57.066 1.00 55.25  ? 291 ILE   A CG1 1 
ATOM   2201 C CG2 . ILE   A 1 291 ? -14.574 19.275  59.385 1.00 58.81  ? 291 ILE   A CG2 1 
ATOM   2202 C CD1 . ILE   A 1 291 ? -12.313 20.065  57.381 1.00 51.70  ? 291 ILE   A CD1 1 
ATOM   2203 N N   . ALA   A 1 292 ? -16.310 19.377  54.962 1.00 60.13  ? 292 ALA   A N   1 
ATOM   2204 C CA  . ALA   A 1 292 ? -16.584 20.017  53.680 1.00 50.45  ? 292 ALA   A CA  1 
ATOM   2205 C C   . ALA   A 1 292 ? -17.098 18.987  52.685 1.00 49.57  ? 292 ALA   A C   1 
ATOM   2206 O O   . ALA   A 1 292 ? -16.914 17.780  52.857 1.00 50.61  ? 292 ALA   A O   1 
ATOM   2207 C CB  . ALA   A 1 292 ? -15.344 20.723  53.126 1.00 53.32  ? 292 ALA   A CB  1 
ATOM   2208 N N   . LYS   A 1 293 ? -17.710 19.484  51.613 1.00 46.16  ? 293 LYS   A N   1 
ATOM   2209 C CA  . LYS   A 1 293 ? -18.390 18.619  50.661 1.00 48.21  ? 293 LYS   A CA  1 
ATOM   2210 C C   . LYS   A 1 293 ? -18.437 19.285  49.293 1.00 49.26  ? 293 LYS   A C   1 
ATOM   2211 O O   . LYS   A 1 293 ? -18.745 20.475  49.180 1.00 59.31  ? 293 LYS   A O   1 
ATOM   2212 C CB  . LYS   A 1 293 ? -19.808 18.295  51.142 1.00 54.63  ? 293 LYS   A CB  1 
ATOM   2213 C CG  . LYS   A 1 293 ? -20.603 17.385  50.226 1.00 54.63  ? 293 LYS   A CG  1 
ATOM   2214 C CD  . LYS   A 1 293 ? -22.027 17.245  50.737 1.00 62.47  ? 293 LYS   A CD  1 
ATOM   2215 C CE  . LYS   A 1 293 ? -22.905 16.478  49.765 1.00 61.71  ? 293 LYS   A CE  1 
ATOM   2216 N NZ  . LYS   A 1 293 ? -24.313 16.388  50.245 1.00 55.27  ? 293 LYS   A NZ  1 
ATOM   2217 N N   . LYS   A 1 294 ? -18.129 18.508  48.259 1.00 44.90  ? 294 LYS   A N   1 
ATOM   2218 C CA  . LYS   A 1 294 ? -18.241 18.948  46.876 1.00 57.06  ? 294 LYS   A CA  1 
ATOM   2219 C C   . LYS   A 1 294 ? -18.977 17.885  46.079 1.00 55.56  ? 294 LYS   A C   1 
ATOM   2220 O O   . LYS   A 1 294 ? -18.781 16.687  46.299 1.00 54.63  ? 294 LYS   A O   1 
ATOM   2221 C CB  . LYS   A 1 294 ? -16.867 19.203  46.244 1.00 53.60  ? 294 LYS   A CB  1 
ATOM   2222 C CG  . LYS   A 1 294 ? -16.078 20.341  46.864 1.00 55.85  ? 294 LYS   A CG  1 
ATOM   2223 C CD  . LYS   A 1 294 ? -14.718 20.479  46.195 1.00 52.15  ? 294 LYS   A CD  1 
ATOM   2224 C CE  . LYS   A 1 294 ? -13.907 21.610  46.807 1.00 63.51  ? 294 LYS   A CE  1 
ATOM   2225 N NZ  . LYS   A 1 294 ? -12.549 21.715  46.202 1.00 65.68  ? 294 LYS   A NZ  1 
ATOM   2226 N N   . ILE   A 1 295 ? -19.825 18.324  45.154 1.00 67.17  ? 295 ILE   A N   1 
ATOM   2227 C CA  . ILE   A 1 295 ? -20.577 17.427  44.284 1.00 72.11  ? 295 ILE   A CA  1 
ATOM   2228 C C   . ILE   A 1 295 ? -20.076 17.603  42.856 1.00 66.95  ? 295 ILE   A C   1 
ATOM   2229 O O   . ILE   A 1 295 ? -20.037 18.725  42.335 1.00 74.74  ? 295 ILE   A O   1 
ATOM   2230 C CB  . ILE   A 1 295 ? -22.093 17.676  44.391 1.00 68.67  ? 295 ILE   A CB  1 
ATOM   2231 C CG1 . ILE   A 1 295 ? -22.849 16.796  43.393 1.00 80.70  ? 295 ILE   A CG1 1 
ATOM   2232 C CG2 . ILE   A 1 295 ? -22.432 19.157  44.219 1.00 58.64  ? 295 ILE   A CG2 1 
ATOM   2233 C CD1 . ILE   A 1 295 ? -24.349 16.876  43.532 1.00 90.74  ? 295 ILE   A CD1 1 
ATOM   2234 N N   . VAL   A 1 296 ? -19.674 16.499  42.233 1.00 72.93  ? 296 VAL   A N   1 
ATOM   2235 C CA  . VAL   A 1 296 ? -19.148 16.492  40.874 1.00 77.20  ? 296 VAL   A CA  1 
ATOM   2236 C C   . VAL   A 1 296 ? -20.064 15.634  40.012 1.00 78.62  ? 296 VAL   A C   1 
ATOM   2237 O O   . VAL   A 1 296 ? -20.343 14.478  40.351 1.00 87.06  ? 296 VAL   A O   1 
ATOM   2238 C CB  . VAL   A 1 296 ? -17.702 15.964  40.829 1.00 75.97  ? 296 VAL   A CB  1 
ATOM   2239 C CG1 . VAL   A 1 296 ? -17.141 16.076  39.422 1.00 78.82  ? 296 VAL   A CG1 1 
ATOM   2240 C CG2 . VAL   A 1 296 ? -16.831 16.719  41.819 1.00 69.48  ? 296 VAL   A CG2 1 
ATOM   2241 N N   . LEU   A 1 297 ? -20.524 16.193  38.897 1.00 80.52  ? 297 LEU   A N   1 
ATOM   2242 C CA  . LEU   A 1 297 ? -21.397 15.466  37.987 1.00 82.83  ? 297 LEU   A CA  1 
ATOM   2243 C C   . LEU   A 1 297 ? -20.555 14.773  36.925 1.00 86.65  ? 297 LEU   A C   1 
ATOM   2244 O O   . LEU   A 1 297 ? -19.702 15.402  36.291 1.00 93.96  ? 297 LEU   A O   1 
ATOM   2245 C CB  . LEU   A 1 297 ? -22.406 16.413  37.337 1.00 74.06  ? 297 LEU   A CB  1 
ATOM   2246 C CG  . LEU   A 1 297 ? -23.410 17.075  38.286 1.00 95.18  ? 297 LEU   A CG  1 
ATOM   2247 C CD1 . LEU   A 1 297 ? -24.245 18.113  37.555 1.00 88.11  ? 297 LEU   A CD1 1 
ATOM   2248 C CD2 . LEU   A 1 297 ? -24.304 16.036  38.943 1.00 88.46  ? 297 LEU   A CD2 1 
ATOM   2249 N N   . LYS   A 1 298 ? -20.794 13.479  36.736 1.00 96.19  ? 298 LYS   A N   1 
ATOM   2250 C CA  . LYS   A 1 298 ? -20.053 12.713  35.742 1.00 99.53  ? 298 LYS   A CA  1 
ATOM   2251 C C   . LYS   A 1 298 ? -20.936 12.359  34.550 1.00 107.81 ? 298 LYS   A C   1 
ATOM   2252 O O   . LYS   A 1 298 ? -20.805 12.943  33.474 1.00 97.96  ? 298 LYS   A O   1 
ATOM   2253 C CB  . LYS   A 1 298 ? -19.469 11.443  36.363 1.00 96.72  ? 298 LYS   A CB  1 
ATOM   2254 C CG  . LYS   A 1 298 ? -18.217 10.945  35.660 1.00 98.05  ? 298 LYS   A CG  1 
ATOM   2255 C CD  . LYS   A 1 298 ? -17.758 9.608   36.213 1.00 117.56 ? 298 LYS   A CD  1 
ATOM   2256 C CE  . LYS   A 1 298 ? -18.769 8.514   35.928 1.00 124.07 ? 298 LYS   A CE  1 
ATOM   2257 N NZ  . LYS   A 1 298 ? -18.159 7.158   36.014 1.00 129.97 ? 298 LYS   A NZ  1 
ATOM   2258 N N   . GLU   A 1 311 ? -24.764 11.324  36.546 1.00 115.90 ? 311 GLU   A N   1 
ATOM   2259 C CA  . GLU   A 1 311 ? -24.376 10.573  37.735 1.00 111.11 ? 311 GLU   A CA  1 
ATOM   2260 C C   . GLU   A 1 311 ? -23.629 11.455  38.730 1.00 103.78 ? 311 GLU   A C   1 
ATOM   2261 O O   . GLU   A 1 311 ? -22.632 12.090  38.389 1.00 89.88  ? 311 GLU   A O   1 
ATOM   2262 C CB  . GLU   A 1 311 ? -23.516 9.367   37.355 1.00 107.24 ? 311 GLU   A CB  1 
ATOM   2263 C CG  . GLU   A 1 311 ? -22.870 8.675   38.545 1.00 115.32 ? 311 GLU   A CG  1 
ATOM   2264 C CD  . GLU   A 1 311 ? -21.797 7.689   38.132 1.00 131.93 ? 311 GLU   A CD  1 
ATOM   2265 O OE1 . GLU   A 1 311 ? -21.586 7.519   36.914 1.00 142.31 ? 311 GLU   A OE1 1 
ATOM   2266 O OE2 . GLU   A 1 311 ? -21.164 7.087   39.025 1.00 131.87 ? 311 GLU   A OE2 1 
ATOM   2267 N N   . GLN   A 1 312 ? -24.127 11.486  39.963 1.00 94.86  ? 312 GLN   A N   1 
ATOM   2268 C CA  . GLN   A 1 312 ? -23.573 12.326  41.016 1.00 89.84  ? 312 GLN   A CA  1 
ATOM   2269 C C   . GLN   A 1 312 ? -22.470 11.582  41.758 1.00 87.10  ? 312 GLN   A C   1 
ATOM   2270 O O   . GLN   A 1 312 ? -22.660 10.435  42.176 1.00 98.55  ? 312 GLN   A O   1 
ATOM   2271 C CB  . GLN   A 1 312 ? -24.668 12.743  41.999 1.00 97.40  ? 312 GLN   A CB  1 
ATOM   2272 C CG  . GLN   A 1 312 ? -25.668 13.752  41.458 1.00 95.50  ? 312 GLN   A CG  1 
ATOM   2273 C CD  . GLN   A 1 312 ? -26.654 14.216  42.516 1.00 106.32 ? 312 GLN   A CD  1 
ATOM   2274 O OE1 . GLN   A 1 312 ? -27.001 15.395  42.585 1.00 105.99 ? 312 GLN   A OE1 1 
ATOM   2275 N NE2 . GLN   A 1 312 ? -27.110 13.286  43.349 1.00 98.77  ? 312 GLN   A NE2 1 
ATOM   2276 N N   . THR   A 1 313 ? -21.317 12.230  41.915 1.00 78.28  ? 313 THR   A N   1 
ATOM   2277 C CA  . THR   A 1 313 ? -20.241 11.739  42.757 1.00 80.71  ? 313 THR   A CA  1 
ATOM   2278 C C   . THR   A 1 313 ? -19.898 12.815  43.778 1.00 70.84  ? 313 THR   A C   1 
ATOM   2279 O O   . THR   A 1 313 ? -20.190 13.997  43.582 1.00 70.77  ? 313 THR   A O   1 
ATOM   2280 C CB  . THR   A 1 313 ? -19.002 11.372  41.930 1.00 60.77  ? 313 THR   A CB  1 
ATOM   2281 O OG1 . THR   A 1 313 ? -18.456 12.556  41.337 1.00 69.13  ? 313 THR   A OG1 1 
ATOM   2282 C CG2 . THR   A 1 313 ? -19.365 10.382  40.837 1.00 71.87  ? 313 THR   A CG2 1 
ATOM   2283 N N   . PHE   A 1 314 ? -19.273 12.406  44.877 1.00 68.18  ? 314 PHE   A N   1 
ATOM   2284 C CA  . PHE   A 1 314 ? -19.059 13.316  45.991 1.00 64.65  ? 314 PHE   A CA  1 
ATOM   2285 C C   . PHE   A 1 314 ? -17.616 13.271  46.467 1.00 60.95  ? 314 PHE   A C   1 
ATOM   2286 O O   . PHE   A 1 314 ? -16.975 12.217  46.456 1.00 59.40  ? 314 PHE   A O   1 
ATOM   2287 C CB  . PHE   A 1 314 ? -20.000 12.987  47.149 1.00 58.06  ? 314 PHE   A CB  1 
ATOM   2288 C CG  . PHE   A 1 314 ? -21.444 13.234  46.837 1.00 61.92  ? 314 PHE   A CG  1 
ATOM   2289 C CD1 . PHE   A 1 314 ? -21.994 14.493  47.004 1.00 61.44  ? 314 PHE   A CD1 1 
ATOM   2290 C CD2 . PHE   A 1 314 ? -22.251 12.212  46.369 1.00 74.67  ? 314 PHE   A CD2 1 
ATOM   2291 C CE1 . PHE   A 1 314 ? -23.323 14.727  46.715 1.00 65.05  ? 314 PHE   A CE1 1 
ATOM   2292 C CE2 . PHE   A 1 314 ? -23.581 12.439  46.078 1.00 76.80  ? 314 PHE   A CE2 1 
ATOM   2293 C CZ  . PHE   A 1 314 ? -24.118 13.699  46.252 1.00 71.66  ? 314 PHE   A CZ  1 
ATOM   2294 N N   . MET   A 1 315 ? -17.115 14.431  46.880 1.00 47.36  ? 315 MET   A N   1 
ATOM   2295 C CA  . MET   A 1 315 ? -15.835 14.557  47.558 1.00 58.72  ? 315 MET   A CA  1 
ATOM   2296 C C   . MET   A 1 315 ? -16.113 15.066  48.962 1.00 53.33  ? 315 MET   A C   1 
ATOM   2297 O O   . MET   A 1 315 ? -16.671 16.156  49.130 1.00 61.00  ? 315 MET   A O   1 
ATOM   2298 C CB  . MET   A 1 315 ? -14.899 15.514  46.818 1.00 64.96  ? 315 MET   A CB  1 
ATOM   2299 C CG  . MET   A 1 315 ? -14.624 15.146  45.373 1.00 56.90  ? 315 MET   A CG  1 
ATOM   2300 S SD  . MET   A 1 315 ? -13.718 16.455  44.525 1.00 79.01  ? 315 MET   A SD  1 
ATOM   2301 C CE  . MET   A 1 315 ? -12.153 16.404  45.395 1.00 69.77  ? 315 MET   A CE  1 
ATOM   2302 N N   . TYR   A 1 316 ? -15.737 14.280  49.963 1.00 49.38  ? 316 TYR   A N   1 
ATOM   2303 C CA  . TYR   A 1 316 ? -15.941 14.643  51.357 1.00 55.22  ? 316 TYR   A CA  1 
ATOM   2304 C C   . TYR   A 1 316 ? -14.602 14.983  51.992 1.00 52.44  ? 316 TYR   A C   1 
ATOM   2305 O O   . TYR   A 1 316 ? -13.628 14.239  51.837 1.00 55.62  ? 316 TYR   A O   1 
ATOM   2306 C CB  . TYR   A 1 316 ? -16.622 13.510  52.125 1.00 50.19  ? 316 TYR   A CB  1 
ATOM   2307 C CG  . TYR   A 1 316 ? -17.961 13.102  51.554 1.00 49.58  ? 316 TYR   A CG  1 
ATOM   2308 C CD1 . TYR   A 1 316 ? -19.069 13.934  51.663 1.00 54.66  ? 316 TYR   A CD1 1 
ATOM   2309 C CD2 . TYR   A 1 316 ? -18.119 11.883  50.910 1.00 56.83  ? 316 TYR   A CD2 1 
ATOM   2310 C CE1 . TYR   A 1 316 ? -20.296 13.561  51.143 1.00 54.32  ? 316 TYR   A CE1 1 
ATOM   2311 C CE2 . TYR   A 1 316 ? -19.339 11.503  50.390 1.00 65.61  ? 316 TYR   A CE2 1 
ATOM   2312 C CZ  . TYR   A 1 316 ? -20.423 12.343  50.508 1.00 56.81  ? 316 TYR   A CZ  1 
ATOM   2313 O OH  . TYR   A 1 316 ? -21.636 11.957  49.985 1.00 60.10  ? 316 TYR   A OH  1 
ATOM   2314 N N   . TYR   A 1 317 ? -14.557 16.105  52.700 1.00 47.53  ? 317 TYR   A N   1 
ATOM   2315 C CA  . TYR   A 1 317 ? -13.376 16.539  53.429 1.00 44.94  ? 317 TYR   A CA  1 
ATOM   2316 C C   . TYR   A 1 317 ? -13.668 16.389  54.913 1.00 50.03  ? 317 TYR   A C   1 
ATOM   2317 O O   . TYR   A 1 317 ? -14.633 16.977  55.417 1.00 55.71  ? 317 TYR   A O   1 
ATOM   2318 C CB  . TYR   A 1 317 ? -13.019 17.990  53.105 1.00 54.09  ? 317 TYR   A CB  1 
ATOM   2319 C CG  . TYR   A 1 317 ? -12.745 18.268  51.645 1.00 61.65  ? 317 TYR   A CG  1 
ATOM   2320 C CD1 . TYR   A 1 317 ? -13.783 18.355  50.725 1.00 64.12  ? 317 TYR   A CD1 1 
ATOM   2321 C CD2 . TYR   A 1 317 ? -11.448 18.459  51.187 1.00 49.37  ? 317 TYR   A CD2 1 
ATOM   2322 C CE1 . TYR   A 1 317 ? -13.537 18.612  49.390 1.00 68.92  ? 317 TYR   A CE1 1 
ATOM   2323 C CE2 . TYR   A 1 317 ? -11.193 18.719  49.854 1.00 65.97  ? 317 TYR   A CE2 1 
ATOM   2324 C CZ  . TYR   A 1 317 ? -12.240 18.794  48.959 1.00 68.68  ? 317 TYR   A CZ  1 
ATOM   2325 O OH  . TYR   A 1 317 ? -11.992 19.052  47.630 1.00 76.48  ? 317 TYR   A OH  1 
ATOM   2326 N N   . VAL   A 1 318 ? -12.837 15.612  55.598 1.00 55.76  ? 318 VAL   A N   1 
ATOM   2327 C CA  . VAL   A 1 318 ? -12.985 15.354  57.021 1.00 53.09  ? 318 VAL   A CA  1 
ATOM   2328 C C   . VAL   A 1 318 ? -11.793 15.973  57.745 1.00 45.89  ? 318 VAL   A C   1 
ATOM   2329 O O   . VAL   A 1 318 ? -10.823 16.410  57.128 1.00 60.12  ? 318 VAL   A O   1 
ATOM   2330 C CB  . VAL   A 1 318 ? -13.110 13.850  57.326 1.00 56.37  ? 318 VAL   A CB  1 
ATOM   2331 C CG1 . VAL   A 1 318 ? -14.344 13.279  56.652 1.00 59.39  ? 318 VAL   A CG1 1 
ATOM   2332 C CG2 . VAL   A 1 318 ? -11.872 13.117  56.864 1.00 41.36  ? 318 VAL   A CG2 1 
ATOM   2333 N N   . ASN   A 1 319 ? -11.878 16.017  59.076 1.00 47.09  ? 319 ASN   A N   1 
ATOM   2334 C CA  . ASN   A 1 319 ? -10.925 16.764  59.890 1.00 52.79  ? 319 ASN   A CA  1 
ATOM   2335 C C   . ASN   A 1 319 ? -9.787  15.893  60.419 1.00 52.24  ? 319 ASN   A C   1 
ATOM   2336 O O   . ASN   A 1 319 ? -9.259  16.153  61.505 1.00 49.33  ? 319 ASN   A O   1 
ATOM   2337 C CB  . ASN   A 1 319 ? -11.645 17.470  61.041 1.00 56.00  ? 319 ASN   A CB  1 
ATOM   2338 C CG  . ASN   A 1 319 ? -12.602 16.558  61.787 1.00 51.30  ? 319 ASN   A CG  1 
ATOM   2339 O OD1 . ASN   A 1 319 ? -12.618 15.345  61.578 1.00 57.15  ? 319 ASN   A OD1 1 
ATOM   2340 N ND2 . ASN   A 1 319 ? -13.413 17.144  62.662 1.00 45.33  ? 319 ASN   A ND2 1 
ATOM   2341 N N   . ASP   A 1 320 ? -9.391  14.869  59.667 1.00 63.41  ? 320 ASP   A N   1 
ATOM   2342 C CA  . ASP   A 1 320 ? -8.135  14.173  59.907 1.00 58.98  ? 320 ASP   A CA  1 
ATOM   2343 C C   . ASP   A 1 320 ? -7.622  13.643  58.575 1.00 57.44  ? 320 ASP   A C   1 
ATOM   2344 O O   . ASP   A 1 320 ? -8.408  13.318  57.681 1.00 55.91  ? 320 ASP   A O   1 
ATOM   2345 C CB  . ASP   A 1 320 ? -8.298  13.038  60.925 1.00 55.55  ? 320 ASP   A CB  1 
ATOM   2346 C CG  . ASP   A 1 320 ? -7.003  12.714  61.646 1.00 80.56  ? 320 ASP   A CG  1 
ATOM   2347 O OD1 . ASP   A 1 320 ? -5.935  13.184  61.198 1.00 75.30  ? 320 ASP   A OD1 1 
ATOM   2348 O OD2 . ASP   A 1 320 ? -7.054  11.993  62.664 1.00 77.85  ? 320 ASP   A OD2 1 
ATOM   2349 N N   . GLY   A 1 321 ? -6.300  13.563  58.443 1.00 58.13  ? 321 GLY   A N   1 
ATOM   2350 C CA  . GLY   A 1 321 ? -5.717  13.226  57.157 1.00 62.61  ? 321 GLY   A CA  1 
ATOM   2351 C C   . GLY   A 1 321 ? -4.394  12.491  57.206 1.00 50.69  ? 321 GLY   A C   1 
ATOM   2352 O O   . GLY   A 1 321 ? -3.987  11.993  58.259 1.00 54.66  ? 321 GLY   A O   1 
ATOM   2353 N N   . VAL   A 1 322 ? -3.713  12.416  56.058 1.00 63.04  ? 322 VAL   A N   1 
ATOM   2354 C CA  . VAL   A 1 322 ? -2.481  11.641  55.958 1.00 55.95  ? 322 VAL   A CA  1 
ATOM   2355 C C   . VAL   A 1 322 ? -1.344  12.256  56.765 1.00 47.23  ? 322 VAL   A C   1 
ATOM   2356 O O   . VAL   A 1 322 ? -0.367  11.567  57.070 1.00 48.62  ? 322 VAL   A O   1 
ATOM   2357 C CB  . VAL   A 1 322 ? -2.061  11.471  54.486 1.00 51.32  ? 322 VAL   A CB  1 
ATOM   2358 C CG1 . VAL   A 1 322 ? -3.172  10.799  53.692 1.00 40.94  ? 322 VAL   A CG1 1 
ATOM   2359 C CG2 . VAL   A 1 322 ? -1.692  12.814  53.878 1.00 62.08  ? 322 VAL   A CG2 1 
ATOM   2360 N N   . TYR   A 1 323 ? -1.424  13.543  57.099 1.00 44.79  ? 323 TYR   A N   1 
ATOM   2361 C CA  . TYR   A 1 323 ? -0.448  14.122  58.010 1.00 42.62  ? 323 TYR   A CA  1 
ATOM   2362 C C   . TYR   A 1 323 ? -0.777  13.824  59.464 1.00 53.38  ? 323 TYR   A C   1 
ATOM   2363 O O   . TYR   A 1 323 ? 0.089   13.982  60.331 1.00 49.21  ? 323 TYR   A O   1 
ATOM   2364 C CB  . TYR   A 1 323 ? -0.347  15.632  57.791 1.00 40.96  ? 323 TYR   A CB  1 
ATOM   2365 C CG  . TYR   A 1 323 ? 0.282   16.005  56.468 1.00 45.23  ? 323 TYR   A CG  1 
ATOM   2366 C CD1 . TYR   A 1 323 ? -0.500  16.239  55.343 1.00 61.50  ? 323 TYR   A CD1 1 
ATOM   2367 C CD2 . TYR   A 1 323 ? 1.660   16.106  56.340 1.00 56.96  ? 323 TYR   A CD2 1 
ATOM   2368 C CE1 . TYR   A 1 323 ? 0.078   16.576  54.128 1.00 72.81  ? 323 TYR   A CE1 1 
ATOM   2369 C CE2 . TYR   A 1 323 ? 2.246   16.441  55.133 1.00 61.37  ? 323 TYR   A CE2 1 
ATOM   2370 C CZ  . TYR   A 1 323 ? 1.452   16.675  54.030 1.00 66.98  ? 323 TYR   A CZ  1 
ATOM   2371 O OH  . TYR   A 1 323 ? 2.039   17.009  52.830 1.00 78.37  ? 323 TYR   A OH  1 
ATOM   2372 N N   . GLY   A 1 324 ? -2.007  13.407  59.745 1.00 55.24  ? 324 GLY   A N   1 
ATOM   2373 C CA  . GLY   A 1 324 ? -2.398  13.028  61.085 1.00 49.68  ? 324 GLY   A CA  1 
ATOM   2374 C C   . GLY   A 1 324 ? -2.457  11.529  61.285 1.00 49.44  ? 324 GLY   A C   1 
ATOM   2375 O O   . GLY   A 1 324 ? -1.477  10.818  61.045 1.00 61.32  ? 324 GLY   A O   1 
ATOM   2376 N N   . SER   A 1 325 ? -3.617  11.040  61.724 1.00 49.03  ? 325 SER   A N   1 
ATOM   2377 C CA  . SER   A 1 325 ? -3.759  9.628   62.059 1.00 56.44  ? 325 SER   A CA  1 
ATOM   2378 C C   . SER   A 1 325 ? -3.607  8.723   60.846 1.00 44.57  ? 325 SER   A C   1 
ATOM   2379 O O   . SER   A 1 325 ? -3.180  7.573   60.989 1.00 57.05  ? 325 SER   A O   1 
ATOM   2380 C CB  . SER   A 1 325 ? -5.114  9.382   62.717 1.00 63.49  ? 325 SER   A CB  1 
ATOM   2381 O OG  . SER   A 1 325 ? -5.257  10.161  63.891 1.00 70.94  ? 325 SER   A OG  1 
ATOM   2382 N N   . PHE   A 1 326 ? -3.956  9.204   59.656 1.00 52.39  ? 326 PHE   A N   1 
ATOM   2383 C CA  . PHE   A 1 326 ? -3.958  8.361   58.470 1.00 55.14  ? 326 PHE   A CA  1 
ATOM   2384 C C   . PHE   A 1 326 ? -2.602  8.294   57.778 1.00 55.78  ? 326 PHE   A C   1 
ATOM   2385 O O   . PHE   A 1 326 ? -2.524  7.821   56.636 1.00 52.38  ? 326 PHE   A O   1 
ATOM   2386 C CB  . PHE   A 1 326 ? -5.038  8.822   57.493 1.00 50.78  ? 326 PHE   A CB  1 
ATOM   2387 C CG  . PHE   A 1 326 ? -6.433  8.579   57.986 1.00 51.99  ? 326 PHE   A CG  1 
ATOM   2388 C CD1 . PHE   A 1 326 ? -7.002  7.319   57.894 1.00 51.90  ? 326 PHE   A CD1 1 
ATOM   2389 C CD2 . PHE   A 1 326 ? -7.170  9.602   58.552 1.00 52.15  ? 326 PHE   A CD2 1 
ATOM   2390 C CE1 . PHE   A 1 326 ? -8.283  7.090   58.349 1.00 54.45  ? 326 PHE   A CE1 1 
ATOM   2391 C CE2 . PHE   A 1 326 ? -8.448  9.380   59.008 1.00 54.42  ? 326 PHE   A CE2 1 
ATOM   2392 C CZ  . PHE   A 1 326 ? -9.007  8.122   58.907 1.00 57.25  ? 326 PHE   A CZ  1 
ATOM   2393 N N   . ASN   A 1 327 ? -1.528  8.716   58.454 1.00 53.15  ? 327 ASN   A N   1 
ATOM   2394 C CA  . ASN   A 1 327 ? -0.201  8.552   57.874 1.00 53.92  ? 327 ASN   A CA  1 
ATOM   2395 C C   . ASN   A 1 327 ? 0.126   7.084   57.666 1.00 57.52  ? 327 ASN   A C   1 
ATOM   2396 O O   . ASN   A 1 327 ? 1.019   6.758   56.873 1.00 57.28  ? 327 ASN   A O   1 
ATOM   2397 C CB  . ASN   A 1 327 ? 0.844   9.211   58.778 1.00 49.16  ? 327 ASN   A CB  1 
ATOM   2398 C CG  . ASN   A 1 327 ? 0.854   8.622   60.173 1.00 60.60  ? 327 ASN   A CG  1 
ATOM   2399 O OD1 . ASN   A 1 327 ? 1.373   7.529   60.396 1.00 59.38  ? 327 ASN   A OD1 1 
ATOM   2400 N ND2 . ASN   A 1 327 ? 0.257   9.337   61.118 1.00 68.38  ? 327 ASN   A ND2 1 
ATOM   2401 N N   . CYS   A 1 328 ? -0.647  6.201   58.302 1.00 64.13  ? 328 CYS   A N   1 
ATOM   2402 C CA  . CYS   A 1 328 ? -0.459  4.766   58.160 1.00 74.91  ? 328 CYS   A CA  1 
ATOM   2403 C C   . CYS   A 1 328 ? -0.723  4.336   56.728 1.00 68.55  ? 328 CYS   A C   1 
ATOM   2404 O O   . CYS   A 1 328 ? -0.210  3.303   56.283 1.00 82.76  ? 328 CYS   A O   1 
ATOM   2405 C CB  . CYS   A 1 328 ? -1.373  4.021   59.136 1.00 77.29  ? 328 CYS   A CB  1 
ATOM   2406 S SG  . CYS   A 1 328 ? -3.131  4.419   58.945 1.00 77.68  ? 328 CYS   A SG  1 
ATOM   2407 N N   . ILE   A 1 329 ? -1.537  5.107   56.001 1.00 70.45  ? 329 ILE   A N   1 
ATOM   2408 C CA  . ILE   A 1 329 ? -1.803  4.806   54.598 1.00 77.25  ? 329 ILE   A CA  1 
ATOM   2409 C C   . ILE   A 1 329 ? -0.504  4.813   53.804 1.00 75.21  ? 329 ILE   A C   1 
ATOM   2410 O O   . ILE   A 1 329 ? -0.319  4.003   52.889 1.00 90.47  ? 329 ILE   A O   1 
ATOM   2411 C CB  . ILE   A 1 329 ? -2.830  5.806   54.027 1.00 74.41  ? 329 ILE   A CB  1 
ATOM   2412 C CG1 . ILE   A 1 329 ? -4.151  5.727   54.799 1.00 64.54  ? 329 ILE   A CG1 1 
ATOM   2413 C CG2 . ILE   A 1 329 ? -3.068  5.569   52.541 1.00 58.19  ? 329 ILE   A CG2 1 
ATOM   2414 C CD1 . ILE   A 1 329 ? -5.191  6.721   54.315 1.00 69.17  ? 329 ILE   A CD1 1 
ATOM   2415 N N   . LEU   A 1 330 ? 0.407   5.735   54.128 1.00 67.82  ? 330 LEU   A N   1 
ATOM   2416 C CA  . LEU   A 1 330 ? 1.688   5.788   53.424 1.00 78.42  ? 330 LEU   A CA  1 
ATOM   2417 C C   . LEU   A 1 330 ? 2.791   5.004   54.136 1.00 75.46  ? 330 LEU   A C   1 
ATOM   2418 O O   . LEU   A 1 330 ? 3.456   4.169   53.517 1.00 69.52  ? 330 LEU   A O   1 
ATOM   2419 C CB  . LEU   A 1 330 ? 2.119   7.242   53.239 1.00 56.69  ? 330 LEU   A CB  1 
ATOM   2420 C CG  . LEU   A 1 330 ? 1.128   8.145   52.510 1.00 69.82  ? 330 LEU   A CG  1 
ATOM   2421 C CD1 . LEU   A 1 330 ? 1.538   9.597   52.638 1.00 64.58  ? 330 LEU   A CD1 1 
ATOM   2422 C CD2 . LEU   A 1 330 ? 1.019   7.749   51.045 1.00 73.76  ? 330 LEU   A CD2 1 
ATOM   2423 N N   . TYR   A 1 331 ? 2.981   5.256   55.435 1.00 73.58  ? 331 TYR   A N   1 
ATOM   2424 C CA  . TYR   A 1 331 ? 4.083   4.638   56.170 1.00 72.55  ? 331 TYR   A CA  1 
ATOM   2425 C C   . TYR   A 1 331 ? 3.880   3.136   56.354 1.00 90.69  ? 331 TYR   A C   1 
ATOM   2426 O O   . TYR   A 1 331 ? 4.811   2.350   56.139 1.00 115.80 ? 331 TYR   A O   1 
ATOM   2427 C CB  . TYR   A 1 331 ? 4.266   5.334   57.521 1.00 73.33  ? 331 TYR   A CB  1 
ATOM   2428 C CG  . TYR   A 1 331 ? 4.927   6.697   57.424 1.00 71.61  ? 331 TYR   A CG  1 
ATOM   2429 C CD1 . TYR   A 1 331 ? 6.220   6.826   56.930 1.00 65.67  ? 331 TYR   A CD1 1 
ATOM   2430 C CD2 . TYR   A 1 331 ? 4.249   7.856   57.787 1.00 68.44  ? 331 TYR   A CD2 1 
ATOM   2431 C CE1 . TYR   A 1 331 ? 6.831   8.061   56.836 1.00 58.17  ? 331 TYR   A CE1 1 
ATOM   2432 C CE2 . TYR   A 1 331 ? 4.853   9.098   57.685 1.00 70.80  ? 331 TYR   A CE2 1 
ATOM   2433 C CZ  . TYR   A 1 331 ? 6.142   9.193   57.207 1.00 60.65  ? 331 TYR   A CZ  1 
ATOM   2434 O OH  . TYR   A 1 331 ? 6.742   10.426  57.107 1.00 67.84  ? 331 TYR   A OH  1 
ATOM   2435 N N   . ASP   A 1 332 ? 2.683   2.712   56.756 1.00 85.43  ? 332 ASP   A N   1 
ATOM   2436 C CA  . ASP   A 1 332 ? 2.413   1.296   56.976 1.00 93.63  ? 332 ASP   A CA  1 
ATOM   2437 C C   . ASP   A 1 332 ? 1.637   0.695   55.813 1.00 102.02 ? 332 ASP   A C   1 
ATOM   2438 O O   . ASP   A 1 332 ? 1.428   -0.521  55.773 1.00 112.84 ? 332 ASP   A O   1 
ATOM   2439 C CB  . ASP   A 1 332 ? 1.645   1.103   58.300 1.00 96.45  ? 332 ASP   A CB  1 
ATOM   2440 C CG  . ASP   A 1 332 ? 1.362   -0.362  58.620 1.00 110.48 ? 332 ASP   A CG  1 
ATOM   2441 O OD1 . ASP   A 1 332 ? 2.330   -1.117  58.853 1.00 110.18 ? 332 ASP   A OD1 1 
ATOM   2442 O OD2 . ASP   A 1 332 ? 0.177   -0.757  58.629 1.00 116.49 ? 332 ASP   A OD2 1 
ATOM   2443 N N   . HIS   A 1 333 ? 1.248   1.530   54.850 1.00 114.65 ? 333 HIS   A N   1 
ATOM   2444 C CA  . HIS   A 1 333 ? 0.456   1.134   53.688 1.00 114.24 ? 333 HIS   A CA  1 
ATOM   2445 C C   . HIS   A 1 333 ? -0.842  0.433   54.095 1.00 121.76 ? 333 HIS   A C   1 
ATOM   2446 O O   . HIS   A 1 333 ? -1.241  -0.578  53.513 1.00 132.55 ? 333 HIS   A O   1 
ATOM   2447 C CB  . HIS   A 1 333 ? 1.271   0.295   52.704 1.00 101.98 ? 333 HIS   A CB  1 
ATOM   2448 C CG  . HIS   A 1 333 ? 0.825   0.469   51.287 1.00 118.90 ? 333 HIS   A CG  1 
ATOM   2449 N ND1 . HIS   A 1 333 ? 1.206   1.548   50.518 1.00 113.38 ? 333 HIS   A ND1 1 
ATOM   2450 C CD2 . HIS   A 1 333 ? -0.006  -0.270  50.515 1.00 119.12 ? 333 HIS   A CD2 1 
ATOM   2451 C CE1 . HIS   A 1 333 ? 0.650   1.452   49.323 1.00 107.36 ? 333 HIS   A CE1 1 
ATOM   2452 N NE2 . HIS   A 1 333 ? -0.093  0.360   49.297 1.00 118.29 ? 333 HIS   A NE2 1 
ATOM   2453 N N   . ALA   A 1 334 ? -1.500  0.979   55.114 1.00 113.42 ? 334 ALA   A N   1 
ATOM   2454 C CA  . ALA   A 1 334 ? -2.747  0.438   55.634 1.00 102.92 ? 334 ALA   A CA  1 
ATOM   2455 C C   . ALA   A 1 334 ? -3.906  0.796   54.707 1.00 109.26 ? 334 ALA   A C   1 
ATOM   2456 O O   . ALA   A 1 334 ? -3.913  1.856   54.073 1.00 110.30 ? 334 ALA   A O   1 
ATOM   2457 C CB  . ALA   A 1 334 ? -3.017  0.970   57.041 1.00 93.77  ? 334 ALA   A CB  1 
ATOM   2458 N N   . HIS   A 1 335 ? -4.879  -0.112  54.616 1.00 115.61 ? 335 HIS   A N   1 
ATOM   2459 C CA  . HIS   A 1 335 ? -6.087  0.097   53.827 1.00 98.20  ? 335 HIS   A CA  1 
ATOM   2460 C C   . HIS   A 1 335 ? -7.227  0.415   54.790 1.00 89.63  ? 335 HIS   A C   1 
ATOM   2461 O O   . HIS   A 1 335 ? -7.529  -0.390  55.677 1.00 82.95  ? 335 HIS   A O   1 
ATOM   2462 C CB  . HIS   A 1 335 ? -6.407  -1.166  53.024 1.00 104.01 ? 335 HIS   A CB  1 
ATOM   2463 C CG  . HIS   A 1 335 ? -5.190  -1.945  52.628 1.00 128.61 ? 335 HIS   A CG  1 
ATOM   2464 N ND1 . HIS   A 1 335 ? -4.314  -1.526  51.650 1.00 133.38 ? 335 HIS   A ND1 1 
ATOM   2465 C CD2 . HIS   A 1 335 ? -4.699  -3.118  53.095 1.00 127.74 ? 335 HIS   A CD2 1 
ATOM   2466 C CE1 . HIS   A 1 335 ? -3.338  -2.409  51.529 1.00 129.53 ? 335 HIS   A CE1 1 
ATOM   2467 N NE2 . HIS   A 1 335 ? -3.549  -3.385  52.394 1.00 144.67 ? 335 HIS   A NE2 1 
ATOM   2468 N N   . VAL   A 1 336 ? -7.862  1.576   54.622 1.00 82.46  ? 336 VAL   A N   1 
ATOM   2469 C CA  . VAL   A 1 336 ? -8.902  2.038   55.540 1.00 74.83  ? 336 VAL   A CA  1 
ATOM   2470 C C   . VAL   A 1 336 ? -10.263 2.048   54.852 1.00 78.85  ? 336 VAL   A C   1 
ATOM   2471 O O   . VAL   A 1 336 ? -10.383 2.474   53.697 1.00 87.07  ? 336 VAL   A O   1 
ATOM   2472 C CB  . VAL   A 1 336 ? -8.571  3.433   56.110 1.00 66.41  ? 336 VAL   A CB  1 
ATOM   2473 C CG1 . VAL   A 1 336 ? -7.408  3.349   57.084 1.00 76.55  ? 336 VAL   A CG1 1 
ATOM   2474 C CG2 . VAL   A 1 336 ? -8.261  4.412   54.993 1.00 64.47  ? 336 VAL   A CG2 1 
ATOM   2475 N N   . LYS   A 1 337 ? -11.285 1.558   55.559 1.00 73.15  ? 337 LYS   A N   1 
ATOM   2476 C CA  . LYS   A 1 337 ? -12.664 1.566   55.067 1.00 81.13  ? 337 LYS   A CA  1 
ATOM   2477 C C   . LYS   A 1 337 ? -13.551 2.411   55.980 1.00 68.71  ? 337 LYS   A C   1 
ATOM   2478 O O   . LYS   A 1 337 ? -13.602 2.159   57.196 1.00 61.42  ? 337 LYS   A O   1 
ATOM   2479 C CB  . LYS   A 1 337 ? -13.220 0.141   54.921 1.00 78.42  ? 337 LYS   A CB  1 
ATOM   2480 C CG  . LYS   A 1 337 ? -13.405 -0.644  56.205 1.00 77.58  ? 337 LYS   A CG  1 
ATOM   2481 C CD  . LYS   A 1 337 ? -14.022 -2.003  55.919 1.00 90.30  ? 337 LYS   A CD  1 
ATOM   2482 C CE  . LYS   A 1 337 ? -14.075 -2.867  57.168 1.00 113.34 ? 337 LYS   A CE  1 
ATOM   2483 N NZ  . LYS   A 1 337 ? -14.681 -4.200  56.895 1.00 99.73  ? 337 LYS   A NZ  1 
ATOM   2484 N N   . PRO   A 1 338 ? -14.225 3.440   55.461 1.00 69.11  ? 338 PRO   A N   1 
ATOM   2485 C CA  . PRO   A 1 338 ? -15.093 4.273   56.308 1.00 64.27  ? 338 PRO   A CA  1 
ATOM   2486 C C   . PRO   A 1 338 ? -16.338 3.540   56.786 1.00 65.78  ? 338 PRO   A C   1 
ATOM   2487 O O   . PRO   A 1 338 ? -16.917 2.722   56.067 1.00 68.29  ? 338 PRO   A O   1 
ATOM   2488 C CB  . PRO   A 1 338 ? -15.464 5.443   55.389 1.00 54.56  ? 338 PRO   A CB  1 
ATOM   2489 C CG  . PRO   A 1 338 ? -15.326 4.887   54.006 1.00 65.72  ? 338 PRO   A CG  1 
ATOM   2490 C CD  . PRO   A 1 338 ? -14.183 3.915   54.068 1.00 68.44  ? 338 PRO   A CD  1 
ATOM   2491 N N   . LEU   A 1 339 ? -16.743 3.837   58.021 1.00 65.89  ? 339 LEU   A N   1 
ATOM   2492 C CA  . LEU   A 1 339 ? -17.915 3.230   58.640 1.00 63.72  ? 339 LEU   A CA  1 
ATOM   2493 C C   . LEU   A 1 339 ? -18.934 4.307   58.989 1.00 75.79  ? 339 LEU   A C   1 
ATOM   2494 O O   . LEU   A 1 339 ? -18.571 5.358   59.529 1.00 80.63  ? 339 LEU   A O   1 
ATOM   2495 C CB  . LEU   A 1 339 ? -17.527 2.461   59.901 1.00 65.57  ? 339 LEU   A CB  1 
ATOM   2496 C CG  . LEU   A 1 339 ? -16.646 1.233   59.700 1.00 74.46  ? 339 LEU   A CG  1 
ATOM   2497 C CD1 . LEU   A 1 339 ? -16.391 0.547   61.031 1.00 76.88  ? 339 LEU   A CD1 1 
ATOM   2498 C CD2 . LEU   A 1 339 ? -17.277 0.274   58.708 1.00 63.51  ? 339 LEU   A CD2 1 
ATOM   2499 N N   . LEU   A 1 340 ? -20.201 4.045   58.674 1.00 75.10  ? 340 LEU   A N   1 
ATOM   2500 C CA  . LEU   A 1 340 ? -21.296 4.957   58.974 1.00 67.92  ? 340 LEU   A CA  1 
ATOM   2501 C C   . LEU   A 1 340 ? -21.814 4.723   60.385 1.00 78.09  ? 340 LEU   A C   1 
ATOM   2502 O O   . LEU   A 1 340 ? -21.989 3.578   60.810 1.00 88.28  ? 340 LEU   A O   1 
ATOM   2503 C CB  . LEU   A 1 340 ? -22.422 4.766   57.959 1.00 79.63  ? 340 LEU   A CB  1 
ATOM   2504 C CG  . LEU   A 1 340 ? -22.300 5.671   56.741 1.00 79.62  ? 340 LEU   A CG  1 
ATOM   2505 C CD1 . LEU   A 1 340 ? -23.300 5.274   55.709 1.00 101.91 ? 340 LEU   A CD1 1 
ATOM   2506 C CD2 . LEU   A 1 340 ? -22.580 7.082   57.179 1.00 91.56  ? 340 LEU   A CD2 1 
ATOM   2507 N N   . GLN   A 1 341 ? -22.047 5.820   61.112 1.00 85.35  ? 341 GLN   A N   1 
ATOM   2508 C CA  . GLN   A 1 341 ? -22.563 5.712   62.474 1.00 96.22  ? 341 GLN   A CA  1 
ATOM   2509 C C   . GLN   A 1 341 ? -23.874 4.931   62.501 1.00 89.58  ? 341 GLN   A C   1 
ATOM   2510 O O   . GLN   A 1 341 ? -24.015 3.954   63.246 1.00 81.52  ? 341 GLN   A O   1 
ATOM   2511 C CB  . GLN   A 1 341 ? -22.756 7.106   63.074 1.00 77.48  ? 341 GLN   A CB  1 
ATOM   2512 C CG  . GLN   A 1 341 ? -23.307 7.089   64.488 1.00 74.65  ? 341 GLN   A CG  1 
ATOM   2513 C CD  . GLN   A 1 341 ? -23.872 8.423   64.911 1.00 92.76  ? 341 GLN   A CD  1 
ATOM   2514 O OE1 . GLN   A 1 341 ? -23.921 9.362   64.121 1.00 94.94  ? 341 GLN   A OE1 1 
ATOM   2515 N NE2 . GLN   A 1 341 ? -24.313 8.513   66.162 1.00 99.30  ? 341 GLN   A NE2 1 
ATOM   2516 N N   . LYS   A 1 342 ? -24.844 5.349   61.689 1.00 90.54  ? 342 LYS   A N   1 
ATOM   2517 C CA  . LYS   A 1 342 ? -26.144 4.699   61.596 1.00 94.79  ? 342 LYS   A CA  1 
ATOM   2518 C C   . LYS   A 1 342 ? -26.190 3.885   60.307 1.00 106.83 ? 342 LYS   A C   1 
ATOM   2519 O O   . LYS   A 1 342 ? -25.921 4.417   59.227 1.00 106.97 ? 342 LYS   A O   1 
ATOM   2520 C CB  . LYS   A 1 342 ? -27.263 5.743   61.615 1.00 99.30  ? 342 LYS   A CB  1 
ATOM   2521 C CG  . LYS   A 1 342 ? -27.176 6.733   62.780 1.00 104.96 ? 342 LYS   A CG  1 
ATOM   2522 C CD  . LYS   A 1 342 ? -27.456 8.167   62.310 1.00 106.81 ? 342 LYS   A CD  1 
ATOM   2523 C CE  . LYS   A 1 342 ? -27.122 9.205   63.376 1.00 102.23 ? 342 LYS   A CE  1 
ATOM   2524 N NZ  . LYS   A 1 342 ? -27.510 10.566  62.919 1.00 111.58 ? 342 LYS   A NZ  1 
ATOM   2525 N N   . ARG   A 1 343 ? -26.511 2.597   60.421 1.00 102.58 ? 343 ARG   A N   1 
ATOM   2526 C CA  . ARG   A 1 343 ? -26.531 1.728   59.238 1.00 103.49 ? 343 ARG   A CA  1 
ATOM   2527 C C   . ARG   A 1 343 ? -27.605 2.116   58.211 1.00 111.09 ? 343 ARG   A C   1 
ATOM   2528 O O   . ARG   A 1 343 ? -28.758 2.362   58.587 1.00 109.92 ? 343 ARG   A O   1 
ATOM   2529 C CB  . ARG   A 1 343 ? -26.690 0.265   59.656 1.00 107.05 ? 343 ARG   A CB  1 
ATOM   2530 C CG  . ARG   A 1 343 ? -26.709 -0.692  58.470 1.00 110.97 ? 343 ARG   A CG  1 
ATOM   2531 C CD  . ARG   A 1 343 ? -26.099 -2.049  58.792 1.00 110.42 ? 343 ARG   A CD  1 
ATOM   2532 N NE  . ARG   A 1 343 ? -25.873 -2.786  57.551 1.00 131.25 ? 343 ARG   A NE  1 
ATOM   2533 C CZ  . ARG   A 1 343 ? -25.172 -3.910  57.451 1.00 136.60 ? 343 ARG   A CZ  1 
ATOM   2534 N NH1 . ARG   A 1 343 ? -24.609 -4.438  58.525 1.00 118.34 ? 343 ARG   A NH1 1 
ATOM   2535 N NH2 . ARG   A 1 343 ? -25.020 -4.496  56.269 1.00 138.05 ? 343 ARG   A NH2 1 
ATOM   2536 N N   . PRO   A 1 344 ? -27.251 2.192   56.915 1.00 111.54 ? 344 PRO   A N   1 
ATOM   2537 C CA  . PRO   A 1 344 ? -28.195 2.538   55.832 1.00 113.93 ? 344 PRO   A CA  1 
ATOM   2538 C C   . PRO   A 1 344 ? -29.047 1.386   55.300 1.00 113.98 ? 344 PRO   A C   1 
ATOM   2539 O O   . PRO   A 1 344 ? -28.591 0.243   55.202 1.00 102.57 ? 344 PRO   A O   1 
ATOM   2540 C CB  . PRO   A 1 344 ? -27.258 3.050   54.713 1.00 114.36 ? 344 PRO   A CB  1 
ATOM   2541 C CG  . PRO   A 1 344 ? -25.921 3.166   55.387 1.00 114.92 ? 344 PRO   A CG  1 
ATOM   2542 C CD  . PRO   A 1 344 ? -25.905 2.058   56.353 1.00 108.48 ? 344 PRO   A CD  1 
ATOM   2543 N N   . LYS   A 1 345 ? -30.297 1.695   54.955 1.00 106.71 ? 345 LYS   A N   1 
ATOM   2544 C CA  . LYS   A 1 345 ? -31.198 0.690   54.401 1.00 94.88  ? 345 LYS   A CA  1 
ATOM   2545 C C   . LYS   A 1 345 ? -30.762 0.270   52.988 1.00 109.90 ? 345 LYS   A C   1 
ATOM   2546 O O   . LYS   A 1 345 ? -30.146 1.052   52.256 1.00 110.19 ? 345 LYS   A O   1 
ATOM   2547 C CB  . LYS   A 1 345 ? -32.635 1.209   54.378 1.00 88.15  ? 345 LYS   A CB  1 
ATOM   2548 C CG  . LYS   A 1 345 ? -32.786 2.727   54.359 1.00 90.78  ? 345 LYS   A CG  1 
ATOM   2549 C CD  . LYS   A 1 345 ? -34.267 3.120   54.345 1.00 109.60 ? 345 LYS   A CD  1 
ATOM   2550 C CE  . LYS   A 1 345 ? -34.466 4.634   54.277 1.00 113.71 ? 345 LYS   A CE  1 
ATOM   2551 N NZ  . LYS   A 1 345 ? -35.912 5.006   54.163 1.00 83.54  ? 345 LYS   A NZ  1 
ATOM   2552 N N   . PRO   A 1 346 ? -31.079 -0.968  52.580 1.00 113.80 ? 346 PRO   A N   1 
ATOM   2553 C CA  . PRO   A 1 346 ? -30.653 -1.447  51.246 1.00 105.89 ? 346 PRO   A CA  1 
ATOM   2554 C C   . PRO   A 1 346 ? -31.219 -0.656  50.079 1.00 112.94 ? 346 PRO   A C   1 
ATOM   2555 O O   . PRO   A 1 346 ? -30.532 -0.472  49.067 1.00 111.35 ? 346 PRO   A O   1 
ATOM   2556 C CB  . PRO   A 1 346 ? -31.145 -2.904  51.225 1.00 95.67  ? 346 PRO   A CB  1 
ATOM   2557 C CG  . PRO   A 1 346 ? -32.195 -2.980  52.282 1.00 93.12  ? 346 PRO   A CG  1 
ATOM   2558 C CD  . PRO   A 1 346 ? -31.810 -1.996  53.337 1.00 89.42  ? 346 PRO   A CD  1 
ATOM   2559 N N   . ASP   A 1 347 ? -32.469 -0.203  50.180 1.00 112.30 ? 347 ASP   A N   1 
ATOM   2560 C CA  . ASP   A 1 347 ? -33.101 0.513   49.075 1.00 118.13 ? 347 ASP   A CA  1 
ATOM   2561 C C   . ASP   A 1 347 ? -32.431 1.853   48.798 1.00 117.43 ? 347 ASP   A C   1 
ATOM   2562 O O   . ASP   A 1 347 ? -32.501 2.355   47.667 1.00 111.89 ? 347 ASP   A O   1 
ATOM   2563 C CB  . ASP   A 1 347 ? -34.587 0.694   49.365 1.00 129.52 ? 347 ASP   A CB  1 
ATOM   2564 C CG  . ASP   A 1 347 ? -35.366 -0.615  49.278 1.00 144.89 ? 347 ASP   A CG  1 
ATOM   2565 O OD1 . ASP   A 1 347 ? -34.801 -1.618  48.799 1.00 142.18 ? 347 ASP   A OD1 1 
ATOM   2566 O OD2 . ASP   A 1 347 ? -36.546 -0.638  49.694 1.00 145.80 ? 347 ASP   A OD2 1 
ATOM   2567 N N   . GLU   A 1 348 ? -31.813 2.457   49.810 1.00 108.09 ? 348 GLU   A N   1 
ATOM   2568 C CA  . GLU   A 1 348 ? -31.155 3.746   49.639 1.00 98.83  ? 348 GLU   A CA  1 
ATOM   2569 C C   . GLU   A 1 348 ? -30.030 3.657   48.613 1.00 103.87 ? 348 GLU   A C   1 
ATOM   2570 O O   . GLU   A 1 348 ? -29.241 2.708   48.612 1.00 99.72  ? 348 GLU   A O   1 
ATOM   2571 C CB  . GLU   A 1 348 ? -30.602 4.239   50.974 1.00 92.15  ? 348 GLU   A CB  1 
ATOM   2572 C CG  . GLU   A 1 348 ? -29.992 5.625   50.901 1.00 94.31  ? 348 GLU   A CG  1 
ATOM   2573 C CD  . GLU   A 1 348 ? -29.525 6.130   52.250 1.00 100.16 ? 348 GLU   A CD  1 
ATOM   2574 O OE1 . GLU   A 1 348 ? -29.670 5.393   53.248 1.00 105.66 ? 348 GLU   A OE1 1 
ATOM   2575 O OE2 . GLU   A 1 348 ? -29.028 7.274   52.311 1.00 103.27 ? 348 GLU   A OE2 1 
ATOM   2576 N N   . LYS   A 1 349 ? -29.964 4.661   47.738 1.00 102.66 ? 349 LYS   A N   1 
ATOM   2577 C CA  . LYS   A 1 349 ? -28.945 4.727   46.698 1.00 97.39  ? 349 LYS   A CA  1 
ATOM   2578 C C   . LYS   A 1 349 ? -27.570 5.070   47.273 1.00 99.91  ? 349 LYS   A C   1 
ATOM   2579 O O   . LYS   A 1 349 ? -27.440 5.844   48.227 1.00 83.28  ? 349 LYS   A O   1 
ATOM   2580 C CB  . LYS   A 1 349 ? -29.334 5.767   45.643 1.00 92.69  ? 349 LYS   A CB  1 
ATOM   2581 C CG  . LYS   A 1 349 ? -28.409 5.817   44.429 1.00 98.61  ? 349 LYS   A CG  1 
ATOM   2582 C CD  . LYS   A 1 349 ? -28.883 6.819   43.382 1.00 113.28 ? 349 LYS   A CD  1 
ATOM   2583 C CE  . LYS   A 1 349 ? -27.910 6.904   42.215 1.00 106.51 ? 349 LYS   A CE  1 
ATOM   2584 N NZ  . LYS   A 1 349 ? -28.327 7.925   41.214 1.00 92.55  ? 349 LYS   A NZ  1 
ATOM   2585 N N   . TYR   A 1 350 ? -26.538 4.481   46.667 1.00 87.56  ? 350 TYR   A N   1 
ATOM   2586 C CA  . TYR   A 1 350 ? -25.140 4.709   47.003 1.00 76.85  ? 350 TYR   A CA  1 
ATOM   2587 C C   . TYR   A 1 350 ? -24.466 5.447   45.853 1.00 80.86  ? 350 TYR   A C   1 
ATOM   2588 O O   . TYR   A 1 350 ? -24.828 5.264   44.687 1.00 95.44  ? 350 TYR   A O   1 
ATOM   2589 C CB  . TYR   A 1 350 ? -24.411 3.385   47.252 1.00 79.28  ? 350 TYR   A CB  1 
ATOM   2590 C CG  . TYR   A 1 350 ? -24.656 2.760   48.608 1.00 79.06  ? 350 TYR   A CG  1 
ATOM   2591 C CD1 . TYR   A 1 350 ? -23.882 3.106   49.706 1.00 75.68  ? 350 TYR   A CD1 1 
ATOM   2592 C CD2 . TYR   A 1 350 ? -25.651 1.805   48.782 1.00 80.61  ? 350 TYR   A CD2 1 
ATOM   2593 C CE1 . TYR   A 1 350 ? -24.101 2.528   50.944 1.00 81.65  ? 350 TYR   A CE1 1 
ATOM   2594 C CE2 . TYR   A 1 350 ? -25.876 1.223   50.013 1.00 91.69  ? 350 TYR   A CE2 1 
ATOM   2595 C CZ  . TYR   A 1 350 ? -25.099 1.587   51.090 1.00 89.68  ? 350 TYR   A CZ  1 
ATOM   2596 O OH  . TYR   A 1 350 ? -25.320 1.011   52.318 1.00 101.62 ? 350 TYR   A OH  1 
ATOM   2597 N N   . TYR   A 1 351 ? -23.479 6.283   46.180 1.00 79.01  ? 351 TYR   A N   1 
ATOM   2598 C CA  . TYR   A 1 351 ? -22.757 7.063   45.188 1.00 73.44  ? 351 TYR   A CA  1 
ATOM   2599 C C   . TYR   A 1 351 ? -21.259 6.840   45.324 1.00 69.82  ? 351 TYR   A C   1 
ATOM   2600 O O   . TYR   A 1 351 ? -20.751 6.477   46.390 1.00 73.26  ? 351 TYR   A O   1 
ATOM   2601 C CB  . TYR   A 1 351 ? -23.027 8.566   45.324 1.00 72.94  ? 351 TYR   A CB  1 
ATOM   2602 C CG  . TYR   A 1 351 ? -24.481 8.956   45.306 1.00 83.96  ? 351 TYR   A CG  1 
ATOM   2603 C CD1 . TYR   A 1 351 ? -25.114 9.325   44.126 1.00 84.25  ? 351 TYR   A CD1 1 
ATOM   2604 C CD2 . TYR   A 1 351 ? -25.218 8.979   46.482 1.00 92.08  ? 351 TYR   A CD2 1 
ATOM   2605 C CE1 . TYR   A 1 351 ? -26.446 9.691   44.121 1.00 91.57  ? 351 TYR   A CE1 1 
ATOM   2606 C CE2 . TYR   A 1 351 ? -26.547 9.341   46.486 1.00 94.42  ? 351 TYR   A CE2 1 
ATOM   2607 C CZ  . TYR   A 1 351 ? -27.155 9.696   45.304 1.00 93.01  ? 351 TYR   A CZ  1 
ATOM   2608 O OH  . TYR   A 1 351 ? -28.477 10.060  45.306 1.00 96.40  ? 351 TYR   A OH  1 
ATOM   2609 N N   . SER   A 1 352 ? -20.564 7.079   44.210 1.00 73.87  ? 352 SER   A N   1 
ATOM   2610 C CA  . SER   A 1 352 ? -19.107 7.066   44.186 1.00 55.32  ? 352 SER   A CA  1 
ATOM   2611 C C   . SER   A 1 352 ? -18.574 8.289   44.914 1.00 67.71  ? 352 SER   A C   1 
ATOM   2612 O O   . SER   A 1 352 ? -18.952 9.423   44.601 1.00 67.07  ? 352 SER   A O   1 
ATOM   2613 C CB  . SER   A 1 352 ? -18.597 7.070   42.749 1.00 60.76  ? 352 SER   A CB  1 
ATOM   2614 O OG  . SER   A 1 352 ? -19.091 5.949   42.033 1.00 103.21 ? 352 SER   A OG  1 
ATOM   2615 N N   . SER   A 1 353 ? -17.674 8.067   45.866 1.00 58.60  ? 353 SER   A N   1 
ATOM   2616 C CA  . SER   A 1 353 ? -17.219 9.146   46.721 1.00 64.28  ? 353 SER   A CA  1 
ATOM   2617 C C   . SER   A 1 353 ? -15.739 8.993   47.036 1.00 57.58  ? 353 SER   A C   1 
ATOM   2618 O O   . SER   A 1 353 ? -15.190 7.890   47.010 1.00 58.86  ? 353 SER   A O   1 
ATOM   2619 C CB  . SER   A 1 353 ? -18.032 9.192   48.022 1.00 62.41  ? 353 SER   A CB  1 
ATOM   2620 O OG  . SER   A 1 353 ? -19.404 9.429   47.753 1.00 80.49  ? 353 SER   A OG  1 
ATOM   2621 N N   . SER   A 1 354 ? -15.099 10.124  47.319 1.00 53.65  ? 354 SER   A N   1 
ATOM   2622 C CA  . SER   A 1 354 ? -13.728 10.172  47.797 1.00 47.76  ? 354 SER   A CA  1 
ATOM   2623 C C   . SER   A 1 354 ? -13.688 10.947  49.108 1.00 58.31  ? 354 SER   A C   1 
ATOM   2624 O O   . SER   A 1 354 ? -14.532 11.814  49.359 1.00 60.28  ? 354 SER   A O   1 
ATOM   2625 C CB  . SER   A 1 354 ? -12.798 10.826  46.771 1.00 51.27  ? 354 SER   A CB  1 
ATOM   2626 O OG  . SER   A 1 354 ? -13.243 12.130  46.446 1.00 60.98  ? 354 SER   A OG  1 
ATOM   2627 N N   . ILE   A 1 355 ? -12.703 10.629  49.944 1.00 47.40  ? 355 ILE   A N   1 
ATOM   2628 C CA  . ILE   A 1 355 ? -12.562 11.224  51.268 1.00 49.82  ? 355 ILE   A CA  1 
ATOM   2629 C C   . ILE   A 1 355 ? -11.197 11.892  51.354 1.00 53.63  ? 355 ILE   A C   1 
ATOM   2630 O O   . ILE   A 1 355 ? -10.180 11.285  50.998 1.00 53.79  ? 355 ILE   A O   1 
ATOM   2631 C CB  . ILE   A 1 355 ? -12.737 10.176  52.382 1.00 43.41  ? 355 ILE   A CB  1 
ATOM   2632 C CG1 . ILE   A 1 355 ? -14.027 9.385   52.159 1.00 40.89  ? 355 ILE   A CG1 1 
ATOM   2633 C CG2 . ILE   A 1 355 ? -12.766 10.848  53.739 1.00 39.43  ? 355 ILE   A CG2 1 
ATOM   2634 C CD1 . ILE   A 1 355 ? -14.252 8.297   53.173 1.00 44.63  ? 355 ILE   A CD1 1 
ATOM   2635 N N   . TRP   A 1 356 ? -11.177 13.142  51.821 1.00 46.81  ? 356 TRP   A N   1 
ATOM   2636 C CA  . TRP   A 1 356 ? -9.983  13.974  51.794 1.00 40.15  ? 356 TRP   A CA  1 
ATOM   2637 C C   . TRP   A 1 356 ? -9.685  14.536  53.178 1.00 52.04  ? 356 TRP   A C   1 
ATOM   2638 O O   . TRP   A 1 356 ? -10.583 14.713  54.005 1.00 56.30  ? 356 TRP   A O   1 
ATOM   2639 C CB  . TRP   A 1 356 ? -10.138 15.117  50.791 1.00 43.63  ? 356 TRP   A CB  1 
ATOM   2640 C CG  . TRP   A 1 356 ? -10.451 14.641  49.412 1.00 62.04  ? 356 TRP   A CG  1 
ATOM   2641 C CD1 . TRP   A 1 356 ? -11.664 14.227  48.943 1.00 70.32  ? 356 TRP   A CD1 1 
ATOM   2642 C CD2 . TRP   A 1 356 ? -9.537  14.530  48.317 1.00 60.69  ? 356 TRP   A CD2 1 
ATOM   2643 N NE1 . TRP   A 1 356 ? -11.561 13.865  47.621 1.00 68.55  ? 356 TRP   A NE1 1 
ATOM   2644 C CE2 . TRP   A 1 356 ? -10.265 14.042  47.214 1.00 64.84  ? 356 TRP   A CE2 1 
ATOM   2645 C CE3 . TRP   A 1 356 ? -8.175  14.796  48.163 1.00 51.95  ? 356 TRP   A CE3 1 
ATOM   2646 C CZ2 . TRP   A 1 356 ? -9.676  13.816  45.975 1.00 69.37  ? 356 TRP   A CZ2 1 
ATOM   2647 C CZ3 . TRP   A 1 356 ? -7.593  14.572  46.934 1.00 65.12  ? 356 TRP   A CZ3 1 
ATOM   2648 C CH2 . TRP   A 1 356 ? -8.342  14.086  45.855 1.00 60.41  ? 356 TRP   A CH2 1 
ATOM   2649 N N   . GLY   A 1 357 ? -8.404  14.820  53.413 1.00 56.12  ? 357 GLY   A N   1 
ATOM   2650 C CA  . GLY   A 1 357 ? -7.945  15.366  54.672 1.00 49.00  ? 357 GLY   A CA  1 
ATOM   2651 C C   . GLY   A 1 357 ? -8.113  16.869  54.754 1.00 55.69  ? 357 GLY   A C   1 
ATOM   2652 O O   . GLY   A 1 357 ? -8.418  17.563  53.772 1.00 52.02  ? 357 GLY   A O   1 
ATOM   2653 N N   . PRO   A 1 358 ? -7.916  17.396  55.965 1.00 57.48  ? 358 PRO   A N   1 
ATOM   2654 C CA  . PRO   A 1 358 ? -8.058  18.845  56.172 1.00 51.56  ? 358 PRO   A CA  1 
ATOM   2655 C C   . PRO   A 1 358 ? -6.984  19.687  55.496 1.00 56.72  ? 358 PRO   A C   1 
ATOM   2656 O O   . PRO   A 1 358 ? -7.253  20.851  55.173 1.00 71.93  ? 358 PRO   A O   1 
ATOM   2657 C CB  . PRO   A 1 358 ? -8.000  18.973  57.700 1.00 43.41  ? 358 PRO   A CB  1 
ATOM   2658 C CG  . PRO   A 1 358 ? -7.139  17.818  58.098 1.00 57.05  ? 358 PRO   A CG  1 
ATOM   2659 C CD  . PRO   A 1 358 ? -7.659  16.704  57.239 1.00 46.01  ? 358 PRO   A CD  1 
ATOM   2660 N N   . THR   A 1 359 ? -5.777  19.159  55.298 1.00 58.63  ? 359 THR   A N   1 
ATOM   2661 C CA  . THR   A 1 359 ? -4.675  19.974  54.798 1.00 68.87  ? 359 THR   A CA  1 
ATOM   2662 C C   . THR   A 1 359 ? -4.901  20.415  53.353 1.00 70.35  ? 359 THR   A C   1 
ATOM   2663 O O   . THR   A 1 359 ? -5.618  19.773  52.580 1.00 66.26  ? 359 THR   A O   1 
ATOM   2664 C CB  . THR   A 1 359 ? -3.348  19.218  54.898 1.00 66.59  ? 359 THR   A CB  1 
ATOM   2665 O OG1 . THR   A 1 359 ? -3.322  18.163  53.932 1.00 77.81  ? 359 THR   A OG1 1 
ATOM   2666 C CG2 . THR   A 1 359 ? -3.174  18.632  56.291 1.00 70.77  ? 359 THR   A CG2 1 
ATOM   2667 N N   . CYS   A 1 360 ? -4.274  21.542  53.001 1.00 68.93  ? 360 CYS   A N   1 
ATOM   2668 C CA  . CYS   A 1 360 ? -4.403  22.100  51.659 1.00 90.02  ? 360 CYS   A CA  1 
ATOM   2669 C C   . CYS   A 1 360 ? -3.773  21.210  50.593 1.00 89.95  ? 360 CYS   A C   1 
ATOM   2670 O O   . CYS   A 1 360 ? -4.147  21.302  49.418 1.00 102.16 ? 360 CYS   A O   1 
ATOM   2671 C CB  . CYS   A 1 360 ? -3.774  23.493  51.612 1.00 91.33  ? 360 CYS   A CB  1 
ATOM   2672 S SG  . CYS   A 1 360 ? -4.548  24.707  52.710 1.00 95.68  ? 360 CYS   A SG  1 
ATOM   2673 N N   . ASP   A 1 361 ? -2.797  20.385  50.960 1.00 75.61  ? 361 ASP   A N   1 
ATOM   2674 C CA  . ASP   A 1 361 ? -2.123  19.546  49.977 1.00 90.52  ? 361 ASP   A CA  1 
ATOM   2675 C C   . ASP   A 1 361 ? -3.109  18.603  49.294 1.00 81.61  ? 361 ASP   A C   1 
ATOM   2676 O O   . ASP   A 1 361 ? -3.974  18.004  49.941 1.00 76.95  ? 361 ASP   A O   1 
ATOM   2677 C CB  . ASP   A 1 361 ? -1.004  18.746  50.647 1.00 79.93  ? 361 ASP   A CB  1 
ATOM   2678 C CG  . ASP   A 1 361 ? -0.239  17.862  49.668 1.00 98.33  ? 361 ASP   A CG  1 
ATOM   2679 O OD1 . ASP   A 1 361 ? -0.461  17.972  48.443 1.00 95.04  ? 361 ASP   A OD1 1 
ATOM   2680 O OD2 . ASP   A 1 361 ? 0.598   17.055  50.130 1.00 89.66  ? 361 ASP   A OD2 1 
ATOM   2681 N N   . GLY   A 1 362 ? -2.963  18.465  47.972 1.00 73.93  ? 362 GLY   A N   1 
ATOM   2682 C CA  . GLY   A 1 362 ? -3.834  17.580  47.217 1.00 76.44  ? 362 GLY   A CA  1 
ATOM   2683 C C   . GLY   A 1 362 ? -3.514  16.115  47.429 1.00 65.64  ? 362 GLY   A C   1 
ATOM   2684 O O   . GLY   A 1 362 ? -4.332  15.256  47.081 1.00 80.93  ? 362 GLY   A O   1 
ATOM   2685 N N   . LEU   A 1 363 ? -2.338  15.818  47.971 1.00 64.90  ? 363 LEU   A N   1 
ATOM   2686 C CA  . LEU   A 1 363 ? -1.907  14.458  48.254 1.00 68.25  ? 363 LEU   A CA  1 
ATOM   2687 C C   . LEU   A 1 363 ? -2.553  13.911  49.520 1.00 68.65  ? 363 LEU   A C   1 
ATOM   2688 O O   . LEU   A 1 363 ? -2.457  12.709  49.782 1.00 59.57  ? 363 LEU   A O   1 
ATOM   2689 C CB  . LEU   A 1 363 ? -0.376  14.433  48.371 1.00 81.02  ? 363 LEU   A CB  1 
ATOM   2690 C CG  . LEU   A 1 363 ? 0.397   13.171  48.751 1.00 86.59  ? 363 LEU   A CG  1 
ATOM   2691 C CD1 . LEU   A 1 363 ? 1.522   12.917  47.762 1.00 80.04  ? 363 LEU   A CD1 1 
ATOM   2692 C CD2 . LEU   A 1 363 ? 0.942   13.303  50.166 1.00 73.08  ? 363 LEU   A CD2 1 
ATOM   2693 N N   . ASP   A 1 364 ? -3.240  14.766  50.284 1.00 61.38  ? 364 ASP   A N   1 
ATOM   2694 C CA  . ASP   A 1 364 ? -3.930  14.380  51.515 1.00 61.05  ? 364 ASP   A CA  1 
ATOM   2695 C C   . ASP   A 1 364 ? -5.281  13.776  51.146 1.00 52.93  ? 364 ASP   A C   1 
ATOM   2696 O O   . ASP   A 1 364 ? -6.339  14.388  51.308 1.00 55.21  ? 364 ASP   A O   1 
ATOM   2697 C CB  . ASP   A 1 364 ? -4.094  15.587  52.433 1.00 66.74  ? 364 ASP   A CB  1 
ATOM   2698 C CG  . ASP   A 1 364 ? -4.527  15.204  53.840 1.00 71.15  ? 364 ASP   A CG  1 
ATOM   2699 O OD1 . ASP   A 1 364 ? -4.943  14.048  54.050 1.00 61.32  ? 364 ASP   A OD1 1 
ATOM   2700 O OD2 . ASP   A 1 364 ? -4.453  16.064  54.743 1.00 62.65  ? 364 ASP   A OD2 1 
ATOM   2701 N N   . ARG   A 1 365 ? -5.243  12.543  50.649 1.00 49.11  ? 365 ARG   A N   1 
ATOM   2702 C CA  . ARG   A 1 365 ? -6.442  11.802  50.290 1.00 42.46  ? 365 ARG   A CA  1 
ATOM   2703 C C   . ARG   A 1 365 ? -6.495  10.522  51.111 1.00 51.11  ? 365 ARG   A C   1 
ATOM   2704 O O   . ARG   A 1 365 ? -5.504  9.787   51.182 1.00 53.92  ? 365 ARG   A O   1 
ATOM   2705 C CB  . ARG   A 1 365 ? -6.471  11.486  48.790 1.00 41.42  ? 365 ARG   A CB  1 
ATOM   2706 C CG  . ARG   A 1 365 ? -7.709  10.722  48.357 1.00 62.43  ? 365 ARG   A CG  1 
ATOM   2707 C CD  . ARG   A 1 365 ? -7.717  10.457  46.864 1.00 70.97  ? 365 ARG   A CD  1 
ATOM   2708 N NE  . ARG   A 1 365 ? -6.579  9.648   46.447 1.00 77.16  ? 365 ARG   A NE  1 
ATOM   2709 C CZ  . ARG   A 1 365 ? -6.168  9.540   45.190 1.00 69.30  ? 365 ARG   A CZ  1 
ATOM   2710 N NH1 . ARG   A 1 365 ? -6.805  10.194  44.231 1.00 73.48  ? 365 ARG   A NH1 1 
ATOM   2711 N NH2 . ARG   A 1 365 ? -5.124  8.780   44.893 1.00 59.36  ? 365 ARG   A NH2 1 
ATOM   2712 N N   . ILE   A 1 366 ? -7.650  10.255  51.718 1.00 51.19  ? 366 ILE   A N   1 
ATOM   2713 C CA  . ILE   A 1 366 ? -7.808  9.083   52.583 1.00 50.89  ? 366 ILE   A CA  1 
ATOM   2714 C C   . ILE   A 1 366 ? -8.320  7.883   51.805 1.00 51.22  ? 366 ILE   A C   1 
ATOM   2715 O O   . ILE   A 1 366 ? -7.816  6.767   51.961 1.00 44.58  ? 366 ILE   A O   1 
ATOM   2716 C CB  . ILE   A 1 366 ? -8.741  9.433   53.762 1.00 55.22  ? 366 ILE   A CB  1 
ATOM   2717 C CG1 . ILE   A 1 366 ? -8.189  10.622  54.536 1.00 41.27  ? 366 ILE   A CG1 1 
ATOM   2718 C CG2 . ILE   A 1 366 ? -8.923  8.236   54.688 1.00 54.04  ? 366 ILE   A CG2 1 
ATOM   2719 C CD1 . ILE   A 1 366 ? -9.198  11.222  55.466 1.00 62.44  ? 366 ILE   A CD1 1 
ATOM   2720 N N   . VAL   A 1 367 ? -9.342  8.090   50.975 1.00 52.03  ? 367 VAL   A N   1 
ATOM   2721 C CA  . VAL   A 1 367 ? -9.977  7.019   50.217 1.00 44.33  ? 367 VAL   A CA  1 
ATOM   2722 C C   . VAL   A 1 367 ? -10.206 7.536   48.807 1.00 50.46  ? 367 VAL   A C   1 
ATOM   2723 O O   . VAL   A 1 367 ? -10.849 8.575   48.622 1.00 60.29  ? 367 VAL   A O   1 
ATOM   2724 C CB  . VAL   A 1 367 ? -11.304 6.561   50.840 1.00 46.04  ? 367 VAL   A CB  1 
ATOM   2725 C CG1 . VAL   A 1 367 ? -12.008 5.588   49.915 1.00 60.09  ? 367 VAL   A CG1 1 
ATOM   2726 C CG2 . VAL   A 1 367 ? -11.059 5.923   52.202 1.00 48.28  ? 367 VAL   A CG2 1 
