data_8YY7
# 
_entry.id   8YY7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8YY7         pdb_00008yy7 10.2210/pdb8yy7/pdb 
WWPDB D_1300046633 ?            ?                   
# 
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 
1 'Structure model' 1 0 2024-11-20 
2 'Structure model' 1 1 2024-11-27 
3 'Structure model' 1 2 2025-01-22 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' '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 
3 3 'Structure model' citation        
4 3 '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.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
4 2 'Structure model' '_citation_author.name'             
5 3 'Structure model' '_citation.page_first'              
6 3 'Structure model' '_citation.page_last'               
7 3 '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                        8YY7 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_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 
3 zhengyu.zhang@whu.edu.cn Zhengyu Zhang ? 'principal investigator/group leader' 0000-0001-5035-1229 
4 quxd19@sjtu.edu.cn       Xudong  Qu    ? 'principal investigator/group leader' 0000-0002-3301-8536 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhang, Z.Y.' 1 ? 
'Qu, X.D.'    2 ? 
'Duan, B.R.'  3 ? 
'Wei, G.Z.'   4 ? 
# 
_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            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            121 
_citation.language                  ? 
_citation.page_first                e2412890121 
_citation.page_last                 e2412890121 
_citation.title                     
'A nucleobase-driven P450 peroxidase system enables regio- and stereo-specific formation of C&#9472;C and C&#9472;N bonds.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2412890121 
_citation.pdbx_database_id_PubMed   39508763 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wei, G.'    1  0000-0002-5967-3168 
primary 'Duan, B.'   2  0000-0002-1043-502X 
primary 'Zhou, T.P.' 3  ?                   
primary 'Tian, W.'   4  ?                   
primary 'Sun, C.'    5  ?                   
primary 'Lin, Z.'    6  0009-0005-2240-449X 
primary 'Deng, Z.'   7  ?                   
primary 'Wang, B.'   8  0000-0002-3353-9411 
primary 'Zhang, Z.'  9  ?                   
primary 'Qu, X.'     10 0000-0002-3301-8536 
# 
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 PtmB                                                         45299.418 2   ? ? ? 
;Sequence reference for Kitasatospora medicidica KCTC 9733 strain (TAX ID 1449347) is not available in UniProt at the time of biocuration. Kitasatospora medicidica KCTC 9733: NCBI RefSeq assembly is GCF_000744225.1 and GenBank assembly is GCA_000744225.1.
;
2 non-polymer syn '(3S,6S)-3,6-bis[(1H-indol-3-yl)methyl]piperazine-2,5-dione' 372.420   2   ? ? ? ? 
3 non-polymer syn HYPOXANTHINE                                                 136.111   2   ? ? ? ? 
4 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                            616.487   2   ? ? ? ? 
5 water       nat water                                                        18.015    677 ? ? ? ? 
# 
_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       
;MTTTAQRDPVLPGTAHHPPLPDFPLSRRGDILPAEAERLRAEQPVARVRTMTGDEAWLVSSYELAKQVLEDDRFSLKDTA
NPGVPRQYALTIPPEVVNNMGNINSAGLRNAVMKTLSPQADRELGGWLEAQAHQLLDRLIEQGPPADLRDGFTEPYSAAL
HCRLLGIPTDDWRRLMSGIDVAFITSPRTFEGSAVNWYKDLGYMVDRLNADPEPTEGLLGRFAELRRSPDVSDQVSDELL
ATVALSLFGAGAVSTSAFLQHAIIALAQQPELADRLRAEPAVIGRAVDELLRYNLSIGDALPRIALADVRLGEVEIRAGE
LVLVLIEGANYDPAVFPHPERIDFDRESNPHLAFGGGQHFCPASALGRTHAEIALTALVEKLPALRLALPVEQLAWRPGF
IKRLPERLPVLW
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTTTAQRDPVLPGTAHHPPLPDFPLSRRGDILPAEAERLRAEQPVARVRTMTGDEAWLVSSYELAKQVLEDDRFSLKDTA
NPGVPRQYALTIPPEVVNNMGNINSAGLRNAVMKTLSPQADRELGGWLEAQAHQLLDRLIEQGPPADLRDGFTEPYSAAL
HCRLLGIPTDDWRRLMSGIDVAFITSPRTFEGSAVNWYKDLGYMVDRLNADPEPTEGLLGRFAELRRSPDVSDQVSDELL
ATVALSLFGAGAVSTSAFLQHAIIALAQQPELADRLRAEPAVIGRAVDELLRYNLSIGDALPRIALADVRLGEVEIRAGE
LVLVLIEGANYDPAVFPHPERIDFDRESNPHLAFGGGQHFCPASALGRTHAEIALTALVEKLPALRLALPVEQLAWRPGF
IKRLPERLPVLW
;
_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 '(3S,6S)-3,6-bis[(1H-indol-3-yl)methyl]piperazine-2,5-dione' UYM 
3 HYPOXANTHINE                                                 HPA 
4 'PROTOPORPHYRIN IX CONTAINING FE'                            HEM 
5 water                                                        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   THR n 
1 3   THR n 
1 4   THR n 
1 5   ALA n 
1 6   GLN n 
1 7   ARG n 
1 8   ASP n 
1 9   PRO n 
1 10  VAL n 
1 11  LEU n 
1 12  PRO n 
1 13  GLY n 
1 14  THR n 
1 15  ALA n 
1 16  HIS n 
1 17  HIS n 
1 18  PRO n 
1 19  PRO n 
1 20  LEU n 
1 21  PRO n 
1 22  ASP n 
1 23  PHE n 
1 24  PRO n 
1 25  LEU n 
1 26  SER n 
1 27  ARG n 
1 28  ARG n 
1 29  GLY n 
1 30  ASP n 
1 31  ILE n 
1 32  LEU n 
1 33  PRO n 
1 34  ALA n 
1 35  GLU n 
1 36  ALA n 
1 37  GLU n 
1 38  ARG n 
1 39  LEU n 
1 40  ARG n 
1 41  ALA n 
1 42  GLU n 
1 43  GLN n 
1 44  PRO n 
1 45  VAL n 
1 46  ALA n 
1 47  ARG n 
1 48  VAL n 
1 49  ARG n 
1 50  THR n 
1 51  MET n 
1 52  THR n 
1 53  GLY n 
1 54  ASP n 
1 55  GLU n 
1 56  ALA n 
1 57  TRP n 
1 58  LEU n 
1 59  VAL n 
1 60  SER n 
1 61  SER n 
1 62  TYR n 
1 63  GLU n 
1 64  LEU n 
1 65  ALA n 
1 66  LYS n 
1 67  GLN n 
1 68  VAL n 
1 69  LEU n 
1 70  GLU n 
1 71  ASP n 
1 72  ASP n 
1 73  ARG n 
1 74  PHE n 
1 75  SER n 
1 76  LEU n 
1 77  LYS n 
1 78  ASP n 
1 79  THR n 
1 80  ALA n 
1 81  ASN n 
1 82  PRO n 
1 83  GLY n 
1 84  VAL n 
1 85  PRO n 
1 86  ARG n 
1 87  GLN n 
1 88  TYR n 
1 89  ALA n 
1 90  LEU n 
1 91  THR n 
1 92  ILE n 
1 93  PRO n 
1 94  PRO n 
1 95  GLU n 
1 96  VAL n 
1 97  VAL n 
1 98  ASN n 
1 99  ASN n 
1 100 MET n 
1 101 GLY n 
1 102 ASN n 
1 103 ILE n 
1 104 ASN n 
1 105 SER n 
1 106 ALA n 
1 107 GLY n 
1 108 LEU n 
1 109 ARG n 
1 110 ASN n 
1 111 ALA n 
1 112 VAL n 
1 113 MET n 
1 114 LYS n 
1 115 THR n 
1 116 LEU n 
1 117 SER n 
1 118 PRO n 
1 119 GLN n 
1 120 ALA n 
1 121 ASP n 
1 122 ARG n 
1 123 GLU n 
1 124 LEU n 
1 125 GLY n 
1 126 GLY n 
1 127 TRP n 
1 128 LEU n 
1 129 GLU n 
1 130 ALA n 
1 131 GLN n 
1 132 ALA n 
1 133 HIS n 
1 134 GLN n 
1 135 LEU n 
1 136 LEU n 
1 137 ASP n 
1 138 ARG n 
1 139 LEU n 
1 140 ILE n 
1 141 GLU n 
1 142 GLN n 
1 143 GLY n 
1 144 PRO n 
1 145 PRO n 
1 146 ALA n 
1 147 ASP n 
1 148 LEU n 
1 149 ARG n 
1 150 ASP n 
1 151 GLY n 
1 152 PHE n 
1 153 THR n 
1 154 GLU n 
1 155 PRO n 
1 156 TYR n 
1 157 SER n 
1 158 ALA n 
1 159 ALA n 
1 160 LEU n 
1 161 HIS n 
1 162 CYS n 
1 163 ARG n 
1 164 LEU n 
1 165 LEU n 
1 166 GLY n 
1 167 ILE n 
1 168 PRO n 
1 169 THR n 
1 170 ASP n 
1 171 ASP n 
1 172 TRP n 
1 173 ARG n 
1 174 ARG n 
1 175 LEU n 
1 176 MET n 
1 177 SER n 
1 178 GLY n 
1 179 ILE n 
1 180 ASP n 
1 181 VAL n 
1 182 ALA n 
1 183 PHE n 
1 184 ILE n 
1 185 THR n 
1 186 SER n 
1 187 PRO n 
1 188 ARG n 
1 189 THR n 
1 190 PHE n 
1 191 GLU n 
1 192 GLY n 
1 193 SER n 
1 194 ALA n 
1 195 VAL n 
1 196 ASN n 
1 197 TRP n 
1 198 TYR n 
1 199 LYS n 
1 200 ASP n 
1 201 LEU n 
1 202 GLY n 
1 203 TYR n 
1 204 MET n 
1 205 VAL n 
1 206 ASP n 
1 207 ARG n 
1 208 LEU n 
1 209 ASN n 
1 210 ALA n 
1 211 ASP n 
1 212 PRO n 
1 213 GLU n 
1 214 PRO n 
1 215 THR n 
1 216 GLU n 
1 217 GLY n 
1 218 LEU n 
1 219 LEU n 
1 220 GLY n 
1 221 ARG n 
1 222 PHE n 
1 223 ALA n 
1 224 GLU n 
1 225 LEU n 
1 226 ARG n 
1 227 ARG n 
1 228 SER n 
1 229 PRO n 
1 230 ASP n 
1 231 VAL n 
1 232 SER n 
1 233 ASP n 
1 234 GLN n 
1 235 VAL n 
1 236 SER n 
1 237 ASP n 
1 238 GLU n 
1 239 LEU n 
1 240 LEU n 
1 241 ALA n 
1 242 THR n 
1 243 VAL n 
1 244 ALA n 
1 245 LEU n 
1 246 SER n 
1 247 LEU n 
1 248 PHE n 
1 249 GLY n 
1 250 ALA n 
1 251 GLY n 
1 252 ALA n 
1 253 VAL n 
1 254 SER n 
1 255 THR n 
1 256 SER n 
1 257 ALA n 
1 258 PHE n 
1 259 LEU n 
1 260 GLN n 
1 261 HIS n 
1 262 ALA n 
1 263 ILE n 
1 264 ILE n 
1 265 ALA n 
1 266 LEU n 
1 267 ALA n 
1 268 GLN n 
1 269 GLN n 
1 270 PRO n 
1 271 GLU n 
1 272 LEU n 
1 273 ALA n 
1 274 ASP n 
1 275 ARG n 
1 276 LEU n 
1 277 ARG n 
1 278 ALA n 
1 279 GLU n 
1 280 PRO n 
1 281 ALA n 
1 282 VAL n 
1 283 ILE n 
1 284 GLY n 
1 285 ARG n 
1 286 ALA n 
1 287 VAL n 
1 288 ASP n 
1 289 GLU n 
1 290 LEU n 
1 291 LEU n 
1 292 ARG n 
1 293 TYR n 
1 294 ASN n 
1 295 LEU n 
1 296 SER n 
1 297 ILE n 
1 298 GLY n 
1 299 ASP n 
1 300 ALA n 
1 301 LEU n 
1 302 PRO n 
1 303 ARG n 
1 304 ILE n 
1 305 ALA n 
1 306 LEU n 
1 307 ALA n 
1 308 ASP n 
1 309 VAL n 
1 310 ARG n 
1 311 LEU n 
1 312 GLY n 
1 313 GLU n 
1 314 VAL n 
1 315 GLU n 
1 316 ILE n 
1 317 ARG n 
1 318 ALA n 
1 319 GLY n 
1 320 GLU n 