ATOM   2727 N N   . GLU   A 1 368 ? -9.677  6.820   47.811 1.00 62.05  ? 368 GLU   A N   1 
ATOM   2728 C CA  . GLU   A 1 368 ? -9.801  7.280   46.432 1.00 50.22  ? 368 GLU   A CA  1 
ATOM   2729 C C   . GLU   A 1 368 ? -11.234 7.151   45.934 1.00 60.47  ? 368 GLU   A C   1 
ATOM   2730 O O   . GLU   A 1 368 ? -11.794 8.103   45.380 1.00 75.18  ? 368 GLU   A O   1 
ATOM   2731 C CB  . GLU   A 1 368 ? -8.849  6.501   45.526 1.00 53.36  ? 368 GLU   A CB  1 
ATOM   2732 C CG  . GLU   A 1 368 ? -8.876  6.984   44.082 1.00 73.86  ? 368 GLU   A CG  1 
ATOM   2733 C CD  . GLU   A 1 368 ? -7.976  6.179   43.169 1.00 91.86  ? 368 GLU   A CD  1 
ATOM   2734 O OE1 . GLU   A 1 368 ? -7.463  5.131   43.612 1.00 104.37 ? 368 GLU   A OE1 1 
ATOM   2735 O OE2 . GLU   A 1 368 ? -7.784  6.594   42.005 1.00 84.09  ? 368 GLU   A OE2 1 
ATOM   2736 N N   . ARG   A 1 369 ? -11.850 5.986   46.125 1.00 61.95  ? 369 ARG   A N   1 
ATOM   2737 C CA  . ARG   A 1 369 ? -13.210 5.785   45.645 1.00 61.54  ? 369 ARG   A CA  1 
ATOM   2738 C C   . ARG   A 1 369 ? -13.879 4.719   46.497 1.00 67.45  ? 369 ARG   A C   1 
ATOM   2739 O O   . ARG   A 1 369 ? -13.289 3.667   46.758 1.00 64.26  ? 369 ARG   A O   1 
ATOM   2740 C CB  . ARG   A 1 369 ? -13.234 5.361   44.173 1.00 57.10  ? 369 ARG   A CB  1 
ATOM   2741 C CG  . ARG   A 1 369 ? -14.622 5.427   43.550 1.00 77.42  ? 369 ARG   A CG  1 
ATOM   2742 C CD  . ARG   A 1 369 ? -14.829 4.374   42.476 1.00 83.52  ? 369 ARG   A CD  1 
ATOM   2743 N NE  . ARG   A 1 369 ? -14.591 3.028   42.991 1.00 89.25  ? 369 ARG   A NE  1 
ATOM   2744 C CZ  . ARG   A 1 369 ? -15.505 2.306   43.636 1.00 95.10  ? 369 ARG   A CZ  1 
ATOM   2745 N NH1 . ARG   A 1 369 ? -16.717 2.797   43.847 1.00 91.94  ? 369 ARG   A NH1 1 
ATOM   2746 N NH2 . ARG   A 1 369 ? -15.210 1.090   44.073 1.00 93.35  ? 369 ARG   A NH2 1 
ATOM   2747 N N   . CYS   A 1 370 ? -15.105 5.000   46.925 1.00 76.18  ? 370 CYS   A N   1 
ATOM   2748 C CA  . CYS   A 1 370 ? -15.899 4.065   47.704 1.00 65.68  ? 370 CYS   A CA  1 
ATOM   2749 C C   . CYS   A 1 370 ? -17.368 4.373   47.453 1.00 72.26  ? 370 CYS   A C   1 
ATOM   2750 O O   . CYS   A 1 370 ? -17.711 5.366   46.810 1.00 79.78  ? 370 CYS   A O   1 
ATOM   2751 C CB  . CYS   A 1 370 ? -15.547 4.148   49.192 1.00 65.08  ? 370 CYS   A CB  1 
ATOM   2752 S SG  . CYS   A 1 370 ? -15.899 5.755   49.933 1.00 86.53  ? 370 CYS   A SG  1 
ATOM   2753 N N   . ASP   A 1 371 ? -18.238 3.499   47.944 1.00 84.68  ? 371 ASP   A N   1 
ATOM   2754 C CA  . ASP   A 1 371 ? -19.677 3.671   47.787 1.00 68.23  ? 371 ASP   A CA  1 
ATOM   2755 C C   . ASP   A 1 371 ? -20.266 4.141   49.110 1.00 66.92  ? 371 ASP   A C   1 
ATOM   2756 O O   . ASP   A 1 371 ? -20.176 3.434   50.119 1.00 77.46  ? 371 ASP   A O   1 
ATOM   2757 C CB  . ASP   A 1 371 ? -20.334 2.371   47.330 1.00 79.05  ? 371 ASP   A CB  1 
ATOM   2758 C CG  . ASP   A 1 371 ? -19.911 1.970   45.934 1.00 94.48  ? 371 ASP   A CG  1 
ATOM   2759 O OD1 . ASP   A 1 371 ? -19.884 2.849   45.047 1.00 88.16  ? 371 ASP   A OD1 1 
ATOM   2760 O OD2 . ASP   A 1 371 ? -19.603 0.778   45.723 1.00 92.62  ? 371 ASP   A OD2 1 
ATOM   2761 N N   . LEU   A 1 372 ? -20.867 5.326   49.102 1.00 68.54  ? 372 LEU   A N   1 
ATOM   2762 C CA  . LEU   A 1 372 ? -21.447 5.906   50.305 1.00 71.42  ? 372 LEU   A CA  1 
ATOM   2763 C C   . LEU   A 1 372 ? -22.772 6.566   49.964 1.00 68.89  ? 372 LEU   A C   1 
ATOM   2764 O O   . LEU   A 1 372 ? -22.939 7.086   48.857 1.00 68.97  ? 372 LEU   A O   1 
ATOM   2765 C CB  . LEU   A 1 372 ? -20.515 6.951   50.941 1.00 72.75  ? 372 LEU   A CB  1 
ATOM   2766 C CG  . LEU   A 1 372 ? -19.176 6.484   51.513 1.00 68.61  ? 372 LEU   A CG  1 
ATOM   2767 C CD1 . LEU   A 1 372 ? -18.362 7.680   51.981 1.00 68.72  ? 372 LEU   A CD1 1 
ATOM   2768 C CD2 . LEU   A 1 372 ? -19.382 5.493   52.646 1.00 62.31  ? 372 LEU   A CD2 1 
ATOM   2769 N N   . PRO   A 1 373 ? -23.734 6.548   50.881 1.00 76.21  ? 373 PRO   A N   1 
ATOM   2770 C CA  . PRO   A 1 373 ? -24.931 7.369   50.694 1.00 76.66  ? 373 PRO   A CA  1 
ATOM   2771 C C   . PRO   A 1 373 ? -24.573 8.842   50.783 1.00 69.26  ? 373 PRO   A C   1 
ATOM   2772 O O   . PRO   A 1 373 ? -23.521 9.223   51.300 1.00 77.21  ? 373 PRO   A O   1 
ATOM   2773 C CB  . PRO   A 1 373 ? -25.842 6.943   51.848 1.00 76.53  ? 373 PRO   A CB  1 
ATOM   2774 C CG  . PRO   A 1 373 ? -24.907 6.477   52.893 1.00 67.33  ? 373 PRO   A CG  1 
ATOM   2775 C CD  . PRO   A 1 373 ? -23.755 5.832   52.167 1.00 76.31  ? 373 PRO   A CD  1 
ATOM   2776 N N   . GLU   A 1 374 ? -25.463 9.680   50.259 1.00 76.73  ? 374 GLU   A N   1 
ATOM   2777 C CA  . GLU   A 1 374 ? -25.221 11.115  50.305 1.00 64.87  ? 374 GLU   A CA  1 
ATOM   2778 C C   . GLU   A 1 374 ? -25.158 11.582  51.751 1.00 62.83  ? 374 GLU   A C   1 
ATOM   2779 O O   . GLU   A 1 374 ? -26.113 11.411  52.514 1.00 72.30  ? 374 GLU   A O   1 
ATOM   2780 C CB  . GLU   A 1 374 ? -26.308 11.871  49.547 1.00 69.77  ? 374 GLU   A CB  1 
ATOM   2781 C CG  . GLU   A 1 374 ? -26.196 13.382  49.697 1.00 79.87  ? 374 GLU   A CG  1 
ATOM   2782 C CD  . GLU   A 1 374 ? -27.074 14.141  48.724 1.00 94.54  ? 374 GLU   A CD  1 
ATOM   2783 O OE1 . GLU   A 1 374 ? -27.896 13.502  48.033 1.00 109.60 ? 374 GLU   A OE1 1 
ATOM   2784 O OE2 . GLU   A 1 374 ? -26.942 15.381  48.650 1.00 92.66  ? 374 GLU   A OE2 1 
ATOM   2785 N N   . MET   A 1 375 ? -24.026 12.161  52.127 1.00 61.51  ? 375 MET   A N   1 
ATOM   2786 C CA  . MET   A 1 375 ? -23.791 12.648  53.474 1.00 60.16  ? 375 MET   A CA  1 
ATOM   2787 C C   . MET   A 1 375 ? -23.652 14.163  53.458 1.00 69.60  ? 375 MET   A C   1 
ATOM   2788 O O   . MET   A 1 375 ? -23.508 14.788  52.406 1.00 75.05  ? 375 MET   A O   1 
ATOM   2789 C CB  . MET   A 1 375 ? -22.544 11.992  54.074 1.00 75.54  ? 375 MET   A CB  1 
ATOM   2790 C CG  . MET   A 1 375 ? -22.617 10.480  54.135 1.00 59.29  ? 375 MET   A CG  1 
ATOM   2791 S SD  . MET   A 1 375 ? -21.154 9.810   54.938 1.00 128.86 ? 375 MET   A SD  1 
ATOM   2792 C CE  . MET   A 1 375 ? -21.469 10.264  56.643 1.00 91.41  ? 375 MET   A CE  1 
ATOM   2793 N N   . HIS   A 1 376 ? -23.698 14.753  54.647 1.00 54.76  ? 376 HIS   A N   1 
ATOM   2794 C CA  . HIS   A 1 376 ? -23.716 16.199  54.780 1.00 63.94  ? 376 HIS   A CA  1 
ATOM   2795 C C   . HIS   A 1 376 ? -22.669 16.642  55.791 1.00 59.71  ? 376 HIS   A C   1 
ATOM   2796 O O   . HIS   A 1 376 ? -22.233 15.869  56.648 1.00 49.42  ? 376 HIS   A O   1 
ATOM   2797 C CB  . HIS   A 1 376 ? -25.104 16.693  55.200 1.00 62.39  ? 376 HIS   A CB  1 
ATOM   2798 C CG  . HIS   A 1 376 ? -26.215 16.134  54.368 1.00 77.05  ? 376 HIS   A CG  1 
ATOM   2799 N ND1 . HIS   A 1 376 ? -26.721 16.788  53.266 1.00 84.23  ? 376 HIS   A ND1 1 
ATOM   2800 C CD2 . HIS   A 1 376 ? -26.913 14.979  54.474 1.00 85.37  ? 376 HIS   A CD2 1 
ATOM   2801 C CE1 . HIS   A 1 376 ? -27.685 16.061  52.729 1.00 92.39  ? 376 HIS   A CE1 1 
ATOM   2802 N NE2 . HIS   A 1 376 ? -27.822 14.958  53.443 1.00 88.48  ? 376 HIS   A NE2 1 
ATOM   2803 N N   . VAL   A 1 377 ? -22.249 17.903  55.655 1.00 48.79  ? 377 VAL   A N   1 
ATOM   2804 C CA  . VAL   A 1 377 ? -21.324 18.490  56.614 1.00 53.76  ? 377 VAL   A CA  1 
ATOM   2805 C C   . VAL   A 1 377 ? -21.914 18.376  58.012 1.00 54.18  ? 377 VAL   A C   1 
ATOM   2806 O O   . VAL   A 1 377 ? -23.092 18.678  58.236 1.00 61.20  ? 377 VAL   A O   1 
ATOM   2807 C CB  . VAL   A 1 377 ? -21.019 19.947  56.234 1.00 49.36  ? 377 VAL   A CB  1 
ATOM   2808 C CG1 . VAL   A 1 377 ? -20.262 20.649  57.348 1.00 51.34  ? 377 VAL   A CG1 1 
ATOM   2809 C CG2 . VAL   A 1 377 ? -20.221 19.992  54.942 1.00 59.48  ? 377 VAL   A CG2 1 
ATOM   2810 N N   . GLY   A 1 378 ? -21.098 17.921  58.959 1.00 53.20  ? 378 GLY   A N   1 
ATOM   2811 C CA  . GLY   A 1 378 ? -21.539 17.643  60.303 1.00 56.18  ? 378 GLY   A CA  1 
ATOM   2812 C C   . GLY   A 1 378 ? -21.787 16.176  60.590 1.00 59.79  ? 378 GLY   A C   1 
ATOM   2813 O O   . GLY   A 1 378 ? -21.853 15.791  61.763 1.00 63.00  ? 378 GLY   A O   1 
ATOM   2814 N N   . ASP   A 1 379 ? -21.925 15.352  59.554 1.00 55.39  ? 379 ASP   A N   1 
ATOM   2815 C CA  . ASP   A 1 379 ? -22.036 13.916  59.749 1.00 57.82  ? 379 ASP   A CA  1 
ATOM   2816 C C   . ASP   A 1 379 ? -20.683 13.333  60.150 1.00 64.79  ? 379 ASP   A C   1 
ATOM   2817 O O   . ASP   A 1 379 ? -19.622 13.897  59.865 1.00 71.96  ? 379 ASP   A O   1 
ATOM   2818 C CB  . ASP   A 1 379 ? -22.550 13.237  58.480 1.00 58.73  ? 379 ASP   A CB  1 
ATOM   2819 C CG  . ASP   A 1 379 ? -24.007 13.547  58.205 1.00 77.86  ? 379 ASP   A CG  1 
ATOM   2820 O OD1 . ASP   A 1 379 ? -24.655 14.164  59.076 1.00 69.35  ? 379 ASP   A OD1 1 
ATOM   2821 O OD2 . ASP   A 1 379 ? -24.505 13.178  57.119 1.00 73.56  ? 379 ASP   A OD2 1 
ATOM   2822 N N   . TRP   A 1 380 ? -20.730 12.188  60.822 1.00 58.49  ? 380 TRP   A N   1 
ATOM   2823 C CA  . TRP   A 1 380 ? -19.533 11.539  61.327 1.00 51.04  ? 380 TRP   A CA  1 
ATOM   2824 C C   . TRP   A 1 380 ? -19.225 10.271  60.541 1.00 54.75  ? 380 TRP   A C   1 
ATOM   2825 O O   . TRP   A 1 380 ? -20.125 9.576   60.062 1.00 70.89  ? 380 TRP   A O   1 
ATOM   2826 C CB  . TRP   A 1 380 ? -19.676 11.205  62.814 1.00 51.51  ? 380 TRP   A CB  1 
ATOM   2827 C CG  . TRP   A 1 380 ? -19.744 12.411  63.701 1.00 65.09  ? 380 TRP   A CG  1 
ATOM   2828 C CD1 . TRP   A 1 380 ? -20.852 13.150  63.996 1.00 57.78  ? 380 TRP   A CD1 1 
ATOM   2829 C CD2 . TRP   A 1 380 ? -18.658 13.011  64.421 1.00 62.21  ? 380 TRP   A CD2 1 
ATOM   2830 N NE1 . TRP   A 1 380 ? -20.523 14.176  64.850 1.00 59.14  ? 380 TRP   A NE1 1 
ATOM   2831 C CE2 . TRP   A 1 380 ? -19.183 14.112  65.126 1.00 55.96  ? 380 TRP   A CE2 1 
ATOM   2832 C CE3 . TRP   A 1 380 ? -17.294 12.724  64.535 1.00 48.68  ? 380 TRP   A CE3 1 
ATOM   2833 C CZ2 . TRP   A 1 380 ? -18.392 14.927  65.934 1.00 49.63  ? 380 TRP   A CZ2 1 
ATOM   2834 C CZ3 . TRP   A 1 380 ? -16.510 13.536  65.338 1.00 60.57  ? 380 TRP   A CZ3 1 
ATOM   2835 C CH2 . TRP   A 1 380 ? -17.062 14.623  66.026 1.00 50.00  ? 380 TRP   A CH2 1 
ATOM   2836 N N   . MET   A 1 381 ? -17.933 9.988   60.416 1.00 54.88  ? 381 MET   A N   1 
ATOM   2837 C CA  . MET   A 1 381 ? -17.421 8.750   59.852 1.00 47.33  ? 381 MET   A CA  1 
ATOM   2838 C C   . MET   A 1 381 ? -16.563 8.058   60.898 1.00 56.08  ? 381 MET   A C   1 
ATOM   2839 O O   . MET   A 1 381 ? -15.800 8.710   61.623 1.00 59.84  ? 381 MET   A O   1 
ATOM   2840 C CB  . MET   A 1 381 ? -16.593 9.005   58.593 1.00 61.41  ? 381 MET   A CB  1 
ATOM   2841 C CG  . MET   A 1 381 ? -17.409 9.251   57.342 1.00 68.62  ? 381 MET   A CG  1 
ATOM   2842 S SD  . MET   A 1 381 ? -16.345 9.399   55.896 1.00 91.86  ? 381 MET   A SD  1 
ATOM   2843 C CE  . MET   A 1 381 ? -17.444 10.199  54.732 1.00 91.41  ? 381 MET   A CE  1 
ATOM   2844 N N   . LEU   A 1 382 ? -16.686 6.737   60.974 1.00 51.46  ? 382 LEU   A N   1 
ATOM   2845 C CA  . LEU   A 1 382 ? -15.972 5.941   61.960 1.00 62.68  ? 382 LEU   A CA  1 
ATOM   2846 C C   . LEU   A 1 382 ? -14.945 5.047   61.279 1.00 58.50  ? 382 LEU   A C   1 
ATOM   2847 O O   . LEU   A 1 382 ? -15.186 4.524   60.187 1.00 58.67  ? 382 LEU   A O   1 
ATOM   2848 C CB  . LEU   A 1 382 ? -16.942 5.089   62.781 1.00 58.61  ? 382 LEU   A CB  1 
ATOM   2849 C CG  . LEU   A 1 382 ? -18.047 5.871   63.493 1.00 60.92  ? 382 LEU   A CG  1 
ATOM   2850 C CD1 . LEU   A 1 382 ? -18.917 4.945   64.331 1.00 76.42  ? 382 LEU   A CD1 1 
ATOM   2851 C CD2 . LEU   A 1 382 ? -17.463 6.987   64.338 1.00 51.04  ? 382 LEU   A CD2 1 
ATOM   2852 N N   . PHE   A 1 383 ? -13.793 4.891   61.926 1.00 48.16  ? 383 PHE   A N   1 
ATOM   2853 C CA  . PHE   A 1 383 ? -12.730 4.011   61.455 1.00 56.32  ? 383 PHE   A CA  1 
ATOM   2854 C C   . PHE   A 1 383 ? -12.300 3.129   62.618 1.00 58.76  ? 383 PHE   A C   1 
ATOM   2855 O O   . PHE   A 1 383 ? -11.778 3.628   63.621 1.00 47.63  ? 383 PHE   A O   1 
ATOM   2856 C CB  . PHE   A 1 383 ? -11.549 4.809   60.900 1.00 44.40  ? 383 PHE   A CB  1 
ATOM   2857 C CG  . PHE   A 1 383 ? -11.879 5.596   59.663 1.00 46.60  ? 383 PHE   A CG  1 
ATOM   2858 C CD1 . PHE   A 1 383 ? -12.399 6.877   59.757 1.00 60.89  ? 383 PHE   A CD1 1 
ATOM   2859 C CD2 . PHE   A 1 383 ? -11.676 5.052   58.406 1.00 54.71  ? 383 PHE   A CD2 1 
ATOM   2860 C CE1 . PHE   A 1 383 ? -12.705 7.603   58.619 1.00 55.34  ? 383 PHE   A CE1 1 
ATOM   2861 C CE2 . PHE   A 1 383 ? -11.980 5.772   57.264 1.00 53.68  ? 383 PHE   A CE2 1 
ATOM   2862 C CZ  . PHE   A 1 383 ? -12.495 7.048   57.372 1.00 51.13  ? 383 PHE   A CZ  1 
ATOM   2863 N N   . GLU   A 1 384 ? -12.537 1.828   62.495 1.00 58.97  ? 384 GLU   A N   1 
ATOM   2864 C CA  . GLU   A 1 384 ? -12.154 0.879   63.526 1.00 58.00  ? 384 GLU   A CA  1 
ATOM   2865 C C   . GLU   A 1 384 ? -10.718 0.408   63.316 1.00 54.02  ? 384 GLU   A C   1 
ATOM   2866 O O   . GLU   A 1 384 ? -10.119 0.602   62.255 1.00 70.27  ? 384 GLU   A O   1 
ATOM   2867 C CB  . GLU   A 1 384 ? -13.107 -0.316  63.537 1.00 57.98  ? 384 GLU   A CB  1 
ATOM   2868 C CG  . GLU   A 1 384 ? -14.505 0.005   64.030 1.00 73.77  ? 384 GLU   A CG  1 
ATOM   2869 C CD  . GLU   A 1 384 ? -15.443 -1.182  63.925 1.00 93.92  ? 384 GLU   A CD  1 
ATOM   2870 O OE1 . GLU   A 1 384 ? -15.111 -2.142  63.198 1.00 91.05  ? 384 GLU   A OE1 1 
ATOM   2871 O OE2 . GLU   A 1 384 ? -16.512 -1.157  64.568 1.00 99.46  ? 384 GLU   A OE2 1 
ATOM   2872 N N   . ASN   A 1 385 ? -10.168 -0.222  64.355 1.00 58.67  ? 385 ASN   A N   1 
ATOM   2873 C CA  . ASN   A 1 385 ? -8.835  -0.820  64.309 1.00 49.86  ? 385 ASN   A CA  1 
ATOM   2874 C C   . ASN   A 1 385 ? -7.768  0.225   63.979 1.00 57.40  ? 385 ASN   A C   1 
ATOM   2875 O O   . ASN   A 1 385 ? -6.877  0.002   63.157 1.00 62.26  ? 385 ASN   A O   1 
ATOM   2876 C CB  . ASN   A 1 385 ? -8.795  -1.987  63.318 1.00 56.84  ? 385 ASN   A CB  1 
ATOM   2877 C CG  . ASN   A 1 385 ? -9.872  -3.019  63.592 1.00 62.05  ? 385 ASN   A CG  1 
ATOM   2878 O OD1 . ASN   A 1 385 ? -10.143 -3.357  64.744 1.00 69.37  ? 385 ASN   A OD1 1 
ATOM   2879 N ND2 . ASN   A 1 385 ? -10.493 -3.523  62.532 1.00 60.47  ? 385 ASN   A ND2 1 
ATOM   2880 N N   . MET   A 1 386 ? -7.862  1.379   64.643 1.00 49.66  ? 386 MET   A N   1 
ATOM   2881 C CA  . MET   A 1 386 ? -6.962  2.503   64.410 1.00 54.91  ? 386 MET   A CA  1 
ATOM   2882 C C   . MET   A 1 386 ? -5.963  2.694   65.548 1.00 62.35  ? 386 MET   A C   1 
ATOM   2883 O O   . MET   A 1 386 ? -5.461  3.800   65.762 1.00 56.65  ? 386 MET   A O   1 
ATOM   2884 C CB  . MET   A 1 386 ? -7.762  3.785   64.191 1.00 47.77  ? 386 MET   A CB  1 
ATOM   2885 C CG  . MET   A 1 386 ? -8.504  3.819   62.871 1.00 52.78  ? 386 MET   A CG  1 
ATOM   2886 S SD  . MET   A 1 386 ? -7.375  3.901   61.469 1.00 70.34  ? 386 MET   A SD  1 
ATOM   2887 C CE  . MET   A 1 386 ? -6.736  5.565   61.649 1.00 56.17  ? 386 MET   A CE  1 
ATOM   2888 N N   . GLY   A 1 387 ? -5.663  1.624   66.286 1.00 52.67  ? 387 GLY   A N   1 
ATOM   2889 C CA  . GLY   A 1 387 ? -4.777  1.747   67.429 1.00 53.53  ? 387 GLY   A CA  1 
ATOM   2890 C C   . GLY   A 1 387 ? -3.301  1.702   67.094 1.00 46.71  ? 387 GLY   A C   1 
ATOM   2891 O O   . GLY   A 1 387 ? -2.481  2.243   67.841 1.00 52.68  ? 387 GLY   A O   1 
ATOM   2892 N N   . ALA   A 1 388 ? -2.936  1.059   65.989 1.00 53.86  ? 388 ALA   A N   1 
ATOM   2893 C CA  . ALA   A 1 388 ? -1.545  0.746   65.694 1.00 49.16  ? 388 ALA   A CA  1 
ATOM   2894 C C   . ALA   A 1 388 ? -0.970  1.723   64.679 1.00 48.76  ? 388 ALA   A C   1 
ATOM   2895 O O   . ALA   A 1 388 ? -1.517  1.882   63.583 1.00 64.58  ? 388 ALA   A O   1 
ATOM   2896 C CB  . ALA   A 1 388 ? -1.415  -0.683  65.167 1.00 51.07  ? 388 ALA   A CB  1 
ATOM   2897 N N   . TYR   A 1 389 ? 0.145   2.357   65.044 1.00 49.03  ? 389 TYR   A N   1 
ATOM   2898 C CA  . TYR   A 1 389 ? 0.922   3.197   64.133 1.00 52.77  ? 389 TYR   A CA  1 
ATOM   2899 C C   . TYR   A 1 389 ? 0.068   4.295   63.502 1.00 52.52  ? 389 TYR   A C   1 
ATOM   2900 O O   . TYR   A 1 389 ? 0.190   4.595   62.313 1.00 58.32  ? 389 TYR   A O   1 
ATOM   2901 C CB  . TYR   A 1 389 ? 1.599   2.346   63.058 1.00 52.02  ? 389 TYR   A CB  1 
ATOM   2902 C CG  . TYR   A 1 389 ? 2.453   1.236   63.624 1.00 51.35  ? 389 TYR   A CG  1 
ATOM   2903 C CD1 . TYR   A 1 389 ? 3.697   1.504   64.179 1.00 54.01  ? 389 TYR   A CD1 1 
ATOM   2904 C CD2 . TYR   A 1 389 ? 2.006   -0.079  63.623 1.00 58.48  ? 389 TYR   A CD2 1 
ATOM   2905 C CE1 . TYR   A 1 389 ? 4.477   0.493   64.704 1.00 54.15  ? 389 TYR   A CE1 1 
ATOM   2906 C CE2 . TYR   A 1 389 ? 2.777   -1.095  64.147 1.00 52.96  ? 389 TYR   A CE2 1 
ATOM   2907 C CZ  . TYR   A 1 389 ? 4.011   -0.803  64.687 1.00 51.60  ? 389 TYR   A CZ  1 
ATOM   2908 O OH  . TYR   A 1 389 ? 4.781   -1.814  65.209 1.00 57.49  ? 389 TYR   A OH  1 
ATOM   2909 N N   . THR   A 1 390 ? -0.818  4.893   64.298 1.00 62.43  ? 390 THR   A N   1 
ATOM   2910 C CA  . THR   A 1 390 ? -1.632  6.010   63.839 1.00 58.88  ? 390 THR   A CA  1 
ATOM   2911 C C   . THR   A 1 390 ? -1.304  7.301   64.580 1.00 60.91  ? 390 THR   A C   1 
ATOM   2912 O O   . THR   A 1 390 ? -0.887  8.283   63.959 1.00 64.51  ? 390 THR   A O   1 
ATOM   2913 C CB  . THR   A 1 390 ? -3.122  5.675   63.994 1.00 51.16  ? 390 THR   A CB  1 
ATOM   2914 O OG1 . THR   A 1 390 ? -3.388  5.290   65.347 1.00 62.28  ? 390 THR   A OG1 1 
ATOM   2915 C CG2 . THR   A 1 390 ? -3.508  4.532   63.068 1.00 43.33  ? 390 THR   A CG2 1 
ATOM   2916 N N   . VAL   A 1 391 ? -1.464  7.321   65.904 1.00 70.06  ? 391 VAL   A N   1 
ATOM   2917 C CA  . VAL   A 1 391 ? -1.140  8.521   66.669 1.00 54.96  ? 391 VAL   A CA  1 
ATOM   2918 C C   . VAL   A 1 391 ? 0.359   8.632   66.913 1.00 44.64  ? 391 VAL   A C   1 
ATOM   2919 O O   . VAL   A 1 391 ? 0.888   9.743   67.039 1.00 63.38  ? 391 VAL   A O   1 
ATOM   2920 C CB  . VAL   A 1 391 ? -1.926  8.549   67.992 1.00 51.90  ? 391 VAL   A CB  1 
ATOM   2921 C CG1 . VAL   A 1 391 ? -3.410  8.641   67.715 1.00 52.23  ? 391 VAL   A CG1 1 
ATOM   2922 C CG2 . VAL   A 1 391 ? -1.616  7.320   68.838 1.00 58.65  ? 391 VAL   A CG2 1 
ATOM   2923 N N   . ALA   A 1 392 ? 1.063   7.499   66.994 1.00 45.92  ? 392 ALA   A N   1 
ATOM   2924 C CA  . ALA   A 1 392 ? 2.491   7.518   67.283 1.00 55.23  ? 392 ALA   A CA  1 
ATOM   2925 C C   . ALA   A 1 392 ? 3.296   8.254   66.220 1.00 52.31  ? 392 ALA   A C   1 
ATOM   2926 O O   . ALA   A 1 392 ? 4.385   8.754   66.523 1.00 62.70  ? 392 ALA   A O   1 
ATOM   2927 C CB  . ALA   A 1 392 ? 3.015   6.088   67.432 1.00 63.90  ? 392 ALA   A CB  1 
ATOM   2928 N N   . ALA   A 1 393 ? 2.789   8.342   64.988 1.00 55.77  ? 393 ALA   A N   1 
ATOM   2929 C CA  . ALA   A 1 393 ? 3.524   8.958   63.889 1.00 58.79  ? 393 ALA   A CA  1 
ATOM   2930 C C   . ALA   A 1 393 ? 2.798   10.169  63.312 1.00 51.26  ? 393 ALA   A C   1 
ATOM   2931 O O   . ALA   A 1 393 ? 3.126   10.616  62.209 1.00 70.20  ? 393 ALA   A O   1 
ATOM   2932 C CB  . ALA   A 1 393 ? 3.800   7.931   62.789 1.00 49.41  ? 393 ALA   A CB  1 
ATOM   2933 N N   . ALA   A 1 394 ? 1.826   10.713  64.033 1.00 51.77  ? 394 ALA   A N   1 
ATOM   2934 C CA  . ALA   A 1 394 ? 1.090   11.872  63.553 1.00 49.20  ? 394 ALA   A CA  1 
ATOM   2935 C C   . ALA   A 1 394 ? 1.894   13.151  63.764 1.00 55.74  ? 394 ALA   A C   1 
ATOM   2936 O O   . ALA   A 1 394 ? 2.686   13.267  64.703 1.00 61.59  ? 394 ALA   A O   1 
ATOM   2937 C CB  . ALA   A 1 394 ? -0.260  11.983  64.262 1.00 53.46  ? 394 ALA   A CB  1 
ATOM   2938 N N   . SER   A 1 395 ? 1.682   14.114  62.873 1.00 56.30  ? 395 SER   A N   1 
ATOM   2939 C CA  . SER   A 1 395 ? 2.308   15.425  62.954 1.00 58.62  ? 395 SER   A CA  1 
ATOM   2940 C C   . SER   A 1 395 ? 1.234   16.506  62.996 1.00 57.99  ? 395 SER   A C   1 
ATOM   2941 O O   . SER   A 1 395 ? 0.043   16.244  62.815 1.00 69.30  ? 395 SER   A O   1 
ATOM   2942 C CB  . SER   A 1 395 ? 3.258   15.663  61.771 1.00 57.95  ? 395 SER   A CB  1 
ATOM   2943 O OG  . SER   A 1 395 ? 2.537   15.936  60.582 1.00 52.40  ? 395 SER   A OG  1 
ATOM   2944 N N   . THR   A 1 396 ? 1.672   17.740  63.244 1.00 58.06  ? 396 THR   A N   1 
ATOM   2945 C CA  . THR   A 1 396 ? 0.787   18.898  63.281 1.00 63.20  ? 396 THR   A CA  1 
ATOM   2946 C C   . THR   A 1 396 ? 0.927   19.774  62.039 1.00 61.21  ? 396 THR   A C   1 
ATOM   2947 O O   . THR   A 1 396 ? 0.794   20.998  62.124 1.00 65.95  ? 396 THR   A O   1 
ATOM   2948 C CB  . THR   A 1 396 ? 1.041   19.726  64.540 1.00 73.19  ? 396 THR   A CB  1 
ATOM   2949 O OG1 . THR   A 1 396 ? 2.414   20.136  64.575 1.00 74.89  ? 396 THR   A OG1 1 
ATOM   2950 C CG2 . THR   A 1 396 ? 0.721   18.915  65.785 1.00 58.03  ? 396 THR   A CG2 1 
ATOM   2951 N N   . PHE   A 1 397 ? 1.211   19.166  60.888 1.00 60.36  ? 397 PHE   A N   1 
ATOM   2952 C CA  . PHE   A 1 397 ? 1.291   19.920  59.643 1.00 59.40  ? 397 PHE   A CA  1 
ATOM   2953 C C   . PHE   A 1 397 ? 0.001   20.696  59.409 1.00 66.09  ? 397 PHE   A C   1 
ATOM   2954 O O   . PHE   A 1 397 ? -1.098  20.201  59.677 1.00 60.79  ? 397 PHE   A O   1 
ATOM   2955 C CB  . PHE   A 1 397 ? 1.570   18.982  58.470 1.00 55.80  ? 397 PHE   A CB  1 
ATOM   2956 C CG  . PHE   A 1 397 ? 1.699   19.683  57.147 1.00 58.58  ? 397 PHE   A CG  1 
ATOM   2957 C CD1 . PHE   A 1 397 ? 2.749   20.556  56.910 1.00 57.11  ? 397 PHE   A CD1 1 
ATOM   2958 C CD2 . PHE   A 1 397 ? 0.781   19.457  56.135 1.00 59.85  ? 397 PHE   A CD2 1 
ATOM   2959 C CE1 . PHE   A 1 397 ? 2.874   21.197  55.691 1.00 63.62  ? 397 PHE   A CE1 1 
ATOM   2960 C CE2 . PHE   A 1 397 ? 0.904   20.091  54.913 1.00 72.48  ? 397 PHE   A CE2 1 
ATOM   2961 C CZ  . PHE   A 1 397 ? 1.950   20.965  54.692 1.00 70.78  ? 397 PHE   A CZ  1 
ATOM   2962 N N   . ASN   A 1 398 ? 0.146   21.930  58.923 1.00 69.09  ? 398 ASN   A N   1 
ATOM   2963 C CA  . ASN   A 1 398 ? -0.924  22.899  58.695 1.00 68.73  ? 398 ASN   A CA  1 
ATOM   2964 C C   . ASN   A 1 398 ? -1.516  23.416  59.998 1.00 69.00  ? 398 ASN   A C   1 
ATOM   2965 O O   . ASN   A 1 398 ? -2.494  24.170  59.960 1.00 76.08  ? 398 ASN   A O   1 
ATOM   2966 C CB  . ASN   A 1 398 ? -2.056  22.344  57.816 1.00 75.05  ? 398 ASN   A CB  1 
ATOM   2967 C CG  . ASN   A 1 398 ? -1.891  22.706  56.355 1.00 73.55  ? 398 ASN   A CG  1 
ATOM   2968 O OD1 . ASN   A 1 398 ? -0.878  22.389  55.736 1.00 93.26  ? 398 ASN   A OD1 1 
ATOM   2969 N ND2 . ASN   A 1 398 ? -2.899  23.358  55.789 1.00 80.20  ? 398 ASN   A ND2 1 
ATOM   2970 N N   . GLY   A 1 399 ? -0.962  23.039  61.149 1.00 64.15  ? 399 GLY   A N   1 
ATOM   2971 C CA  . GLY   A 1 399 ? -1.448  23.500  62.430 1.00 62.75  ? 399 GLY   A CA  1 
ATOM   2972 C C   . GLY   A 1 399 ? -2.599  22.714  63.017 1.00 65.18  ? 399 GLY   A C   1 
ATOM   2973 O O   . GLY   A 1 399 ? -3.118  23.105  64.069 1.00 74.17  ? 399 GLY   A O   1 
ATOM   2974 N N   . PHE   A 1 400 ? -3.014  21.620  62.384 1.00 65.18  ? 400 PHE   A N   1 
ATOM   2975 C CA  . PHE   A 1 400 ? -4.132  20.832  62.888 1.00 55.16  ? 400 PHE   A CA  1 
ATOM   2976 C C   . PHE   A 1 400 ? -3.660  19.951  64.039 1.00 72.56  ? 400 PHE   A C   1 
ATOM   2977 O O   . PHE   A 1 400 ? -2.702  19.185  63.891 1.00 83.31  ? 400 PHE   A O   1 
ATOM   2978 C CB  . PHE   A 1 400 ? -4.737  19.987  61.770 1.00 60.52  ? 400 PHE   A CB  1 
ATOM   2979 C CG  . PHE   A 1 400 ? -5.374  20.795  60.677 1.00 64.86  ? 400 PHE   A CG  1 
ATOM   2980 C CD1 . PHE   A 1 400 ? -4.874  20.759  59.386 1.00 73.32  ? 400 PHE   A CD1 1 
ATOM   2981 C CD2 . PHE   A 1 400 ? -6.475  21.593  60.941 1.00 66.07  ? 400 PHE   A CD2 1 
ATOM   2982 C CE1 . PHE   A 1 400 ? -5.461  21.503  58.378 1.00 79.59  ? 400 PHE   A CE1 1 
ATOM   2983 C CE2 . PHE   A 1 400 ? -7.066  22.340  59.939 1.00 60.20  ? 400 PHE   A CE2 1 
ATOM   2984 C CZ  . PHE   A 1 400 ? -6.559  22.295  58.655 1.00 67.94  ? 400 PHE   A CZ  1 
ATOM   2985 N N   . GLN   A 1 401 ? -4.328  20.068  65.184 1.00 78.28  ? 401 GLN   A N   1 
ATOM   2986 C CA  . GLN   A 1 401 ? -3.920  19.365  66.390 1.00 68.01  ? 401 GLN   A CA  1 
ATOM   2987 C C   . GLN   A 1 401 ? -4.388  17.914  66.373 1.00 75.38  ? 401 GLN   A C   1 
ATOM   2988 O O   . GLN   A 1 401 ? -5.391  17.565  65.743 1.00 70.69  ? 401 GLN   A O   1 
ATOM   2989 C CB  . GLN   A 1 401 ? -4.462  20.071  67.632 1.00 66.01  ? 401 GLN   A CB  1 
ATOM   2990 C CG  . GLN   A 1 401 ? -3.880  21.454  67.852 1.00 65.36  ? 401 GLN   A CG  1 
ATOM   2991 C CD  . GLN   A 1 401 ? -2.367  21.429  67.975 1.00 93.74  ? 401 GLN   A CD  1 
ATOM   2992 O OE1 . GLN   A 1 401 ? -1.811  20.671  68.771 1.00 106.85 ? 401 GLN   A OE1 1 
ATOM   2993 N NE2 . GLN   A 1 401 ? -1.694  22.257  67.185 1.00 86.14  ? 401 GLN   A NE2 1 
ATOM   2994 N N   . ARG   A 1 402 ? -3.640  17.069  67.076 1.00 82.83  ? 402 ARG   A N   1 
ATOM   2995 C CA  . ARG   A 1 402 ? -3.966  15.652  67.163 1.00 78.54  ? 402 ARG   A CA  1 
ATOM   2996 C C   . ARG   A 1 402 ? -5.272  15.437  67.930 1.00 67.40  ? 402 ARG   A C   1 
ATOM   2997 O O   . ARG   A 1 402 ? -5.521  16.106  68.938 1.00 72.95  ? 402 ARG   A O   1 
ATOM   2998 C CB  . ARG   A 1 402 ? -2.811  14.894  67.816 1.00 77.36  ? 402 ARG   A CB  1 
ATOM   2999 C CG  . ARG   A 1 402 ? -1.735  14.492  66.808 1.00 87.46  ? 402 ARG   A CG  1 
ATOM   3000 C CD  . ARG   A 1 402 ? -0.413  14.108  67.456 1.00 90.28  ? 402 ARG   A CD  1 
ATOM   3001 N NE  . ARG   A 1 402 ? 0.370   15.300  67.775 1.00 95.54  ? 402 ARG   A NE  1 
ATOM   3002 C CZ  . ARG   A 1 402 ? 1.495   15.298  68.482 1.00 101.47 ? 402 ARG   A CZ  1 
ATOM   3003 N NH1 . ARG   A 1 402 ? 2.134   16.438  68.711 1.00 95.41  ? 402 ARG   A NH1 1 
ATOM   3004 N NH2 . ARG   A 1 402 ? 1.984   14.162  68.959 1.00 112.59 ? 402 ARG   A NH2 1 
ATOM   3005 N N   . PRO   A 1 403 ? -6.125  14.520  67.468 1.00 64.78  ? 403 PRO   A N   1 
ATOM   3006 C CA  . PRO   A 1 403 ? -7.440  14.335  68.094 1.00 61.50  ? 403 PRO   A CA  1 
ATOM   3007 C C   . PRO   A 1 403 ? -7.346  13.913  69.552 1.00 61.42  ? 403 PRO   A C   1 
ATOM   3008 O O   . PRO   A 1 403 ? -6.446  13.175  69.956 1.00 71.14  ? 403 PRO   A O   1 
ATOM   3009 C CB  . PRO   A 1 403 ? -8.084  13.230  67.243 1.00 46.51  ? 403 PRO   A CB  1 
ATOM   3010 C CG  . PRO   A 1 403 ? -7.349  13.263  65.950 1.00 52.18  ? 403 PRO   A CG  1 
ATOM   3011 C CD  . PRO   A 1 403 ? -5.944  13.643  66.299 1.00 76.62  ? 403 PRO   A CD  1 
ATOM   3012 N N   . THR   A 1 404 ? -8.301  14.399  70.343 1.00 54.65  ? 404 THR   A N   1 
ATOM   3013 C CA  . THR   A 1 404 ? -8.417  13.976  71.731 1.00 63.43  ? 404 THR   A CA  1 
ATOM   3014 C C   . THR   A 1 404 ? -8.746  12.491  71.807 1.00 63.41  ? 404 THR   A C   1 
ATOM   3015 O O   . THR   A 1 404 ? -9.555  11.978  71.032 1.00 59.98  ? 404 THR   A O   1 
ATOM   3016 C CB  . THR   A 1 404 ? -9.502  14.790  72.439 1.00 68.50  ? 404 THR   A CB  1 
ATOM   3017 O OG1 . THR   A 1 404 ? -9.237  16.188  72.268 1.00 89.48  ? 404 THR   A OG1 1 
ATOM   3018 C CG2 . THR   A 1 404 ? -9.538  14.463  73.925 1.00 72.58  ? 404 THR   A CG2 1 
ATOM   3019 N N   . ILE   A 1 405 ? -8.106  11.797  72.745 1.00 72.79  ? 405 ILE   A N   1 
ATOM   3020 C CA  . ILE   A 1 405 ? -8.347  10.380  72.993 1.00 61.34  ? 405 ILE   A CA  1 
ATOM   3021 C C   . ILE   A 1 405 ? -9.103  10.253  74.307 1.00 63.25  ? 405 ILE   A C   1 
ATOM   3022 O O   . ILE   A 1 405 ? -8.648  10.757  75.341 1.00 77.17  ? 405 ILE   A O   1 
ATOM   3023 C CB  . ILE   A 1 405 ? -7.034  9.580   73.041 1.00 51.04  ? 405 ILE   A CB  1 
ATOM   3024 C CG1 . ILE   A 1 405 ? -6.236  9.787   71.755 1.00 56.59  ? 405 ILE   A CG1 1 
ATOM   3025 C CG2 . ILE   A 1 405 ? -7.318  8.102   73.260 1.00 52.77  ? 405 ILE   A CG2 1 
ATOM   3026 C CD1 . ILE   A 1 405 ? -4.850  9.192   71.808 1.00 61.79  ? 405 ILE   A CD1 1 
ATOM   3027 N N   . TYR   A 1 406 ? -10.251 9.582   74.270 1.00 52.08  ? 406 TYR   A N   1 
ATOM   3028 C CA  . TYR   A 1 406 ? -11.035 9.294   75.462 1.00 54.46  ? 406 TYR   A CA  1 
ATOM   3029 C C   . TYR   A 1 406 ? -10.848 7.824   75.820 1.00 58.91  ? 406 TYR   A C   1 
ATOM   3030 O O   . TYR   A 1 406 ? -11.223 6.940   75.042 1.00 62.34  ? 406 TYR   A O   1 
ATOM   3031 C CB  . TYR   A 1 406 ? -12.513 9.612   75.234 1.00 58.72  ? 406 TYR   A CB  1 
ATOM   3032 C CG  . TYR   A 1 406 ? -12.780 11.052  74.850 1.00 72.61  ? 406 TYR   A CG  1 
ATOM   3033 C CD1 . TYR   A 1 406 ? -12.588 12.081  75.759 1.00 71.78  ? 406 TYR   A CD1 1 
ATOM   3034 C CD2 . TYR   A 1 406 ? -13.244 11.379  73.581 1.00 69.15  ? 406 TYR   A CD2 1 
ATOM   3035 C CE1 . TYR   A 1 406 ? -12.827 13.401  75.410 1.00 73.33  ? 406 TYR   A CE1 1 
ATOM   3036 C CE2 . TYR   A 1 406 ? -13.494 12.694  73.226 1.00 74.47  ? 406 TYR   A CE2 1 
ATOM   3037 C CZ  . TYR   A 1 406 ? -13.285 13.701  74.146 1.00 74.43  ? 406 TYR   A CZ  1 
ATOM   3038 O OH  . TYR   A 1 406 ? -13.532 15.011  73.801 1.00 77.16  ? 406 TYR   A OH  1 
ATOM   3039 N N   . TYR   A 1 407 ? -10.252 7.568   76.983 1.00 61.51  ? 407 TYR   A N   1 
ATOM   3040 C CA  . TYR   A 1 407 ? -10.024 6.211   77.461 1.00 57.66  ? 407 TYR   A CA  1 
ATOM   3041 C C   . TYR   A 1 407 ? -11.227 5.741   78.267 1.00 60.85  ? 407 TYR   A C   1 
ATOM   3042 O O   . TYR   A 1 407 ? -11.734 6.476   79.121 1.00 64.73  ? 407 TYR   A O   1 
ATOM   3043 C CB  . TYR   A 1 407 ? -8.762  6.148   78.319 1.00 44.48  ? 407 TYR   A CB  1 
ATOM   3044 C CG  . TYR   A 1 407 ? -7.501  6.500   77.571 1.00 59.54  ? 407 TYR   A CG  1 
ATOM   3045 C CD1 . TYR   A 1 407 ? -6.948  7.770   77.664 1.00 75.06  ? 407 TYR   A CD1 1 
ATOM   3046 C CD2 . TYR   A 1 407 ? -6.862  5.562   76.773 1.00 61.48  ? 407 TYR   A CD2 1 
ATOM   3047 C CE1 . TYR   A 1 407 ? -5.793  8.096   76.982 1.00 75.42  ? 407 TYR   A CE1 1 
ATOM   3048 C CE2 . TYR   A 1 407 ? -5.707  5.878   76.087 1.00 64.00  ? 407 TYR   A CE2 1 
ATOM   3049 C CZ  . TYR   A 1 407 ? -5.177  7.147   76.196 1.00 77.06  ? 407 TYR   A CZ  1 
ATOM   3050 O OH  . TYR   A 1 407 ? -4.027  7.468   75.516 1.00 83.41  ? 407 TYR   A OH  1 
ATOM   3051 N N   . VAL   A 1 408 ? -11.681 4.518   77.998 1.00 56.14  ? 408 VAL   A N   1 
ATOM   3052 C CA  . VAL   A 1 408 ? -12.801 3.933   78.722 1.00 63.90  ? 408 VAL   A CA  1 
ATOM   3053 C C   . VAL   A 1 408 ? -12.387 2.578   79.276 1.00 56.91  ? 408 VAL   A C   1 
ATOM   3054 O O   . VAL   A 1 408 ? -11.490 1.910   78.749 1.00 53.97  ? 408 VAL   A O   1 
ATOM   3055 C CB  . VAL   A 1 408 ? -14.059 3.791   77.834 1.00 56.07  ? 408 VAL   A CB  1 
ATOM   3056 C CG1 . VAL   A 1 408 ? -14.443 5.135   77.237 1.00 59.25  ? 408 VAL   A CG1 1 
ATOM   3057 C CG2 . VAL   A 1 408 ? -13.830 2.760   76.742 1.00 54.53  ? 408 VAL   A CG2 1 
ATOM   3058 N N   . MET   A 1 409 ? -13.062 2.172   80.350 1.00 59.35  ? 409 MET   A N   1 
ATOM   3059 C CA  . MET   A 1 409 ? -12.804 0.890   80.994 1.00 59.24  ? 409 MET   A CA  1 
ATOM   3060 C C   . MET   A 1 409 ? -13.942 0.524   81.938 1.00 59.85  ? 409 MET   A C   1 
ATOM   3061 O O   . MET   A 1 409 ? -14.339 1.332   82.783 1.00 57.43  ? 409 MET   A O   1 
ATOM   3062 C CB  . MET   A 1 409 ? -11.485 0.932   81.763 1.00 48.99  ? 409 MET   A CB  1 
ATOM   3063 C CG  . MET   A 1 409 ? -10.960 -0.428  82.172 1.00 47.65  ? 409 MET   A CG  1 
ATOM   3064 S SD  . MET   A 1 409 ? -9.495  -0.244  83.201 1.00 81.48  ? 409 MET   A SD  1 
ATOM   3065 C CE  . MET   A 1 409 ? -8.774  -1.872  83.060 1.00 86.97  ? 409 MET   A CE  1 
ATOM   3066 N N   . SER   A 1 410 ? -14.471 -0.686  81.801 1.00 66.62  ? 410 SER   A N   1 
ATOM   3067 C CA  . SER   A 1 410 ? -15.525 -1.148  82.688 1.00 51.84  ? 410 SER   A CA  1 
ATOM   3068 C C   . SER   A 1 410 ? -14.935 -1.630  84.009 1.00 62.77  ? 410 SER   A C   1 
ATOM   3069 O O   . SER   A 1 410 ? -13.732 -1.878  84.121 1.00 65.79  ? 410 SER   A O   1 
ATOM   3070 C CB  . SER   A 1 410 ? -16.325 -2.275  82.040 1.00 64.19  ? 410 SER   A CB  1 
ATOM   3071 O OG  . SER   A 1 410 ? -15.494 -3.386  81.760 1.00 70.50  ? 410 SER   A OG  1 
ATOM   3072 N N   . GLY   A 1 411 ? -15.803 -1.759  85.020 1.00 68.43  ? 411 GLY   A N   1 
ATOM   3073 C CA  . GLY   A 1 411 ? -15.398 -2.270  86.309 1.00 55.98  ? 411 GLY   A CA  1 
ATOM   3074 C C   . GLY   A 1 411 ? -14.878 -3.693  86.284 1.00 58.00  ? 411 GLY   A C   1 
ATOM   3075 O O   . GLY   A 1 411 ? -13.856 -3.977  86.923 1.00 60.11  ? 411 GLY   A O   1 
ATOM   3076 N N   . PRO   A 1 412 ? -15.527 -4.614  85.558 1.00 58.16  ? 412 PRO   A N   1 
ATOM   3077 C CA  . PRO   A 1 412 ? -14.975 -5.978  85.483 1.00 63.01  ? 412 PRO   A CA  1 
ATOM   3078 C C   . PRO   A 1 412 ? -13.581 -6.007  84.877 1.00 65.67  ? 412 PRO   A C   1 
ATOM   3079 O O   . PRO   A 1 412 ? -12.723 -6.780  85.329 1.00 64.58  ? 412 PRO   A O   1 
ATOM   3080 C CB  . PRO   A 1 412 ? -16.000 -6.719  84.612 1.00 44.25  ? 412 PRO   A CB  1 
ATOM   3081 C CG  . PRO   A 1 412 ? -17.269 -5.959  84.800 1.00 54.95  ? 412 PRO   A CG  1 
ATOM   3082 C CD  . PRO   A 1 412 ? -16.847 -4.527  84.910 1.00 51.17  ? 412 PRO   A CD  1 
ATOM   3083 N N   . ALA   A 1 413 ? -13.328 -5.171  83.863 1.00 54.87  ? 413 ALA   A N   1 
ATOM   3084 C CA  . ALA   A 1 413 ? -11.997 -5.107  83.270 1.00 50.21  ? 413 ALA   A CA  1 
ATOM   3085 C C   . ALA   A 1 413 ? -10.970 -4.650  84.298 1.00 54.43  ? 413 ALA   A C   1 
ATOM   3086 O O   . ALA   A 1 413 ? -9.860  -5.198  84.378 1.00 63.87  ? 413 ALA   A O   1 
ATOM   3087 C CB  . ALA   A 1 413 ? -12.005 -4.172  82.062 1.00 55.65  ? 413 ALA   A CB  1 
ATOM   3088 N N   . TRP   A 1 414 ? -11.339 -3.664  85.117 1.00 53.97  ? 414 TRP   A N   1 
ATOM   3089 C CA  . TRP   A 1 414 ? -10.443 -3.192  86.163 1.00 50.68  ? 414 TRP   A CA  1 
ATOM   3090 C C   . TRP   A 1 414 ? -10.157 -4.311  87.154 1.00 64.71  ? 414 TRP   A C   1 
ATOM   3091 O O   . TRP   A 1 414 ? -9.027  -4.445  87.647 1.00 66.33  ? 414 TRP   A O   1 
ATOM   3092 C CB  . TRP   A 1 414 ? -11.056 -1.978  86.862 1.00 55.13  ? 414 TRP   A CB  1 
ATOM   3093 C CG  . TRP   A 1 414 ? -10.250 -1.483  88.013 1.00 58.50  ? 414 TRP   A CG  1 
ATOM   3094 C CD1 . TRP   A 1 414 ? -9.258  -0.550  87.977 1.00 61.94  ? 414 TRP   A CD1 1 
ATOM   3095 C CD2 . TRP   A 1 414 ? -10.352 -1.910  89.376 1.00 61.84  ? 414 TRP   A CD2 1 
ATOM   3096 N NE1 . TRP   A 1 414 ? -8.739  -0.363  89.233 1.00 60.70  ? 414 TRP   A NE1 1 
ATOM   3097 C CE2 . TRP   A 1 414 ? -9.393  -1.187  90.111 1.00 58.02  ? 414 TRP   A CE2 1 
ATOM   3098 C CE3 . TRP   A 1 414 ? -11.161 -2.833  90.046 1.00 51.39  ? 414 TRP   A CE3 1 
ATOM   3099 C CZ2 . TRP   A 1 414 ? -9.222  -1.355  91.483 1.00 59.29  ? 414 TRP   A CZ2 1 
ATOM   3100 C CZ3 . TRP   A 1 414 ? -10.990 -3.000  91.408 1.00 59.66  ? 414 TRP   A CZ3 1 
ATOM   3101 C CH2 . TRP   A 1 414 ? -10.028 -2.265  92.112 1.00 69.36  ? 414 TRP   A CH2 1 
ATOM   3102 N N   . GLN   A 1 415 ? -11.174 -5.127  87.456 1.00 54.97  ? 415 GLN   A N   1 
ATOM   3103 C CA  . GLN   A 1 415 ? -10.972 -6.253  88.363 1.00 70.46  ? 415 GLN   A CA  1 
ATOM   3104 C C   . GLN   A 1 415 ? -9.957  -7.231  87.793 1.00 71.96  ? 415 GLN   A C   1 
ATOM   3105 O O   . GLN   A 1 415 ? -9.085  -7.732  88.516 1.00 77.14  ? 415 GLN   A O   1 
ATOM   3106 C CB  . GLN   A 1 415 ? -12.293 -6.978  88.606 1.00 67.07  ? 415 GLN   A CB  1 
ATOM   3107 C CG  . GLN   A 1 415 ? -13.173 -6.381  89.670 1.00 79.69  ? 415 GLN   A CG  1 
ATOM   3108 C CD  . GLN   A 1 415 ? -14.469 -7.151  89.816 1.00 91.58  ? 415 GLN   A CD  1 
ATOM   3109 O OE1 . GLN   A 1 415 ? -14.989 -7.702  88.844 1.00 96.75  ? 415 GLN   A OE1 1 
ATOM   3110 N NE2 . GLN   A 1 415 ? -15.000 -7.193  91.029 1.00 83.40  ? 415 GLN   A NE2 1 
ATOM   3111 N N   . LEU   A 1 416 ? -10.062 -7.514  86.493 1.00 66.54  ? 416 LEU   A N   1 
ATOM   3112 C CA  . LEU   A 1 416 ? -9.112  -8.425  85.861 1.00 71.22  ? 416 LEU   A CA  1 
ATOM   3113 C C   . LEU   A 1 416 ? -7.695  -7.866  85.940 1.00 76.30  ? 416 LEU   A C   1 
ATOM   3114 O O   . LEU   A 1 416 ? -6.734  -8.605  86.211 1.00 87.13  ? 416 LEU   A O   1 
ATOM   3115 C CB  . LEU   A 1 416 ? -9.522  -8.671  84.409 1.00 68.09  ? 416 LEU   A CB  1 
ATOM   3116 C CG  . LEU   A 1 416 ? -8.702  -9.678  83.602 1.00 80.59  ? 416 LEU   A CG  1 
ATOM   3117 C CD1 . LEU   A 1 416 ? -8.894  -11.085 84.139 1.00 72.12  ? 416 LEU   A CD1 1 
ATOM   3118 C CD2 . LEU   A 1 416 ? -9.075  -9.598  82.135 1.00 74.93  ? 416 LEU   A CD2 1 
ATOM   3119 N N   . MET   A 1 417 ? -7.550  -6.555  85.720 1.00 67.92  ? 417 MET   A N   1 
ATOM   3120 C CA  . MET   A 1 417 ? -6.231  -5.931  85.807 1.00 66.47  ? 417 MET   A CA  1 
ATOM   3121 C C   . MET   A 1 417 ? -5.654  -6.078  87.210 1.00 71.61  ? 417 MET   A C   1 
ATOM   3122 O O   . MET   A 1 417 ? -4.465  -6.394  87.382 1.00 79.97  ? 417 MET   A O   1 
ATOM   3123 C CB  . MET   A 1 417 ? -6.340  -4.455  85.427 1.00 68.20  ? 417 MET   A CB  1 
ATOM   3124 C CG  . MET   A 1 417 ? -5.026  -3.701  85.376 1.00 73.27  ? 417 MET   A CG  1 
ATOM   3125 S SD  . MET   A 1 417 ? -5.281  -1.970  84.932 1.00 77.29  ? 417 MET   A SD  1 
ATOM   3126 C CE  . MET   A 1 417 ? -6.476  -1.486  86.181 1.00 73.30  ? 417 MET   A CE  1 
ATOM   3127 N N   . GLN   A 1 418 ? -6.500  -5.886  88.227 1.00 82.20  ? 418 GLN   A N   1 
ATOM   3128 C CA  . GLN   A 1 418 ? -6.049  -6.033  89.607 1.00 86.90  ? 418 GLN   A CA  1 
ATOM   3129 C C   . GLN   A 1 418 ? -5.618  -7.465  89.881 1.00 78.71  ? 418 GLN   A C   1 
ATOM   3130 O O   . GLN   A 1 418 ? -4.639  -7.703  90.600 1.00 83.72  ? 418 GLN   A O   1 
ATOM   3131 C CB  . GLN   A 1 418 ? -7.151  -5.598  90.571 1.00 66.80  ? 418 GLN   A CB  1 
ATOM   3132 C CG  . GLN   A 1 418 ? -7.460  -4.119  90.489 1.00 71.11  ? 418 GLN   A CG  1 
ATOM   3133 C CD  . GLN   A 1 418 ? -6.205  -3.272  90.486 1.00 95.64  ? 418 GLN   A CD  1 
ATOM   3134 O OE1 . GLN   A 1 418 ? -5.927  -2.559  89.527 1.00 96.00  ? 418 GLN   A OE1 1 
ATOM   3135 N NE2 . GLN   A 1 418 ? -5.437  -3.349  91.561 1.00 85.99  ? 418 GLN   A NE2 1 
ATOM   3136 N N   . GLN   A 1 419 ? -6.347  -8.433  89.322 1.00 76.20  ? 419 GLN   A N   1 
ATOM   3137 C CA  . GLN   A 1 419 ? -5.973  -9.832  89.496 1.00 87.46  ? 419 GLN   A CA  1 
ATOM   3138 C C   . GLN   A 1 419 ? -4.597  -10.098 88.905 1.00 91.78  ? 419 GLN   A C   1 
ATOM   3139 O O   . GLN   A 1 419 ? -3.794  -10.836 89.490 1.00 95.54  ? 419 GLN   A O   1 
ATOM   3140 C CB  . GLN   A 1 419 ? -7.016  -10.731 88.843 1.00 89.20  ? 419 GLN   A CB  1 
ATOM   3141 C CG  . GLN   A 1 419 ? -8.359  -10.693 89.525 1.00 89.33  ? 419 GLN   A CG  1 
ATOM   3142 C CD  . GLN   A 1 419 ? -9.427  -11.384 88.713 1.00 97.69  ? 419 GLN   A CD  1 
ATOM   3143 O OE1 . GLN   A 1 419 ? -9.136  -12.238 87.875 1.00 114.37 ? 419 GLN   A OE1 1 
ATOM   3144 N NE2 . GLN   A 1 419 ? -10.676 -11.003 88.941 1.00 95.82  ? 419 GLN   A NE2 1 
ATOM   3145 N N   . PHE   A 1 420 ? -4.310  -9.503  87.742 1.00 92.26  ? 420 PHE   A N   1 
ATOM   3146 C CA  . PHE   A 1 420 ? -2.983  -9.659  87.149 1.00 73.25  ? 420 PHE   A CA  1 
ATOM   3147 C C   . PHE   A 1 420 ? -1.922  -9.074  88.063 1.00 78.97  ? 420 PHE   A C   1 
ATOM   3148 O O   . PHE   A 1 420 ? -0.827  -9.630  88.191 1.00 88.42  ? 420 PHE   A O   1 
ATOM   3149 C CB  . PHE   A 1 420 ? -2.933  -9.024  85.765 1.00 75.66  ? 420 PHE   A CB  1 
ATOM   3150 C CG  . PHE   A 1 420 ? -3.573  -9.865  84.717 1.00 79.28  ? 420 PHE   A CG  1 
ATOM   3151 C CD1 . PHE   A 1 420 ? -4.458  -9.315  83.811 1.00 84.20  ? 420 PHE   A CD1 1 
ATOM   3152 C CD2 . PHE   A 1 420 ? -3.298  -11.219 84.650 1.00 75.72  ? 420 PHE   A CD2 1 
ATOM   3153 C CE1 . PHE   A 1 420 ? -5.057  -10.103 82.852 1.00 102.90 ? 420 PHE   A CE1 1 
ATOM   3154 C CE2 . PHE   A 1 420 ? -3.889  -12.012 83.695 1.00 84.00  ? 420 PHE   A CE2 1 
ATOM   3155 C CZ  . PHE   A 1 420 ? -4.770  -11.454 82.793 1.00 101.40 ? 420 PHE   A CZ  1 
ATOM   3156 N N   . GLN   A 1 421 ? -2.223  -7.943  88.704 1.00 90.57  ? 421 GLN   A N   1 
ATOM   3157 C CA  . GLN   A 1 421 ? -1.266  -7.407  89.662 1.00 96.33  ? 421 GLN   A CA  1 
ATOM   3158 C C   . GLN   A 1 421 ? -1.053  -8.389  90.811 1.00 94.92  ? 421 GLN   A C   1 
ATOM   3159 O O   . GLN   A 1 421 ? 0.055   -8.478  91.359 1.00 96.65  ? 421 GLN   A O   1 
ATOM   3160 C CB  . GLN   A 1 421 ? -1.734  -6.058  90.200 1.00 93.59  ? 421 GLN   A CB  1 
ATOM   3161 C CG  . GLN   A 1 421 ? -1.592  -4.905  89.224 1.00 93.16  ? 421 GLN   A CG  1 
ATOM   3162 C CD  . GLN   A 1 421 ? -1.914  -3.557  89.849 1.00 98.66  ? 421 GLN   A CD  1 
ATOM   3163 O OE1 . GLN   A 1 421 ? -1.794  -2.521  89.201 1.00 97.14  ? 421 GLN   A OE1 1 
ATOM   3164 N NE2 . GLN   A 1 421 ? -2.324  -3.565  91.104 1.00 95.24  ? 421 GLN   A NE2 1 
ATOM   3165 N N   . ASN   A 1 422 ? -2.100  -9.111  91.205 1.00 98.97  ? 422 ASN   A N   1 
ATOM   3166 C CA  . ASN   A 1 422 ? -2.014  -10.135 92.246 1.00 98.28  ? 422 ASN   A CA  1 
ATOM   3167 C C   . ASN   A 1 422 ? -1.519  -11.492 91.740 1.00 90.55  ? 422 ASN   A C   1 
ATOM   3168 O O   . ASN   A 1 422 ? -0.653  -12.131 92.350 1.00 90.34  ? 422 ASN   A O   1 
ATOM   3169 C CB  . ASN   A 1 422 ? -3.374  -10.337 92.898 1.00 94.67  ? 422 ASN   A CB  1 
ATOM   3170 C CG  . ASN   A 1 422 ? -3.303  -11.163 94.180 1.00 124.28 ? 422 ASN   A CG  1 
ATOM   3171 O OD1 . ASN   A 1 422 ? -2.300  -11.117 94.882 1.00 136.37 ? 422 ASN   A OD1 1 
ATOM   3172 N ND2 . ASN   A 1 422 ? -4.370  -11.905 94.497 1.00 127.51 ? 422 ASN   A ND2 1 
ATOM   3173 N N   . MET   B 1 1   ? 28.692  26.876  69.802 1.00 92.69  ? 1   MET   B N   1 
ATOM   3174 C CA  . MET   B 1 1   ? 27.359  27.457  69.705 1.00 88.88  ? 1   MET   B CA  1 
ATOM   3175 C C   . MET   B 1 1   ? 26.336  26.622  70.464 1.00 97.06  ? 1   MET   B C   1 
ATOM   3176 O O   . MET   B 1 1   ? 26.051  25.484  70.091 1.00 108.63 ? 1   MET   B O   1 
ATOM   3177 C CB  . MET   B 1 1   ? 26.939  27.591  68.242 1.00 89.34  ? 1   MET   B CB  1 
ATOM   3178 C CG  . MET   B 1 1   ? 25.525  28.108  68.049 1.00 75.62  ? 1   MET   B CG  1 
ATOM   3179 S SD  . MET   B 1 1   ? 25.086  28.187  66.306 1.00 88.12  ? 1   MET   B SD  1 
ATOM   3180 C CE  . MET   B 1 1   ? 25.380  26.489  65.815 1.00 86.20  ? 1   MET   B CE  1 
ATOM   3181 N N   . ASN   B 1 2   ? 25.783  27.196  71.530 1.00 84.91  ? 2   ASN   B N   1 
ATOM   3182 C CA  . ASN   B 1 2   ? 24.779  26.519  72.340 1.00 83.36  ? 2   ASN   B CA  1 
ATOM   3183 C C   . ASN   B 1 2   ? 23.661  27.491  72.674 1.00 88.04  ? 2   ASN   B C   1 
ATOM   3184 O O   . ASN   B 1 2   ? 23.918  28.587  73.180 1.00 86.69  ? 2   ASN   B O   1 
ATOM   3185 C CB  . ASN   B 1 2   ? 25.390  25.953  73.627 1.00 87.75  ? 2   ASN   B CB  1 
ATOM   3186 C CG  . ASN   B 1 2   ? 26.256  24.737  73.372 1.00 115.40 ? 2   ASN   B CG  1 
ATOM   3187 O OD1 . ASN   B 1 2   ? 27.465  24.762  73.602 1.00 119.34 ? 2   ASN   B OD1 1 
ATOM   3188 N ND2 . ASN   B 1 2   ? 25.640  23.661  72.897 1.00 98.63  ? 2   ASN   B ND2 1 
ATOM   3189 N N   . ASN   B 1 3   ? 22.427  27.087  72.386 1.00 93.65  ? 3   ASN   B N   1 
ATOM   3190 C CA  . ASN   B 1 3   ? 21.272  27.902  72.732 1.00 98.70  ? 3   ASN   B CA  1 
ATOM   3191 C C   . ASN   B 1 3   ? 21.134  28.018  74.244 1.00 99.74  ? 3   ASN   B C   1 
ATOM   3192 O O   . ASN   B 1 3   ? 21.389  27.065  74.986 1.00 87.37  ? 3   ASN   B O   1 
ATOM   3193 C CB  . ASN   B 1 3   ? 19.994  27.303  72.142 1.00 104.10 ? 3   ASN   B CB  1 
ATOM   3194 C CG  . ASN   B 1 3   ? 19.871  27.538  70.649 1.00 90.68  ? 3   ASN   B CG  1 
ATOM   3195 O OD1 . ASN   B 1 3   ? 20.210  28.610  70.146 1.00 93.06  ? 3   ASN   B OD1 1 
ATOM   3196 N ND2 . ASN   B 1 3   ? 19.381  26.534  69.932 1.00 95.86  ? 3   ASN   B ND2 1 
ATOM   3197 N N   . PHE   B 1 4   ? 20.728  29.199  74.698 1.00 91.77  ? 4   PHE   B N   1 
ATOM   3198 C CA  . PHE   B 1 4   ? 20.427  29.443  76.099 1.00 100.99 ? 4   PHE   B CA  1 
ATOM   3199 C C   . PHE   B 1 4   ? 18.998  29.951  76.214 1.00 103.72 ? 4   PHE   B C   1 
ATOM   3200 O O   . PHE   B 1 4   ? 18.531  30.723  75.370 1.00 92.51  ? 4   PHE   B O   1 
ATOM   3201 C CB  . PHE   B 1 4   ? 21.400  30.448  76.713 1.00 102.61 ? 4   PHE   B CB  1 
ATOM   3202 C CG  . PHE   B 1 4   ? 21.026  31.877  76.478 1.00 101.37 ? 4   PHE   B CG  1 
ATOM   3203 C CD1 . PHE   B 1 4   ? 20.565  32.659  77.520 1.00 97.89  ? 4   PHE   B CD1 1 
ATOM   3204 C CD2 . PHE   B 1 4   ? 21.128  32.439  75.218 1.00 105.15 ? 4   PHE   B CD2 1 
ATOM   3205 C CE1 . PHE   B 1 4   ? 20.218  33.971  77.310 1.00 87.68  ? 4   PHE   B CE1 1 
ATOM   3206 C CE2 . PHE   B 1 4   ? 20.779  33.755  75.002 1.00 101.20 ? 4   PHE   B CE2 1 
ATOM   3207 C CZ  . PHE   B 1 4   ? 20.324  34.522  76.050 1.00 96.48  ? 4   PHE   B CZ  1 
ATOM   3208 N N   . GLY   B 1 5   ? 18.304  29.502  77.253 1.00 109.97 ? 5   GLY   B N   1 
ATOM   3209 C CA  . GLY   B 1 5   ? 16.901  29.857  77.385 1.00 106.59 ? 5   GLY   B CA  1 
ATOM   3210 C C   . GLY   B 1 5   ? 16.074  29.150  76.330 1.00 127.34 ? 5   GLY   B C   1 
ATOM   3211 O O   . GLY   B 1 5   ? 16.171  27.932  76.147 1.00 122.19 ? 5   GLY   B O   1 
ATOM   3212 N N   . ASN   B 1 6   ? 15.253  29.920  75.616 1.00 130.16 ? 6   ASN   B N   1 
ATOM   3213 C CA  . ASN   B 1 6   ? 14.363  29.378  74.596 1.00 125.53 ? 6   ASN   B CA  1 
ATOM   3214 C C   . ASN   B 1 6   ? 15.044  29.393  73.234 1.00 119.29 ? 6   ASN   B C   1 
ATOM   3215 O O   . ASN   B 1 6   ? 15.520  30.439  72.781 1.00 122.78 ? 6   ASN   B O   1 
ATOM   3216 C CB  . ASN   B 1 6   ? 13.060  30.177  74.534 1.00 127.11 ? 6   ASN   B CB  1 
ATOM   3217 C CG  . ASN   B 1 6   ? 11.965  29.456  73.761 1.00 126.14 ? 6   ASN   B CG  1 
ATOM   3218 O OD1 . ASN   B 1 6   ? 11.949  28.228  73.683 1.00 129.59 ? 6   ASN   B OD1 1 
ATOM   3219 N ND2 . ASN   B 1 6   ? 11.044  30.223  73.184 1.00 108.81 ? 6   ASN   B ND2 1 
ATOM   3220 N N   . GLU   B 1 7   ? 15.084  28.226  72.587 1.00 119.28 ? 7   GLU   B N   1 
ATOM   3221 C CA  . GLU   B 1 7   ? 15.719  28.118  71.277 1.00 114.37 ? 7   GLU   B CA  1 
ATOM   3222 C C   . GLU   B 1 7   ? 14.971  28.922  70.222 1.00 106.02 ? 7   GLU   B C   1 
ATOM   3223 O O   . GLU   B 1 7   ? 15.589  29.511  69.328 1.00 105.65 ? 7   GLU   B O   1 
ATOM   3224 C CB  . GLU   B 1 7   ? 15.791  26.650  70.856 1.00 121.72 ? 7   GLU   B CB  1 
ATOM   3225 C CG  . GLU   B 1 7   ? 16.051  26.452  69.372 1.00 107.68 ? 7   GLU   B CG  1 
ATOM   3226 C CD  . GLU   B 1 7   ? 15.550  25.117  68.851 1.00 110.21 ? 7   GLU   B CD  1 
ATOM   3227 O OE1 . GLU   B 1 7   ? 15.833  24.079  69.483 1.00 112.99 ? 7   GLU   B OE1 1 
ATOM   3228 O OE2 . GLU   B 1 7   ? 14.863  25.110  67.807 1.00 93.69  ? 7   GLU   B OE2 1 
ATOM   3229 N N   . GLU   B 1 8   ? 13.642  28.966  70.323 1.00 100.77 ? 8   GLU   B N   1 
ATOM   3230 C CA  . GLU   B 1 8   ? 12.824  29.603  69.297 1.00 105.25 ? 8   GLU   B CA  1 
ATOM   3231 C C   . GLU   B 1 8   ? 13.159  31.083  69.131 1.00 104.26 ? 8   GLU   B C   1 
ATOM   3232 O O   . GLU   B 1 8   ? 13.257  31.582  68.003 1.00 98.86  ? 8   GLU   B O   1 
ATOM   3233 C CB  . GLU   B 1 8   ? 11.349  29.411  69.646 1.00 107.45 ? 8   GLU   B CB  1 
ATOM   3234 C CG  . GLU   B 1 8   ? 11.013  27.955  69.955 1.00 117.34 ? 8   GLU   B CG  1 
ATOM   3235 C CD  . GLU   B 1 8   ? 9.563   27.750  70.340 1.00 124.88 ? 8   GLU   B CD  1 
ATOM   3236 O OE1 . GLU   B 1 8   ? 8.852   28.755  70.549 1.00 120.66 ? 8   GLU   B OE1 1 
ATOM   3237 O OE2 . GLU   B 1 8   ? 9.134   26.581  70.438 1.00 132.15 ? 8   GLU   B OE2 1 
ATOM   3238 N N   . PHE   B 1 9   ? 13.339  31.801  70.237 1.00 107.49 ? 9   PHE   B N   1 
ATOM   3239 C CA  . PHE   B 1 9   ? 13.628  33.229  70.190 1.00 101.25 ? 9   PHE   B CA  1 
ATOM   3240 C C   . PHE   B 1 9   ? 15.102  33.556  70.396 1.00 91.49  ? 9   PHE   B C   1 
ATOM   3241 O O   . PHE   B 1 9   ? 15.453  34.736  70.493 1.00 105.27 ? 9   PHE   B O   1 
ATOM   3242 C CB  . PHE   B 1 9   ? 12.766  33.969  71.215 1.00 94.00  ? 9   PHE   B CB  1 
ATOM   3243 C CG  . PHE   B 1 9   ? 11.291  33.865  70.945 1.00 96.66  ? 9   PHE   B CG  1 
ATOM   3244 C CD1 . PHE   B 1 9   ? 10.484  33.049  71.720 1.00 93.04  ? 9   PHE   B CD1 1 
ATOM   3245 C CD2 . PHE   B 1 9   ? 10.706  34.611  69.933 1.00 101.14 ? 9   PHE   B CD2 1 
ATOM   3246 C CE1 . PHE   B 1 9   ? 9.125   32.956  71.473 1.00 110.59 ? 9   PHE   B CE1 1 
ATOM   3247 C CE2 . PHE   B 1 9   ? 9.350   34.523  69.681 1.00 104.04 ? 9   PHE   B CE2 1 
ATOM   3248 C CZ  . PHE   B 1 9   ? 8.557   33.696  70.453 1.00 113.59 ? 9   PHE   B CZ  1 
ATOM   3249 N N   . ASP   B 1 10  ? 15.970  32.551  70.470 1.00 77.81  ? 10  ASP   B N   1 
ATOM   3250 C CA  . ASP   B 1 10  ? 17.403  32.777  70.624 1.00 70.87  ? 10  ASP   B CA  1 
ATOM   3251 C C   . ASP   B 1 10  ? 18.046  32.901  69.247 1.00 75.49  ? 10  ASP   B C   1 
ATOM   3252 O O   . ASP   B 1 10  ? 17.917  31.998  68.414 1.00 76.89  ? 10  ASP   B O   1 