1 321 LEU n 
1 322 VAL n 
1 323 LEU n 
1 324 VAL n 
1 325 LEU n 
1 326 ILE n 
1 327 GLU n 
1 328 GLY n 
1 329 ALA n 
1 330 ASN n 
1 331 TYR n 
1 332 ASP n 
1 333 PRO n 
1 334 ALA n 
1 335 VAL n 
1 336 PHE n 
1 337 PRO n 
1 338 HIS n 
1 339 PRO n 
1 340 GLU n 
1 341 ARG n 
1 342 ILE n 
1 343 ASP n 
1 344 PHE n 
1 345 ASP n 
1 346 ARG n 
1 347 GLU n 
1 348 SER n 
1 349 ASN n 
1 350 PRO n 
1 351 HIS n 
1 352 LEU n 
1 353 ALA n 
1 354 PHE n 
1 355 GLY n 
1 356 GLY n 
1 357 GLY n 
1 358 GLN n 
1 359 HIS n 
1 360 PHE n 
1 361 CYS n 
1 362 PRO n 
1 363 ALA n 
1 364 SER n 
1 365 ALA n 
1 366 LEU n 
1 367 GLY n 
1 368 ARG n 
1 369 THR n 
1 370 HIS n 
1 371 ALA n 
1 372 GLU n 
1 373 ILE n 
1 374 ALA n 
1 375 LEU n 
1 376 THR n 
1 377 ALA n 
1 378 LEU n 
1 379 VAL n 
1 380 GLU n 
1 381 LYS n 
1 382 LEU n 
1 383 PRO n 
1 384 ALA n 
1 385 LEU n 
1 386 ARG n 
1 387 LEU n 
1 388 ALA n 
1 389 LEU n 
1 390 PRO n 
1 391 VAL n 
1 392 GLU n 
1 393 GLN n 
1 394 LEU n 
1 395 ALA n 
1 396 TRP n 
1 397 ARG n 
1 398 PRO n 
1 399 GLY n 
1 400 PHE n 
1 401 ILE n 
1 402 LYS n 
1 403 ARG n 
1 404 LEU n 
1 405 PRO n 
1 406 GLU n 
1 407 ARG n 
1 408 LEU n 
1 409 PRO n 
1 410 VAL n 
1 411 LEU n 
1 412 TRP 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                   412 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Kitasatospora mediocidica KCTC 9733' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1449347 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                      ?    'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                                                     ?    'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                   ?    'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                              ?    'C4 H7 N O4'       133.103 
CYS 'L-peptide linking' y CYSTEINE                                                     ?    'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                    ?    'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                              ?    'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                                                      ?    'C2 H5 N O2'       75.067  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                            HEME 'C34 H32 Fe N4 O4' 616.487 
HIS 'L-peptide linking' y HISTIDINE                                                    ?    'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                                                        ?    'H2 O'             18.015  
HPA non-polymer         . HYPOXANTHINE                                                 ?    'C5 H4 N4 O'       136.111 
ILE 'L-peptide linking' y ISOLEUCINE                                                   ?    'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                                                      ?    'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                                                       ?    'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                                                   ?    'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                ?    'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                                                      ?    'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                                                       ?    'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                                                    ?    'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                   ?    'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                                                     ?    'C9 H11 N O3'      181.189 
UYM non-polymer         . '(3S,6S)-3,6-bis[(1H-indol-3-yl)methyl]piperazine-2,5-dione' ?    'C22 H20 N4 O2'    372.420 
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   THR 2   2   ?   ?   ?   A . n 
A 1 3   THR 3   3   ?   ?   ?   A . n 
A 1 4   THR 4   4   ?   ?   ?   A . n 
A 1 5   ALA 5   5   ?   ?   ?   A . n 
A 1 6   GLN 6   6   ?   ?   ?   A . n 
A 1 7   ARG 7   7   ?   ?   ?   A . n 
A 1 8   ASP 8   8   ?   ?   ?   A . n 
A 1 9   PRO 9   9   ?   ?   ?   A . n 
A 1 10  VAL 10  10  ?   ?   ?   A . n 
A 1 11  LEU 11  11  ?   ?   ?   A . n 
A 1 12  PRO 12  12  ?   ?   ?   A . n 
A 1 13  GLY 13  13  ?   ?   ?   A . n 
A 1 14  THR 14  14  ?   ?   ?   A . n 
A 1 15  ALA 15  15  ?   ?   ?   A . n 
A 1 16  HIS 16  16  ?   ?   ?   A . n 
A 1 17  HIS 17  17  ?   ?   ?   A . n 
A 1 18  PRO 18  18  ?   ?   ?   A . n 
A 1 19  PRO 19  19  19  PRO PRO A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  PHE 23  23  23  PHE PHE A . n 
A 1 24  PRO 24  24  24  PRO PRO A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  ASP 30  30  30  ASP ASP A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  MET 51  51  51  MET MET A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  TRP 57  57  57  TRP TRP A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  TYR 62  62  62  TYR TYR A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  LYS 66  66  66  LYS LYS A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  GLU 70  70  70  GLU GLU A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  ASN 81  81  81  ASN ASN A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  ARG 86  86  86  ARG ARG A . n 
A 1 87  GLN 87  87  87  GLN GLN A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  PRO 94  94  94  PRO PRO A . n 
A 1 95  GLU 95  95  95  GLU GLU A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 MET 100 100 100 MET MET A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 ASN 104 104 104 ASN ASN A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 MET 113 113 113 MET MET A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 THR 115 115 115 THR THR A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 PRO 118 118 118 PRO PRO A . n 
A 1 119 GLN 119 119 119 GLN GLN A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 GLY 126 126 126 GLY GLY A . n 
A 1 127 TRP 127 127 127 TRP TRP A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 HIS 133 133 133 HIS HIS A . n 
A 1 134 GLN 134 134 134 GLN GLN A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 ASP 137 137 137 ASP ASP A . n 
A 1 138 ARG 138 138 138 ARG ARG A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 GLN 142 142 142 GLN GLN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 PRO 144 144 144 PRO PRO A . n 
A 1 145 PRO 145 145 145 PRO PRO A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 ARG 149 149 149 ARG ARG A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 TYR 156 156 156 TYR TYR A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 CYS 162 162 162 CYS CYS A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 GLY 166 166 166 GLY GLY A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 ASP 170 170 170 ASP ASP A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 TRP 172 172 172 TRP TRP A . n 
A 1 173 ARG 173 173 173 ARG ARG A . n 
A 1 174 ARG 174 174 174 ARG ARG A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 MET 176 176 176 MET MET A . n 
A 1 177 SER 177 177 177 SER SER A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 ASP 180 180 180 ASP ASP A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 PHE 183 183 183 PHE PHE A . n 
A 1 184 ILE 184 184 184 ILE ILE A . n 
A 1 185 THR 185 185 185 THR THR A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 PRO 187 187 187 PRO PRO A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 PHE 190 190 190 PHE PHE A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 GLY 192 192 192 GLY GLY A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 ASN 196 196 196 ASN ASN A . n 
A 1 197 TRP 197 197 197 TRP TRP A . n 
A 1 198 TYR 198 198 198 TYR TYR A . n 
A 1 199 LYS 199 199 199 LYS LYS A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 TYR 203 203 203 TYR TYR A . n 
A 1 204 MET 204 204 204 MET MET A . n 
A 1 205 VAL 205 205 205 VAL VAL A . n 
A 1 206 ASP 206 206 206 ASP ASP A . n 
A 1 207 ARG 207 207 207 ARG ARG A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 ASN 209 209 209 ASN ASN A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ASP 211 211 211 ASP ASP A . n 
A 1 212 PRO 212 212 212 PRO PRO A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 THR 215 215 215 THR THR A . n 
A 1 216 GLU 216 216 216 GLU GLU A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 ARG 221 221 221 ARG ARG A . n 
A 1 222 PHE 222 222 222 PHE PHE 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 LEU 225 225 225 LEU LEU A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 SER 228 228 228 SER SER A . n 