ATOM   3253 C CB  . ASP   B 1 10  ? 18.054  31.648  71.417 1.00 82.87  ? 10  ASP   B CB  1 
ATOM   3254 C CG  . ASP   B 1 10  ? 19.515  31.915  71.715 1.00 84.84  ? 10  ASP   B CG  1 
ATOM   3255 O OD1 . ASP   B 1 10  ? 19.908  33.102  71.737 1.00 82.75  ? 10  ASP   B OD1 1 
ATOM   3256 O OD2 . ASP   B 1 10  ? 20.270  30.943  71.922 1.00 101.43 ? 10  ASP   B OD2 1 
ATOM   3257 N N   . CYS   B 1 11  ? 18.745  34.009  69.016 1.00 66.13  ? 11  CYS   B N   1 
ATOM   3258 C CA  . CYS   B 1 11  ? 19.416  34.271  67.752 1.00 51.03  ? 11  CYS   B CA  1 
ATOM   3259 C C   . CYS   B 1 11  ? 20.890  34.540  68.011 1.00 58.85  ? 11  CYS   B C   1 
ATOM   3260 O O   . CYS   B 1 11  ? 21.234  35.302  68.919 1.00 70.02  ? 11  CYS   B O   1 
ATOM   3261 C CB  . CYS   B 1 11  ? 18.777  35.458  67.025 1.00 60.56  ? 11  CYS   B CB  1 
ATOM   3262 S SG  . CYS   B 1 11  ? 19.351  35.686  65.326 1.00 73.91  ? 11  CYS   B SG  1 
ATOM   3263 N N   . HIS   B 1 12  ? 21.753  33.918  67.214 1.00 65.25  ? 12  HIS   B N   1 
ATOM   3264 C CA  . HIS   B 1 12  ? 23.194  34.055  67.354 1.00 62.11  ? 12  HIS   B CA  1 
ATOM   3265 C C   . HIS   B 1 12  ? 23.745  35.013  66.304 1.00 69.24  ? 12  HIS   B C   1 
ATOM   3266 O O   . HIS   B 1 12  ? 23.227  35.107  65.189 1.00 70.33  ? 12  HIS   B O   1 
ATOM   3267 C CB  . HIS   B 1 12  ? 23.888  32.697  67.223 1.00 58.24  ? 12  HIS   B CB  1 
ATOM   3268 C CG  . HIS   B 1 12  ? 23.359  31.652  68.156 1.00 73.67  ? 12  HIS   B CG  1 
ATOM   3269 N ND1 . HIS   B 1 12  ? 24.014  31.286  69.312 1.00 74.56  ? 12  HIS   B ND1 1 
ATOM   3270 C CD2 . HIS   B 1 12  ? 22.237  30.894  68.104 1.00 78.21  ? 12  HIS   B CD2 1 
ATOM   3271 C CE1 . HIS   B 1 12  ? 23.321  30.346  69.930 1.00 75.40  ? 12  HIS   B CE1 1 
ATOM   3272 N NE2 . HIS   B 1 12  ? 22.238  30.091  69.218 1.00 75.56  ? 12  HIS   B NE2 1 
ATOM   3273 N N   . PHE   B 1 13  ? 24.803  35.730  66.679 1.00 75.50  ? 13  PHE   B N   1 
ATOM   3274 C CA  . PHE   B 1 13  ? 25.456  36.647  65.753 1.00 69.79  ? 13  PHE   B CA  1 
ATOM   3275 C C   . PHE   B 1 13  ? 26.272  35.888  64.715 1.00 67.79  ? 13  PHE   B C   1 
ATOM   3276 O O   . PHE   B 1 13  ? 26.971  34.921  65.031 1.00 62.13  ? 13  PHE   B O   1 
ATOM   3277 C CB  . PHE   B 1 13  ? 26.361  37.617  66.510 1.00 60.50  ? 13  PHE   B CB  1 
ATOM   3278 C CG  . PHE   B 1 13  ? 25.738  38.958  66.759 1.00 73.17  ? 13  PHE   B CG  1 
ATOM   3279 C CD1 . PHE   B 1 13  ? 25.925  40.000  65.865 1.00 72.75  ? 13  PHE   B CD1 1 
ATOM   3280 C CD2 . PHE   B 1 13  ? 24.963  39.178  67.885 1.00 69.72  ? 13  PHE   B CD2 1 
ATOM   3281 C CE1 . PHE   B 1 13  ? 25.353  41.238  66.091 1.00 70.90  ? 13  PHE   B CE1 1 
ATOM   3282 C CE2 . PHE   B 1 13  ? 24.388  40.412  68.116 1.00 64.33  ? 13  PHE   B CE2 1 
ATOM   3283 C CZ  . PHE   B 1 13  ? 24.583  41.444  67.219 1.00 62.84  ? 13  PHE   B CZ  1 
ATOM   3284 N N   . LEU   B 1 14  ? 26.190  36.346  63.470 1.00 75.51  ? 14  LEU   B N   1 
ATOM   3285 C CA  . LEU   B 1 14  ? 27.014  35.844  62.378 1.00 86.12  ? 14  LEU   B CA  1 
ATOM   3286 C C   . LEU   B 1 14  ? 28.062  36.906  62.071 1.00 88.95  ? 14  LEU   B C   1 
ATOM   3287 O O   . LEU   B 1 14  ? 27.737  37.972  61.538 1.00 95.37  ? 14  LEU   B O   1 
ATOM   3288 C CB  . LEU   B 1 14  ? 26.160  35.523  61.152 1.00 87.07  ? 14  LEU   B CB  1 
ATOM   3289 C CG  . LEU   B 1 14  ? 26.858  34.852  59.967 1.00 87.54  ? 14  LEU   B CG  1 
ATOM   3290 C CD1 . LEU   B 1 14  ? 27.489  33.541  60.397 1.00 83.52  ? 14  LEU   B CD1 1 
ATOM   3291 C CD2 . LEU   B 1 14  ? 25.876  34.626  58.826 1.00 76.58  ? 14  LEU   B CD2 1 
ATOM   3292 N N   . ASP   B 1 15  ? 29.316  36.612  62.402 1.00 94.34  ? 15  ASP   B N   1 
ATOM   3293 C CA  . ASP   B 1 15  ? 30.373  37.600  62.263 1.00 102.77 ? 15  ASP   B CA  1 
ATOM   3294 C C   . ASP   B 1 15  ? 30.705  37.833  60.792 1.00 104.36 ? 15  ASP   B C   1 
ATOM   3295 O O   . ASP   B 1 15  ? 30.375  37.030  59.913 1.00 99.12  ? 15  ASP   B O   1 
ATOM   3296 C CB  . ASP   B 1 15  ? 31.622  37.162  63.030 1.00 104.78 ? 15  ASP   B CB  1 
ATOM   3297 C CG  . ASP   B 1 15  ? 31.410  37.153  64.535 1.00 118.53 ? 15  ASP   B CG  1 
ATOM   3298 O OD1 . ASP   B 1 15  ? 30.540  37.908  65.019 1.00 112.83 ? 15  ASP   B OD1 1 
ATOM   3299 O OD2 . ASP   B 1 15  ? 32.117  36.398  65.235 1.00 118.75 ? 15  ASP   B OD2 1 
ATOM   3300 N N   . GLU   B 1 16  ? 31.345  38.972  60.533 1.00 114.82 ? 16  GLU   B N   1 
ATOM   3301 C CA  . GLU   B 1 16  ? 31.709  39.347  59.173 1.00 114.39 ? 16  GLU   B CA  1 
ATOM   3302 C C   . GLU   B 1 16  ? 32.586  38.278  58.535 1.00 108.98 ? 16  GLU   B C   1 
ATOM   3303 O O   . GLU   B 1 16  ? 33.499  37.737  59.166 1.00 105.93 ? 16  GLU   B O   1 
ATOM   3304 C CB  . GLU   B 1 16  ? 32.442  40.690  59.177 1.00 117.27 ? 16  GLU   B CB  1 
ATOM   3305 C CG  . GLU   B 1 16  ? 31.582  41.875  59.589 1.00 118.47 ? 16  GLU   B CG  1 
ATOM   3306 C CD  . GLU   B 1 16  ? 32.366  43.172  59.651 1.00 129.75 ? 16  GLU   B CD  1 
ATOM   3307 O OE1 . GLU   B 1 16  ? 33.611  43.124  59.559 1.00 122.89 ? 16  GLU   B OE1 1 
ATOM   3308 O OE2 . GLU   B 1 16  ? 31.737  44.241  59.792 1.00 130.27 ? 16  GLU   B OE2 1 
ATOM   3309 N N   . GLY   B 1 17  ? 32.305  37.976  57.269 1.00 98.29  ? 17  GLY   B N   1 
ATOM   3310 C CA  . GLY   B 1 17  ? 33.055  36.970  56.549 1.00 100.08 ? 17  GLY   B CA  1 
ATOM   3311 C C   . GLY   B 1 17  ? 32.664  35.540  56.839 1.00 104.28 ? 17  GLY   B C   1 
ATOM   3312 O O   . GLY   B 1 17  ? 33.331  34.623  56.344 1.00 100.87 ? 17  GLY   B O   1 
ATOM   3313 N N   . PHE   B 1 18  ? 31.611  35.313  57.618 1.00 106.71 ? 18  PHE   B N   1 
ATOM   3314 C CA  . PHE   B 1 18  ? 31.172  33.970  57.971 1.00 102.33 ? 18  PHE   B CA  1 
ATOM   3315 C C   . PHE   B 1 18  ? 29.826  33.663  57.330 1.00 101.52 ? 18  PHE   B C   1 
ATOM   3316 O O   . PHE   B 1 18  ? 28.946  34.527  57.257 1.00 111.36 ? 18  PHE   B O   1 
ATOM   3317 C CB  . PHE   B 1 18  ? 31.068  33.804  59.489 1.00 97.13  ? 18  PHE   B CB  1 
ATOM   3318 C CG  . PHE   B 1 18  ? 32.395  33.696  60.179 1.00 105.91 ? 18  PHE   B CG  1 
ATOM   3319 C CD1 . PHE   B 1 18  ? 33.147  34.827  60.448 1.00 111.07 ? 18  PHE   B CD1 1 
ATOM   3320 C CD2 . PHE   B 1 18  ? 32.895  32.460  60.553 1.00 109.23 ? 18  PHE   B CD2 1 
ATOM   3321 C CE1 . PHE   B 1 18  ? 34.370  34.728  61.084 1.00 110.67 ? 18  PHE   B CE1 1 
ATOM   3322 C CE2 . PHE   B 1 18  ? 34.118  32.355  61.186 1.00 102.87 ? 18  PHE   B CE2 1 
ATOM   3323 C CZ  . PHE   B 1 18  ? 34.855  33.490  61.453 1.00 104.57 ? 18  PHE   B CZ  1 
ATOM   3324 N N   . THR   B 1 19  ? 29.679  32.428  56.864 1.00 96.70  ? 19  THR   B N   1 
ATOM   3325 C CA  . THR   B 1 19  ? 28.438  31.911  56.309 1.00 99.12  ? 19  THR   B CA  1 
ATOM   3326 C C   . THR   B 1 19  ? 27.917  30.785  57.194 1.00 103.68 ? 19  THR   B C   1 
ATOM   3327 O O   . THR   B 1 19  ? 28.595  30.324  58.117 1.00 105.01 ? 19  THR   B O   1 
ATOM   3328 C CB  . THR   B 1 19  ? 28.636  31.413  54.872 1.00 97.19  ? 19  THR   B CB  1 
ATOM   3329 O OG1 . THR   B 1 19  ? 29.477  30.254  54.880 1.00 98.69  ? 19  THR   B OG1 1 
ATOM   3330 C CG2 . THR   B 1 19  ? 29.279  32.496  54.020 1.00 91.82  ? 19  THR   B CG2 1 
ATOM   3331 N N   . ALA   B 1 20  ? 26.683  30.355  56.910 1.00 99.63  ? 20  ALA   B N   1 
ATOM   3332 C CA  . ALA   B 1 20  ? 26.100  29.226  57.630 1.00 99.03  ? 20  ALA   B CA  1 
ATOM   3333 C C   . ALA   B 1 20  ? 26.994  27.993  57.577 1.00 103.61 ? 20  ALA   B C   1 
ATOM   3334 O O   . ALA   B 1 20  ? 27.046  27.220  58.541 1.00 96.51  ? 20  ALA   B O   1 
ATOM   3335 C CB  . ALA   B 1 20  ? 24.716  28.901  57.064 1.00 88.83  ? 20  ALA   B CB  1 
ATOM   3336 N N   . LYS   B 1 21  ? 27.699  27.790  56.460 1.00 96.10  ? 21  LYS   B N   1 
ATOM   3337 C CA  . LYS   B 1 21  ? 28.599  26.646  56.338 1.00 93.02  ? 21  LYS   B CA  1 
ATOM   3338 C C   . LYS   B 1 21  ? 29.708  26.705  57.382 1.00 92.90  ? 21  LYS   B C   1 
ATOM   3339 O O   . LYS   B 1 21  ? 30.065  25.685  57.985 1.00 92.46  ? 21  LYS   B O   1 
ATOM   3340 C CB  . LYS   B 1 21  ? 29.194  26.599  54.931 1.00 97.83  ? 21  LYS   B CB  1 
ATOM   3341 C CG  . LYS   B 1 21  ? 28.160  26.616  53.816 1.00 112.40 ? 21  LYS   B CG  1 
ATOM   3342 C CD  . LYS   B 1 21  ? 28.820  26.519  52.448 1.00 102.37 ? 21  LYS   B CD  1 
ATOM   3343 C CE  . LYS   B 1 21  ? 27.820  26.119  51.374 1.00 104.84 ? 21  LYS   B CE  1 
ATOM   3344 N NZ  . LYS   B 1 21  ? 28.450  26.027  50.026 1.00 92.89  ? 21  LYS   B NZ  1 
ATOM   3345 N N   . ASP   B 1 22  ? 30.279  27.892  57.592 1.00 100.33 ? 22  ASP   B N   1 
ATOM   3346 C CA  . ASP   B 1 22  ? 31.331  28.041  58.591 1.00 94.40  ? 22  ASP   B CA  1 
ATOM   3347 C C   . ASP   B 1 22  ? 30.798  27.787  59.996 1.00 86.37  ? 22  ASP   B C   1 
ATOM   3348 O O   . ASP   B 1 22  ? 31.493  27.195  60.830 1.00 88.11  ? 22  ASP   B O   1 
ATOM   3349 C CB  . ASP   B 1 22  ? 31.951  29.433  58.488 1.00 101.32 ? 22  ASP   B CB  1 
ATOM   3350 C CG  . ASP   B 1 22  ? 32.461  29.738  57.093 1.00 103.83 ? 22  ASP   B CG  1 
ATOM   3351 O OD1 . ASP   B 1 22  ? 32.173  30.839  56.577 1.00 108.27 ? 22  ASP   B OD1 1 
ATOM   3352 O OD2 . ASP   B 1 22  ? 33.137  28.868  56.505 1.00 91.82  ? 22  ASP   B OD2 1 
ATOM   3353 N N   . ILE   B 1 23  ? 29.573  28.236  60.279 1.00 87.40  ? 23  ILE   B N   1 
ATOM   3354 C CA  . ILE   B 1 23  ? 28.955  27.949  61.572 1.00 95.61  ? 23  ILE   B CA  1 
ATOM   3355 C C   . ILE   B 1 23  ? 28.765  26.447  61.747 1.00 89.33  ? 23  ILE   B C   1 
ATOM   3356 O O   . ILE   B 1 23  ? 28.964  25.902  62.841 1.00 89.74  ? 23  ILE   B O   1 
ATOM   3357 C CB  . ILE   B 1 23  ? 27.627  28.716  61.710 1.00 98.01  ? 23  ILE   B CB  1 
ATOM   3358 C CG1 . ILE   B 1 23  ? 27.892  30.217  61.830 1.00 90.92  ? 23  ILE   B CG1 1 
ATOM   3359 C CG2 . ILE   B 1 23  ? 26.844  28.227  62.918 1.00 77.52  ? 23  ILE   B CG2 1 
ATOM   3360 C CD1 . ILE   B 1 23  ? 28.779  30.588  62.997 1.00 81.44  ? 23  ILE   B CD1 1 
ATOM   3361 N N   . LEU   B 1 24  ? 28.368  25.757  60.674 1.00 84.07  ? 24  LEU   B N   1 
ATOM   3362 C CA  . LEU   B 1 24  ? 28.281  24.299  60.710 1.00 86.16  ? 24  LEU   B CA  1 
ATOM   3363 C C   . LEU   B 1 24  ? 29.628  23.679  61.056 1.00 100.06 ? 24  LEU   B C   1 
ATOM   3364 O O   . LEU   B 1 24  ? 29.716  22.785  61.907 1.00 90.74  ? 24  LEU   B O   1 
ATOM   3365 C CB  . LEU   B 1 24  ? 27.795  23.772  59.361 1.00 76.35  ? 24  LEU   B CB  1 
ATOM   3366 C CG  . LEU   B 1 24  ? 26.307  23.796  59.037 1.00 86.01  ? 24  LEU   B CG  1 
ATOM   3367 C CD1 . LEU   B 1 24  ? 26.127  23.414  57.588 1.00 85.16  ? 24  LEU   B CD1 1 
ATOM   3368 C CD2 . LEU   B 1 24  ? 25.565  22.825  59.934 1.00 91.29  ? 24  LEU   B CD2 1 
ATOM   3369 N N   . ASP   B 1 25  ? 30.683  24.121  60.369 1.00 93.90  ? 25  ASP   B N   1 
ATOM   3370 C CA  . ASP   B 1 25  ? 32.026  23.618  60.644 1.00 99.10  ? 25  ASP   B CA  1 
ATOM   3371 C C   . ASP   B 1 25  ? 32.402  23.828  62.105 1.00 94.00  ? 25  ASP   B C   1 
ATOM   3372 O O   . ASP   B 1 25  ? 32.934  22.923  62.759 1.00 84.63  ? 25  ASP   B O   1 
ATOM   3373 C CB  . ASP   B 1 25  ? 33.036  24.302  59.724 1.00 92.99  ? 25  ASP   B CB  1 
ATOM   3374 C CG  . ASP   B 1 25  ? 32.870  23.896  58.276 1.00 96.22  ? 25  ASP   B CG  1 
ATOM   3375 O OD1 . ASP   B 1 25  ? 31.888  23.189  57.969 1.00 94.38  ? 25  ASP   B OD1 1 
ATOM   3376 O OD2 . ASP   B 1 25  ? 33.720  24.283  57.447 1.00 106.36 ? 25  ASP   B OD2 1 
ATOM   3377 N N   . GLN   B 1 26  ? 32.128  25.023  62.633 1.00 84.41  ? 26  GLN   B N   1 
ATOM   3378 C CA  . GLN   B 1 26  ? 32.460  25.324  64.023 1.00 89.26  ? 26  GLN   B CA  1 
ATOM   3379 C C   . GLN   B 1 26  ? 31.707  24.409  64.979 1.00 100.39 ? 26  GLN   B C   1 
ATOM   3380 O O   . GLN   B 1 26  ? 32.301  23.827  65.893 1.00 113.39 ? 26  GLN   B O   1 
ATOM   3381 C CB  . GLN   B 1 26  ? 32.164  26.790  64.338 1.00 102.09 ? 26  GLN   B CB  1 
ATOM   3382 C CG  . GLN   B 1 26  ? 33.121  27.776  63.696 1.00 106.34 ? 26  GLN   B CG  1 
ATOM   3383 C CD  . GLN   B 1 26  ? 32.790  29.213  64.046 1.00 102.36 ? 26  GLN   B CD  1 
ATOM   3384 O OE1 . GLN   B 1 26  ? 32.150  29.485  65.061 1.00 103.03 ? 26  GLN   B OE1 1 
ATOM   3385 N NE2 . GLN   B 1 26  ? 33.224  30.140  63.203 1.00 89.68  ? 26  GLN   B NE2 1 
ATOM   3386 N N   . LYS   B 1 27  ? 30.386  24.300  64.804 1.00 89.84  ? 27  LYS   B N   1 
ATOM   3387 C CA  . LYS   B 1 27  ? 29.590  23.440  65.677 1.00 98.57  ? 27  LYS   B CA  1 
ATOM   3388 C C   . LYS   B 1 27  ? 30.067  21.995  65.623 1.00 101.59 ? 27  LYS   B C   1 
ATOM   3389 O O   . LYS   B 1 27  ? 30.114  21.311  66.653 1.00 101.78 ? 27  LYS   B O   1 
ATOM   3390 C CB  . LYS   B 1 27  ? 28.111  23.531  65.299 1.00 101.48 ? 27  LYS   B CB  1 
ATOM   3391 C CG  . LYS   B 1 27  ? 27.170  22.792  66.246 1.00 84.21  ? 27  LYS   B CG  1 
ATOM   3392 C CD  . LYS   B 1 27  ? 27.354  23.190  67.699 1.00 102.33 ? 27  LYS   B CD  1 
ATOM   3393 C CE  . LYS   B 1 27  ? 26.421  22.383  68.592 1.00 88.84  ? 27  LYS   B CE  1 
ATOM   3394 N NZ  . LYS   B 1 27  ? 26.572  22.735  70.029 1.00 86.18  ? 27  LYS   B NZ  1 
ATOM   3395 N N   . ILE   B 1 28  ? 30.418  21.508  64.431 1.00 100.31 ? 28  ILE   B N   1 
ATOM   3396 C CA  . ILE   B 1 28  ? 30.896  20.135  64.304 1.00 91.80  ? 28  ILE   B CA  1 
ATOM   3397 C C   . ILE   B 1 28  ? 32.222  19.960  65.039 1.00 106.77 ? 28  ILE   B C   1 
ATOM   3398 O O   . ILE   B 1 28  ? 32.420  18.984  65.773 1.00 112.06 ? 28  ILE   B O   1 
ATOM   3399 C CB  . ILE   B 1 28  ? 31.011  19.746  62.820 1.00 81.22  ? 28  ILE   B CB  1 
ATOM   3400 C CG1 . ILE   B 1 28  ? 29.618  19.584  62.209 1.00 69.69  ? 28  ILE   B CG1 1 
ATOM   3401 C CG2 . ILE   B 1 28  ? 31.813  18.468  62.665 1.00 77.97  ? 28  ILE   B CG2 1 
ATOM   3402 C CD1 . ILE   B 1 28  ? 29.630  19.314  60.723 1.00 80.40  ? 28  ILE   B CD1 1 
ATOM   3403 N N   . ASN   B 1 29  ? 33.148  20.905  64.855 1.00 103.19 ? 29  ASN   B N   1 
ATOM   3404 C CA  . ASN   B 1 29  ? 34.434  20.834  65.544 1.00 91.48  ? 29  ASN   B CA  1 
ATOM   3405 C C   . ASN   B 1 29  ? 34.277  20.928  67.058 1.00 98.72  ? 29  ASN   B C   1 
ATOM   3406 O O   . ASN   B 1 29  ? 35.080  20.353  67.802 1.00 103.23 ? 29  ASN   B O   1 
ATOM   3407 C CB  . ASN   B 1 29  ? 35.361  21.940  65.038 1.00 97.86  ? 29  ASN   B CB  1 
ATOM   3408 C CG  . ASN   B 1 29  ? 35.616  21.850  63.544 1.00 111.33 ? 29  ASN   B CG  1 
ATOM   3409 O OD1 . ASN   B 1 29  ? 35.450  20.792  62.936 1.00 105.06 ? 29  ASN   B OD1 1 
ATOM   3410 N ND2 . ASN   B 1 29  ? 36.018  22.965  62.944 1.00 98.35  ? 29  ASN   B ND2 1 
ATOM   3411 N N   . GLU   B 1 30  ? 33.259  21.651  67.530 1.00 109.66 ? 30  GLU   B N   1 
ATOM   3412 C CA  . GLU   B 1 30  ? 33.085  21.862  68.965 1.00 111.41 ? 30  GLU   B CA  1 
ATOM   3413 C C   . GLU   B 1 30  ? 32.742  20.567  69.696 1.00 109.12 ? 30  GLU   B C   1 
ATOM   3414 O O   . GLU   B 1 30  ? 33.198  20.347  70.824 1.00 111.36 ? 30  GLU   B O   1 
ATOM   3415 C CB  . GLU   B 1 30  ? 31.997  22.911  69.195 1.00 116.42 ? 30  GLU   B CB  1 
ATOM   3416 C CG  . GLU   B 1 30  ? 31.741  23.272  70.646 1.00 130.92 ? 30  GLU   B CG  1 
ATOM   3417 C CD  . GLU   B 1 30  ? 30.681  24.350  70.792 1.00 133.47 ? 30  GLU   B CD  1 
ATOM   3418 O OE1 . GLU   B 1 30  ? 30.132  24.791  69.761 1.00 115.23 ? 30  GLU   B OE1 1 
ATOM   3419 O OE2 . GLU   B 1 30  ? 30.383  24.743  71.939 1.00 147.10 ? 30  GLU   B OE2 1 
ATOM   3420 N N   . VAL   B 1 31  ? 31.950  19.698  69.075 1.00 107.48 ? 31  VAL   B N   1 
ATOM   3421 C CA  . VAL   B 1 31  ? 31.546  18.440  69.690 1.00 107.86 ? 31  VAL   B CA  1 
ATOM   3422 C C   . VAL   B 1 31  ? 32.414  17.276  69.206 1.00 111.06 ? 31  VAL   B C   1 
ATOM   3423 O O   . VAL   B 1 31  ? 32.013  16.118  69.314 1.00 102.98 ? 31  VAL   B O   1 
ATOM   3424 C CB  . VAL   B 1 31  ? 30.054  18.157  69.462 1.00 103.15 ? 31  VAL   B CB  1 
ATOM   3425 C CG1 . VAL   B 1 31  ? 29.205  19.180  70.200 1.00 103.23 ? 31  VAL   B CG1 1 
ATOM   3426 C CG2 . VAL   B 1 31  ? 29.737  18.173  67.977 1.00 93.41  ? 31  VAL   B CG2 1 
ATOM   3427 N N   . SER   B 1 32  ? 33.600  17.575  68.670 1.00 121.35 ? 32  SER   B N   1 
ATOM   3428 C CA  . SER   B 1 32  ? 34.450  16.553  68.063 1.00 117.01 ? 32  SER   B CA  1 
ATOM   3429 C C   . SER   B 1 32  ? 34.839  15.458  69.049 1.00 114.55 ? 32  SER   B C   1 
ATOM   3430 O O   . SER   B 1 32  ? 34.984  14.295  68.655 1.00 109.70 ? 32  SER   B O   1 
ATOM   3431 C CB  . SER   B 1 32  ? 35.705  17.200  67.476 1.00 110.60 ? 32  SER   B CB  1 
ATOM   3432 O OG  . SER   B 1 32  ? 36.439  16.269  66.701 1.00 118.02 ? 32  SER   B OG  1 
ATOM   3433 N N   . SER   B 1 33  ? 35.005  15.798  70.324 1.00 122.28 ? 33  SER   B N   1 
ATOM   3434 C CA  . SER   B 1 33  ? 35.517  14.879  71.334 1.00 108.04 ? 33  SER   B CA  1 
ATOM   3435 C C   . SER   B 1 33  ? 34.467  14.543  72.390 1.00 114.31 ? 33  SER   B C   1 
ATOM   3436 O O   . SER   B 1 33  ? 34.781  14.367  73.569 1.00 125.08 ? 33  SER   B O   1 
ATOM   3437 C CB  . SER   B 1 33  ? 36.767  15.452  71.995 1.00 109.79 ? 33  SER   B CB  1 
ATOM   3438 O OG  . SER   B 1 33  ? 36.636  16.850  72.194 1.00 120.21 ? 33  SER   B OG  1 
ATOM   3439 N N   . SER   B 1 34  ? 33.206  14.453  71.975 1.00 111.54 ? 34  SER   B N   1 
ATOM   3440 C CA  . SER   B 1 34  ? 32.117  14.091  72.868 1.00 114.90 ? 34  SER   B CA  1 
ATOM   3441 C C   . SER   B 1 34  ? 31.129  13.220  72.105 1.00 123.90 ? 34  SER   B C   1 
ATOM   3442 O O   . SER   B 1 34  ? 31.142  13.166  70.874 1.00 116.41 ? 34  SER   B O   1 
ATOM   3443 C CB  . SER   B 1 34  ? 31.416  15.330  73.441 1.00 109.84 ? 34  SER   B CB  1 
ATOM   3444 O OG  . SER   B 1 34  ? 30.557  15.921  72.483 1.00 116.24 ? 34  SER   B OG  1 
ATOM   3445 N N   . ASP   B 1 35  ? 30.272  12.528  72.853 1.00 133.25 ? 35  ASP   B N   1 
ATOM   3446 C CA  . ASP   B 1 35  ? 29.330  11.573  72.283 1.00 127.65 ? 35  ASP   B CA  1 
ATOM   3447 C C   . ASP   B 1 35  ? 27.923  12.131  72.116 1.00 116.48 ? 35  ASP   B C   1 
ATOM   3448 O O   . ASP   B 1 35  ? 27.030  11.393  71.685 1.00 105.97 ? 35  ASP   B O   1 
ATOM   3449 C CB  . ASP   B 1 35  ? 29.281  10.301  73.137 1.00 124.37 ? 35  ASP   B CB  1 
ATOM   3450 C CG  . ASP   B 1 35  ? 30.560  9.490   73.052 1.00 119.91 ? 35  ASP   B CG  1 
ATOM   3451 O OD1 . ASP   B 1 35  ? 31.003  8.965   74.095 1.00 121.45 ? 35  ASP   B OD1 1 
ATOM   3452 O OD2 . ASP   B 1 35  ? 31.121  9.374   71.941 1.00 102.29 ? 35  ASP   B OD2 1 
ATOM   3453 N N   . ASP   B 1 36  ? 27.697  13.404  72.436 1.00 110.21 ? 36  ASP   B N   1 
ATOM   3454 C CA  . ASP   B 1 36  ? 26.408  14.037  72.157 1.00 104.89 ? 36  ASP   B CA  1 
ATOM   3455 C C   . ASP   B 1 36  ? 26.487  14.725  70.798 1.00 112.61 ? 36  ASP   B C   1 
ATOM   3456 O O   . ASP   B 1 36  ? 26.916  15.872  70.666 1.00 104.37 ? 36  ASP   B O   1 
ATOM   3457 C CB  . ASP   B 1 36  ? 26.020  14.996  73.278 1.00 109.56 ? 36  ASP   B CB  1 
ATOM   3458 C CG  . ASP   B 1 36  ? 27.093  16.031  73.575 1.00 121.06 ? 36  ASP   B CG  1 
ATOM   3459 O OD1 . ASP   B 1 36  ? 28.205  15.930  73.015 1.00 120.79 ? 36  ASP   B OD1 1 
ATOM   3460 O OD2 . ASP   B 1 36  ? 26.820  16.952  74.373 1.00 132.35 ? 36  ASP   B OD2 1 
ATOM   3461 N N   . LYS   B 1 37  ? 26.048  14.003  69.771 1.00 93.43  ? 37  LYS   B N   1 
ATOM   3462 C CA  . LYS   B 1 37  ? 26.135  14.426  68.379 1.00 69.93  ? 37  LYS   B CA  1 
ATOM   3463 C C   . LYS   B 1 37  ? 24.764  14.361  67.722 1.00 69.95  ? 37  LYS   B C   1 
ATOM   3464 O O   . LYS   B 1 37  ? 24.588  13.797  66.641 1.00 71.94  ? 37  LYS   B O   1 
ATOM   3465 C CB  . LYS   B 1 37  ? 27.146  13.578  67.613 1.00 74.14  ? 37  LYS   B CB  1 
ATOM   3466 C CG  . LYS   B 1 37  ? 28.572  13.668  68.135 1.00 75.65  ? 37  LYS   B CG  1 
ATOM   3467 C CD  . LYS   B 1 37  ? 29.505  12.791  67.316 1.00 81.72  ? 37  LYS   B CD  1 
ATOM   3468 C CE  . LYS   B 1 37  ? 30.952  12.959  67.745 1.00 88.72  ? 37  LYS   B CE  1 
ATOM   3469 N NZ  . LYS   B 1 37  ? 31.595  11.661  68.085 1.00 99.56  ? 37  LYS   B NZ  1 
ATOM   3470 N N   . ASP   B 1 38  ? 23.763  14.930  68.389 1.00 69.23  ? 38  ASP   B N   1 
ATOM   3471 C CA  . ASP   B 1 38  ? 22.421  14.986  67.825 1.00 61.64  ? 38  ASP   B CA  1 
ATOM   3472 C C   . ASP   B 1 38  ? 22.399  15.837  66.559 1.00 55.94  ? 38  ASP   B C   1 
ATOM   3473 O O   . ASP   B 1 38  ? 23.181  16.778  66.399 1.00 68.57  ? 38  ASP   B O   1 
ATOM   3474 C CB  . ASP   B 1 38  ? 21.437  15.545  68.852 1.00 78.14  ? 38  ASP   B CB  1 
ATOM   3475 C CG  . ASP   B 1 38  ? 21.336  14.682  70.098 1.00 89.53  ? 38  ASP   B CG  1 
ATOM   3476 O OD1 . ASP   B 1 38  ? 21.580  13.460  70.005 1.00 91.89  ? 38  ASP   B OD1 1 
ATOM   3477 O OD2 . ASP   B 1 38  ? 21.012  15.229  71.172 1.00 93.56  ? 38  ASP   B OD2 1 
ATOM   3478 N N   . ALA   B 1 39  ? 21.486  15.495  65.652 1.00 56.00  ? 39  ALA   B N   1 
ATOM   3479 C CA  . ALA   B 1 39  ? 21.313  16.267  64.428 1.00 52.38  ? 39  ALA   B CA  1 
ATOM   3480 C C   . ALA   B 1 39  ? 20.832  17.676  64.751 1.00 46.05  ? 39  ALA   B C   1 
ATOM   3481 O O   . ALA   B 1 39  ? 20.131  17.904  65.741 1.00 55.58  ? 39  ALA   B O   1 
ATOM   3482 C CB  . ALA   B 1 39  ? 20.319  15.572  63.497 1.00 53.69  ? 39  ALA   B CB  1 
ATOM   3483 N N   . PHE   B 1 40  ? 21.210  18.633  63.907 1.00 49.79  ? 40  PHE   B N   1 
ATOM   3484 C CA  . PHE   B 1 40  ? 20.812  20.009  64.165 1.00 53.21  ? 40  PHE   B CA  1 
ATOM   3485 C C   . PHE   B 1 40  ? 20.708  20.788  62.862 1.00 56.53  ? 40  PHE   B C   1 
ATOM   3486 O O   . PHE   B 1 40  ? 21.353  20.468  61.863 1.00 60.45  ? 40  PHE   B O   1 
ATOM   3487 C CB  . PHE   B 1 40  ? 21.793  20.703  65.120 1.00 51.59  ? 40  PHE   B CB  1 
ATOM   3488 C CG  . PHE   B 1 40  ? 23.178  20.849  64.562 1.00 56.59  ? 40  PHE   B CG  1 
ATOM   3489 C CD1 . PHE   B 1 40  ? 24.086  19.808  64.651 1.00 70.23  ? 40  PHE   B CD1 1 
ATOM   3490 C CD2 . PHE   B 1 40  ? 23.571  22.025  63.947 1.00 64.61  ? 40  PHE   B CD2 1 
ATOM   3491 C CE1 . PHE   B 1 40  ? 25.360  19.936  64.136 1.00 64.90  ? 40  PHE   B CE1 1 
ATOM   3492 C CE2 . PHE   B 1 40  ? 24.845  22.158  63.429 1.00 70.81  ? 40  PHE   B CE2 1 
ATOM   3493 C CZ  . PHE   B 1 40  ? 25.739  21.111  63.524 1.00 68.45  ? 40  PHE   B CZ  1 
ATOM   3494 N N   . TYR   B 1 41  ? 19.891  21.834  62.903 1.00 53.96  ? 41  TYR   B N   1 
ATOM   3495 C CA  . TYR   B 1 41  ? 19.727  22.774  61.806 1.00 51.14  ? 41  TYR   B CA  1 
ATOM   3496 C C   . TYR   B 1 41  ? 20.523  24.040  62.080 1.00 57.18  ? 41  TYR   B C   1 
ATOM   3497 O O   . TYR   B 1 41  ? 20.614  24.490  63.225 1.00 57.07  ? 41  TYR   B O   1 
ATOM   3498 C CB  . TYR   B 1 41  ? 18.258  23.159  61.623 1.00 68.01  ? 41  TYR   B CB  1 
ATOM   3499 C CG  . TYR   B 1 41  ? 17.411  22.168  60.874 1.00 62.78  ? 41  TYR   B CG  1 
ATOM   3500 C CD1 . TYR   B 1 41  ? 17.350  22.198  59.488 1.00 65.12  ? 41  TYR   B CD1 1 
ATOM   3501 C CD2 . TYR   B 1 41  ? 16.646  21.224  61.546 1.00 60.63  ? 41  TYR   B CD2 1 
ATOM   3502 C CE1 . TYR   B 1 41  ? 16.568  21.309  58.790 1.00 64.19  ? 41  TYR   B CE1 1 
ATOM   3503 C CE2 . TYR   B 1 41  ? 15.860  20.325  60.853 1.00 57.22  ? 41  TYR   B CE2 1 
ATOM   3504 C CZ  . TYR   B 1 41  ? 15.826  20.376  59.473 1.00 65.18  ? 41  TYR   B CZ  1 
ATOM   3505 O OH  . TYR   B 1 41  ? 15.050  19.497  58.760 1.00 72.55  ? 41  TYR   B OH  1 
ATOM   3506 N N   . VAL   B 1 42  ? 21.073  24.624  61.021 1.00 60.61  ? 42  VAL   B N   1 
ATOM   3507 C CA  . VAL   B 1 42  ? 21.533  26.008  61.029 1.00 58.07  ? 42  VAL   B CA  1 
ATOM   3508 C C   . VAL   B 1 42  ? 20.620  26.792  60.098 1.00 60.74  ? 42  VAL   B C   1 
ATOM   3509 O O   . VAL   B 1 42  ? 20.519  26.476  58.904 1.00 63.10  ? 42  VAL   B O   1 
ATOM   3510 C CB  . VAL   B 1 42  ? 23.004  26.131  60.609 1.00 59.98  ? 42  VAL   B CB  1 
ATOM   3511 C CG1 . VAL   B 1 42  ? 23.382  27.594  60.446 1.00 58.29  ? 42  VAL   B CG1 1 
ATOM   3512 C CG2 . VAL   B 1 42  ? 23.893  25.474  61.647 1.00 62.79  ? 42  VAL   B CG2 1 
ATOM   3513 N N   . ALA   B 1 43  ? 19.950  27.805  60.645 1.00 53.01  ? 43  ALA   B N   1 
ATOM   3514 C CA  . ALA   B 1 43  ? 18.973  28.604  59.913 1.00 59.84  ? 43  ALA   B CA  1 
ATOM   3515 C C   . ALA   B 1 43  ? 19.480  30.036  59.822 1.00 51.36  ? 43  ALA   B C   1 
ATOM   3516 O O   . ALA   B 1 43  ? 19.567  30.734  60.838 1.00 58.67  ? 43  ALA   B O   1 
ATOM   3517 C CB  . ALA   B 1 43  ? 17.606  28.548  60.594 1.00 55.90  ? 43  ALA   B CB  1 
ATOM   3518 N N   . ASP   B 1 44  ? 19.801  30.476  58.607 1.00 58.85  ? 44  ASP   B N   1 
ATOM   3519 C CA  . ASP   B 1 44  ? 20.312  31.824  58.370 1.00 66.50  ? 44  ASP   B CA  1 
ATOM   3520 C C   . ASP   B 1 44  ? 19.131  32.720  58.015 1.00 60.76  ? 44  ASP   B C   1 
ATOM   3521 O O   . ASP   B 1 44  ? 18.629  32.692  56.889 1.00 66.69  ? 44  ASP   B O   1 
ATOM   3522 C CB  . ASP   B 1 44  ? 21.364  31.813  57.265 1.00 72.63  ? 44  ASP   B CB  1 
ATOM   3523 C CG  . ASP   B 1 44  ? 22.044  33.159  57.086 1.00 80.90  ? 44  ASP   B CG  1 
ATOM   3524 O OD1 . ASP   B 1 44  ? 21.751  34.092  57.866 1.00 79.74  ? 44  ASP   B OD1 1 
ATOM   3525 O OD2 . ASP   B 1 44  ? 22.872  33.287  56.159 1.00 77.66  ? 44  ASP   B OD2 1 
ATOM   3526 N N   . LEU   B 1 45  ? 18.684  33.523  58.985 1.00 56.25  ? 45  LEU   B N   1 
ATOM   3527 C CA  . LEU   B 1 45  ? 17.594  34.463  58.739 1.00 57.12  ? 45  LEU   B CA  1 
ATOM   3528 C C   . LEU   B 1 45  ? 17.987  35.523  57.716 1.00 66.10  ? 45  LEU   B C   1 
ATOM   3529 O O   . LEU   B 1 45  ? 17.121  36.076  57.019 1.00 72.71  ? 45  LEU   B O   1 
ATOM   3530 C CB  . LEU   B 1 45  ? 17.162  35.108  60.057 1.00 60.56  ? 45  LEU   B CB  1 
ATOM   3531 C CG  . LEU   B 1 45  ? 16.779  34.126  61.172 1.00 63.32  ? 45  LEU   B CG  1 
ATOM   3532 C CD1 . LEU   B 1 45  ? 16.486  34.843  62.480 1.00 51.65  ? 45  LEU   B CD1 1 
ATOM   3533 C CD2 . LEU   B 1 45  ? 15.589  33.276  60.761 1.00 65.05  ? 45  LEU   B CD2 1 
ATOM   3534 N N   . GLY   B 1 46  ? 19.283  35.827  57.619 1.00 66.72  ? 46  GLY   B N   1 
ATOM   3535 C CA  . GLY   B 1 46  ? 19.744  36.733  56.584 1.00 64.75  ? 46  GLY   B CA  1 
ATOM   3536 C C   . GLY   B 1 46  ? 19.418  36.242  55.189 1.00 61.06  ? 46  GLY   B C   1 
ATOM   3537 O O   . GLY   B 1 46  ? 19.171  37.045  54.288 1.00 67.04  ? 46  GLY   B O   1 
ATOM   3538 N N   . ASP   B 1 47  ? 19.395  34.920  54.992 1.00 61.69  ? 47  ASP   B N   1 
ATOM   3539 C CA  . ASP   B 1 47  ? 18.975  34.378  53.704 1.00 65.60  ? 47  ASP   B CA  1 
ATOM   3540 C C   . ASP   B 1 47  ? 17.510  34.692  53.430 1.00 59.29  ? 47  ASP   B C   1 
ATOM   3541 O O   . ASP   B 1 47  ? 17.136  34.986  52.291 1.00 63.44  ? 47  ASP   B O   1 
ATOM   3542 C CB  . ASP   B 1 47  ? 19.221  32.869  53.659 1.00 73.62  ? 47  ASP   B CB  1 
ATOM   3543 C CG  . ASP   B 1 47  ? 19.064  32.292  52.260 1.00 81.47  ? 47  ASP   B CG  1 
ATOM   3544 O OD1 . ASP   B 1 47  ? 19.816  32.708  51.353 1.00 89.16  ? 47  ASP   B OD1 1 
ATOM   3545 O OD2 . ASP   B 1 47  ? 18.189  31.421  52.068 1.00 81.44  ? 47  ASP   B OD2 1 
ATOM   3546 N N   . ILE   B 1 48  ? 16.669  34.657  54.465 1.00 57.93  ? 48  ILE   B N   1 
ATOM   3547 C CA  . ILE   B 1 48  ? 15.265  35.016  54.291 1.00 60.83  ? 48  ILE   B CA  1 
ATOM   3548 C C   . ILE   B 1 48  ? 15.126  36.494  53.945 1.00 57.55  ? 48  ILE   B C   1 
ATOM   3549 O O   . ILE   B 1 48  ? 14.318  36.874  53.088 1.00 55.89  ? 48  ILE   B O   1 
ATOM   3550 C CB  . ILE   B 1 48  ? 14.464  34.644  55.551 1.00 49.84  ? 48  ILE   B CB  1 
ATOM   3551 C CG1 . ILE   B 1 48  ? 14.531  33.137  55.785 1.00 52.56  ? 48  ILE   B CG1 1 
ATOM   3552 C CG2 . ILE   B 1 48  ? 13.021  35.092  55.426 1.00 54.39  ? 48  ILE   B CG2 1 
ATOM   3553 C CD1 . ILE   B 1 48  ? 13.968  32.712  57.104 1.00 49.23  ? 48  ILE   B CD1 1 
ATOM   3554 N N   . LEU   B 1 49  ? 15.907  37.353  54.605 1.00 62.68  ? 49  LEU   B N   1 
ATOM   3555 C CA  . LEU   B 1 49  ? 15.872  38.775  54.267 1.00 56.41  ? 49  LEU   B CA  1 
ATOM   3556 C C   . LEU   B 1 49  ? 16.344  39.012  52.834 1.00 57.53  ? 49  LEU   B C   1 
ATOM   3557 O O   . LEU   B 1 49  ? 15.787  39.854  52.115 1.00 62.70  ? 49  LEU   B O   1 
ATOM   3558 C CB  . LEU   B 1 49  ? 16.716  39.566  55.263 1.00 53.07  ? 49  LEU   B CB  1 
ATOM   3559 C CG  . LEU   B 1 49  ? 16.065  39.677  56.645 1.00 57.95  ? 49  LEU   B CG  1 
ATOM   3560 C CD1 . LEU   B 1 49  ? 17.081  40.081  57.696 1.00 65.28  ? 49  LEU   B CD1 1 
ATOM   3561 C CD2 . LEU   B 1 49  ? 14.903  40.660  56.613 1.00 53.20  ? 49  LEU   B CD2 1 
ATOM   3562 N N   . LYS   B 1 50  ? 17.374  38.280  52.407 1.00 56.95  ? 50  LYS   B N   1 
ATOM   3563 C CA  . LYS   B 1 50  ? 17.814  38.341  51.018 1.00 52.30  ? 50  LYS   B CA  1 
ATOM   3564 C C   . LYS   B 1 50  ? 16.700  37.911  50.073 1.00 57.45  ? 50  LYS   B C   1 
ATOM   3565 O O   . LYS   B 1 50  ? 16.496  38.526  49.021 1.00 65.73  ? 50  LYS   B O   1 
ATOM   3566 C CB  . LYS   B 1 50  ? 19.049  37.462  50.823 1.00 64.25  ? 50  LYS   B CB  1 
ATOM   3567 C CG  . LYS   B 1 50  ? 20.357  38.119  51.230 1.00 69.02  ? 50  LYS   B CG  1 
ATOM   3568 C CD  . LYS   B 1 50  ? 21.529  37.180  50.991 1.00 91.48  ? 50  LYS   B CD  1 
ATOM   3569 C CE  . LYS   B 1 50  ? 22.854  37.829  51.361 1.00 91.12  ? 50  LYS   B CE  1 
ATOM   3570 N NZ  . LYS   B 1 50  ? 24.003  36.901  51.155 1.00 93.22  ? 50  LYS   B NZ  1 
ATOM   3571 N N   . LYS   B 1 51  ? 15.987  36.837  50.422 1.00 60.30  ? 51  LYS   B N   1 
ATOM   3572 C CA  . LYS   B 1 51  ? 14.869  36.381  49.601 1.00 57.57  ? 51  LYS   B CA  1 
ATOM   3573 C C   . LYS   B 1 51  ? 13.796  37.454  49.492 1.00 56.13  ? 51  LYS   B C   1 
ATOM   3574 O O   . LYS   B 1 51  ? 13.219  37.657  48.419 1.00 54.18  ? 51  LYS   B O   1 
ATOM   3575 C CB  . LYS   B 1 51  ? 14.274  35.096  50.180 1.00 50.73  ? 51  LYS   B CB  1 
ATOM   3576 C CG  . LYS   B 1 51  ? 15.169  33.875  50.076 1.00 49.26  ? 51  LYS   B CG  1 
ATOM   3577 C CD  . LYS   B 1 51  ? 15.336  33.430  48.635 1.00 49.84  ? 51  LYS   B CD  1 
ATOM   3578 C CE  . LYS   B 1 51  ? 16.139  32.145  48.559 1.00 66.41  ? 51  LYS   B CE  1 
ATOM   3579 N NZ  . LYS   B 1 51  ? 15.435  31.022  49.235 1.00 70.45  ? 51  LYS   B NZ  1 
ATOM   3580 N N   . HIS   B 1 52  ? 13.512  38.151  50.594 1.00 49.56  ? 52  HIS   B N   1 
ATOM   3581 C CA  . HIS   B 1 52  ? 12.518  39.219  50.538 1.00 56.85  ? 52  HIS   B CA  1 
ATOM   3582 C C   . HIS   B 1 52  ? 12.981  40.366  49.649 1.00 62.18  ? 52  HIS   B C   1 
ATOM   3583 O O   . HIS   B 1 52  ? 12.186  40.923  48.882 1.00 61.86  ? 52  HIS   B O   1 
ATOM   3584 C CB  . HIS   B 1 52  ? 12.201  39.752  51.930 1.00 55.03  ? 52  HIS   B CB  1 
ATOM   3585 C CG  . HIS   B 1 52  ? 11.127  40.795  51.929 1.00 64.26  ? 52  HIS   B CG  1 
ATOM   3586 N ND1 . HIS   B 1 52  ? 9.787   40.486  51.832 1.00 61.23  ? 52  HIS   B ND1 1 
ATOM   3587 C CD2 . HIS   B 1 52  ? 11.200  42.147  51.957 1.00 61.43  ? 52  HIS   B CD2 1 
ATOM   3588 C CE1 . HIS   B 1 52  ? 9.079   41.601  51.836 1.00 54.06  ? 52  HIS   B CE1 1 
ATOM   3589 N NE2 . HIS   B 1 52  ? 9.912   42.623  51.913 1.00 64.98  ? 52  HIS   B NE2 1 
ATOM   3590 N N   . LEU   B 1 53  ? 14.247  40.768  49.778 1.00 62.37  ? 53  LEU   B N   1 
ATOM   3591 C CA  . LEU   B 1 53  ? 14.784  41.801  48.896 1.00 59.46  ? 53  LEU   B CA  1 
ATOM   3592 C C   . LEU   B 1 53  ? 14.658  41.383  47.435 1.00 56.56  ? 53  LEU   B C   1 
ATOM   3593 O O   . LEU   B 1 53  ? 14.224  42.170  46.581 1.00 64.84  ? 53  LEU   B O   1 
ATOM   3594 C CB  . LEU   B 1 53  ? 16.243  42.080  49.262 1.00 62.81  ? 53  LEU   B CB  1 
ATOM   3595 C CG  . LEU   B 1 53  ? 16.926  43.315  48.677 1.00 63.46  ? 53  LEU   B CG  1 
ATOM   3596 C CD1 . LEU   B 1 53  ? 16.279  44.581  49.214 1.00 63.45  ? 53  LEU   B CD1 1 
ATOM   3597 C CD2 . LEU   B 1 53  ? 18.415  43.293  48.993 1.00 58.78  ? 53  LEU   B CD2 1 
ATOM   3598 N N   . ARG   B 1 54  ? 15.012  40.132  47.143 1.00 60.87  ? 54  ARG   B N   1 
ATOM   3599 C CA  . ARG   B 1 54  ? 14.924  39.598  45.789 1.00 56.84  ? 54  ARG   B CA  1 
ATOM   3600 C C   . ARG   B 1 54  ? 13.486  39.612  45.280 1.00 58.09  ? 54  ARG   B C   1 
ATOM   3601 O O   . ARG   B 1 54  ? 13.235  39.930  44.111 1.00 56.06  ? 54  ARG   B O   1 
ATOM   3602 C CB  . ARG   B 1 54  ? 15.502  38.184  45.787 1.00 47.76  ? 54  ARG   B CB  1 
ATOM   3603 C CG  . ARG   B 1 54  ? 15.691  37.522  44.445 1.00 57.62  ? 54  ARG   B CG  1 
ATOM   3604 C CD  . ARG   B 1 54  ? 16.465  36.232  44.664 1.00 55.27  ? 54  ARG   B CD  1 
ATOM   3605 N NE  . ARG   B 1 54  ? 16.497  35.364  43.493 1.00 61.55  ? 54  ARG   B NE  1 
ATOM   3606 C CZ  . ARG   B 1 54  ? 16.878  34.091  43.532 1.00 75.16  ? 54  ARG   B CZ  1 
ATOM   3607 N NH1 . ARG   B 1 54  ? 16.882  33.360  42.426 1.00 74.65  ? 54  ARG   B NH1 1 
ATOM   3608 N NH2 . ARG   B 1 54  ? 17.253  33.548  44.683 1.00 83.00  ? 54  ARG   B NH2 1 
ATOM   3609 N N   . TRP   B 1 55  ? 12.528  39.275  46.148 1.00 57.39  ? 55  TRP   B N   1 
ATOM   3610 C CA  . TRP   B 1 55  ? 11.119  39.304  45.764 1.00 53.56  ? 55  TRP   B CA  1 
ATOM   3611 C C   . TRP   B 1 55  ? 10.663  40.725  45.457 1.00 58.32  ? 55  TRP   B C   1 
ATOM   3612 O O   . TRP   B 1 55  ? 10.018  40.974  44.431 1.00 65.03  ? 55  TRP   B O   1 
ATOM   3613 C CB  . TRP   B 1 55  ? 10.259  38.691  46.875 1.00 56.90  ? 55  TRP   B CB  1 
ATOM   3614 C CG  . TRP   B 1 55  ? 8.775   38.727  46.590 1.00 47.90  ? 55  TRP   B CG  1 
ATOM   3615 C CD1 . TRP   B 1 55  ? 7.939   39.801  46.716 1.00 47.71  ? 55  TRP   B CD1 1 
ATOM   3616 C CD2 . TRP   B 1 55  ? 7.958   37.637  46.140 1.00 50.13  ? 55  TRP   B CD2 1 
ATOM   3617 N NE1 . TRP   B 1 55  ? 6.658   39.449  46.364 1.00 47.99  ? 55  TRP   B NE1 1 
ATOM   3618 C CE2 . TRP   B 1 55  ? 6.643   38.126  46.009 1.00 49.16  ? 55  TRP   B CE2 1 
ATOM   3619 C CE3 . TRP   B 1 55  ? 8.212   36.296  45.833 1.00 50.64  ? 55  TRP   B CE3 1 
ATOM   3620 C CZ2 . TRP   B 1 55  ? 5.586   37.323  45.584 1.00 54.45  ? 55  TRP   B CZ2 1 
ATOM   3621 C CZ3 . TRP   B 1 55  ? 7.160   35.500  45.411 1.00 57.50  ? 55  TRP   B CZ3 1 
ATOM   3622 C CH2 . TRP   B 1 55  ? 5.864   36.016  45.291 1.00 54.30  ? 55  TRP   B CH2 1 
ATOM   3623 N N   . LEU   B 1 56  ? 10.966  41.666  46.357 1.00 59.27  ? 56  LEU   B N   1 
ATOM   3624 C CA  . LEU   B 1 56  ? 10.623  43.066  46.114 1.00 59.85  ? 56  LEU   B CA  1 
ATOM   3625 C C   . LEU   B 1 56  ? 11.206  43.562  44.799 1.00 58.24  ? 56  LEU   B C   1 
ATOM   3626 O O   . LEU   B 1 56  ? 10.585  44.370  44.101 1.00 60.55  ? 56  LEU   B O   1 
ATOM   3627 C CB  . LEU   B 1 56  ? 11.111  43.944  47.267 1.00 54.76  ? 56  LEU   B CB  1 
ATOM   3628 C CG  . LEU   B 1 56  ? 10.472  43.766  48.643 1.00 66.66  ? 56  LEU   B CG  1 
ATOM   3629 C CD1 . LEU   B 1 56  ? 11.110  44.718  49.642 1.00 64.18  ? 56  LEU   B CD1 1 
ATOM   3630 C CD2 . LEU   B 1 56  ? 8.971   43.980  48.583 1.00 56.54  ? 56  LEU   B CD2 1 
ATOM   3631 N N   . LYS   B 1 57  ? 12.396  43.084  44.438 1.00 68.00  ? 57  LYS   B N   1 
ATOM   3632 C CA  . LYS   B 1 57  ? 13.000  43.534  43.191 1.00 63.25  ? 57  LYS   B CA  1 
ATOM   3633 C C   . LYS   B 1 57  ? 12.388  42.846  41.974 1.00 66.22  ? 57  LYS   B C   1 
ATOM   3634 O O   . LYS   B 1 57  ? 12.310  43.453  40.899 1.00 71.47  ? 57  LYS   B O   1 
ATOM   3635 C CB  . LYS   B 1 57  ? 14.516  43.322  43.230 1.00 71.27  ? 57  LYS   B CB  1 
ATOM   3636 C CG  . LYS   B 1 57  ? 15.236  44.356  44.088 1.00 67.25  ? 57  LYS   B CG  1 
ATOM   3637 C CD  . LYS   B 1 57  ? 16.742  44.144  44.102 1.00 77.14  ? 57  LYS   B CD  1 
ATOM   3638 C CE  . LYS   B 1 57  ? 17.417  45.122  45.056 1.00 85.20  ? 57  LYS   B CE  1 
ATOM   3639 N NZ  . LYS   B 1 57  ? 18.857  44.813  45.275 1.00 75.06  ? 57  LYS   B NZ  1 
ATOM   3640 N N   . ALA   B 1 58  ? 11.949  41.594  42.112 1.00 64.62  ? 58  ALA   B N   1 
ATOM   3641 C CA  . ALA   B 1 58  ? 11.454  40.841  40.964 1.00 56.49  ? 58  ALA   B CA  1 
ATOM   3642 C C   . ALA   B 1 58  ? 9.957   41.006  40.728 1.00 59.45  ? 58  ALA   B C   1 
ATOM   3643 O O   . ALA   B 1 58  ? 9.519   40.994  39.573 1.00 68.51  ? 58  ALA   B O   1 
ATOM   3644 C CB  . ALA   B 1 58  ? 11.780  39.355  41.127 1.00 53.58  ? 58  ALA   B CB  1 
ATOM   3645 N N   . LEU   B 1 59  ? 9.160   41.163  41.782 1.00 66.36  ? 59  LEU   B N   1 
ATOM   3646 C CA  . LEU   B 1 59  ? 7.704   41.263  41.671 1.00 54.89  ? 59  LEU   B CA  1 
ATOM   3647 C C   . LEU   B 1 59  ? 7.220   42.499  42.419 1.00 61.44  ? 59  LEU   B C   1 
ATOM   3648 O O   . LEU   B 1 59  ? 6.551   42.393  43.454 1.00 59.49  ? 59  LEU   B O   1 
ATOM   3649 C CB  . LEU   B 1 59  ? 7.026   40.002  42.206 1.00 49.75  ? 59  LEU   B CB  1 
ATOM   3650 C CG  . LEU   B 1 59  ? 7.229   38.728  41.387 1.00 57.73  ? 59  LEU   B CG  1 
ATOM   3651 C CD1 . LEU   B 1 59  ? 6.723   37.519  42.154 1.00 60.66  ? 59  LEU   B CD1 1 
ATOM   3652 C CD2 . LEU   B 1 59  ? 6.531   38.846  40.043 1.00 52.70  ? 59  LEU   B CD2 1 
ATOM   3653 N N   . PRO   B 1 60  ? 7.539   43.694  41.915 1.00 65.14  ? 60  PRO   B N   1 
ATOM   3654 C CA  . PRO   B 1 60  ? 7.204   44.917  42.663 1.00 60.67  ? 60  PRO   B CA  1 
ATOM   3655 C C   . PRO   B 1 60  ? 5.713   45.136  42.852 1.00 58.57  ? 60  PRO   B C   1 
ATOM   3656 O O   . PRO   B 1 60  ? 5.326   45.863  43.774 1.00 58.11  ? 60  PRO   B O   1 
ATOM   3657 C CB  . PRO   B 1 60  ? 7.827   46.032  41.812 1.00 54.02  ? 60  PRO   B CB  1 
ATOM   3658 C CG  . PRO   B 1 60  ? 7.926   45.458  40.445 1.00 51.28  ? 60  PRO   B CG  1 
ATOM   3659 C CD  . PRO   B 1 60  ? 8.165   43.989  40.615 1.00 59.04  ? 60  PRO   B CD  1 
ATOM   3660 N N   . ARG   B 1 61  ? 4.866   44.540  42.017 1.00 55.55  ? 61  ARG   B N   1 
ATOM   3661 C CA  . ARG   B 1 61  ? 3.425   44.719  42.128 1.00 48.42  ? 61  ARG   B CA  1 
ATOM   3662 C C   . ARG   B 1 61  ? 2.752   43.678  43.011 1.00 61.83  ? 61  ARG   B C   1 
ATOM   3663 O O   . ARG   B 1 61  ? 1.544   43.780  43.247 1.00 68.56  ? 61  ARG   B O   1 
ATOM   3664 C CB  . ARG   B 1 61  ? 2.776   44.684  40.740 1.00 61.09  ? 61  ARG   B CB  1 
ATOM   3665 C CG  . ARG   B 1 61  ? 3.218   45.785  39.796 1.00 72.59  ? 61  ARG   B CG  1 
ATOM   3666 C CD  . ARG   B 1 61  ? 2.414   45.730  38.506 1.00 76.24  ? 61  ARG   B CD  1 
ATOM   3667 N NE  . ARG   B 1 61  ? 0.984   45.897  38.758 1.00 67.01  ? 61  ARG   B NE  1 
ATOM   3668 C CZ  . ARG   B 1 61  ? 0.024   45.518  37.920 1.00 64.04  ? 61  ARG   B CZ  1 
ATOM   3669 N NH1 . ARG   B 1 61  ? 0.334   44.943  36.766 1.00 62.43  ? 61  ARG   B NH1 1 
ATOM   3670 N NH2 . ARG   B 1 61  ? -1.249  45.710  38.238 1.00 66.78  ? 61  ARG   B NH2 1 
ATOM   3671 N N   . VAL   B 1 62  ? 3.493   42.693  43.510 1.00 58.84  ? 62  VAL   B N   1 
ATOM   3672 C CA  . VAL   B 1 62  ? 2.913   41.542  44.192 1.00 47.26  ? 62  VAL   B CA  1 
ATOM   3673 C C   . VAL   B 1 62  ? 3.354   41.571  45.647 1.00 46.81  ? 62  VAL   B C   1 
ATOM   3674 O O   . VAL   B 1 62  ? 4.551   41.479  45.944 1.00 56.00  ? 62  VAL   B O   1 
ATOM   3675 C CB  . VAL   B 1 62  ? 3.324   40.222  43.524 1.00 51.90  ? 62  VAL   B CB  1 
ATOM   3676 C CG1 . VAL   B 1 62  ? 2.561   39.066  44.139 1.00 52.56  ? 62  VAL   B CG1 1 
ATOM   3677 C CG2 . VAL   B 1 62  ? 3.088   40.290  42.026 1.00 47.94  ? 62  VAL   B CG2 1 
ATOM   3678 N N   . THR   B 1 63  ? 2.389   41.688  46.550 1.00 50.91  ? 63  THR   B N   1 
ATOM   3679 C CA  . THR   B 1 63  ? 2.679   41.660  47.977 1.00 56.52  ? 63  THR   B CA  1 
ATOM   3680 C C   . THR   B 1 63  ? 2.766   40.216  48.456 1.00 60.39  ? 63  THR   B C   1 
ATOM   3681 O O   . THR   B 1 63  ? 1.808   39.456  48.274 1.00 55.87  ? 63  THR   B O   1 
ATOM   3682 C CB  . THR   B 1 63  ? 1.606   42.404  48.758 1.00 67.32  ? 63  THR   B CB  1 
ATOM   3683 O OG1 . THR   B 1 63  ? 1.508   43.749  48.273 1.00 73.18  ? 63  THR   B OG1 1 
ATOM   3684 C CG2 . THR   B 1 63  ? 1.950   42.425  50.240 1.00 59.50  ? 63  THR   B CG2 1 
ATOM   3685 N N   . PRO   B 1 64  ? 3.877   39.798  49.061 1.00 53.85  ? 64  PRO   B N   1 
ATOM   3686 C CA  . PRO   B 1 64  ? 4.007   38.397  49.488 1.00 51.47  ? 64  PRO   B CA  1 
ATOM   3687 C C   . PRO   B 1 64  ? 3.299   38.143  50.815 1.00 57.85  ? 64  PRO   B C   1 
ATOM   3688 O O   . PRO   B 1 64  ? 3.459   38.897  51.779 1.00 49.99  ? 64  PRO   B O   1 
ATOM   3689 C CB  . PRO   B 1 64  ? 5.521   38.209  49.618 1.00 57.29  ? 64  PRO   B CB  1 
ATOM   3690 C CG  . PRO   B 1 64  ? 6.027   39.577  49.950 1.00 49.96  ? 64  PRO   B CG  1 
ATOM   3691 C CD  . PRO   B 1 64  ? 5.129   40.553  49.235 1.00 48.76  ? 64  PRO   B CD  1 
ATOM   3692 N N   . PHE   B 1 65  ? 2.512   37.070  50.853 1.00 54.90  ? 65  PHE   B N   1 
ATOM   3693 C CA  . PHE   B 1 65  ? 1.897   36.554  52.073 1.00 48.28  ? 65  PHE   B CA  1 
ATOM   3694 C C   . PHE   B 1 65  ? 2.516   35.189  52.355 1.00 56.14  ? 65  PHE   B C   1 
ATOM   3695 O O   . PHE   B 1 65  ? 2.250   34.222  51.634 1.00 63.54  ? 65  PHE   B O   1 
ATOM   3696 C CB  . PHE   B 1 65  ? 0.378   36.450  51.929 1.00 52.93  ? 65  PHE   B CB  1 
ATOM   3697 C CG  . PHE   B 1 65  ? -0.350  37.747  52.162 1.00 44.82  ? 65  PHE   B CG  1 
ATOM   3698 C CD1 . PHE   B 1 65  ? -0.125  38.845  51.349 1.00 51.33  ? 65  PHE   B CD1 1 
ATOM   3699 C CD2 . PHE   B 1 65  ? -1.284  37.855  53.181 1.00 48.11  ? 65  PHE   B CD2 1 
ATOM   3700 C CE1 . PHE   B 1 65  ? -0.803  40.035  51.561 1.00 51.59  ? 65  PHE   B CE1 1 
ATOM   3701 C CE2 . PHE   B 1 65  ? -1.965  39.040  53.397 1.00 47.07  ? 65  PHE   B CE2 1 
ATOM   3702 C CZ  . PHE   B 1 65  ? -1.725  40.130  52.586 1.00 45.37  ? 65  PHE   B CZ  1 
ATOM   3703 N N   . TYR   B 1 66  ? 3.347   35.115  53.390 1.00 64.95  ? 66  TYR   B N   1 
ATOM   3704 C CA  . TYR   B 1 66  ? 4.082   33.891  53.679 1.00 46.58  ? 66  TYR   B CA  1 
ATOM   3705 C C   . TYR   B 1 66  ? 3.135   32.759  54.067 1.00 47.90  ? 66  TYR   B C   1 
ATOM   3706 O O   . TYR   B 1 66  ? 2.252   32.933  54.912 1.00 50.25  ? 66  TYR   B O   1 
ATOM   3707 C CB  . TYR   B 1 66  ? 5.098   34.138  54.790 1.00 44.57  ? 66  TYR   B CB  1 
ATOM   3708 C CG  . TYR   B 1 66  ? 5.806   32.886  55.243 1.00 44.15  ? 66  TYR   B CG  1 
ATOM   3709 C CD1 . TYR   B 1 66  ? 6.646   32.197  54.380 1.00 47.31  ? 66  TYR   B CD1 1 
ATOM   3710 C CD2 . TYR   B 1 66  ? 5.641   32.397  56.530 1.00 49.83  ? 66  TYR   B CD2 1 
ATOM   3711 C CE1 . TYR   B 1 66  ? 7.299   31.053  54.784 1.00 53.39  ? 66  TYR   B CE1 1 
ATOM   3712 C CE2 . TYR   B 1 66  ? 6.290   31.254  56.944 1.00 45.67  ? 66  TYR   B CE2 1 
ATOM   3713 C CZ  . TYR   B 1 66  ? 7.117   30.587  56.067 1.00 51.76  ? 66  TYR   B CZ  1 
ATOM   3714 O OH  . TYR   B 1 66  ? 7.764   29.449  56.479 1.00 56.91  ? 66  TYR   B OH  1 
ATOM   3715 N N   . ALA   B 1 67  ? 3.317   31.600  53.435 1.00 57.21  ? 67  ALA   B N   1 
ATOM   3716 C CA  . ALA   B 1 67  ? 2.531   30.403  53.734 1.00 51.51  ? 67  ALA   B CA  1 
ATOM   3717 C C   . ALA   B 1 67  ? 3.105   29.757  54.988 1.00 50.58  ? 67  ALA   B C   1 
ATOM   3718 O O   . ALA   B 1 67  ? 4.128   29.070  54.941 1.00 58.90  ? 67  ALA   B O   1 
ATOM   3719 C CB  . ALA   B 1 67  ? 2.541   29.437  52.553 1.00 47.89  ? 67  ALA   B CB  1 
ATOM   3720 N N   . VAL   B 1 68  ? 2.435   29.982  56.119 1.00 51.10  ? 68  VAL   B N   1 
ATOM   3721 C CA  . VAL   B 1 68  ? 2.935   29.526  57.416 1.00 52.69  ? 68  VAL   B CA  1 
ATOM   3722 C C   . VAL   B 1 68  ? 3.102   28.013  57.473 1.00 53.36  ? 68  VAL   B C   1 
ATOM   3723 O O   . VAL   B 1 68  ? 3.945   27.508  58.226 1.00 56.67  ? 68  VAL   B O   1 
ATOM   3724 C CB  . VAL   B 1 68  ? 1.994   30.043  58.524 1.00 55.82  ? 68  VAL   B CB  1 
ATOM   3725 C CG1 . VAL   B 1 68  ? 2.446   29.581  59.891 1.00 67.92  ? 68  VAL   B CG1 1 
ATOM   3726 C CG2 . VAL   B 1 68  ? 1.918   31.557  58.474 1.00 51.19  ? 68  VAL   B CG2 1 
ATOM   3727 N N   . LYS   B 1 69  ? 2.344   27.264  56.669 1.00 51.38  ? 69  LYS   B N   1 
ATOM   3728 C CA  . LYS   B 1 69  ? 2.425   25.807  56.755 1.00 59.58  ? 69  LYS   B CA  1 
ATOM   3729 C C   . LYS   B 1 69  ? 3.780   25.278  56.303 1.00 55.30  ? 69  LYS   B C   1 
ATOM   3730 O O   . LYS   B 1 69  ? 4.209   24.210  56.759 1.00 58.58  ? 69  LYS   B O   1 
ATOM   3731 C CB  . LYS   B 1 69  ? 1.303   25.154  55.944 1.00 51.80  ? 69  LYS   B CB  1 
ATOM   3732 C CG  . LYS   B 1 69  ? 1.300   25.488  54.468 1.00 67.23  ? 69  LYS   B CG  1 
ATOM   3733 C CD  . LYS   B 1 69  ? 0.225   24.690  53.758 1.00 79.30  ? 69  LYS   B CD  1 
ATOM   3734 C CE  . LYS   B 1 69  ? -0.161  25.331  52.445 1.00 76.15  ? 69  LYS   B CE  1 
ATOM   3735 N NZ  . LYS   B 1 69  ? -0.631  26.731  52.640 1.00 87.16  ? 69  LYS   B NZ  1 
ATOM   3736 N N   . CYS   B 1 70  ? 4.466   26.003  55.418 1.00 59.85  ? 70  CYS   B N   1 
ATOM   3737 C CA  . CYS   B 1 70  ? 5.768   25.556  54.931 1.00 50.64  ? 70  CYS   B CA  1 
ATOM   3738 C C   . CYS   B 1 70  ? 6.785   25.465  56.063 1.00 49.88  ? 70  CYS   B C   1 
ATOM   3739 O O   . CYS   B 1 70  ? 7.559   24.503  56.137 1.00 51.26  ? 70  CYS   B O   1 
ATOM   3740 C CB  . CYS   B 1 70  ? 6.257   26.504  53.836 1.00 43.73  ? 70  CYS   B CB  1 
ATOM   3741 S SG  . CYS   B 1 70  ? 7.945   26.219  53.312 1.00 74.37  ? 70  CYS   B SG  1 
ATOM   3742 N N   . ASN   B 1 71  ? 6.795   26.455  56.957 1.00 58.10  ? 71  ASN   B N   1 
ATOM   3743 C CA  . ASN   B 1 71  ? 7.700   26.454  58.107 1.00 49.53  ? 71  ASN   B CA  1 
ATOM   3744 C C   . ASN   B 1 71  ? 7.078   27.349  59.170 1.00 59.42  ? 71  ASN   B C   1 
ATOM   3745 O O   . ASN   B 1 71  ? 7.051   28.573  59.004 1.00 59.98  ? 71  ASN   B O   1 
ATOM   3746 C CB  . ASN   B 1 71  ? 9.095   26.937  57.715 1.00 45.03  ? 71  ASN   B CB  1 
ATOM   3747 C CG  . ASN   B 1 71  ? 10.129  26.690  58.801 1.00 52.68  ? 71  ASN   B CG  1 
ATOM   3748 O OD1 . ASN   B 1 71  ? 9.830   26.767  59.991 1.00 56.29  ? 71  ASN   B OD1 1 
ATOM   3749 N ND2 . ASN   B 1 71  ? 11.355  26.390  58.392 1.00 49.98  ? 71  ASN   B ND2 1 
ATOM   3750 N N   . ASP   B 1 72  ? 6.577   26.744  60.250 1.00 57.64  ? 72  ASP   B N   1 
ATOM   3751 C CA  . ASP   B 1 72  ? 5.894   27.482  61.304 1.00 62.01  ? 72  ASP   B CA  1 
ATOM   3752 C C   . ASP   B 1 72  ? 6.820   27.882  62.449 1.00 68.14  ? 72  ASP   B C   1 
ATOM   3753 O O   . ASP   B 1 72  ? 6.337   28.156  63.555 1.00 65.10  ? 72  ASP   B O   1 
ATOM   3754 C CB  . ASP   B 1 72  ? 4.721   26.662  61.846 1.00 71.02  ? 72  ASP   B CB  1 
ATOM   3755 C CG  . ASP   B 1 72  ? 5.151   25.305  62.368 1.00 84.93  ? 72  ASP   B CG  1 
ATOM   3756 O OD1 . ASP   B 1 72  ? 6.246   24.840  61.989 1.00 83.00  ? 72  ASP   B OD1 1 
ATOM   3757 O OD2 . ASP   B 1 72  ? 4.393   24.703  63.158 1.00 95.07  ? 72  ASP   B OD2 1 
ATOM   3758 N N   . SER   B 1 73  ? 8.130   27.913  62.217 1.00 60.60  ? 73  SER   B N   1 
ATOM   3759 C CA  . SER   B 1 73  ? 9.058   28.347  63.252 1.00 70.19  ? 73  SER   B CA  1 
ATOM   3760 C C   . SER   B 1 73  ? 8.778   29.792  63.643 1.00 61.38  ? 73  SER   B C   1 
ATOM   3761 O O   . SER   B 1 73  ? 8.665   30.671  62.783 1.00 59.50  ? 73  SER   B O   1 
ATOM   3762 C CB  . SER   B 1 73  ? 10.499  28.194  62.773 1.00 62.09  ? 73  SER   B CB  1 
ATOM   3763 O OG  . SER   B 1 73  ? 10.802  26.834  62.510 1.00 85.41  ? 73  SER   B OG  1 
ATOM   3764 N N   . LYS   B 1 74  ? 8.677   30.034  64.952 1.00 71.65  ? 74  LYS   B N   1 
ATOM   3765 C CA  . LYS   B 1 74  ? 8.308   31.360  65.436 1.00 62.88  ? 74  LYS   B CA  1 
ATOM   3766 C C   . LYS   B 1 74  ? 9.332   32.412  65.039 1.00 58.46  ? 74  LYS   B C   1 
ATOM   3767 O O   . LYS   B 1 74  ? 8.965   33.564  64.785 1.00 61.56  ? 74  LYS   B O   1 
ATOM   3768 C CB  . LYS   B 1 74  ? 8.130   31.339  66.954 1.00 63.00  ? 74  LYS   B CB  1 
ATOM   3769 C CG  . LYS   B 1 74  ? 6.935   30.526  67.418 1.00 71.20  ? 74  LYS   B CG  1 
ATOM   3770 C CD  . LYS   B 1 74  ? 6.799   30.535  68.930 1.00 95.15  ? 74  LYS   B CD  1 
ATOM   3771 C CE  . LYS   B 1 74  ? 5.681   29.611  69.386 1.00 99.08  ? 74  LYS   B CE  1 
ATOM   3772 N NZ  . LYS   B 1 74  ? 5.480   29.671  70.860 1.00 110.10 ? 74  LYS   B NZ  1 
ATOM   3773 N N   . ALA   B 1 75  ? 10.615  32.047  64.985 1.00 53.18  ? 75  ALA   B N   1 
ATOM   3774 C CA  . ALA   B 1 75  ? 11.629  33.001  64.548 1.00 59.30  ? 75  ALA   B CA  1 
ATOM   3775 C C   . ALA   B 1 75  ? 11.391  33.438  63.108 1.00 62.16  ? 75  ALA   B C   1 
ATOM   3776 O O   . ALA   B 1 75  ? 11.524  34.624  62.781 1.00 59.78  ? 75  ALA   B O   1 
ATOM   3777 C CB  . ALA   B 1 75  ? 13.023  32.392  64.698 1.00 61.19  ? 75  ALA   B CB  1 
ATOM   3778 N N   . ILE   B 1 76  ? 11.039  32.491  62.236 1.00 64.53  ? 76  ILE   B N   1 
ATOM   3779 C CA  . ILE   B 1 76  ? 10.779  32.813  60.834 1.00 55.64  ? 76  ILE   B CA  1 
ATOM   3780 C C   . ILE   B 1 76  ? 9.613   33.785  60.726 1.00 58.30  ? 76  ILE   B C   1 
ATOM   3781 O O   . ILE   B 1 76  ? 9.684   34.802  60.023 1.00 55.33  ? 76  ILE   B O   1 
ATOM   3782 C CB  . ILE   B 1 76  ? 10.505  31.527  60.034 1.00 68.10  ? 76  ILE   B CB  1 
ATOM   3783 C CG1 . ILE   B 1 76  ? 11.564  30.469  60.343 1.00 64.54  ? 76  ILE   B CG1 1 
ATOM   3784 C CG2 . ILE   B 1 76  ? 10.446  31.829  58.543 1.00 54.93  ? 76  ILE   B CG2 1 
ATOM   3785 C CD1 . ILE   B 1 76  ? 12.937  30.803  59.858 1.00 70.79  ? 76  ILE   B CD1 1 
ATOM   3786 N N   . VAL   B 1 77  ? 8.513   33.472  61.413 1.00 50.06  ? 77  VAL   B N   1 
ATOM   3787 C CA  . VAL   B 1 77  ? 7.322   34.308  61.335 1.00 48.70  ? 77  VAL   B CA  1 
ATOM   3788 C C   . VAL   B 1 77  ? 7.597   35.683  61.926 1.00 56.24  ? 77  VAL   B C   1 
ATOM   3789 O O   . VAL   B 1 77  ? 7.123   36.698  61.408 1.00 68.52  ? 77  VAL   B O   1 
ATOM   3790 C CB  . VAL   B 1 77  ? 6.140   33.611  62.032 1.00 51.01  ? 77  VAL   B CB  1 
ATOM   3791 C CG1 . VAL   B 1 77  ? 4.890   34.470  61.942 1.00 59.84  ? 77  VAL   B CG1 1 
ATOM   3792 C CG2 . VAL   B 1 77  ? 5.899   32.241  61.416 1.00 44.09  ? 77  VAL   B CG2 1 
ATOM   3793 N N   . LYS   B 1 78  ? 8.382   35.744  63.004 1.00 65.47  ? 78  LYS   B N   1 
ATOM   3794 C CA  . LYS   B 1 78  ? 8.732   37.030  63.601 1.00 63.87  ? 78  LYS   B CA  1 
ATOM   3795 C C   . LYS   B 1 78  ? 9.558   37.877  62.641 1.00 60.14  ? 78  LYS   B C   1 
ATOM   3796 O O   . LYS   B 1 78  ? 9.300   39.075  62.471 1.00 57.35  ? 78  LYS   B O   1 
ATOM   3797 C CB  . LYS   B 1 78  ? 9.494   36.809  64.908 1.00 54.10  ? 78  LYS   B CB  1 
ATOM   3798 C CG  . LYS   B 1 78  ? 9.850   38.097  65.631 1.00 68.03  ? 78  LYS   B CG  1 
ATOM   3799 C CD  . LYS   B 1 78  ? 10.729  37.828  66.841 1.00 83.75  ? 78  LYS   B CD  1 
ATOM   3800 C CE  . LYS   B 1 78  ? 11.077  39.116  67.572 1.00 87.97  ? 78  LYS   B CE  1 
ATOM   3801 N NZ  . LYS   B 1 78  ? 11.874  38.855  68.802 1.00 96.22  ? 78  LYS   B NZ  1 
ATOM   3802 N N   . THR   B 1 79  ? 10.569  37.271  62.014 1.00 59.22  ? 79  THR   B N   1 
ATOM   3803 C CA  . THR   B 1 79  ? 11.394  38.001  61.057 1.00 62.77  ? 79  THR   B CA  1 
ATOM   3804 C C   . THR   B 1 79  ? 10.558  38.513  59.891 1.00 69.18  ? 79  THR   B C   1 
ATOM   3805 O O   . THR   B 1 79  ? 10.686  39.672  59.477 1.00 65.96  ? 79  THR   B O   1 
ATOM   3806 C CB  . THR   B 1 79  ? 12.526  37.108  60.553 1.00 61.14  ? 79  THR   B CB  1 
ATOM   3807 O OG1 . THR   B 1 79  ? 13.276  36.612  61.668 1.00 62.35  ? 79  THR   B OG1 1 
ATOM   3808 C CG2 . THR   B 1 79  ? 13.450  37.894  59.639 1.00 56.52  ? 79  THR   B CG2 1 
ATOM   3809 N N   . LEU   B 1 80  ? 9.691   37.657  59.345 1.00 66.92  ? 80  LEU   B N   1 
ATOM   3810 C CA  . LEU   B 1 80  ? 8.878   38.065  58.205 1.00 58.32  ? 80  LEU   B CA  1 
ATOM   3811 C C   . LEU   B 1 80  ? 7.863   39.135  58.593 1.00 55.94  ? 80  LEU   B C   1 
ATOM   3812 O O   . LEU   B 1 80  ? 7.576   40.039  57.799 1.00 60.60  ? 80  LEU   B O   1 
ATOM   3813 C CB  . LEU   B 1 80  ? 8.188   36.847  57.594 1.00 58.56  ? 80  LEU   B CB  1 
ATOM   3814 C CG  . LEU   B 1 80  ? 9.156   35.949  56.821 1.00 49.87  ? 80  LEU   B CG  1 
ATOM   3815 C CD1 . LEU   B 1 80  ? 8.468   34.701  56.305 1.00 56.31  ? 80  LEU   B CD1 1 
ATOM   3816 C CD2 . LEU   B 1 80  ? 9.782   36.729  55.678 1.00 44.47  ? 80  LEU   B CD2 1 
ATOM   3817 N N   . ALA   B 1 81  ? 7.302   39.051  59.802 1.00 57.62  ? 81  ALA   B N   1 
ATOM   3818 C CA  . ALA   B 1 81  ? 6.384   40.085  60.267 1.00 60.56  ? 81  ALA   B CA  1 
ATOM   3819 C C   . ALA   B 1 81  ? 7.096   41.420  60.435 1.00 61.91  ? 81  ALA   B C   1 
ATOM   3820 O O   . ALA   B 1 81  ? 6.562   42.466  60.048 1.00 67.91  ? 81  ALA   B O   1 
ATOM   3821 C CB  . ALA   B 1 81  ? 5.732   39.654  61.580 1.00 61.87  ? 81  ALA   B CB  1 
ATOM   3822 N N   . ALA   B 1 82  ? 8.299   41.405  61.016 1.00 71.49  ? 82  ALA   B N   1 
ATOM   3823 C CA  . ALA   B 1 82  ? 9.100   42.623  61.084 1.00 65.36  ? 82  ALA   B CA  1 
ATOM   3824 C C   . ALA   B 1 82  ? 9.403   43.160  59.693 1.00 67.99  ? 82  ALA   B C   1 
ATOM   3825 O O   . ALA   B 1 82  ? 9.471   44.378  59.495 1.00 76.53  ? 82  ALA   B O   1 
ATOM   3826 C CB  . ALA   B 1 82  ? 10.397  42.361  61.851 1.00 66.83  ? 82  ALA   B CB  1 
ATOM   3827 N N   . THR   B 1 83  ? 9.581   42.265  58.721 1.00 79.20  ? 83  THR   B N   1 
ATOM   3828 C CA  . THR   B 1 83  ? 9.814   42.671  57.340 1.00 72.13  ? 83  THR   B CA  1 
ATOM   3829 C C   . THR   B 1 83  ? 8.578   43.312  56.713 1.00 72.95  ? 83  THR   B C   1 
ATOM   3830 O O   . THR   B 1 83  ? 8.710   44.118  55.783 1.00 69.07  ? 83  THR   B O   1 
ATOM   3831 C CB  . THR   B 1 83  ? 10.277  41.447  56.540 1.00 67.57  ? 83  THR   B CB  1 
ATOM   3832 O OG1 . THR   B 1 83  ? 11.584  41.054  56.982 1.00 81.88  ? 83  THR   B OG1 1 
ATOM   3833 C CG2 . THR   B 1 83  ? 10.333  41.737  55.071 1.00 51.04  ? 83  THR   B CG2 1 
ATOM   3834 N N   . GLY   B 1 84  ? 7.390   43.021  57.238 1.00 84.62  ? 84  GLY   B N   1 
ATOM   3835 C CA  . GLY   B 1 84  ? 6.162   43.601  56.730 1.00 72.54  ? 84  GLY   B CA  1 
ATOM   3836 C C   . GLY   B 1 84  ? 5.425   42.787  55.691 1.00 68.12  ? 84  GLY   B C   1 
ATOM   3837 O O   . GLY   B 1 84  ? 4.539   43.327  55.020 1.00 71.75  ? 84  GLY   B O   1 
ATOM   3838 N N   . THR   B 1 85  ? 5.748   41.506  55.541 1.00 59.45  ? 85  THR   B N   1 
ATOM   3839 C CA  . THR   B 1 85  ? 4.988   40.659  54.637 1.00 55.78  ? 85  THR   B CA  1 
ATOM   3840 C C   . THR   B 1 85  ? 3.630   40.320  55.243 1.00 58.21  ? 85  THR   B C   1 
ATOM   3841 O O   . THR   B 1 85  ? 3.386   40.500  56.439 1.00 63.56  ? 85  THR   B O   1 
ATOM   3842 C CB  . THR   B 1 85  ? 5.748   39.367  54.329 1.00 63.21  ? 85  THR   B CB  1 
ATOM   3843 O OG1 . THR   B 1 85  ? 5.722   38.509  55.476 1.00 54.60  ? 85  THR   B OG1 1 
ATOM   3844 C CG2 . THR   B 1 85  ? 7.193   39.670  53.965 1.00 64.22  ? 85  THR   B CG2 1 
ATOM   3845 N N   . GLY   B 1 86  ? 2.735   39.827  54.392 1.00 58.99  ? 86  GLY   B N   1 
ATOM   3846 C CA  . GLY   B 1 86  ? 1.493   39.252  54.855 1.00 54.63  ? 86  GLY   B CA  1 
ATOM   3847 C C   . GLY   B 1 86  ? 1.682   37.807  55.267 1.00 52.80  ? 86  GLY   B C   1 
ATOM   3848 O O   . GLY   B 1 86  ? 2.779   37.252  55.227 1.00 53.36  ? 86  GLY   B O   1 
ATOM   3849 N N   . PHE   B 1 87  ? 0.582   37.183  55.681 1.00 53.16  ? 87  PHE   B N   1 
ATOM   3850 C CA  . PHE   B 1 87  ? 0.634   35.786  56.089 1.00 58.72  ? 87  PHE   B CA  1 
ATOM   3851 C C   . PHE   B 1 87  ? -0.591  35.028  55.607 1.00 58.91  ? 87  PHE   B C   1 
ATOM   3852 O O   . PHE   B 1 87  ? -1.727  35.468  55.808 1.00 56.26  ? 87  PHE   B O   1 
ATOM   3853 C CB  . PHE   B 1 87  ? 0.771   35.661  57.610 1.00 52.83  ? 87  PHE   B CB  1 
ATOM   3854 C CG  . PHE   B 1 87  ? 2.077   36.172  58.130 1.00 51.17  ? 87  PHE   B CG  1 
ATOM   3855 C CD1 . PHE   B 1 87  ? 3.187   35.345  58.168 1.00 55.89  ? 87  PHE   B CD1 1 
ATOM   3856 C CD2 . PHE   B 1 87  ? 2.203   37.479  58.563 1.00 52.11  ? 87  PHE   B CD2 1 
ATOM   3857 C CE1 . PHE   B 1 87  ? 4.398   35.810  58.635 1.00 55.58  ? 87  PHE   B CE1 1 
ATOM   3858 C CE2 . PHE   B 1 87  ? 3.413   37.950  59.033 1.00 65.24  ? 87  PHE   B CE2 1 
ATOM   3859 C CZ  . PHE   B 1 87  ? 4.512   37.114  59.069 1.00 52.84  ? 87  PHE   B CZ  1 
ATOM   3860 N N   . ASP   B 1 88  ? -0.342  33.882  54.980 1.00 65.08  ? 88  ASP   B N   1 
ATOM   3861 C CA  . ASP   B 1 88  ? -1.378  32.945  54.571 1.00 71.61  ? 88  ASP   B CA  1 
ATOM   3862 C C   . ASP   B 1 88  ? -1.510  31.879  55.651 1.00 74.20  ? 88  ASP   B C   1 
ATOM   3863 O O   . ASP   B 1 88  ? -0.572  31.111  55.891 1.00 62.24  ? 88  ASP   B O   1 
ATOM   3864 C CB  . ASP   B 1 88  ? -1.039  32.323  53.213 1.00 72.18  ? 88  ASP   B CB  1 
ATOM   3865 C CG  . ASP   B 1 88  ? -1.774  31.011  52.953 1.00 89.27  ? 88  ASP   B CG  1 
ATOM   3866 O OD1 . ASP   B 1 88  ? -2.884  30.808  53.489 1.00 90.59  ? 88  ASP   B OD1 1 
ATOM   3867 O OD2 . ASP   B 1 88  ? -1.233  30.175  52.199 1.00 92.71  ? 88  ASP   B OD2 1 
ATOM   3868 N N   . CYS   B 1 89  ? -2.672  31.836  56.295 1.00 76.11  ? 89  CYS   B N   1 
ATOM   3869 C CA  . CYS   B 1 89  ? -2.933  30.892  57.369 1.00 62.22  ? 89  CYS   B CA  1 
ATOM   3870 C C   . CYS   B 1 89  ? -3.994  29.895  56.929 1.00 76.65  ? 89  CYS   B C   1 
ATOM   3871 O O   . CYS   B 1 89  ? -4.974  30.263  56.271 1.00 76.94  ? 89  CYS   B O   1 
ATOM   3872 C CB  . CYS   B 1 89  ? -3.380  31.620  58.635 1.00 65.67  ? 89  CYS   B CB  1 
ATOM   3873 S SG  . CYS   B 1 89  ? -2.121  32.728  59.298 1.00 70.22  ? 89  CYS   B SG  1 
ATOM   3874 N N   . ALA   B 1 90  ? -3.782  28.627  57.281 1.00 64.66  ? 90  ALA   B N   1 
ATOM   3875 C CA  . ALA   B 1 90  ? -4.672  27.550  56.880 1.00 59.50  ? 90  ALA   B CA  1 
ATOM   3876 C C   . ALA   B 1 90  ? -5.492  26.972  58.025 1.00 67.33  ? 90  ALA   B C   1 
ATOM   3877 O O   . ALA   B 1 90  ? -6.349  26.117  57.776 1.00 67.26  ? 90  ALA   B O   1 
ATOM   3878 C CB  . ALA   B 1 90  ? -3.869  26.422  56.216 1.00 71.41  ? 90  ALA   B CB  1 
ATOM   3879 N N   . SER   B 1 91  ? -5.253  27.398  59.262 1.00 74.54  ? 91  SER   B N   1 
ATOM   3880 C CA  . SER   B 1 91  ? -5.931  26.795  60.401 1.00 68.01  ? 91  SER   B CA  1 
ATOM   3881 C C   . SER   B 1 91  ? -5.961  27.786  61.554 1.00 64.53  ? 91  SER   B C   1 
ATOM   3882 O O   . SER   B 1 91  ? -5.325  28.843  61.517 1.00 67.02  ? 91  SER   B O   1 
ATOM   3883 C CB  . SER   B 1 91  ? -5.254  25.491  60.834 1.00 76.66  ? 91  SER   B CB  1 
ATOM   3884 O OG  . SER   B 1 91  ? -3.996  25.747  61.434 1.00 74.81  ? 91  SER   B OG  1 
ATOM   3885 N N   . LYS   B 1 92  ? -6.724  27.418  62.585 1.00 72.74  ? 92  LYS   B N   1 
ATOM   3886 C CA  . LYS   B 1 92  ? -6.837  28.242  63.783 1.00 65.30  ? 92  LYS   B CA  1 
ATOM   3887 C C   . LYS   B 1 92  ? -5.487  28.420  64.468 1.00 54.15  ? 92  LYS   B C   1 
ATOM   3888 O O   . LYS   B 1 92  ? -5.163  29.515  64.945 1.00 54.69  ? 92  LYS   B O   1 
ATOM   3889 C CB  . LYS   B 1 92  ? -7.859  27.609  64.727 1.00 65.06  ? 92  LYS   B CB  1 
ATOM   3890 C CG  . LYS   B 1 92  ? -7.775  28.044  66.176 1.00 69.38  ? 92  LYS   B CG  1 
ATOM   3891 C CD  . LYS   B 1 92  ? -8.829  27.310  66.996 1.00 69.15  ? 92  LYS   B CD  1 
ATOM   3892 C CE  . LYS   B 1 92  ? -8.743  27.646  68.476 1.00 96.44  ? 92  LYS   B CE  1 
ATOM   3893 N NZ  . LYS   B 1 92  ? -9.813  26.962  69.260 1.00 78.01  ? 92  LYS   B NZ  1 
ATOM   3894 N N   . THR   B 1 93  ? -4.683  27.354  64.522 1.00 56.61  ? 93  THR   B N   1 
ATOM   3895 C CA  . THR   B 1 93  ? -3.394  27.422  65.204 1.00 54.20  ? 93  THR   B CA  1 
ATOM   3896 C C   . THR   B 1 93  ? -2.450  28.400  64.515 1.00 62.77  ? 93  THR   B C   1 
ATOM   3897 O O   . THR   B 1 93  ? -1.715  29.139  65.181 1.00 63.32  ? 93  THR   B O   1 
ATOM   3898 C CB  . THR   B 1 93  ? -2.764  26.030  65.276 1.00 63.31  ? 93  THR   B CB  1 
ATOM   3899 O OG1 . THR   B 1 93  ? -3.582  25.174  66.082 1.00 56.48  ? 93  THR   B OG1 1 
ATOM   3900 C CG2 . THR   B 1 93  ? -1.368  26.097  65.878 1.00 47.81  ? 93  THR   B CG2 1 
ATOM   3901 N N   . GLU   B 1 94  ? -2.451  28.418  63.180 1.00 68.10  ? 94  GLU   B N   1 
ATOM   3902 C CA  . GLU   B 1 94  ? -1.568  29.333  62.462 1.00 66.73  ? 94  GLU   B CA  1 
ATOM   3903 C C   . GLU   B 1 94  ? -1.985  30.783  62.674 1.00 64.94  ? 94  GLU   B C   1 
ATOM   3904 O O   . GLU   B 1 94  ? -1.130  31.666  62.817 1.00 64.19  ? 94  GLU   B O   1 
ATOM   3905 C CB  . GLU   B 1 94  ? -1.548  28.989  60.972 1.00 66.99  ? 94  GLU   B CB  1 
ATOM   3906 C CG  . GLU   B 1 94  ? -0.887  27.655  60.646 1.00 86.23  ? 94  GLU   B CG  1 
ATOM   3907 C CD  . GLU   B 1 94  ? -0.837  27.368  59.154 1.00 96.72  ? 94  GLU   B CD  1 
ATOM   3908 O OE1 . GLU   B 1 94  ? -1.462  28.119  58.376 1.00 89.65  ? 94  GLU   B OE1 1 
ATOM   3909 O OE2 . GLU   B 1 94  ? -0.168  26.389  58.758 1.00 94.55  ? 94  GLU   B OE2 1 
ATOM   3910 N N   . ILE   B 1 95  ? -3.293  31.049  62.695 1.00 64.29  ? 95  ILE   B N   1 
ATOM   3911 C CA  . ILE   B 1 95  ? -3.772  32.392  63.010 1.00 66.71  ? 95  ILE   B CA  1 
ATOM   3912 C C   . ILE   B 1 95  ? -3.352  32.786  64.420 1.00 65.99  ? 95  ILE   B C   1 
ATOM   3913 O O   . ILE   B 1 95  ? -2.933  33.925  64.663 1.00 70.88  ? 95  ILE   B O   1 
ATOM   3914 C CB  . ILE   B 1 95  ? -5.299  32.476  62.824 1.00 61.98  ? 95  ILE   B CB  1 
ATOM   3915 C CG1 . ILE   B 1 95  ? -5.673  32.247  61.361 1.00 54.35  ? 95  ILE   B CG1 1 
ATOM   3916 C CG2 . ILE   B 1 95  ? -5.819  33.824  63.287 1.00 59.72  ? 95  ILE   B CG2 1 
ATOM   3917 C CD1 . ILE   B 1 95  ? -7.165  32.201  61.116 1.00 54.43  ? 95  ILE   B CD1 1 
ATOM   3918 N N   . GLN   B 1 96  ? -3.474  31.858  65.374 1.00 64.22  ? 96  GLN   B N   1 
ATOM   3919 C CA  . GLN   B 1 96  ? -3.021  32.119  66.738 1.00 64.87  ? 96  GLN   B CA  1 
ATOM   3920 C C   . GLN   B 1 96  ? -1.543  32.483  66.763 1.00 66.72  ? 96  GLN   B C   1 
ATOM   3921 O O   . GLN   B 1 96  ? -1.136  33.448  67.420 1.00 64.31  ? 96  GLN   B O   1 
ATOM   3922 C CB  . GLN   B 1 96  ? -3.271  30.893  67.615 1.00 61.93  ? 96  GLN   B CB  1 
ATOM   3923 C CG  . GLN   B 1 96  ? -4.700  30.721  68.066 1.00 74.98  ? 96  GLN   B CG  1 
ATOM   3924 C CD  . GLN   B 1 96  ? -4.904  29.466  68.887 1.00 84.35  ? 96  GLN   B CD  1 
ATOM   3925 O OE1 . GLN   B 1 96  ? -4.193  28.475  68.714 1.00 91.01  ? 96  GLN   B OE1 1 
ATOM   3926 N NE2 . GLN   B 1 96  ? -5.885  29.496  69.780 1.00 94.71  ? 96  GLN   B NE2 1 
ATOM   3927 N N   . LEU   B 1 97  ? -0.725  31.706  66.055 1.00 64.61  ? 97  LEU   B N   1 
ATOM   3928 C CA  . LEU   B 1 97  ? 0.711   31.959  66.015 1.00 64.68  ? 97  LEU   B CA  1 
ATOM   3929 C C   . LEU   B 1 97  ? 1.010   33.333  65.431 1.00 68.72  ? 97  LEU   B C   1 
ATOM   3930 O O   . LEU   B 1 97  ? 1.819   34.092  65.977 1.00 69.75  ? 97  LEU   B O   1 
ATOM   3931 C CB  . LEU   B 1 97  ? 1.407   30.865  65.205 1.00 64.96  ? 97  LEU   B CB  1 
ATOM   3932 C CG  . LEU   B 1 97  ? 2.880   31.103  64.870 1.00 57.16  ? 97  LEU   B CG  1 
ATOM   3933 C CD1 . LEU   B 1 97  ? 3.696   31.188  66.144 1.00 65.56  ? 97  LEU   B CD1 1 
ATOM   3934 C CD2 . LEU   B 1 97  ? 3.415   30.012  63.954 1.00 65.71  ? 97  LEU   B CD2 1 
ATOM   3935 N N   . VAL   B 1 98  ? 0.365   33.669  64.314 1.00 76.39  ? 98  VAL   B N   1 
ATOM   3936 C CA  . VAL   B 1 98  ? 0.658   34.930  63.642 1.00 72.98  ? 98  VAL   B CA  1 
ATOM   3937 C C   . VAL   B 1 98  ? 0.216   36.113  64.496 1.00 66.18  ? 98  VAL   B C   1 
ATOM   3938 O O   . VAL   B 1 98  ? 0.959   37.088  64.660 1.00 59.91  ? 98  VAL   B O   1 
ATOM   3939 C CB  . VAL   B 1 98  ? 0.007   34.949  62.248 1.00 62.94  ? 98  VAL   B CB  1 
ATOM   3940 C CG1 . VAL   B 1 98  ? 0.104   36.328  61.633 1.00 69.40  ? 98  VAL   B CG1 1 
ATOM   3941 C CG2 . VAL   B 1 98  ? 0.676   33.925  61.350 1.00 63.91  ? 98  VAL   B CG2 1 
ATOM   3942 N N   . GLN   B 1 99  ? -0.987  36.043  65.072 1.00 73.92  ? 99  GLN   B N   1 
ATOM   3943 C CA  . GLN   B 1 99  ? -1.478  37.152  65.882 1.00 69.78  ? 99  GLN   B CA  1 
ATOM   3944 C C   . GLN   B 1 99  ? -0.697  37.293  67.182 1.00 65.32  ? 99  GLN   B C   1 
ATOM   3945 O O   . GLN   B 1 99  ? -0.528  38.412  67.679 1.00 71.18  ? 99  GLN   B O   1 
ATOM   3946 C CB  . GLN   B 1 99  ? -2.968  36.973  66.172 1.00 60.84  ? 99  GLN   B CB  1 
ATOM   3947 C CG  . GLN   B 1 99  ? -3.853  37.159  64.951 1.00 74.87  ? 99  GLN   B CG  1 
ATOM   3948 C CD  . GLN   B 1 99  ? -5.318  37.313  65.307 1.00 79.17  ? 99  GLN   B CD  1 
ATOM   3949 O OE1 . GLN   B 1 99  ? -5.874  36.509  66.054 1.00 78.28  ? 99  GLN   B OE1 1 
ATOM   3950 N NE2 . GLN   B 1 99  ? -5.952  38.350  64.770 1.00 79.00  ? 99  GLN   B NE2 1 
ATOM   3951 N N   . SER   B 1 100 ? -0.216  36.181  67.746 1.00 59.68  ? 100 SER   B N   1 
ATOM   3952 C CA  . SER   B 1 100 ? 0.572   36.256  68.971 1.00 58.41  ? 100 SER   B CA  1 
ATOM   3953 C C   . SER   B 1 100 ? 1.831   37.095  68.786 1.00 71.61  ? 100 SER   B C   1 
ATOM   3954 O O   . SER   B 1 100 ? 2.293   37.735  69.738 1.00 73.97  ? 100 SER   B O   1 
ATOM   3955 C CB  . SER   B 1 100 ? 0.937   34.850  69.449 1.00 65.06  ? 100 SER   B CB  1 
ATOM   3956 O OG  . SER   B 1 100 ? 2.030   34.325  68.714 1.00 71.71  ? 100 SER   B OG  1 
ATOM   3957 N N   . LEU   B 1 101 ? 2.397   37.108  67.580 1.00 76.13  ? 101 LEU   B N   1 
ATOM   3958 C CA  . LEU   B 1 101 ? 3.579   37.913  67.299 1.00 76.98  ? 101 LEU   B CA  1 
ATOM   3959 C C   . LEU   B 1 101 ? 3.256   39.369  66.988 1.00 72.38  ? 101 LEU   B C   1 
ATOM   3960 O O   . LEU   B 1 101 ? 4.174   40.133  66.669 1.00 67.36  ? 101 LEU   B O   1 
ATOM   3961 C CB  . LEU   B 1 101 ? 4.372   37.298  66.143 1.00 71.95  ? 101 LEU   B CB  1 
ATOM   3962 C CG  . LEU   B 1 101 ? 5.049   35.964  66.467 1.00 68.00  ? 101 LEU   B CG  1 
ATOM   3963 C CD1 . LEU   B 1 101 ? 5.823   35.444  65.271 1.00 78.03  ? 101 LEU   B CD1 1 
ATOM   3964 C CD2 . LEU   B 1 101 ? 5.961   36.105  67.674 1.00 80.21  ? 101 LEU   B CD2 1 
ATOM   3965 N N   . GLY   B 1 102 ? 1.989   39.768  67.060 1.00 70.69  ? 102 GLY   B N   1 
ATOM   3966 C CA  . GLY   B 1 102 ? 1.611   41.155  66.891 1.00 64.12  ? 102 GLY   B CA  1 
ATOM   3967 C C   . GLY   B 1 102 ? 1.133   41.557  65.514 1.00 72.20  ? 102 GLY   B C   1 
ATOM   3968 O O   . GLY   B 1 102 ? 1.055   42.759  65.237 1.00 91.43  ? 102 GLY   B O   1 
ATOM   3969 N N   . VAL   B 1 103 ? 0.819   40.606  64.646 1.00 81.40  ? 103 VAL   B N   1 
ATOM   3970 C CA  . VAL   B 1 103 ? 0.412   40.935  63.278 1.00 72.41  ? 103 VAL   B CA  1 
ATOM   3971 C C   . VAL   B 1 103 ? -1.075  41.282  63.273 1.00 74.14  ? 103 VAL   B C   1 
ATOM   3972 O O   . VAL   B 1 103 ? -1.885  40.506  63.803 1.00 75.48  ? 103 VAL   B O   1 
ATOM   3973 C CB  . VAL   B 1 103 ? 0.707   39.772  62.337 1.00 65.86  ? 103 VAL   B CB  1 
ATOM   3974 C CG1 . VAL   B 1 103 ? 0.208   40.079  60.933 1.00 71.83  ? 103 VAL   B CG1 1 
ATOM   3975 C CG2 . VAL   B 1 103 ? 2.193   39.468  62.324 1.00 72.37  ? 103 VAL   B CG2 1 
ATOM   3976 N N   . PRO   B 1 104 ? -1.467  42.419  62.702 1.00 76.29  ? 104 PRO   B N   1 
ATOM   3977 C CA  . PRO   B 1 104 ? -2.889  42.777  62.645 1.00 67.19  ? 104 PRO   B CA  1 
ATOM   3978 C C   . PRO   B 1 104 ? -3.637  41.891  61.665 1.00 81.74  ? 104 PRO   B C   1 
ATOM   3979 O O   . PRO   B 1 104 ? -3.028  41.295  60.764 1.00 84.11  ? 104 PRO   B O   1 
ATOM   3980 C CB  . PRO   B 1 104 ? -2.862  44.238  62.172 1.00 78.60  ? 104 PRO   B CB  1 
ATOM   3981 C CG  . PRO   B 1 104 ? -1.585  44.354  61.407 1.00 84.27  ? 104 PRO   B CG  1 
ATOM   3982 C CD  . PRO   B 1 104 ? -0.606  43.463  62.121 1.00 71.92  ? 104 PRO   B CD  1 
ATOM   3983 N N   . PRO   B 1 105 ? -4.963  41.781  61.805 1.00 84.81  ? 105 PRO   B N   1 
ATOM   3984 C CA  . PRO   B 1 105 ? -5.710  40.833  60.960 1.00 82.69  ? 105 PRO   B CA  1 
ATOM   3985 C C   . PRO   B 1 105 ? -5.713  41.180  59.479 1.00 79.86  ? 105 PRO   B C   1 
ATOM   3986 O O   . PRO   B 1 105 ? -5.850  40.270  58.651 1.00 82.47  ? 105 PRO   B O   1 
ATOM   3987 C CB  . PRO   B 1 105 ? -7.127  40.876  61.550 1.00 73.21  ? 105 PRO   B CB  1 
ATOM   3988 C CG  . PRO   B 1 105 ? -6.957  41.423  62.932 1.00 79.66  ? 105 PRO   B CG  1 
ATOM   3989 C CD  . PRO   B 1 105 ? -5.812  42.379  62.848 1.00 70.06  ? 105 PRO   B CD  1 
ATOM   3990 N N   . GLU   B 1 106 ? -5.573  42.455  59.109 1.00 81.52  ? 106 GLU   B N   1 
ATOM   3991 C CA  . GLU   B 1 106 ? -5.616  42.812  57.694 1.00 84.14  ? 106 GLU   B CA  1 
ATOM   3992 C C   . GLU   B 1 106 ? -4.384  42.347  56.928 1.00 72.30  ? 106 GLU   B C   1 
ATOM   3993 O O   . GLU   B 1 106 ? -4.352  42.485  55.700 1.00 71.96  ? 106 GLU   B O   1 
ATOM   3994 C CB  . GLU   B 1 106 ? -5.785  44.325  57.524 1.00 87.67  ? 106 GLU   B CB  1 
ATOM   3995 C CG  . GLU   B 1 106 ? -4.637  45.157  58.064 1.00 88.23  ? 106 GLU   B CG  1 
ATOM   3996 C CD  . GLU   B 1 106 ? -4.840  45.560  59.510 1.00 105.09 ? 106 GLU   B CD  1 
ATOM   3997 O OE1 . GLU   B 1 106 ? -4.192  46.533  59.950 1.00 114.81 ? 106 GLU   B OE1 1 
ATOM   3998 O OE2 . GLU   B 1 106 ? -5.649  44.910  60.206 1.00 94.69  ? 106 GLU   B OE2 1 
ATOM   3999 N N   . ARG   B 1 107 ? -3.375  41.813  57.615 1.00 62.94  ? 107 ARG   B N   1 
ATOM   4000 C CA  . ARG   B 1 107 ? -2.222  41.198  56.975 1.00 57.90  ? 107 ARG   B CA  1 
ATOM   4001 C C   . ARG   B 1 107 ? -2.300  39.675  56.982 1.00 58.60  ? 107 ARG   B C   1 
ATOM   4002 O O   . ARG   B 1 107 ? -1.280  39.005  56.792 1.00 62.19  ? 107 ARG   B O   1 
ATOM   4003 C CB  . ARG   B 1 107 ? -0.936  41.667  57.654 1.00 54.44  ? 107 ARG   B CB  1 
ATOM   4004 C CG  . ARG   B 1 107 ? -0.570  43.108  57.350 1.00 59.47  ? 107 ARG   B CG  1 
ATOM   4005 C CD  . ARG   B 1 107 ? 0.545   43.594  58.258 1.00 68.45  ? 107 ARG   B CD  1 
ATOM   4006 N NE  . ARG   B 1 107 ? 1.773   42.824  58.088 1.00 72.71  ? 107 ARG   B NE  1 
ATOM   4007 C CZ  . ARG   B 1 107 ? 2.814   42.896  58.910 1.00 72.63  ? 107 ARG   B CZ  1 
ATOM   4008 N NH1 . ARG   B 1 107 ? 2.773   43.700  59.964 1.00 62.97  ? 107 ARG   B NH1 1 
ATOM   4009 N NH2 . ARG   B 1 107 ? 3.895   42.162  58.683 1.00 71.99  ? 107 ARG   B NH2 1 
ATOM   4010 N N   . ILE   B 1 108 ? -3.491  39.117  57.193 1.00 50.49  ? 108 ILE   B N   1 
ATOM   4011 C CA  . ILE   B 1 108 ? -3.698  37.676  57.249 1.00 56.25  ? 108 ILE   B CA  1 
ATOM   4012 C C   . ILE   B 1 108 ? -4.773  37.296  56.242 1.00 62.93  ? 108 ILE   B C   1 
ATOM   4013 O O   . ILE   B 1 108 ? -5.831  37.932  56.189 1.00 71.59  ? 108 ILE   B O   1 
ATOM   4014 C CB  . ILE   B 1 108 ? -4.106  37.214  58.661 1.00 50.06  ? 108 ILE   B CB  1 
ATOM   4015 C CG1 . ILE   B 1 108 ? -2.989  37.503  59.662 1.00 63.93  ? 108 ILE   B CG1 1 
ATOM   4016 C CG2 . ILE   B 1 108 ? -4.456  35.732  58.657 1.00 48.31  ? 108 ILE   B CG2 1 
ATOM   4017 C CD1 . ILE   B 1 108 ? -3.379  37.224  61.097 1.00 73.47  ? 108 ILE   B CD1 1 
ATOM   4018 N N   . ILE   B 1 109 ? -4.505  36.261  55.451 1.00 55.90  ? 109 ILE   B N   1 
ATOM   4019 C CA  . ILE   B 1 109 ? -5.473  35.714  54.505 1.00 62.19  ? 109 ILE   B CA  1 
ATOM   4020 C C   . ILE   B 1 109 ? -5.708  34.248  54.864 1.00 62.72  ? 109 ILE   B C   1 
ATOM   4021 O O   . ILE   B 1 109 ? -4.752  33.471  55.002 1.00 70.29  ? 109 ILE   B O   1 
ATOM   4022 C CB  . ILE   B 1 109 ? -5.011  35.893  53.046 1.00 56.07  ? 109 ILE   B CB  1 
ATOM   4023 C CG1 . ILE   B 1 109 ? -6.118  35.480  52.069 1.00 65.92  ? 109 ILE   B CG1 1 
ATOM   4024 C CG2 . ILE   B 1 109 ? -3.699  35.164  52.770 1.00 66.82  ? 109 ILE   B CG2 1 
ATOM   4025 C CD1 . ILE   B 1 109 ? -5.725  35.633  50.612 1.00 89.61  ? 109 ILE   B CD1 1 
ATOM   4026 N N   . TYR   B 1 110 ? -6.975  33.890  55.084 1.00 62.18  ? 110 TYR   B N   1 
ATOM   4027 C CA  . TYR   B 1 110 ? -7.367  32.520  55.422 1.00 52.12  ? 110 TYR   B CA  1 
ATOM   4028 C C   . TYR   B 1 110 ? -7.509  31.720  54.127 1.00 59.51  ? 110 TYR   B C   1 
ATOM   4029 O O   . TYR   B 1 110 ? -8.610  31.448  53.642 1.00 61.76  ? 110 TYR   B O   1 
ATOM   4030 C CB  . TYR   B 1 110 ? -8.667  32.538  56.216 1.00 50.33  ? 110 TYR   B CB  1 
ATOM   4031 C CG  . TYR   B 1 110 ? -8.956  31.295  57.026 1.00 62.51  ? 110 TYR   B CG  1 
ATOM   4032 C CD1 . TYR   B 1 110 ? -8.218  30.132  56.849 1.00 64.74  ? 110 TYR   B CD1 1 
ATOM   4033 C CD2 . TYR   B 1 110 ? -9.986  31.281  57.957 1.00 63.14  ? 110 TYR   B CD2 1 
ATOM   4034 C CE1 . TYR   B 1 110 ? -8.488  28.998  57.587 1.00 73.21  ? 110 TYR   B CE1 1 
ATOM   4035 C CE2 . TYR   B 1 110 ? -10.266 30.153  58.696 1.00 65.78  ? 110 TYR   B CE2 1 
ATOM   4036 C CZ  . TYR   B 1 110 ? -9.513  29.014  58.508 1.00 72.89  ? 110 TYR   B CZ  1 
ATOM   4037 O OH  . TYR   B 1 110 ? -9.786  27.884  59.238 1.00 73.17  ? 110 TYR   B OH  1 
ATOM   4038 N N   . ALA   B 1 111 ? -6.364  31.326  53.559 1.00 55.83  ? 111 ALA   B N   1 
ATOM   4039 C CA  . ALA   B 1 111 ? -6.358  30.651  52.264 1.00 61.58  ? 111 ALA   B CA  1 
ATOM   4040 C C   . ALA   B 1 111 ? -6.577  29.141  52.358 1.00 64.29  ? 111 ALA   B C   1 
ATOM   4041 O O   . ALA   B 1 111 ? -5.816  28.374  51.761 1.00 92.50  ? 111 ALA   B O   1 
ATOM   4042 C CB  . ALA   B 1 111 ? -5.053  30.920  51.513 1.00 76.47  ? 111 ALA   B CB  1 
ATOM   4043 N N   . ASN   B 1 112 ? -7.590  28.699  53.102 1.00 58.17  ? 112 ASN   B N   1 
ATOM   4044 C CA  . ASN   B 1 112 ? -7.935  27.285  53.116 1.00 61.59  ? 112 ASN   B CA  1 
ATOM   4045 C C   . ASN   B 1 112 ? -9.302  27.144  52.473 1.00 65.81  ? 112 ASN   B C   1 
ATOM   4046 O O   . ASN   B 1 112 ? -10.281 27.689  53.003 1.00 69.71  ? 112 ASN   B O   1 
ATOM   4047 C CB  . ASN   B 1 112 ? -7.945  26.726  54.539 1.00 62.49  ? 112 ASN   B CB  1 
ATOM   4048 C CG  . ASN   B 1 112 ? -8.233  25.229  54.590 1.00 72.97  ? 112 ASN   B CG  1 
ATOM   4049 O OD1 . ASN   B 1 112 ? -8.618  24.617  53.594 1.00 80.37  ? 112 ASN   B OD1 1 
ATOM   4050 N ND2 . ASN   B 1 112 ? -8.044  24.634  55.764 1.00 68.20  ? 112 ASN   B ND2 1 
ATOM   4051 N N   . PRO   B 1 113 ? -9.424  26.455  51.336 1.00 65.62  ? 113 PRO   B N   1 
ATOM   4052 C CA  . PRO   B 1 113 ? -10.722 26.416  50.643 1.00 74.08  ? 113 PRO   B CA  1 
ATOM   4053 C C   . PRO   B 1 113 ? -11.779 25.582  51.350 1.00 80.99  ? 113 PRO   B C   1 
ATOM   4054 O O   . PRO   B 1 113 ? -12.970 25.765  51.068 1.00 74.57  ? 113 PRO   B O   1 
ATOM   4055 C CB  . PRO   B 1 113 ? -10.370 25.816  49.272 1.00 57.82  ? 113 PRO   B CB  1 
ATOM   4056 C CG  . PRO   B 1 113 ? -8.884  25.975  49.142 1.00 67.90  ? 113 PRO   B CG  1 
ATOM   4057 C CD  . PRO   B 1 113 ? -8.353  25.847  50.533 1.00 63.87  ? 113 PRO   B CD  1 
ATOM   4058 N N   . CYS   B 1 114 ? -11.392 24.677  52.252 1.00 79.74  ? 114 CYS   B N   1 
ATOM   4059 C CA  . CYS   B 1 114 ? -12.323 23.770  52.929 1.00 70.36  ? 114 CYS   B CA  1 
ATOM   4060 C C   . CYS   B 1 114 ? -12.052 23.848  54.429 1.00 70.24  ? 114 CYS   B C   1 
ATOM   4061 O O   . CYS   B 1 114 ? -11.228 23.098  54.962 1.00 72.42  ? 114 CYS   B O   1 
ATOM   4062 C CB  . CYS   B 1 114 ? -12.187 22.345  52.398 1.00 73.56  ? 114 CYS   B CB  1 
ATOM   4063 S SG  . CYS   B 1 114 ? -12.682 22.145  50.670 1.00 85.90  ? 114 CYS   B SG  1 
ATOM   4064 N N   . LYS   B 1 115 ? -12.753 24.752  55.107 1.00 65.99  ? 115 LYS   B N   1 
ATOM   4065 C CA  . LYS   B 1 115 ? -12.495 25.078  56.502 1.00 63.83  ? 115 LYS   B CA  1 
ATOM   4066 C C   . LYS   B 1 115 ? -13.590 24.504  57.390 1.00 64.18  ? 115 LYS   B C   1 
ATOM   4067 O O   . LYS   B 1 115 ? -14.773 24.550  57.039 1.00 67.32  ? 115 LYS   B O   1 
ATOM   4068 C CB  . LYS   B 1 115 ? -12.419 26.594  56.698 1.00 58.15  ? 115 LYS   B CB  1 
ATOM   4069 C CG  . LYS   B 1 115 ? -11.336 27.266  55.884 1.00 60.67  ? 115 LYS   B CG  1 
ATOM   4070 C CD  . LYS   B 1 115 ? -11.582 28.761  55.757 1.00 67.59  ? 115 LYS   B CD  1 
ATOM   4071 C CE  . LYS   B 1 115 ? -12.801 29.055  54.895 1.00 63.52  ? 115 LYS   B CE  1 
ATOM   4072 N NZ  . LYS   B 1 115 ? -12.713 28.418  53.552 1.00 71.87  ? 115 LYS   B NZ  1 
ATOM   4073 N N   . GLN   B 1 116 ? -13.189 23.955  58.536 1.00 67.74  ? 116 GLN   B N   1 
ATOM   4074 C CA  . GLN   B 1 116 ? -14.156 23.521  59.535 1.00 66.76  ? 116 GLN   B CA  1 
ATOM   4075 C C   . GLN   B 1 116 ? -14.914 24.722  60.087 1.00 67.52  ? 116 GLN   B C   1 
ATOM   4076 O O   . GLN   B 1 116 ? -14.352 25.809  60.249 1.00 69.68  ? 116 GLN   B O   1 
ATOM   4077 C CB  . GLN   B 1 116 ? -13.461 22.760  60.666 1.00 76.33  ? 116 GLN   B CB  1 
ATOM   4078 C CG  . GLN   B 1 116 ? -14.424 22.154  61.682 1.00 69.94  ? 116 GLN   B CG  1 
ATOM   4079 C CD  . GLN   B 1 116 ? -13.733 21.265  62.696 1.00 73.73  ? 116 GLN   B CD  1 
ATOM   4080 O OE1 . GLN   B 1 116 ? -12.847 20.483  62.352 1.00 74.47  ? 116 GLN   B OE1 1 
ATOM   4081 N NE2 . GLN   B 1 116 ? -14.136 21.380  63.957 1.00 79.96  ? 116 GLN   B NE2 1 
ATOM   4082 N N   . VAL   B 1 117 ? -16.203 24.516  60.367 1.00 69.67  ? 117 VAL   B N   1 
ATOM   4083 C CA  . VAL   B 1 117 ? -17.076 25.616  60.774 1.00 63.62  ? 117 VAL   B CA  1 
ATOM   4084 C C   . VAL   B 1 117 ? -16.535 26.318  62.014 1.00 58.24  ? 117 VAL   B C   1 
ATOM   4085 O O   . VAL   B 1 117 ? -16.518 27.553  62.085 1.00 55.96  ? 117 VAL   B O   1 
ATOM   4086 C CB  . VAL   B 1 117 ? -18.510 25.107  61.001 1.00 68.36  ? 117 VAL   B CB  1 
ATOM   4087 C CG1 . VAL   B 1 117 ? -19.351 26.204  61.609 1.00 69.97  ? 117 VAL   B CG1 1 
ATOM   4088 C CG2 . VAL   B 1 117 ? -19.116 24.623  59.697 1.00 70.58  ? 117 VAL   B CG2 1 
ATOM   4089 N N   . SER   B 1 118 ? -16.096 25.549  63.016 1.00 62.95  ? 118 SER   B N   1 
ATOM   4090 C CA  . SER   B 1 118 ? -15.592 26.163  64.241 1.00 59.66  ? 118 SER   B CA  1 
ATOM   4091 C C   . SER   B 1 118 ? -14.372 27.034  63.970 1.00 58.77  ? 118 SER   B C   1 
ATOM   4092 O O   . SER   B 1 118 ? -14.192 28.073  64.616 1.00 55.60  ? 118 SER   B O   1 
ATOM   4093 C CB  . SER   B 1 118 ? -15.253 25.088  65.274 1.00 53.19  ? 118 SER   B CB  1 
ATOM   4094 O OG  . SER   B 1 118 ? -14.249 24.215  64.790 1.00 76.31  ? 118 SER   B OG  1 
ATOM   4095 N N   . GLN   B 1 119 ? -13.540 26.647  62.999 1.00 67.95  ? 119 GLN   B N   1 
ATOM   4096 C CA  . GLN   B 1 119 ? -12.376 27.462  62.671 1.00 57.86  ? 119 GLN   B CA  1 
ATOM   4097 C C   . GLN   B 1 119 ? -12.772 28.724  61.913 1.00 54.46  ? 119 GLN   B C   1 
ATOM   4098 O O   . GLN   B 1 119 ? -12.150 29.776  62.097 1.00 59.24  ? 119 GLN   B O   1 
ATOM   4099 C CB  . GLN   B 1 119 ? -11.366 26.637  61.877 1.00 65.37  ? 119 GLN   B CB  1 
ATOM   4100 C CG  . GLN   B 1 119 ? -11.026 25.306  62.530 1.00 59.24  ? 119 GLN   B CG  1 
ATOM   4101 C CD  . GLN   B 1 119 ? -9.537  25.027  62.547 1.00 62.04  ? 119 GLN   B CD  1 
ATOM   4102 O OE1 . GLN   B 1 119 ? -8.743  25.803  62.017 1.00 83.46  ? 119 GLN   B OE1 1 
ATOM   4103 N NE2 . GLN   B 1 119 ? -9.150  23.913  63.159 1.00 62.10  ? 119 GLN   B NE2 1 
ATOM   4104 N N   . ILE   B 1 120 ? -13.805 28.646  61.071 1.00 60.86  ? 120 ILE   B N   1 
ATOM   4105 C CA  . ILE   B 1 120 ? -14.360 29.855  60.465 1.00 61.40  ? 120 ILE   B CA  1 
ATOM   4106 C C   . ILE   B 1 120 ? -14.877 30.793  61.547 1.00 64.68  ? 120 ILE   B C   1 
ATOM   4107 O O   . ILE   B 1 120 ? -14.675 32.014  61.489 1.00 53.56  ? 120 ILE   B O   1 
ATOM   4108 C CB  . ILE   B 1 120 ? -15.465 29.490  59.458 1.00 60.44  ? 120 ILE   B CB  1 
ATOM   4109 C CG1 . ILE   B 1 120 ? -14.887 28.677  58.299 1.00 73.07  ? 120 ILE   B CG1 1 
ATOM   4110 C CG2 . ILE   B 1 120 ? -16.151 30.743  58.942 1.00 62.33  ? 120 ILE   B CG2 1 
ATOM   4111 C CD1 . ILE   B 1 120 ? -15.931 28.154  57.340 1.00 68.06  ? 120 ILE   B CD1 1 
ATOM   4112 N N   . LYS   B 1 121 ? -15.557 30.232  62.551 1.00 65.07  ? 121 LYS   B N   1 
ATOM   4113 C CA  . LYS   B 1 121 ? -16.062 31.031  63.661 1.00 65.06  ? 121 LYS   B CA  1 
ATOM   4114 C C   . LYS   B 1 121 ? -14.913 31.711  64.394 1.00 60.25  ? 121 LYS   B C   1 
ATOM   4115 O O   . LYS   B 1 121 ? -14.996 32.896  64.739 1.00 58.37  ? 121 LYS   B O   1 
ATOM   4116 C CB  . LYS   B 1 121 ? -16.866 30.144  64.614 1.00 60.65  ? 121 LYS   B CB  1 
ATOM   4117 C CG  . LYS   B 1 121 ? -17.665 30.893  65.666 1.00 70.31  ? 121 LYS   B CG  1 
ATOM   4118 C CD  . LYS   B 1 121 ? -18.468 32.027  65.056 1.00 75.64  ? 121 LYS   B CD  1 
ATOM   4119 C CE  . LYS   B 1 121 ? -19.121 32.879  66.132 1.00 89.94  ? 121 LYS   B CE  1 
ATOM   4120 N NZ  . LYS   B 1 121 ? -19.791 34.081  65.566 1.00 88.96  ? 121 LYS   B NZ  1 
ATOM   4121 N N   . TYR   B 1 122 ? -13.837 30.962  64.659 1.00 50.79  ? 122 TYR   B N   1 
ATOM   4122 C CA  . TYR   B 1 122 ? -12.669 31.549  65.309 1.00 52.85  ? 122 TYR   B CA  1 
ATOM   4123 C C   . TYR   B 1 122 ? -12.087 32.683  64.476 1.00 56.20  ? 122 TYR   B C   1 
ATOM   4124 O O   . TYR   B 1 122 ? -11.727 33.736  65.014 1.00 61.86  ? 122 TYR   B O   1 
ATOM   4125 C CB  . TYR   B 1 122 ? -11.598 30.487  65.570 1.00 53.27  ? 122 TYR   B CB  1 
ATOM   4126 C CG  . TYR   B 1 122 ? -10.368 31.066  66.238 1.00 66.19  ? 122 TYR   B CG  1 
ATOM   4127 C CD1 . TYR   B 1 122 ? -10.268 31.118  67.621 1.00 64.86  ? 122 TYR   B CD1 1 
ATOM   4128 C CD2 . TYR   B 1 122 ? -9.316  31.582  65.486 1.00 61.61  ? 122 TYR   B CD2 1 
ATOM   4129 C CE1 . TYR   B 1 122 ? -9.157  31.658  68.237 1.00 73.10  ? 122 TYR   B CE1 1 
ATOM   4130 C CE2 . TYR   B 1 122 ? -8.201  32.128  66.094 1.00 71.77  ? 122 TYR   B CE2 1 
ATOM   4131 C CZ  . TYR   B 1 122 ? -8.127  32.160  67.470 1.00 72.80  ? 122 TYR   B CZ  1 
ATOM   4132 O OH  . TYR   B 1 122 ? -7.022  32.702  68.084 1.00 68.15  ? 122 TYR   B OH  1 
ATOM   4133 N N   . ALA   B 1 123 ? -11.964 32.474  63.162 1.00 72.34  ? 123 ALA   B N   1 
ATOM   4134 C CA  . ALA   B 1 123 ? -11.436 33.520  62.290 1.00 56.28  ? 123 ALA   B CA  1 
ATOM   4135 C C   . ALA   B 1 123 ? -12.302 34.770  62.349 1.00 62.83  ? 123 ALA   B C   1 
ATOM   4136 O O   . ALA   B 1 123 ? -11.785 35.894  62.357 1.00 59.90  ? 123 ALA   B O   1 
ATOM   4137 C CB  . ALA   B 1 123 ? -11.329 33.007  60.854 1.00 54.25  ? 123 ALA   B CB  1 
ATOM   4138 N N   . ALA   B 1 124 ? -13.624 34.592  62.383 1.00 54.23  ? 124 ALA   B N   1 
ATOM   4139 C CA  . ALA   B 1 124 ? -14.519 35.737  62.510 1.00 57.56  ? 124 ALA   B CA  1 
ATOM   4140 C C   . ALA   B 1 124 ? -14.327 36.441  63.849 1.00 68.48  ? 124 ALA   B C   1 
ATOM   4141 O O   . ALA   B 1 124 ? -14.306 37.676  63.912 1.00 69.09  ? 124 ALA   B O   1 
ATOM   4142 C CB  . ALA   B 1 124 ? -15.971 35.291  62.343 1.00 58.37  ? 124 ALA   B CB  1 
ATOM   4143 N N   . ASN   B 1 125 ? -14.182 35.669  64.930 1.00 64.85  ? 125 ASN   B N   1 
ATOM   4144 C CA  . ASN   B 1 125 ? -14.060 36.255  66.262 1.00 56.34  ? 125 ASN   B CA  1 
ATOM   4145 C C   . ASN   B 1 125 ? -12.801 37.102  66.407 1.00 60.04  ? 125 ASN   B C   1 
ATOM   4146 O O   . ASN   B 1 125 ? -12.765 38.019  67.235 1.00 66.68  ? 125 ASN   B O   1 
ATOM   4147 C CB  . ASN   B 1 125 ? -14.076 35.152  67.323 1.00 56.75  ? 125 ASN   B CB  1 
ATOM   4148 C CG  . ASN   B 1 125 ? -15.446 34.521  67.489 1.00 69.29  ? 125 ASN   B CG  1 
ATOM   4149 O OD1 . ASN   B 1 125 ? -16.454 35.058  67.028 1.00 74.99  ? 125 ASN   B OD1 1 
ATOM   4150 N ND2 . ASN   B 1 125 ? -15.488 33.370  68.151 1.00 78.25  ? 125 ASN   B ND2 1 
ATOM   4151 N N   . ASN   B 1 126 ? -11.756 36.809  65.632 1.00 77.08  ? 126 ASN   B N   1 
ATOM   4152 C CA  . ASN   B 1 126 ? -10.481 37.507  65.758 1.00 76.21  ? 126 ASN   B CA  1 
ATOM   4153 C C   . ASN   B 1 126 ? -10.229 38.480  64.609 1.00 70.20  ? 126 ASN   B C   1 
ATOM   4154 O O   . ASN   B 1 126 ? -9.091  38.919  64.411 1.00 71.63  ? 126 ASN   B O   1 
ATOM   4155 C CB  . ASN   B 1 126 ? -9.338  36.499  65.877 1.00 52.69  ? 126 ASN   B CB  1 
ATOM   4156 C CG  . ASN   B 1 126 ? -9.338  35.780  67.215 1.00 67.48  ? 126 ASN   B CG  1 
ATOM   4157 O OD1 . ASN   B 1 126 ? -8.638  36.176  68.147 1.00 70.13  ? 126 ASN   B OD1 1 
ATOM   4158 N ND2 . ASN   B 1 126 ? -10.139 34.726  67.321 1.00 58.89  ? 126 ASN   B ND2 1 
ATOM   4159 N N   . GLY   B 1 127 ? -11.267 38.828  63.851 1.00 55.95  ? 127 GLY   B N   1 
ATOM   4160 C CA  . GLY   B 1 127 ? -11.175 39.897  62.878 1.00 62.98  ? 127 GLY   B CA  1 
ATOM   4161 C C   . GLY   B 1 127 ? -10.505 39.553  61.568 1.00 61.36  ? 127 GLY   B C   1 
ATOM   4162 O O   . GLY   B 1 127 ? -10.196 40.467  60.795 1.00 67.42  ? 127 GLY   B O   1 
ATOM   4163 N N   . VAL   B 1 128 ? -10.270 38.275  61.285 1.00 55.94  ? 128 VAL   B N   1 
ATOM   4164 C CA  . VAL   B 1 128 ? -9.717  37.871  59.997 1.00 59.39  ? 128 VAL   B CA  1 
ATOM   4165 C C   . VAL   B 1 128 ? -10.868 37.818  58.999 1.00 55.50  ? 128 VAL   B C   1 
ATOM   4166 O O   . VAL   B 1 128 ? -11.696 36.906  59.040 1.00 66.27  ? 128 VAL   B O   1 
ATOM   4167 C CB  . VAL   B 1 128 ? -8.993  36.523  60.088 1.00 65.84  ? 128 VAL   B CB  1 
ATOM   4168 C CG1 . VAL   B 1 128 ? -8.524  36.084  58.710 1.00 55.05  ? 128 VAL   B CG1 1 
ATOM   4169 C CG2 . VAL   B 1 128 ? -7.815  36.622  61.044 1.00 56.19  ? 128 VAL   B CG2 1 
ATOM   4170 N N   . GLN   B 1 129 ? -10.916 38.794  58.093 1.00 53.67  ? 129 GLN   B N   1 
ATOM   4171 C CA  . GLN   B 1 129 ? -12.073 38.971  57.223 1.00 63.36  ? 129 GLN   B CA  1 
ATOM   4172 C C   . GLN   B 1 129 ? -11.959 38.215  55.909 1.00 56.61  ? 129 GLN   B C   1 
ATOM   4173 O O   . GLN   B 1 129 ? -12.980 37.791  55.358 1.00 58.97  ? 129 GLN   B O   1 
ATOM   4174 C CB  . GLN   B 1 129 ? -12.287 40.458  56.926 1.00 70.09  ? 129 GLN   B CB  1 
ATOM   4175 C CG  . GLN   B 1 129 ? -12.500 41.313  58.161 1.00 79.07  ? 129 GLN   B CG  1 
ATOM   4176 C CD  . GLN   B 1 129 ? -13.671 40.837  58.997 1.00 92.62  ? 129 GLN   B CD  1 
ATOM   4177 O OE1 . GLN   B 1 129 ? -13.490 40.208  60.040 1.00 92.38  ? 129 GLN   B OE1 1 
ATOM   4178 N NE2 . GLN   B 1 129 ? -14.883 41.132  58.540 1.00 79.09  ? 129 GLN   B NE2 1 
ATOM   4179 N N   . MET   B 1 130 ? -10.748 38.037  55.395 1.00 68.06  ? 130 MET   B N   1 
ATOM   4180 C CA  . MET   B 1 130 ? -10.541 37.516  54.051 1.00 52.08  ? 130 MET   B CA  1 
ATOM   4181 C C   . MET   B 1 130 ? -10.317 36.010  54.099 1.00 59.68  ? 130 MET   B C   1 
ATOM   4182 O O   . MET   B 1 130 ? -9.404  35.531  54.782 1.00 61.42  ? 130 MET   B O   1 
ATOM   4183 C CB  . MET   B 1 130 ? -9.353  38.219  53.406 1.00 53.10  ? 130 MET   B CB  1 
ATOM   4184 C CG  . MET   B 1 130 ? -9.254  38.038  51.921 1.00 65.27  ? 130 MET   B CG  1 
ATOM   4185 S SD  . MET   B 1 130 ? -8.101  39.253  51.285 1.00 95.59  ? 130 MET   B SD  1 
ATOM   4186 C CE  . MET   B 1 130 ? -9.073  40.748  51.464 1.00 82.60  ? 130 MET   B CE  1 
ATOM   4187 N N   . MET   B 1 131 ? -11.142 35.269  53.361 1.00 55.98  ? 131 MET   B N   1 
ATOM   4188 C CA  . MET   B 1 131 ? -11.032 33.818  53.295 1.00 55.85  ? 131 MET   B CA  1 
ATOM   4189 C C   . MET   B 1 131 ? -11.251 33.358  51.863 1.00 56.06  ? 131 MET   B C   1 
ATOM   4190 O O   . MET   B 1 131 ? -11.967 34.002  51.098 1.00 51.92  ? 131 MET   B O   1 
ATOM   4191 C CB  . MET   B 1 131 ? -12.047 33.115  54.207 1.00 62.75  ? 131 MET   B CB  1 
ATOM   4192 C CG  . MET   B 1 131 ? -12.091 33.626  55.633 1.00 74.71  ? 131 MET   B CG  1 
ATOM   4193 S SD  . MET   B 1 131 ? -13.242 32.676  56.640 1.00 76.01  ? 131 MET   B SD  1 
ATOM   4194 C CE  . MET   B 1 131 ? -14.765 32.951  55.742 1.00 60.57  ? 131 MET   B CE  1 
ATOM   4195 N N   . THR   B 1 132 ? -10.639 32.233  51.509 1.00 55.87  ? 132 THR   B N   1 
ATOM   4196 C CA  . THR   B 1 132 ? -10.839 31.662  50.187 1.00 52.96  ? 132 THR   B CA  1 
ATOM   4197 C C   . THR   B 1 132 ? -11.957 30.624  50.213 1.00 53.56  ? 132 THR   B C   1 
ATOM   4198 O O   . THR   B 1 132 ? -12.331 30.100  51.266 1.00 54.51  ? 132 THR   B O   1 
ATOM   4199 C CB  . THR   B 1 132 ? -9.551  31.025  49.664 1.00 51.75  ? 132 THR   B CB  1 
ATOM   4200 O OG1 . THR   B 1 132 ? -9.145  29.970  50.544 1.00 71.21  ? 132 THR   B OG1 1 
ATOM   4201 C CG2 . THR   B 1 132 ? -8.441  32.064  49.575 1.00 54.91  ? 132 THR   B CG2 1 
ATOM   4202 N N   . PHE   B 1 133 ? -12.487 30.329  49.027 1.00 58.02  ? 133 PHE   B N   1 
ATOM   4203 C CA  . PHE   B 1 133 ? -13.539 29.328  48.891 1.00 51.27  ? 133 PHE   B CA  1 
ATOM   4204 C C   . PHE   B 1 133 ? -13.603 28.864  47.443 1.00 55.75  ? 133 PHE   B C   1 
ATOM   4205 O O   . PHE   B 1 133 ? -13.214 29.595  46.529 1.00 66.13  ? 133 PHE   B O   1 
ATOM   4206 C CB  . PHE   B 1 133 ? -14.902 29.879  49.325 1.00 40.29  ? 133 PHE   B CB  1 
ATOM   4207 C CG  . PHE   B 1 133 ? -15.576 30.714  48.275 1.00 56.85  ? 133 PHE   B CG  1 
ATOM   4208 C CD1 . PHE   B 1 133 ? -15.106 31.980  47.967 1.00 57.08  ? 133 PHE   B CD1 1 
ATOM   4209 C CD2 . PHE   B 1 133 ? -16.678 30.229  47.588 1.00 56.98  ? 133 PHE   B CD2 1 
ATOM   4210 C CE1 . PHE   B 1 133 ? -15.724 32.749  46.997 1.00 54.85  ? 133 PHE   B CE1 1 
ATOM   4211 C CE2 . PHE   B 1 133 ? -17.300 30.991  46.617 1.00 51.71  ? 133 PHE   B CE2 1 
ATOM   4212 C CZ  . PHE   B 1 133 ? -16.823 32.253  46.322 1.00 60.30  ? 133 PHE   B CZ  1 
ATOM   4213 N N   . ASP   B 1 134 ? -14.086 27.628  47.247 1.00 64.50  ? 134 ASP   B N   1 
ATOM   4214 C CA  . ASP   B 1 134 ? -14.300 27.114  45.898 1.00 60.52  ? 134 ASP   B CA  1 
ATOM   4215 C C   . ASP   B 1 134 ? -15.540 26.226  45.767 1.00 67.74  ? 134 ASP   B C   1 
ATOM   4216 O O   . ASP   B 1 134 ? -15.622 25.441  44.814 1.00 66.81  ? 134 ASP   B O   1 
ATOM   4217 C CB  . ASP   B 1 134 ? -13.065 26.343  45.405 1.00 62.35  ? 134 ASP   B CB  1 
ATOM   4218 C CG  . ASP   B 1 134 ? -12.744 25.126  46.262 1.00 76.25  ? 134 ASP   B CG  1 
ATOM   4219 O OD1 . ASP   B 1 134 ? -13.437 24.889  47.275 1.00 72.64  ? 134 ASP   B OD1 1 
ATOM   4220 O OD2 . ASP   B 1 134 ? -11.791 24.396  45.914 1.00 77.34  ? 134 ASP   B OD2 1 
ATOM   4221 N N   . SER   B 1 135 ? -16.504 26.317  46.683 1.00 60.86  ? 135 SER   B N   1 
ATOM   4222 C CA  . SER   B 1 135 ? -17.660 25.434  46.624 1.00 48.54  ? 135 SER   B CA  1 
ATOM   4223 C C   . SER   B 1 135 ? -18.869 26.111  47.253 1.00 56.44  ? 135 SER   B C   1 
ATOM   4224 O O   . SER   B 1 135 ? -18.744 27.054  48.038 1.00 57.92  ? 135 SER   B O   1 
ATOM   4225 C CB  . SER   B 1 135 ? -17.385 24.098  47.325 1.00 54.70  ? 135 SER   B CB  1 
ATOM   4226 O OG  . SER   B 1 135 ? -17.298 24.267  48.727 1.00 65.23  ? 135 SER   B OG  1 
ATOM   4227 N N   . GLU   B 1 136 ? -20.052 25.601  46.891 1.00 63.90  ? 136 GLU   B N   1 
ATOM   4228 C CA  . GLU   B 1 136 ? -21.306 26.162  47.387 1.00 67.48  ? 136 GLU   B CA  1 
ATOM   4229 C C   . GLU   B 1 136 ? -21.507 25.865  48.870 1.00 73.73  ? 136 GLU   B C   1 
ATOM   4230 O O   . GLU   B 1 136 ? -21.991 26.723  49.621 1.00 65.47  ? 136 GLU   B O   1 
ATOM   4231 C CB  . GLU   B 1 136 ? -22.474 25.615  46.564 1.00 68.63  ? 136 GLU   B CB  1 
ATOM   4232 C CG  . GLU   B 1 136 ? -23.853 26.022  47.058 1.00 83.59  ? 136 GLU   B CG  1 
ATOM   4233 C CD  . GLU   B 1 136 ? -24.968 25.508  46.163 1.00 96.95  ? 136 GLU   B CD  1 
ATOM   4234 O OE1 . GLU   B 1 136 ? -24.673 24.744  45.220 1.00 84.37  ? 136 GLU   B OE1 1 
ATOM   4235 O OE2 . GLU   B 1 136 ? -26.139 25.872  46.402 1.00 112.38 ? 136 GLU   B OE2 1 
ATOM   4236 N N   . VAL   B 1 137 ? -21.161 24.650  49.305 1.00 69.54  ? 137 VAL   B N   1 
ATOM   4237 C CA  . VAL   B 1 137 ? -21.270 24.306  50.720 1.00 65.01  ? 137 VAL   B CA  1 
ATOM   4238 C C   . VAL   B 1 137 ? -20.426 25.257  51.558 1.00 65.06  ? 137 VAL   B C   1 
ATOM   4239 O O   . VAL   B 1 137 ? -20.808 25.641  52.673 1.00 75.41  ? 137 VAL   B O   1 
ATOM   4240 C CB  . VAL   B 1 137 ? -20.865 22.837  50.945 1.00 74.97  ? 137 VAL   B CB  1 
ATOM   4241 C CG1 . VAL   B 1 137 ? -20.756 22.530  52.433 1.00 48.55  ? 137 VAL   B CG1 1 
ATOM   4242 C CG2 . VAL   B 1 137 ? -21.854 21.902  50.264 1.00 64.83  ? 137 VAL   B CG2 1 
ATOM   4243 N N   . GLU   B 1 138 ? -19.266 25.656  51.031 1.00 68.66  ? 138 GLU   B N   1 
ATOM   4244 C CA  . GLU   B 1 138 ? -18.443 26.640  51.722 1.00 62.75  ? 138 GLU   B CA  1 
ATOM   4245 C C   . GLU   B 1 138 ? -19.171 27.973  51.840 1.00 63.01  ? 138 GLU   B C   1 
ATOM   4246 O O   . GLU   B 1 138 ? -19.068 28.653  52.865 1.00 66.70  ? 138 GLU   B O   1 
ATOM   4247 C CB  . GLU   B 1 138 ? -17.108 26.809  50.996 1.00 64.93  ? 138 GLU   B CB  1 
ATOM   4248 C CG  . GLU   B 1 138 ? -15.954 27.231  51.899 1.00 89.04  ? 138 GLU   B CG  1 
ATOM   4249 C CD  . GLU   B 1 138 ? -15.483 26.117  52.827 1.00 94.57  ? 138 GLU   B CD  1 
ATOM   4250 O OE1 . GLU   B 1 138 ? -15.921 24.958  52.655 1.00 81.32  ? 138 GLU   B OE1 1 
ATOM   4251 O OE2 . GLU   B 1 138 ? -14.665 26.400  53.727 1.00 80.54  ? 138 GLU   B OE2 1 
ATOM   4252 N N   . LEU   B 1 139 ? -19.918 28.360  50.799 1.00 69.56  ? 139 LEU   B N   1 
ATOM   4253 C CA  . LEU   B 1 139 ? -20.715 29.583  50.870 1.00 59.29  ? 139 LEU   B CA  1 
ATOM   4254 C C   . LEU   B 1 139 ? -21.792 29.482  51.942 1.00 65.68  ? 139 LEU   B C   1 
ATOM   4255 O O   . LEU   B 1 139 ? -22.043 30.448  52.670 1.00 66.33  ? 139 LEU   B O   1 
ATOM   4256 C CB  . LEU   B 1 139 ? -21.344 29.887  49.511 1.00 57.72  ? 139 LEU   B CB  1 
ATOM   4257 C CG  . LEU   B 1 139 ? -20.437 30.494  48.441 1.00 75.95  ? 139 LEU   B CG  1 
ATOM   4258 C CD1 . LEU   B 1 139 ? -21.176 30.621  47.119 1.00 66.56  ? 139 LEU   B CD1 1 
ATOM   4259 C CD2 . LEU   B 1 139 ? -19.938 31.850  48.901 1.00 65.69  ? 139 LEU   B CD2 1 
ATOM   4260 N N   . MET   B 1 140 ? -22.452 28.325  52.041 1.00 72.03  ? 140 MET   B N   1 
ATOM   4261 C CA  . MET   B 1 140 ? -23.432 28.116  53.105 1.00 63.29  ? 140 MET   B CA  1 
ATOM   4262 C C   . MET   B 1 140 ? -22.784 28.282  54.476 1.00 71.12  ? 140 MET   B C   1 
ATOM   4263 O O   . MET   B 1 140 ? -23.288 29.014  55.343 1.00 65.56  ? 140 MET   B O   1 
ATOM   4264 C CB  . MET   B 1 140 ? -24.044 26.720  52.976 1.00 65.02  ? 140 MET   B CB  1 
ATOM   4265 C CG  . MET   B 1 140 ? -24.834 26.462  51.697 1.00 77.40  ? 140 MET   B CG  1 
ATOM   4266 S SD  . MET   B 1 140 ? -26.606 26.780  51.830 1.00 128.99 ? 140 MET   B SD  1 
ATOM   4267 C CE  . MET   B 1 140 ? -26.668 28.554  51.618 1.00 102.54 ? 140 MET   B CE  1 
ATOM   4268 N N   . LYS   B 1 141 ? -21.643 27.619  54.675 1.00 65.98  ? 141 LYS   B N   1 
ATOM   4269 C CA  . LYS   B 1 141 ? -20.950 27.681  55.956 1.00 59.89  ? 141 LYS   B CA  1 
ATOM   4270 C C   . LYS   B 1 141 ? -20.523 29.105  56.290 1.00 63.84  ? 141 LYS   B C   1 
ATOM   4271 O O   . LYS   B 1 141 ? -20.621 29.534  57.445 1.00 65.19  ? 141 LYS   B O   1 
ATOM   4272 C CB  . LYS   B 1 141 ? -19.743 26.745  55.934 1.00 69.91  ? 141 LYS   B CB  1 
ATOM   4273 C CG  . LYS   B 1 141 ? -20.106 25.269  55.955 1.00 62.33  ? 141 LYS   B CG  1 
ATOM   4274 C CD  . LYS   B 1 141 ? -19.076 24.444  55.202 1.00 74.50  ? 141 LYS   B CD  1 
ATOM   4275 C CE  . LYS   B 1 141 ? -17.678 24.685  55.740 1.00 69.61  ? 141 LYS   B CE  1 
ATOM   4276 N NZ  . LYS   B 1 141 ? -16.645 23.962  54.948 1.00 72.05  ? 141 LYS   B NZ  1 
ATOM   4277 N N   . VAL   B 1 142 ? -20.037 29.850  55.296 1.00 66.40  ? 142 VAL   B N   1 
ATOM   4278 C CA  . VAL   B 1 142 ? -19.606 31.224  55.537 1.00 63.13  ? 142 VAL   B CA  1 
ATOM   4279 C C   . VAL   B 1 142 ? -20.803 32.104  55.876 1.00 66.38  ? 142 VAL   B C   1 
ATOM   4280 O O   . VAL   B 1 142 ? -20.759 32.897  56.822 1.00 72.91  ? 142 VAL   B O   1 
ATOM   4281 C CB  . VAL   B 1 142 ? -18.826 31.763  54.326 1.00 63.14  ? 142 VAL   B CB  1 
ATOM   4282 C CG1 . VAL   B 1 142 ? -18.613 33.260  54.456 1.00 73.76  ? 142 VAL   B CG1 1 
ATOM   4283 C CG2 . VAL   B 1 142 ? -17.488 31.054  54.210 1.00 63.26  ? 142 VAL   B CG2 1 
ATOM   4284 N N   . ALA   B 1 143 ? -21.894 31.971  55.116 1.00 70.17  ? 143 ALA   B N   1 
ATOM   4285 C CA  . ALA   B 1 143 ? -23.110 32.717  55.411 1.00 66.49  ? 143 ALA   B CA  1 
ATOM   4286 C C   . ALA   B 1 143 ? -23.632 32.413  56.802 1.00 69.40  ? 143 ALA   B C   1 
ATOM   4287 O O   . ALA   B 1 143 ? -24.318 33.252  57.399 1.00 73.88  ? 143 ALA   B O   1 
ATOM   4288 C CB  . ALA   B 1 143 ? -24.189 32.404  54.372 1.00 67.59  ? 143 ALA   B CB  1 
ATOM   4289 N N   . ARG   B 1 144 ? -23.295 31.244  57.343 1.00 81.75  ? 144 ARG   B N   1 
ATOM   4290 C CA  . ARG   B 1 144 ? -23.787 30.860  58.660 1.00 71.60  ? 144 ARG   B CA  1 
ATOM   4291 C C   . ARG   B 1 144 ? -22.873 31.348  59.783 1.00 72.67  ? 144 ARG   B C   1 
ATOM   4292 O O   . ARG   B 1 144 ? -23.354 31.905  60.773 1.00 79.62  ? 144 ARG   B O   1 
ATOM   4293 C CB  . ARG   B 1 144 ? -23.938 29.338  58.735 1.00 70.81  ? 144 ARG   B CB  1 
ATOM   4294 C CG  . ARG   B 1 144 ? -24.998 28.864  59.709 1.00 77.36  ? 144 ARG   B CG  1 
ATOM   4295 C CD  . ARG   B 1 144 ? -24.756 27.431  60.156 1.00 95.30  ? 144 ARG   B CD  1 
ATOM   4296 N NE  . ARG   B 1 144 ? -23.681 27.324  61.138 1.00 98.52  ? 144 ARG   B NE  1 
ATOM   4297 C CZ  . ARG   B 1 144 ? -23.266 26.175  61.660 1.00 103.82 ? 144 ARG   B CZ  1 
ATOM   4298 N NH1 . ARG   B 1 144 ? -23.831 25.034  61.289 1.00 107.78 ? 144 ARG   B NH1 1 
ATOM   4299 N NH2 . ARG   B 1 144 ? -22.295 26.166  62.561 1.00 97.60  ? 144 ARG   B NH2 1 
ATOM   4300 N N   . ALA   B 1 145 ? -21.556 31.160  59.642 1.00 79.00  ? 145 ALA   B N   1 
ATOM   4301 C CA  . ALA   B 1 145 ? -20.608 31.473  60.704 1.00 73.91  ? 145 ALA   B CA  1 
ATOM   4302 C C   . ALA   B 1 145 ? -19.757 32.723  60.490 1.00 78.13  ? 145 ALA   B C   1 
ATOM   4303 O O   . ALA   B 1 145 ? -19.074 33.140  61.434 1.00 88.09  ? 145 ALA   B O   1 
ATOM   4304 C CB  . ALA   B 1 145 ? -19.669 30.278  60.927 1.00 74.25  ? 145 ALA   B CB  1 