A 1 229 PRO 229 229 ?   ?   ?   A . n 
A 1 230 ASP 230 230 ?   ?   ?   A . n 
A 1 231 VAL 231 231 ?   ?   ?   A . n 
A 1 232 SER 232 232 ?   ?   ?   A . n 
A 1 233 ASP 233 233 ?   ?   ?   A . n 
A 1 234 GLN 234 234 ?   ?   ?   A . n 
A 1 235 VAL 235 235 235 VAL VAL A . n 
A 1 236 SER 236 236 236 SER SER A . n 
A 1 237 ASP 237 237 237 ASP ASP A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 THR 242 242 242 THR THR A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 LEU 247 247 247 LEU LEU A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 GLY 249 249 249 GLY GLY A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 ALA 252 252 252 ALA ALA A . n 
A 1 253 VAL 253 253 253 VAL VAL A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 THR 255 255 255 THR THR A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 PHE 258 258 258 PHE PHE A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 GLN 260 260 260 GLN GLN A . n 
A 1 261 HIS 261 261 261 HIS HIS A . n 
A 1 262 ALA 262 262 262 ALA ALA A . n 
A 1 263 ILE 263 263 263 ILE ILE A . n 
A 1 264 ILE 264 264 264 ILE ILE A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 ALA 267 267 267 ALA ALA A . n 
A 1 268 GLN 268 268 268 GLN GLN A . n 
A 1 269 GLN 269 269 269 GLN GLN A . n 
A 1 270 PRO 270 270 270 PRO PRO A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 ASP 274 274 274 ASP ASP A . n 
A 1 275 ARG 275 275 275 ARG ARG A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 ARG 277 277 277 ARG ARG A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 PRO 280 280 280 PRO PRO A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 VAL 282 282 282 VAL VAL A . n 
A 1 283 ILE 283 283 283 ILE ILE A . n 
A 1 284 GLY 284 284 284 GLY GLY A . n 
A 1 285 ARG 285 285 285 ARG ARG A . n 
A 1 286 ALA 286 286 286 ALA ALA A . n 
A 1 287 VAL 287 287 287 VAL VAL A . n 
A 1 288 ASP 288 288 288 ASP ASP A . n 
A 1 289 GLU 289 289 289 GLU GLU A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 LEU 291 291 291 LEU LEU A . n 
A 1 292 ARG 292 292 292 ARG ARG A . n 
A 1 293 TYR 293 293 293 TYR TYR A . n 
A 1 294 ASN 294 294 294 ASN ASN A . n 
A 1 295 LEU 295 295 295 LEU LEU A . n 
A 1 296 SER 296 296 296 SER SER A . n 
A 1 297 ILE 297 297 297 ILE ILE A . n 
A 1 298 GLY 298 298 298 GLY GLY A . n 
A 1 299 ASP 299 299 299 ASP ASP A . n 
A 1 300 ALA 300 300 300 ALA ALA A . n 
A 1 301 LEU 301 301 301 LEU LEU A . n 
A 1 302 PRO 302 302 302 PRO PRO A . n 
A 1 303 ARG 303 303 303 ARG ARG A . n 
A 1 304 ILE 304 304 304 ILE ILE A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 ALA 307 307 307 ALA ALA A . n 
A 1 308 ASP 308 308 308 ASP ASP A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 ARG 310 310 310 ARG ARG A . n 
A 1 311 LEU 311 311 311 LEU LEU A . n 
A 1 312 GLY 312 312 312 GLY GLY A . n 
A 1 313 GLU 313 313 313 GLU GLU A . n 
A 1 314 VAL 314 314 314 VAL VAL A . n 
A 1 315 GLU 315 315 315 GLU GLU A . n 
A 1 316 ILE 316 316 316 ILE ILE A . n 
A 1 317 ARG 317 317 317 ARG ARG A . n 
A 1 318 ALA 318 318 318 ALA ALA A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 LEU 321 321 321 LEU LEU A . n 
A 1 322 VAL 322 322 322 VAL VAL A . n 
A 1 323 LEU 323 323 323 LEU LEU A . n 
A 1 324 VAL 324 324 324 VAL VAL A . n 
A 1 325 LEU 325 325 325 LEU LEU A . n 
A 1 326 ILE 326 326 326 ILE ILE A . n 
A 1 327 GLU 327 327 327 GLU GLU A . n 
A 1 328 GLY 328 328 328 GLY GLY A . n 
A 1 329 ALA 329 329 329 ALA ALA A . n 
A 1 330 ASN 330 330 330 ASN ASN 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 PRO 333 333 333 PRO PRO A . n 
A 1 334 ALA 334 334 334 ALA ALA A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 PHE 336 336 336 PHE PHE A . n 
A 1 337 PRO 337 337 337 PRO PRO A . n 
A 1 338 HIS 338 338 338 HIS HIS A . n 
A 1 339 PRO 339 339 339 PRO PRO A . n 
A 1 340 GLU 340 340 340 GLU GLU A . n 
A 1 341 ARG 341 341 341 ARG ARG A . n 
A 1 342 ILE 342 342 342 ILE ILE A . n 
A 1 343 ASP 343 343 343 ASP ASP A . n 
A 1 344 PHE 344 344 344 PHE PHE A . n 
A 1 345 ASP 345 345 345 ASP ASP A . n 
A 1 346 ARG 346 346 346 ARG ARG A . n 
A 1 347 GLU 347 347 347 GLU GLU A . n 
A 1 348 SER 348 348 348 SER SER A . n 
A 1 349 ASN 349 349 349 ASN ASN A . n 
A 1 350 PRO 350 350 350 PRO PRO A . n 
A 1 351 HIS 351 351 351 HIS HIS A . n 
A 1 352 LEU 352 352 352 LEU LEU A . n 
A 1 353 ALA 353 353 353 ALA ALA A . n 
A 1 354 PHE 354 354 354 PHE PHE A . n 
A 1 355 GLY 355 355 355 GLY GLY A . n 
A 1 356 GLY 356 356 356 GLY GLY A . n 
A 1 357 GLY 357 357 357 GLY GLY A . n 
A 1 358 GLN 358 358 358 GLN GLN A . n 
A 1 359 HIS 359 359 359 HIS HIS A . n 
A 1 360 PHE 360 360 360 PHE PHE A . n 
A 1 361 CYS 361 361 361 CYS CYS A . n 
A 1 362 PRO 362 362 362 PRO PRO A . n 
A 1 363 ALA 363 363 363 ALA ALA A . n 
A 1 364 SER 364 364 364 SER SER A . n 
A 1 365 ALA 365 365 365 ALA ALA A . n 
A 1 366 LEU 366 366 366 LEU LEU A . n 
A 1 367 GLY 367 367 367 GLY GLY A . n 
A 1 368 ARG 368 368 368 ARG ARG A . n 
A 1 369 THR 369 369 369 THR THR A . n 
A 1 370 HIS 370 370 370 HIS HIS A . n 
A 1 371 ALA 371 371 371 ALA ALA A . n 
A 1 372 GLU 372 372 372 GLU GLU A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 ALA 374 374 374 ALA ALA A . n 
A 1 375 LEU 375 375 375 LEU LEU A . n 
A 1 376 THR 376 376 376 THR THR A . n 
A 1 377 ALA 377 377 377 ALA ALA A . n 
A 1 378 LEU 378 378 378 LEU LEU A . n 
A 1 379 VAL 379 379 379 VAL VAL A . n 
A 1 380 GLU 380 380 380 GLU GLU A . n 
A 1 381 LYS 381 381 381 LYS LYS A . n 
A 1 382 LEU 382 382 382 LEU LEU A . n 
A 1 383 PRO 383 383 383 PRO PRO A . n 
A 1 384 ALA 384 384 384 ALA ALA A . n 
A 1 385 LEU 385 385 385 LEU LEU A . n 
A 1 386 ARG 386 386 386 ARG ARG A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 ALA 388 388 388 ALA ALA A . n 
A 1 389 LEU 389 389 389 LEU LEU A . n 
A 1 390 PRO 390 390 390 PRO PRO A . n 
A 1 391 VAL 391 391 391 VAL VAL A . n 
A 1 392 GLU 392 392 392 GLU GLU A . n 
A 1 393 GLN 393 393 393 GLN GLN A . n 
A 1 394 LEU 394 394 394 LEU LEU A . n 
A 1 395 ALA 395 395 395 ALA ALA A . n 
A 1 396 TRP 396 396 396 TRP TRP A . n 
A 1 397 ARG 397 397 397 ARG ARG A . n 
A 1 398 PRO 398 398 398 PRO PRO 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 ILE 401 401 401 ILE ILE A . n 
A 1 402 LYS 402 402 402 LYS LYS A . n 
A 1 403 ARG 403 403 403 ARG ARG A . n 
A 1 404 LEU 404 404 404 LEU LEU A . n 
A 1 405 PRO 405 405 405 PRO PRO A . n 
A 1 406 GLU 406 406 406 GLU GLU A . n 
A 1 407 ARG 407 407 407 ARG ARG A . n 
A 1 408 LEU 408 408 408 LEU LEU A . n 
A 1 409 PRO 409 409 409 PRO PRO A . n 
A 1 410 VAL 410 410 410 VAL VAL A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 TRP 412 412 412 TRP TRP A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   THR 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   ?   ?   ?   B . n 
B 1 4   THR 4   4   ?   ?   ?   B . n 
B 1 5   ALA 5   5   ?   ?   ?   B . n 
B 1 6   GLN 6   6   ?   ?   ?   B . n 
B 1 7   ARG 7   7   ?   ?   ?   B . n 
B 1 8   ASP 8   8   ?   ?   ?   B . n 
B 1 9   PRO 9   9   ?   ?   ?   B . n 
B 1 10  VAL 10  10  ?   ?   ?   B . n 
B 1 11  LEU 11  11  ?   ?   ?   B . n 
B 1 12  PRO 12  12  ?   ?   ?   B . n 
B 1 13  GLY 13  13  ?   ?   ?   B . n 
B 1 14  THR 14  14  ?   ?   ?   B . n 
B 1 15  ALA 15  15  ?   ?   ?   B . n 
B 1 16  HIS 16  16  ?   ?   ?   B . n 
B 1 17  HIS 17  17  ?   ?   ?   B . n 
B 1 18  PRO 18  18  ?   ?   ?   B . n 
B 1 19  PRO 19  19  19  PRO PRO B . n 
B 1 20  LEU 20  20  20  LEU LEU B . n 
B 1 21  PRO 21  21  21  PRO PRO B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  PHE 23  23  23  PHE PHE B . n 
B 1 24  PRO 24  24  24  PRO PRO B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  SER 26  26  26  SER SER B . n 
B 1 27  ARG 27  27  27  ARG ARG B . n 
B 1 28  ARG 28  28  28  ARG ARG B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  ASP 30  30  30  ASP ASP B . n 
B 1 31  ILE 31  31  31  ILE ILE B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  PRO 33  33  33  PRO PRO B . n 
B 1 34  ALA 34  34  34  ALA ALA B . n 
B 1 35  GLU 35  35  35  GLU GLU B . n 
B 1 36  ALA 36  36  36  ALA ALA B . n 
B 1 37  GLU 37  37  37  GLU GLU B . n 
B 1 38  ARG 38  38  38  ARG ARG B . n 
B 1 39  LEU 39  39  39  LEU LEU B . n 
B 1 40  ARG 40  40  40  ARG ARG B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  GLN 43  43  43  GLN GLN B . n 
B 1 44  PRO 44  44  44  PRO PRO B . n 
B 1 45  VAL 45  45  45  VAL VAL B . n 
B 1 46  ALA 46  46  46  ALA ALA B . n 
B 1 47  ARG 47  47  47  ARG ARG B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  ARG 49  49  49  ARG ARG B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  MET 51  51  51  MET MET B . n 
B 1 52  THR 52  52  52  THR THR B . n 