ATOM   4305 N N   . HIS   B 1 146 ? -19.752 33.329  59.296 1.00 80.40  ? 146 HIS   B N   1 
ATOM   4306 C CA  . HIS   B 1 146 ? -18.938 34.522  59.039 1.00 68.12  ? 146 HIS   B CA  1 
ATOM   4307 C C   . HIS   B 1 146 ? -19.587 35.347  57.935 1.00 77.66  ? 146 HIS   B C   1 
ATOM   4308 O O   . HIS   B 1 146 ? -19.067 35.443  56.819 1.00 76.25  ? 146 HIS   B O   1 
ATOM   4309 C CB  . HIS   B 1 146 ? -17.513 34.115  58.662 1.00 74.23  ? 146 HIS   B CB  1 
ATOM   4310 C CG  . HIS   B 1 146 ? -16.501 35.202  58.831 1.00 70.08  ? 146 HIS   B CG  1 
ATOM   4311 N ND1 . HIS   B 1 146 ? -16.844 36.533  58.913 1.00 77.10  ? 146 HIS   B ND1 1 
ATOM   4312 C CD2 . HIS   B 1 146 ? -15.153 35.151  58.946 1.00 69.44  ? 146 HIS   B CD2 1 
ATOM   4313 C CE1 . HIS   B 1 146 ? -15.750 37.258  59.065 1.00 75.20  ? 146 HIS   B CE1 1 
ATOM   4314 N NE2 . HIS   B 1 146 ? -14.710 36.444  59.088 1.00 65.67  ? 146 HIS   B NE2 1 
ATOM   4315 N N   . PRO   B 1 147 ? -20.733 35.976  58.226 1.00 83.94  ? 147 PRO   B N   1 
ATOM   4316 C CA  . PRO   B 1 147 ? -21.481 36.679  57.162 1.00 75.45  ? 147 PRO   B CA  1 
ATOM   4317 C C   . PRO   B 1 147 ? -20.760 37.854  56.515 1.00 70.14  ? 147 PRO   B C   1 
ATOM   4318 O O   . PRO   B 1 147 ? -20.942 38.082  55.312 1.00 74.37  ? 147 PRO   B O   1 
ATOM   4319 C CB  . PRO   B 1 147 ? -22.760 37.128  57.886 1.00 68.08  ? 147 PRO   B CB  1 
ATOM   4320 C CG  . PRO   B 1 147 ? -22.365 37.211  59.324 1.00 72.31  ? 147 PRO   B CG  1 
ATOM   4321 C CD  . PRO   B 1 147 ? -21.391 36.096  59.537 1.00 68.92  ? 147 PRO   B CD  1 
ATOM   4322 N N   . LYS   B 1 148 ? -19.965 38.621  57.262 1.00 69.25  ? 148 LYS   B N   1 
ATOM   4323 C CA  . LYS   B 1 148 ? -19.303 39.802  56.716 1.00 75.75  ? 148 LYS   B CA  1 
ATOM   4324 C C   . LYS   B 1 148 ? -17.905 39.514  56.181 1.00 78.21  ? 148 LYS   B C   1 
ATOM   4325 O O   . LYS   B 1 148 ? -17.095 40.441  56.065 1.00 76.67  ? 148 LYS   B O   1 
ATOM   4326 C CB  . LYS   B 1 148 ? -19.238 40.934  57.753 1.00 75.56  ? 148 LYS   B CB  1 
ATOM   4327 C CG  . LYS   B 1 148 ? -20.558 41.681  58.033 1.00 67.59  ? 148 LYS   B CG  1 
ATOM   4328 C CD  . LYS   B 1 148 ? -21.752 40.765  58.193 1.00 83.95  ? 148 LYS   B CD  1 
ATOM   4329 C CE  . LYS   B 1 148 ? -23.066 41.485  57.976 1.00 84.64  ? 148 LYS   B CE  1 
ATOM   4330 N NZ  . LYS   B 1 148 ? -24.167 40.503  57.769 1.00 91.98  ? 148 LYS   B NZ  1 
ATOM   4331 N N   . ALA   B 1 149 ? -17.608 38.263  55.848 1.00 71.97  ? 149 ALA   B N   1 
ATOM   4332 C CA  . ALA   B 1 149 ? -16.290 37.933  55.333 1.00 75.04  ? 149 ALA   B CA  1 
ATOM   4333 C C   . ALA   B 1 149 ? -16.120 38.417  53.895 1.00 77.29  ? 149 ALA   B C   1 
ATOM   4334 O O   . ALA   B 1 149 ? -17.088 38.569  53.143 1.00 74.93  ? 149 ALA   B O   1 
ATOM   4335 C CB  . ALA   B 1 149 ? -16.057 36.423  55.402 1.00 72.08  ? 149 ALA   B CB  1 
ATOM   4336 N N   . LYS   B 1 150 ? -14.866 38.665  53.524 1.00 65.80  ? 150 LYS   B N   1 
ATOM   4337 C CA  . LYS   B 1 150 ? -14.487 38.974  52.150 1.00 55.81  ? 150 LYS   B CA  1 
ATOM   4338 C C   . LYS   B 1 150 ? -13.941 37.690  51.537 1.00 64.19  ? 150 LYS   B C   1 
ATOM   4339 O O   . LYS   B 1 150 ? -12.892 37.187  51.961 1.00 65.35  ? 150 LYS   B O   1 
ATOM   4340 C CB  . LYS   B 1 150 ? -13.452 40.097  52.100 1.00 61.37  ? 150 LYS   B CB  1 
ATOM   4341 C CG  . LYS   B 1 150 ? -13.885 41.380  52.793 1.00 58.19  ? 150 LYS   B CG  1 
ATOM   4342 C CD  . LYS   B 1 150 ? -15.282 41.795  52.360 1.00 79.85  ? 150 LYS   B CD  1 
ATOM   4343 C CE  . LYS   B 1 150 ? -15.653 43.164  52.904 1.00 70.56  ? 150 LYS   B CE  1 
ATOM   4344 N NZ  . LYS   B 1 150 ? -17.044 43.545  52.528 1.00 79.89  ? 150 LYS   B NZ  1 
ATOM   4345 N N   . LEU   B 1 151 ? -14.652 37.154  50.550 1.00 60.06  ? 151 LEU   B N   1 
ATOM   4346 C CA  . LEU   B 1 151 ? -14.317 35.854  49.994 1.00 54.91  ? 151 LEU   B CA  1 
ATOM   4347 C C   . LEU   B 1 151 ? -13.517 35.996  48.708 1.00 58.80  ? 151 LEU   B C   1 
ATOM   4348 O O   . LEU   B 1 151 ? -13.774 36.881  47.886 1.00 61.71  ? 151 LEU   B O   1 
ATOM   4349 C CB  . LEU   B 1 151 ? -15.575 35.027  49.737 1.00 55.03  ? 151 LEU   B CB  1 
ATOM   4350 C CG  . LEU   B 1 151 ? -16.294 34.569  51.004 1.00 55.99  ? 151 LEU   B CG  1 
ATOM   4351 C CD1 . LEU   B 1 151 ? -17.262 33.448  50.680 1.00 62.28  ? 151 LEU   B CD1 1 
ATOM   4352 C CD2 . LEU   B 1 151 ? -15.290 34.132  52.061 1.00 55.75  ? 151 LEU   B CD2 1 
ATOM   4353 N N   . VAL   B 1 152 ? -12.540 35.111  48.552 1.00 55.32  ? 152 VAL   B N   1 
ATOM   4354 C CA  . VAL   B 1 152 ? -11.700 35.027  47.368 1.00 53.94  ? 152 VAL   B CA  1 
ATOM   4355 C C   . VAL   B 1 152 ? -11.952 33.667  46.734 1.00 49.56  ? 152 VAL   B C   1 
ATOM   4356 O O   . VAL   B 1 152 ? -11.755 32.628  47.377 1.00 55.49  ? 152 VAL   B O   1 
ATOM   4357 C CB  . VAL   B 1 152 ? -10.216 35.214  47.716 1.00 46.54  ? 152 VAL   B CB  1 
ATOM   4358 C CG1 . VAL   B 1 152 ? -9.367  35.100  46.477 1.00 55.91  ? 152 VAL   B CG1 1 
ATOM   4359 C CG2 . VAL   B 1 152 ? -10.000 36.554  48.401 1.00 45.92  ? 152 VAL   B CG2 1 
ATOM   4360 N N   . LEU   B 1 153 ? -12.394 33.671  45.483 1.00 48.73  ? 153 LEU   B N   1 
ATOM   4361 C CA  . LEU   B 1 153 ? -12.731 32.432  44.798 1.00 47.54  ? 153 LEU   B CA  1 
ATOM   4362 C C   . LEU   B 1 153 ? -11.452 31.788  44.275 1.00 50.45  ? 153 LEU   B C   1 
ATOM   4363 O O   . LEU   B 1 153 ? -10.719 32.400  43.492 1.00 56.29  ? 153 LEU   B O   1 
ATOM   4364 C CB  . LEU   B 1 153 ? -13.716 32.715  43.665 1.00 47.30  ? 153 LEU   B CB  1 
ATOM   4365 C CG  . LEU   B 1 153 ? -14.556 31.582  43.061 1.00 55.75  ? 153 LEU   B CG  1 
ATOM   4366 C CD1 . LEU   B 1 153 ? -15.614 32.174  42.147 1.00 65.94  ? 153 LEU   B CD1 1 
ATOM   4367 C CD2 . LEU   B 1 153 ? -13.727 30.557  42.303 1.00 56.43  ? 153 LEU   B CD2 1 
ATOM   4368 N N   . ARG   B 1 154 ? -11.176 30.562  44.713 1.00 44.52  ? 154 ARG   B N   1 
ATOM   4369 C CA  . ARG   B 1 154 ? -10.015 29.826  44.231 1.00 58.25  ? 154 ARG   B CA  1 
ATOM   4370 C C   . ARG   B 1 154 ? -10.411 29.026  42.997 1.00 53.12  ? 154 ARG   B C   1 
ATOM   4371 O O   . ARG   B 1 154 ? -11.310 28.180  43.060 1.00 51.11  ? 154 ARG   B O   1 
ATOM   4372 C CB  . ARG   B 1 154 ? -9.441  28.905  45.306 1.00 49.77  ? 154 ARG   B CB  1 
ATOM   4373 C CG  . ARG   B 1 154 ? -8.239  28.113  44.806 1.00 50.56  ? 154 ARG   B CG  1 
ATOM   4374 C CD  . ARG   B 1 154 ? -7.431  27.499  45.935 1.00 54.45  ? 154 ARG   B CD  1 
ATOM   4375 N NE  . ARG   B 1 154 ? -6.439  26.555  45.428 1.00 48.48  ? 154 ARG   B NE  1 
ATOM   4376 C CZ  . ARG   B 1 154 ? -5.676  25.785  46.197 1.00 70.73  ? 154 ARG   B CZ  1 
ATOM   4377 N NH1 . ARG   B 1 154 ? -5.784  25.846  47.517 1.00 78.20  ? 154 ARG   B NH1 1 
ATOM   4378 N NH2 . ARG   B 1 154 ? -4.800  24.956  45.645 1.00 78.39  ? 154 ARG   B NH2 1 
ATOM   4379 N N   . ILE   B 1 155 ? -9.728  29.280  41.889 1.00 46.90  ? 155 ILE   B N   1 
ATOM   4380 C CA  . ILE   B 1 155 ? -10.049 28.658  40.619 1.00 60.27  ? 155 ILE   B CA  1 
ATOM   4381 C C   . ILE   B 1 155 ? -9.047  27.547  40.337 1.00 50.64  ? 155 ILE   B C   1 
ATOM   4382 O O   . ILE   B 1 155 ? -7.946  27.504  40.893 1.00 55.67  ? 155 ILE   B O   1 
ATOM   4383 C CB  . ILE   B 1 155 ? -10.074 29.685  39.464 1.00 57.29  ? 155 ILE   B CB  1 
ATOM   4384 C CG1 . ILE   B 1 155 ? -8.697  30.317  39.281 1.00 65.19  ? 155 ILE   B CG1 1 
ATOM   4385 C CG2 . ILE   B 1 155 ? -11.112 30.759  39.731 1.00 53.53  ? 155 ILE   B CG2 1 
ATOM   4386 C CD1 . ILE   B 1 155 ? -8.580  31.155  38.031 1.00 67.97  ? 155 ILE   B CD1 1 
ATOM   4387 N N   . ALA   B 1 156 ? -9.447  26.622  39.471 1.00 56.34  ? 156 ALA   B N   1 
ATOM   4388 C CA  . ALA   B 1 156 ? -8.592  25.507  39.100 1.00 55.30  ? 156 ALA   B CA  1 
ATOM   4389 C C   . ALA   B 1 156 ? -7.511  25.967  38.129 1.00 60.24  ? 156 ALA   B C   1 
ATOM   4390 O O   . ALA   B 1 156 ? -7.675  26.949  37.399 1.00 68.20  ? 156 ALA   B O   1 
ATOM   4391 C CB  . ALA   B 1 156 ? -9.417  24.380  38.477 1.00 60.29  ? 156 ALA   B CB  1 
ATOM   4392 N N   . THR   B 1 157 ? -6.390  25.250  38.137 1.00 70.71  ? 157 THR   B N   1 
ATOM   4393 C CA  . THR   B 1 157 ? -5.269  25.508  37.244 1.00 68.54  ? 157 THR   B CA  1 
ATOM   4394 C C   . THR   B 1 157 ? -4.800  24.205  36.614 1.00 86.58  ? 157 THR   B C   1 
ATOM   4395 O O   . THR   B 1 157 ? -4.979  23.123  37.178 1.00 100.26 ? 157 THR   B O   1 
ATOM   4396 C CB  . THR   B 1 157 ? -4.086  26.166  37.970 1.00 66.98  ? 157 THR   B CB  1 
ATOM   4397 O OG1 . THR   B 1 157 ? -3.542  25.248  38.924 1.00 79.88  ? 157 THR   B OG1 1 
ATOM   4398 C CG2 . THR   B 1 157 ? -4.524  27.438  38.683 1.00 65.52  ? 157 THR   B CG2 1 
ATOM   4399 N N   . ASP   B 1 158 ? -4.206  24.318  35.431 1.00 88.68  ? 158 ASP   B N   1 
ATOM   4400 C CA  . ASP   B 1 158 ? -3.640  23.157  34.756 1.00 84.52  ? 158 ASP   B CA  1 
ATOM   4401 C C   . ASP   B 1 158 ? -2.195  22.949  35.200 1.00 98.24  ? 158 ASP   B C   1 
ATOM   4402 O O   . ASP   B 1 158 ? -1.291  23.658  34.763 1.00 97.36  ? 158 ASP   B O   1 
ATOM   4403 C CB  . ASP   B 1 158 ? -3.701  23.333  33.239 1.00 96.30  ? 158 ASP   B CB  1 
ATOM   4404 C CG  . ASP   B 1 158 ? -3.269  22.088  32.487 1.00 118.10 ? 158 ASP   B CG  1 
ATOM   4405 O OD1 . ASP   B 1 158 ? -3.039  21.044  33.133 1.00 119.27 ? 158 ASP   B OD1 1 
ATOM   4406 O OD2 . ASP   B 1 158 ? -3.142  22.159  31.246 1.00 127.59 ? 158 ASP   B OD2 1 
ATOM   4407 N N   . LEU   B 1 166 ? -2.308  20.142  43.283 1.00 111.60 ? 166 LEU   B N   1 
ATOM   4408 C CA  . LEU   B 1 166 ? -3.334  20.632  44.198 1.00 112.11 ? 166 LEU   B CA  1 
ATOM   4409 C C   . LEU   B 1 166 ? -4.688  20.774  43.497 1.00 102.09 ? 166 LEU   B C   1 
ATOM   4410 O O   . LEU   B 1 166 ? -5.738  20.708  44.146 1.00 91.52  ? 166 LEU   B O   1 
ATOM   4411 C CB  . LEU   B 1 166 ? -2.930  21.983  44.817 1.00 98.85  ? 166 LEU   B CB  1 
ATOM   4412 C CG  . LEU   B 1 166 ? -1.597  22.095  45.558 1.00 101.38 ? 166 LEU   B CG  1 
ATOM   4413 C CD1 . LEU   B 1 166 ? -1.499  23.436  46.263 1.00 97.20  ? 166 LEU   B CD1 1 
ATOM   4414 C CD2 . LEU   B 1 166 ? -1.406  20.962  46.525 1.00 92.91  ? 166 LEU   B CD2 1 
ATOM   4415 N N   . SER   B 1 167 ? -4.644  20.946  42.173 1.00 112.60 ? 167 SER   B N   1 
ATOM   4416 C CA  . SER   B 1 167 ? -5.843  21.189  41.373 1.00 113.61 ? 167 SER   B CA  1 
ATOM   4417 C C   . SER   B 1 167 ? -6.919  20.121  41.549 1.00 103.59 ? 167 SER   B C   1 
ATOM   4418 O O   . SER   B 1 167 ? -8.112  20.434  41.476 1.00 98.99  ? 167 SER   B O   1 
ATOM   4419 C CB  . SER   B 1 167 ? -5.476  21.306  39.893 1.00 98.49  ? 167 SER   B CB  1 
ATOM   4420 O OG  . SER   B 1 167 ? -6.619  21.615  39.122 1.00 100.34 ? 167 SER   B OG  1 
ATOM   4421 N N   . VAL   B 1 168 ? -6.532  18.860  41.764 1.00 101.52 ? 168 VAL   B N   1 
ATOM   4422 C CA  . VAL   B 1 168 ? -7.534  17.807  41.919 1.00 83.89  ? 168 VAL   B CA  1 
ATOM   4423 C C   . VAL   B 1 168 ? -8.367  18.043  43.175 1.00 84.26  ? 168 VAL   B C   1 
ATOM   4424 O O   . VAL   B 1 168 ? -9.589  17.849  43.174 1.00 79.36  ? 168 VAL   B O   1 
ATOM   4425 C CB  . VAL   B 1 168 ? -6.865  16.417  41.920 1.00 89.54  ? 168 VAL   B CB  1 
ATOM   4426 C CG1 . VAL   B 1 168 ? -5.771  16.327  42.989 1.00 78.73  ? 168 VAL   B CG1 1 
ATOM   4427 C CG2 . VAL   B 1 168 ? -7.909  15.323  42.112 1.00 70.56  ? 168 VAL   B CG2 1 
ATOM   4428 N N   . LYS   B 1 169 ? -7.721  18.462  44.264 1.00 81.76  ? 169 LYS   B N   1 
ATOM   4429 C CA  . LYS   B 1 169 ? -8.423  18.649  45.528 1.00 66.95  ? 169 LYS   B CA  1 
ATOM   4430 C C   . LYS   B 1 169 ? -9.157  19.986  45.585 1.00 71.91  ? 169 LYS   B C   1 
ATOM   4431 O O   . LYS   B 1 169 ? -10.268 20.061  46.122 1.00 77.95  ? 169 LYS   B O   1 
ATOM   4432 C CB  . LYS   B 1 169 ? -7.439  18.526  46.692 1.00 74.00  ? 169 LYS   B CB  1 
ATOM   4433 C CG  . LYS   B 1 169 ? -8.082  18.581  48.067 1.00 75.00  ? 169 LYS   B CG  1 
ATOM   4434 C CD  . LYS   B 1 169 ? -7.072  18.225  49.144 1.00 64.64  ? 169 LYS   B CD  1 
ATOM   4435 C CE  . LYS   B 1 169 ? -7.731  18.115  50.506 1.00 66.88  ? 169 LYS   B CE  1 
ATOM   4436 N NZ  . LYS   B 1 169 ? -6.768  17.691  51.558 1.00 61.87  ? 169 LYS   B NZ  1 
ATOM   4437 N N   . PHE   B 1 170 ? -8.553  21.051  45.058 1.00 76.56  ? 170 PHE   B N   1 
ATOM   4438 C CA  . PHE   B 1 170 ? -9.103  22.396  45.173 1.00 74.24  ? 170 PHE   B CA  1 
ATOM   4439 C C   . PHE   B 1 170 ? -9.121  23.099  43.822 1.00 66.53  ? 170 PHE   B C   1 
ATOM   4440 O O   . PHE   B 1 170 ? -8.370  22.760  42.905 1.00 76.18  ? 170 PHE   B O   1 
ATOM   4441 C CB  . PHE   B 1 170 ? -8.308  23.242  46.172 1.00 71.43  ? 170 PHE   B CB  1 
ATOM   4442 C CG  . PHE   B 1 170 ? -8.283  22.675  47.557 1.00 77.53  ? 170 PHE   B CG  1 
ATOM   4443 C CD1 . PHE   B 1 170 ? -9.446  22.585  48.300 1.00 72.49  ? 170 PHE   B CD1 1 
ATOM   4444 C CD2 . PHE   B 1 170 ? -7.097  22.245  48.123 1.00 76.71  ? 170 PHE   B CD2 1 
ATOM   4445 C CE1 . PHE   B 1 170 ? -9.426  22.071  49.579 1.00 86.12  ? 170 PHE   B CE1 1 
ATOM   4446 C CE2 . PHE   B 1 170 ? -7.075  21.731  49.401 1.00 68.79  ? 170 PHE   B CE2 1 
ATOM   4447 C CZ  . PHE   B 1 170 ? -8.239  21.643  50.131 1.00 87.39  ? 170 PHE   B CZ  1 
ATOM   4448 N N   . GLY   B 1 171 ? -9.987  24.106  43.723 1.00 62.03  ? 171 GLY   B N   1 
ATOM   4449 C CA  . GLY   B 1 171 ? -10.068 24.945  42.543 1.00 56.53  ? 171 GLY   B CA  1 
ATOM   4450 C C   . GLY   B 1 171 ? -11.335 24.732  41.741 1.00 63.66  ? 171 GLY   B C   1 
ATOM   4451 O O   . GLY   B 1 171 ? -11.611 23.619  41.285 1.00 69.81  ? 171 GLY   B O   1 
ATOM   4452 N N   . ALA   B 1 172 ? -12.114 25.797  41.568 1.00 70.64  ? 172 ALA   B N   1 
ATOM   4453 C CA  . ALA   B 1 172 ? -13.344 25.745  40.791 1.00 56.37  ? 172 ALA   B CA  1 
ATOM   4454 C C   . ALA   B 1 172 ? -13.072 26.063  39.327 1.00 61.21  ? 172 ALA   B C   1 
ATOM   4455 O O   . ALA   B 1 172 ? -12.239 26.916  39.008 1.00 62.66  ? 172 ALA   B O   1 
ATOM   4456 C CB  . ALA   B 1 172 ? -14.377 26.723  41.355 1.00 52.75  ? 172 ALA   B CB  1 
ATOM   4457 N N   . THR   B 1 173 ? -13.775 25.364  38.439 1.00 52.89  ? 173 THR   B N   1 
ATOM   4458 C CA  . THR   B 1 173 ? -13.750 25.693  37.022 1.00 49.66  ? 173 THR   B CA  1 
ATOM   4459 C C   . THR   B 1 173 ? -14.489 27.009  36.763 1.00 54.43  ? 173 THR   B C   1 
ATOM   4460 O O   . THR   B 1 173 ? -15.233 27.514  37.607 1.00 59.79  ? 173 THR   B O   1 
ATOM   4461 C CB  . THR   B 1 173 ? -14.374 24.565  36.201 1.00 64.17  ? 173 THR   B CB  1 
ATOM   4462 O OG1 . THR   B 1 173 ? -15.740 24.382  36.597 1.00 58.35  ? 173 THR   B OG1 1 
ATOM   4463 C CG2 . THR   B 1 173 ? -13.610 23.264  36.416 1.00 43.11  ? 173 THR   B CG2 1 
ATOM   4464 N N   . LEU   B 1 174 ? -14.278 27.561  35.563 1.00 53.95  ? 174 LEU   B N   1 
ATOM   4465 C CA  . LEU   B 1 174 ? -14.970 28.790  35.178 1.00 59.32  ? 174 LEU   B CA  1 
ATOM   4466 C C   . LEU   B 1 174 ? -16.480 28.589  35.178 1.00 66.67  ? 174 LEU   B C   1 
ATOM   4467 O O   . LEU   B 1 174 ? -17.234 29.451  35.656 1.00 69.57  ? 174 LEU   B O   1 
ATOM   4468 C CB  . LEU   B 1 174 ? -14.494 29.254  33.800 1.00 65.79  ? 174 LEU   B CB  1 
ATOM   4469 C CG  . LEU   B 1 174 ? -13.015 29.616  33.634 1.00 63.45  ? 174 LEU   B CG  1 
ATOM   4470 C CD1 . LEU   B 1 174 ? -12.728 30.062  32.209 1.00 68.18  ? 174 LEU   B CD1 1 
ATOM   4471 C CD2 . LEU   B 1 174 ? -12.610 30.697  34.615 1.00 64.68  ? 174 LEU   B CD2 1 
ATOM   4472 N N   . ARG   B 1 175 ? -16.938 27.456  34.640 1.00 53.44  ? 175 ARG   B N   1 
ATOM   4473 C CA  . ARG   B 1 175 ? -18.359 27.131  34.680 1.00 60.13  ? 175 ARG   B CA  1 
ATOM   4474 C C   . ARG   B 1 175 ? -18.869 27.109  36.112 1.00 59.86  ? 175 ARG   B C   1 
ATOM   4475 O O   . ARG   B 1 175 ? -19.888 27.730  36.433 1.00 66.88  ? 175 ARG   B O   1 
ATOM   4476 C CB  . ARG   B 1 175 ? -18.604 25.780  34.011 1.00 52.31  ? 175 ARG   B CB  1 
ATOM   4477 C CG  . ARG   B 1 175 ? -20.068 25.488  33.785 1.00 74.31  ? 175 ARG   B CG  1 
ATOM   4478 C CD  . ARG   B 1 175 ? -20.277 24.084  33.263 1.00 87.59  ? 175 ARG   B CD  1 
ATOM   4479 N NE  . ARG   B 1 175 ? -21.689 23.818  33.022 1.00 102.78 ? 175 ARG   B NE  1 
ATOM   4480 C CZ  . ARG   B 1 175 ? -22.531 23.396  33.960 1.00 103.97 ? 175 ARG   B CZ  1 
ATOM   4481 N NH1 . ARG   B 1 175 ? -22.098 23.195  35.198 1.00 82.42  ? 175 ARG   B NH1 1 
ATOM   4482 N NH2 . ARG   B 1 175 ? -23.804 23.176  33.664 1.00 107.63 ? 175 ARG   B NH2 1 
ATOM   4483 N N   . THR   B 1 176 ? -18.166 26.392  36.988 1.00 60.57  ? 176 THR   B N   1 
ATOM   4484 C CA  . THR   B 1 176 ? -18.526 26.388  38.399 1.00 59.71  ? 176 THR   B CA  1 
ATOM   4485 C C   . THR   B 1 176 ? -18.366 27.772  39.014 1.00 59.93  ? 176 THR   B C   1 
ATOM   4486 O O   . THR   B 1 176 ? -19.128 28.141  39.914 1.00 60.40  ? 176 THR   B O   1 
ATOM   4487 C CB  . THR   B 1 176 ? -17.674 25.358  39.142 1.00 60.28  ? 176 THR   B CB  1 
ATOM   4488 O OG1 . THR   B 1 176 ? -17.973 24.050  38.641 1.00 63.90  ? 176 THR   B OG1 1 
ATOM   4489 C CG2 . THR   B 1 176 ? -17.957 25.389  40.638 1.00 63.29  ? 176 THR   B CG2 1 
ATOM   4490 N N   . SER   B 1 177 ? -17.386 28.550  38.543 1.00 53.55  ? 177 SER   B N   1 
ATOM   4491 C CA  . SER   B 1 177 ? -17.165 29.885  39.093 1.00 57.34  ? 177 SER   B CA  1 
ATOM   4492 C C   . SER   B 1 177 ? -18.365 30.793  38.862 1.00 61.53  ? 177 SER   B C   1 
ATOM   4493 O O   . SER   B 1 177 ? -18.724 31.590  39.738 1.00 63.73  ? 177 SER   B O   1 
ATOM   4494 C CB  . SER   B 1 177 ? -15.905 30.503  38.489 1.00 64.38  ? 177 SER   B CB  1 
ATOM   4495 O OG  . SER   B 1 177 ? -14.746 29.822  38.932 1.00 67.77  ? 177 SER   B OG  1 
ATOM   4496 N N   . ARG   B 1 178 ? -18.991 30.700  37.685 1.00 56.86  ? 178 ARG   B N   1 
ATOM   4497 C CA  . ARG   B 1 178 ? -20.181 31.507  37.423 1.00 63.32  ? 178 ARG   B CA  1 
ATOM   4498 C C   . ARG   B 1 178 ? -21.278 31.209  38.438 1.00 68.81  ? 178 ARG   B C   1 
ATOM   4499 O O   . ARG   B 1 178 ? -21.869 32.124  39.033 1.00 54.85  ? 178 ARG   B O   1 
ATOM   4500 C CB  . ARG   B 1 178 ? -20.703 31.239  36.011 1.00 66.81  ? 178 ARG   B CB  1 
ATOM   4501 C CG  . ARG   B 1 178 ? -21.770 32.225  35.557 1.00 73.88  ? 178 ARG   B CG  1 
ATOM   4502 C CD  . ARG   B 1 178 ? -22.188 31.999  34.110 1.00 72.88  ? 178 ARG   B CD  1 
ATOM   4503 N NE  . ARG   B 1 178 ? -21.084 32.055  33.158 1.00 107.74 ? 178 ARG   B NE  1 
ATOM   4504 C CZ  . ARG   B 1 178 ? -20.649 33.170  32.580 1.00 106.32 ? 178 ARG   B CZ  1 
ATOM   4505 N NH1 . ARG   B 1 178 ? -21.219 34.336  32.856 1.00 87.65  ? 178 ARG   B NH1 1 
ATOM   4506 N NH2 . ARG   B 1 178 ? -19.646 33.115  31.718 1.00 78.13  ? 178 ARG   B NH2 1 
ATOM   4507 N N   . LEU   B 1 179 ? -21.554 29.921  38.651 1.00 63.25  ? 179 LEU   B N   1 
ATOM   4508 C CA  . LEU   B 1 179 ? -22.593 29.522  39.590 1.00 64.23  ? 179 LEU   B CA  1 
ATOM   4509 C C   . LEU   B 1 179 ? -22.234 29.924  41.012 1.00 64.28  ? 179 LEU   B C   1 
ATOM   4510 O O   . LEU   B 1 179 ? -23.103 30.336  41.784 1.00 73.16  ? 179 LEU   B O   1 
ATOM   4511 C CB  . LEU   B 1 179 ? -22.819 28.013  39.498 1.00 73.82  ? 179 LEU   B CB  1 
ATOM   4512 C CG  . LEU   B 1 179 ? -23.226 27.498  38.116 1.00 69.54  ? 179 LEU   B CG  1 
ATOM   4513 C CD1 . LEU   B 1 179 ? -23.351 25.981  38.116 1.00 74.22  ? 179 LEU   B CD1 1 
ATOM   4514 C CD2 . LEU   B 1 179 ? -24.519 28.152  37.658 1.00 83.66  ? 179 LEU   B CD2 1 
ATOM   4515 N N   . LEU   B 1 180 ? -20.954 29.817  41.374 1.00 63.59  ? 180 LEU   B N   1 
ATOM   4516 C CA  . LEU   B 1 180 ? -20.534 30.214  42.713 1.00 63.60  ? 180 LEU   B CA  1 
ATOM   4517 C C   . LEU   B 1 180 ? -20.726 31.708  42.932 1.00 61.91  ? 180 LEU   B C   1 
ATOM   4518 O O   . LEU   B 1 180 ? -21.198 32.128  43.994 1.00 65.87  ? 180 LEU   B O   1 
ATOM   4519 C CB  . LEU   B 1 180 ? -19.078 29.817  42.949 1.00 60.66  ? 180 LEU   B CB  1 
ATOM   4520 C CG  . LEU   B 1 180 ? -18.830 28.318  43.126 1.00 58.06  ? 180 LEU   B CG  1 
ATOM   4521 C CD1 . LEU   B 1 180 ? -17.352 28.036  43.346 1.00 69.21  ? 180 LEU   B CD1 1 
ATOM   4522 C CD2 . LEU   B 1 180 ? -19.665 27.779  44.276 1.00 61.69  ? 180 LEU   B CD2 1 
ATOM   4523 N N   . LEU   B 1 181 ? -20.384 32.526  41.934 1.00 61.82  ? 181 LEU   B N   1 
ATOM   4524 C CA  . LEU   B 1 181 ? -20.578 33.967  42.072 1.00 71.72  ? 181 LEU   B CA  1 
ATOM   4525 C C   . LEU   B 1 181 ? -22.056 34.321  42.175 1.00 74.10  ? 181 LEU   B C   1 
ATOM   4526 O O   . LEU   B 1 181 ? -22.447 35.152  43.006 1.00 78.43  ? 181 LEU   B O   1 
ATOM   4527 C CB  . LEU   B 1 181 ? -19.929 34.704  40.902 1.00 57.89  ? 181 LEU   B CB  1 
ATOM   4528 C CG  . LEU   B 1 181 ? -18.404 34.722  40.909 1.00 62.23  ? 181 LEU   B CG  1 
ATOM   4529 C CD1 . LEU   B 1 181 ? -17.877 35.281  39.604 1.00 72.86  ? 181 LEU   B CD1 1 
ATOM   4530 C CD2 . LEU   B 1 181 ? -17.896 35.538  42.088 1.00 69.25  ? 181 LEU   B CD2 1 
ATOM   4531 N N   . GLU   B 1 182 ? -22.896 33.699  41.344 1.00 61.22  ? 182 GLU   B N   1 
ATOM   4532 C CA  . GLU   B 1 182 ? -24.326 33.984  41.418 1.00 65.87  ? 182 GLU   B CA  1 
ATOM   4533 C C   . GLU   B 1 182 ? -24.914 33.530  42.753 1.00 67.24  ? 182 GLU   B C   1 
ATOM   4534 O O   . GLU   B 1 182 ? -25.732 34.239  43.354 1.00 73.96  ? 182 GLU   B O   1 
ATOM   4535 C CB  . GLU   B 1 182 ? -25.043 33.329  40.239 1.00 74.24  ? 182 GLU   B CB  1 
ATOM   4536 C CG  . GLU   B 1 182 ? -24.724 34.002  38.909 1.00 84.50  ? 182 GLU   B CG  1 
ATOM   4537 C CD  . GLU   B 1 182 ? -25.236 33.227  37.714 1.00 99.16  ? 182 GLU   B CD  1 
ATOM   4538 O OE1 . GLU   B 1 182 ? -25.399 33.836  36.635 1.00 102.86 ? 182 GLU   B OE1 1 
ATOM   4539 O OE2 . GLU   B 1 182 ? -25.466 32.007  37.847 1.00 100.94 ? 182 GLU   B OE2 1 
ATOM   4540 N N   . ARG   B 1 183 ? -24.493 32.361  43.242 1.00 66.65  ? 183 ARG   B N   1 
ATOM   4541 C CA  . ARG   B 1 183 ? -24.958 31.872  44.536 1.00 73.52  ? 183 ARG   B CA  1 
ATOM   4542 C C   . ARG   B 1 183 ? -24.513 32.790  45.669 1.00 76.82  ? 183 ARG   B C   1 
ATOM   4543 O O   . ARG   B 1 183 ? -25.278 33.047  46.606 1.00 87.38  ? 183 ARG   B O   1 
ATOM   4544 C CB  . ARG   B 1 183 ? -24.450 30.447  44.759 1.00 77.51  ? 183 ARG   B CB  1 
ATOM   4545 C CG  . ARG   B 1 183 ? -24.955 29.775  46.023 1.00 73.69  ? 183 ARG   B CG  1 
ATOM   4546 C CD  . ARG   B 1 183 ? -26.470 29.748  46.080 1.00 79.89  ? 183 ARG   B CD  1 
ATOM   4547 N NE  . ARG   B 1 183 ? -26.945 28.893  47.164 1.00 102.09 ? 183 ARG   B NE  1 
ATOM   4548 C CZ  . ARG   B 1 183 ? -28.104 29.057  47.791 1.00 97.83  ? 183 ARG   B CZ  1 
ATOM   4549 N NH1 . ARG   B 1 183 ? -28.455 28.230  48.766 1.00 85.46  ? 183 ARG   B NH1 1 
ATOM   4550 N NH2 . ARG   B 1 183 ? -28.914 30.048  47.444 1.00 91.70  ? 183 ARG   B NH2 1 
ATOM   4551 N N   . ALA   B 1 184 ? -23.273 33.283  45.608 1.00 78.05  ? 184 ALA   B N   1 
ATOM   4552 C CA  . ALA   B 1 184 ? -22.800 34.227  46.615 1.00 80.21  ? 184 ALA   B CA  1 
ATOM   4553 C C   . ALA   B 1 184 ? -23.614 35.511  46.584 1.00 75.97  ? 184 ALA   B C   1 
ATOM   4554 O O   . ALA   B 1 184 ? -23.907 36.096  47.633 1.00 69.54  ? 184 ALA   B O   1 
ATOM   4555 C CB  . ALA   B 1 184 ? -21.317 34.528  46.399 1.00 65.98  ? 184 ALA   B CB  1 
ATOM   4556 N N   . LYS   B 1 185 ? -23.982 35.970  45.384 1.00 88.48  ? 185 LYS   B N   1 
ATOM   4557 C CA  . LYS   B 1 185 ? -24.850 37.138  45.280 1.00 80.63  ? 185 LYS   B CA  1 
ATOM   4558 C C   . LYS   B 1 185 ? -26.208 36.871  45.918 1.00 78.31  ? 185 LYS   B C   1 
ATOM   4559 O O   . LYS   B 1 185 ? -26.770 37.747  46.587 1.00 76.66  ? 185 LYS   B O   1 
ATOM   4560 C CB  . LYS   B 1 185 ? -25.012 37.550  43.817 1.00 80.36  ? 185 LYS   B CB  1 
ATOM   4561 C CG  . LYS   B 1 185 ? -25.418 39.004  43.639 1.00 81.18  ? 185 LYS   B CG  1 
ATOM   4562 C CD  . LYS   B 1 185 ? -24.358 39.930  44.218 1.00 77.55  ? 185 LYS   B CD  1 
ATOM   4563 C CE  . LYS   B 1 185 ? -24.780 41.388  44.151 1.00 73.08  ? 185 LYS   B CE  1 
ATOM   4564 N NZ  . LYS   B 1 185 ? -23.922 42.247  45.017 1.00 87.29  ? 185 LYS   B NZ  1 
ATOM   4565 N N   . GLU   B 1 186 ? -26.758 35.669  45.713 1.00 84.52  ? 186 GLU   B N   1 
ATOM   4566 C CA  . GLU   B 1 186 ? -28.020 35.313  46.359 1.00 77.30  ? 186 GLU   B CA  1 
ATOM   4567 C C   . GLU   B 1 186 ? -27.920 35.417  47.877 1.00 75.45  ? 186 GLU   B C   1 
ATOM   4568 O O   . GLU   B 1 186 ? -28.837 35.923  48.534 1.00 80.43  ? 186 GLU   B O   1 
ATOM   4569 C CB  . GLU   B 1 186 ? -28.445 33.898  45.962 1.00 81.58  ? 186 GLU   B CB  1 
ATOM   4570 C CG  . GLU   B 1 186 ? -28.959 33.749  44.543 1.00 86.41  ? 186 GLU   B CG  1 
ATOM   4571 C CD  . GLU   B 1 186 ? -29.283 32.306  44.199 1.00 106.59 ? 186 GLU   B CD  1 
ATOM   4572 O OE1 . GLU   B 1 186 ? -29.711 31.561  45.106 1.00 107.86 ? 186 GLU   B OE1 1 
ATOM   4573 O OE2 . GLU   B 1 186 ? -29.117 31.918  43.024 1.00 118.29 ? 186 GLU   B OE2 1 
ATOM   4574 N N   . LEU   B 1 187 ? -26.818 34.941  48.450 1.00 82.73  ? 187 LEU   B N   1 
ATOM   4575 C CA  . LEU   B 1 187 ? -26.657 34.865  49.896 1.00 71.43  ? 187 LEU   B CA  1 
ATOM   4576 C C   . LEU   B 1 187 ? -26.117 36.150  50.512 1.00 75.22  ? 187 LEU   B C   1 
ATOM   4577 O O   . LEU   B 1 187 ? -25.854 36.170  51.719 1.00 77.92  ? 187 LEU   B O   1 
ATOM   4578 C CB  . LEU   B 1 187 ? -25.733 33.699  50.255 1.00 72.31  ? 187 LEU   B CB  1 
ATOM   4579 C CG  . LEU   B 1 187 ? -26.180 32.333  49.739 1.00 71.54  ? 187 LEU   B CG  1 
ATOM   4580 C CD1 . LEU   B 1 187 ? -25.068 31.309  49.889 1.00 83.84  ? 187 LEU   B CD1 1 
ATOM   4581 C CD2 . LEU   B 1 187 ? -27.434 31.880  50.461 1.00 74.25  ? 187 LEU   B CD2 1 
ATOM   4582 N N   . ASN   B 1 188 ? -25.943 37.210  49.719 1.00 75.96  ? 188 ASN   B N   1 
ATOM   4583 C CA  . ASN   B 1 188 ? -25.457 38.500  50.213 1.00 69.41  ? 188 ASN   B CA  1 
ATOM   4584 C C   . ASN   B 1 188 ? -24.065 38.371  50.834 1.00 69.49  ? 188 ASN   B C   1 
ATOM   4585 O O   . ASN   B 1 188 ? -23.782 38.932  51.894 1.00 75.90  ? 188 ASN   B O   1 
ATOM   4586 C CB  . ASN   B 1 188 ? -26.446 39.121  51.205 1.00 73.03  ? 188 ASN   B CB  1 
ATOM   4587 C CG  . ASN   B 1 188 ? -26.175 40.593  51.459 1.00 102.75 ? 188 ASN   B CG  1 
ATOM   4588 O OD1 . ASN   B 1 188 ? -25.689 41.307  50.583 1.00 93.89  ? 188 ASN   B OD1 1 
ATOM   4589 N ND2 . ASN   B 1 188 ? -26.486 41.052  52.666 1.00 105.81 ? 188 ASN   B ND2 1 
ATOM   4590 N N   . ILE   B 1 189 ? -23.192 37.614  50.176 1.00 78.27  ? 189 ILE   B N   1 
ATOM   4591 C CA  . ILE   B 1 189 ? -21.809 37.436  50.606 1.00 67.40  ? 189 ILE   B CA  1 
ATOM   4592 C C   . ILE   B 1 189 ? -20.909 38.199  49.644 1.00 57.55  ? 189 ILE   B C   1 
ATOM   4593 O O   . ILE   B 1 189 ? -21.077 38.106  48.422 1.00 64.47  ? 189 ILE   B O   1 
ATOM   4594 C CB  . ILE   B 1 189 ? -21.424 35.948  50.661 1.00 72.52  ? 189 ILE   B CB  1 
ATOM   4595 C CG1 . ILE   B 1 189 ? -22.244 35.225  51.729 1.00 61.55  ? 189 ILE   B CG1 1 
ATOM   4596 C CG2 . ILE   B 1 189 ? -19.940 35.791  50.942 1.00 71.22  ? 189 ILE   B CG2 1 
ATOM   4597 C CD1 . ILE   B 1 189 ? -21.963 33.743  51.804 1.00 74.25  ? 189 ILE   B CD1 1 
ATOM   4598 N N   . ASP   B 1 190 ? -19.948 38.939  50.191 1.00 59.97  ? 190 ASP   B N   1 
ATOM   4599 C CA  . ASP   B 1 190 ? -19.081 39.800  49.397 1.00 64.93  ? 190 ASP   B CA  1 
ATOM   4600 C C   . ASP   B 1 190 ? -17.898 39.001  48.860 1.00 71.99  ? 190 ASP   B C   1 
ATOM   4601 O O   . ASP   B 1 190 ? -17.086 38.482  49.637 1.00 73.02  ? 190 ASP   B O   1 
ATOM   4602 C CB  . ASP   B 1 190 ? -18.593 40.984  50.230 1.00 77.59  ? 190 ASP   B CB  1 
ATOM   4603 C CG  . ASP   B 1 190 ? -18.002 42.089  49.380 1.00 92.15  ? 190 ASP   B CG  1 
ATOM   4604 O OD1 . ASP   B 1 190 ? -18.225 42.078  48.150 1.00 97.95  ? 190 ASP   B OD1 1 
ATOM   4605 O OD2 . ASP   B 1 190 ? -17.317 42.970  49.940 1.00 85.67  ? 190 ASP   B OD2 1 
ATOM   4606 N N   . VAL   B 1 191 ? -17.793 38.925  47.536 1.00 60.25  ? 191 VAL   B N   1 
ATOM   4607 C CA  . VAL   B 1 191 ? -16.652 38.317  46.861 1.00 57.12  ? 191 VAL   B CA  1 
ATOM   4608 C C   . VAL   B 1 191 ? -15.768 39.443  46.345 1.00 56.39  ? 191 VAL   B C   1 
ATOM   4609 O O   . VAL   B 1 191 ? -16.219 40.290  45.565 1.00 57.79  ? 191 VAL   B O   1 
ATOM   4610 C CB  . VAL   B 1 191 ? -17.096 37.393  45.718 1.00 53.49  ? 191 VAL   B CB  1 
ATOM   4611 C CG1 . VAL   B 1 191 ? -15.884 36.839  44.992 1.00 56.34  ? 191 VAL   B CG1 1 
ATOM   4612 C CG2 . VAL   B 1 191 ? -17.957 36.265  46.257 1.00 63.11  ? 191 VAL   B CG2 1 
ATOM   4613 N N   . VAL   B 1 192 ? -14.510 39.458  46.784 1.00 56.13  ? 192 VAL   B N   1 
ATOM   4614 C CA  . VAL   B 1 192 ? -13.616 40.583  46.529 1.00 51.17  ? 192 VAL   B CA  1 
ATOM   4615 C C   . VAL   B 1 192 ? -12.474 40.244  45.585 1.00 57.23  ? 192 VAL   B C   1 
ATOM   4616 O O   . VAL   B 1 192 ? -11.712 41.155  45.214 1.00 61.08  ? 192 VAL   B O   1 
ATOM   4617 C CB  . VAL   B 1 192 ? -13.053 41.160  47.843 1.00 49.04  ? 192 VAL   B CB  1 
ATOM   4618 C CG1 . VAL   B 1 192 ? -14.186 41.612  48.744 1.00 57.25  ? 192 VAL   B CG1 1 
ATOM   4619 C CG2 . VAL   B 1 192 ? -12.181 40.133  48.549 1.00 53.70  ? 192 VAL   B CG2 1 
ATOM   4620 N N   . GLY   B 1 193 ? -12.319 38.990  45.182 1.00 45.33  ? 193 GLY   B N   1 
ATOM   4621 C CA  . GLY   B 1 193 ? -11.219 38.667  44.299 1.00 46.73  ? 193 GLY   B CA  1 
ATOM   4622 C C   . GLY   B 1 193 ? -11.177 37.195  43.960 1.00 52.12  ? 193 GLY   B C   1 
ATOM   4623 O O   . GLY   B 1 193 ? -12.113 36.438  44.226 1.00 46.55  ? 193 GLY   B O   1 
ATOM   4624 N N   . VAL   B 1 194 ? -10.051 36.813  43.365 1.00 51.71  ? 194 VAL   B N   1 
ATOM   4625 C CA  . VAL   B 1 194 ? -9.817  35.469  42.846 1.00 53.89  ? 194 VAL   B CA  1 
ATOM   4626 C C   . VAL   B 1 194 ? -8.417  35.034  43.247 1.00 55.99  ? 194 VAL   B C   1 
ATOM   4627 O O   . VAL   B 1 194 ? -7.485  35.844  43.249 1.00 59.95  ? 194 VAL   B O   1 
ATOM   4628 C CB  . VAL   B 1 194 ? -9.977  35.413  41.310 1.00 49.55  ? 194 VAL   B CB  1 
ATOM   4629 C CG1 . VAL   B 1 194 ? -9.671  34.018  40.785 1.00 48.24  ? 194 VAL   B CG1 1 
ATOM   4630 C CG2 . VAL   B 1 194 ? -11.370 35.841  40.905 1.00 53.25  ? 194 VAL   B CG2 1 
ATOM   4631 N N   . SER   B 1 195 ? -8.270  33.756  43.593 1.00 55.80  ? 195 SER   B N   1 
ATOM   4632 C CA  . SER   B 1 195 ? -6.975  33.183  43.922 1.00 54.83  ? 195 SER   B CA  1 
ATOM   4633 C C   . SER   B 1 195 ? -6.760  31.913  43.113 1.00 49.56  ? 195 SER   B C   1 
ATOM   4634 O O   . SER   B 1 195 ? -7.708  31.270  42.659 1.00 53.58  ? 195 SER   B O   1 
ATOM   4635 C CB  . SER   B 1 195 ? -6.849  32.853  45.416 1.00 52.94  ? 195 SER   B CB  1 
ATOM   4636 O OG  . SER   B 1 195 ? -7.561  31.671  45.737 1.00 57.19  ? 195 SER   B OG  1 
ATOM   4637 N N   . PHE   B 1 196 ? -5.491  31.568  42.926 1.00 40.34  ? 196 PHE   B N   1 
ATOM   4638 C CA  . PHE   B 1 196 ? -5.151  30.301  42.296 1.00 44.34  ? 196 PHE   B CA  1 
ATOM   4639 C C   . PHE   B 1 196 ? -3.796  29.849  42.819 1.00 50.39  ? 196 PHE   B C   1 
ATOM   4640 O O   . PHE   B 1 196 ? -3.035  30.635  43.387 1.00 54.80  ? 196 PHE   B O   1 
ATOM   4641 C CB  . PHE   B 1 196 ? -5.160  30.395  40.761 1.00 42.49  ? 196 PHE   B CB  1 
ATOM   4642 C CG  . PHE   B 1 196 ? -4.139  31.341  40.190 1.00 54.98  ? 196 PHE   B CG  1 
ATOM   4643 C CD1 . PHE   B 1 196 ? -2.820  30.946  40.018 1.00 49.58  ? 196 PHE   B CD1 1 
ATOM   4644 C CD2 . PHE   B 1 196 ? -4.502  32.622  39.810 1.00 51.66  ? 196 PHE   B CD2 1 
ATOM   4645 C CE1 . PHE   B 1 196 ? -1.884  31.813  39.491 1.00 53.33  ? 196 PHE   B CE1 1 
ATOM   4646 C CE2 . PHE   B 1 196 ? -3.568  33.493  39.281 1.00 56.26  ? 196 PHE   B CE2 1 
ATOM   4647 C CZ  . PHE   B 1 196 ? -2.258  33.088  39.120 1.00 49.67  ? 196 PHE   B CZ  1 
ATOM   4648 N N   . HIS   B 1 197 ? -3.505  28.565  42.624 1.00 42.19  ? 197 HIS   B N   1 
ATOM   4649 C CA  . HIS   B 1 197 ? -2.221  27.998  43.025 1.00 43.63  ? 197 HIS   B CA  1 
ATOM   4650 C C   . HIS   B 1 197 ? -1.731  27.121  41.883 1.00 43.26  ? 197 HIS   B C   1 
ATOM   4651 O O   . HIS   B 1 197 ? -2.302  26.058  41.622 1.00 51.87  ? 197 HIS   B O   1 
ATOM   4652 C CB  . HIS   B 1 197 ? -2.340  27.208  44.330 1.00 44.49  ? 197 HIS   B CB  1 
ATOM   4653 C CG  . HIS   B 1 197 ? -1.020  26.834  44.929 1.00 55.77  ? 197 HIS   B CG  1 
ATOM   4654 N ND1 . HIS   B 1 197 ? -0.193  25.879  44.380 1.00 71.74  ? 197 HIS   B ND1 1 
ATOM   4655 C CD2 . HIS   B 1 197 ? -0.370  27.312  46.016 1.00 62.22  ? 197 HIS   B CD2 1 
ATOM   4656 C CE1 . HIS   B 1 197 ? 0.902   25.773  45.112 1.00 62.32  ? 197 HIS   B CE1 1 
ATOM   4657 N NE2 . HIS   B 1 197 ? 0.819   26.633  46.110 1.00 62.52  ? 197 HIS   B NE2 1 
ATOM   4658 N N   . VAL   B 1 198 ? -0.667  27.564  41.209 1.00 52.80  ? 198 VAL   B N   1 
ATOM   4659 C CA  . VAL   B 1 198 ? -0.157  26.857  40.039 1.00 60.60  ? 198 VAL   B CA  1 
ATOM   4660 C C   . VAL   B 1 198 ? 0.455   25.514  40.422 1.00 60.43  ? 198 VAL   B C   1 
ATOM   4661 O O   . VAL   B 1 198 ? 0.551   24.609  39.584 1.00 78.12  ? 198 VAL   B O   1 
ATOM   4662 C CB  . VAL   B 1 198 ? 0.836   27.778  39.301 1.00 64.62  ? 198 VAL   B CB  1 
ATOM   4663 C CG1 . VAL   B 1 198 ? 1.680   27.014  38.302 1.00 70.33  ? 198 VAL   B CG1 1 
ATOM   4664 C CG2 . VAL   B 1 198 ? 0.081   28.897  38.601 1.00 68.36  ? 198 VAL   B CG2 1 
ATOM   4665 N N   . GLY   B 1 199 ? 0.812   25.340  41.678 1.00 55.21  ? 199 GLY   B N   1 
ATOM   4666 C CA  . GLY   B 1 199 ? 1.403   24.119  42.174 1.00 54.00  ? 199 GLY   B CA  1 
ATOM   4667 C C   . GLY   B 1 199 ? 2.881   24.282  42.471 1.00 79.27  ? 199 GLY   B C   1 
ATOM   4668 O O   . GLY   B 1 199 ? 3.604   25.038  41.808 1.00 72.75  ? 199 GLY   B O   1 
ATOM   4669 N N   . SER   B 1 200 ? 3.333   23.566  43.495 1.00 94.46  ? 200 SER   B N   1 
ATOM   4670 C CA  . SER   B 1 200 ? 4.727   23.611  43.912 1.00 93.59  ? 200 SER   B CA  1 
ATOM   4671 C C   . SER   B 1 200 ? 5.621   22.953  42.870 1.00 88.76  ? 200 SER   B C   1 
ATOM   4672 O O   . SER   B 1 200 ? 5.312   21.868  42.368 1.00 94.83  ? 200 SER   B O   1 
ATOM   4673 C CB  . SER   B 1 200 ? 4.888   22.922  45.264 1.00 95.11  ? 200 SER   B CB  1 
ATOM   4674 O OG  . SER   B 1 200 ? 6.230   22.983  45.700 1.00 108.90 ? 200 SER   B OG  1 
ATOM   4675 N N   . GLY   B 1 201 ? 6.729   23.613  42.546 1.00 91.56  ? 201 GLY   B N   1 
ATOM   4676 C CA  . GLY   B 1 201 ? 7.647   23.094  41.554 1.00 101.62 ? 201 GLY   B CA  1 
ATOM   4677 C C   . GLY   B 1 201 ? 7.040   22.934  40.177 1.00 114.57 ? 201 GLY   B C   1 
ATOM   4678 O O   . GLY   B 1 201 ? 7.180   21.881  39.547 1.00 130.68 ? 201 GLY   B O   1 
ATOM   4679 N N   . CYS   B 1 202 ? 6.352   23.974  39.706 1.00 122.58 ? 202 CYS   B N   1 
ATOM   4680 C CA  . CYS   B 1 202 ? 5.755   23.955  38.376 1.00 117.99 ? 202 CYS   B CA  1 
ATOM   4681 C C   . CYS   B 1 202 ? 6.850   23.932  37.316 1.00 110.61 ? 202 CYS   B C   1 
ATOM   4682 O O   . CYS   B 1 202 ? 7.825   24.685  37.401 1.00 118.21 ? 202 CYS   B O   1 
ATOM   4683 C CB  . CYS   B 1 202 ? 4.847   25.163  38.172 1.00 110.66 ? 202 CYS   B CB  1 
ATOM   4684 S SG  . CYS   B 1 202 ? 4.052   25.178  36.547 1.00 103.27 ? 202 CYS   B SG  1 
ATOM   4685 N N   . THR   B 1 203 ? 6.690   23.061  36.317 1.00 108.49 ? 203 THR   B N   1 
ATOM   4686 C CA  . THR   B 1 203 ? 7.696   22.938  35.267 1.00 113.09 ? 203 THR   B CA  1 
ATOM   4687 C C   . THR   B 1 203 ? 7.551   24.012  34.191 1.00 107.25 ? 203 THR   B C   1 
ATOM   4688 O O   . THR   B 1 203 ? 8.559   24.516  33.682 1.00 96.63  ? 203 THR   B O   1 
ATOM   4689 C CB  . THR   B 1 203 ? 7.621   21.542  34.638 1.00 99.22  ? 203 THR   B CB  1 
ATOM   4690 O OG1 . THR   B 1 203 ? 7.928   20.555  35.629 1.00 120.23 ? 203 THR   B OG1 1 
ATOM   4691 C CG2 . THR   B 1 203 ? 8.610   21.407  33.486 1.00 75.18  ? 203 THR   B CG2 1 
ATOM   4692 N N   . ASP   B 1 204 ? 6.325   24.401  33.843 1.00 101.18 ? 204 ASP   B N   1 
ATOM   4693 C CA  . ASP   B 1 204 ? 6.134   25.328  32.736 1.00 80.76  ? 204 ASP   B CA  1 
ATOM   4694 C C   . ASP   B 1 204 ? 5.559   26.638  33.250 1.00 82.19  ? 204 ASP   B C   1 
ATOM   4695 O O   . ASP   B 1 204 ? 4.441   26.653  33.787 1.00 87.32  ? 204 ASP   B O   1 
ATOM   4696 C CB  . ASP   B 1 204 ? 5.207   24.712  31.688 1.00 82.23  ? 204 ASP   B CB  1 
ATOM   4697 C CG  . ASP   B 1 204 ? 5.000   25.607  30.478 1.00 101.19 ? 204 ASP   B CG  1 
ATOM   4698 O OD1 . ASP   B 1 204 ? 5.699   26.633  30.353 1.00 104.12 ? 204 ASP   B OD1 1 
ATOM   4699 O OD2 . ASP   B 1 204 ? 4.134   25.275  29.641 1.00 100.89 ? 204 ASP   B OD2 1 
ATOM   4700 N N   . PRO   B 1 205 ? 6.273   27.756  33.083 1.00 80.78  ? 205 PRO   B N   1 
ATOM   4701 C CA  . PRO   B 1 205 ? 5.751   29.038  33.582 1.00 70.25  ? 205 PRO   B CA  1 
ATOM   4702 C C   . PRO   B 1 205 ? 4.499   29.512  32.864 1.00 75.59  ? 205 PRO   B C   1 
ATOM   4703 O O   . PRO   B 1 205 ? 3.727   30.284  33.447 1.00 77.83  ? 205 PRO   B O   1 
ATOM   4704 C CB  . PRO   B 1 205 ? 6.925   30.004  33.362 1.00 74.82  ? 205 PRO   B CB  1 
ATOM   4705 C CG  . PRO   B 1 205 ? 7.759   29.366  32.301 1.00 81.31  ? 205 PRO   B CG  1 
ATOM   4706 C CD  . PRO   B 1 205 ? 7.619   27.887  32.500 1.00 81.15  ? 205 PRO   B CD  1 
ATOM   4707 N N   . GLU   B 1 206 ? 4.294   29.101  31.606 1.00 72.88  ? 206 GLU   B N   1 
ATOM   4708 C CA  . GLU   B 1 206 ? 3.116   29.519  30.846 1.00 72.98  ? 206 GLU   B CA  1 
ATOM   4709 C C   . GLU   B 1 206 ? 1.816   29.261  31.592 1.00 66.92  ? 206 GLU   B C   1 
ATOM   4710 O O   . GLU   B 1 206 ? 0.834   29.991  31.398 1.00 70.16  ? 206 GLU   B O   1 
ATOM   4711 C CB  . GLU   B 1 206 ? 3.088   28.817  29.491 1.00 77.13  ? 206 GLU   B CB  1 
ATOM   4712 C CG  . GLU   B 1 206 ? 4.224   29.222  28.571 1.00 99.94  ? 206 GLU   B CG  1 
ATOM   4713 C CD  . GLU   B 1 206 ? 4.255   30.721  28.320 1.00 104.82 ? 206 GLU   B CD  1 
ATOM   4714 O OE1 . GLU   B 1 206 ? 3.180   31.310  28.071 1.00 92.45  ? 206 GLU   B OE1 1 
ATOM   4715 O OE2 . GLU   B 1 206 ? 5.355   31.312  28.367 1.00 90.58  ? 206 GLU   B OE2 1 
ATOM   4716 N N   . THR   B 1 207 ? 1.797   28.243  32.456 1.00 65.94  ? 207 THR   B N   1 
ATOM   4717 C CA  . THR   B 1 207 ? 0.622   27.974  33.275 1.00 68.64  ? 207 THR   B CA  1 
ATOM   4718 C C   . THR   B 1 207 ? 0.149   29.242  33.977 1.00 63.42  ? 207 THR   B C   1 
ATOM   4719 O O   . THR   B 1 207 ? -1.039  29.584  33.931 1.00 68.18  ? 207 THR   B O   1 
ATOM   4720 C CB  . THR   B 1 207 ? 0.940   26.897  34.315 1.00 67.76  ? 207 THR   B CB  1 
ATOM   4721 O OG1 . THR   B 1 207 ? 1.315   25.678  33.664 1.00 77.07  ? 207 THR   B OG1 1 
ATOM   4722 C CG2 . THR   B 1 207 ? -0.264  26.649  35.206 1.00 64.94  ? 207 THR   B CG2 1 
ATOM   4723 N N   . PHE   B 1 208 ? 1.082   29.966  34.610 1.00 60.66  ? 208 PHE   B N   1 
ATOM   4724 C CA  . PHE   B 1 208 ? 0.743   31.221  35.277 1.00 56.95  ? 208 PHE   B CA  1 
ATOM   4725 C C   . PHE   B 1 208 ? -0.046  32.135  34.352 1.00 57.13  ? 208 PHE   B C   1 
ATOM   4726 O O   . PHE   B 1 208 ? -1.126  32.620  34.712 1.00 56.87  ? 208 PHE   B O   1 
ATOM   4727 C CB  . PHE   B 1 208 ? 2.012   31.925  35.757 1.00 58.51  ? 208 PHE   B CB  1 
ATOM   4728 C CG  . PHE   B 1 208 ? 2.488   31.464  37.098 1.00 68.79  ? 208 PHE   B CG  1 
ATOM   4729 C CD1 . PHE   B 1 208 ? 3.461   30.489  37.197 1.00 62.30  ? 208 PHE   B CD1 1 
ATOM   4730 C CD2 . PHE   B 1 208 ? 1.973   32.014  38.262 1.00 59.30  ? 208 PHE   B CD2 1 
ATOM   4731 C CE1 . PHE   B 1 208 ? 3.908   30.058  38.428 1.00 67.34  ? 208 PHE   B CE1 1 
ATOM   4732 C CE2 . PHE   B 1 208 ? 2.416   31.586  39.503 1.00 66.83  ? 208 PHE   B CE2 1 
ATOM   4733 C CZ  . PHE   B 1 208 ? 3.387   30.606  39.585 1.00 79.45  ? 208 PHE   B CZ  1 
ATOM   4734 N N   . VAL   B 1 209 ? 0.457   32.332  33.129 1.00 57.51  ? 209 VAL   B N   1 
ATOM   4735 C CA  . VAL   B 1 209 ? -0.241  33.179  32.165 1.00 55.61  ? 209 VAL   B CA  1 
ATOM   4736 C C   . VAL   B 1 209 ? -1.677  32.705  32.011 1.00 60.36  ? 209 VAL   B C   1 
ATOM   4737 O O   . VAL   B 1 209 ? -2.632  33.469  32.219 1.00 61.10  ? 209 VAL   B O   1 
ATOM   4738 C CB  . VAL   B 1 209 ? 0.499   33.179  30.816 1.00 54.86  ? 209 VAL   B CB  1 
ATOM   4739 C CG1 . VAL   B 1 209 ? -0.218  34.070  29.820 1.00 49.08  ? 209 VAL   B CG1 1 
ATOM   4740 C CG2 . VAL   B 1 209 ? 1.938   33.626  31.006 1.00 56.21  ? 209 VAL   B CG2 1 
ATOM   4741 N N   . GLN   B 1 210 ? -1.846  31.410  31.729 1.00 54.50  ? 210 GLN   B N   1 
ATOM   4742 C CA  . GLN   B 1 210 ? -3.187  30.858  31.595 1.00 61.59  ? 210 GLN   B CA  1 
ATOM   4743 C C   . GLN   B 1 210 ? -4.009  31.154  32.836 1.00 58.12  ? 210 GLN   B C   1 
ATOM   4744 O O   . GLN   B 1 210 ? -5.113  31.706  32.748 1.00 58.67  ? 210 GLN   B O   1 
ATOM   4745 C CB  . GLN   B 1 210 ? -3.114  29.352  31.336 1.00 60.05  ? 210 GLN   B CB  1 
ATOM   4746 C CG  . GLN   B 1 210 ? -4.474  28.697  31.180 1.00 67.08  ? 210 GLN   B CG  1 
ATOM   4747 C CD  . GLN   B 1 210 ? -5.257  29.248  30.010 1.00 89.85  ? 210 GLN   B CD  1 
ATOM   4748 O OE1 . GLN   B 1 210 ? -4.793  29.230  28.870 1.00 105.81 ? 210 GLN   B OE1 1 
ATOM   4749 N NE2 . GLN   B 1 210 ? -6.456  29.747  30.289 1.00 77.38  ? 210 GLN   B NE2 1 
ATOM   4750 N N   . ALA   B 1 211 ? -3.442  30.868  34.011 1.00 61.12  ? 211 ALA   B N   1 
ATOM   4751 C CA  . ALA   B 1 211 ? -4.159  31.120  35.252 1.00 52.50  ? 211 ALA   B CA  1 
ATOM   4752 C C   . ALA   B 1 211 ? -4.559  32.582  35.346 1.00 61.00  ? 211 ALA   B C   1 
ATOM   4753 O O   . ALA   B 1 211 ? -5.727  32.904  35.608 1.00 60.15  ? 211 ALA   B O   1 
ATOM   4754 C CB  . ALA   B 1 211 ? -3.301  30.706  36.447 1.00 53.32  ? 211 ALA   B CB  1 
ATOM   4755 N N   . ILE   B 1 212 ? -3.616  33.483  35.059 1.00 61.48  ? 212 ILE   B N   1 
ATOM   4756 C CA  . ILE   B 1 212 ? -3.924  34.907  35.125 1.00 60.08  ? 212 ILE   B CA  1 
ATOM   4757 C C   . ILE   B 1 212 ? -5.079  35.225  34.188 1.00 65.55  ? 212 ILE   B C   1 
ATOM   4758 O O   . ILE   B 1 212 ? -6.052  35.886  34.575 1.00 70.24  ? 212 ILE   B O   1 
ATOM   4759 C CB  . ILE   B 1 212 ? -2.675  35.747  34.809 1.00 52.73  ? 212 ILE   B CB  1 
ATOM   4760 C CG1 . ILE   B 1 212 ? -1.634  35.566  35.914 1.00 42.06  ? 212 ILE   B CG1 1 
ATOM   4761 C CG2 . ILE   B 1 212 ? -3.043  37.215  34.648 1.00 50.72  ? 212 ILE   B CG2 1 
ATOM   4762 C CD1 . ILE   B 1 212 ? -0.280  36.131  35.580 1.00 61.89  ? 212 ILE   B CD1 1 
ATOM   4763 N N   . SER   B 1 213 ? -5.025  34.682  32.967 1.00 58.02  ? 213 SER   B N   1 
ATOM   4764 C CA  . SER   B 1 213 ? -6.114  34.896  32.024 1.00 60.72  ? 213 SER   B CA  1 
ATOM   4765 C C   . SER   B 1 213 ? -7.430  34.433  32.624 1.00 63.92  ? 213 SER   B C   1 
ATOM   4766 O O   . SER   B 1 213 ? -8.413  35.187  32.657 1.00 59.07  ? 213 SER   B O   1 
ATOM   4767 C CB  . SER   B 1 213 ? -5.837  34.147  30.722 1.00 63.03  ? 213 SER   B CB  1 
ATOM   4768 O OG  . SER   B 1 213 ? -4.693  34.657  30.067 1.00 102.53 ? 213 SER   B OG  1 
ATOM   4769 N N   . ASP   B 1 214 ? -7.437  33.217  33.178 1.00 64.27  ? 214 ASP   B N   1 
ATOM   4770 C CA  . ASP   B 1 214 ? -8.654  32.697  33.784 1.00 59.76  ? 214 ASP   B CA  1 
ATOM   4771 C C   . ASP   B 1 214 ? -9.146  33.632  34.874 1.00 59.85  ? 214 ASP   B C   1 
ATOM   4772 O O   . ASP   B 1 214 ? -10.341 33.951  34.934 1.00 63.09  ? 214 ASP   B O   1 
ATOM   4773 C CB  . ASP   B 1 214 ? -8.404  31.294  34.339 1.00 65.35  ? 214 ASP   B CB  1 
ATOM   4774 C CG  . ASP   B 1 214 ? -8.161  30.269  33.246 1.00 72.23  ? 214 ASP   B CG  1 
ATOM   4775 O OD1 . ASP   B 1 214 ? -8.497  30.553  32.078 1.00 87.29  ? 214 ASP   B OD1 1 
ATOM   4776 O OD2 . ASP   B 1 214 ? -7.625  29.183  33.555 1.00 75.39  ? 214 ASP   B OD2 1 
ATOM   4777 N N   . ALA   B 1 215 ? -8.223  34.144  35.695 1.00 66.57  ? 215 ALA   B N   1 
ATOM   4778 C CA  . ALA   B 1 215 ? -8.620  35.054  36.760 1.00 54.34  ? 215 ALA   B CA  1 
ATOM   4779 C C   . ALA   B 1 215 ? -9.338  36.262  36.185 1.00 59.36  ? 215 ALA   B C   1 
ATOM   4780 O O   . ALA   B 1 215 ? -10.415 36.640  36.666 1.00 60.89  ? 215 ALA   B O   1 
ATOM   4781 C CB  . ALA   B 1 215 ? -7.398  35.478  37.571 1.00 70.37  ? 215 ALA   B CB  1 
ATOM   4782 N N   . ARG   B 1 216 ? -8.791  36.832  35.106 1.00 64.80  ? 216 ARG   B N   1 
ATOM   4783 C CA  . ARG   B 1 216 ? -9.427  37.972  34.461 1.00 68.54  ? 216 ARG   B CA  1 
ATOM   4784 C C   . ARG   B 1 216 ? -10.871 37.640  34.124 1.00 65.00  ? 216 ARG   B C   1 
ATOM   4785 O O   . ARG   B 1 216 ? -11.794 38.392  34.464 1.00 71.51  ? 216 ARG   B O   1 
ATOM   4786 C CB  . ARG   B 1 216 ? -8.649  38.348  33.199 1.00 73.89  ? 216 ARG   B CB  1 
ATOM   4787 C CG  . ARG   B 1 216 ? -9.247  39.478  32.372 1.00 79.54  ? 216 ARG   B CG  1 
ATOM   4788 C CD  . ARG   B 1 216 ? -9.049  40.834  33.027 1.00 73.57  ? 216 ARG   B CD  1 
ATOM   4789 N NE  . ARG   B 1 216 ? -10.192 41.263  33.823 1.00 79.28  ? 216 ARG   B NE  1 
ATOM   4790 C CZ  . ARG   B 1 216 ? -10.170 42.305  34.649 1.00 86.03  ? 216 ARG   B CZ  1 
ATOM   4791 N NH1 . ARG   B 1 216 ? -9.061  43.020  34.786 1.00 81.25  ? 216 ARG   B NH1 1 
ATOM   4792 N NH2 . ARG   B 1 216 ? -11.254 42.633  35.338 1.00 91.78  ? 216 ARG   B NH2 1 
ATOM   4793 N N   . CYS   B 1 217 ? -11.084 36.460  33.533 1.00 57.61  ? 217 CYS   B N   1 
ATOM   4794 C CA  . CYS   B 1 217 ? -12.430 36.041  33.169 1.00 63.69  ? 217 CYS   B CA  1 
ATOM   4795 C C   . CYS   B 1 217 ? -13.355 36.090  34.377 1.00 66.76  ? 217 CYS   B C   1 
ATOM   4796 O O   . CYS   B 1 217 ? -14.427 36.708  34.329 1.00 67.75  ? 217 CYS   B O   1 
ATOM   4797 C CB  . CYS   B 1 217 ? -12.388 34.636  32.565 1.00 63.57  ? 217 CYS   B CB  1 
ATOM   4798 S SG  . CYS   B 1 217 ? -13.993 33.972  32.085 1.00 112.83 ? 217 CYS   B SG  1 
ATOM   4799 N N   . VAL   B 1 218 ? -12.924 35.499  35.495 1.00 67.18  ? 218 VAL   B N   1 
ATOM   4800 C CA  . VAL   B 1 218 ? -13.788 35.461  36.670 1.00 66.17  ? 218 VAL   B CA  1 
ATOM   4801 C C   . VAL   B 1 218 ? -14.037 36.873  37.176 1.00 64.92  ? 218 VAL   B C   1 
ATOM   4802 O O   . VAL   B 1 218 ? -15.155 37.212  37.587 1.00 74.16  ? 218 VAL   B O   1 
ATOM   4803 C CB  . VAL   B 1 218 ? -13.186 34.558  37.762 1.00 62.79  ? 218 VAL   B CB  1 
ATOM   4804 C CG1 . VAL   B 1 218 ? -14.068 34.562  39.002 1.00 51.83  ? 218 VAL   B CG1 1 
ATOM   4805 C CG2 . VAL   B 1 218 ? -13.021 33.143  37.238 1.00 56.21  ? 218 VAL   B CG2 1 
ATOM   4806 N N   . PHE   B 1 219 ? -13.009 37.727  37.127 1.00 64.99  ? 219 PHE   B N   1 
ATOM   4807 C CA  . PHE   B 1 219 ? -13.202 39.127  37.483 1.00 61.68  ? 219 PHE   B CA  1 
ATOM   4808 C C   . PHE   B 1 219 ? -14.347 39.717  36.674 1.00 68.08  ? 219 PHE   B C   1 
ATOM   4809 O O   . PHE   B 1 219 ? -15.278 40.315  37.230 1.00 64.93  ? 219 PHE   B O   1 
ATOM   4810 C CB  . PHE   B 1 219 ? -11.906 39.910  37.258 1.00 65.45  ? 219 PHE   B CB  1 
ATOM   4811 C CG  . PHE   B 1 219 ? -11.080 40.095  38.503 1.00 71.27  ? 219 PHE   B CG  1 
ATOM   4812 C CD1 . PHE   B 1 219 ? -10.508 39.006  39.143 1.00 83.53  ? 219 PHE   B CD1 1 
ATOM   4813 C CD2 . PHE   B 1 219 ? -10.860 41.360  39.023 1.00 72.39  ? 219 PHE   B CD2 1 
ATOM   4814 C CE1 . PHE   B 1 219 ? -9.743  39.174  40.287 1.00 66.02  ? 219 PHE   B CE1 1 
ATOM   4815 C CE2 . PHE   B 1 219 ? -10.095 41.536  40.167 1.00 67.62  ? 219 PHE   B CE2 1 
ATOM   4816 C CZ  . PHE   B 1 219 ? -9.536  40.441  40.798 1.00 58.06  ? 219 PHE   B CZ  1 
ATOM   4817 N N   . ASP   B 1 220 ? -14.324 39.491  35.357 1.00 71.06  ? 220 ASP   B N   1 
ATOM   4818 C CA  . ASP   B 1 220 ? -15.399 39.983  34.506 1.00 69.25  ? 220 ASP   B CA  1 
ATOM   4819 C C   . ASP   B 1 220 ? -16.733 39.387  34.928 1.00 79.78  ? 220 ASP   B C   1 
ATOM   4820 O O   . ASP   B 1 220 ? -17.745 40.099  34.990 1.00 85.12  ? 220 ASP   B O   1 
ATOM   4821 C CB  . ASP   B 1 220 ? -15.092 39.671  33.042 1.00 78.55  ? 220 ASP   B CB  1 
ATOM   4822 C CG  . ASP   B 1 220 ? -13.835 40.368  32.551 1.00 92.00  ? 220 ASP   B CG  1 
ATOM   4823 O OD1 . ASP   B 1 220 ? -13.388 41.329  33.214 1.00 87.66  ? 220 ASP   B OD1 1 
ATOM   4824 O OD2 . ASP   B 1 220 ? -13.292 39.954  31.505 1.00 100.57 ? 220 ASP   B OD2 1 
ATOM   4825 N N   . MET   B 1 221 ? -16.750 38.088  35.251 1.00 83.23  ? 221 MET   B N   1 
ATOM   4826 C CA  . MET   B 1 221 ? -17.973 37.474  35.756 1.00 65.00  ? 221 MET   B CA  1 
ATOM   4827 C C   . MET   B 1 221 ? -18.510 38.256  36.944 1.00 71.09  ? 221 MET   B C   1 
ATOM   4828 O O   . MET   B 1 221 ? -19.701 38.583  37.001 1.00 86.25  ? 221 MET   B O   1 
ATOM   4829 C CB  . MET   B 1 221 ? -17.726 36.012  36.139 1.00 66.09  ? 221 MET   B CB  1 
ATOM   4830 C CG  . MET   B 1 221 ? -17.521 35.065  34.967 1.00 63.76  ? 221 MET   B CG  1 