B 1 53  GLY 53  53  53  GLY GLY B . n 
B 1 54  ASP 54  54  54  ASP ASP B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  TRP 57  57  57  TRP TRP B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  SER 60  60  60  SER SER B . n 
B 1 61  SER 61  61  61  SER SER B . n 
B 1 62  TYR 62  62  62  TYR TYR B . n 
B 1 63  GLU 63  63  63  GLU GLU B . n 
B 1 64  LEU 64  64  64  LEU LEU B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  LYS 66  66  66  LYS LYS B . n 
B 1 67  GLN 67  67  67  GLN GLN B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  LEU 69  69  69  LEU LEU B . n 
B 1 70  GLU 70  70  70  GLU GLU B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  ARG 73  73  73  ARG ARG B . n 
B 1 74  PHE 74  74  74  PHE PHE B . n 
B 1 75  SER 75  75  75  SER SER B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  LYS 77  77  77  LYS LYS B . n 
B 1 78  ASP 78  78  78  ASP ASP B . n 
B 1 79  THR 79  79  79  THR THR B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  ASN 81  81  81  ASN ASN B . n 
B 1 82  PRO 82  82  82  PRO PRO B . n 
B 1 83  GLY 83  83  83  GLY GLY B . n 
B 1 84  VAL 84  84  84  VAL VAL B . n 
B 1 85  PRO 85  85  85  PRO PRO B . n 
B 1 86  ARG 86  86  86  ARG ARG B . n 
B 1 87  GLN 87  87  87  GLN GLN B . n 
B 1 88  TYR 88  88  88  TYR TYR B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  THR 91  91  91  THR THR B . n 
B 1 92  ILE 92  92  92  ILE ILE B . n 
B 1 93  PRO 93  93  93  PRO PRO B . n 
B 1 94  PRO 94  94  94  PRO PRO B . n 
B 1 95  GLU 95  95  95  GLU GLU B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 MET 100 100 100 MET MET B . n 
B 1 101 GLY 101 101 101 GLY GLY B . n 
B 1 102 ASN 102 102 102 ASN ASN B . n 
B 1 103 ILE 103 103 103 ILE ILE B . n 
B 1 104 ASN 104 104 104 ASN ASN B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 ALA 106 106 106 ALA ALA B . n 
B 1 107 GLY 107 107 107 GLY GLY B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 ARG 109 109 109 ARG ARG B . n 
B 1 110 ASN 110 110 110 ASN ASN B . n 
B 1 111 ALA 111 111 111 ALA ALA B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 MET 113 113 113 MET MET B . n 
B 1 114 LYS 114 114 114 LYS LYS B . n 
B 1 115 THR 115 115 115 THR THR B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 PRO 118 118 118 PRO PRO B . n 
B 1 119 GLN 119 119 119 GLN GLN B . n 
B 1 120 ALA 120 120 120 ALA ALA B . n 
B 1 121 ASP 121 121 121 ASP ASP B . n 
B 1 122 ARG 122 122 122 ARG ARG B . n 
B 1 123 GLU 123 123 123 GLU GLU B . n 
B 1 124 LEU 124 124 124 LEU LEU B . n 
B 1 125 GLY 125 125 125 GLY GLY B . n 
B 1 126 GLY 126 126 126 GLY GLY B . n 
B 1 127 TRP 127 127 127 TRP TRP B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 GLU 129 129 129 GLU GLU B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 GLN 131 131 131 GLN GLN B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 HIS 133 133 133 HIS HIS B . n 
B 1 134 GLN 134 134 134 GLN GLN B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 LEU 136 136 136 LEU LEU B . n 
B 1 137 ASP 137 137 137 ASP ASP B . n 
B 1 138 ARG 138 138 138 ARG ARG B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ILE 140 140 140 ILE ILE B . n 
B 1 141 GLU 141 141 141 GLU GLU B . n 
B 1 142 GLN 142 142 142 GLN GLN B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 PRO 144 144 144 PRO PRO B . n 
B 1 145 PRO 145 145 145 PRO PRO B . n 
B 1 146 ALA 146 146 146 ALA ALA B . n 
B 1 147 ASP 147 147 147 ASP ASP B . n 
B 1 148 LEU 148 148 148 LEU LEU B . n 
B 1 149 ARG 149 149 149 ARG ARG B . n 
B 1 150 ASP 150 150 150 ASP ASP B . n 
B 1 151 GLY 151 151 151 GLY GLY B . n 
B 1 152 PHE 152 152 152 PHE PHE B . n 
B 1 153 THR 153 153 153 THR THR B . n 
B 1 154 GLU 154 154 154 GLU GLU B . n 
B 1 155 PRO 155 155 155 PRO PRO B . n 
B 1 156 TYR 156 156 156 TYR TYR B . n 
B 1 157 SER 157 157 157 SER SER B . n 
B 1 158 ALA 158 158 158 ALA ALA B . n 
B 1 159 ALA 159 159 159 ALA ALA B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 HIS 161 161 161 HIS HIS B . n 
B 1 162 CYS 162 162 162 CYS CYS B . n 
B 1 163 ARG 163 163 163 ARG ARG B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 LEU 165 165 165 LEU LEU B . n 
B 1 166 GLY 166 166 166 GLY GLY B . n 
B 1 167 ILE 167 167 167 ILE ILE B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 ASP 170 170 170 ASP ASP B . n 
B 1 171 ASP 171 171 171 ASP ASP B . n 
B 1 172 TRP 172 172 172 TRP TRP B . n 
B 1 173 ARG 173 173 173 ARG ARG B . n 
B 1 174 ARG 174 174 174 ARG ARG B . n 
B 1 175 LEU 175 175 175 LEU LEU B . n 
B 1 176 MET 176 176 176 MET MET B . n 
B 1 177 SER 177 177 177 SER SER B . n 
B 1 178 GLY 178 178 178 GLY GLY B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 ASP 180 180 180 ASP ASP B . n 
B 1 181 VAL 181 181 181 VAL VAL B . n 
B 1 182 ALA 182 182 182 ALA ALA B . n 
B 1 183 PHE 183 183 183 PHE PHE B . n 
B 1 184 ILE 184 184 184 ILE ILE B . n 
B 1 185 THR 185 185 185 THR THR B . n 
B 1 186 SER 186 186 186 SER SER B . n 
B 1 187 PRO 187 187 187 PRO PRO B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 THR 189 189 189 THR THR B . n 
B 1 190 PHE 190 190 190 PHE PHE B . n 
B 1 191 GLU 191 191 191 GLU GLU B . n 
B 1 192 GLY 192 192 192 GLY GLY B . n 
B 1 193 SER 193 193 193 SER SER B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 VAL 195 195 195 VAL VAL B . n 
B 1 196 ASN 196 196 196 ASN ASN B . n 
B 1 197 TRP 197 197 197 TRP TRP B . n 
B 1 198 TYR 198 198 198 TYR TYR B . n 
B 1 199 LYS 199 199 199 LYS LYS B . n 
B 1 200 ASP 200 200 200 ASP ASP B . n 
B 1 201 LEU 201 201 201 LEU LEU B . n 
B 1 202 GLY 202 202 202 GLY GLY B . n 
B 1 203 TYR 203 203 203 TYR TYR B . n 
B 1 204 MET 204 204 204 MET MET B . n 
B 1 205 VAL 205 205 205 VAL VAL B . n 
B 1 206 ASP 206 206 206 ASP ASP B . n 
B 1 207 ARG 207 207 207 ARG ARG B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 ASN 209 209 209 ASN ASN B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 ASP 211 211 211 ASP ASP B . n 
B 1 212 PRO 212 212 212 PRO PRO B . n 
B 1 213 GLU 213 213 213 GLU GLU B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 THR 215 215 215 THR THR B . n 
B 1 216 GLU 216 216 216 GLU GLU B . n 
B 1 217 GLY 217 217 217 GLY GLY B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 LEU 219 219 219 LEU LEU B . n 
B 1 220 GLY 220 220 220 GLY GLY B . n 
B 1 221 ARG 221 221 221 ARG ARG B . n 
B 1 222 PHE 222 222 222 PHE PHE 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 LEU 225 225 225 LEU LEU B . n 
B 1 226 ARG 226 226 226 ARG ARG B . n 
B 1 227 ARG 227 227 227 ARG ARG B . n 
B 1 228 SER 228 228 228 SER SER B . n 
B 1 229 PRO 229 229 ?   ?   ?   B . n 
B 1 230 ASP 230 230 ?   ?   ?   B . n 
B 1 231 VAL 231 231 ?   ?   ?   B . n 
B 1 232 SER 232 232 ?   ?   ?   B . n 
B 1 233 ASP 233 233 ?   ?   ?   B . n 
B 1 234 GLN 234 234 ?   ?   ?   B . n 
B 1 235 VAL 235 235 235 VAL VAL B . n 
B 1 236 SER 236 236 236 SER SER B . n 
B 1 237 ASP 237 237 237 ASP ASP B . n 
B 1 238 GLU 238 238 238 GLU GLU B . n 
B 1 239 LEU 239 239 239 LEU LEU B . n 
B 1 240 LEU 240 240 240 LEU LEU B . n 
B 1 241 ALA 241 241 241 ALA ALA B . n 
B 1 242 THR 242 242 242 THR THR B . n 
B 1 243 VAL 243 243 243 VAL VAL B . n 
B 1 244 ALA 244 244 244 ALA ALA B . n 
B 1 245 LEU 245 245 245 LEU LEU B . n 
B 1 246 SER 246 246 246 SER SER B . n 
B 1 247 LEU 247 247 247 LEU LEU B . n 
B 1 248 PHE 248 248 248 PHE PHE B . n 
B 1 249 GLY 249 249 249 GLY GLY B . n 
B 1 250 ALA 250 250 250 ALA ALA B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 ALA 252 252 252 ALA ALA B . n 
B 1 253 VAL 253 253 253 VAL VAL B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 THR 255 255 255 THR THR B . n 
B 1 256 SER 256 256 256 SER SER B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 PHE 258 258 258 PHE PHE B . n 
B 1 259 LEU 259 259 259 LEU LEU B . n 
B 1 260 GLN 260 260 260 GLN GLN B . n 
B 1 261 HIS 261 261 261 HIS HIS B . n 
B 1 262 ALA 262 262 262 ALA ALA B . n 
B 1 263 ILE 263 263 263 ILE ILE B . n 
B 1 264 ILE 264 264 264 ILE ILE B . n 
B 1 265 ALA 265 265 265 ALA ALA B . n 
B 1 266 LEU 266 266 266 LEU LEU B . n 
B 1 267 ALA 267 267 267 ALA ALA B . n 
B 1 268 GLN 268 268 268 GLN GLN B . n 
B 1 269 GLN 269 269 269 GLN GLN B . n 
B 1 270 PRO 270 270 270 PRO PRO B . n 
B 1 271 GLU 271 271 271 GLU GLU B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 ALA 273 273 273 ALA ALA B . n 
B 1 274 ASP 274 274 274 ASP ASP B . n 
B 1 275 ARG 275 275 275 ARG ARG B . n 
B 1 276 LEU 276 276 276 LEU LEU B . n 
B 1 277 ARG 277 277 277 ARG ARG B . n 
B 1 278 ALA 278 278 278 ALA ALA B . n 
B 1 279 GLU 279 279 279 GLU GLU B . n 
B 1 280 PRO 280 280 280 PRO PRO B . n 
B 1 281 ALA 281 281 281 ALA ALA B . n 
B 1 282 VAL 282 282 282 VAL VAL B . n 