ATOM   4831 S SD  . MET   B 1 221 ? -17.195 33.359  35.442 1.00 81.34  ? 221 MET   B SD  1 
ATOM   4832 C CE  . MET   B 1 221 ? -16.934 32.597  33.841 1.00 75.62  ? 221 MET   B CE  1 
ATOM   4833 N N   . GLY   B 1 222 ? -17.625 38.612  37.880 1.00 69.39  ? 222 GLY   B N   1 
ATOM   4834 C CA  . GLY   B 1 222 ? -18.061 39.392  39.024 1.00 74.89  ? 222 GLY   B CA  1 
ATOM   4835 C C   . GLY   B 1 222 ? -18.695 40.701  38.606 1.00 76.57  ? 222 GLY   B C   1 
ATOM   4836 O O   . GLY   B 1 222 ? -19.758 41.078  39.109 1.00 77.02  ? 222 GLY   B O   1 
ATOM   4837 N N   . ALA   B 1 223 ? -18.080 41.385  37.638 1.00 80.25  ? 223 ALA   B N   1 
ATOM   4838 C CA  . ALA   B 1 223 ? -18.642 42.640  37.159 1.00 77.01  ? 223 ALA   B CA  1 
ATOM   4839 C C   . ALA   B 1 223 ? -20.055 42.447  36.628 1.00 82.58  ? 223 ALA   B C   1 
ATOM   4840 O O   . ALA   B 1 223 ? -20.900 43.336  36.783 1.00 91.20  ? 223 ALA   B O   1 
ATOM   4841 C CB  . ALA   B 1 223 ? -17.739 43.245  36.084 1.00 79.20  ? 223 ALA   B CB  1 
ATOM   4842 N N   . GLU   B 1 224 ? -20.336 41.296  36.011 1.00 79.98  ? 224 GLU   B N   1 
ATOM   4843 C CA  . GLU   B 1 224 ? -21.684 41.062  35.505 1.00 74.87  ? 224 GLU   B CA  1 
ATOM   4844 C C   . GLU   B 1 224 ? -22.684 40.881  36.640 1.00 79.21  ? 224 GLU   B C   1 
ATOM   4845 O O   . GLU   B 1 224 ? -23.840 41.302  36.524 1.00 96.95  ? 224 GLU   B O   1 
ATOM   4846 C CB  . GLU   B 1 224 ? -21.703 39.853  34.569 1.00 79.84  ? 224 GLU   B CB  1 
ATOM   4847 C CG  . GLU   B 1 224 ? -21.093 40.128  33.202 1.00 95.59  ? 224 GLU   B CG  1 
ATOM   4848 C CD  . GLU   B 1 224 ? -21.293 38.984  32.225 1.00 106.70 ? 224 GLU   B CD  1 
ATOM   4849 O OE1 . GLU   B 1 224 ? -22.075 38.061  32.537 1.00 102.21 ? 224 GLU   B OE1 1 
ATOM   4850 O OE2 . GLU   B 1 224 ? -20.670 39.011  31.143 1.00 99.93  ? 224 GLU   B OE2 1 
ATOM   4851 N N   . VAL   B 1 225 ? -22.264 40.258  37.748 1.00 73.27  ? 225 VAL   B N   1 
ATOM   4852 C CA  . VAL   B 1 225 ? -23.198 39.970  38.832 1.00 79.16  ? 225 VAL   B CA  1 
ATOM   4853 C C   . VAL   B 1 225 ? -23.249 41.078  39.874 1.00 83.08  ? 225 VAL   B C   1 
ATOM   4854 O O   . VAL   B 1 225 ? -24.068 41.006  40.801 1.00 85.84  ? 225 VAL   B O   1 
ATOM   4855 C CB  . VAL   B 1 225 ? -22.881 38.615  39.500 1.00 74.29  ? 225 VAL   B CB  1 
ATOM   4856 C CG1 . VAL   B 1 225 ? -23.054 37.482  38.501 1.00 70.61  ? 225 VAL   B CG1 1 
ATOM   4857 C CG2 . VAL   B 1 225 ? -21.479 38.612  40.056 1.00 95.46  ? 225 VAL   B CG2 1 
ATOM   4858 N N   . GLY   B 1 226 ? -22.409 42.101  39.753 1.00 79.97  ? 226 GLY   B N   1 
ATOM   4859 C CA  . GLY   B 1 226 ? -22.444 43.234  40.653 1.00 89.03  ? 226 GLY   B CA  1 
ATOM   4860 C C   . GLY   B 1 226 ? -21.353 43.306  41.698 1.00 85.90  ? 226 GLY   B C   1 
ATOM   4861 O O   . GLY   B 1 226 ? -21.401 44.201  42.549 1.00 85.62  ? 226 GLY   B O   1 
ATOM   4862 N N   . PHE   B 1 227 ? -20.377 42.403  41.670 1.00 85.87  ? 227 PHE   B N   1 
ATOM   4863 C CA  . PHE   B 1 227 ? -19.281 42.464  42.624 1.00 78.71  ? 227 PHE   B CA  1 
ATOM   4864 C C   . PHE   B 1 227 ? -18.204 43.437  42.158 1.00 85.61  ? 227 PHE   B C   1 
ATOM   4865 O O   . PHE   B 1 227 ? -17.969 43.612  40.958 1.00 88.02  ? 227 PHE   B O   1 
ATOM   4866 C CB  . PHE   B 1 227 ? -18.662 41.083  42.839 1.00 72.00  ? 227 PHE   B CB  1 
ATOM   4867 C CG  . PHE   B 1 227 ? -19.516 40.154  43.647 1.00 59.75  ? 227 PHE   B CG  1 
ATOM   4868 C CD1 . PHE   B 1 227 ? -19.837 40.456  44.958 1.00 62.12  ? 227 PHE   B CD1 1 
ATOM   4869 C CD2 . PHE   B 1 227 ? -19.976 38.967  43.107 1.00 62.89  ? 227 PHE   B CD2 1 
ATOM   4870 C CE1 . PHE   B 1 227 ? -20.618 39.603  45.708 1.00 67.09  ? 227 PHE   B CE1 1 
ATOM   4871 C CE2 . PHE   B 1 227 ? -20.756 38.108  43.851 1.00 67.23  ? 227 PHE   B CE2 1 
ATOM   4872 C CZ  . PHE   B 1 227 ? -21.077 38.426  45.154 1.00 77.40  ? 227 PHE   B CZ  1 
ATOM   4873 N N   . SER   B 1 228 ? -17.543 44.067  43.127 1.00 87.51  ? 228 SER   B N   1 
ATOM   4874 C CA  . SER   B 1 228 ? -16.391 44.931  42.870 1.00 90.06  ? 228 SER   B CA  1 
ATOM   4875 C C   . SER   B 1 228 ? -15.144 44.120  43.205 1.00 74.71  ? 228 SER   B C   1 
ATOM   4876 O O   . SER   B 1 228 ? -14.672 44.106  44.342 1.00 79.27  ? 228 SER   B O   1 
ATOM   4877 C CB  . SER   B 1 228 ? -16.471 46.217  43.685 1.00 86.68  ? 228 SER   B CB  1 
ATOM   4878 O OG  . SER   B 1 228 ? -17.526 47.046  43.229 1.00 88.98  ? 228 SER   B OG  1 
ATOM   4879 N N   . MET   B 1 229 ? -14.606 43.444  42.196 1.00 74.19  ? 229 MET   B N   1 
ATOM   4880 C CA  . MET   B 1 229 ? -13.460 42.569  42.390 1.00 65.85  ? 229 MET   B CA  1 
ATOM   4881 C C   . MET   B 1 229 ? -12.181 43.392  42.349 1.00 58.43  ? 229 MET   B C   1 
ATOM   4882 O O   . MET   B 1 229 ? -11.957 44.157  41.406 1.00 66.67  ? 229 MET   B O   1 
ATOM   4883 C CB  . MET   B 1 229 ? -13.432 41.493  41.307 1.00 71.96  ? 229 MET   B CB  1 
ATOM   4884 C CG  . MET   B 1 229 ? -14.774 40.825  41.068 1.00 75.12  ? 229 MET   B CG  1 
ATOM   4885 S SD  . MET   B 1 229 ? -15.046 39.384  42.109 1.00 71.79  ? 229 MET   B SD  1 
ATOM   4886 C CE  . MET   B 1 229 ? -14.014 38.184  41.278 1.00 60.39  ? 229 MET   B CE  1 
ATOM   4887 N N   . TYR   B 1 230 ? -11.342 43.239  43.371 1.00 54.58  ? 230 TYR   B N   1 
ATOM   4888 C CA  . TYR   B 1 230 ? -10.088 43.980  43.406 1.00 63.31  ? 230 TYR   B CA  1 
ATOM   4889 C C   . TYR   B 1 230 ? -8.873  43.161  43.813 1.00 64.92  ? 230 TYR   B C   1 
ATOM   4890 O O   . TYR   B 1 230 ? -7.755  43.655  43.644 1.00 63.73  ? 230 TYR   B O   1 
ATOM   4891 C CB  . TYR   B 1 230 ? -10.204 45.196  44.342 1.00 46.63  ? 230 TYR   B CB  1 
ATOM   4892 C CG  . TYR   B 1 230 ? -10.356 44.851  45.807 1.00 65.07  ? 230 TYR   B CG  1 
ATOM   4893 C CD1 . TYR   B 1 230 ? -9.245  44.728  46.633 1.00 56.65  ? 230 TYR   B CD1 1 
ATOM   4894 C CD2 . TYR   B 1 230 ? -11.612 44.663  46.369 1.00 73.20  ? 230 TYR   B CD2 1 
ATOM   4895 C CE1 . TYR   B 1 230 ? -9.380  44.416  47.974 1.00 66.53  ? 230 TYR   B CE1 1 
ATOM   4896 C CE2 . TYR   B 1 230 ? -11.757 44.356  47.711 1.00 66.50  ? 230 TYR   B CE2 1 
ATOM   4897 C CZ  . TYR   B 1 230 ? -10.639 44.230  48.508 1.00 70.68  ? 230 TYR   B CZ  1 
ATOM   4898 O OH  . TYR   B 1 230 ? -10.782 43.920  49.843 1.00 76.78  ? 230 TYR   B OH  1 
ATOM   4899 N N   . LEU   B 1 231 ? -9.030  41.956  44.352 1.00 59.04  ? 231 LEU   B N   1 
ATOM   4900 C CA  . LEU   B 1 231 ? -7.909  41.194  44.886 1.00 57.24  ? 231 LEU   B CA  1 
ATOM   4901 C C   . LEU   B 1 231 ? -7.563  40.035  43.957 1.00 52.62  ? 231 LEU   B C   1 
ATOM   4902 O O   . LEU   B 1 231 ? -8.419  39.194  43.661 1.00 56.10  ? 231 LEU   B O   1 
ATOM   4903 C CB  . LEU   B 1 231 ? -8.223  40.666  46.282 1.00 57.37  ? 231 LEU   B CB  1 
ATOM   4904 C CG  . LEU   B 1 231 ? -7.065  39.823  46.813 1.00 67.20  ? 231 LEU   B CG  1 
ATOM   4905 C CD1 . LEU   B 1 231 ? -5.806  40.666  46.992 1.00 69.58  ? 231 LEU   B CD1 1 
ATOM   4906 C CD2 . LEU   B 1 231 ? -7.442  39.124  48.083 1.00 72.82  ? 231 LEU   B CD2 1 
ATOM   4907 N N   . LEU   B 1 232 ? -6.313  39.997  43.499 1.00 49.25  ? 232 LEU   B N   1 
ATOM   4908 C CA  . LEU   B 1 232 ? -5.788  38.895  42.700 1.00 44.65  ? 232 LEU   B CA  1 
ATOM   4909 C C   . LEU   B 1 232 ? -4.683  38.201  43.482 1.00 56.71  ? 232 LEU   B C   1 
ATOM   4910 O O   . LEU   B 1 232 ? -3.681  38.833  43.830 1.00 55.85  ? 232 LEU   B O   1 
ATOM   4911 C CB  . LEU   B 1 232 ? -5.252  39.396  41.361 1.00 41.55  ? 232 LEU   B CB  1 
ATOM   4912 C CG  . LEU   B 1 232 ? -4.537  38.322  40.547 1.00 41.49  ? 232 LEU   B CG  1 
ATOM   4913 C CD1 . LEU   B 1 232 ? -5.506  37.219  40.153 1.00 39.09  ? 232 LEU   B CD1 1 
ATOM   4914 C CD2 . LEU   B 1 232 ? -3.867  38.929  39.329 1.00 44.23  ? 232 LEU   B CD2 1 
ATOM   4915 N N   . ASP   B 1 233 ? -4.851  36.902  43.731 1.00 57.76  ? 233 ASP   B N   1 
ATOM   4916 C CA  . ASP   B 1 233 ? -3.916  36.110  44.524 1.00 60.03  ? 233 ASP   B CA  1 
ATOM   4917 C C   . ASP   B 1 233 ? -3.336  35.023  43.623 1.00 59.11  ? 233 ASP   B C   1 
ATOM   4918 O O   . ASP   B 1 233 ? -4.054  34.105  43.204 1.00 54.93  ? 233 ASP   B O   1 
ATOM   4919 C CB  . ASP   B 1 233 ? -4.626  35.523  45.746 1.00 67.48  ? 233 ASP   B CB  1 
ATOM   4920 C CG  . ASP   B 1 233 ? -3.684  34.827  46.710 1.00 74.86  ? 233 ASP   B CG  1 
ATOM   4921 O OD1 . ASP   B 1 233 ? -2.572  34.436  46.308 1.00 64.92  ? 233 ASP   B OD1 1 
ATOM   4922 O OD2 . ASP   B 1 233 ? -4.071  34.679  47.889 1.00 81.42  ? 233 ASP   B OD2 1 
ATOM   4923 N N   . ILE   B 1 234 ? -2.040  35.128  43.334 1.00 52.19  ? 234 ILE   B N   1 
ATOM   4924 C CA  . ILE   B 1 234 ? -1.386  34.241  42.375 1.00 48.47  ? 234 ILE   B CA  1 
ATOM   4925 C C   . ILE   B 1 234 ? -0.717  33.068  43.083 1.00 54.43  ? 234 ILE   B C   1 
ATOM   4926 O O   . ILE   B 1 234 ? 0.019   32.299  42.457 1.00 55.52  ? 234 ILE   B O   1 
ATOM   4927 C CB  . ILE   B 1 234 ? -0.372  35.021  41.520 1.00 47.92  ? 234 ILE   B CB  1 
ATOM   4928 C CG1 . ILE   B 1 234 ? 0.806   35.485  42.374 1.00 53.93  ? 234 ILE   B CG1 1 
ATOM   4929 C CG2 . ILE   B 1 234 ? -1.049  36.219  40.872 1.00 43.20  ? 234 ILE   B CG2 1 
ATOM   4930 C CD1 . ILE   B 1 234 ? 1.932   36.105  41.572 1.00 36.18  ? 234 ILE   B CD1 1 
ATOM   4931 N N   . GLY   B 1 235 ? -0.983  32.911  44.384 1.00 59.65  ? 235 GLY   B N   1 
ATOM   4932 C CA  . GLY   B 1 235 ? -0.541  31.719  45.085 1.00 50.88  ? 235 GLY   B CA  1 
ATOM   4933 C C   . GLY   B 1 235 ? 0.966   31.634  45.255 1.00 50.32  ? 235 GLY   B C   1 
ATOM   4934 O O   . GLY   B 1 235 ? 1.678   32.638  45.338 1.00 47.71  ? 235 GLY   B O   1 
ATOM   4935 N N   . GLY   B 1 236 ? 1.454   30.398  45.311 1.00 53.18  ? 236 GLY   B N   1 
ATOM   4936 C CA  . GLY   B 1 236 ? 2.854   30.115  45.527 1.00 53.62  ? 236 GLY   B CA  1 
ATOM   4937 C C   . GLY   B 1 236 ? 3.407   29.201  44.449 1.00 61.09  ? 236 GLY   B C   1 
ATOM   4938 O O   . GLY   B 1 236 ? 2.992   29.242  43.289 1.00 56.56  ? 236 GLY   B O   1 
ATOM   4939 N N   . GLY   B 1 237 ? 4.364   28.369  44.855 1.00 49.80  ? 237 GLY   B N   1 
ATOM   4940 C CA  . GLY   B 1 237 ? 5.028   27.453  43.952 1.00 54.19  ? 237 GLY   B CA  1 
ATOM   4941 C C   . GLY   B 1 237 ? 6.379   27.910  43.448 1.00 59.79  ? 237 GLY   B C   1 
ATOM   4942 O O   . GLY   B 1 237 ? 7.035   27.159  42.714 1.00 78.88  ? 237 GLY   B O   1 
ATOM   4943 N N   . PHE   B 1 238 ? 6.818   29.106  43.820 1.00 62.01  ? 238 PHE   B N   1 
ATOM   4944 C CA  . PHE   B 1 238 ? 8.109   29.595  43.368 1.00 55.93  ? 238 PHE   B CA  1 
ATOM   4945 C C   . PHE   B 1 238 ? 9.226   28.792  44.030 1.00 58.13  ? 238 PHE   B C   1 
ATOM   4946 O O   . PHE   B 1 238 ? 9.093   28.382  45.186 1.00 73.75  ? 238 PHE   B O   1 
ATOM   4947 C CB  . PHE   B 1 238 ? 8.261   31.079  43.698 1.00 55.65  ? 238 PHE   B CB  1 
ATOM   4948 C CG  . PHE   B 1 238 ? 7.095   31.919  43.263 1.00 63.89  ? 238 PHE   B CG  1 
ATOM   4949 C CD1 . PHE   B 1 238 ? 7.036   32.432  41.977 1.00 69.39  ? 238 PHE   B CD1 1 
ATOM   4950 C CD2 . PHE   B 1 238 ? 6.058   32.198  44.139 1.00 68.55  ? 238 PHE   B CD2 1 
ATOM   4951 C CE1 . PHE   B 1 238 ? 5.964   33.207  41.572 1.00 66.73  ? 238 PHE   B CE1 1 
ATOM   4952 C CE2 . PHE   B 1 238 ? 4.982   32.973  43.739 1.00 73.89  ? 238 PHE   B CE2 1 
ATOM   4953 C CZ  . PHE   B 1 238 ? 4.936   33.478  42.453 1.00 53.84  ? 238 PHE   B CZ  1 
ATOM   4954 N N   . PRO   B 1 239 ? 10.326  28.543  43.326 1.00 52.34  ? 239 PRO   B N   1 
ATOM   4955 C CA  . PRO   B 1 239 ? 11.409  27.752  43.918 1.00 53.14  ? 239 PRO   B CA  1 
ATOM   4956 C C   . PRO   B 1 239 ? 12.092  28.503  45.050 1.00 55.33  ? 239 PRO   B C   1 
ATOM   4957 O O   . PRO   B 1 239 ? 12.161  29.735  45.061 1.00 61.21  ? 239 PRO   B O   1 
ATOM   4958 C CB  . PRO   B 1 239 ? 12.365  27.527  42.742 1.00 54.99  ? 239 PRO   B CB  1 
ATOM   4959 C CG  . PRO   B 1 239 ? 12.125  28.699  41.852 1.00 58.57  ? 239 PRO   B CG  1 
ATOM   4960 C CD  . PRO   B 1 239 ? 10.654  28.995  41.963 1.00 54.98  ? 239 PRO   B CD  1 
ATOM   4961 N N   . GLY   B 1 240 ? 12.590  27.740  46.017 1.00 59.86  ? 240 GLY   B N   1 
ATOM   4962 C CA  . GLY   B 1 240 ? 13.270  28.294  47.164 1.00 61.22  ? 240 GLY   B CA  1 
ATOM   4963 C C   . GLY   B 1 240 ? 14.774  28.178  47.151 1.00 58.96  ? 240 GLY   B C   1 
ATOM   4964 O O   . GLY   B 1 240 ? 15.423  28.617  48.105 1.00 67.21  ? 240 GLY   B O   1 
ATOM   4965 N N   . SER   B 1 241 ? 15.352  27.599  46.102 1.00 62.41  ? 241 SER   B N   1 
ATOM   4966 C CA  . SER   B 1 241 ? 16.797  27.484  45.985 1.00 71.98  ? 241 SER   B CA  1 
ATOM   4967 C C   . SER   B 1 241 ? 17.170  27.562  44.513 1.00 74.80  ? 241 SER   B C   1 
ATOM   4968 O O   . SER   B 1 241 ? 16.320  27.448  43.626 1.00 68.87  ? 241 SER   B O   1 
ATOM   4969 C CB  . SER   B 1 241 ? 17.312  26.183  46.611 1.00 75.78  ? 241 SER   B CB  1 
ATOM   4970 O OG  . SER   B 1 241 ? 17.067  25.071  45.767 1.00 71.35  ? 241 SER   B OG  1 
ATOM   4971 N N   . GLU   B 1 242 ? 18.460  27.761  44.260 1.00 83.57  ? 242 GLU   B N   1 
ATOM   4972 C CA  . GLU   B 1 242 ? 18.971  27.799  42.897 1.00 77.30  ? 242 GLU   B CA  1 
ATOM   4973 C C   . GLU   B 1 242 ? 19.189  26.410  42.313 1.00 78.83  ? 242 GLU   B C   1 
ATOM   4974 O O   . GLU   B 1 242 ? 19.542  26.300  41.134 1.00 81.26  ? 242 GLU   B O   1 
ATOM   4975 C CB  . GLU   B 1 242 ? 20.279  28.592  42.850 1.00 81.10  ? 242 GLU   B CB  1 
ATOM   4976 C CG  . GLU   B 1 242 ? 20.112  30.070  43.153 1.00 87.06  ? 242 GLU   B CG  1 
ATOM   4977 C CD  . GLU   B 1 242 ? 18.979  30.698  42.368 1.00 89.05  ? 242 GLU   B CD  1 
ATOM   4978 O OE1 . GLU   B 1 242 ? 19.100  30.800  41.129 1.00 103.42 ? 242 GLU   B OE1 1 
ATOM   4979 O OE2 . GLU   B 1 242 ? 17.968  31.089  42.988 1.00 97.65  ? 242 GLU   B OE2 1 
ATOM   4980 N N   . ASP   B 1 243 ? 18.987  25.357  43.103 1.00 94.64  ? 243 ASP   B N   1 
ATOM   4981 C CA  . ASP   B 1 243 ? 19.204  23.988  42.653 1.00 97.19  ? 243 ASP   B CA  1 
ATOM   4982 C C   . ASP   B 1 243 ? 17.967  23.459  41.934 1.00 83.67  ? 243 ASP   B C   1 
ATOM   4983 O O   . ASP   B 1 243 ? 17.452  22.389  42.272 1.00 91.32  ? 243 ASP   B O   1 
ATOM   4984 C CB  . ASP   B 1 243 ? 19.570  23.101  43.848 1.00 106.79 ? 243 ASP   B CB  1 
ATOM   4985 C CG  . ASP   B 1 243 ? 20.103  21.744  43.435 1.00 127.36 ? 243 ASP   B CG  1 
ATOM   4986 O OD1 . ASP   B 1 243 ? 20.553  21.606  42.278 1.00 132.37 ? 243 ASP   B OD1 1 
ATOM   4987 O OD2 . ASP   B 1 243 ? 20.076  20.817  44.272 1.00 131.61 ? 243 ASP   B OD2 1 
ATOM   4988 N N   . VAL   B 1 244 ? 17.484  24.205  40.936 1.00 84.76  ? 244 VAL   B N   1 
ATOM   4989 C CA  . VAL   B 1 244 ? 16.297  23.844  40.170 1.00 86.47  ? 244 VAL   B CA  1 
ATOM   4990 C C   . VAL   B 1 244 ? 16.499  24.256  38.717 1.00 79.88  ? 244 VAL   B C   1 
ATOM   4991 O O   . VAL   B 1 244 ? 17.293  25.146  38.402 1.00 85.04  ? 244 VAL   B O   1 
ATOM   4992 C CB  . VAL   B 1 244 ? 15.006  24.494  40.727 1.00 92.83  ? 244 VAL   B CB  1 
ATOM   4993 C CG1 . VAL   B 1 244 ? 14.662  23.938  42.105 1.00 80.55  ? 244 VAL   B CG1 1 
ATOM   4994 C CG2 . VAL   B 1 244 ? 15.153  26.009  40.776 1.00 82.94  ? 244 VAL   B CG2 1 
ATOM   4995 N N   . LYS   B 1 245 ? 15.763  23.589  37.825 1.00 68.44  ? 245 LYS   B N   1 
ATOM   4996 C CA  . LYS   B 1 245 ? 15.856  23.915  36.404 1.00 76.26  ? 245 LYS   B CA  1 
ATOM   4997 C C   . LYS   B 1 245 ? 15.148  25.226  36.079 1.00 89.17  ? 245 LYS   B C   1 
ATOM   4998 O O   . LYS   B 1 245 ? 15.680  26.054  35.330 1.00 95.84  ? 245 LYS   B O   1 
ATOM   4999 C CB  . LYS   B 1 245 ? 15.271  22.779  35.565 1.00 78.78  ? 245 LYS   B CB  1 
ATOM   5000 C CG  . LYS   B 1 245 ? 15.327  23.036  34.069 1.00 88.15  ? 245 LYS   B CG  1 
ATOM   5001 C CD  . LYS   B 1 245 ? 14.520  22.006  33.295 1.00 92.74  ? 245 LYS   B CD  1 
ATOM   5002 C CE  . LYS   B 1 245 ? 14.620  22.241  31.795 1.00 84.49  ? 245 LYS   B CE  1 
ATOM   5003 N NZ  . LYS   B 1 245 ? 13.958  21.162  31.011 1.00 84.78  ? 245 LYS   B NZ  1 
ATOM   5004 N N   . LEU   B 1 246 ? 13.956  25.438  36.634 1.00 75.19  ? 246 LEU   B N   1 
ATOM   5005 C CA  . LEU   B 1 246 ? 13.160  26.631  36.364 1.00 63.87  ? 246 LEU   B CA  1 
ATOM   5006 C C   . LEU   B 1 246 ? 13.347  27.605  37.521 1.00 71.95  ? 246 LEU   B C   1 
ATOM   5007 O O   . LEU   B 1 246 ? 12.799  27.399  38.609 1.00 76.06  ? 246 LEU   B O   1 
ATOM   5008 C CB  . LEU   B 1 246 ? 11.688  26.276  36.170 1.00 72.22  ? 246 LEU   B CB  1 
ATOM   5009 C CG  . LEU   B 1 246 ? 10.769  27.451  35.838 1.00 76.95  ? 246 LEU   B CG  1 
ATOM   5010 C CD1 . LEU   B 1 246 ? 11.168  28.082  34.515 1.00 69.76  ? 246 LEU   B CD1 1 
ATOM   5011 C CD2 . LEU   B 1 246 ? 9.323   27.000  35.795 1.00 75.27  ? 246 LEU   B CD2 1 
ATOM   5012 N N   . LYS   B 1 247 ? 14.118  28.660  37.286 1.00 76.16  ? 247 LYS   B N   1 
ATOM   5013 C CA  . LYS   B 1 247 ? 14.506  29.584  38.341 1.00 77.25  ? 247 LYS   B CA  1 
ATOM   5014 C C   . LYS   B 1 247 ? 13.471  30.691  38.534 1.00 69.03  ? 247 LYS   B C   1 
ATOM   5015 O O   . LYS   B 1 247 ? 12.641  30.969  37.665 1.00 73.59  ? 247 LYS   B O   1 
ATOM   5016 C CB  . LYS   B 1 247 ? 15.880  30.188  38.046 1.00 79.28  ? 247 LYS   B CB  1 
ATOM   5017 C CG  . LYS   B 1 247 ? 17.031  29.278  38.440 1.00 84.26  ? 247 LYS   B CG  1 
ATOM   5018 C CD  . LYS   B 1 247 ? 18.288  29.574  37.645 1.00 95.19  ? 247 LYS   B CD  1 
ATOM   5019 C CE  . LYS   B 1 247 ? 19.372  28.554  37.953 1.00 97.34  ? 247 LYS   B CE  1 
ATOM   5020 N NZ  . LYS   B 1 247 ? 18.952  27.175  37.578 1.00 78.86  ? 247 LYS   B NZ  1 
ATOM   5021 N N   . PHE   B 1 248 ? 13.536  31.309  39.716 1.00 63.48  ? 248 PHE   B N   1 
ATOM   5022 C CA  . PHE   B 1 248 ? 12.566  32.321  40.130 1.00 63.06  ? 248 PHE   B CA  1 
ATOM   5023 C C   . PHE   B 1 248 ? 12.427  33.437  39.097 1.00 65.18  ? 248 PHE   B C   1 
ATOM   5024 O O   . PHE   B 1 248 ? 11.310  33.842  38.747 1.00 59.99  ? 248 PHE   B O   1 
ATOM   5025 C CB  . PHE   B 1 248 ? 12.987  32.878  41.494 1.00 59.41  ? 248 PHE   B CB  1 
ATOM   5026 C CG  . PHE   B 1 248 ? 12.060  33.919  42.051 1.00 62.40  ? 248 PHE   B CG  1 
ATOM   5027 C CD1 . PHE   B 1 248 ? 10.735  33.618  42.322 1.00 57.82  ? 248 PHE   B CD1 1 
ATOM   5028 C CD2 . PHE   B 1 248 ? 12.525  35.193  42.337 1.00 54.81  ? 248 PHE   B CD2 1 
ATOM   5029 C CE1 . PHE   B 1 248 ? 9.885   34.576  42.846 1.00 64.73  ? 248 PHE   B CE1 1 
ATOM   5030 C CE2 . PHE   B 1 248 ? 11.682  36.153  42.862 1.00 48.79  ? 248 PHE   B CE2 1 
ATOM   5031 C CZ  . PHE   B 1 248 ? 10.360  35.846  43.118 1.00 53.10  ? 248 PHE   B CZ  1 
ATOM   5032 N N   . GLU   B 1 249 ? 13.555  33.945  38.596 1.00 76.15  ? 249 GLU   B N   1 
ATOM   5033 C CA  . GLU   B 1 249 ? 13.514  35.124  37.737 1.00 71.78  ? 249 GLU   B CA  1 
ATOM   5034 C C   . GLU   B 1 249 ? 12.860  34.838  36.390 1.00 68.06  ? 249 GLU   B C   1 
ATOM   5035 O O   . GLU   B 1 249 ? 12.204  35.721  35.831 1.00 68.12  ? 249 GLU   B O   1 
ATOM   5036 C CB  . GLU   B 1 249 ? 14.924  35.682  37.547 1.00 63.68  ? 249 GLU   B CB  1 
ATOM   5037 C CG  . GLU   B 1 249 ? 15.352  36.647  38.648 1.00 77.10  ? 249 GLU   B CG  1 
ATOM   5038 C CD  . GLU   B 1 249 ? 15.643  35.955  39.970 1.00 81.35  ? 249 GLU   B CD  1 
ATOM   5039 O OE1 . GLU   B 1 249 ? 15.721  34.708  39.992 1.00 87.35  ? 249 GLU   B OE1 1 
ATOM   5040 O OE2 . GLU   B 1 249 ? 15.798  36.660  40.990 1.00 78.73  ? 249 GLU   B OE2 1 
ATOM   5041 N N   . GLU   B 1 250 ? 13.007  33.622  35.858 1.00 64.69  ? 250 GLU   B N   1 
ATOM   5042 C CA  . GLU   B 1 250 ? 12.287  33.263  34.638 1.00 66.23  ? 250 GLU   B CA  1 
ATOM   5043 C C   . GLU   B 1 250 ? 10.781  33.306  34.865 1.00 66.24  ? 250 GLU   B C   1 
ATOM   5044 O O   . GLU   B 1 250 ? 10.025  33.861  34.054 1.00 65.92  ? 250 GLU   B O   1 
ATOM   5045 C CB  . GLU   B 1 250 ? 12.713  31.874  34.167 1.00 51.69  ? 250 GLU   B CB  1 
ATOM   5046 C CG  . GLU   B 1 250 ? 14.211  31.657  34.131 1.00 58.62  ? 250 GLU   B CG  1 
ATOM   5047 C CD  . GLU   B 1 250 ? 14.572  30.228  33.786 1.00 84.85  ? 250 GLU   B CD  1 
ATOM   5048 O OE1 . GLU   B 1 250 ? 14.001  29.689  32.814 1.00 101.28 ? 250 GLU   B OE1 1 
ATOM   5049 O OE2 . GLU   B 1 250 ? 15.422  29.641  34.488 1.00 89.08  ? 250 GLU   B OE2 1 
ATOM   5050 N N   . ILE   B 1 251 ? 10.329  32.713  35.971 1.00 68.20  ? 251 ILE   B N   1 
ATOM   5051 C CA  . ILE   B 1 251 ? 8.908   32.718  36.299 1.00 60.92  ? 251 ILE   B CA  1 
ATOM   5052 C C   . ILE   B 1 251 ? 8.399   34.146  36.433 1.00 56.89  ? 251 ILE   B C   1 
ATOM   5053 O O   . ILE   B 1 251 ? 7.329   34.485  35.919 1.00 61.52  ? 251 ILE   B O   1 
ATOM   5054 C CB  . ILE   B 1 251 ? 8.655   31.898  37.577 1.00 58.52  ? 251 ILE   B CB  1 
ATOM   5055 C CG1 . ILE   B 1 251 ? 9.115   30.453  37.376 1.00 56.61  ? 251 ILE   B CG1 1 
ATOM   5056 C CG2 . ILE   B 1 251 ? 7.185   31.929  37.946 1.00 54.21  ? 251 ILE   B CG2 1 
ATOM   5057 C CD1 . ILE   B 1 251 ? 9.053   29.618  38.632 1.00 53.82  ? 251 ILE   B CD1 1 
ATOM   5058 N N   . THR   B 1 252 ? 9.158   35.009  37.115 1.00 61.61  ? 252 THR   B N   1 
ATOM   5059 C CA  . THR   B 1 252 ? 8.706   36.387  37.296 1.00 62.93  ? 252 THR   B CA  1 
ATOM   5060 C C   . THR   B 1 252 ? 8.707   37.153  35.977 1.00 62.93  ? 252 THR   B C   1 
ATOM   5061 O O   . THR   B 1 252 ? 7.827   37.991  35.738 1.00 61.99  ? 252 THR   B O   1 
ATOM   5062 C CB  . THR   B 1 252 ? 9.577   37.103  38.329 1.00 70.69  ? 252 THR   B CB  1 
ATOM   5063 O OG1 . THR   B 1 252 ? 10.935  37.146  37.869 1.00 68.74  ? 252 THR   B OG1 1 
ATOM   5064 C CG2 . THR   B 1 252 ? 9.516   36.382  39.666 1.00 54.35  ? 252 THR   B CG2 1 
ATOM   5065 N N   . GLY   B 1 253 ? 9.695   36.892  35.115 1.00 63.62  ? 253 GLY   B N   1 
ATOM   5066 C CA  . GLY   B 1 253 ? 9.719   37.514  33.804 1.00 57.05  ? 253 GLY   B CA  1 
ATOM   5067 C C   . GLY   B 1 253 ? 8.571   37.080  32.921 1.00 60.76  ? 253 GLY   B C   1 
ATOM   5068 O O   . GLY   B 1 253 ? 8.182   37.805  32.001 1.00 64.77  ? 253 GLY   B O   1 
ATOM   5069 N N   . VAL   B 1 254 ? 8.038   35.882  33.158 1.00 58.88  ? 254 VAL   B N   1 
ATOM   5070 C CA  . VAL   B 1 254 ? 6.837   35.473  32.435 1.00 46.94  ? 254 VAL   B CA  1 
ATOM   5071 C C   . VAL   B 1 254 ? 5.577   36.040  33.098 1.00 55.60  ? 254 VAL   B C   1 
ATOM   5072 O O   . VAL   B 1 254 ? 4.595   36.349  32.413 1.00 62.82  ? 254 VAL   B O   1 
ATOM   5073 C CB  . VAL   B 1 254 ? 6.784   33.939  32.329 1.00 49.72  ? 254 VAL   B CB  1 
ATOM   5074 C CG1 . VAL   B 1 254 ? 5.450   33.481  31.777 1.00 39.54  ? 254 VAL   B CG1 1 
ATOM   5075 C CG2 . VAL   B 1 254 ? 7.922   33.434  31.454 1.00 50.57  ? 254 VAL   B CG2 1 
ATOM   5076 N N   . ILE   B 1 255 ? 5.595   36.214  34.420 1.00 55.35  ? 255 ILE   B N   1 
ATOM   5077 C CA  . ILE   B 1 255 ? 4.399   36.627  35.151 1.00 49.53  ? 255 ILE   B CA  1 
ATOM   5078 C C   . ILE   B 1 255 ? 4.113   38.110  34.950 1.00 53.03  ? 255 ILE   B C   1 
ATOM   5079 O O   . ILE   B 1 255 ? 2.966   38.504  34.705 1.00 60.94  ? 255 ILE   B O   1 
ATOM   5080 C CB  . ILE   B 1 255 ? 4.546   36.283  36.646 1.00 49.30  ? 255 ILE   B CB  1 
ATOM   5081 C CG1 . ILE   B 1 255 ? 4.330   34.791  36.885 1.00 51.63  ? 255 ILE   B CG1 1 
ATOM   5082 C CG2 . ILE   B 1 255 ? 3.582   37.096  37.489 1.00 46.22  ? 255 ILE   B CG2 1 
ATOM   5083 C CD1 . ILE   B 1 255 ? 4.526   34.395  38.328 1.00 62.39  ? 255 ILE   B CD1 1 
ATOM   5084 N N   . ASN   B 1 256 ? 5.143   38.952  35.054 1.00 48.42  ? 256 ASN   B N   1 
ATOM   5085 C CA  . ASN   B 1 256 ? 4.923   40.399  35.052 1.00 54.21  ? 256 ASN   B CA  1 
ATOM   5086 C C   . ASN   B 1 256 ? 4.239   40.913  33.790 1.00 66.43  ? 256 ASN   B C   1 
ATOM   5087 O O   . ASN   B 1 256 ? 3.316   41.740  33.912 1.00 71.51  ? 256 ASN   B O   1 
ATOM   5088 C CB  . ASN   B 1 256 ? 6.253   41.124  35.292 1.00 68.17  ? 256 ASN   B CB  1 
ATOM   5089 C CG  . ASN   B 1 256 ? 6.703   41.065  36.743 1.00 67.22  ? 256 ASN   B CG  1 
ATOM   5090 O OD1 . ASN   B 1 256 ? 5.886   41.134  37.661 1.00 64.04  ? 256 ASN   B OD1 1 
ATOM   5091 N ND2 . ASN   B 1 256 ? 8.009   40.936  36.954 1.00 62.52  ? 256 ASN   B ND2 1 
ATOM   5092 N N   . PRO   B 1 257 ? 4.626   40.506  32.570 1.00 61.65  ? 257 PRO   B N   1 
ATOM   5093 C CA  . PRO   B 1 257 ? 3.856   40.948  31.395 1.00 55.47  ? 257 PRO   B CA  1 
ATOM   5094 C C   . PRO   B 1 257 ? 2.407   40.500  31.427 1.00 68.77  ? 257 PRO   B C   1 
ATOM   5095 O O   . PRO   B 1 257 ? 1.519   41.267  31.038 1.00 69.10  ? 257 PRO   B O   1 
ATOM   5096 C CB  . PRO   B 1 257 ? 4.616   40.319  30.220 1.00 51.86  ? 257 PRO   B CB  1 
ATOM   5097 C CG  . PRO   B 1 257 ? 5.986   40.111  30.730 1.00 61.44  ? 257 PRO   B CG  1 
ATOM   5098 C CD  . PRO   B 1 257 ? 5.830   39.757  32.171 1.00 55.37  ? 257 PRO   B CD  1 
ATOM   5099 N N   . ALA   B 1 258 ? 2.142   39.275  31.885 1.00 57.23  ? 258 ALA   B N   1 
ATOM   5100 C CA  . ALA   B 1 258 ? 0.763   38.809  31.973 1.00 51.72  ? 258 ALA   B CA  1 
ATOM   5101 C C   . ALA   B 1 258 ? -0.037  39.646  32.963 1.00 57.54  ? 258 ALA   B C   1 
ATOM   5102 O O   . ALA   B 1 258 ? -1.196  39.991  32.703 1.00 65.78  ? 258 ALA   B O   1 
ATOM   5103 C CB  . ALA   B 1 258 ? 0.731   37.331  32.359 1.00 50.01  ? 258 ALA   B CB  1 
ATOM   5104 N N   . LEU   B 1 259 ? 0.565   39.984  34.106 1.00 52.09  ? 259 LEU   B N   1 
ATOM   5105 C CA  . LEU   B 1 259 ? -0.115  40.847  35.067 1.00 56.87  ? 259 LEU   B CA  1 
ATOM   5106 C C   . LEU   B 1 259 ? -0.395  42.220  34.473 1.00 57.08  ? 259 LEU   B C   1 
ATOM   5107 O O   . LEU   B 1 259 ? -1.484  42.773  34.662 1.00 63.45  ? 259 LEU   B O   1 
ATOM   5108 C CB  . LEU   B 1 259 ? 0.711   40.978  36.346 1.00 54.60  ? 259 LEU   B CB  1 
ATOM   5109 C CG  . LEU   B 1 259 ? 0.809   39.735  37.229 1.00 56.70  ? 259 LEU   B CG  1 
ATOM   5110 C CD1 . LEU   B 1 259 ? 1.632   40.035  38.471 1.00 53.95  ? 259 LEU   B CD1 1 
ATOM   5111 C CD2 . LEU   B 1 259 ? -0.577  39.231  37.605 1.00 49.25  ? 259 LEU   B CD2 1 
ATOM   5112 N N   . ASP   B 1 260 ? 0.579   42.793  33.761 1.00 72.13  ? 260 ASP   B N   1 
ATOM   5113 C CA  . ASP   B 1 260 ? 0.361   44.099  33.146 1.00 77.69  ? 260 ASP   B CA  1 
ATOM   5114 C C   . ASP   B 1 260 ? -0.716  44.041  32.069 1.00 71.57  ? 260 ASP   B C   1 
ATOM   5115 O O   . ASP   B 1 260 ? -1.469  45.004  31.889 1.00 68.88  ? 260 ASP   B O   1 
ATOM   5116 C CB  . ASP   B 1 260 ? 1.672   44.630  32.567 1.00 74.69  ? 260 ASP   B CB  1 
ATOM   5117 C CG  . ASP   B 1 260 ? 2.705   44.927  33.640 1.00 99.80  ? 260 ASP   B CG  1 
ATOM   5118 O OD1 . ASP   B 1 260 ? 2.343   44.928  34.837 1.00 99.43  ? 260 ASP   B OD1 1 
ATOM   5119 O OD2 . ASP   B 1 260 ? 3.881   45.158  33.288 1.00 103.99 ? 260 ASP   B OD2 1 
ATOM   5120 N N   . LYS   B 1 261 ? -0.808  42.920  31.352 1.00 60.89  ? 261 LYS   B N   1 
ATOM   5121 C CA  . LYS   B 1 261 ? -1.781  42.796  30.271 1.00 62.93  ? 261 LYS   B CA  1 
ATOM   5122 C C   . LYS   B 1 261 ? -3.193  42.604  30.812 1.00 72.46  ? 261 LYS   B C   1 
ATOM   5123 O O   . LYS   B 1 261 ? -4.133  43.280  30.376 1.00 74.53  ? 261 LYS   B O   1 
ATOM   5124 C CB  . LYS   B 1 261 ? -1.391  41.635  29.357 1.00 68.80  ? 261 LYS   B CB  1 
ATOM   5125 C CG  . LYS   B 1 261 ? -2.447  41.246  28.340 1.00 67.33  ? 261 LYS   B CG  1 
ATOM   5126 C CD  . LYS   B 1 261 ? -1.939  40.131  27.444 1.00 67.55  ? 261 LYS   B CD  1 
ATOM   5127 C CE  . LYS   B 1 261 ? -2.996  39.684  26.453 1.00 71.04  ? 261 LYS   B CE  1 
ATOM   5128 N NZ  . LYS   B 1 261 ? -2.478  38.621  25.550 1.00 78.89  ? 261 LYS   B NZ  1 
ATOM   5129 N N   . TYR   B 1 262 ? -3.365  41.686  31.764 1.00 65.62  ? 262 TYR   B N   1 
ATOM   5130 C CA  . TYR   B 1 262 ? -4.699  41.334  32.235 1.00 60.30  ? 262 TYR   B CA  1 
ATOM   5131 C C   . TYR   B 1 262 ? -5.143  42.145  33.444 1.00 64.59  ? 262 TYR   B C   1 
ATOM   5132 O O   . TYR   B 1 262 ? -6.349  42.318  33.653 1.00 61.34  ? 262 TYR   B O   1 
ATOM   5133 C CB  . TYR   B 1 262 ? -4.760  39.844  32.572 1.00 56.15  ? 262 TYR   B CB  1 
ATOM   5134 C CG  . TYR   B 1 262 ? -4.531  38.948  31.378 1.00 61.63  ? 262 TYR   B CG  1 
ATOM   5135 C CD1 . TYR   B 1 262 ? -5.561  38.654  30.495 1.00 68.72  ? 262 TYR   B CD1 1 
ATOM   5136 C CD2 . TYR   B 1 262 ? -3.281  38.400  31.133 1.00 71.82  ? 262 TYR   B CD2 1 
ATOM   5137 C CE1 . TYR   B 1 262 ? -5.349  37.837  29.402 1.00 78.44  ? 262 TYR   B CE1 1 
ATOM   5138 C CE2 . TYR   B 1 262 ? -3.060  37.584  30.046 1.00 72.83  ? 262 TYR   B CE2 1 
ATOM   5139 C CZ  . TYR   B 1 262 ? -4.095  37.307  29.182 1.00 71.91  ? 262 TYR   B CZ  1 
ATOM   5140 O OH  . TYR   B 1 262 ? -3.868  36.489  28.099 1.00 84.34  ? 262 TYR   B OH  1 
ATOM   5141 N N   . PHE   B 1 263 ? -4.207  42.635  34.251 1.00 63.32  ? 263 PHE   B N   1 
ATOM   5142 C CA  . PHE   B 1 263 ? -4.518  43.409  35.453 1.00 60.38  ? 263 PHE   B CA  1 
ATOM   5143 C C   . PHE   B 1 263 ? -3.642  44.655  35.486 1.00 72.09  ? 263 PHE   B C   1 
ATOM   5144 O O   . PHE   B 1 263 ? -2.707  44.752  36.290 1.00 66.76  ? 263 PHE   B O   1 
ATOM   5145 C CB  . PHE   B 1 263 ? -4.319  42.564  36.710 1.00 62.27  ? 263 PHE   B CB  1 
ATOM   5146 C CG  . PHE   B 1 263 ? -5.281  41.420  36.825 1.00 55.87  ? 263 PHE   B CG  1 
ATOM   5147 C CD1 . PHE   B 1 263 ? -6.469  41.566  37.520 1.00 58.57  ? 263 PHE   B CD1 1 
ATOM   5148 C CD2 . PHE   B 1 263 ? -5.000  40.200  36.233 1.00 54.43  ? 263 PHE   B CD2 1 
ATOM   5149 C CE1 . PHE   B 1 263 ? -7.358  40.515  37.627 1.00 63.56  ? 263 PHE   B CE1 1 
ATOM   5150 C CE2 . PHE   B 1 263 ? -5.885  39.145  36.335 1.00 63.06  ? 263 PHE   B CE2 1 
ATOM   5151 C CZ  . PHE   B 1 263 ? -7.066  39.302  37.033 1.00 64.46  ? 263 PHE   B CZ  1 
ATOM   5152 N N   . PRO   B 1 264 ? -3.913  45.627  34.615 1.00 82.30  ? 264 PRO   B N   1 
ATOM   5153 C CA  . PRO   B 1 264 ? -3.106  46.853  34.614 1.00 70.37  ? 264 PRO   B CA  1 
ATOM   5154 C C   . PRO   B 1 264 ? -3.235  47.600  35.933 1.00 73.13  ? 264 PRO   B C   1 
ATOM   5155 O O   . PRO   B 1 264 ? -4.246  47.505  36.631 1.00 80.47  ? 264 PRO   B O   1 
ATOM   5156 C CB  . PRO   B 1 264 ? -3.687  47.663  33.449 1.00 82.99  ? 264 PRO   B CB  1 
ATOM   5157 C CG  . PRO   B 1 264 ? -5.061  47.123  33.249 1.00 64.62  ? 264 PRO   B CG  1 
ATOM   5158 C CD  . PRO   B 1 264 ? -5.007  45.677  33.630 1.00 66.26  ? 264 PRO   B CD  1 
ATOM   5159 N N   . SER   B 1 265 ? -2.180  48.345  36.273 1.00 74.77  ? 265 SER   B N   1 
ATOM   5160 C CA  . SER   B 1 265 ? -2.137  49.023  37.565 1.00 83.99  ? 265 SER   B CA  1 
ATOM   5161 C C   . SER   B 1 265 ? -3.241  50.064  37.698 1.00 94.78  ? 265 SER   B C   1 
ATOM   5162 O O   . SER   B 1 265 ? -3.774  50.264  38.795 1.00 96.01  ? 265 SER   B O   1 
ATOM   5163 C CB  . SER   B 1 265 ? -0.767  49.668  37.771 1.00 86.46  ? 265 SER   B CB  1 
ATOM   5164 O OG  . SER   B 1 265 ? -0.407  50.463  36.656 1.00 105.18 ? 265 SER   B OG  1 
ATOM   5165 N N   . ASP   B 1 266 ? -3.596  50.738  36.601 1.00 105.39 ? 266 ASP   B N   1 
ATOM   5166 C CA  . ASP   B 1 266 ? -4.638  51.758  36.655 1.00 107.06 ? 266 ASP   B CA  1 
ATOM   5167 C C   . ASP   B 1 266 ? -6.007  51.176  36.983 1.00 108.84 ? 266 ASP   B C   1 
ATOM   5168 O O   . ASP   B 1 266 ? -6.900  51.924  37.396 1.00 114.79 ? 266 ASP   B O   1 
ATOM   5169 C CB  . ASP   B 1 266 ? -4.697  52.525  35.331 1.00 114.28 ? 266 ASP   B CB  1 
ATOM   5170 C CG  . ASP   B 1 266 ? -5.266  51.694  34.195 1.00 124.03 ? 266 ASP   B CG  1 
ATOM   5171 O OD1 . ASP   B 1 266 ? -6.145  52.201  33.467 1.00 133.47 ? 266 ASP   B OD1 1 
ATOM   5172 O OD2 . ASP   B 1 266 ? -4.837  50.534  34.031 1.00 117.05 ? 266 ASP   B OD2 1 
ATOM   5173 N N   . SER   B 1 267 ? -6.196  49.865  36.806 1.00 102.10 ? 267 SER   B N   1 
ATOM   5174 C CA  . SER   B 1 267 ? -7.478  49.242  37.113 1.00 97.86  ? 267 SER   B CA  1 
ATOM   5175 C C   . SER   B 1 267 ? -7.796  49.247  38.605 1.00 99.41  ? 267 SER   B C   1 
ATOM   5176 O O   . SER   B 1 267 ? -8.961  49.063  38.975 1.00 92.30  ? 267 SER   B O   1 
ATOM   5177 C CB  . SER   B 1 267 ? -7.503  47.809  36.579 1.00 89.90  ? 267 SER   B CB  1 
ATOM   5178 O OG  . SER   B 1 267 ? -6.530  47.007  37.224 1.00 82.39  ? 267 SER   B OG  1 
ATOM   5179 N N   . GLY   B 1 268 ? -6.800  49.452  39.463 1.00 95.87  ? 268 GLY   B N   1 
ATOM   5180 C CA  . GLY   B 1 268 ? -7.014  49.450  40.896 1.00 85.29  ? 268 GLY   B CA  1 
ATOM   5181 C C   . GLY   B 1 268 ? -6.895  48.102  41.568 1.00 88.62  ? 268 GLY   B C   1 
ATOM   5182 O O   . GLY   B 1 268 ? -7.171  48.001  42.771 1.00 78.82  ? 268 GLY   B O   1 
ATOM   5183 N N   . VAL   B 1 269 ? -6.497  47.063  40.834 1.00 84.30  ? 269 VAL   B N   1 
ATOM   5184 C CA  . VAL   B 1 269 ? -6.377  45.733  41.413 1.00 63.92  ? 269 VAL   B CA  1 
ATOM   5185 C C   . VAL   B 1 269 ? -5.235  45.706  42.425 1.00 68.71  ? 269 VAL   B C   1 
ATOM   5186 O O   . VAL   B 1 269 ? -4.239  46.432  42.300 1.00 74.11  ? 269 VAL   B O   1 
ATOM   5187 C CB  . VAL   B 1 269 ? -6.167  44.691  40.297 1.00 69.39  ? 269 VAL   B CB  1 
ATOM   5188 C CG1 . VAL   B 1 269 ? -4.852  44.941  39.572 1.00 73.54  ? 269 VAL   B CG1 1 
ATOM   5189 C CG2 . VAL   B 1 269 ? -6.230  43.273  40.846 1.00 68.37  ? 269 VAL   B CG2 1 
ATOM   5190 N N   . ARG   B 1 270 ? -5.389  44.872  43.449 1.00 66.79  ? 270 ARG   B N   1 
ATOM   5191 C CA  . ARG   B 1 270 ? -4.342  44.611  44.428 1.00 60.51  ? 270 ARG   B CA  1 
ATOM   5192 C C   . ARG   B 1 270 ? -3.894  43.165  44.264 1.00 56.99  ? 270 ARG   B C   1 
ATOM   5193 O O   . ARG   B 1 270 ? -4.707  42.243  44.384 1.00 59.51  ? 270 ARG   B O   1 
ATOM   5194 C CB  . ARG   B 1 270 ? -4.839  44.867  45.851 1.00 66.11  ? 270 ARG   B CB  1 
ATOM   5195 C CG  . ARG   B 1 270 ? -3.724  45.094  46.855 1.00 83.13  ? 270 ARG   B CG  1 
ATOM   5196 C CD  . ARG   B 1 270 ? -4.168  44.757  48.268 1.00 91.64  ? 270 ARG   B CD  1 
ATOM   5197 N NE  . ARG   B 1 270 ? -3.028  44.626  49.171 1.00 89.24  ? 270 ARG   B NE  1 
ATOM   5198 C CZ  . ARG   B 1 270 ? -3.115  44.230  50.436 1.00 79.10  ? 270 ARG   B CZ  1 
ATOM   5199 N NH1 . ARG   B 1 270 ? -4.295  43.925  50.959 1.00 88.06  ? 270 ARG   B NH1 1 
ATOM   5200 N NH2 . ARG   B 1 270 ? -2.022  44.142  51.180 1.00 94.17  ? 270 ARG   B NH2 1 
ATOM   5201 N N   . ILE   B 1 271 ? -2.610  42.971  43.976 1.00 58.42  ? 271 ILE   B N   1 
ATOM   5202 C CA  . ILE   B 1 271 ? -2.058  41.662  43.645 1.00 53.15  ? 271 ILE   B CA  1 
ATOM   5203 C C   . ILE   B 1 271 ? -1.200  41.175  44.804 1.00 54.12  ? 271 ILE   B C   1 
ATOM   5204 O O   . ILE   B 1 271 ? -0.347  41.915  45.310 1.00 61.82  ? 271 ILE   B O   1 
ATOM   5205 C CB  . ILE   B 1 271 ? -1.243  41.714  42.343 1.00 50.26  ? 271 ILE   B CB  1 
ATOM   5206 C CG1 . ILE   B 1 271 ? -2.088  42.322  41.220 1.00 53.77  ? 271 ILE   B CG1 1 
ATOM   5207 C CG2 . ILE   B 1 271 ? -0.762  40.322  41.969 1.00 45.53  ? 271 ILE   B CG2 1 
ATOM   5208 C CD1 . ILE   B 1 271 ? -1.345  42.495  39.917 1.00 61.26  ? 271 ILE   B CD1 1 
ATOM   5209 N N   . ILE   B 1 272 ? -1.432  39.931  45.225 1.00 56.44  ? 272 ILE   B N   1 
ATOM   5210 C CA  . ILE   B 1 272 ? -0.688  39.295  46.302 1.00 58.52  ? 272 ILE   B CA  1 
ATOM   5211 C C   . ILE   B 1 272 ? -0.294  37.891  45.857 1.00 63.31  ? 272 ILE   B C   1 
ATOM   5212 O O   . ILE   B 1 272 ? -0.769  37.376  44.844 1.00 54.59  ? 272 ILE   B O   1 
ATOM   5213 C CB  . ILE   B 1 272 ? -1.487  39.233  47.621 1.00 52.08  ? 272 ILE   B CB  1 
ATOM   5214 C CG1 . ILE   B 1 272 ? -2.665  38.268  47.487 1.00 55.90  ? 272 ILE   B CG1 1 
ATOM   5215 C CG2 . ILE   B 1 272 ? -1.971  40.616  48.022 1.00 54.25  ? 272 ILE   B CG2 1 
ATOM   5216 C CD1 . ILE   B 1 272 ? -3.415  38.039  48.781 1.00 61.00  ? 272 ILE   B CD1 1 
ATOM   5217 N N   . ALA   B 1 273 ? 0.589   37.272  46.641 1.00 60.19  ? 273 ALA   B N   1 
ATOM   5218 C CA  . ALA   B 1 273 ? 1.015   35.900  46.407 1.00 52.66  ? 273 ALA   B CA  1 
ATOM   5219 C C   . ALA   B 1 273 ? 1.136   35.183  47.744 1.00 55.52  ? 273 ALA   B C   1 
ATOM   5220 O O   . ALA   B 1 273 ? 1.097   35.802  48.809 1.00 56.37  ? 273 ALA   B O   1 
ATOM   5221 C CB  . ALA   B 1 273 ? 2.343   35.839  45.642 1.00 42.83  ? 273 ALA   B CB  1 
ATOM   5222 N N   . GLU   B 1 274 ? 1.288   33.862  47.679 1.00 57.57  ? 274 GLU   B N   1 
ATOM   5223 C CA  . GLU   B 1 274 ? 1.411   33.016  48.869 1.00 45.68  ? 274 GLU   B CA  1 
ATOM   5224 C C   . GLU   B 1 274 ? 2.659   32.139  48.789 1.00 55.46  ? 274 GLU   B C   1 
ATOM   5225 O O   . GLU   B 1 274 ? 2.570   30.910  48.858 1.00 63.12  ? 274 GLU   B O   1 
ATOM   5226 C CB  . GLU   B 1 274 ? 0.163   32.150  49.035 1.00 55.95  ? 274 GLU   B CB  1 
ATOM   5227 C CG  . GLU   B 1 274 ? -1.142  32.917  49.128 1.00 69.06  ? 274 GLU   B CG  1 
ATOM   5228 C CD  . GLU   B 1 274 ? -2.348  32.033  48.864 1.00 89.85  ? 274 GLU   B CD  1 
ATOM   5229 O OE1 . GLU   B 1 274 ? -2.178  30.943  48.278 1.00 94.42  ? 274 GLU   B OE1 1 
ATOM   5230 O OE2 . GLU   B 1 274 ? -3.467  32.420  49.256 1.00 81.82  ? 274 GLU   B OE2 1 
ATOM   5231 N N   . PRO   B 1 275 ? 3.846   32.733  48.650 1.00 42.25  ? 275 PRO   B N   1 
ATOM   5232 C CA  . PRO   B 1 275 ? 5.058   31.909  48.534 1.00 45.35  ? 275 PRO   B CA  1 
ATOM   5233 C C   . PRO   B 1 275 ? 5.410   31.277  49.874 1.00 54.39  ? 275 PRO   B C   1 
ATOM   5234 O O   . PRO   B 1 275 ? 5.578   31.973  50.877 1.00 55.06  ? 275 PRO   B O   1 
ATOM   5235 C CB  . PRO   B 1 275 ? 6.122   32.912  48.081 1.00 47.17  ? 275 PRO   B CB  1 
ATOM   5236 C CG  . PRO   B 1 275 ? 5.680   34.195  48.697 1.00 50.26  ? 275 PRO   B CG  1 
ATOM   5237 C CD  . PRO   B 1 275 ? 4.171   34.173  48.686 1.00 40.68  ? 275 PRO   B CD  1 
ATOM   5238 N N   . GLY   B 1 276 ? 5.484   29.948  49.898 1.00 53.51  ? 276 GLY   B N   1 
ATOM   5239 C CA  . GLY   B 1 276 ? 5.983   29.274  51.079 1.00 47.15  ? 276 GLY   B CA  1 
ATOM   5240 C C   . GLY   B 1 276 ? 7.447   28.878  51.031 1.00 53.54  ? 276 GLY   B C   1 
ATOM   5241 O O   . GLY   B 1 276 ? 8.245   29.334  51.854 1.00 58.53  ? 276 GLY   B O   1 
ATOM   5242 N N   . ARG   B 1 277 ? 7.828   28.063  50.045 1.00 52.51  ? 277 ARG   B N   1 
ATOM   5243 C CA  . ARG   B 1 277 ? 9.180   27.514  50.030 1.00 45.93  ? 277 ARG   B CA  1 
ATOM   5244 C C   . ARG   B 1 277 ? 10.213  28.525  49.553 1.00 49.55  ? 277 ARG   B C   1 
ATOM   5245 O O   . ARG   B 1 277 ? 11.390  28.410  49.912 1.00 53.80  ? 277 ARG   B O   1 
ATOM   5246 C CB  . ARG   B 1 277 ? 9.231   26.248  49.170 1.00 42.04  ? 277 ARG   B CB  1 
ATOM   5247 C CG  . ARG   B 1 277 ? 9.152   26.483  47.681 1.00 52.38  ? 277 ARG   B CG  1 
ATOM   5248 C CD  . ARG   B 1 277 ? 9.328   25.185  46.912 1.00 47.71  ? 277 ARG   B CD  1 
ATOM   5249 N NE  . ARG   B 1 277 ? 8.195   24.284  47.096 1.00 56.67  ? 277 ARG   B NE  1 
ATOM   5250 C CZ  . ARG   B 1 277 ? 8.280   23.089  47.673 1.00 55.89  ? 277 ARG   B CZ  1 
ATOM   5251 N NH1 . ARG   B 1 277 ? 7.194   22.338  47.801 1.00 49.74  ? 277 ARG   B NH1 1 
ATOM   5252 N NH2 . ARG   B 1 277 ? 9.450   22.636  48.098 1.00 61.42  ? 277 ARG   B NH2 1 
ATOM   5253 N N   . TYR   B 1 278 ? 9.796   29.510  48.753 1.00 54.50  ? 278 TYR   B N   1 
ATOM   5254 C CA  . TYR   B 1 278 ? 10.734  30.496  48.226 1.00 43.56  ? 278 TYR   B CA  1 
ATOM   5255 C C   . TYR   B 1 278 ? 11.488  31.206  49.343 1.00 52.13  ? 278 TYR   B C   1 
ATOM   5256 O O   . TYR   B 1 278 ? 12.682  31.502  49.208 1.00 53.75  ? 278 TYR   B O   1 
ATOM   5257 C CB  . TYR   B 1 278 ? 9.991   31.509  47.354 1.00 41.23  ? 278 TYR   B CB  1 
ATOM   5258 C CG  . TYR   B 1 278 ? 10.789  32.757  47.066 1.00 47.51  ? 278 TYR   B CG  1 
ATOM   5259 C CD1 . TYR   B 1 278 ? 11.748  32.774  46.063 1.00 44.31  ? 278 TYR   B CD1 1 
ATOM   5260 C CD2 . TYR   B 1 278 ? 10.581  33.921  47.796 1.00 48.71  ? 278 TYR   B CD2 1 
ATOM   5261 C CE1 . TYR   B 1 278 ? 12.482  33.913  45.798 1.00 44.65  ? 278 TYR   B CE1 1 
ATOM   5262 C CE2 . TYR   B 1 278 ? 11.310  35.063  47.538 1.00 44.68  ? 278 TYR   B CE2 1 
ATOM   5263 C CZ  . TYR   B 1 278 ? 12.258  35.055  46.537 1.00 44.83  ? 278 TYR   B CZ  1 
ATOM   5264 O OH  . TYR   B 1 278 ? 12.986  36.193  46.277 1.00 50.01  ? 278 TYR   B OH  1 
ATOM   5265 N N   . TYR   B 1 279 ? 10.810  31.488  50.456 1.00 55.09  ? 279 TYR   B N   1 
ATOM   5266 C CA  . TYR   B 1 279 ? 11.416  32.288  51.512 1.00 49.70  ? 279 TYR   B CA  1 
ATOM   5267 C C   . TYR   B 1 279 ? 12.380  31.491  52.384 1.00 57.43  ? 279 TYR   B C   1 
ATOM   5268 O O   . TYR   B 1 279 ? 13.363  32.053  52.878 1.00 53.07  ? 279 TYR   B O   1 
ATOM   5269 C CB  . TYR   B 1 279 ? 10.326  32.902  52.391 1.00 44.72  ? 279 TYR   B CB  1 
ATOM   5270 C CG  . TYR   B 1 279 ? 9.885   34.276  51.950 1.00 58.39  ? 279 TYR   B CG  1 
ATOM   5271 C CD1 . TYR   B 1 279 ? 10.699  35.382  52.153 1.00 59.30  ? 279 TYR   B CD1 1 
ATOM   5272 C CD2 . TYR   B 1 279 ? 8.654   34.471  51.338 1.00 54.59  ? 279 TYR   B CD2 1 
ATOM   5273 C CE1 . TYR   B 1 279 ? 10.303  36.642  51.755 1.00 65.02  ? 279 TYR   B CE1 1 
ATOM   5274 C CE2 . TYR   B 1 279 ? 8.249   35.730  50.937 1.00 45.60  ? 279 TYR   B CE2 1 
ATOM   5275 C CZ  . TYR   B 1 279 ? 9.078   36.811  51.148 1.00 57.72  ? 279 TYR   B CZ  1 
ATOM   5276 O OH  . TYR   B 1 279 ? 8.683   38.066  50.751 1.00 54.58  ? 279 TYR   B OH  1 
ATOM   5277 N N   . VAL   B 1 280 ? 12.138  30.196  52.573 1.00 55.03  ? 280 VAL   B N   1 
ATOM   5278 C CA  . VAL   B 1 280 ? 12.792  29.458  53.645 1.00 54.99  ? 280 VAL   B CA  1 
ATOM   5279 C C   . VAL   B 1 280 ? 13.585  28.251  53.165 1.00 61.22  ? 280 VAL   B C   1 
ATOM   5280 O O   . VAL   B 1 280 ? 14.395  27.725  53.948 1.00 57.57  ? 280 VAL   B O   1 
ATOM   5281 C CB  . VAL   B 1 280 ? 11.769  29.018  54.715 1.00 53.03  ? 280 VAL   B CB  1 
ATOM   5282 C CG1 . VAL   B 1 280 ? 11.063  30.225  55.309 1.00 56.88  ? 280 VAL   B CG1 1 
ATOM   5283 C CG2 . VAL   B 1 280 ? 10.770  28.051  54.120 1.00 42.86  ? 280 VAL   B CG2 1 
ATOM   5284 N N   . ALA   B 1 281 ? 13.384  27.773  51.932 1.00 53.00  ? 281 ALA   B N   1 
ATOM   5285 C CA  . ALA   B 1 281 ? 13.986  26.513  51.504 1.00 48.42  ? 281 ALA   B CA  1 
ATOM   5286 C C   . ALA   B 1 281 ? 15.497  26.505  51.714 1.00 52.79  ? 281 ALA   B C   1 
ATOM   5287 O O   . ALA   B 1 281 ? 16.037  25.633  52.403 1.00 45.78  ? 281 ALA   B O   1 
ATOM   5288 C CB  . ALA   B 1 281 ? 13.648  26.247  50.038 1.00 50.23  ? 281 ALA   B CB  1 
ATOM   5289 N N   . SER   B 1 282 ? 16.193  27.484  51.139 1.00 53.37  ? 282 SER   B N   1 
ATOM   5290 C CA  . SER   B 1 282 ? 17.649  27.508  51.202 1.00 53.87  ? 282 SER   B CA  1 
ATOM   5291 C C   . SER   B 1 282 ? 18.185  28.062  52.516 1.00 53.48  ? 282 SER   B C   1 
ATOM   5292 O O   . SER   B 1 282 ? 19.396  27.991  52.748 1.00 56.15  ? 282 SER   B O   1 
ATOM   5293 C CB  . SER   B 1 282 ? 18.211  28.325  50.036 1.00 49.79  ? 282 SER   B CB  1 
ATOM   5294 O OG  . SER   B 1 282 ? 17.709  29.650  50.050 1.00 63.83  ? 282 SER   B OG  1 
ATOM   5295 N N   . ALA   B 1 283 ? 17.321  28.606  53.376 1.00 52.25  ? 283 ALA   B N   1 
ATOM   5296 C CA  . ALA   B 1 283 ? 17.782  29.205  54.623 1.00 55.91  ? 283 ALA   B CA  1 
ATOM   5297 C C   . ALA   B 1 283 ? 18.230  28.170  55.651 1.00 66.90  ? 283 ALA   B C   1 
ATOM   5298 O O   . ALA   B 1 283 ? 18.997  28.512  56.557 1.00 66.63  ? 283 ALA   B O   1 
ATOM   5299 C CB  . ALA   B 1 283 ? 16.683  30.087  55.217 1.00 51.32  ? 283 ALA   B CB  1 
ATOM   5300 N N   . PHE   B 1 284 ? 17.776  26.925  55.536 1.00 56.65  ? 284 PHE   B N   1 
ATOM   5301 C CA  . PHE   B 1 284 ? 18.058  25.888  56.520 1.00 46.25  ? 284 PHE   B CA  1 
ATOM   5302 C C   . PHE   B 1 284 ? 19.049  24.885  55.950 1.00 51.44  ? 284 PHE   B C   1 
ATOM   5303 O O   . PHE   B 1 284 ? 18.876  24.411  54.822 1.00 53.32  ? 284 PHE   B O   1 
ATOM   5304 C CB  . PHE   B 1 284 ? 16.779  25.160  56.935 1.00 52.00  ? 284 PHE   B CB  1 
ATOM   5305 C CG  . PHE   B 1 284 ? 15.889  25.955  57.845 1.00 54.38  ? 284 PHE   B CG  1 
ATOM   5306 C CD1 . PHE   B 1 284 ? 15.256  27.102  57.396 1.00 59.37  ? 284 PHE   B CD1 1 
ATOM   5307 C CD2 . PHE   B 1 284 ? 15.675  25.546  59.150 1.00 56.49  ? 284 PHE   B CD2 1 
ATOM   5308 C CE1 . PHE   B 1 284 ? 14.434  27.830  58.235 1.00 55.08  ? 284 PHE   B CE1 1 
ATOM   5309 C CE2 . PHE   B 1 284 ? 14.855  26.267  59.993 1.00 56.88  ? 284 PHE   B CE2 1 
ATOM   5310 C CZ  . PHE   B 1 284 ? 14.234  27.411  59.536 1.00 54.25  ? 284 PHE   B CZ  1 
ATOM   5311 N N   . THR   B 1 285 ? 20.084  24.565  56.724 1.00 53.36  ? 285 THR   B N   1 
ATOM   5312 C CA  . THR   B 1 285 ? 20.983  23.466  56.401 1.00 45.91  ? 285 THR   B CA  1 
ATOM   5313 C C   . THR   B 1 285 ? 20.974  22.470  57.552 1.00 52.91  ? 285 THR   B C   1 
ATOM   5314 O O   . THR   B 1 285 ? 21.128  22.858  58.715 1.00 54.10  ? 285 THR   B O   1 
ATOM   5315 C CB  . THR   B 1 285 ? 22.407  23.957  56.133 1.00 49.70  ? 285 THR   B CB  1 
ATOM   5316 O OG1 . THR   B 1 285 ? 22.385  24.946  55.099 1.00 58.08  ? 285 THR   B OG1 1 
ATOM   5317 C CG2 . THR   B 1 285 ? 23.270  22.798  55.665 1.00 55.27  ? 285 THR   B CG2 1 
ATOM   5318 N N   . LEU   B 1 286 ? 20.805  21.192  57.226 1.00 45.46  ? 286 LEU   B N   1 
ATOM   5319 C CA  . LEU   B 1 286 ? 20.655  20.136  58.215 1.00 49.26  ? 286 LEU   B CA  1 
ATOM   5320 C C   . LEU   B 1 286 ? 21.953  19.349  58.336 1.00 52.95  ? 286 LEU   B C   1 
ATOM   5321 O O   . LEU   B 1 286 ? 22.563  18.989  57.326 1.00 55.41  ? 286 LEU   B O   1 
ATOM   5322 C CB  . LEU   B 1 286 ? 19.506  19.203  57.827 1.00 48.85  ? 286 LEU   B CB  1 
ATOM   5323 C CG  . LEU   B 1 286 ? 19.326  17.922  58.640 1.00 48.38  ? 286 LEU   B CG  1 
ATOM   5324 C CD1 . LEU   B 1 286 ? 18.977  18.239  60.086 1.00 52.12  ? 286 LEU   B CD1 1 
ATOM   5325 C CD2 . LEU   B 1 286 ? 18.263  17.041  58.003 1.00 52.03  ? 286 LEU   B CD2 1 
ATOM   5326 N N   . ALA   B 1 287 ? 22.374  19.088  59.570 1.00 54.84  ? 287 ALA   B N   1 
ATOM   5327 C CA  . ALA   B 1 287 ? 23.536  18.260  59.855 1.00 50.32  ? 287 ALA   B CA  1 
ATOM   5328 C C   . ALA   B 1 287 ? 23.067  17.035  60.622 1.00 53.14  ? 287 ALA   B C   1 
ATOM   5329 O O   . ALA   B 1 287 ? 22.454  17.165  61.688 1.00 59.79  ? 287 ALA   B O   1 
ATOM   5330 C CB  . ALA   B 1 287 ? 24.582  19.037  60.657 1.00 61.86  ? 287 ALA   B CB  1 
ATOM   5331 N N   . VAL   B 1 288 ? 23.352  15.854  60.080 1.00 52.83  ? 288 VAL   B N   1 
ATOM   5332 C CA  . VAL   B 1 288 ? 23.031  14.594  60.735 1.00 57.49  ? 288 VAL   B CA  1 
ATOM   5333 C C   . VAL   B 1 288 ? 24.331  13.854  61.008 1.00 58.73  ? 288 VAL   B C   1 
ATOM   5334 O O   . VAL   B 1 288 ? 25.329  14.030  60.303 1.00 53.81  ? 288 VAL   B O   1 
ATOM   5335 C CB  . VAL   B 1 288 ? 22.073  13.724  59.893 1.00 56.89  ? 288 VAL   B CB  1 
ATOM   5336 C CG1 . VAL   B 1 288 ? 20.762  14.458  59.659 1.00 61.33  ? 288 VAL   B CG1 1 
ATOM   5337 C CG2 . VAL   B 1 288 ? 22.721  13.347  58.568 1.00 48.03  ? 288 VAL   B CG2 1 
ATOM   5338 N N   . ASN   B 1 289 ? 24.322  13.032  62.051 1.00 55.21  ? 289 ASN   B N   1 
ATOM   5339 C CA  . ASN   B 1 289 ? 25.487  12.248  62.431 1.00 56.23  ? 289 ASN   B CA  1 
ATOM   5340 C C   . ASN   B 1 289 ? 25.295  10.793  62.035 1.00 51.94  ? 289 ASN   B C   1 
ATOM   5341 O O   . ASN   B 1 289 ? 24.207  10.233  62.203 1.00 56.35  ? 289 ASN   B O   1 
ATOM   5342 C CB  . ASN   B 1 289 ? 25.752  12.342  63.933 1.00 57.62  ? 289 ASN   B CB  1 
ATOM   5343 C CG  . ASN   B 1 289 ? 27.146  11.887  64.300 1.00 61.75  ? 289 ASN   B CG  1 
ATOM   5344 O OD1 . ASN   B 1 289 ? 27.334  10.795  64.837 1.00 58.60  ? 289 ASN   B OD1 1 
ATOM   5345 N ND2 . ASN   B 1 289 ? 28.136  12.720  64.003 1.00 75.29  ? 289 ASN   B ND2 1 
ATOM   5346 N N   . ILE   B 1 290 ? 26.357  10.184  61.514 1.00 48.09  ? 290 ILE   B N   1 
ATOM   5347 C CA  . ILE   B 1 290 ? 26.339  8.760   61.192 1.00 53.11  ? 290 ILE   B CA  1 
ATOM   5348 C C   . ILE   B 1 290 ? 26.441  7.980   62.499 1.00 51.86  ? 290 ILE   B C   1 
ATOM   5349 O O   . ILE   B 1 290 ? 27.505  7.932   63.121 1.00 53.07  ? 290 ILE   B O   1 
ATOM   5350 C CB  . ILE   B 1 290 ? 27.471  8.387   60.233 1.00 48.40  ? 290 ILE   B CB  1 
ATOM   5351 C CG1 . ILE   B 1 290 ? 27.287  9.103   58.897 1.00 41.92  ? 290 ILE   B CG1 1 
ATOM   5352 C CG2 . ILE   B 1 290 ? 27.513  6.879   60.026 1.00 40.11  ? 290 ILE   B CG2 1 
ATOM   5353 C CD1 . ILE   B 1 290 ? 28.438  8.904   57.951 1.00 54.52  ? 290 ILE   B CD1 1 
ATOM   5354 N N   . ILE   B 1 291 ? 25.344  7.349   62.910 1.00 51.38  ? 291 ILE   B N   1 
ATOM   5355 C CA  . ILE   B 1 291 ? 25.325  6.637   64.179 1.00 43.02  ? 291 ILE   B CA  1 
ATOM   5356 C C   . ILE   B 1 291 ? 25.600  5.147   64.017 1.00 48.39  ? 291 ILE   B C   1 
ATOM   5357 O O   . ILE   B 1 291 ? 25.939  4.484   65.010 1.00 56.18  ? 291 ILE   B O   1 
ATOM   5358 C CB  . ILE   B 1 291 ? 23.988  6.860   64.918 1.00 55.92  ? 291 ILE   B CB  1 
ATOM   5359 C CG1 . ILE   B 1 291 ? 22.815  6.349   64.083 1.00 58.56  ? 291 ILE   B CG1 1 
ATOM   5360 C CG2 . ILE   B 1 291 ? 23.802  8.335   65.242 1.00 50.53  ? 291 ILE   B CG2 1 
ATOM   5361 C CD1 . ILE   B 1 291 ? 21.521  6.256   64.854 1.00 48.29  ? 291 ILE   B CD1 1 
ATOM   5362 N N   . ALA   B 1 292 ? 25.478  4.602   62.807 1.00 57.10  ? 292 ALA   B N   1 
ATOM   5363 C CA  . ALA   B 1 292 ? 25.758  3.184   62.613 1.00 42.80  ? 292 ALA   B CA  1 
ATOM   5364 C C   . ALA   B 1 292 ? 26.261  2.944   61.197 1.00 46.78  ? 292 ALA   B C   1 
ATOM   5365 O O   . ALA   B 1 292 ? 26.075  3.771   60.302 1.00 49.52  ? 292 ALA   B O   1 
ATOM   5366 C CB  . ALA   B 1 292 ? 24.523  2.322   62.894 1.00 49.97  ? 292 ALA   B CB  1 
ATOM   5367 N N   . LYS   B 1 293 ? 26.870  1.776   60.998 1.00 47.83  ? 293 LYS   B N   1 
ATOM   5368 C CA  . LYS   B 1 293 ? 27.550  1.467   59.749 1.00 46.52  ? 293 LYS   B CA  1 
ATOM   5369 C C   . LYS   B 1 293 ? 27.581  -0.040  59.531 1.00 48.20  ? 293 LYS   B C   1 
ATOM   5370 O O   . LYS   B 1 293 ? 27.869  -0.803  60.457 1.00 60.16  ? 293 LYS   B O   1 
ATOM   5371 C CB  . LYS   B 1 293 ? 28.975  2.031   59.751 1.00 46.83  ? 293 LYS   B CB  1 
ATOM   5372 C CG  . LYS   B 1 293 ? 29.758  1.765   58.481 1.00 50.25  ? 293 LYS   B CG  1 
ATOM   5373 C CD  . LYS   B 1 293 ? 31.193  2.237   58.632 1.00 55.58  ? 293 LYS   B CD  1 
ATOM   5374 C CE  . LYS   B 1 293 ? 32.038  1.833   57.440 1.00 73.76  ? 293 LYS   B CE  1 
ATOM   5375 N NZ  . LYS   B 1 293 ? 33.458  2.248   57.609 1.00 78.98  ? 293 LYS   B NZ  1 
ATOM   5376 N N   . LYS   B 1 294 ? 27.283  -0.457  58.300 1.00 45.71  ? 294 LYS   B N   1 
ATOM   5377 C CA  . LYS   B 1 294 ? 27.371  -1.848  57.879 1.00 53.33  ? 294 LYS   B CA  1 
ATOM   5378 C C   . LYS   B 1 294 ? 28.119  -1.932  56.555 1.00 57.33  ? 294 LYS   B C   1 
ATOM   5379 O O   . LYS   B 1 294 ? 27.954  -1.074  55.683 1.00 58.20  ? 294 LYS   B O   1 
ATOM   5380 C CB  . LYS   B 1 294 ? 25.984  -2.487  57.730 1.00 53.57  ? 294 LYS   B CB  1 
ATOM   5381 C CG  . LYS   B 1 294 ? 25.204  -2.606  59.026 1.00 55.51  ? 294 LYS   B CG  1 
ATOM   5382 C CD  . LYS   B 1 294 ? 23.832  -3.211  58.781 1.00 56.37  ? 294 LYS   B CD  1 
ATOM   5383 C CE  . LYS   B 1 294 ? 23.045  -3.330  60.073 1.00 48.19  ? 294 LYS   B CE  1 
ATOM   5384 N NZ  . LYS   B 1 294 ? 21.679  -3.863  59.827 1.00 64.97  ? 294 LYS   B NZ  1 
ATOM   5385 N N   . ILE   B 1 295 ? 28.930  -2.977  56.409 1.00 57.36  ? 295 ILE   B N   1 
ATOM   5386 C CA  . ILE   B 1 295 ? 29.713  -3.225  55.203 1.00 70.50  ? 295 ILE   B CA  1 
ATOM   5387 C C   . ILE   B 1 295 ? 29.158  -4.468  54.522 1.00 66.18  ? 295 ILE   B C   1 
ATOM   5388 O O   . ILE   B 1 295 ? 29.057  -5.530  55.146 1.00 71.31  ? 295 ILE   B O   1 
ATOM   5389 C CB  . ILE   B 1 295 ? 31.205  -3.396  55.523 1.00 73.19  ? 295 ILE   B CB  1 
ATOM   5390 C CG1 . ILE   B 1 295 ? 31.670  -2.304  56.491 1.00 84.91  ? 295 ILE   B CG1 1 
ATOM   5391 C CG2 . ILE   B 1 295 ? 32.032  -3.377  54.245 1.00 62.41  ? 295 ILE   B CG2 1 
ATOM   5392 C CD1 . ILE   B 1 295 ? 33.102  -2.471  56.962 1.00 75.91  ? 295 ILE   B CD1 1 
ATOM   5393 N N   . VAL   B 1 296 ? 28.790  -4.339  53.247 1.00 71.52  ? 296 VAL   B N   1 
ATOM   5394 C CA  . VAL   B 1 296 ? 28.236  -5.441  52.470 1.00 68.92  ? 296 VAL   B CA  1 
ATOM   5395 C C   . VAL   B 1 296 ? 29.212  -5.800  51.358 1.00 65.53  ? 296 VAL   B C   1 
ATOM   5396 O O   . VAL   B 1 296 ? 29.758  -4.916  50.682 1.00 84.11  ? 296 VAL   B O   1 
ATOM   5397 C CB  . VAL   B 1 296 ? 26.851  -5.086  51.894 1.00 74.60  ? 296 VAL   B CB  1 
ATOM   5398 C CG1 . VAL   B 1 296 ? 26.227  -6.298  51.231 1.00 75.28  ? 296 VAL   B CG1 1 
ATOM   5399 C CG2 . VAL   B 1 296 ? 25.946  -4.553  52.988 1.00 58.07  ? 296 VAL   B CG2 1 
ATOM   5400 N N   . LEU   B 1 297 ? 29.435  -7.099  51.178 1.00 70.86  ? 297 LEU   B N   1 
ATOM   5401 C CA  . LEU   B 1 297 ? 30.340  -7.618  50.162 1.00 78.88  ? 297 LEU   B CA  1 
ATOM   5402 C C   . LEU   B 1 297 ? 29.530  -8.161  48.992 1.00 89.26  ? 297 LEU   B C   1 
ATOM   5403 O O   . LEU   B 1 297 ? 28.610  -8.962  49.192 1.00 94.52  ? 297 LEU   B O   1 
ATOM   5404 C CB  . LEU   B 1 297 ? 31.230  -8.712  50.754 1.00 87.76  ? 297 LEU   B CB  1 
ATOM   5405 C CG  . LEU   B 1 297 ? 32.230  -8.244  51.814 1.00 89.99  ? 297 LEU   B CG  1 
ATOM   5406 C CD1 . LEU   B 1 297 ? 33.018  -9.420  52.372 1.00 81.83  ? 297 LEU   B CD1 1 
ATOM   5407 C CD2 . LEU   B 1 297 ? 33.165  -7.188  51.244 1.00 83.29  ? 297 LEU   B CD2 1 
ATOM   5408 N N   . LYS   B 1 298 ? 29.871  -7.728  47.778 1.00 95.35  ? 298 LYS   B N   1 
ATOM   5409 C CA  . LYS   B 1 298 ? 29.175  -8.156  46.567 1.00 99.98  ? 298 LYS   B CA  1 
ATOM   5410 C C   . LYS   B 1 298 ? 30.013  -9.200  45.839 1.00 108.40 ? 298 LYS   B C   1 
ATOM   5411 O O   . LYS   B 1 298 ? 31.176  -8.946  45.505 1.00 119.37 ? 298 LYS   B O   1 
ATOM   5412 C CB  . LYS   B 1 298 ? 28.884  -6.973  45.642 1.00 94.72  ? 298 LYS   B CB  1 
ATOM   5413 C CG  . LYS   B 1 298 ? 27.839  -5.994  46.165 1.00 102.55 ? 298 LYS   B CG  1 
ATOM   5414 C CD  . LYS   B 1 298 ? 27.662  -4.826  45.206 1.00 103.75 ? 298 LYS   B CD  1 
ATOM   5415 C CE  . LYS   B 1 298 ? 26.422  -4.005  45.523 1.00 111.22 ? 298 LYS   B CE  1 
ATOM   5416 N NZ  . LYS   B 1 298 ? 26.334  -2.791  44.660 1.00 91.96  ? 298 LYS   B NZ  1 
ATOM   5417 N N   . GLU   B 1 299 ? 29.420  -10.366 45.590 1.00 116.73 ? 299 GLU   B N   1 
ATOM   5418 C CA  . GLU   B 1 299 ? 30.105  -11.452 44.898 1.00 118.00 ? 299 GLU   B CA  1 
ATOM   5419 C C   . GLU   B 1 299 ? 29.537  -11.643 43.495 1.00 106.67 ? 299 GLU   B C   1 
ATOM   5420 O O   . GLU   B 1 299 ? 29.977  -12.521 42.752 1.00 120.62 ? 299 GLU   B O   1 
ATOM   5421 C CB  . GLU   B 1 299 ? 29.994  -12.750 45.700 1.00 128.92 ? 299 GLU   B CB  1 
ATOM   5422 C CG  . GLU   B 1 299 ? 30.693  -12.697 47.051 1.00 128.16 ? 299 GLU   B CG  1 
ATOM   5423 C CD  . GLU   B 1 299 ? 30.959  -14.074 47.630 1.00 132.28 ? 299 GLU   B CD  1 
ATOM   5424 O OE1 . GLU   B 1 299 ? 30.881  -15.065 46.873 1.00 135.28 ? 299 GLU   B OE1 1 
ATOM   5425 O OE2 . GLU   B 1 299 ? 31.250  -14.163 48.841 1.00 126.07 ? 299 GLU   B OE2 1 
ATOM   5426 N N   . SER   B 1 310 ? 36.414  -8.372  45.917 1.00 131.14 ? 310 SER   B N   1 
ATOM   5427 C CA  . SER   B 1 310 ? 35.134  -8.113  46.566 1.00 126.86 ? 310 SER   B CA  1 
ATOM   5428 C C   . SER   B 1 310 ? 34.784  -6.633  46.496 1.00 125.95 ? 310 SER   B C   1 
ATOM   5429 O O   . SER   B 1 310 ? 35.496  -5.795  47.052 1.00 130.94 ? 310 SER   B O   1 
ATOM   5430 C CB  . SER   B 1 310 ? 35.162  -8.568  48.025 1.00 132.13 ? 310 SER   B CB  1 
ATOM   5431 O OG  . SER   B 1 310 ? 35.748  -7.580  48.854 1.00 139.51 ? 310 SER   B OG  1 
ATOM   5432 N N   . GLU   B 1 311 ? 33.689  -6.316  45.808 1.00 115.97 ? 311 GLU   B N   1 
ATOM   5433 C CA  . GLU   B 1 311 ? 33.212  -4.942  45.719 1.00 106.39 ? 311 GLU   B CA  1 
ATOM   5434 C C   . GLU   B 1 311 ? 32.550  -4.550  47.034 1.00 106.33 ? 311 GLU   B C   1 
ATOM   5435 O O   . GLU   B 1 311 ? 31.575  -5.180  47.458 1.00 99.80  ? 311 GLU   B O   1 
ATOM   5436 C CB  . GLU   B 1 311 ? 32.233  -4.784  44.560 1.00 102.79 ? 311 GLU   B CB  1 
ATOM   5437 C CG  . GLU   B 1 311 ? 31.577  -3.417  44.505 1.00 114.02 ? 311 GLU   B CG  1 
ATOM   5438 C CD  . GLU   B 1 311 ? 30.381  -3.381  43.577 1.00 125.40 ? 311 GLU   B CD  1 
ATOM   5439 O OE1 . GLU   B 1 311 ? 30.094  -4.416  42.939 1.00 127.12 ? 311 GLU   B OE1 1 
ATOM   5440 O OE2 . GLU   B 1 311 ? 29.726  -2.321  43.490 1.00 116.93 ? 311 GLU   B OE2 1 
ATOM   5441 N N   . GLN   B 1 312 ? 33.069  -3.506  47.670 1.00 103.15 ? 312 GLN   B N   1 
ATOM   5442 C CA  . GLN   B 1 312 ? 32.599  -3.081  48.980 1.00 92.10  ? 312 GLN   B CA  1 
ATOM   5443 C C   . GLN   B 1 312 ? 31.495  -2.044  48.828 1.00 85.81  ? 312 GLN   B C   1 
ATOM   5444 O O   . GLN   B 1 312 ? 31.667  -1.048  48.119 1.00 99.65  ? 312 GLN   B O   1 
ATOM   5445 C CB  . GLN   B 1 312 ? 33.755  -2.498  49.791 1.00 97.86  ? 312 GLN   B CB  1 
ATOM   5446 C CG  . GLN   B 1 312 ? 33.951  -3.130  51.152 1.00 101.28 ? 312 GLN   B CG  1 
ATOM   5447 C CD  . GLN   B 1 312 ? 35.293  -2.777  51.761 1.00 112.70 ? 312 GLN   B CD  1 
ATOM   5448 O OE1 . GLN   B 1 312 ? 36.054  -1.988  51.200 1.00 105.64 ? 312 GLN   B OE1 1 
ATOM   5449 N NE2 . GLN   B 1 312 ? 35.587  -3.355  52.919 1.00 109.68 ? 312 GLN   B NE2 1 
ATOM   5450 N N   . THR   B 1 313 ? 30.359  -2.281  49.480 1.00 73.33  ? 313 THR   B N   1 
ATOM   5451 C CA  . THR   B 1 313 ? 29.296  -1.292  49.559 1.00 64.26  ? 313 THR   B CA  1 
ATOM   5452 C C   . THR   B 1 313 ? 28.962  -1.018  51.018 1.00 74.72  ? 313 THR   B C   1 
ATOM   5453 O O   . THR   B 1 313 ? 29.254  -1.824  51.905 1.00 68.88  ? 313 THR   B O   1 
ATOM   5454 C CB  . THR   B 1 313 ? 28.054  -1.744  48.796 1.00 62.74  ? 313 THR   B CB  1 
ATOM   5455 O OG1 . THR   B 1 313 ? 27.497  -2.906  49.424 1.00 76.14  ? 313 THR   B OG1 1 
ATOM   5456 C CG2 . THR   B 1 313 ? 28.423  -2.048  47.363 1.00 81.62  ? 313 THR   B CG2 1 
ATOM   5457 N N   . PHE   B 1 314 ? 28.341  0.131   51.267 1.00 61.38  ? 314 PHE   B N   1 
ATOM   5458 C CA  . PHE   B 1 314 ? 28.148  0.567   52.642 1.00 57.88  ? 314 PHE   B CA  1 
ATOM   5459 C C   . PHE   B 1 314 ? 26.710  0.982   52.911 1.00 55.97  ? 314 PHE   B C   1 
ATOM   5460 O O   . PHE   B 1 314 ? 26.037  1.554   52.047 1.00 65.82  ? 314 PHE   B O   1 
ATOM   5461 C CB  . PHE   B 1 314 ? 29.093  1.719   52.978 1.00 59.25  ? 314 PHE   B CB  1 
ATOM   5462 C CG  . PHE   B 1 314 ? 30.537  1.321   53.005 1.00 58.55  ? 314 PHE   B CG  1 
ATOM   5463 C CD1 . PHE   B 1 314 ? 31.098  0.789   54.152 1.00 65.49  ? 314 PHE   B CD1 1 
ATOM   5464 C CD2 . PHE   B 1 314 ? 31.331  1.466   51.881 1.00 72.32  ? 314 PHE   B CD2 1 
ATOM   5465 C CE1 . PHE   B 1 314 ? 32.426  0.417   54.182 1.00 75.67  ? 314 PHE   B CE1 1 
ATOM   5466 C CE2 . PHE   B 1 314 ? 32.661  1.095   51.903 1.00 73.47  ? 314 PHE   B CE2 1 
ATOM   5467 C CZ  . PHE   B 1 314 ? 33.208  0.570   53.056 1.00 77.86  ? 314 PHE   B CZ  1 
ATOM   5468 N N   . MET   B 1 315 ? 26.249  0.682   54.123 1.00 48.23  ? 315 MET   B N   1 
ATOM   5469 C CA  . MET   B 1 315 ? 24.981  1.172   54.643 1.00 47.65  ? 315 MET   B CA  1 
ATOM   5470 C C   . MET   B 1 315 ? 25.285  2.050   55.846 1.00 55.62  ? 315 MET   B C   1 
ATOM   5471 O O   . MET   B 1 315 ? 25.861  1.577   56.831 1.00 54.62  ? 315 MET   B O   1 
ATOM   5472 C CB  . MET   B 1 315 ? 24.062  0.018   55.047 1.00 53.08  ? 315 MET   B CB  1 
ATOM   5473 C CG  . MET   B 1 315 ? 23.765  -0.970  53.938 1.00 69.11  ? 315 MET   B CG  1 
ATOM   5474 S SD  . MET   B 1 315 ? 22.888  -2.424  54.545 1.00 69.22  ? 315 MET   B SD  1 
ATOM   5475 C CE  . MET   B 1 315 ? 21.321  -1.707  55.033 1.00 57.34  ? 315 MET   B CE  1 
ATOM   5476 N N   . TYR   B 1 316 ? 24.910  3.320   55.767 1.00 48.92  ? 316 TYR   B N   1 
ATOM   5477 C CA  . TYR   B 1 316 ? 25.125  4.268   56.849 1.00 49.86  ? 316 TYR   B CA  1 
ATOM   5478 C C   . TYR   B 1 316 ? 23.783  4.596   57.484 1.00 51.32  ? 316 TYR   B C   1 
ATOM   5479 O O   . TYR   B 1 316 ? 22.822  4.903   56.776 1.00 50.47  ? 316 TYR   B O   1 
ATOM   5480 C CB  . TYR   B 1 316 ? 25.795  5.540   56.328 1.00 43.29  ? 316 TYR   B CB  1 
ATOM   5481 C CG  . TYR   B 1 316 ? 27.122  5.300   55.645 1.00 59.15  ? 316 TYR   B CG  1 
ATOM   5482 C CD1 . TYR   B 1 316 ? 28.248  4.937   56.375 1.00 57.96  ? 316 TYR   B CD1 1 
ATOM   5483 C CD2 . TYR   B 1 316 ? 27.248  5.424   54.267 1.00 60.24  ? 316 TYR   B CD2 1 
ATOM   5484 C CE1 . TYR   B 1 316 ? 29.464  4.715   55.752 1.00 54.77  ? 316 TYR   B CE1 1 
ATOM   5485 C CE2 . TYR   B 1 316 ? 28.458  5.202   53.636 1.00 68.39  ? 316 TYR   B CE2 1 
ATOM   5486 C CZ  . TYR   B 1 316 ? 29.563  4.850   54.383 1.00 71.60  ? 316 TYR   B CZ  1 
ATOM   5487 O OH  . TYR   B 1 316 ? 30.768  4.629   53.753 1.00 77.74  ? 316 TYR   B OH  1 
ATOM   5488 N N   . TYR   B 1 317 ? 23.722  4.545   58.811 1.00 44.83  ? 317 TYR   B N   1 
ATOM   5489 C CA  . TYR   B 1 317 ? 22.522  4.890   59.562 1.00 47.57  ? 317 TYR   B CA  1 
ATOM   5490 C C   . TYR   B 1 317 ? 22.782  6.201   60.286 1.00 51.59  ? 317 TYR   B C   1 
ATOM   5491 O O   . TYR   B 1 317 ? 23.729  6.294   61.079 1.00 57.36  ? 317 TYR   B O   1 
ATOM   5492 C CB  . TYR   B 1 317 ? 22.152  3.796   60.565 1.00 48.32  ? 317 TYR   B CB  1 
ATOM   5493 C CG  . TYR   B 1 317 ? 21.874  2.435   59.964 1.00 55.35  ? 317 TYR   B CG  1 
ATOM   5494 C CD1 . TYR   B 1 317 ? 22.908  1.625   59.514 1.00 54.66  ? 317 TYR   B CD1 1 
ATOM   5495 C CD2 . TYR   B 1 317 ? 20.575  1.952   59.870 1.00 50.29  ? 317 TYR   B CD2 1 
ATOM   5496 C CE1 . TYR   B 1 317 ? 22.656  0.379   58.970 1.00 53.02  ? 317 TYR   B CE1 1 
ATOM   5497 C CE2 . TYR   B 1 317 ? 20.313  0.708   59.329 1.00 52.30  ? 317 TYR   B CE2 1 
ATOM   5498 C CZ  . TYR   B 1 317 ? 21.356  -0.074  58.881 1.00 56.14  ? 317 TYR   B CZ  1 
ATOM   5499 O OH  . TYR   B 1 317 ? 21.094  -1.313  58.343 1.00 57.77  ? 317 TYR   B OH  1 
ATOM   5500 N N   . VAL   B 1 318 ? 21.939  7.195   60.023 1.00 44.45  ? 318 VAL   B N   1 
ATOM   5501 C CA  . VAL   B 1 318 ? 22.076  8.520   60.608 1.00 43.97  ? 318 VAL   B CA  1 
ATOM   5502 C C   . VAL   B 1 318 ? 20.889  8.780   61.532 1.00 46.90  ? 318 VAL   B C   1 
ATOM   5503 O O   . VAL   B 1 318 ? 19.910  8.036   61.549 1.00 58.47  ? 318 VAL   B O   1 
ATOM   5504 C CB  . VAL   B 1 318 ? 22.195  9.615   59.534 1.00 45.32  ? 318 VAL   B CB  1 
ATOM   5505 C CG1 . VAL   B 1 318 ? 23.431  9.382   58.688 1.00 49.63  ? 318 VAL   B CG1 1 
ATOM   5506 C CG2 . VAL   B 1 318 ? 20.954  9.631   58.672 1.00 42.26  ? 318 VAL   B CG2 1 
ATOM   5507 N N   . ASN   B 1 319 ? 20.982  9.864   62.305 1.00 52.52  ? 319 ASN   B N   1 
ATOM   5508 C CA  . ASN   B 1 319 ? 20.051  10.140  63.393 1.00 54.80  ? 319 ASN   B CA  1 
ATOM   5509 C C   . ASN   B 1 319 ? 18.911  11.068  62.983 1.00 52.89  ? 319 ASN   B C   1 
ATOM   5510 O O   . ASN   B 1 319 ? 18.412  11.839  63.809 1.00 62.09  ? 319 ASN   B O   1 
ATOM   5511 C CB  . ASN   B 1 319 ? 20.799  10.715  64.596 1.00 50.11  ? 319 ASN   B CB  1 
ATOM   5512 C CG  . ASN   B 1 319 ? 21.749  11.835  64.214 1.00 55.84  ? 319 ASN   B CG  1 
ATOM   5513 O OD1 . ASN   B 1 319 ? 21.743  12.316  63.079 1.00 67.02  ? 319 ASN   B OD1 1 
ATOM   5514 N ND2 . ASN   B 1 319 ? 22.573  12.257  65.165 1.00 59.66  ? 319 ASN   B ND2 1 
ATOM   5515 N N   . ASP   B 1 320 ? 18.490  11.012  61.723 1.00 65.39  ? 320 ASP   B N   1 
ATOM   5516 C CA  . ASP   B 1 320 ? 17.230  11.607  61.301 1.00 59.26  ? 320 ASP   B CA  1 
ATOM   5517 C C   . ASP   B 1 320 ? 16.710  10.793  60.127 1.00 57.40  ? 320 ASP   B C   1 
ATOM   5518 O O   . ASP   B 1 320 ? 17.491  10.205  59.378 1.00 75.56  ? 320 ASP   B O   1 
ATOM   5519 C CB  . ASP   B 1 320 ? 17.388  13.083  60.923 1.00 58.68  ? 320 ASP   B CB  1 
ATOM   5520 C CG  . ASP   B 1 320 ? 16.101  13.865  61.090 1.00 83.43  ? 320 ASP   B CG  1 
ATOM   5521 O OD1 . ASP   B 1 320 ? 15.037  13.233  61.266 1.00 78.25  ? 320 ASP   B OD1 1 
ATOM   5522 O OD2 . ASP   B 1 320 ? 16.153  15.112  61.048 1.00 77.87  ? 320 ASP   B OD2 1 
ATOM   5523 N N   . GLY   B 1 321 ? 15.390  10.736  59.984 1.00 55.86  ? 321 GLY   B N   1 
ATOM   5524 C CA  . GLY   B 1 321 ? 14.823  9.846   58.989 1.00 55.67  ? 321 GLY   B CA  1 
ATOM   5525 C C   . GLY   B 1 321 ? 13.512  10.293  58.380 1.00 53.05  ? 321 GLY   B C   1 
ATOM   5526 O O   . GLY   B 1 321 ? 13.114  11.454  58.517 1.00 52.64  ? 321 GLY   B O   1 
ATOM   5527 N N   . VAL   B 1 322 ? 12.841  9.369   57.684 1.00 53.12  ? 322 VAL   B N   1 
ATOM   5528 C CA  . VAL   B 1 322 ? 11.618  9.704   56.964 1.00 52.77  ? 322 VAL   B CA  1 
ATOM   5529 C C   . VAL   B 1 322 ? 10.475  10.048  57.907 1.00 47.62  ? 322 VAL   B C   1 
ATOM   5530 O O   . VAL   B 1 322 ? 9.498   10.670  57.483 1.00 48.83  ? 322 VAL   B O   1 
ATOM   5531 C CB  . VAL   B 1 322 ? 11.195  8.560   56.024 1.00 48.68  ? 322 VAL   B CB  1 
ATOM   5532 C CG1 . VAL   B 1 322 ? 12.308  8.239   55.044 1.00 52.00  ? 322 VAL   B CG1 1 
ATOM   5533 C CG2 . VAL   B 1 322 ? 10.789  7.332   56.820 1.00 63.22  ? 322 VAL   B CG2 1 
ATOM   5534 N N   . TYR   B 1 323 ? 10.542  9.627   59.168 1.00 47.78  ? 323 TYR   B N   1 
ATOM   5535 C CA  . TYR   B 1 323 ? 9.559   10.089  60.137 1.00 49.36  ? 323 TYR   B CA  1 
ATOM   5536 C C   . TYR   B 1 323 ? 9.901   11.465  60.688 1.00 47.22  ? 323 TYR   B C   1 
ATOM   5537 O O   . TYR   B 1 323 ? 9.032   12.123  61.269 1.00 49.19  ? 323 TYR   B O   1 
ATOM   5538 C CB  . TYR   B 1 323 ? 9.425   9.085   61.283 1.00 57.01  ? 323 TYR   B CB  1 
ATOM   5539 C CG  . TYR   B 1 323 ? 8.794   7.775   60.871 1.00 51.35  ? 323 TYR   B CG  1 
ATOM   5540 C CD1 . TYR   B 1 323 ? 9.576   6.692   60.487 1.00 61.55  ? 323 TYR   B CD1 1 
ATOM   5541 C CD2 . TYR   B 1 323 ? 7.415   7.625   60.856 1.00 49.27  ? 323 TYR   B CD2 1 
ATOM   5542 C CE1 . TYR   B 1 323 ? 9.000   5.493   60.111 1.00 54.69  ? 323 TYR   B CE1 1 
ATOM   5543 C CE2 . TYR   B 1 323 ? 6.830   6.434   60.479 1.00 52.20  ? 323 TYR   B CE2 1 
ATOM   5544 C CZ  . TYR   B 1 323 ? 7.626   5.372   60.108 1.00 67.48  ? 323 TYR   B CZ  1 
ATOM   5545 O OH  . TYR   B 1 323 ? 7.041   4.185   59.734 1.00 81.35  ? 323 TYR   B OH  1 
ATOM   5546 N N   . GLY   B 1 324 ? 11.142  11.909  60.516 1.00 51.83  ? 324 GLY   B N   1 
ATOM   5547 C CA  . GLY   B 1 324 ? 11.553  13.227  60.948 1.00 50.91  ? 324 GLY   B CA  1 
ATOM   5548 C C   . GLY   B 1 324 ? 11.637  14.229  59.817 1.00 59.53  ? 324 GLY   B C   1 
ATOM   5549 O O   . GLY   B 1 324 ? 10.664  14.446  59.088 1.00 66.32  ? 324 GLY   B O   1 
ATOM   5550 N N   . SER   B 1 325 ? 12.810  14.845  59.660 1.00 61.68  ? 325 SER   B N   1 
ATOM   5551 C CA  . SER   B 1 325 ? 12.974  15.913  58.680 1.00 50.49  ? 325 SER   B CA  1 
ATOM   5552 C C   . SER   B 1 325 ? 12.805  15.418  57.251 1.00 60.28  ? 325 SER   B C   1 
ATOM   5553 O O   . SER   B 1 325 ? 12.378  16.186  56.380 1.00 54.46  ? 325 SER   B O   1 
ATOM   5554 C CB  . SER   B 1 325 ? 14.344  16.559  58.845 1.00 62.46  ? 325 SER   B CB  1 
ATOM   5555 O OG  . SER   B 1 325 ? 14.498  17.080  60.154 1.00 57.66  ? 325 SER   B OG  1 
ATOM   5556 N N   . PHE   B 1 326 ? 13.133  14.155  56.986 1.00 56.48  ? 326 PHE   B N   1 
ATOM   5557 C CA  . PHE   B 1 326 ? 13.116  13.631  55.629 1.00 49.03  ? 326 PHE   B CA  1 
ATOM   5558 C C   . PHE   B 1 326 ? 11.750  13.105  55.210 1.00 56.61  ? 326 PHE   B C   1 
ATOM   5559 O O   . PHE   B 1 326 ? 11.645  12.441  54.168 1.00 53.96  ? 326 PHE   B O   1 
ATOM   5560 C CB  . PHE   B 1 326 ? 14.184  12.547  55.478 1.00 43.53  ? 326 PHE   B CB  1 
ATOM   5561 C CG  . PHE   B 1 326 ? 15.582  13.081  55.555 1.00 56.92  ? 326 PHE   B CG  1 
ATOM   5562 C CD1 . PHE   B 1 326 ? 16.167  13.685  54.454 1.00 58.51  ? 326 PHE   B CD1 1 
ATOM   5563 C CD2 . PHE   B 1 326 ? 16.302  13.005  56.735 1.00 58.69  ? 326 PHE   B CD2 1 
ATOM   5564 C CE1 . PHE   B 1 326 ? 17.451  14.189  54.524 1.00 45.45  ? 326 PHE   B CE1 1 
ATOM   5565 C CE2 . PHE   B 1 326 ? 17.583  13.506  56.812 1.00 58.10  ? 326 PHE   B CE2 1 
ATOM   5566 C CZ  . PHE   B 1 326 ? 18.160  14.099  55.705 1.00 55.22  ? 326 PHE   B CZ  1 
ATOM   5567 N N   . ASN   B 1 327 ? 10.694  13.426  55.966 1.00 53.95  ? 327 ASN   B N   1 
ATOM   5568 C CA  . ASN   B 1 327 ? 9.353   13.039  55.549 1.00 54.05  ? 327 ASN   B CA  1 
ATOM   5569 C C   . ASN   B 1 327 ? 8.998   13.657  54.210 1.00 51.01  ? 327 ASN   B C   1 
ATOM   5570 O O   . ASN   B 1 327 ? 8.093   13.165  53.521 1.00 61.92  ? 327 ASN   B O   1 
ATOM   5571 C CB  . ASN   B 1 327 ? 8.336   13.464  56.613 1.00 53.04  ? 327 ASN   B CB  1 
ATOM   5572 C CG  . ASN   B 1 327 ? 8.287   14.969  56.803 1.00 52.85  ? 327 ASN   B CG  1 
ATOM   5573 O OD1 . ASN   B 1 327 ? 7.775   15.698  55.955 1.00 53.97  ? 327 ASN   B OD1 1 
ATOM   5574 N ND2 . ASN   B 1 327 ? 8.838   15.442  57.915 1.00 50.52  ? 327 ASN   B ND2 1 
ATOM   5575 N N   . CYS   B 1 328 ? 9.778   14.652  53.789 1.00 49.32  ? 328 CYS   B N   1 
ATOM   5576 C CA  . CYS   B 1 328 ? 9.547   15.318  52.519 1.00 61.46  ? 328 CYS   B CA  1 
ATOM   5577 C C   . CYS   B 1 328 ? 9.725   14.355  51.360 1.00 63.27  ? 328 CYS   B C   1 
ATOM   5578 O O   . CYS   B 1 328 ? 9.148   14.566  50.289 1.00 65.12  ? 328 CYS   B O   1 
ATOM   5579 C CB  . CYS   B 1 328 ? 10.482  16.520  52.392 1.00 55.78  ? 328 CYS   B CB  1 
ATOM   5580 S SG  . CYS   B 1 328 ? 12.222  16.101  52.630 1.00 67.96  ? 328 CYS   B SG  1 
ATOM   5581 N N   . ILE   B 1 329 ? 10.538  13.310  51.537 1.00 55.52  ? 329 ILE   B N   1 
ATOM   5582 C CA  . ILE   B 1 329 ? 10.699  12.334  50.463 1.00 56.77  ? 329 ILE   B CA  1 
ATOM   5583 C C   . ILE   B 1 329 ? 9.356   11.697  50.135 1.00 60.24  ? 329 ILE   B C   1 
ATOM   5584 O O   . ILE   B 1 329 ? 8.981   11.561  48.963 1.00 67.23  ? 329 ILE   B O   1 
ATOM   5585 C CB  . ILE   B 1 329 ? 11.739  11.267  50.850 1.00 48.50  ? 329 ILE   B CB  1 
ATOM   5586 C CG1 . ILE   B 1 329 ? 13.108  11.897  51.093 1.00 47.91  ? 329 ILE   B CG1 1 
ATOM   5587 C CG2 . ILE   B 1 329 ? 11.831  10.187  49.785 1.00 67.51  ? 329 ILE   B CG2 1 
ATOM   5588 C CD1 . ILE   B 1 329 ? 14.148  10.896  51.532 1.00 54.32  ? 329 ILE   B CD1 1 
ATOM   5589 N N   . LEU   B 1 330 ? 8.608   11.300  51.169 1.00 62.83  ? 330 LEU   B N   1 
ATOM   5590 C CA  . LEU   B 1 330 ? 7.308   10.673  50.950 1.00 66.42  ? 330 LEU   B CA  1 
ATOM   5591 C C   . LEU   B 1 330 ? 6.227   11.691  50.595 1.00 61.48  ? 330 LEU   B C   1 
ATOM   5592 O O   . LEU   B 1 330 ? 5.418   11.451  49.690 1.00 73.75  ? 330 LEU   B O   1 
ATOM   5593 C CB  . LEU   B 1 330 ? 6.910   9.857   52.180 1.00 62.61  ? 330 LEU   B CB  1 
ATOM   5594 C CG  . LEU   B 1 330 ? 7.939   8.781   52.537 1.00 64.20  ? 330 LEU   B CG  1 
ATOM   5595 C CD1 . LEU   B 1 330 ? 7.431   7.906   53.667 1.00 58.80  ? 330 LEU   B CD1 1 
ATOM   5596 C CD2 . LEU   B 1 330 ? 8.303   7.934   51.321 1.00 64.67  ? 330 LEU   B CD2 1 
ATOM   5597 N N   . TYR   B 1 331 ? 6.199   12.831  51.288 1.00 57.49  ? 331 TYR   B N   1 
ATOM   5598 C CA  . TYR   B 1 331 ? 5.122   13.805  51.132 1.00 62.92  ? 331 TYR   B CA  1 
ATOM   5599 C C   . TYR   B 1 331 ? 5.392   14.854  50.056 1.00 63.59  ? 331 TYR   B C   1 
ATOM   5600 O O   . TYR   B 1 331 ? 4.511   15.143  49.243 1.00 84.74  ? 331 TYR   B O   1 
ATOM   5601 C CB  . TYR   B 1 331 ? 4.873   14.525  52.460 1.00 65.97  ? 331 TYR   B CB  1 
ATOM   5602 C CG  . TYR   B 1 331 ? 4.158   13.712  53.514 1.00 55.29  ? 331 TYR   B CG  1 
ATOM   5603 C CD1 . TYR   B 1 331 ? 2.829   13.344  53.355 1.00 68.31  ? 331 TYR   B CD1 1 
ATOM   5604 C CD2 . TYR   B 1 331 ? 4.813   13.315  54.670 1.00 61.61  ? 331 TYR   B CD2 1 
ATOM   5605 C CE1 . TYR   B 1 331 ? 2.171   12.603  54.320 1.00 66.88  ? 331 TYR   B CE1 1 
ATOM   5606 C CE2 . TYR   B 1 331 ? 4.165   12.572  55.642 1.00 70.14  ? 331 TYR   B CE2 1 
ATOM   5607 C CZ  . TYR   B 1 331 ? 2.844   12.218  55.461 1.00 69.94  ? 331 TYR   B CZ  1 
ATOM   5608 O OH  . TYR   B 1 331 ? 2.191   11.481  56.422 1.00 71.52  ? 331 TYR   B OH  1 
ATOM   5609 N N   . ASP   B 1 332 ? 6.591   15.430  50.041 1.00 63.47  ? 332 ASP   B N   1 
ATOM   5610 C CA  . ASP   B 1 332 ? 6.907   16.553  49.166 1.00 68.36  ? 332 ASP   B CA  1 
ATOM   5611 C C   . ASP   B 1 332 ? 7.610   16.142  47.872 1.00 74.55  ? 332 ASP   B C   1 
ATOM   5612 O O   . ASP   B 1 332 ? 7.930   17.010  47.052 1.00 73.48  ? 332 ASP   B O   1 
ATOM   5613 C CB  . ASP   B 1 332 ? 7.757   17.568  49.954 1.00 67.01  ? 332 ASP   B CB  1 
ATOM   5614 C CG  . ASP   B 1 332 ? 8.098   18.811  49.162 1.00 73.09  ? 332 ASP   B CG  1 
ATOM   5615 O OD1 . ASP   B 1 332 ? 7.168   19.570  48.823 1.00 67.17  ? 332 ASP   B OD1 1 
ATOM   5616 O OD2 . ASP   B 1 332 ? 9.295   19.036  48.889 1.00 91.32  ? 332 ASP   B OD2 1 
ATOM   5617 N N   . HIS   B 1 333 ? 7.830   14.843  47.655 1.00 72.88  ? 333 HIS   B N   1 
ATOM   5618 C CA  . HIS   B 1 333 ? 8.545   14.343  46.476 1.00 86.98  ? 333 HIS   B CA  1 
ATOM   5619 C C   . HIS   B 1 333 ? 9.908   15.021  46.338 1.00 76.51  ? 333 HIS   B C   1 
ATOM   5620 O O   . HIS   B 1 333 ? 10.309  15.460  45.258 1.00 75.55  ? 333 HIS   B O   1 
ATOM   5621 C CB  . HIS   B 1 333 ? 7.718   14.529  45.200 1.00 76.21  ? 333 HIS   B CB  1 
ATOM   5622 C CG  . HIS   B 1 333 ? 6.290   14.107  45.333 1.00 98.09  ? 333 HIS   B CG  1 
ATOM   5623 N ND1 . HIS   B 1 333 ? 5.917   12.796  45.536 1.00 110.00 ? 333 HIS   B ND1 1 
ATOM   5624 C CD2 . HIS   B 1 333 ? 5.141   14.823  45.284 1.00 84.94  ? 333 HIS   B CD2 1 
ATOM   5625 C CE1 . HIS   B 1 333 ? 4.600   12.723  45.610 1.00 112.37 ? 333 HIS   B CE1 1 
ATOM   5626 N NE2 . HIS   B 1 333 ? 4.105   13.939  45.460 1.00 107.32 ? 333 HIS   B NE2 1 
ATOM   5627 N N   . ALA   B 1 334 ? 10.627  15.104  47.455 1.00 73.31  ? 334 ALA   B N   1 
ATOM   5628 C CA  . ALA   B 1 334 ? 11.911  15.788  47.505 1.00 73.10  ? 334 ALA   B CA  1 
ATOM   5629 C C   . ALA   B 1 334 ? 13.059  14.804  47.336 1.00 68.18  ? 334 ALA   B C   1 
ATOM   5630 O O   . ALA   B 1 334 ? 13.049  13.716  47.917 1.00 69.56  ? 334 ALA   B O   1 
ATOM   5631 C CB  . ALA   B 1 334 ? 12.069  16.546  48.824 1.00 75.82  ? 334 ALA   B CB  1 
ATOM   5632 N N   . HIS   B 1 335 ? 14.035  15.187  46.511 1.00 79.12  ? 335 HIS   B N   1 
ATOM   5633 C CA  . HIS   B 1 335 ? 15.257  14.420  46.300 1.00 69.79  ? 335 HIS   B CA  1 
ATOM   5634 C C   . HIS   B 1 335 ? 16.373  15.086  47.093 1.00 57.23  ? 335 HIS   B C   1 
ATOM   5635 O O   . HIS   B 1 335 ? 16.669  16.268  46.884 1.00 67.42  ? 335 HIS   B O   1 
ATOM   5636 C CB  . HIS   B 1 335 ? 15.594  14.329  44.813 1.00 82.90  ? 335 HIS   B CB  1 
ATOM   5637 C CG  . HIS   B 1 335 ? 14.427  13.930  43.967 1.00 80.76  ? 335 HIS   B CG  1 
ATOM   5638 N ND1 . HIS   B 1 335 ? 13.980  12.628  43.890 1.00 84.39  ? 335 HIS   B ND1 1 
ATOM   5639 C CD2 . HIS   B 1 335 ? 13.598  14.660  43.186 1.00 76.78  ? 335 HIS   B CD2 1 
ATOM   5640 C CE1 . HIS   B 1 335 ? 12.933  12.573  43.087 1.00 82.20  ? 335 HIS   B CE1 1 
ATOM   5641 N NE2 . HIS   B 1 335 ? 12.681  13.792  42.646 1.00 88.18  ? 335 HIS   B NE2 1 
ATOM   5642 N N   . VAL   B 1 336 ? 16.993  14.332  47.994 1.00 62.64  ? 336 VAL   B N   1 
ATOM   5643 C CA  . VAL   B 1 336 ? 17.998  14.864  48.909 1.00 64.65  ? 336 VAL   B CA  1 
ATOM   5644 C C   . VAL   B 1 336 ? 19.387  14.473  48.427 1.00 63.46  ? 336 VAL   B C   1 
ATOM   5645 O O   . VAL   B 1 336 ? 19.608  13.345  47.962 1.00 54.13  ? 336 VAL   B O   1 
ATOM   5646 C CB  . VAL   B 1 336 ? 17.751  14.374  50.349 1.00 58.22  ? 336 VAL   B CB  1 
ATOM   5647 C CG1 . VAL   B 1 336 ? 16.490  15.012  50.914 1.00 43.60  ? 336 VAL   B CG1 1 
ATOM   5648 C CG2 . VAL   B 1 336 ? 17.655  12.860  50.390 1.00 52.24  ? 336 VAL   B CG2 1 
ATOM   5649 N N   . LYS   B 1 337 ? 20.322  15.418  48.516 1.00 69.30  ? 337 LYS   B N   1 
ATOM   5650 C CA  . LYS   B 1 337 ? 21.706  15.182  48.125 1.00 66.78  ? 337 LYS   B CA  1 
ATOM   5651 C C   . LYS   B 1 337 ? 22.605  15.266  49.351 1.00 67.17  ? 337 LYS   B C   1 
ATOM   5652 O O   . LYS   B 1 337 ? 22.787  16.363  49.902 1.00 61.73  ? 337 LYS   B O   1 
ATOM   5653 C CB  . LYS   B 1 337 ? 22.142  16.210  47.080 1.00 72.98  ? 337 LYS   B CB  1 
ATOM   5654 C CG  . LYS   B 1 337 ? 21.139  16.419  45.959 1.00 78.38  ? 337 LYS   B CG  1 
ATOM   5655 C CD  . LYS   B 1 337 ? 21.645  17.456  44.968 1.00 103.22 ? 337 LYS   B CD  1 
ATOM   5656 C CE  . LYS   B 1 337 ? 20.675  17.649  43.813 1.00 107.41 ? 337 LYS   B CE  1 
ATOM   5657 N NZ  . LYS   B 1 337 ? 21.242  18.534  42.757 1.00 98.60  ? 337 LYS   B NZ  1 
ATOM   5658 N N   . PRO   B 1 338 ? 23.172  14.156  49.824 1.00 53.58  ? 338 PRO   B N   1 
ATOM   5659 C CA  . PRO   B 1 338 ? 24.058  14.227  50.992 1.00 49.05  ? 338 PRO   B CA  1 
ATOM   5660 C C   . PRO   B 1 338 ? 25.364  14.926  50.648 1.00 53.04  ? 338 PRO   B C   1 
ATOM   5661 O O   . PRO   B 1 338 ? 25.942  14.714  49.579 1.00 60.97  ? 338 PRO   B O   1 
ATOM   5662 C CB  . PRO   B 1 338 ? 24.283  12.755  51.358 1.00 41.95  ? 338 PRO   B CB  1 
ATOM   5663 C CG  . PRO   B 1 338 ? 24.066  12.019  50.078 1.00 56.58  ? 338 PRO   B CG  1 
ATOM   5664 C CD  . PRO   B 1 338 ? 23.005  12.778  49.333 1.00 53.03  ? 338 PRO   B CD  1 
ATOM   5665 N N   . LEU   B 1 339 ? 25.833  15.759  51.570 1.00 62.17  ? 339 LEU   B N   1 
ATOM   5666 C CA  . LEU   B 1 339 ? 27.061  16.521  51.394 1.00 60.45  ? 339 LEU   B CA  1 
ATOM   5667 C C   . LEU   B 1 339 ? 28.037  16.217  52.519 1.00 72.27  ? 339 LEU   B C   1 
ATOM   5668 O O   . LEU   B 1 339 ? 27.637  16.035  53.675 1.00 66.99  ? 339 LEU   B O   1 
ATOM   5669 C CB  . LEU   B 1 339 ? 26.782  18.027  51.340 1.00 58.13  ? 339 LEU   B CB  1 
ATOM   5670 C CG  . LEU   B 1 339 ? 25.934  18.488  50.156 1.00 59.86  ? 339 LEU   B CG  1 
ATOM   5671 C CD1 . LEU   B 1 339 ? 25.686  19.982  50.235 1.00 71.46  ? 339 LEU   B CD1 1 
ATOM   5672 C CD2 . LEU   B 1 339 ? 26.608  18.118  48.844 1.00 47.61  ? 339 LEU   B CD2 1 
ATOM   5673 N N   . LEU   B 1 340 ? 29.318  16.160  52.167 1.00 66.58  ? 340 LEU   B N   1 
ATOM   5674 C CA  . LEU   B 1 340 ? 30.377  15.901  53.129 1.00 57.37  ? 340 LEU   B CA  1 
ATOM   5675 C C   . LEU   B 1 340 ? 30.876  17.212  53.723 1.00 82.73  ? 340 LEU   B C   1 
ATOM   5676 O O   . LEU   B 1 340 ? 30.923  18.240  53.038 1.00 77.75  ? 340 LEU   B O   1 
ATOM   5677 C CB  . LEU   B 1 340 ? 31.526  15.150  52.462 1.00 72.41  ? 340 LEU   B CB  1 
ATOM   5678 C CG  . LEU   B 1 340 ? 31.151  13.726  52.058 1.00 76.12  ? 340 LEU   B CG  1 
ATOM   5679 C CD1 . LEU   B 1 340 ? 32.264  13.081  51.276 1.00 82.38  ? 340 LEU   B CD1 1 
ATOM   5680 C CD2 . LEU   B 1 340 ? 30.806  12.910  53.282 1.00 78.20  ? 340 LEU   B CD2 1 
ATOM   5681 N N   . GLN   B 1 341 ? 31.228  17.174  55.011 1.00 84.93  ? 341 GLN   B N   1 
ATOM   5682 C CA  . GLN   B 1 341 ? 31.711  18.377  55.683 1.00 87.15  ? 341 GLN   B CA  1 
ATOM   5683 C C   . GLN   B 1 341 ? 32.958  18.928  54.997 1.00 95.02  ? 341 GLN   B C   1 
ATOM   5684 O O   . GLN   B 1 341 ? 33.068  20.138  54.775 1.00 99.66  ? 341 GLN   B O   1 
ATOM   5685 C CB  . GLN   B 1 341 ? 31.987  18.077  57.157 1.00 83.02  ? 341 GLN   B CB  1 
ATOM   5686 C CG  . GLN   B 1 341 ? 32.508  19.262  57.961 1.00 85.87  ? 341 GLN   B CG  1 
ATOM   5687 C CD  . GLN   B 1 341 ? 32.990  18.866  59.343 1.00 100.52 ? 341 GLN   B CD  1 
ATOM   5688 O OE1 . GLN   B 1 341 ? 33.002  17.686  59.696 1.00 88.74  ? 341 GLN   B OE1 1 
ATOM   5689 N NE2 . GLN   B 1 341 ? 33.390  19.854  60.134 1.00 96.11  ? 341 GLN   B NE2 1 
ATOM   5690 N N   . LYS   B 1 342 ? 33.906  18.056  54.661 1.00 99.94  ? 342 LYS   B N   1 
ATOM   5691 C CA  . LYS   B 1 342 ? 35.132  18.427  53.966 1.00 101.79 ? 342 LYS   B CA  1 
ATOM   5692 C C   . LYS   B 1 342 ? 35.112  17.854  52.554 1.00 93.22  ? 342 LYS   B C   1 
ATOM   5693 O O   . LYS   B 1 342 ? 34.789  16.678  52.362 1.00 90.30  ? 342 LYS   B O   1 
ATOM   5694 C CB  . LYS   B 1 342 ? 36.369  17.937  54.725 1.00 116.35 ? 342 LYS   B CB  1 
ATOM   5695 C CG  . LYS   B 1 342 ? 37.662  18.086  53.943 1.00 111.75 ? 342 LYS   B CG  1 
ATOM   5696 C CD  . LYS   B 1 342 ? 38.836  17.495  54.701 1.00 122.86 ? 342 LYS   B CD  1 
ATOM   5697 C CE  . LYS   B 1 342 ? 40.085  17.438  53.835 1.00 126.84 ? 342 LYS   B CE  1 
ATOM   5698 N NZ  . LYS   B 1 342 ? 41.204  16.740  54.528 1.00 105.99 ? 342 LYS   B NZ  1 
ATOM   5699 N N   . ARG   B 1 343 ? 35.444  18.686  51.571 1.00 96.13  ? 343 ARG   B N   1 
ATOM   5700 C CA  . ARG   B 1 343 ? 35.433  18.250  50.177 1.00 95.34  ? 343 ARG   B CA  1 
ATOM   5701 C C   . ARG   B 1 343 ? 36.427  17.106  49.968 1.00 108.92 ? 343 ARG   B C   1 
ATOM   5702 O O   . ARG   B 1 343 ? 37.594  17.223  50.364 1.00 119.89 ? 343 ARG   B O   1 
ATOM   5703 C CB  . ARG   B 1 343 ? 35.766  19.415  49.247 1.00 96.71  ? 343 ARG   B CB  1 
ATOM   5704 C CG  . ARG   B 1 343 ? 35.612  19.088  47.769 1.00 107.42 ? 343 ARG   B CG  1 
ATOM   5705 C CD  . ARG   B 1 343 ? 36.074  20.236  46.885 1.00 109.90 ? 343 ARG   B CD  1 
ATOM   5706 N NE  . ARG   B 1 343 ? 35.626  20.077  45.503 1.00 121.37 ? 343 ARG   B NE  1 
ATOM   5707 C CZ  . ARG   B 1 343 ? 36.351  19.528  44.535 1.00 114.94 ? 343 ARG   B CZ  1 
ATOM   5708 N NH1 . ARG   B 1 343 ? 37.569  19.074  44.789 1.00 112.90 ? 343 ARG   B NH1 1 
ATOM   5709 N NH2 . ARG   B 1 343 ? 35.855  19.432  43.310 1.00 102.38 ? 343 ARG   B NH2 1 
ATOM   5710 N N   . PRO   B 1 344 ? 36.006  15.997  49.362 1.00 114.86 ? 344 PRO   B N   1 
ATOM   5711 C CA  . PRO   B 1 344 ? 36.902  14.848  49.171 1.00 117.36 ? 344 PRO   B CA  1 
ATOM   5712 C C   . PRO   B 1 344 ? 37.966  15.060  48.103 1.00 122.81 ? 344 PRO   B C   1 
ATOM   5713 O O   . PRO   B 1 344 ? 37.791  15.820  47.147 1.00 117.57 ? 344 PRO   B O   1 
ATOM   5714 C CB  . PRO   B 1 344 ? 35.944  13.721  48.752 1.00 109.16 ? 344 PRO   B CB  1 
ATOM   5715 C CG  . PRO   B 1 344 ? 34.577  14.234  49.074 1.00 99.97  ? 344 PRO   B CG  1 
ATOM   5716 C CD  . PRO   B 1 344 ? 34.658  15.703  48.858 1.00 111.59 ? 344 PRO   B CD  1 
ATOM   5717 N N   . LYS   B 1 345 ? 39.084  14.357  48.285 1.00 129.76 ? 345 LYS   B N   1 
ATOM   5718 C CA  . LYS   B 1 345 ? 40.190  14.406  47.340 1.00 119.85 ? 345 LYS   B CA  1 
ATOM   5719 C C   . LYS   B 1 345 ? 39.762  13.781  46.013 1.00 120.18 ? 345 LYS   B C   1 
ATOM   5720 O O   . LYS   B 1 345 ? 38.921  12.878  45.989 1.00 125.72 ? 345 LYS   B O   1 
ATOM   5721 C CB  . LYS   B 1 345 ? 41.386  13.628  47.881 1.00 104.68 ? 345 LYS   B CB  1 
ATOM   5722 C CG  . LYS   B 1 345 ? 41.365  13.404  49.383 1.00 107.43 ? 345 LYS   B CG  1 
ATOM   5723 C CD  . LYS   B 1 345 ? 42.166  12.160  49.761 1.00 111.90 ? 345 LYS   B CD  1 
ATOM   5724 C CE  . LYS   B 1 345 ? 41.907  11.729  51.202 1.00 97.53  ? 345 LYS   B CE  1 
ATOM   5725 N NZ  . LYS   B 1 345 ? 42.493  10.388  51.493 1.00 81.63  ? 345 LYS   B NZ  1 
ATOM   5726 N N   . PRO   B 1 346 ? 40.319  14.249  44.890 1.00 115.17 ? 346 PRO   B N   1 
ATOM   5727 C CA  . PRO   B 1 346 ? 39.921  13.668  43.593 1.00 115.63 ? 346 PRO   B CA  1 
ATOM   5728 C C   . PRO   B 1 346 ? 40.258  12.192  43.474 1.00 119.96 ? 346 PRO   B C   1 
ATOM   5729 O O   . PRO   B 1 346 ? 39.488  11.421  42.886 1.00 108.67 ? 346 PRO   B O   1 
ATOM   5730 C CB  . PRO   B 1 346 ? 40.698  14.516  42.574 1.00 107.78 ? 346 PRO   B CB  1 
ATOM   5731 C CG  . PRO   B 1 346 ? 41.820  15.131  43.357 1.00 120.44 ? 346 PRO   B CG  1 
ATOM   5732 C CD  . PRO   B 1 346 ? 41.305  15.331  44.743 1.00 108.94 ? 346 PRO   B CD  1 
ATOM   5733 N N   . ASP   B 1 347 ? 41.404  11.778  44.014 1.00 121.82 ? 347 ASP   B N   1 
ATOM   5734 C CA  . ASP   B 1 347 ? 41.845  10.391  43.949 1.00 112.38 ? 347 ASP   B CA  1 
ATOM   5735 C C   . ASP   B 1 347 ? 41.190  9.504   44.998 1.00 108.00 ? 347 ASP   B C   1 
ATOM   5736 O O   . ASP   B 1 347 ? 41.386  8.284   44.955 1.00 119.93 ? 347 ASP   B O   1 
ATOM   5737 C CB  . ASP   B 1 347 ? 43.369  10.309  44.081 1.00 117.98 ? 347 ASP   B CB  1 
ATOM   5738 C CG  . ASP   B 1 347 ? 44.090  10.881  42.874 1.00 123.91 ? 347 ASP   B CG  1 
ATOM   5739 O OD1 . ASP   B 1 347 ? 43.436  11.569  42.064 1.00 131.35 ? 347 ASP   B OD1 1 
ATOM   5740 O OD2 . ASP   B 1 347 ? 45.307  10.639  42.734 1.00 123.36 ? 347 ASP   B OD2 1 
ATOM   5741 N N   . GLU   B 1 348 ? 40.446  10.077  45.945 1.00 110.42 ? 348 GLU   B N   1 
ATOM   5742 C CA  . GLU   B 1 348 ? 39.816  9.271   46.986 1.00 103.26 ? 348 GLU   B CA  1 
ATOM   5743 C C   . GLU   B 1 348 ? 38.813  8.302   46.374 1.00 101.20 ? 348 GLU   B C   1 
ATOM   5744 O O   . GLU   B 1 348 ? 38.044  8.663   45.479 1.00 95.44  ? 348 GLU   B O   1 
ATOM   5745 C CB  . GLU   B 1 348 ? 39.130  10.173  48.013 1.00 89.76  ? 348 GLU   B CB  1 
ATOM   5746 C CG  . GLU   B 1 348 ? 38.661  9.439   49.259 1.00 81.12  ? 348 GLU   B CG  1 
ATOM   5747 C CD  . GLU   B 1 348 ? 38.190  10.388  50.344 1.00 108.93 ? 348 GLU   B CD  1 
ATOM   5748 O OE1 . GLU   B 1 348 ? 37.671  9.910   51.374 1.00 106.99 ? 348 GLU   B OE1 1 
ATOM   5749 O OE2 . GLU   B 1 348 ? 38.285  11.618  50.142 1.00 121.27 ? 348 GLU   B OE2 1 
ATOM   5750 N N   . LYS   B 1 349 ? 38.827  7.061   46.859 1.00 93.39  ? 349 LYS   B N   1 
ATOM   5751 C CA  . LYS   B 1 349 ? 37.936  6.027   46.344 1.00 80.50  ? 349 LYS   B CA  1 
ATOM   5752 C C   . LYS   B 1 349 ? 36.512  6.215   46.852 1.00 82.13  ? 349 LYS   B C   1 
ATOM   5753 O O   . LYS   B 1 349 ? 36.287  6.495   48.033 1.00 76.14  ? 349 LYS   B O   1 
ATOM   5754 C CB  . LYS   B 1 349 ? 38.458  4.646   46.743 1.00 75.87  ? 349 LYS   B CB  1 
ATOM   5755 C CG  . LYS   B 1 349 ? 37.617  3.481   46.253 1.00 85.82  ? 349 LYS   B CG  1 
ATOM   5756 C CD  . LYS   B 1 349 ? 38.355  2.168   46.439 1.00 104.32 ? 349 LYS   B CD  1 
ATOM   5757 C CE  . LYS   B 1 349 ? 37.507  0.983   46.011 1.00 101.83 ? 349 LYS   B CE  1 
ATOM   5758 N NZ  . LYS   B 1 349 ? 36.943  1.153   44.647 1.00 100.10 ? 349 LYS   B NZ  1 
ATOM   5759 N N   . TYR   B 1 350 ? 35.548  6.053   45.946 1.00 86.66  ? 350 TYR   B N   1 
ATOM   5760 C CA  . TYR   B 1 350 ? 34.129  6.149   46.253 1.00 67.31  ? 350 TYR   B CA  1 
ATOM   5761 C C   . TYR   B 1 350 ? 33.490  4.765   46.215 1.00 70.36  ? 350 TYR   B C   1 
ATOM   5762 O O   . TYR   B 1 350 ? 33.961  3.863   45.516 1.00 83.22  ? 350 TYR   B O   1 
ATOM   5763 C CB  . TYR   B 1 350 ? 33.416  7.076   45.267 1.00 70.21  ? 350 TYR   B CB  1 
ATOM   5764 C CG  . TYR   B 1 350 ? 33.599  8.553   45.545 1.00 72.12  ? 350 TYR   B CG  1 
ATOM   5765 C CD1 . TYR   B 1 350 ? 32.527  9.340   45.945 1.00 76.46  ? 350 TYR   B CD1 1 
ATOM   5766 C CD2 . TYR   B 1 350 ? 34.836  9.164   45.386 1.00 79.61  ? 350 TYR   B CD2 1 
ATOM   5767 C CE1 . TYR   B 1 350 ? 32.684  10.691  46.194 1.00 75.08  ? 350 TYR   B CE1 1 
ATOM   5768 C CE2 . TYR   B 1 350 ? 35.002  10.514  45.631 1.00 82.56  ? 350 TYR   B CE2 1 
ATOM   5769 C CZ  . TYR   B 1 350 ? 33.923  11.272  46.034 1.00 75.57  ? 350 TYR   B CZ  1 
ATOM   5770 O OH  . TYR   B 1 350 ? 34.074  12.616  46.280 1.00 81.15  ? 350 TYR   B OH  1 
ATOM   5771 N N   . TYR   B 1 351 ? 32.409  4.606   46.977 1.00 65.40  ? 351 TYR   B N   1 
ATOM   5772 C CA  . TYR   B 1 351 ? 31.671  3.357   47.070 1.00 70.09  ? 351 TYR   B CA  1 
ATOM   5773 C C   . TYR   B 1 351 ? 30.178  3.600   46.932 1.00 67.78  ? 351 TYR   B C   1 
ATOM   5774 O O   . TYR   B 1 351 ? 29.672  4.689   47.228 1.00 77.71  ? 351 TYR   B O   1 
ATOM   5775 C CB  . TYR   B 1 351 ? 31.907  2.647   48.397 1.00 77.21  ? 351 TYR   B CB  1 
ATOM   5776 C CG  . TYR   B 1 351 ? 33.345  2.364   48.688 1.00 80.77  ? 351 TYR   B CG  1 
ATOM   5777 C CD1 . TYR   B 1 351 ? 33.914  1.150   48.338 1.00 87.24  ? 351 TYR   B CD1 1 
ATOM   5778 C CD2 . TYR   B 1 351 ? 34.135  3.307   49.321 1.00 79.00  ? 351 TYR   B CD2 1 
ATOM   5779 C CE1 . TYR   B 1 351 ? 35.228  0.887   48.609 1.00 95.97  ? 351 TYR   B CE1 1 
ATOM   5780 C CE2 . TYR   B 1 351 ? 35.449  3.056   49.593 1.00 79.53  ? 351 TYR   B CE2 1 
ATOM   5781 C CZ  . TYR   B 1 351 ? 35.989  1.847   49.236 1.00 88.84  ? 351 TYR   B CZ  1 
ATOM   5782 O OH  . TYR   B 1 351 ? 37.300  1.604   49.515 1.00 100.31 ? 351 TYR   B OH  1 
ATOM   5783 N N   . SER   B 1 352 ? 29.490  2.558   46.473 1.00 66.25  ? 352 SER   B N   1 
ATOM   5784 C CA  . SER   B 1 352 ? 28.037  2.532   46.490 1.00 68.81  ? 352 SER   B CA  1 
ATOM   5785 C C   . SER   B 1 352 ? 27.542  2.435   47.931 1.00 70.25  ? 352 SER   B C   1 
ATOM   5786 O O   . SER   B 1 352 ? 27.987  1.577   48.705 1.00 65.42  ? 352 SER   B O   1 
ATOM   5787 C CB  . SER   B 1 352 ? 27.527  1.353   45.663 1.00 62.44  ? 352 SER   B CB  1 
ATOM   5788 O OG  . SER   B 1 352 ? 26.115  1.355   45.580 1.00 81.59  ? 352 SER   B OG  1 
ATOM   5789 N N   . SER   B 1 353 ? 26.623  3.325   48.297 1.00 62.23  ? 353 SER   B N   1 
ATOM   5790 C CA  . SER   B 1 353 ? 26.194  3.448   49.679 1.00 67.78  ? 353 SER   B CA  1 
ATOM   5791 C C   . SER   B 1 353 ? 24.709  3.774   49.739 1.00 71.08  ? 353 SER   B C   1 
ATOM   5792 O O   . SER   B 1 353 ? 24.142  4.359   48.812 1.00 59.69  ? 353 SER   B O   1 
ATOM   5793 C CB  . SER   B 1 353 ? 26.999  4.530   50.414 1.00 63.05  ? 353 SER   B CB  1 
ATOM   5794 O OG  . SER   B 1 353 ? 28.377  4.201   50.444 1.00 86.19  ? 353 SER   B OG  1 
ATOM   5795 N N   . SER   B 1 354 ? 24.093  3.378   50.848 1.00 57.77  ? 354 SER   B N   1 
ATOM   5796 C CA  . SER   B 1 354 ? 22.713  3.710   51.172 1.00 52.83  ? 354 SER   B CA  1 
ATOM   5797 C C   . SER   B 1 354 ? 22.668  4.387   52.537 1.00 59.94  ? 354 SER   B C   1 
ATOM   5798 O O   . SER   B 1 354 ? 23.554  4.183   53.370 1.00 56.98  ? 354 SER   B O   1 
ATOM   5799 C CB  . SER   B 1 354 ? 21.823  2.460   51.157 1.00 49.27  ? 354 SER   B CB  1 
ATOM   5800 O OG  . SER   B 1 354 ? 22.304  1.468   52.048 1.00 54.28  ? 354 SER   B OG  1 
ATOM   5801 N N   . ILE   B 1 355 ? 21.652  5.228   52.750 1.00 59.18  ? 355 ILE   B N   1 
ATOM   5802 C CA  . ILE   B 1 355 ? 21.505  6.007   53.978 1.00 54.18  ? 355 ILE   B CA  1 
ATOM   5803 C C   . ILE   B 1 355 ? 20.149  5.690   54.606 1.00 54.13  ? 355 ILE   B C   1 
ATOM   5804 O O   . ILE   B 1 355 ? 19.121  5.724   53.921 1.00 53.77  ? 355 ILE   B O   1 
ATOM   5805 C CB  . ILE   B 1 355 ? 21.658  7.514   53.702 1.00 63.67  ? 355 ILE   B CB  1 
ATOM   5806 C CG1 . ILE   B 1 355 ? 22.939  7.775   52.899 1.00 58.34  ? 355 ILE   B CG1 1 
ATOM   5807 C CG2 . ILE   B 1 355 ? 21.687  8.293   55.001 1.00 61.02  ? 355 ILE   B CG2 1 
ATOM   5808 C CD1 . ILE   B 1 355 ? 23.158  9.224   52.526 1.00 52.46  ? 355 ILE   B CD1 1 
ATOM   5809 N N   . TRP   B 1 356 ? 20.150  5.390   55.911 1.00 53.79  ? 356 TRP   B N   1 
ATOM   5810 C CA  . TRP   B 1 356 ? 18.981  4.893   56.634 1.00 49.45  ? 356 TRP   B CA  1 
ATOM   5811 C C   . TRP   B 1 356 ? 18.720  5.741   57.879 1.00 46.66  ? 356 TRP   B C   1 
ATOM   5812 O O   . TRP   B 1 356 ? 19.631  6.369   58.430 1.00 66.38  ? 356 TRP   B O   1 
ATOM   5813 C CB  . TRP   B 1 356 ? 19.154  3.417   57.027 1.00 51.83  ? 356 TRP   B CB  1 
ATOM   5814 C CG  . TRP   B 1 356 ? 19.458  2.520   55.855 1.00 62.40  ? 356 TRP   B CG  1 
ATOM   5815 C CD1 . TRP   B 1 356 ? 20.668  2.362   55.237 1.00 61.49  ? 356 TRP   B CD1 1 
ATOM   5816 C CD2 . TRP   B 1 356 ? 18.541  1.665   55.161 1.00 70.08  ? 356 TRP   B CD2 1 
ATOM   5817 N NE1 . TRP   B 1 356 ? 20.559  1.462   54.204 1.00 66.45  ? 356 TRP   B NE1 1 
ATOM   5818 C CE2 . TRP   B 1 356 ? 19.264  1.020   54.136 1.00 63.51  ? 356 TRP   B CE2 1 
ATOM   5819 C CE3 . TRP   B 1 356 ? 17.180  1.382   55.307 1.00 64.72  ? 356 TRP   B CE3 1 
ATOM   5820 C CZ2 . TRP   B 1 356 ? 18.669  0.111   53.262 1.00 64.90  ? 356 TRP   B CZ2 1 
ATOM   5821 C CZ3 . TRP   B 1 356 ? 16.592  0.479   54.438 1.00 59.86  ? 356 TRP   B CZ3 1 
ATOM   5822 C CH2 . TRP   B 1 356 ? 17.336  -0.145  53.430 1.00 64.89  ? 356 TRP   B CH2 1 
ATOM   5823 N N   . GLY   B 1 357 ? 17.449  5.765   58.307 1.00 52.78  ? 357 GLY   B N   1 
ATOM   5824 C CA  . GLY   B 1 357 ? 17.017  6.524   59.470 1.00 41.29  ? 357 GLY   B CA  1 
ATOM   5825 C C   . GLY   B 1 357 ? 17.213  5.812   60.798 1.00 55.64  ? 357 GLY   B C   1 
ATOM   5826 O O   . GLY   B 1 357 ? 17.523  4.618   60.878 1.00 43.95  ? 357 GLY   B O   1 
ATOM   5827 N N   . PRO   B 1 358 ? 17.040  6.581   61.884 1.00 57.39  ? 358 PRO   B N   1 
ATOM   5828 C CA  . PRO   B 1 358 ? 17.169  6.032   63.256 1.00 43.67  ? 358 PRO   B CA  1 
ATOM   5829 C C   . PRO   B 1 358 ? 16.123  4.990   63.627 1.00 61.46  ? 358 PRO   B C   1 
ATOM   5830 O O   . PRO   B 1 358 ? 16.430  4.095   64.421 1.00 65.06  ? 358 PRO   B O   1 
ATOM   5831 C CB  . PRO   B 1 358 ? 17.025  7.287   64.129 1.00 55.89  ? 358 PRO   B CB  1 
ATOM   5832 C CG  . PRO   B 1 358 ? 16.162  8.191   63.258 1.00 59.92  ? 358 PRO   B CG  1 
ATOM   5833 C CD  . PRO   B 1 358 ? 16.799  8.027   61.927 1.00 54.65  ? 358 PRO   B CD  1 
ATOM   5834 N N   . THR   B 1 359 ? 14.903  5.100   63.098 1.00 58.12  ? 359 THR   B N   1 
ATOM   5835 C CA  . THR   B 1 359 ? 13.781  4.254   63.488 1.00 59.71  ? 359 THR   B CA  1 
ATOM   5836 C C   . THR   B 1 359 ? 13.950  2.811   63.017 1.00 56.15  ? 359 THR   B C   1 
ATOM   5837 O O   . THR   B 1 359 ? 14.675  2.514   62.066 1.00 61.15  ? 359 THR   B O   1 
ATOM   5838 C CB  . THR   B 1 359 ? 12.461  4.812   62.941 1.00 57.16  ? 359 THR   B CB  1 
ATOM   5839 O OG1 . THR   B 1 359 ? 12.416  4.630   61.521 1.00 55.06  ? 359 THR   B OG1 1 
ATOM   5840 C CG2 . THR   B 1 359 ? 12.334  6.282   63.267 1.00 58.13  ? 359 THR   B CG2 1 
ATOM   5841 N N   . CYS   B 1 360 ? 13.268  1.906   63.732 1.00 69.23  ? 360 CYS   B N   1 
ATOM   5842 C CA  . CYS   B 1 360 ? 13.293  0.481   63.422 1.00 82.11  ? 360 CYS   B CA  1 
ATOM   5843 C C   . CYS   B 1 360 ? 12.576  0.149   62.123 1.00 72.87  ? 360 CYS   B C   1 
ATOM   5844 O O   . CYS   B 1 360 ? 12.846  -0.908  61.538 1.00 91.34  ? 360 CYS   B O   1 
ATOM   5845 C CB  . CYS   B 1 360 ? 12.674  -0.326  64.566 1.00 67.65  ? 360 CYS   B CB  1 
ATOM   5846 S SG  . CYS   B 1 360 ? 13.616  -0.273  66.097 1.00 96.36  ? 360 CYS   B SG  1 
ATOM   5847 N N   . ASP   B 1 361 ? 11.659  1.005   61.668 1.00 69.37  ? 361 ASP   B N   1 
ATOM   5848 C CA  . ASP   B 1 361 ? 10.916  0.717   60.447 1.00 71.50  ? 361 ASP   B CA  1 
ATOM   5849 C C   . ASP   B 1 361 ? 11.880  0.550   59.278 1.00 73.54  ? 361 ASP   B C   1 
ATOM   5850 O O   . ASP   B 1 361 ? 12.798  1.354   59.095 1.00 76.00  ? 361 ASP   B O   1 
ATOM   5851 C CB  . ASP   B 1 361 ? 9.910   1.832   60.157 1.00 69.19  ? 361 ASP   B CB  1 
ATOM   5852 C CG  . ASP   B 1 361 ? 9.105   1.581   58.890 1.00 81.78  ? 361 ASP   B CG  1 
ATOM   5853 O OD1 . ASP   B 1 361 ? 9.066   0.427   58.417 1.00 83.11  ? 361 ASP   B OD1 1 
ATOM   5854 O OD2 . ASP   B 1 361 ? 8.512   2.546   58.363 1.00 95.07  ? 361 ASP   B OD2 1 
ATOM   5855 N N   . GLY   B 1 362 ? 11.664  -0.504  58.487 1.00 65.44  ? 362 GLY   B N   1 
ATOM   5856 C CA  . GLY   B 1 362 ? 12.537  -0.770  57.354 1.00 62.60  ? 362 GLY   B CA  1 
ATOM   5857 C C   . GLY   B 1 362 ? 12.446  0.275   56.258 1.00 67.77  ? 362 GLY   B C   1 
ATOM   5858 O O   . GLY   B 1 362 ? 13.451  0.603   55.622 1.00 90.55  ? 362 GLY   B O   1 
ATOM   5859 N N   . LEU   B 1 363 ? 11.248  0.813   56.020 1.00 58.20  ? 363 LEU   B N   1 
ATOM   5860 C CA  . LEU   B 1 363 ? 11.041  1.792   54.956 1.00 73.99  ? 363 LEU   B CA  1 
ATOM   5861 C C   . LEU   B 1 363 ? 11.701  3.139   55.254 1.00 63.33  ? 363 LEU   B C   1 
ATOM   5862 O O   . LEU   B 1 363 ? 11.664  4.031   54.400 1.00 71.63  ? 363 LEU   B O   1 
ATOM   5863 C CB  . LEU   B 1 363 ? 9.535   1.954   54.699 1.00 97.17  ? 363 LEU   B CB  1 
ATOM   5864 C CG  . LEU   B 1 363 ? 9.005   2.112   53.260 1.00 115.85 ? 363 LEU   B CG  1 
ATOM   5865 C CD1 . LEU   B 1 363 ? 7.498   1.917   53.248 1.00 114.14 ? 363 LEU   B CD1 1 
ATOM   5866 C CD2 . LEU   B 1 363 ? 9.364   3.450   52.606 1.00 92.43  ? 363 LEU   B CD2 1 
ATOM   5867 N N   . ASP   B 1 364 ? 12.319  3.309   56.426 1.00 64.79  ? 364 ASP   B N   1 
ATOM   5868 C CA  . ASP   B 1 364 ? 12.976  4.568   56.785 1.00 61.69  ? 364 ASP   B CA  1 
ATOM   5869 C C   . ASP   B 1 364 ? 14.370  4.603   56.161 1.00 66.66  ? 364 ASP   B C   1 
ATOM   5870 O O   . ASP   B 1 364 ? 15.392  4.402   56.822 1.00 56.41  ? 364 ASP   B O   1 
ATOM   5871 C CB  . ASP   B 1 364 ? 13.043  4.725   58.301 1.00 61.04  ? 364 ASP   B CB  1 
ATOM   5872 C CG  . ASP   B 1 364 ? 13.486  6.118   58.734 1.00 65.35  ? 364 ASP   B CG  1 
ATOM   5873 O OD1 . ASP   B 1 364 ? 14.052  6.866   57.909 1.00 56.73  ? 364 ASP   B OD1 1 
ATOM   5874 O OD2 . ASP   B 1 364 ? 13.273  6.464   59.915 1.00 61.36  ? 364 ASP   B OD2 1 
ATOM   5875 N N   . ARG   B 1 365 ? 14.403  4.857   54.851 1.00 55.95  ? 365 ARG   B N   1 
ATOM   5876 C CA  . ARG   B 1 365 ? 15.648  4.977   54.101 1.00 46.50  ? 365 ARG   B CA  1 
ATOM   5877 C C   . ARG   B 1 365 ? 15.695  6.347   53.435 1.00 38.97  ? 365 ARG   B C   1 
ATOM   5878 O O   . ARG   B 1 365 ? 14.805  6.684   52.650 1.00 58.10  ? 365 ARG   B O   1 
ATOM   5879 C CB  . ARG   B 1 365 ? 15.770  3.870   53.053 1.00 52.48  ? 365 ARG   B CB  1 
ATOM   5880 C CG  . ARG   B 1 365 ? 17.052  3.926   52.244 1.00 70.81  ? 365 ARG   B CG  1 
ATOM   5881 C CD  . ARG   B 1 365 ? 17.076  2.832   51.196 1.00 62.15  ? 365 ARG   B CD  1 
ATOM   5882 N NE  . ARG   B 1 365 ? 15.892  2.918   50.350 1.00 71.79  ? 365 ARG   B NE  1 