B 1 283 ILE 283 283 283 ILE ILE B . n 
B 1 284 GLY 284 284 284 GLY GLY B . n 
B 1 285 ARG 285 285 285 ARG ARG B . n 
B 1 286 ALA 286 286 286 ALA ALA B . n 
B 1 287 VAL 287 287 287 VAL VAL B . n 
B 1 288 ASP 288 288 288 ASP ASP B . n 
B 1 289 GLU 289 289 289 GLU GLU B . n 
B 1 290 LEU 290 290 290 LEU LEU B . n 
B 1 291 LEU 291 291 291 LEU LEU B . n 
B 1 292 ARG 292 292 292 ARG ARG B . n 
B 1 293 TYR 293 293 293 TYR TYR B . n 
B 1 294 ASN 294 294 294 ASN ASN B . n 
B 1 295 LEU 295 295 295 LEU LEU B . n 
B 1 296 SER 296 296 296 SER SER B . n 
B 1 297 ILE 297 297 297 ILE ILE B . n 
B 1 298 GLY 298 298 298 GLY GLY B . n 
B 1 299 ASP 299 299 299 ASP ASP B . n 
B 1 300 ALA 300 300 300 ALA ALA B . n 
B 1 301 LEU 301 301 301 LEU LEU B . n 
B 1 302 PRO 302 302 302 PRO PRO B . n 
B 1 303 ARG 303 303 303 ARG ARG B . n 
B 1 304 ILE 304 304 304 ILE ILE B . n 
B 1 305 ALA 305 305 305 ALA ALA B . n 
B 1 306 LEU 306 306 306 LEU LEU B . n 
B 1 307 ALA 307 307 307 ALA ALA B . n 
B 1 308 ASP 308 308 308 ASP ASP B . n 
B 1 309 VAL 309 309 309 VAL VAL B . n 
B 1 310 ARG 310 310 310 ARG ARG B . n 
B 1 311 LEU 311 311 311 LEU LEU B . n 
B 1 312 GLY 312 312 312 GLY GLY B . n 
B 1 313 GLU 313 313 313 GLU GLU B . n 
B 1 314 VAL 314 314 314 VAL VAL B . n 
B 1 315 GLU 315 315 315 GLU GLU B . n 
B 1 316 ILE 316 316 316 ILE ILE B . n 
B 1 317 ARG 317 317 317 ARG ARG B . n 
B 1 318 ALA 318 318 318 ALA ALA B . n 
B 1 319 GLY 319 319 319 GLY GLY B . n 
B 1 320 GLU 320 320 320 GLU GLU B . n 
B 1 321 LEU 321 321 321 LEU LEU B . n 
B 1 322 VAL 322 322 322 VAL VAL B . n 
B 1 323 LEU 323 323 323 LEU LEU B . n 
B 1 324 VAL 324 324 324 VAL VAL B . n 
B 1 325 LEU 325 325 325 LEU LEU B . n 
B 1 326 ILE 326 326 326 ILE ILE B . n 
B 1 327 GLU 327 327 327 GLU GLU B . n 
B 1 328 GLY 328 328 328 GLY GLY B . n 
B 1 329 ALA 329 329 329 ALA ALA B . n 
B 1 330 ASN 330 330 330 ASN ASN 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 PRO 333 333 333 PRO PRO B . n 
B 1 334 ALA 334 334 334 ALA ALA B . n 
B 1 335 VAL 335 335 335 VAL VAL B . n 
B 1 336 PHE 336 336 336 PHE PHE B . n 
B 1 337 PRO 337 337 337 PRO PRO B . n 
B 1 338 HIS 338 338 338 HIS HIS B . n 
B 1 339 PRO 339 339 339 PRO PRO B . n 
B 1 340 GLU 340 340 340 GLU GLU B . n 
B 1 341 ARG 341 341 341 ARG ARG B . n 
B 1 342 ILE 342 342 342 ILE ILE B . n 
B 1 343 ASP 343 343 343 ASP ASP B . n 
B 1 344 PHE 344 344 344 PHE PHE B . n 
B 1 345 ASP 345 345 345 ASP ASP B . n 
B 1 346 ARG 346 346 346 ARG ARG B . n 
B 1 347 GLU 347 347 347 GLU GLU B . n 
B 1 348 SER 348 348 348 SER SER B . n 
B 1 349 ASN 349 349 349 ASN ASN B . n 
B 1 350 PRO 350 350 350 PRO PRO B . n 
B 1 351 HIS 351 351 351 HIS HIS B . n 
B 1 352 LEU 352 352 352 LEU LEU B . n 
B 1 353 ALA 353 353 353 ALA ALA B . n 
B 1 354 PHE 354 354 354 PHE PHE B . n 
B 1 355 GLY 355 355 355 GLY GLY B . n 
B 1 356 GLY 356 356 356 GLY GLY B . n 
B 1 357 GLY 357 357 357 GLY GLY B . n 
B 1 358 GLN 358 358 358 GLN GLN B . n 
B 1 359 HIS 359 359 359 HIS HIS B . n 
B 1 360 PHE 360 360 360 PHE PHE B . n 
B 1 361 CYS 361 361 361 CYS CYS B . n 
B 1 362 PRO 362 362 362 PRO PRO B . n 
B 1 363 ALA 363 363 363 ALA ALA B . n 
B 1 364 SER 364 364 364 SER SER B . n 
B 1 365 ALA 365 365 365 ALA ALA B . n 
B 1 366 LEU 366 366 366 LEU LEU B . n 
B 1 367 GLY 367 367 367 GLY GLY B . n 
B 1 368 ARG 368 368 368 ARG ARG B . n 
B 1 369 THR 369 369 369 THR THR B . n 
B 1 370 HIS 370 370 370 HIS HIS B . n 
B 1 371 ALA 371 371 371 ALA ALA B . n 
B 1 372 GLU 372 372 372 GLU GLU B . n 
B 1 373 ILE 373 373 373 ILE ILE B . n 
B 1 374 ALA 374 374 374 ALA ALA B . n 
B 1 375 LEU 375 375 375 LEU LEU B . n 
B 1 376 THR 376 376 376 THR THR B . n 
B 1 377 ALA 377 377 377 ALA ALA B . n 
B 1 378 LEU 378 378 378 LEU LEU B . n 
B 1 379 VAL 379 379 379 VAL VAL B . n 
B 1 380 GLU 380 380 380 GLU GLU B . n 
B 1 381 LYS 381 381 381 LYS LYS B . n 
B 1 382 LEU 382 382 382 LEU LEU B . n 
B 1 383 PRO 383 383 383 PRO PRO B . n 
B 1 384 ALA 384 384 384 ALA ALA B . n 
B 1 385 LEU 385 385 385 LEU LEU B . n 
B 1 386 ARG 386 386 386 ARG ARG B . n 
B 1 387 LEU 387 387 387 LEU LEU B . n 
B 1 388 ALA 388 388 388 ALA ALA B . n 
B 1 389 LEU 389 389 389 LEU LEU B . n 
B 1 390 PRO 390 390 390 PRO PRO B . n 
B 1 391 VAL 391 391 391 VAL VAL B . n 
B 1 392 GLU 392 392 392 GLU GLU B . n 
B 1 393 GLN 393 393 393 GLN GLN B . n 
B 1 394 LEU 394 394 394 LEU LEU B . n 
B 1 395 ALA 395 395 395 ALA ALA B . n 
B 1 396 TRP 396 396 396 TRP TRP B . n 
B 1 397 ARG 397 397 397 ARG ARG B . n 
B 1 398 PRO 398 398 398 PRO PRO 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 ILE 401 401 401 ILE ILE B . n 
B 1 402 LYS 402 402 402 LYS LYS B . n 
B 1 403 ARG 403 403 403 ARG ARG B . n 
B 1 404 LEU 404 404 404 LEU LEU B . n 
B 1 405 PRO 405 405 405 PRO PRO B . n 
B 1 406 GLU 406 406 406 GLU GLU B . n 
B 1 407 ARG 407 407 407 ARG ARG B . n 
B 1 408 LEU 408 408 408 LEU LEU B . n 
B 1 409 PRO 409 409 409 PRO PRO B . n 
B 1 410 VAL 410 410 410 VAL VAL B . n 
B 1 411 LEU 411 411 411 LEU LEU B . n 
B 1 412 TRP 412 412 412 TRP TRP B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 UYM 1   501 463 UYM CWW A . 
D 3 HPA 1   502 464 HPA Hyp A . 
E 4 HEM 1   503 465 HEM HEM A . 
F 2 UYM 1   501 463 UYM CWW B . 
G 3 HPA 1   502 464 HPA Hyp B . 
H 4 HEM 1   503 465 HEM HEM B . 
I 5 HOH 1   601 24  HOH HOH A . 
I 5 HOH 2   602 533 HOH HOH A . 
I 5 HOH 3   603 507 HOH HOH A . 
I 5 HOH 4   604 30  HOH HOH A . 
I 5 HOH 5   605 427 HOH HOH A . 
I 5 HOH 6   606 119 HOH HOH A . 
I 5 HOH 7   607 166 HOH HOH A . 
I 5 HOH 8   608 531 HOH HOH A . 
I 5 HOH 9   609 380 HOH HOH A . 
I 5 HOH 10  610 305 HOH HOH A . 
I 5 HOH 11  611 353 HOH HOH A . 
I 5 HOH 12  612 374 HOH HOH A . 
I 5 HOH 13  613 131 HOH HOH A . 
I 5 HOH 14  614 341 HOH HOH A . 
I 5 HOH 15  615 410 HOH HOH A . 
I 5 HOH 16  616 483 HOH HOH A . 
I 5 HOH 17  617 195 HOH HOH A . 
I 5 HOH 18  618 333 HOH HOH A . 
I 5 HOH 19  619 241 HOH HOH A . 
I 5 HOH 20  620 38  HOH HOH A . 
I 5 HOH 21  621 222 HOH HOH A . 
I 5 HOH 22  622 532 HOH HOH A . 
I 5 HOH 23  623 185 HOH HOH A . 
I 5 HOH 24  624 449 HOH HOH A . 
I 5 HOH 25  625 104 HOH HOH A . 
I 5 HOH 26  626 192 HOH HOH A . 
I 5 HOH 27  627 493 HOH HOH A . 
I 5 HOH 28  628 18  HOH HOH A . 
I 5 HOH 29  629 148 HOH HOH A . 
I 5 HOH 30  630 284 HOH HOH A . 
I 5 HOH 31  631 272 HOH HOH A . 
I 5 HOH 32  632 545 HOH HOH A . 
I 5 HOH 33  633 57  HOH HOH A . 
I 5 HOH 34  634 163 HOH HOH A . 
I 5 HOH 35  635 469 HOH HOH A . 
I 5 HOH 36  636 13  HOH HOH A . 
I 5 HOH 37  637 225 HOH HOH A . 
I 5 HOH 38  638 244 HOH HOH A . 
I 5 HOH 39  639 22  HOH HOH A . 
I 5 HOH 40  640 54  HOH HOH A . 
I 5 HOH 41  641 474 HOH HOH A . 
I 5 HOH 42  642 405 HOH HOH A . 
I 5 HOH 43  643 231 HOH HOH A . 
I 5 HOH 44  644 294 HOH HOH A . 
I 5 HOH 45  645 20  HOH HOH A . 
I 5 HOH 46  646 79  HOH HOH A . 
I 5 HOH 47  647 15  HOH HOH A . 
I 5 HOH 48  648 433 HOH HOH A . 
I 5 HOH 49  649 105 HOH HOH A . 
I 5 HOH 50  650 116 HOH HOH A . 
I 5 HOH 51  651 107 HOH HOH A . 
I 5 HOH 52  652 6   HOH HOH A . 
I 5 HOH 53  653 207 HOH HOH A . 
I 5 HOH 54  654 251 HOH HOH A . 
I 5 HOH 55  655 295 HOH HOH A . 
I 5 HOH 56  656 667 HOH HOH A . 
I 5 HOH 57  657 140 HOH HOH A . 
I 5 HOH 58  658 160 HOH HOH A . 
I 5 HOH 59  659 315 HOH HOH A . 
I 5 HOH 60  660 275 HOH HOH A . 
I 5 HOH 61  661 396 HOH HOH A . 
I 5 HOH 62  662 216 HOH HOH A . 
I 5 HOH 63  663 460 HOH HOH A . 
I 5 HOH 64  664 220 HOH HOH A . 
I 5 HOH 65  665 549 HOH HOH A . 
I 5 HOH 66  666 49  HOH HOH A . 
I 5 HOH 67  667 212 HOH HOH A . 
I 5 HOH 68  668 255 HOH HOH A . 
I 5 HOH 69  669 210 HOH HOH A . 
I 5 HOH 70  670 501 HOH HOH A . 
I 5 HOH 71  671 252 HOH HOH A . 
I 5 HOH 72  672 296 HOH HOH A . 
I 5 HOH 73  673 198 HOH HOH A . 
I 5 HOH 74  674 453 HOH HOH A . 
I 5 HOH 75  675 45  HOH HOH A . 
I 5 HOH 76  676 540 HOH HOH A . 
I 5 HOH 77  677 81  HOH HOH A . 
I 5 HOH 78  678 78  HOH HOH A . 
I 5 HOH 79  679 597 HOH HOH A . 
I 5 HOH 80  680 518 HOH HOH A . 
I 5 HOH 81  681 263 HOH HOH A . 
I 5 HOH 82  682 648 HOH HOH A . 
I 5 HOH 83  683 103 HOH HOH A . 
I 5 HOH 84  684 150 HOH HOH A . 
I 5 HOH 85  685 300 HOH HOH A . 
I 5 HOH 86  686 435 HOH HOH A . 
I 5 HOH 87  687 129 HOH HOH A . 
I 5 HOH 88  688 142 HOH HOH A . 
I 5 HOH 89  689 319 HOH HOH A . 
I 5 HOH 90  690 5   HOH HOH A . 
I 5 HOH 91  691 43  HOH HOH A . 
I 5 HOH 92  692 14  HOH HOH A . 
I 5 HOH 93  693 28  HOH HOH A . 
I 5 HOH 94  694 574 HOH HOH A . 
I 5 HOH 95  695 94  HOH HOH A . 
I 5 HOH 96  696 478 HOH HOH A . 
I 5 HOH 97  697 71  HOH HOH A . 
I 5 HOH 98  698 35  HOH HOH A . 
I 5 HOH 99  699 269 HOH HOH A . 
I 5 HOH 100 700 19  HOH HOH A . 
I 5 HOH 101 701 62  HOH HOH A . 
I 5 HOH 102 702 386 HOH HOH A . 
I 5 HOH 103 703 92  HOH HOH A . 