ATOM   5883 C CZ  . ARG   B 1 365 ? 15.498  1.962   49.518 1.00 82.71  ? 365 ARG   B CZ  1 
ATOM   5884 N NH1 . ARG   B 1 365 ? 16.198  0.842   49.423 1.00 79.74  ? 365 ARG   B NH1 1 
ATOM   5885 N NH2 . ARG   B 1 365 ? 14.405  2.124   48.785 1.00 73.94  ? 365 ARG   B NH2 1 
ATOM   5886 N N   . ILE   B 1 366 ? 16.722  7.134   53.757 1.00 53.36  ? 366 ILE   B N   1 
ATOM   5887 C CA  . ILE   B 1 366 ? 16.869  8.470   53.183 1.00 53.46  ? 366 ILE   B CA  1 
ATOM   5888 C C   . ILE   B 1 366 ? 17.366  8.409   51.743 1.00 50.74  ? 366 ILE   B C   1 
ATOM   5889 O O   . ILE   B 1 366 ? 16.852  9.114   50.868 1.00 57.63  ? 366 ILE   B O   1 
ATOM   5890 C CB  . ILE   B 1 366 ? 17.799  9.322   54.062 1.00 48.66  ? 366 ILE   B CB  1 
ATOM   5891 C CG1 . ILE   B 1 366 ? 17.182  9.511   55.444 1.00 43.72  ? 366 ILE   B CG1 1 
ATOM   5892 C CG2 . ILE   B 1 366 ? 18.086  10.663  53.403 1.00 54.01  ? 366 ILE   B CG2 1 
ATOM   5893 C CD1 . ILE   B 1 366 ? 18.197  9.810   56.483 1.00 69.12  ? 366 ILE   B CD1 1 
ATOM   5894 N N   . VAL   B 1 367 ? 18.374  7.582   51.468 1.00 53.34  ? 367 VAL   B N   1 
ATOM   5895 C CA  . VAL   B 1 367 ? 18.963  7.493   50.134 1.00 51.21  ? 367 VAL   B CA  1 
ATOM   5896 C C   . VAL   B 1 367 ? 19.175  6.026   49.794 1.00 56.76  ? 367 VAL   B C   1 
ATOM   5897 O O   . VAL   B 1 367 ? 19.758  5.278   50.586 1.00 56.01  ? 367 VAL   B O   1 
ATOM   5898 C CB  . VAL   B 1 367 ? 20.298  8.261   50.036 1.00 48.24  ? 367 VAL   B CB  1 
ATOM   5899 C CG1 . VAL   B 1 367 ? 20.955  8.018   48.688 1.00 51.86  ? 367 VAL   B CG1 1 
ATOM   5900 C CG2 . VAL   B 1 367 ? 20.089  9.753   50.260 1.00 48.30  ? 367 VAL   B CG2 1 
ATOM   5901 N N   . GLU   B 1 368 ? 18.715  5.619   48.608 1.00 61.89  ? 368 GLU   B N   1 
ATOM   5902 C CA  . GLU   B 1 368 ? 18.838  4.226   48.198 1.00 60.49  ? 368 GLU   B CA  1 
ATOM   5903 C C   . GLU   B 1 368 ? 20.258  3.897   47.756 1.00 70.79  ? 368 GLU   B C   1 
ATOM   5904 O O   . GLU   B 1 368 ? 20.827  2.887   48.183 1.00 72.08  ? 368 GLU   B O   1 
ATOM   5905 C CB  . GLU   B 1 368 ? 17.847  3.913   47.078 1.00 65.61  ? 368 GLU   B CB  1 
ATOM   5906 C CG  . GLU   B 1 368 ? 17.860  2.457   46.647 1.00 82.87  ? 368 GLU   B CG  1 
ATOM   5907 C CD  . GLU   B 1 368 ? 16.905  2.176   45.507 1.00 104.02 ? 368 GLU   B CD  1 
ATOM   5908 O OE1 . GLU   B 1 368 ? 16.359  3.142   44.932 1.00 102.46 ? 368 GLU   B OE1 1 
ATOM   5909 O OE2 . GLU   B 1 368 ? 16.703  0.986   45.184 1.00 106.98 ? 368 GLU   B OE2 1 
ATOM   5910 N N   . ARG   B 1 369 ? 20.841  4.726   46.892 1.00 67.92  ? 369 ARG   B N   1 
ATOM   5911 C CA  . ARG   B 1 369 ? 22.188  4.467   46.401 1.00 68.92  ? 369 ARG   B CA  1 
ATOM   5912 C C   . ARG   B 1 369 ? 22.842  5.766   45.955 1.00 80.30  ? 369 ARG   B C   1 
ATOM   5913 O O   . ARG   B 1 369 ? 22.233  6.558   45.230 1.00 71.92  ? 369 ARG   B O   1 
ATOM   5914 C CB  . ARG   B 1 369 ? 22.160  3.443   45.263 1.00 68.14  ? 369 ARG   B CB  1 
ATOM   5915 C CG  . ARG   B 1 369 ? 23.526  3.028   44.744 1.00 81.18  ? 369 ARG   B CG  1 
ATOM   5916 C CD  . ARG   B 1 369 ? 23.419  1.794   43.859 1.00 86.99  ? 369 ARG   B CD  1 
ATOM   5917 N NE  . ARG   B 1 369 ? 22.403  1.949   42.824 1.00 102.60 ? 369 ARG   B NE  1 
ATOM   5918 C CZ  . ARG   B 1 369 ? 21.201  1.384   42.880 1.00 106.39 ? 369 ARG   B CZ  1 
ATOM   5919 N NH1 . ARG   B 1 369 ? 20.326  1.581   41.905 1.00 105.91 ? 369 ARG   B NH1 1 
ATOM   5920 N NH2 . ARG   B 1 369 ? 20.877  0.617   43.913 1.00 89.46  ? 369 ARG   B NH2 1 
ATOM   5921 N N   . CYS   B 1 370 ? 24.079  5.975   46.402 1.00 69.73  ? 370 CYS   B N   1 
ATOM   5922 C CA  . CYS   B 1 370 ? 24.876  7.130   46.022 1.00 65.96  ? 370 CYS   B CA  1 
ATOM   5923 C C   . CYS   B 1 370 ? 26.343  6.744   46.141 1.00 81.65  ? 370 CYS   B C   1 
ATOM   5924 O O   . CYS   B 1 370 ? 26.684  5.672   46.645 1.00 77.51  ? 370 CYS   B O   1 
ATOM   5925 C CB  . CYS   B 1 370 ? 24.551  8.351   46.888 1.00 69.15  ? 370 CYS   B CB  1 
ATOM   5926 S SG  . CYS   B 1 370 ? 24.934  8.142   48.640 1.00 83.76  ? 370 CYS   B SG  1 
ATOM   5927 N N   . ASP   B 1 371 ? 27.217  7.620   45.659 1.00 80.19  ? 371 ASP   B N   1 
ATOM   5928 C CA  . ASP   B 1 371 ? 28.653  7.383   45.714 1.00 63.97  ? 371 ASP   B CA  1 
ATOM   5929 C C   . ASP   B 1 371 ? 29.259  8.238   46.818 1.00 68.80  ? 371 ASP   B C   1 
ATOM   5930 O O   . ASP   B 1 371 ? 29.186  9.471   46.766 1.00 71.09  ? 371 ASP   B O   1 
ATOM   5931 C CB  . ASP   B 1 371 ? 29.312  7.684   44.369 1.00 81.04  ? 371 ASP   B CB  1 
ATOM   5932 C CG  . ASP   B 1 371 ? 28.889  6.713   43.284 1.00 89.75  ? 371 ASP   B CG  1 
ATOM   5933 O OD1 . ASP   B 1 371 ? 28.856  5.494   43.558 1.00 83.56  ? 371 ASP   B OD1 1 
ATOM   5934 O OD2 . ASP   B 1 371 ? 28.598  7.165   42.157 1.00 90.17  ? 371 ASP   B OD2 1 
ATOM   5935 N N   . LEU   B 1 372 ? 29.858  7.583   47.807 1.00 74.81  ? 372 LEU   B N   1 
ATOM   5936 C CA  . LEU   B 1 372 ? 30.467  8.264   48.940 1.00 71.51  ? 372 LEU   B CA  1 
ATOM   5937 C C   . LEU   B 1 372 ? 31.778  7.582   49.289 1.00 68.73  ? 372 LEU   B C   1 
ATOM   5938 O O   . LEU   B 1 372 ? 31.904  6.365   49.131 1.00 71.44  ? 372 LEU   B O   1 
ATOM   5939 C CB  . LEU   B 1 372 ? 29.557  8.255   50.177 1.00 63.67  ? 372 LEU   B CB  1 
ATOM   5940 C CG  . LEU   B 1 372 ? 28.239  9.023   50.130 1.00 67.54  ? 372 LEU   B CG  1 
ATOM   5941 C CD1 . LEU   B 1 372 ? 27.447  8.770   51.404 1.00 55.36  ? 372 LEU   B CD1 1 
ATOM   5942 C CD2 . LEU   B 1 372 ? 28.501  10.507  49.936 1.00 57.47  ? 372 LEU   B CD2 1 
ATOM   5943 N N   . PRO   B 1 373 ? 32.770  8.333   49.755 1.00 67.04  ? 373 PRO   B N   1 
ATOM   5944 C CA  . PRO   B 1 373 ? 33.958  7.693   50.323 1.00 72.87  ? 373 PRO   B CA  1 
ATOM   5945 C C   . PRO   B 1 373 ? 33.607  6.973   51.615 1.00 70.71  ? 373 PRO   B C   1 
ATOM   5946 O O   . PRO   B 1 373 ? 32.569  7.222   52.234 1.00 68.04  ? 373 PRO   B O   1 
ATOM   5947 C CB  . PRO   B 1 373 ? 34.909  8.865   50.571 1.00 75.48  ? 373 PRO   B CB  1 
ATOM   5948 C CG  . PRO   B 1 373 ? 34.010  10.037  50.747 1.00 67.08  ? 373 PRO   B CG  1 
ATOM   5949 C CD  . PRO   B 1 373 ? 32.843  9.802   49.827 1.00 64.31  ? 373 PRO   B CD  1 
ATOM   5950 N N   . GLU   B 1 374 ? 34.481  6.047   52.007 1.00 73.55  ? 374 GLU   B N   1 
ATOM   5951 C CA  . GLU   B 1 374 ? 34.246  5.291   53.231 1.00 71.19  ? 374 GLU   B CA  1 
ATOM   5952 C C   . GLU   B 1 374 ? 34.250  6.221   54.434 1.00 68.06  ? 374 GLU   B C   1 
ATOM   5953 O O   . GLU   B 1 374 ? 35.249  6.892   54.716 1.00 80.27  ? 374 GLU   B O   1 
ATOM   5954 C CB  . GLU   B 1 374 ? 35.293  4.196   53.411 1.00 89.26  ? 374 GLU   B CB  1 
ATOM   5955 C CG  . GLU   B 1 374 ? 35.171  3.484   54.751 1.00 85.33  ? 374 GLU   B CG  1 
ATOM   5956 C CD  . GLU   B 1 374 ? 35.999  2.221   54.818 1.00 95.77  ? 374 GLU   B CD  1 
ATOM   5957 O OE1 . GLU   B 1 374 ? 36.799  1.984   53.889 1.00 95.73  ? 374 GLU   B OE1 1 
ATOM   5958 O OE2 . GLU   B 1 374 ? 35.844  1.461   55.797 1.00 88.72  ? 374 GLU   B OE2 1 
ATOM   5959 N N   . MET   B 1 375 ? 33.126  6.259   55.131 1.00 67.02  ? 375 MET   B N   1 
ATOM   5960 C CA  . MET   B 1 375 ? 32.915  7.088   56.305 1.00 69.39  ? 375 MET   B CA  1 
ATOM   5961 C C   . MET   B 1 375 ? 32.765  6.222   57.546 1.00 68.25  ? 375 MET   B C   1 
ATOM   5962 O O   . MET   B 1 375 ? 32.568  5.007   57.464 1.00 82.59  ? 375 MET   B O   1 
ATOM   5963 C CB  . MET   B 1 375 ? 31.691  7.969   56.081 1.00 73.93  ? 375 MET   B CB  1 
ATOM   5964 C CG  . MET   B 1 375 ? 31.850  8.826   54.851 1.00 72.62  ? 375 MET   B CG  1 
ATOM   5965 S SD  . MET   B 1 375 ? 30.367  9.784   54.603 1.00 106.11 ? 375 MET   B SD  1 
ATOM   5966 C CE  . MET   B 1 375 ? 29.184  8.440   54.687 1.00 108.52 ? 375 MET   B CE  1 
ATOM   5967 N N   . HIS   B 1 376 ? 32.850  6.869   58.706 1.00 60.52  ? 376 HIS   B N   1 
ATOM   5968 C CA  . HIS   B 1 376 ? 32.856  6.169   59.980 1.00 58.43  ? 376 HIS   B CA  1 
ATOM   5969 C C   . HIS   B 1 376 ? 31.848  6.793   60.933 1.00 58.36  ? 376 HIS   B C   1 
ATOM   5970 O O   . HIS   B 1 376 ? 31.442  7.947   60.778 1.00 59.73  ? 376 HIS   B O   1 
ATOM   5971 C CB  . HIS   B 1 376 ? 34.256  6.181   60.602 1.00 61.37  ? 376 HIS   B CB  1 
ATOM   5972 C CG  . HIS   B 1 376 ? 35.333  5.741   59.660 1.00 73.64  ? 376 HIS   B CG  1 
ATOM   5973 N ND1 . HIS   B 1 376 ? 35.775  4.438   59.590 1.00 86.85  ? 376 HIS   B ND1 1 
ATOM   5974 C CD2 . HIS   B 1 376 ? 36.049  6.432   58.742 1.00 82.08  ? 376 HIS   B CD2 1 
ATOM   5975 C CE1 . HIS   B 1 376 ? 36.721  4.345   58.672 1.00 86.16  ? 376 HIS   B CE1 1 
ATOM   5976 N NE2 . HIS   B 1 376 ? 36.907  5.541   58.143 1.00 86.18  ? 376 HIS   B NE2 1 
ATOM   5977 N N   . VAL   B 1 377 ? 31.429  5.992   61.917 1.00 56.15  ? 377 VAL   B N   1 
ATOM   5978 C CA  . VAL   B 1 377 ? 30.532  6.482   62.957 1.00 55.12  ? 377 VAL   B CA  1 
ATOM   5979 C C   . VAL   B 1 377 ? 31.140  7.710   63.616 1.00 59.42  ? 377 VAL   B C   1 
ATOM   5980 O O   . VAL   B 1 377 ? 32.326  7.726   63.968 1.00 78.65  ? 377 VAL   B O   1 
ATOM   5981 C CB  . VAL   B 1 377 ? 30.250  5.374   63.979 1.00 51.86  ? 377 VAL   B CB  1 
ATOM   5982 C CG1 . VAL   B 1 377 ? 29.526  5.935   65.192 1.00 61.68  ? 377 VAL   B CG1 1 
ATOM   5983 C CG2 . VAL   B 1 377 ? 29.433  4.268   63.332 1.00 59.07  ? 377 VAL   B CG2 1 
ATOM   5984 N N   . GLY   B 1 378 ? 30.326  8.753   63.780 1.00 65.68  ? 378 GLY   B N   1 
ATOM   5985 C CA  . GLY   B 1 378 ? 30.773  10.030  64.282 1.00 65.17  ? 378 GLY   B CA  1 
ATOM   5986 C C   . GLY   B 1 378 ? 30.981  11.085  63.215 1.00 66.62  ? 378 GLY   B C   1 
ATOM   5987 O O   . GLY   B 1 378 ? 31.046  12.274  63.546 1.00 71.14  ? 378 GLY   B O   1 
ATOM   5988 N N   . ASP   B 1 379 ? 31.082  10.685  61.950 1.00 60.00  ? 379 ASP   B N   1 
ATOM   5989 C CA  . ASP   B 1 379 ? 31.159  11.651  60.866 1.00 61.27  ? 379 ASP   B CA  1 
ATOM   5990 C C   . ASP   B 1 379 ? 29.801  12.309  60.644 1.00 56.54  ? 379 ASP   B C   1 
ATOM   5991 O O   . ASP   B 1 379 ? 28.750  11.773  61.006 1.00 65.03  ? 379 ASP   B O   1 
ATOM   5992 C CB  . ASP   B 1 379 ? 31.636  10.986  59.575 1.00 49.55  ? 379 ASP   B CB  1 
ATOM   5993 C CG  . ASP   B 1 379 ? 33.100  10.599  59.627 1.00 83.07  ? 379 ASP   B CG  1 
ATOM   5994 O OD1 . ASP   B 1 379 ? 33.780  10.980  60.603 1.00 98.03  ? 379 ASP   B OD1 1 
ATOM   5995 O OD2 . ASP   B 1 379 ? 33.571  9.913   58.696 1.00 75.80  ? 379 ASP   B OD2 1 
ATOM   5996 N N   . TRP   B 1 380 ? 29.836  13.500  60.056 1.00 52.23  ? 380 TRP   B N   1 
ATOM   5997 C CA  . TRP   B 1 380 ? 28.641  14.288  59.809 1.00 48.98  ? 380 TRP   B CA  1 
ATOM   5998 C C   . TRP   B 1 380 ? 28.326  14.341  58.320 1.00 52.07  ? 380 TRP   B C   1 
ATOM   5999 O O   . TRP   B 1 380 ? 29.225  14.332  57.473 1.00 60.83  ? 380 TRP   B O   1 
ATOM   6000 C CB  . TRP   B 1 380 ? 28.804  15.709  60.351 1.00 47.51  ? 380 TRP   B CB  1 
ATOM   6001 C CG  . TRP   B 1 380 ? 28.910  15.771  61.839 1.00 59.90  ? 380 TRP   B CG  1 
ATOM   6002 C CD1 . TRP   B 1 380 ? 30.037  15.602  62.585 1.00 53.98  ? 380 TRP   B CD1 1 
ATOM   6003 C CD2 . TRP   B 1 380 ? 27.850  16.034  62.766 1.00 67.08  ? 380 TRP   B CD2 1 
ATOM   6004 N NE1 . TRP   B 1 380 ? 29.747  15.741  63.919 1.00 65.51  ? 380 TRP   B NE1 1 
ATOM   6005 C CE2 . TRP   B 1 380 ? 28.410  16.005  64.058 1.00 56.64  ? 380 TRP   B CE2 1 
ATOM   6006 C CE3 . TRP   B 1 380 ? 26.481  16.288  62.629 1.00 57.35  ? 380 TRP   B CE3 1 
ATOM   6007 C CZ2 . TRP   B 1 380 ? 27.651  16.221  65.206 1.00 57.11  ? 380 TRP   B CZ2 1 
ATOM   6008 C CZ3 . TRP   B 1 380 ? 25.729  16.501  63.771 1.00 67.03  ? 380 TRP   B CZ3 1 
ATOM   6009 C CH2 . TRP   B 1 380 ? 26.316  16.467  65.042 1.00 62.59  ? 380 TRP   B CH2 1 
ATOM   6010 N N   . MET   B 1 381 ? 27.032  14.400  58.017 1.00 55.74  ? 381 MET   B N   1 
ATOM   6011 C CA  . MET   B 1 381 ? 26.522  14.625  56.673 1.00 59.65  ? 381 MET   B CA  1 
ATOM   6012 C C   . MET   B 1 381 ? 25.657  15.877  56.663 1.00 53.18  ? 381 MET   B C   1 
ATOM   6013 O O   . MET   B 1 381 ? 24.883  16.119  57.597 1.00 63.22  ? 381 MET   B O   1 
ATOM   6014 C CB  . MET   B 1 381 ? 25.683  13.451  56.168 1.00 66.30  ? 381 MET   B CB  1 
ATOM   6015 C CG  . MET   B 1 381 ? 26.435  12.262  55.637 1.00 64.30  ? 381 MET   B CG  1 
ATOM   6016 S SD  . MET   B 1 381 ? 25.203  11.125  54.966 1.00 89.52  ? 381 MET   B SD  1 
ATOM   6017 C CE  . MET   B 1 381 ? 26.119  9.597   54.871 1.00 80.26  ? 381 MET   B CE  1 
ATOM   6018 N N   . LEU   B 1 382 ? 25.779  16.662  55.598 1.00 53.88  ? 382 LEU   B N   1 
ATOM   6019 C CA  . LEU   B 1 382 ? 25.045  17.910  55.457 1.00 58.30  ? 382 LEU   B CA  1 
ATOM   6020 C C   . LEU   B 1 382 ? 24.029  17.795  54.331 1.00 59.46  ? 382 LEU   B C   1 
ATOM   6021 O O   . LEU   B 1 382 ? 24.298  17.177  53.296 1.00 62.46  ? 382 LEU   B O   1 
ATOM   6022 C CB  . LEU   B 1 382 ? 25.989  19.083  55.185 1.00 68.53  ? 382 LEU   B CB  1 
ATOM   6023 C CG  . LEU   B 1 382 ? 27.082  19.320  56.225 1.00 72.77  ? 382 LEU   B CG  1 
ATOM   6024 C CD1 . LEU   B 1 382 ? 27.907  20.540  55.854 1.00 77.46  ? 382 LEU   B CD1 1 
ATOM   6025 C CD2 . LEU   B 1 382 ? 26.476  19.477  57.610 1.00 63.29  ? 382 LEU   B CD2 1 
ATOM   6026 N N   . PHE   B 1 383 ? 22.862  18.392  54.547 1.00 54.37  ? 383 PHE   B N   1 
ATOM   6027 C CA  . PHE   B 1 383 ? 21.793  18.453  53.557 1.00 57.84  ? 383 PHE   B CA  1 
ATOM   6028 C C   . PHE   B 1 383 ? 21.358  19.906  53.451 1.00 63.32  ? 383 PHE   B C   1 
ATOM   6029 O O   . PHE   B 1 383 ? 20.854  20.479  54.422 1.00 49.66  ? 383 PHE   B O   1 
ATOM   6030 C CB  . PHE   B 1 383 ? 20.617  17.555  53.940 1.00 51.97  ? 383 PHE   B CB  1 
ATOM   6031 C CG  . PHE   B 1 383 ? 20.944  16.091  53.945 1.00 49.62  ? 383 PHE   B CG  1 
ATOM   6032 C CD1 . PHE   B 1 383 ? 21.473  15.489  55.073 1.00 48.96  ? 383 PHE   B CD1 1 
ATOM   6033 C CD2 . PHE   B 1 383 ? 20.716  15.314  52.820 1.00 51.12  ? 383 PHE   B CD2 1 
ATOM   6034 C CE1 . PHE   B 1 383 ? 21.772  14.142  55.080 1.00 51.44  ? 383 PHE   B CE1 1 
ATOM   6035 C CE2 . PHE   B 1 383 ? 21.013  13.966  52.821 1.00 52.99  ? 383 PHE   B CE2 1 
ATOM   6036 C CZ  . PHE   B 1 383 ? 21.542  13.379  53.952 1.00 59.43  ? 383 PHE   B CZ  1 
ATOM   6037 N N   . GLU   B 1 384 ? 21.582  20.506  52.289 1.00 58.42  ? 384 GLU   B N   1 
ATOM   6038 C CA  . GLU   B 1 384 ? 21.192  21.887  52.067 1.00 57.63  ? 384 GLU   B CA  1 
ATOM   6039 C C   . GLU   B 1 384 ? 19.751  21.963  51.571 1.00 62.54  ? 384 GLU   B C   1 
ATOM   6040 O O   . GLU   B 1 384 ? 19.147  20.965  51.171 1.00 60.71  ? 384 GLU   B O   1 
ATOM   6041 C CB  . GLU   B 1 384 ? 22.141  22.553  51.073 1.00 63.89  ? 384 GLU   B CB  1 
ATOM   6042 C CG  . GLU   B 1 384 ? 23.539  22.776  51.624 1.00 75.83  ? 384 GLU   B CG  1 
ATOM   6043 C CD  . GLU   B 1 384 ? 24.492  23.339  50.591 1.00 100.04 ? 384 GLU   B CD  1 
ATOM   6044 O OE1 . GLU   B 1 384 ? 24.174  23.272  49.385 1.00 91.82  ? 384 GLU   B OE1 1 
ATOM   6045 O OE2 . GLU   B 1 384 ? 25.563  23.843  50.987 1.00 106.76 ? 384 GLU   B OE2 1 
ATOM   6046 N N   . ASN   B 1 385 ? 19.200  23.178  51.612 1.00 61.45  ? 385 ASN   B N   1 
ATOM   6047 C CA  . ASN   B 1 385 ? 17.859  23.460  51.098 1.00 43.48  ? 385 ASN   B CA  1 
ATOM   6048 C C   . ASN   B 1 385 ? 16.804  22.611  51.803 1.00 47.30  ? 385 ASN   B C   1 
ATOM   6049 O O   . ASN   B 1 385 ? 15.914  22.040  51.170 1.00 64.18  ? 385 ASN   B O   1 
ATOM   6050 C CB  . ASN   B 1 385 ? 17.799  23.264  49.583 1.00 59.46  ? 385 ASN   B CB  1 
ATOM   6051 C CG  . ASN   B 1 385 ? 18.868  24.052  48.853 1.00 60.72  ? 385 ASN   B CG  1 
ATOM   6052 O OD1 . ASN   B 1 385 ? 19.149  25.202  49.193 1.00 59.26  ? 385 ASN   B OD1 1 
ATOM   6053 N ND2 . ASN   B 1 385 ? 19.476  23.433  47.849 1.00 70.50  ? 385 ASN   B ND2 1 
ATOM   6054 N N   . MET   B 1 386 ? 16.906  22.526  53.130 1.00 57.98  ? 386 MET   B N   1 
ATOM   6055 C CA  . MET   B 1 386 ? 16.004  21.721  53.944 1.00 49.10  ? 386 MET   B CA  1 
ATOM   6056 C C   . MET   B 1 386 ? 15.024  22.574  54.742 1.00 49.49  ? 386 MET   B C   1 
ATOM   6057 O O   . MET   B 1 386 ? 14.529  22.133  55.784 1.00 48.45  ? 386 MET   B O   1 
ATOM   6058 C CB  . MET   B 1 386 ? 16.804  20.819  54.882 1.00 45.04  ? 386 MET   B CB  1 
ATOM   6059 C CG  . MET   B 1 386 ? 17.534  19.684  54.185 1.00 47.20  ? 386 MET   B CG  1 
ATOM   6060 S SD  . MET   B 1 386 ? 16.406  18.462  53.485 1.00 60.25  ? 386 MET   B SD  1 
ATOM   6061 C CE  . MET   B 1 386 ? 15.751  17.704  54.970 1.00 60.07  ? 386 MET   B CE  1 
ATOM   6062 N N   . GLY   B 1 387 ? 14.735  23.790  54.274 1.00 55.67  ? 387 GLY   B N   1 
ATOM   6063 C CA  . GLY   B 1 387 ? 13.861  24.678  55.018 1.00 54.02  ? 387 GLY   B CA  1 
ATOM   6064 C C   . GLY   B 1 387 ? 12.385  24.448  54.786 1.00 51.40  ? 387 GLY   B C   1 
ATOM   6065 O O   . GLY   B 1 387 ? 11.566  24.768  55.653 1.00 54.22  ? 387 GLY   B O   1 
ATOM   6066 N N   . ALA   B 1 388 ? 12.018  23.902  53.631 1.00 60.43  ? 388 ALA   B N   1 
ATOM   6067 C CA  . ALA   B 1 388 ? 10.627  23.849  53.201 1.00 51.47  ? 388 ALA   B CA  1 
ATOM   6068 C C   . ALA   B 1 388 ? 10.040  22.465  53.437 1.00 52.08  ? 388 ALA   B C   1 
ATOM   6069 O O   . ALA   B 1 388 ? 10.585  21.464  52.960 1.00 53.32  ? 388 ALA   B O   1 
ATOM   6070 C CB  . ALA   B 1 388 ? 10.504  24.217  51.724 1.00 47.65  ? 388 ALA   B CB  1 
ATOM   6071 N N   . TYR   B 1 389 ? 8.923   22.422  54.167 1.00 57.19  ? 389 TYR   B N   1 
ATOM   6072 C CA  . TYR   B 1 389 ? 8.128   21.206  54.353 1.00 42.31  ? 389 TYR   B CA  1 
ATOM   6073 C C   . TYR   B 1 389 ? 8.968   20.055  54.899 1.00 49.51  ? 389 TYR   B C   1 
ATOM   6074 O O   . TYR   B 1 389 ? 8.821   18.902  54.489 1.00 54.45  ? 389 TYR   B O   1 
ATOM   6075 C CB  . TYR   B 1 389 ? 7.435   20.807  53.050 1.00 45.02  ? 389 TYR   B CB  1 
ATOM   6076 C CG  . TYR   B 1 389 ? 6.584   21.910  52.473 1.00 49.93  ? 389 TYR   B CG  1 
ATOM   6077 C CD1 . TYR   B 1 389 ? 5.352   22.223  53.030 1.00 46.95  ? 389 TYR   B CD1 1 
ATOM   6078 C CD2 . TYR   B 1 389 ? 7.022   22.654  51.385 1.00 50.95  ? 389 TYR   B CD2 1 
ATOM   6079 C CE1 . TYR   B 1 389 ? 4.573   23.235  52.512 1.00 48.07  ? 389 TYR   B CE1 1 
ATOM   6080 C CE2 . TYR   B 1 389 ? 6.249   23.670  50.862 1.00 53.74  ? 389 TYR   B CE2 1 
ATOM   6081 C CZ  . TYR   B 1 389 ? 5.025   23.956  51.431 1.00 51.16  ? 389 TYR   B CZ  1 
ATOM   6082 O OH  . TYR   B 1 389 ? 4.247   24.965  50.919 1.00 60.70  ? 389 TYR   B OH  1 
ATOM   6083 N N   . THR   B 1 390 ? 9.868   20.374  55.829 1.00 58.57  ? 390 THR   B N   1 
ATOM   6084 C CA  . THR   B 1 390 ? 10.677  19.367  56.501 1.00 52.45  ? 390 THR   B CA  1 
ATOM   6085 C C   . THR   B 1 390 ? 10.369  19.282  57.991 1.00 49.06  ? 390 THR   B C   1 
ATOM   6086 O O   . THR   B 1 390 ? 9.952   18.228  58.477 1.00 67.93  ? 390 THR   B O   1 
ATOM   6087 C CB  . THR   B 1 390 ? 12.166  19.662  56.282 1.00 57.15  ? 390 THR   B CB  1 
ATOM   6088 O OG1 . THR   B 1 390 ? 12.448  21.008  56.684 1.00 50.21  ? 390 THR   B OG1 1 
ATOM   6089 C CG2 . THR   B 1 390 ? 12.530  19.491  54.814 1.00 43.11  ? 390 THR   B CG2 1 
ATOM   6090 N N   . VAL   B 1 391 ? 10.548  20.375  58.735 1.00 46.17  ? 391 VAL   B N   1 
ATOM   6091 C CA  . VAL   B 1 391 ? 10.246  20.344  60.164 1.00 50.42  ? 391 VAL   B CA  1 
ATOM   6092 C C   . VAL   B 1 391 ? 8.750   20.478  60.415 1.00 47.82  ? 391 VAL   B C   1 
ATOM   6093 O O   . VAL   B 1 391 ? 8.240   19.967  61.417 1.00 61.84  ? 391 VAL   B O   1 
ATOM   6094 C CB  . VAL   B 1 391 ? 11.030  21.434  60.918 1.00 40.74  ? 391 VAL   B CB  1 
ATOM   6095 C CG1 . VAL   B 1 391 ? 12.518  21.179  60.818 1.00 45.77  ? 391 VAL   B CG1 1 
ATOM   6096 C CG2 . VAL   B 1 391 ? 10.681  22.819  60.394 1.00 44.97  ? 391 VAL   B CG2 1 
ATOM   6097 N N   . ALA   B 1 392 ? 8.030   21.170  59.528 1.00 64.63  ? 392 ALA   B N   1 
ATOM   6098 C CA  . ALA   B 1 392 ? 6.605   21.406  59.727 1.00 63.17  ? 392 ALA   B CA  1 
ATOM   6099 C C   . ALA   B 1 392 ? 5.794   20.117  59.780 1.00 61.62  ? 392 ALA   B C   1 
ATOM   6100 O O   . ALA   B 1 392 ? 4.715   20.103  60.381 1.00 65.24  ? 392 ALA   B O   1 
ATOM   6101 C CB  . ALA   B 1 392 ? 6.068   22.314  58.621 1.00 66.19  ? 392 ALA   B CB  1 
ATOM   6102 N N   . ALA   B 1 393 ? 6.285   19.035  59.174 1.00 60.69  ? 393 ALA   B N   1 
ATOM   6103 C CA  . ALA   B 1 393 ? 5.545   17.781  59.116 1.00 55.60  ? 393 ALA   B CA  1 
ATOM   6104 C C   . ALA   B 1 393 ? 6.288   16.646  59.811 1.00 52.69  ? 393 ALA   B C   1 
ATOM   6105 O O   . ALA   B 1 393 ? 5.953   15.474  59.610 1.00 57.92  ? 393 ALA   B O   1 
ATOM   6106 C CB  . ALA   B 1 393 ? 5.236   17.407  57.665 1.00 45.55  ? 393 ALA   B CB  1 
ATOM   6107 N N   . ALA   B 1 394 ? 7.287   16.966  60.626 1.00 51.19  ? 394 ALA   B N   1 
ATOM   6108 C CA  . ALA   B 1 394 ? 8.030   15.940  61.338 1.00 53.12  ? 394 ALA   B CA  1 
ATOM   6109 C C   . ALA   B 1 394 ? 7.250   15.465  62.557 1.00 59.69  ? 394 ALA   B C   1 
ATOM   6110 O O   . ALA   B 1 394 ? 6.502   16.224  63.180 1.00 60.72  ? 394 ALA   B O   1 
ATOM   6111 C CB  . ALA   B 1 394 ? 9.401   16.465  61.765 1.00 59.86  ? 394 ALA   B CB  1 
ATOM   6112 N N   . SER   B 1 395 ? 7.438   14.196  62.899 1.00 62.64  ? 395 SER   B N   1 
ATOM   6113 C CA  . SER   B 1 395 ? 6.818   13.595  64.069 1.00 61.71  ? 395 SER   B CA  1 
ATOM   6114 C C   . SER   B 1 395 ? 7.893   13.028  64.986 1.00 57.88  ? 395 SER   B C   1 
ATOM   6115 O O   . SER   B 1 395 ? 9.081   12.996  64.653 1.00 60.35  ? 395 SER   B O   1 
ATOM   6116 C CB  . SER   B 1 395 ? 5.826   12.493  63.670 1.00 55.97  ? 395 SER   B CB  1 
ATOM   6117 O OG  . SER   B 1 395 ? 6.505   11.317  63.266 1.00 49.88  ? 395 SER   B OG  1 
ATOM   6118 N N   . THR   B 1 396 ? 7.459   12.583  66.163 1.00 58.61  ? 396 THR   B N   1 
ATOM   6119 C CA  . THR   B 1 396 ? 8.337   11.946  67.135 1.00 53.36  ? 396 THR   B CA  1 
ATOM   6120 C C   . THR   B 1 396 ? 8.153   10.435  67.164 1.00 55.79  ? 396 THR   B C   1 
ATOM   6121 O O   . THR   B 1 396 ? 8.268   9.816   68.228 1.00 66.59  ? 396 THR   B O   1 
ATOM   6122 C CB  . THR   B 1 396 ? 8.108   12.535  68.525 1.00 60.42  ? 396 THR   B CB  1 
ATOM   6123 O OG1 . THR   B 1 396 ? 6.733   12.367  68.891 1.00 70.62  ? 396 THR   B OG1 1 
ATOM   6124 C CG2 . THR   B 1 396 ? 8.461   14.013  68.535 1.00 67.59  ? 396 THR   B CG2 1 
ATOM   6125 N N   . PHE   B 1 397 ? 7.843   9.835   66.015 1.00 48.63  ? 397 PHE   B N   1 
ATOM   6126 C CA  . PHE   B 1 397 ? 7.721   8.387   65.925 1.00 50.03  ? 397 PHE   B CA  1 
ATOM   6127 C C   . PHE   B 1 397 ? 8.985   7.718   66.444 1.00 57.71  ? 397 PHE   B C   1 
ATOM   6128 O O   . PHE   B 1 397 ? 10.099  8.200   66.218 1.00 58.68  ? 397 PHE   B O   1 
ATOM   6129 C CB  . PHE   B 1 397 ? 7.463   7.961   64.479 1.00 50.78  ? 397 PHE   B CB  1 
ATOM   6130 C CG  . PHE   B 1 397 ? 7.316   6.474   64.302 1.00 51.70  ? 397 PHE   B CG  1 
ATOM   6131 C CD1 . PHE   B 1 397 ? 6.231   5.800   64.839 1.00 52.91  ? 397 PHE   B CD1 1 
ATOM   6132 C CD2 . PHE   B 1 397 ? 8.277   5.748   63.616 1.00 47.19  ? 397 PHE   B CD2 1 
ATOM   6133 C CE1 . PHE   B 1 397 ? 6.099   4.430   64.678 1.00 60.12  ? 397 PHE   B CE1 1 
ATOM   6134 C CE2 . PHE   B 1 397 ? 8.152   4.380   63.455 1.00 51.95  ? 397 PHE   B CE2 1 
ATOM   6135 C CZ  . PHE   B 1 397 ? 7.063   3.719   63.986 1.00 58.29  ? 397 PHE   B CZ  1 
ATOM   6136 N N   . ASN   B 1 398 ? 8.798   6.621   67.177 1.00 62.79  ? 398 ASN   B N   1 
ATOM   6137 C CA  . ASN   B 1 398 ? 9.858   5.849   67.818 1.00 68.74  ? 398 ASN   B CA  1 
ATOM   6138 C C   . ASN   B 1 398 ? 10.517  6.601   68.968 1.00 54.76  ? 398 ASN   B C   1 
ATOM   6139 O O   . ASN   B 1 398 ? 11.497  6.109   69.540 1.00 57.78  ? 398 ASN   B O   1 
ATOM   6140 C CB  . ASN   B 1 398 ? 10.920  5.390   66.811 1.00 70.04  ? 398 ASN   B CB  1 
ATOM   6141 C CG  . ASN   B 1 398 ? 11.264  3.926   66.962 1.00 79.02  ? 398 ASN   B CG  1 
ATOM   6142 O OD1 . ASN   B 1 398 ? 10.963  3.316   67.985 1.00 84.53  ? 398 ASN   B OD1 1 
ATOM   6143 N ND2 . ASN   B 1 398 ? 11.882  3.350   65.941 1.00 71.05  ? 398 ASN   B ND2 1 
ATOM   6144 N N   . GLY   B 1 399 ? 10.008  7.780   69.323 1.00 60.20  ? 399 GLY   B N   1 
ATOM   6145 C CA  . GLY   B 1 399 ? 10.545  8.566   70.412 1.00 57.07  ? 399 GLY   B CA  1 
ATOM   6146 C C   . GLY   B 1 399 ? 11.710  9.463   70.060 1.00 56.00  ? 399 GLY   B C   1 
ATOM   6147 O O   . GLY   B 1 399 ? 12.269  10.102  70.959 1.00 65.91  ? 399 GLY   B O   1 
ATOM   6148 N N   . PHE   B 1 400 ? 12.093  9.539   68.789 1.00 56.59  ? 400 PHE   B N   1 
ATOM   6149 C CA  . PHE   B 1 400 ? 13.221  10.366  68.387 1.00 52.10  ? 400 PHE   B CA  1 
ATOM   6150 C C   . PHE   B 1 400 ? 12.794  11.827  68.301 1.00 57.59  ? 400 PHE   B C   1 
ATOM   6151 O O   . PHE   B 1 400 ? 11.805  12.160  67.640 1.00 60.09  ? 400 PHE   B O   1 
ATOM   6152 C CB  . PHE   B 1 400 ? 13.790  9.873   67.058 1.00 54.62  ? 400 PHE   B CB  1 
ATOM   6153 C CG  . PHE   B 1 400 ? 14.392  8.498   67.142 1.00 64.79  ? 400 PHE   B CG  1 
ATOM   6154 C CD1 . PHE   B 1 400 ? 13.830  7.435   66.453 1.00 76.29  ? 400 PHE   B CD1 1 
ATOM   6155 C CD2 . PHE   B 1 400 ? 15.505  8.263   67.934 1.00 56.52  ? 400 PHE   B CD2 1 
ATOM   6156 C CE1 . PHE   B 1 400 ? 14.380  6.166   66.539 1.00 68.99  ? 400 PHE   B CE1 1 
ATOM   6157 C CE2 . PHE   B 1 400 ? 16.058  6.997   68.023 1.00 63.31  ? 400 PHE   B CE2 1 
ATOM   6158 C CZ  . PHE   B 1 400 ? 15.493  5.947   67.324 1.00 51.66  ? 400 PHE   B CZ  1 
ATOM   6159 N N   . GLN   B 1 401 ? 13.539  12.692  68.982 1.00 67.74  ? 401 GLN   B N   1 
ATOM   6160 C CA  . GLN   B 1 401 ? 13.164  14.090  69.131 1.00 67.15  ? 401 GLN   B CA  1 
ATOM   6161 C C   . GLN   B 1 401 ? 13.532  14.908  67.899 1.00 63.37  ? 401 GLN   B C   1 
ATOM   6162 O O   . GLN   B 1 401 ? 14.476  14.591  67.169 1.00 59.83  ? 401 GLN   B O   1 
ATOM   6163 C CB  . GLN   B 1 401 ? 13.835  14.685  70.368 1.00 61.39  ? 401 GLN   B CB  1 
ATOM   6164 C CG  . GLN   B 1 401 ? 13.387  14.030  71.657 1.00 67.34  ? 401 GLN   B CG  1 
ATOM   6165 C CD  . GLN   B 1 401 ? 11.883  14.066  71.828 1.00 80.01  ? 401 GLN   B CD  1 
ATOM   6166 O OE1 . GLN   B 1 401 ? 11.265  15.129  71.764 1.00 91.33  ? 401 GLN   B OE1 1 
ATOM   6167 N NE2 . GLN   B 1 401 ? 11.283  12.900  72.036 1.00 68.13  ? 401 GLN   B NE2 1 
ATOM   6168 N N   . ARG   B 1 402 ? 12.761  15.970  67.672 1.00 71.23  ? 402 ARG   B N   1 
ATOM   6169 C CA  . ARG   B 1 402 ? 13.003  16.849  66.539 1.00 58.09  ? 402 ARG   B CA  1 
ATOM   6170 C C   . ARG   B 1 402 ? 14.347  17.559  66.707 1.00 70.73  ? 402 ARG   B C   1 
ATOM   6171 O O   . ARG   B 1 402 ? 14.688  17.988  67.815 1.00 69.21  ? 402 ARG   B O   1 
ATOM   6172 C CB  . ARG   B 1 402 ? 11.887  17.886  66.411 1.00 58.05  ? 402 ARG   B CB  1 
ATOM   6173 C CG  . ARG   B 1 402 ? 10.595  17.370  65.794 1.00 73.51  ? 402 ARG   B CG  1 
ATOM   6174 C CD  . ARG   B 1 402 ? 9.480   18.401  65.945 1.00 77.84  ? 402 ARG   B CD  1 
ATOM   6175 N NE  . ARG   B 1 402 ? 8.945   18.451  67.304 1.00 97.14  ? 402 ARG   B NE  1 
ATOM   6176 C CZ  . ARG   B 1 402 ? 7.801   17.894  67.690 1.00 97.87  ? 402 ARG   B CZ  1 
ATOM   6177 N NH1 . ARG   B 1 402 ? 7.049   17.237  66.818 1.00 96.86  ? 402 ARG   B NH1 1 
ATOM   6178 N NH2 . ARG   B 1 402 ? 7.406   18.001  68.952 1.00 84.66  ? 402 ARG   B NH2 1 
ATOM   6179 N N   . PRO   B 1 403 ? 15.133  17.683  65.638 1.00 63.72  ? 403 PRO   B N   1 
ATOM   6180 C CA  . PRO   B 1 403 ? 16.470  18.282  65.762 1.00 57.69  ? 403 PRO   B CA  1 
ATOM   6181 C C   . PRO   B 1 403 ? 16.424  19.716  66.277 1.00 59.63  ? 403 PRO   B C   1 
ATOM   6182 O O   . PRO   B 1 403 ? 15.506  20.480  65.973 1.00 62.06  ? 403 PRO   B O   1 
ATOM   6183 C CB  . PRO   B 1 403 ? 17.019  18.221  64.331 1.00 50.04  ? 403 PRO   B CB  1 
ATOM   6184 C CG  . PRO   B 1 403 ? 16.227  17.141  63.666 1.00 60.03  ? 403 PRO   B CG  1 
ATOM   6185 C CD  . PRO   B 1 403 ? 14.860  17.219  64.268 1.00 54.22  ? 403 PRO   B CD  1 
ATOM   6186 N N   . THR   B 1 404 ? 17.430  20.066  67.077 1.00 65.62  ? 404 THR   B N   1 
ATOM   6187 C CA  . THR   B 1 404 ? 17.602  21.437  67.541 1.00 64.61  ? 404 THR   B CA  1 
ATOM   6188 C C   . THR   B 1 404 ? 17.904  22.369  66.373 1.00 64.25  ? 404 THR   B C   1 
ATOM   6189 O O   . THR   B 1 404 ? 18.689  22.036  65.484 1.00 60.04  ? 404 THR   B O   1 
ATOM   6190 C CB  . THR   B 1 404 ? 18.736  21.497  68.566 1.00 57.77  ? 404 THR   B CB  1 
ATOM   6191 O OG1 . THR   B 1 404 ? 18.485  20.547  69.609 1.00 69.56  ? 404 THR   B OG1 1 
ATOM   6192 C CG2 . THR   B 1 404 ? 18.845  22.887  69.169 1.00 73.39  ? 404 THR   B CG2 1 
ATOM   6193 N N   . ILE   B 1 405 ? 17.292  23.552  66.385 1.00 57.04  ? 405 ILE   B N   1 
ATOM   6194 C CA  . ILE   B 1 405 ? 17.503  24.569  65.358 1.00 66.06  ? 405 ILE   B CA  1 
ATOM   6195 C C   . ILE   B 1 405 ? 18.305  25.719  65.954 1.00 65.16  ? 405 ILE   B C   1 
ATOM   6196 O O   . ILE   B 1 405 ? 17.912  26.288  66.979 1.00 67.49  ? 405 ILE   B O   1 
ATOM   6197 C CB  . ILE   B 1 405 ? 16.168  25.082  64.792 1.00 66.81  ? 405 ILE   B CB  1 
ATOM   6198 C CG1 . ILE   B 1 405 ? 15.325  23.924  64.257 1.00 56.53  ? 405 ILE   B CG1 1 
ATOM   6199 C CG2 . ILE   B 1 405 ? 16.417  26.113  63.702 1.00 54.64  ? 405 ILE   B CG2 1 
ATOM   6200 C CD1 . ILE   B 1 405 ? 13.921  24.333  63.864 1.00 41.67  ? 405 ILE   B CD1 1 
ATOM   6201 N N   . TYR   B 1 406 ? 19.421  26.064  65.318 1.00 57.94  ? 406 TYR   B N   1 
ATOM   6202 C CA  . TYR   B 1 406 ? 20.226  27.219  65.695 1.00 68.72  ? 406 TYR   B CA  1 
ATOM   6203 C C   . TYR   B 1 406 ? 20.006  28.332  64.678 1.00 64.33  ? 406 TYR   B C   1 
ATOM   6204 O O   . TYR   B 1 406 ? 20.357  28.180  63.502 1.00 58.23  ? 406 TYR   B O   1 
ATOM   6205 C CB  . TYR   B 1 406 ? 21.708  26.854  65.777 1.00 69.69  ? 406 TYR   B CB  1 
ATOM   6206 C CG  . TYR   B 1 406 ? 22.034  25.794  66.804 1.00 68.99  ? 406 TYR   B CG  1 
ATOM   6207 C CD1 . TYR   B 1 406 ? 21.963  26.073  68.161 1.00 72.09  ? 406 TYR   B CD1 1 
ATOM   6208 C CD2 . TYR   B 1 406 ? 22.420  24.517  66.417 1.00 74.81  ? 406 TYR   B CD2 1 
ATOM   6209 C CE1 . TYR   B 1 406 ? 22.264  25.111  69.106 1.00 78.07  ? 406 TYR   B CE1 1 
ATOM   6210 C CE2 . TYR   B 1 406 ? 22.724  23.547  67.356 1.00 82.32  ? 406 TYR   B CE2 1 
ATOM   6211 C CZ  . TYR   B 1 406 ? 22.643  23.851  68.699 1.00 84.15  ? 406 TYR   B CZ  1 
ATOM   6212 O OH  . TYR   B 1 406 ? 22.942  22.894  69.642 1.00 91.98  ? 406 TYR   B OH  1 
ATOM   6213 N N   . TYR   B 1 407 ? 19.427  29.442  65.131 1.00 65.65  ? 407 TYR   B N   1 
ATOM   6214 C CA  . TYR   B 1 407 ? 19.178  30.597  64.278 1.00 54.65  ? 407 TYR   B CA  1 
ATOM   6215 C C   . TYR   B 1 407 ? 20.380  31.534  64.314 1.00 62.81  ? 407 TYR   B C   1 
ATOM   6216 O O   . TYR   B 1 407 ? 20.906  31.837  65.389 1.00 72.35  ? 407 TYR   B O   1 
ATOM   6217 C CB  . TYR   B 1 407 ? 17.921  31.342  64.729 1.00 42.33  ? 407 TYR   B CB  1 
ATOM   6218 C CG  . TYR   B 1 407 ? 16.657  30.521  64.635 1.00 58.36  ? 407 TYR   B CG  1 
ATOM   6219 C CD1 . TYR   B 1 407 ? 16.134  29.888  65.755 1.00 57.73  ? 407 TYR   B CD1 1 
ATOM   6220 C CD2 . TYR   B 1 407 ? 15.989  30.373  63.427 1.00 59.06  ? 407 TYR   B CD2 1 
ATOM   6221 C CE1 . TYR   B 1 407 ? 14.979  29.134  65.676 1.00 63.63  ? 407 TYR   B CE1 1 
ATOM   6222 C CE2 . TYR   B 1 407 ? 14.833  29.619  63.338 1.00 57.22  ? 407 TYR   B CE2 1 
ATOM   6223 C CZ  . TYR   B 1 407 ? 14.334  29.003  64.466 1.00 63.92  ? 407 TYR   B CZ  1 
ATOM   6224 O OH  . TYR   B 1 407 ? 13.186  28.251  64.387 1.00 68.89  ? 407 TYR   B OH  1 
ATOM   6225 N N   . VAL   B 1 408 ? 20.816  31.989  63.137 1.00 59.33  ? 408 VAL   B N   1 
ATOM   6226 C CA  . VAL   B 1 408 ? 21.927  32.923  63.024 1.00 57.27  ? 408 VAL   B CA  1 
ATOM   6227 C C   . VAL   B 1 408 ? 21.495  34.116  62.181 1.00 62.09  ? 408 VAL   B C   1 
ATOM   6228 O O   . VAL   B 1 408 ? 20.586  34.029  61.355 1.00 60.40  ? 408 VAL   B O   1 
ATOM   6229 C CB  . VAL   B 1 408 ? 23.188  32.265  62.421 1.00 58.78  ? 408 VAL   B CB  1 
ATOM   6230 C CG1 . VAL   B 1 408 ? 23.586  31.045  63.230 1.00 52.34  ? 408 VAL   B CG1 1 
ATOM   6231 C CG2 . VAL   B 1 408 ? 22.958  31.892  60.963 1.00 67.43  ? 408 VAL   B CG2 1 
ATOM   6232 N N   . MET   B 1 409 ? 22.168  35.246  62.406 1.00 64.00  ? 409 MET   B N   1 
ATOM   6233 C CA  . MET   B 1 409 ? 21.896  36.474  61.668 1.00 64.09  ? 409 MET   B CA  1 
ATOM   6234 C C   . MET   B 1 409 ? 23.108  37.387  61.762 1.00 65.67  ? 409 MET   B C   1 
ATOM   6235 O O   . MET   B 1 409 ? 23.632  37.613  62.857 1.00 65.18  ? 409 MET   B O   1 
ATOM   6236 C CB  . MET   B 1 409 ? 20.662  37.207  62.210 1.00 59.85  ? 409 MET   B CB  1 
ATOM   6237 C CG  . MET   B 1 409 ? 20.275  38.416  61.364 1.00 72.96  ? 409 MET   B CG  1 
ATOM   6238 S SD  . MET   B 1 409 ? 18.883  39.391  61.971 1.00 76.63  ? 409 MET   B SD  1 
ATOM   6239 C CE  . MET   B 1 409 ? 17.552  38.203  61.890 1.00 73.11  ? 409 MET   B CE  1 
ATOM   6240 N N   . SER   B 1 410 ? 23.543  37.909  60.619 1.00 59.75  ? 410 SER   B N   1 
ATOM   6241 C CA  . SER   B 1 410 ? 24.647  38.852  60.594 1.00 55.18  ? 410 SER   B CA  1 
ATOM   6242 C C   . SER   B 1 410 ? 24.160  40.259  60.938 1.00 56.95  ? 410 SER   B C   1 
ATOM   6243 O O   . SER   B 1 410 ? 22.961  40.556  60.924 1.00 67.98  ? 410 SER   B O   1 
ATOM   6244 C CB  . SER   B 1 410 ? 25.318  38.860  59.223 1.00 51.50  ? 410 SER   B CB  1 
ATOM   6245 O OG  . SER   B 1 410 ? 24.461  39.443  58.260 1.00 61.88  ? 410 SER   B OG  1 
ATOM   6246 N N   . GLY   B 1 411 ? 25.115  41.129  61.249 1.00 66.31  ? 411 GLY   B N   1 
ATOM   6247 C CA  . GLY   B 1 411 ? 24.828  42.519  61.518 1.00 49.92  ? 411 GLY   B CA  1 
ATOM   6248 C C   . GLY   B 1 411 ? 24.206  43.252  60.344 1.00 57.70  ? 411 GLY   B C   1 
ATOM   6249 O O   . GLY   B 1 411 ? 23.191  43.943  60.491 1.00 56.85  ? 411 GLY   B O   1 
ATOM   6250 N N   . PRO   B 1 412 ? 24.805  43.126  59.151 1.00 60.86  ? 412 PRO   B N   1 
ATOM   6251 C CA  . PRO   B 1 412 ? 24.180  43.741  57.967 1.00 50.92  ? 412 PRO   B CA  1 
ATOM   6252 C C   . PRO   B 1 412 ? 22.784  43.216  57.691 1.00 56.37  ? 412 PRO   B C   1 
ATOM   6253 O O   . PRO   B 1 412 ? 21.915  43.979  57.251 1.00 61.46  ? 412 PRO   B O   1 
ATOM   6254 C CB  . PRO   B 1 412 ? 25.162  43.395  56.841 1.00 48.70  ? 412 PRO   B CB  1 
ATOM   6255 C CG  . PRO   B 1 412 ? 26.468  43.247  57.533 1.00 48.42  ? 412 PRO   B CG  1 
ATOM   6256 C CD  . PRO   B 1 412 ? 26.154  42.613  58.849 1.00 42.78  ? 412 PRO   B CD  1 
ATOM   6257 N N   . ALA   B 1 413 ? 22.545  41.924  57.929 1.00 47.14  ? 413 ALA   B N   1 
ATOM   6258 C CA  . ALA   B 1 413 ? 21.196  41.392  57.778 1.00 49.84  ? 413 ALA   B CA  1 
ATOM   6259 C C   . ALA   B 1 413 ? 20.232  42.080  58.735 1.00 52.62  ? 413 ALA   B C   1 
ATOM   6260 O O   . ALA   B 1 413 ? 19.103  42.416  58.358 1.00 72.87  ? 413 ALA   B O   1 
ATOM   6261 C CB  . ALA   B 1 413 ? 21.197  39.881  58.006 1.00 50.60  ? 413 ALA   B CB  1 
ATOM   6262 N N   . TRP   B 1 414 ? 20.663  42.307  59.977 1.00 49.52  ? 414 TRP   B N   1 
ATOM   6263 C CA  . TRP   B 1 414 ? 19.820  43.020  60.930 1.00 55.72  ? 414 TRP   B CA  1 
ATOM   6264 C C   . TRP   B 1 414 ? 19.565  44.452  60.475 1.00 66.26  ? 414 TRP   B C   1 
ATOM   6265 O O   . TRP   B 1 414 ? 18.459  44.978  60.645 1.00 69.05  ? 414 TRP   B O   1 
ATOM   6266 C CB  . TRP   B 1 414 ? 20.460  42.994  62.318 1.00 63.61  ? 414 TRP   B CB  1 
ATOM   6267 C CG  . TRP   B 1 414 ? 19.692  43.767  63.345 1.00 58.57  ? 414 TRP   B CG  1 
ATOM   6268 C CD1 . TRP   B 1 414 ? 18.678  43.303  64.131 1.00 57.67  ? 414 TRP   B CD1 1 
ATOM   6269 C CD2 . TRP   B 1 414 ? 19.881  45.140  63.704 1.00 52.44  ? 414 TRP   B CD2 1 
ATOM   6270 N NE1 . TRP   B 1 414 ? 18.220  44.303  64.952 1.00 57.18  ? 414 TRP   B NE1 1 
ATOM   6271 C CE2 . TRP   B 1 414 ? 18.942  45.441  64.710 1.00 56.24  ? 414 TRP   B CE2 1 
ATOM   6272 C CE3 . TRP   B 1 414 ? 20.751  46.146  63.269 1.00 56.67  ? 414 TRP   B CE3 1 
ATOM   6273 C CZ2 . TRP   B 1 414 ? 18.850  46.705  65.291 1.00 60.04  ? 414 TRP   B CZ2 1 
ATOM   6274 C CZ3 . TRP   B 1 414 ? 20.657  47.400  63.846 1.00 62.21  ? 414 TRP   B CZ3 1 
ATOM   6275 C CH2 . TRP   B 1 414 ? 19.713  47.669  64.845 1.00 63.28  ? 414 TRP   B CH2 1 
ATOM   6276 N N   . GLN   B 1 415 ? 20.581  45.102  59.901 1.00 57.82  ? 415 GLN   B N   1 
ATOM   6277 C CA  . GLN   B 1 415 ? 20.395  46.448  59.366 1.00 51.37  ? 415 GLN   B CA  1 
ATOM   6278 C C   . GLN   B 1 415 ? 19.363  46.457  58.244 1.00 65.82  ? 415 GLN   B C   1 
ATOM   6279 O O   . GLN   B 1 415 ? 18.511  47.352  58.176 1.00 60.75  ? 415 GLN   B O   1 
ATOM   6280 C CB  . GLN   B 1 415 ? 21.731  47.001  58.874 1.00 53.01  ? 415 GLN   B CB  1 
ATOM   6281 C CG  . GLN   B 1 415 ? 22.626  47.519  59.986 1.00 72.08  ? 415 GLN   B CG  1 
ATOM   6282 C CD  . GLN   B 1 415 ? 23.948  48.056  59.479 1.00 71.39  ? 415 GLN   B CD  1 
ATOM   6283 O OE1 . GLN   B 1 415 ? 24.513  47.541  58.515 1.00 73.80  ? 415 GLN   B OE1 1 
ATOM   6284 N NE2 . GLN   B 1 415 ? 24.452  49.098  60.130 1.00 80.70  ? 415 GLN   B NE2 1 
ATOM   6285 N N   . LEU   B 1 416 ? 19.442  45.476  57.344 1.00 56.55  ? 416 LEU   B N   1 
ATOM   6286 C CA  . LEU   B 1 416 ? 18.454  45.357  56.276 1.00 59.23  ? 416 LEU   B CA  1 
ATOM   6287 C C   . LEU   B 1 416 ? 17.054  45.141  56.838 1.00 62.96  ? 416 LEU   B C   1 
ATOM   6288 O O   . LEU   B 1 416 ? 16.078  45.714  56.338 1.00 64.86  ? 416 LEU   B O   1 
ATOM   6289 C CB  . LEU   B 1 416 ? 18.840  44.215  55.337 1.00 63.85  ? 416 LEU   B CB  1 
ATOM   6290 C CG  . LEU   B 1 416 ? 17.882  43.954  54.174 1.00 73.89  ? 416 LEU   B CG  1 
ATOM   6291 C CD1 . LEU   B 1 416 ? 17.782  45.173  53.265 1.00 67.81  ? 416 LEU   B CD1 1 
ATOM   6292 C CD2 . LEU   B 1 416 ? 18.307  42.717  53.395 1.00 61.64  ? 416 LEU   B CD2 1 
ATOM   6293 N N   . MET   B 1 417 ? 16.934  44.293  57.863 1.00 62.97  ? 417 MET   B N   1 
ATOM   6294 C CA  . MET   B 1 417 ? 15.639  44.085  58.505 1.00 68.39  ? 417 MET   B CA  1 
ATOM   6295 C C   . MET   B 1 417 ? 15.102  45.387  59.086 1.00 74.12  ? 417 MET   B C   1 
ATOM   6296 O O   . MET   B 1 417 ? 13.904  45.676  58.980 1.00 79.07  ? 417 MET   B O   1 
ATOM   6297 C CB  . MET   B 1 417 ? 15.753  43.015  59.590 1.00 70.47  ? 417 MET   B CB  1 
ATOM   6298 C CG  . MET   B 1 417 ? 14.430  42.666  60.256 1.00 68.86  ? 417 MET   B CG  1 
ATOM   6299 S SD  . MET   B 1 417 ? 14.568  41.309  61.439 1.00 81.38  ? 417 MET   B SD  1 
ATOM   6300 C CE  . MET   B 1 417 ? 15.719  41.990  62.631 1.00 79.09  ? 417 MET   B CE  1 
ATOM   6301 N N   . GLN   B 1 418 ? 15.971  46.176  59.722 1.00 85.20  ? 418 GLN   B N   1 
ATOM   6302 C CA  . GLN   B 1 418 ? 15.544  47.463  60.265 1.00 91.98  ? 418 GLN   B CA  1 
ATOM   6303 C C   . GLN   B 1 418 ? 15.083  48.403  59.156 1.00 81.49  ? 418 GLN   B C   1 
ATOM   6304 O O   . GLN   B 1 418 ? 14.096  49.132  59.318 1.00 84.37  ? 418 GLN   B O   1 
ATOM   6305 C CB  . GLN   B 1 418 ? 16.676  48.101  61.070 1.00 75.54  ? 418 GLN   B CB  1 
ATOM   6306 C CG  . GLN   B 1 418 ? 17.067  47.327  62.317 1.00 64.72  ? 418 GLN   B CG  1 
ATOM   6307 C CD  . GLN   B 1 418 ? 15.868  46.920  63.151 1.00 81.07  ? 418 GLN   B CD  1 
ATOM   6308 O OE1 . GLN   B 1 418 ? 15.068  47.761  63.561 1.00 104.52 ? 418 GLN   B OE1 1 
ATOM   6309 N NE2 . GLN   B 1 418 ? 15.737  45.623  63.403 1.00 80.79  ? 418 GLN   B NE2 1 
ATOM   6310 N N   . GLN   B 1 419 ? 15.798  48.411  58.028 1.00 69.01  ? 419 GLN   B N   1 
ATOM   6311 C CA  . GLN   B 1 419 ? 15.379  49.232  56.894 1.00 63.42  ? 419 GLN   B CA  1 
ATOM   6312 C C   . GLN   B 1 419 ? 14.005  48.807  56.389 1.00 68.28  ? 419 GLN   B C   1 
ATOM   6313 O O   . GLN   B 1 419 ? 13.161  49.652  56.068 1.00 75.94  ? 419 GLN   B O   1 
ATOM   6314 C CB  . GLN   B 1 419 ? 16.411  49.150  55.772 1.00 53.65  ? 419 GLN   B CB  1 
ATOM   6315 C CG  . GLN   B 1 419 ? 17.771  49.719  56.138 1.00 80.72  ? 419 GLN   B CG  1 
ATOM   6316 C CD  . GLN   B 1 419 ? 18.808  49.472  55.062 1.00 89.35  ? 419 GLN   B CD  1 
ATOM   6317 O OE1 . GLN   B 1 419 ? 18.471  49.156  53.922 1.00 82.70  ? 419 GLN   B OE1 1 
ATOM   6318 N NE2 . GLN   B 1 419 ? 20.080  49.608  55.422 1.00 81.30  ? 419 GLN   B NE2 1 
ATOM   6319 N N   . PHE   B 1 420 ? 13.765  47.497  56.311 1.00 69.94  ? 420 PHE   B N   1 
ATOM   6320 C CA  . PHE   B 1 420 ? 12.448  47.010  55.909 1.00 62.29  ? 420 PHE   B CA  1 
ATOM   6321 C C   . PHE   B 1 420 ? 11.373  47.433  56.900 1.00 72.15  ? 420 PHE   B C   1 
ATOM   6322 O O   . PHE   B 1 420 ? 10.272  47.829  56.500 1.00 87.59  ? 420 PHE   B O   1 
ATOM   6323 C CB  . PHE   B 1 420 ? 12.463  45.488  55.774 1.00 60.31  ? 420 PHE   B CB  1 
ATOM   6324 C CG  . PHE   B 1 420 ? 13.106  44.998  54.515 1.00 55.25  ? 420 PHE   B CG  1 
ATOM   6325 C CD1 . PHE   B 1 420 ? 13.870  43.844  54.519 1.00 64.24  ? 420 PHE   B CD1 1 
ATOM   6326 C CD2 . PHE   B 1 420 ? 12.945  45.687  53.327 1.00 46.31  ? 420 PHE   B CD2 1 
ATOM   6327 C CE1 . PHE   B 1 420 ? 14.463  43.388  53.362 1.00 65.83  ? 420 PHE   B CE1 1 
ATOM   6328 C CE2 . PHE   B 1 420 ? 13.537  45.237  52.167 1.00 72.73  ? 420 PHE   B CE2 1 
ATOM   6329 C CZ  . PHE   B 1 420 ? 14.297  44.084  52.184 1.00 77.21  ? 420 PHE   B CZ  1 
ATOM   6330 N N   . GLN   B 1 421 ? 11.674  47.359  58.199 1.00 75.05  ? 421 GLN   B N   1 
ATOM   6331 C CA  . GLN   B 1 421 ? 10.692  47.735  59.212 1.00 84.25  ? 421 GLN   B CA  1 
ATOM   6332 C C   . GLN   B 1 421 ? 10.306  49.205  59.112 1.00 90.01  ? 421 GLN   B C   1 
ATOM   6333 O O   . GLN   B 1 421 ? 9.174   49.572  59.445 1.00 95.53  ? 421 GLN   B O   1 
ATOM   6334 C CB  . GLN   B 1 421 ? 11.226  47.408  60.607 1.00 86.01  ? 421 GLN   B CB  1 
ATOM   6335 C CG  . GLN   B 1 421 ? 10.141  47.112  61.635 1.00 78.80  ? 421 GLN   B CG  1 
ATOM   6336 C CD  . GLN   B 1 421 ? 10.697  46.500  62.907 1.00 86.72  ? 421 GLN   B CD  1 
ATOM   6337 O OE1 . GLN   B 1 421 ? 11.860  46.705  63.251 1.00 89.27  ? 421 GLN   B OE1 1 
ATOM   6338 N NE2 . GLN   B 1 421 ? 9.865   45.740  63.611 1.00 94.72  ? 421 GLN   B NE2 1 
ATOM   6339 N N   . ASN   B 1 422 ? 11.223  50.059  58.669 1.00 86.76  ? 422 ASN   B N   1 
ATOM   6340 C CA  . ASN   B 1 422 ? 10.907  51.468  58.463 1.00 96.75  ? 422 ASN   B CA  1 
ATOM   6341 C C   . ASN   B 1 422 ? 10.357  51.713  57.061 1.00 84.25  ? 422 ASN   B C   1 
ATOM   6342 O O   . ASN   B 1 422 ? 10.670  52.723  56.429 1.00 73.31  ? 422 ASN   B O   1 
ATOM   6343 C CB  . ASN   B 1 422 ? 12.142  52.335  58.705 1.00 84.43  ? 422 ASN   B CB  1 
ATOM   6344 C CG  . ASN   B 1 422 ? 12.596  52.306  60.150 1.00 108.55 ? 422 ASN   B CG  1 
ATOM   6345 O OD1 . ASN   B 1 422 ? 11.821  51.982  61.050 1.00 90.74  ? 422 ASN   B OD1 1 
ATOM   6346 N ND2 . ASN   B 1 422 ? 13.858  52.648  60.381 1.00 111.45 ? 422 ASN   B ND2 1 
HETATM 6347 C C01 . A1AQO C 2 .   ? 5.072   1.368   60.364 1.00 84.08  ? 501 A1AQO A C01 1 
HETATM 6348 C C02 . A1AQO C 2 .   ? 5.192   -0.936  60.193 1.00 91.30  ? 501 A1AQO A C02 1 
HETATM 6349 C C03 . A1AQO C 2 .   ? 6.397   0.987   61.015 1.00 81.94  ? 501 A1AQO A C03 1 
HETATM 6350 C C04 . A1AQO C 2 .   ? 6.519   -0.522  60.827 1.00 86.66  ? 501 A1AQO A C04 1 
HETATM 6351 C C05 . A1AQO C 2 .   ? 6.813   -1.288  62.133 1.00 78.92  ? 501 A1AQO A C05 1 
HETATM 6352 N N01 . A1AQO C 2 .   ? 4.232   0.164   60.384 1.00 84.97  ? 501 A1AQO A N01 1 
HETATM 6353 N N02 . A1AQO C 2 .   ? 8.088   -3.235  62.852 1.00 85.64  ? 501 A1AQO A N02 1 
HETATM 6354 O O01 . A1AQO C 2 .   ? 7.537   -2.434  61.784 1.00 90.99  ? 501 A1AQO A O01 1 
HETATM 6355 N N1  . PLP   D 3 .   ? 9.804   -5.518  66.987 1.00 46.33  ? 502 PLP   A N1  1 
HETATM 6356 C C2  . PLP   D 3 .   ? 10.587  -4.832  66.076 1.00 60.97  ? 502 PLP   A C2  1 
HETATM 6357 C C2A . PLP   D 3 .   ? 12.077  -5.011  66.120 1.00 62.71  ? 502 PLP   A C2A 1 
HETATM 6358 C C3  . PLP   D 3 .   ? 9.983   -3.988  65.132 1.00 72.78  ? 502 PLP   A C3  1 
HETATM 6359 O O3  . PLP   D 3 .   ? 10.771  -3.319  64.239 1.00 77.09  ? 502 PLP   A O3  1 
HETATM 6360 C C4  . PLP   D 3 .   ? 8.585   -3.832  65.123 1.00 74.95  ? 502 PLP   A C4  1 
HETATM 6361 C C4A . PLP   D 3 .   ? 7.931   -2.944  64.094 1.00 67.02  ? 502 PLP   A C4A 1 
HETATM 6362 C C5  . PLP   D 3 .   ? 7.822   -4.557  66.043 1.00 64.44  ? 502 PLP   A C5  1 
HETATM 6363 C C6  . PLP   D 3 .   ? 8.440   -5.379  66.976 1.00 54.52  ? 502 PLP   A C6  1 
HETATM 6364 C C5A . PLP   D 3 .   ? 6.326   -4.453  66.115 1.00 47.23  ? 502 PLP   A C5A 1 
HETATM 6365 O O4P . PLP   D 3 .   ? 5.720   -5.070  65.008 1.00 60.05  ? 502 PLP   A O4P 1 
HETATM 6366 P P   . PLP   D 3 .   ? 4.131   -5.269  65.014 1.00 51.78  ? 502 PLP   A P   1 
HETATM 6367 O O1P . PLP   D 3 .   ? 3.755   -5.640  63.605 1.00 59.01  ? 502 PLP   A O1P 1 
HETATM 6368 O O2P . PLP   D 3 .   ? 3.507   -3.960  65.404 1.00 49.94  ? 502 PLP   A O2P 1 
HETATM 6369 O O3P . PLP   D 3 .   ? 3.824   -6.330  66.040 1.00 51.01  ? 502 PLP   A O3P 1 
HETATM 6370 C C01 . A1AQO E 2 .   ? 3.979   19.111  50.778 1.00 79.64  ? 501 A1AQO B C01 1 
HETATM 6371 C C02 . A1AQO E 2 .   ? 3.325   19.979  48.731 1.00 80.15  ? 501 A1AQO B C02 1 
HETATM 6372 C C03 . A1AQO E 2 .   ? 2.765   19.980  51.082 1.00 84.33  ? 501 A1AQO B C03 1 
HETATM 6373 C C04 . A1AQO E 2 .   ? 2.281   20.481  49.725 1.00 76.08  ? 501 A1AQO B C04 1 
HETATM 6374 C C05 . A1AQO E 2 .   ? 2.099   22.012  49.696 1.00 83.37  ? 501 A1AQO B C05 1 
HETATM 6375 N N01 . A1AQO E 2 .   ? 4.518   19.582  49.495 1.00 84.55  ? 501 A1AQO B N01 1 
HETATM 6376 N N02 . A1AQO E 2 .   ? 0.240   23.585  49.454 1.00 97.65  ? 501 A1AQO B N02 1 
HETATM 6377 O O01 . A1AQO E 2 .   ? 0.720   22.240  49.659 1.00 109.60 ? 501 A1AQO B O01 1 
HETATM 6378 N N1  . PLP   F 3 .   ? -0.777  28.522  49.032 1.00 66.36  ? 502 PLP   B N1  1 
HETATM 6379 C C2  . PLP   F 3 .   ? -1.586  27.401  49.021 1.00 60.06  ? 502 PLP   B C2  1 
HETATM 6380 C C2A . PLP   F 3 .   ? -3.073  27.570  48.917 1.00 72.61  ? 502 PLP   B C2A 1 
HETATM 6381 C C3  . PLP   F 3 .   ? -1.020  26.124  49.104 1.00 68.42  ? 502 PLP   B C3  1 
HETATM 6382 O O3  . PLP   F 3 .   ? -1.887  25.068  49.085 1.00 72.11  ? 502 PLP   B O3  1 
HETATM 6383 C C4  . PLP   F 3 .   ? 0.383   25.977  49.201 1.00 72.06  ? 502 PLP   B C4  1 
HETATM 6384 C C4A . PLP   F 3 .   ? 1.009   24.599  49.291 1.00 77.36  ? 502 PLP   B C4A 1 
HETATM 6385 C C5  . PLP   F 3 .   ? 1.168   27.138  49.204 1.00 61.01  ? 502 PLP   B C5  1 
HETATM 6386 C C6  . PLP   F 3 .   ? 0.582   28.393  49.126 1.00 60.07  ? 502 PLP   B C6  1 
HETATM 6387 C C5A . PLP   F 3 .   ? 2.664   27.133  49.311 1.00 54.82  ? 502 PLP   B C5A 1 
HETATM 6388 O O4P . PLP   F 3 .   ? 3.244   26.574  48.160 1.00 49.28  ? 502 PLP   B O4P 1 
HETATM 6389 P P   . PLP   F 3 .   ? 4.822   26.733  47.941 1.00 55.57  ? 502 PLP   B P   1 
HETATM 6390 O O1P . PLP   F 3 .   ? 5.176   25.801  46.818 1.00 55.76  ? 502 PLP   B O1P 1 
HETATM 6391 O O2P . PLP   F 3 .   ? 5.506   26.318  49.214 1.00 57.92  ? 502 PLP   B O2P 1 
HETATM 6392 O O3P . PLP   F 3 .   ? 5.102   28.185  47.649 1.00 55.84  ? 502 PLP   B O3P 1 
HETATM 6393 O O   . HOH   G 4 .   ? -17.985 4.247   42.620 1.00 71.00  ? 601 HOH   A O   1 
HETATM 6394 O O   . HOH   G 4 .   ? 5.021   10.103  70.283 1.00 69.26  ? 602 HOH   A O   1 
HETATM 6395 O O   . HOH   G 4 .   ? -0.048  -8.078  93.873 1.00 81.10  ? 603 HOH   A O   1 
HETATM 6396 O O   . HOH   G 4 .   ? -2.344  1.861   52.030 1.00 77.53  ? 604 HOH   A O   1 
HETATM 6397 O O   . HOH   G 4 .   ? 20.784  -8.084  47.652 1.00 64.89  ? 605 HOH   A O   1 
HETATM 6398 O O   . HOH   G 4 .   ? -5.856  7.944   48.660 1.00 53.91  ? 606 HOH   A O   1 
HETATM 6399 O O   . HOH   G 4 .   ? 17.300  13.122  80.245 1.00 66.94  ? 607 HOH   A O   1 
HETATM 6400 O O   . HOH   H 4 .   ? 4.503   22.447  63.552 1.00 63.60  ? 601 HOH   B O   1 
HETATM 6401 O O   . HOH   H 4 .   ? -18.663 30.971  31.211 1.00 57.64  ? 602 HOH   B O   1 
HETATM 6402 O O   . HOH   H 4 .   ? -20.772 32.981  29.503 1.00 54.09  ? 603 HOH   B O   1 
HETATM 6403 O O   . HOH   H 4 .   ? 0.163   47.333  40.648 1.00 57.80  ? 604 HOH   B O   1 
HETATM 6404 O O   . HOH   H 4 .   ? 14.373  1.563   46.157 1.00 68.28  ? 605 HOH   B O   1 
HETATM 6405 O O   . HOH   H 4 .   ? 11.389  11.835  46.700 1.00 59.29  ? 606 HOH   B O   1 
HETATM 6406 O O   . HOH   H 4 .   ? -26.131 38.666  58.762 1.00 59.50  ? 607 HOH   B O   1 
HETATM 6407 O O   . HOH   H 4 .   ? 34.899  9.638   63.203 1.00 62.72  ? 608 HOH   B O   1 
HETATM 6408 O O   . HOH   H 4 .   ? -17.960 29.473  29.754 1.00 58.31  ? 609 HOH   B O   1 
# 