I 5 HOH 104 704 112 HOH HOH A . 
I 5 HOH 105 705 543 HOH HOH A . 
I 5 HOH 106 706 176 HOH HOH A . 
I 5 HOH 107 707 528 HOH HOH A . 
I 5 HOH 108 708 167 HOH HOH A . 
I 5 HOH 109 709 237 HOH HOH A . 
I 5 HOH 110 710 174 HOH HOH A . 
I 5 HOH 111 711 573 HOH HOH A . 
I 5 HOH 112 712 311 HOH HOH A . 
I 5 HOH 113 713 254 HOH HOH A . 
I 5 HOH 114 714 547 HOH HOH A . 
I 5 HOH 115 715 215 HOH HOH A . 
I 5 HOH 116 716 309 HOH HOH A . 
I 5 HOH 117 717 186 HOH HOH A . 
I 5 HOH 118 718 125 HOH HOH A . 
I 5 HOH 119 719 358 HOH HOH A . 
I 5 HOH 120 720 450 HOH HOH A . 
I 5 HOH 121 721 302 HOH HOH A . 
I 5 HOH 122 722 325 HOH HOH A . 
I 5 HOH 123 723 11  HOH HOH A . 
I 5 HOH 124 724 247 HOH HOH A . 
I 5 HOH 125 725 197 HOH HOH A . 
I 5 HOH 126 726 291 HOH HOH A . 
I 5 HOH 127 727 382 HOH HOH A . 
I 5 HOH 128 728 134 HOH HOH A . 
I 5 HOH 129 729 416 HOH HOH A . 
I 5 HOH 130 730 73  HOH HOH A . 
I 5 HOH 131 731 181 HOH HOH A . 
I 5 HOH 132 732 153 HOH HOH A . 
I 5 HOH 133 733 407 HOH HOH A . 
I 5 HOH 134 734 10  HOH HOH A . 
I 5 HOH 135 735 168 HOH HOH A . 
I 5 HOH 136 736 203 HOH HOH A . 
I 5 HOH 137 737 657 HOH HOH A . 
I 5 HOH 138 738 607 HOH HOH A . 
I 5 HOH 139 739 80  HOH HOH A . 
I 5 HOH 140 740 4   HOH HOH A . 
I 5 HOH 141 741 458 HOH HOH A . 
I 5 HOH 142 742 419 HOH HOH A . 
I 5 HOH 143 743 40  HOH HOH A . 
I 5 HOH 144 744 393 HOH HOH A . 
I 5 HOH 145 745 339 HOH HOH A . 
I 5 HOH 146 746 352 HOH HOH A . 
I 5 HOH 147 747 553 HOH HOH A . 
I 5 HOH 148 748 260 HOH HOH A . 
I 5 HOH 149 749 127 HOH HOH A . 
I 5 HOH 150 750 525 HOH HOH A . 
I 5 HOH 151 751 485 HOH HOH A . 
I 5 HOH 152 752 82  HOH HOH A . 
I 5 HOH 153 753 271 HOH HOH A . 
I 5 HOH 154 754 522 HOH HOH A . 
I 5 HOH 155 755 152 HOH HOH A . 
I 5 HOH 156 756 63  HOH HOH A . 
I 5 HOH 157 757 156 HOH HOH A . 
I 5 HOH 158 758 306 HOH HOH A . 
I 5 HOH 159 759 618 HOH HOH A . 
I 5 HOH 160 760 286 HOH HOH A . 
I 5 HOH 161 761 33  HOH HOH A . 
I 5 HOH 162 762 550 HOH HOH A . 
I 5 HOH 163 763 564 HOH HOH A . 
I 5 HOH 164 764 31  HOH HOH A . 
I 5 HOH 165 765 468 HOH HOH A . 
I 5 HOH 166 766 65  HOH HOH A . 
I 5 HOH 167 767 64  HOH HOH A . 
I 5 HOH 168 768 91  HOH HOH A . 
I 5 HOH 169 769 282 HOH HOH A . 
I 5 HOH 170 770 121 HOH HOH A . 
I 5 HOH 171 771 234 HOH HOH A . 
I 5 HOH 172 772 178 HOH HOH A . 
I 5 HOH 173 773 288 HOH HOH A . 
I 5 HOH 174 774 356 HOH HOH A . 
I 5 HOH 175 775 467 HOH HOH A . 
I 5 HOH 176 776 343 HOH HOH A . 
I 5 HOH 177 777 350 HOH HOH A . 
I 5 HOH 178 778 2   HOH HOH A . 
I 5 HOH 179 779 345 HOH HOH A . 
I 5 HOH 180 780 50  HOH HOH A . 
I 5 HOH 181 781 338 HOH HOH A . 
I 5 HOH 182 782 187 HOH HOH A . 
I 5 HOH 183 783 548 HOH HOH A . 
I 5 HOH 184 784 124 HOH HOH A . 
I 5 HOH 185 785 48  HOH HOH A . 
I 5 HOH 186 786 147 HOH HOH A . 
I 5 HOH 187 787 213 HOH HOH A . 
I 5 HOH 188 788 117 HOH HOH A . 
I 5 HOH 189 789 201 HOH HOH A . 
I 5 HOH 190 790 539 HOH HOH A . 
I 5 HOH 191 791 249 HOH HOH A . 
I 5 HOH 192 792 184 HOH HOH A . 
I 5 HOH 193 793 326 HOH HOH A . 
I 5 HOH 194 794 37  HOH HOH A . 
I 5 HOH 195 795 463 HOH HOH A . 
I 5 HOH 196 796 576 HOH HOH A . 
I 5 HOH 197 797 118 HOH HOH A . 
I 5 HOH 198 798 442 HOH HOH A . 
I 5 HOH 199 799 506 HOH HOH A . 
I 5 HOH 200 800 585 HOH HOH A . 
I 5 HOH 201 801 476 HOH HOH A . 
I 5 HOH 202 802 660 HOH HOH A . 
I 5 HOH 203 803 418 HOH HOH A . 
I 5 HOH 204 804 484 HOH HOH A . 
I 5 HOH 205 805 101 HOH HOH A . 
I 5 HOH 206 806 93  HOH HOH A . 
I 5 HOH 207 807 360 HOH HOH A . 
I 5 HOH 208 808 432 HOH HOH A . 
I 5 HOH 209 809 328 HOH HOH A . 
I 5 HOH 210 810 366 HOH HOH A . 
I 5 HOH 211 811 60  HOH HOH A . 
I 5 HOH 212 812 145 HOH HOH A . 
I 5 HOH 213 813 363 HOH HOH A . 
I 5 HOH 214 814 486 HOH HOH A . 
I 5 HOH 215 815 658 HOH HOH A . 
I 5 HOH 216 816 479 HOH HOH A . 
I 5 HOH 217 817 605 HOH HOH A . 
I 5 HOH 218 818 123 HOH HOH A . 
I 5 HOH 219 819 218 HOH HOH A . 
I 5 HOH 220 820 292 HOH HOH A . 
I 5 HOH 221 821 242 HOH HOH A . 
I 5 HOH 222 822 392 HOH HOH A . 
I 5 HOH 223 823 310 HOH HOH A . 
I 5 HOH 224 824 23  HOH HOH A . 
I 5 HOH 225 825 70  HOH HOH A . 
I 5 HOH 226 826 173 HOH HOH A . 
I 5 HOH 227 827 109 HOH HOH A . 
I 5 HOH 228 828 497 HOH HOH A . 
I 5 HOH 229 829 634 HOH HOH A . 
I 5 HOH 230 830 191 HOH HOH A . 
I 5 HOH 231 831 404 HOH HOH A . 
I 5 HOH 232 832 128 HOH HOH A . 
I 5 HOH 233 833 542 HOH HOH A . 
I 5 HOH 234 834 388 HOH HOH A . 
I 5 HOH 235 835 661 HOH HOH A . 
I 5 HOH 236 836 257 HOH HOH A . 
I 5 HOH 237 837 627 HOH HOH A . 
I 5 HOH 238 838 610 HOH HOH A . 
I 5 HOH 239 839 9   HOH HOH A . 
I 5 HOH 240 840 409 HOH HOH A . 
I 5 HOH 241 841 357 HOH HOH A . 
I 5 HOH 242 842 165 HOH HOH A . 
I 5 HOH 243 843 376 HOH HOH A . 
I 5 HOH 244 844 110 HOH HOH A . 
I 5 HOH 245 845 274 HOH HOH A . 
I 5 HOH 246 846 587 HOH HOH A . 
I 5 HOH 247 847 68  HOH HOH A . 
I 5 HOH 248 848 90  HOH HOH A . 
I 5 HOH 249 849 318 HOH HOH A . 
I 5 HOH 250 850 465 HOH HOH A . 
I 5 HOH 251 851 371 HOH HOH A . 
I 5 HOH 252 852 387 HOH HOH A . 
I 5 HOH 253 853 32  HOH HOH A . 
I 5 HOH 254 854 568 HOH HOH A . 
I 5 HOH 255 855 436 HOH HOH A . 
I 5 HOH 256 856 290 HOH HOH A . 
I 5 HOH 257 857 337 HOH HOH A . 
I 5 HOH 258 858 46  HOH HOH A . 
I 5 HOH 259 859 303 HOH HOH A . 
I 5 HOH 260 860 641 HOH HOH A . 
I 5 HOH 261 861 277 HOH HOH A . 
I 5 HOH 262 862 541 HOH HOH A . 
I 5 HOH 263 863 644 HOH HOH A . 
I 5 HOH 264 864 157 HOH HOH A . 
I 5 HOH 265 865 443 HOH HOH A . 
I 5 HOH 266 866 566 HOH HOH A . 
I 5 HOH 267 867 283 HOH HOH A . 
I 5 HOH 268 868 170 HOH HOH A . 
I 5 HOH 269 869 561 HOH HOH A . 
I 5 HOH 270 870 503 HOH HOH A . 
I 5 HOH 271 871 616 HOH HOH A . 
I 5 HOH 272 872 413 HOH HOH A . 
I 5 HOH 273 873 439 HOH HOH A . 
I 5 HOH 274 874 348 HOH HOH A . 
I 5 HOH 275 875 397 HOH HOH A . 
I 5 HOH 276 876 415 HOH HOH A . 
I 5 HOH 277 877 569 HOH HOH A . 
I 5 HOH 278 878 414 HOH HOH A . 
I 5 HOH 279 879 527 HOH HOH A . 
I 5 HOH 280 880 401 HOH HOH A . 
I 5 HOH 281 881 83  HOH HOH A . 
I 5 HOH 282 882 516 HOH HOH A . 
I 5 HOH 283 883 593 HOH HOH A . 
I 5 HOH 284 884 596 HOH HOH A . 
I 5 HOH 285 885 620 HOH HOH A . 
I 5 HOH 286 886 281 HOH HOH A . 
I 5 HOH 287 887 556 HOH HOH A . 
I 5 HOH 288 888 487 HOH HOH A . 
I 5 HOH 289 889 515 HOH HOH A . 
I 5 HOH 290 890 42  HOH HOH A . 
I 5 HOH 291 891 537 HOH HOH A . 
I 5 HOH 292 892 456 HOH HOH A . 
I 5 HOH 293 893 466 HOH HOH A . 
I 5 HOH 294 894 639 HOH HOH A . 
I 5 HOH 295 895 670 HOH HOH A . 
I 5 HOH 296 896 440 HOH HOH A . 
I 5 HOH 297 897 472 HOH HOH A . 
I 5 HOH 298 898 508 HOH HOH A . 
I 5 HOH 299 899 530 HOH HOH A . 
I 5 HOH 300 900 340 HOH HOH A . 
I 5 HOH 301 901 589 HOH HOH A . 
I 5 HOH 302 902 623 HOH HOH A . 
I 5 HOH 303 903 420 HOH HOH A . 
I 5 HOH 304 904 650 HOH HOH A . 
I 5 HOH 305 905 375 HOH HOH A . 
I 5 HOH 306 906 430 HOH HOH A . 
I 5 HOH 307 907 400 HOH HOH A . 
I 5 HOH 308 908 624 HOH HOH A . 
I 5 HOH 309 909 230 HOH HOH A . 
I 5 HOH 310 910 171 HOH HOH A . 
I 5 HOH 311 911 677 HOH HOH A . 
I 5 HOH 312 912 552 HOH HOH A . 
I 5 HOH 313 913 214 HOH HOH A . 
I 5 HOH 314 914 489 HOH HOH A . 
I 5 HOH 315 915 205 HOH HOH A . 
I 5 HOH 316 916 395 HOH HOH A . 
I 5 HOH 317 917 612 HOH HOH A . 
I 5 HOH 318 918 495 HOH HOH A . 
I 5 HOH 319 919 534 HOH HOH A . 
I 5 HOH 320 920 505 HOH HOH A . 
I 5 HOH 321 921 675 HOH HOH A . 
I 5 HOH 322 922 581 HOH HOH A . 
I 5 HOH 323 923 287 HOH HOH A . 
I 5 HOH 324 924 599 HOH HOH A . 
I 5 HOH 325 925 227 HOH HOH A . 
I 5 HOH 326 926 359 HOH HOH A . 
I 5 HOH 327 927 362 HOH HOH A . 
I 5 HOH 328 928 560 HOH HOH A . 
I 5 HOH 329 929 438 HOH HOH A . 
I 5 HOH 330 930 238 HOH HOH A . 
I 5 HOH 331 931 76  HOH HOH A . 
I 5 HOH 332 932 504 HOH HOH A . 
I 5 HOH 333 933 673 HOH HOH A . 
I 5 HOH 334 934 606 HOH HOH A . 
I 5 HOH 335 935 632 HOH HOH A . 
I 5 HOH 336 936 664 HOH HOH A . 
I 5 HOH 337 937 351 HOH HOH A . 
I 5 HOH 338 938 668 HOH HOH A . 
I 5 HOH 339 939 364 HOH HOH A . 
I 5 HOH 340 940 335 HOH HOH A . 
I 5 HOH 341 941 480 HOH HOH A . 
I 5 HOH 342 942 448 HOH HOH A . 
I 5 HOH 343 943 494 HOH HOH A . 
I 5 HOH 344 944 451 HOH HOH A . 
I 5 HOH 345 945 500 HOH HOH A . 
I 5 HOH 346 946 379 HOH HOH A . 
I 5 HOH 347 947 603 HOH HOH A . 
I 5 HOH 348 948 459 HOH HOH A . 
I 5 HOH 349 949 425 HOH HOH A . 
I 5 HOH 350 950 245 HOH HOH A . 
I 5 HOH 351 951 572 HOH HOH A . 
I 5 HOH 352 952 424 HOH HOH A . 
I 5 HOH 353 953 562 HOH HOH A . 
I 5 HOH 354 954 563 HOH HOH A . 
I 5 HOH 355 955 613 HOH HOH A . 
I 5 HOH 356 956 645 HOH HOH A . 
I 5 HOH 357 957 437 HOH HOH A . 
I 5 HOH 358 958 653 HOH HOH A . 
I 5 HOH 359 959 580 HOH HOH A . 
I 5 HOH 360 960 526 HOH HOH A . 
I 5 HOH 361 961 649 HOH HOH A . 
J 5 HOH 1   601 538 HOH HOH B . 
J 5 HOH 2   602 445 HOH HOH B . 
J 5 HOH 3   603 172 HOH HOH B . 
J 5 HOH 4   604 656 HOH HOH B . 
J 5 HOH 5   605 651 HOH HOH B . 
J 5 HOH 6   606 211 HOH HOH B . 
J 5 HOH 7   607 102 HOH HOH B . 
J 5 HOH 8   608 666 HOH HOH B . 
J 5 HOH 9   609 535 HOH HOH B . 
J 5 HOH 10  610 58  HOH HOH B . 
J 5 HOH 11  611 304 HOH HOH B . 
J 5 HOH 12  612 390 HOH HOH B . 
J 5 HOH 13  613 137 HOH HOH B . 
J 5 HOH 14  614 194 HOH HOH B . 
J 5 HOH 15  615 136 HOH HOH B . 
J 5 HOH 16  616 411 HOH HOH B . 
J 5 HOH 17  617 96  HOH HOH B . 
J 5 HOH 18  618 586 HOH HOH B . 
J 5 HOH 19  619 29  HOH HOH B . 
J 5 HOH 20  620 39  HOH HOH B . 
J 5 HOH 21  621 608 HOH HOH B . 
J 5 HOH 22  622 361 HOH HOH B . 
J 5 HOH 23  623 654 HOH HOH B . 
J 5 HOH 24  624 228 HOH HOH B . 
J 5 HOH 25  625 368 HOH HOH B . 
J 5 HOH 26  626 412 HOH HOH B . 
J 5 HOH 27  627 289 HOH HOH B . 
J 5 HOH 28  628 558 HOH HOH B . 
J 5 HOH 29  629 498 HOH HOH B . 
J 5 HOH 30  630 75  HOH HOH B . 
J 5 HOH 31  631 369 HOH HOH B . 
J 5 HOH 32  632 41  HOH HOH B . 
J 5 HOH 33  633 307 HOH HOH B . 
J 5 HOH 34  634 265 HOH HOH B . 
J 5 HOH 35  635 642 HOH HOH B . 
J 5 HOH 36  636 7   HOH HOH B . 
J 5 HOH 37  637 492 HOH HOH B . 
J 5 HOH 38  638 385 HOH HOH B . 
J 5 HOH 39  639 611 HOH HOH B . 
J 5 HOH 40  640 577 HOH HOH B . 
J 5 HOH 41  641 240 HOH HOH B . 
J 5 HOH 42  642 631 HOH HOH B . 
J 5 HOH 43  643 321 HOH HOH B . 
J 5 HOH 44  644 521 HOH HOH B . 
J 5 HOH 45  645 59  HOH HOH B . 
J 5 HOH 46  646 481 HOH HOH B . 
J 5 HOH 47  647 297 HOH HOH B . 
J 5 HOH 48  648 1   HOH HOH B . 
J 5 HOH 49  649 89  HOH HOH B . 
J 5 HOH 50  650 381 HOH HOH B . 
J 5 HOH 51  651 154 HOH HOH B . 
J 5 HOH 52  652 115 HOH HOH B . 
J 5 HOH 53  653 372 HOH HOH B . 
J 5 HOH 54  654 334 HOH HOH B . 
J 5 HOH 55  655 609 HOH HOH B . 
J 5 HOH 56  656 159 HOH HOH B . 
J 5 HOH 57  657 72  HOH HOH B . 
J 5 HOH 58  658 408 HOH HOH B . 
J 5 HOH 59  659 97  HOH HOH B . 
J 5 HOH 60  660 322 HOH HOH B . 
J 5 HOH 61  661 246 HOH HOH B . 
J 5 HOH 62  662 398 HOH HOH B . 
J 5 HOH 63  663 206 HOH HOH B . 
J 5 HOH 64  664 383 HOH HOH B . 
J 5 HOH 65  665 143 HOH HOH B . 
J 5 HOH 66  666 95  HOH HOH B . 
J 5 HOH 67  667 208 HOH HOH B . 
J 5 HOH 68  668 226 HOH HOH B . 
J 5 HOH 69  669 122 HOH HOH B . 
J 5 HOH 70  670 182 HOH HOH B . 
J 5 HOH 71  671 267 HOH HOH B . 
J 5 HOH 72  672 120 HOH HOH B . 
J 5 HOH 73  673 51  HOH HOH B . 
J 5 HOH 74  674 190 HOH HOH B . 
J 5 HOH 75  675 158 HOH HOH B . 
J 5 HOH 76  676 633 HOH HOH B . 
J 5 HOH 77  677 584 HOH HOH B . 
J 5 HOH 78  678 188 HOH HOH B . 
J 5 HOH 79  679 34  HOH HOH B . 
J 5 HOH 80  680 224 HOH HOH B . 
J 5 HOH 81  681 114 HOH HOH B . 
J 5 HOH 82  682 146 HOH HOH B . 
J 5 HOH 83  683 313 HOH HOH B . 
J 5 HOH 84  684 336 HOH HOH B . 
J 5 HOH 85  685 346 HOH HOH B . 
J 5 HOH 86  686 12  HOH HOH B . 
J 5 HOH 87  687 130 HOH HOH B . 
J 5 HOH 88  688 52  HOH HOH B . 
J 5 HOH 89  689 126 HOH HOH B . 
J 5 HOH 90  690 273 HOH HOH B . 
J 5 HOH 91  691 108 HOH HOH B . 
J 5 HOH 92  692 250 HOH HOH B . 
J 5 HOH 93  693 536 HOH HOH B . 
J 5 HOH 94  694 177 HOH HOH B . 
J 5 HOH 95  695 299 HOH HOH B . 
J 5 HOH 96  696 446 HOH HOH B . 
J 5 HOH 97  697 77  HOH HOH B . 
J 5 HOH 98  698 354 HOH HOH B . 
J 5 HOH 99  699 554 HOH HOH B . 
J 5 HOH 100 700 514 HOH HOH B . 
J 5 HOH 101 701 219 HOH HOH B . 
J 5 HOH 102 702 8   HOH HOH B . 
J 5 HOH 103 703 434 HOH HOH B . 
J 5 HOH 104 704 592 HOH HOH B . 
J 5 HOH 105 705 312 HOH HOH B . 
J 5 HOH 106 706 344 HOH HOH B . 
J 5 HOH 107 707 87  HOH HOH B . 
J 5 HOH 108 708 235 HOH HOH B . 
J 5 HOH 109 709 475 HOH HOH B . 
J 5 HOH 110 710 470 HOH HOH B . 
J 5 HOH 111 711 144 HOH HOH B . 
J 5 HOH 112 712 169 HOH HOH B . 
J 5 HOH 113 713 180 HOH HOH B . 
J 5 HOH 114 714 139 HOH HOH B . 
J 5 HOH 115 715 280 HOH HOH B . 
J 5 HOH 116 716 441 HOH HOH B . 
J 5 HOH 117 717 544 HOH HOH B . 
J 5 HOH 118 718 262 HOH HOH B . 
J 5 HOH 119 719 189 HOH HOH B . 
J 5 HOH 120 720 204 HOH HOH B . 
J 5 HOH 121 721 141 HOH HOH B . 
J 5 HOH 122 722 61  HOH HOH B . 
J 5 HOH 123 723 604 HOH HOH B . 
J 5 HOH 124 724 373 HOH HOH B . 
J 5 HOH 125 725 279 HOH HOH B . 
J 5 HOH 126 726 327 HOH HOH B . 
J 5 HOH 127 727 270 HOH HOH B . 
J 5 HOH 128 728 98  HOH HOH B . 
J 5 HOH 129 729 301 HOH HOH B . 
J 5 HOH 130 730 471 HOH HOH B . 
J 5 HOH 131 731 256 HOH HOH B . 
J 5 HOH 132 732 370 HOH HOH B . 
J 5 HOH 133 733 36  HOH HOH B . 
J 5 HOH 134 734 615 HOH HOH B . 
J 5 HOH 135 735 196 HOH HOH B . 
J 5 HOH 136 736 66  HOH HOH B . 
J 5 HOH 137 737 626 HOH HOH B . 
J 5 HOH 138 738 406 HOH HOH B . 
J 5 HOH 139 739 617 HOH HOH B . 
J 5 HOH 140 740 17  HOH HOH B . 
J 5 HOH 141 741 86  HOH HOH B . 
J 5 HOH 142 742 132 HOH HOH B . 
J 5 HOH 143 743 399 HOH HOH B . 
J 5 HOH 144 744 55  HOH HOH B . 
J 5 HOH 145 745 394 HOH HOH B . 
J 5 HOH 146 746 316 HOH HOH B . 
J 5 HOH 147 747 324 HOH HOH B . 
J 5 HOH 148 748 509 HOH HOH B . 
J 5 HOH 149 749 133 HOH HOH B . 
J 5 HOH 150 750 285 HOH HOH B . 
J 5 HOH 151 751 21  HOH HOH B . 
J 5 HOH 152 752 16  HOH HOH B . 
J 5 HOH 153 753 221 HOH HOH B . 
J 5 HOH 154 754 637 HOH HOH B . 
J 5 HOH 155 755 3   HOH HOH B . 
J 5 HOH 156 756 431 HOH HOH B . 
J 5 HOH 157 757 151 HOH HOH B . 
J 5 HOH 158 758 391 HOH HOH B . 
J 5 HOH 159 759 56  HOH HOH B . 
J 5 HOH 160 760 320 HOH HOH B . 
J 5 HOH 161 761 268 HOH HOH B . 
J 5 HOH 162 762 512 HOH HOH B . 
J 5 HOH 163 763 209 HOH HOH B . 
J 5 HOH 164 764 44  HOH HOH B . 
J 5 HOH 165 765 248 HOH HOH B . 
J 5 HOH 166 766 183 HOH HOH B . 
J 5 HOH 167 767 403 HOH HOH B . 
J 5 HOH 168 768 69  HOH HOH B . 
J 5 HOH 169 769 26  HOH HOH B . 
J 5 HOH 170 770 578 HOH HOH B . 
J 5 HOH 171 771 426 HOH HOH B . 
J 5 HOH 172 772 454 HOH HOH B . 
J 5 HOH 173 773 491 HOH HOH B . 
J 5 HOH 174 774 462 HOH HOH B . 
J 5 HOH 175 775 223 HOH HOH B . 
J 5 HOH 176 776 199 HOH HOH B . 
J 5 HOH 177 777 455 HOH HOH B . 
J 5 HOH 178 778 111 HOH HOH B . 
J 5 HOH 179 779 402 HOH HOH B . 
J 5 HOH 180 780 519 HOH HOH B . 
J 5 HOH 181 781 428 HOH HOH B . 
J 5 HOH 182 782 200 HOH HOH B . 
J 5 HOH 183 783 679 HOH HOH B . 
J 5 HOH 184 784 342 HOH HOH B . 
J 5 HOH 185 785 179 HOH HOH B . 
J 5 HOH 186 786 347 HOH HOH B . 
J 5 HOH 187 787 202 HOH HOH B . 
J 5 HOH 188 788 421 HOH HOH B . 
J 5 HOH 189 789 53  HOH HOH B . 
J 5 HOH 190 790 278 HOH HOH B . 
J 5 HOH 191 791 135 HOH HOH B . 
J 5 HOH 192 792 266 HOH HOH B . 
J 5 HOH 193 793 27  HOH HOH B . 
J 5 HOH 194 794 293 HOH HOH B . 
J 5 HOH 195 795 308 HOH HOH B . 
J 5 HOH 196 796 659 HOH HOH B . 
J 5 HOH 197 797 601 HOH HOH B . 
J 5 HOH 198 798 444 HOH HOH B . 
J 5 HOH 199 799 423 HOH HOH B . 
J 5 HOH 200 800 417 HOH HOH B . 
J 5 HOH 201 801 619 HOH HOH B . 
J 5 HOH 202 802 161 HOH HOH B . 
J 5 HOH 203 803 233 HOH HOH B . 
J 5 HOH 204 804 25  HOH HOH B . 
J 5 HOH 205 805 377 HOH HOH B . 
J 5 HOH 206 806 138 HOH HOH B . 
J 5 HOH 207 807 482 HOH HOH B . 
J 5 HOH 208 808 47  HOH HOH B . 
J 5 HOH 209 809 84  HOH HOH B . 
J 5 HOH 210 810 513 HOH HOH B . 
J 5 HOH 211 811 638 HOH HOH B . 
J 5 HOH 212 812 85  HOH HOH B . 
J 5 HOH 213 813 74  HOH HOH B . 
J 5 HOH 214 814 674 HOH HOH B . 
J 5 HOH 215 815 464 HOH HOH B . 
J 5 HOH 216 816 317 HOH HOH B . 
J 5 HOH 217 817 510 HOH HOH B . 
J 5 HOH 218 818 229 HOH HOH B . 
J 5 HOH 219 819 155 HOH HOH B . 
J 5 HOH 220 820 567 HOH HOH B . 
J 5 HOH 221 821 571 HOH HOH B . 
J 5 HOH 222 822 261 HOH HOH B . 
J 5 HOH 223 823 349 HOH HOH B . 
J 5 HOH 224 824 678 HOH HOH B . 
J 5 HOH 225 825 490 HOH HOH B . 
J 5 HOH 226 826 378 HOH HOH B . 
J 5 HOH 227 827 647 HOH HOH B . 
J 5 HOH 228 828 665 HOH HOH B . 
J 5 HOH 229 829 330 HOH HOH B . 
J 5 HOH 230 830 365 HOH HOH B . 
J 5 HOH 231 831 555 HOH HOH B . 
J 5 HOH 232 832 629 HOH HOH B . 
J 5 HOH 233 833 314 HOH HOH B . 
J 5 HOH 234 834 113 HOH HOH B . 
J 5 HOH 235 835 524 HOH HOH B . 
J 5 HOH 236 836 422 HOH HOH B . 
J 5 HOH 237 837 520 HOH HOH B . 
J 5 HOH 238 838 594 HOH HOH B . 
J 5 HOH 239 839 502 HOH HOH B . 
J 5 HOH 240 840 88  HOH HOH B . 
J 5 HOH 241 841 457 HOH HOH B . 
J 5 HOH 242 842 99  HOH HOH B . 
J 5 HOH 243 843 473 HOH HOH B . 
J 5 HOH 244 844 655 HOH HOH B . 
J 5 HOH 245 845 331 HOH HOH B . 
J 5 HOH 246 846 663 HOH HOH B . 
J 5 HOH 247 847 621 HOH HOH B . 
J 5 HOH 248 848 583 HOH HOH B . 
J 5 HOH 249 849 496 HOH HOH B . 
J 5 HOH 250 850 602 HOH HOH B . 
J 5 HOH 251 851 106 HOH HOH B . 
J 5 HOH 252 852 447 HOH HOH B . 
J 5 HOH 253 853 232 HOH HOH B . 
J 5 HOH 254 854 276 HOH HOH B . 
J 5 HOH 255 855 635 HOH HOH B . 
J 5 HOH 256 856 646 HOH HOH B . 
J 5 HOH 257 857 259 HOH HOH B . 
J 5 HOH 258 858 323 HOH HOH B . 
J 5 HOH 259 859 253 HOH HOH B . 
J 5 HOH 260 860 662 HOH HOH B . 
J 5 HOH 261 861 517 HOH HOH B . 
J 5 HOH 262 862 622 HOH HOH B . 
J 5 HOH 263 863 595 HOH HOH B . 
J 5 HOH 264 864 429 HOH HOH B . 
J 5 HOH 265 865 243 HOH HOH B . 
J 5 HOH 266 866 614 HOH HOH B . 
J 5 HOH 267 867 389 HOH HOH B . 
J 5 HOH 268 868 239 HOH HOH B . 
J 5 HOH 269 869 477 HOH HOH B . 
J 5 HOH 270 870 217 HOH HOH B . 
J 5 HOH 271 871 570 HOH HOH B . 
J 5 HOH 272 872 499 HOH HOH B . 
J 5 HOH 273 873 258 HOH HOH B . 
J 5 HOH 274 874 669 HOH HOH B . 
J 5 HOH 275 875 590 HOH HOH B . 
J 5 HOH 276 876 100 HOH HOH B . 
J 5 HOH 277 877 164 HOH HOH B . 
J 5 HOH 278 878 529 HOH HOH B . 
J 5 HOH 279 879 551 HOH HOH B . 
J 5 HOH 280 880 546 HOH HOH B . 
J 5 HOH 281 881 264 HOH HOH B . 
J 5 HOH 282 882 565 HOH HOH B . 
J 5 HOH 283 883 557 HOH HOH B . 
J 5 HOH 284 884 193 HOH HOH B . 
J 5 HOH 285 885 488 HOH HOH B . 
J 5 HOH 286 886 559 HOH HOH B . 
J 5 HOH 287 887 591 HOH HOH B . 
J 5 HOH 288 888 523 HOH HOH B . 
J 5 HOH 289 889 367 HOH HOH B . 
J 5 HOH 290 890 355 HOH HOH B . 
J 5 HOH 291 891 452 HOH HOH B . 
J 5 HOH 292 892 643 HOH HOH B . 
J 5 HOH 293 893 579 HOH HOH B . 
J 5 HOH 294 894 582 HOH HOH B . 
J 5 HOH 295 895 67  HOH HOH B . 
J 5 HOH 296 896 175 HOH HOH B . 
J 5 HOH 297 897 640 HOH HOH B . 
J 5 HOH 298 898 461 HOH HOH B . 
J 5 HOH 299 899 600 HOH HOH B . 
J 5 HOH 300 900 298 HOH HOH B . 
J 5 HOH 301 901 236 HOH HOH B . 
J 5 HOH 302 902 149 HOH HOH B . 
J 5 HOH 303 903 162 HOH HOH B . 
J 5 HOH 304 904 588 HOH HOH B . 
J 5 HOH 305 905 384 HOH HOH B . 
J 5 HOH 306 906 671 HOH HOH B . 
J 5 HOH 307 907 628 HOH HOH B . 
J 5 HOH 308 908 625 HOH HOH B . 
J 5 HOH 309 909 630 HOH HOH B . 
J 5 HOH 310 910 652 HOH HOH B . 
J 5 HOH 311 911 332 HOH HOH B . 
J 5 HOH 312 912 598 HOH HOH B . 
J 5 HOH 313 913 672 HOH HOH B . 
J 5 HOH 314 914 636 HOH HOH B . 
J 5 HOH 315 915 676 HOH HOH B . 
J 5 HOH 316 916 575 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 119 ? CG  ? A GLN 119 CG  
2  1 Y 1 A GLN 119 ? CD  ? A GLN 119 CD  
3  1 Y 1 A GLN 119 ? OE1 ? A GLN 119 OE1 
4  1 Y 1 A GLN 119 ? NE2 ? A GLN 119 NE2 
5  1 Y 1 A ARG 122 ? CG  ? A ARG 122 CG  
6  1 Y 1 A ARG 122 ? CD  ? A ARG 122 CD  
7  1 Y 1 A ARG 122 ? NE  ? A ARG 122 NE  
8  1 Y 1 A ARG 122 ? CZ  ? A ARG 122 CZ  
9  1 Y 1 A ARG 122 ? NH1 ? A ARG 122 NH1 
10 1 Y 1 A ARG 122 ? NH2 ? A ARG 122 NH2 
11 1 Y 1 A ARG 174 ? CG  ? A ARG 174 CG  
12 1 Y 1 A ARG 174 ? CD  ? A ARG 174 CD  
13 1 Y 1 A ARG 174 ? NE  ? A ARG 174 NE  
14 1 Y 1 A ARG 174 ? CZ  ? A ARG 174 CZ  
15 1 Y 1 A ARG 174 ? NH1 ? A ARG 174 NH1 
16 1 Y 1 A ARG 174 ? NH2 ? A ARG 174 NH2 
17 1 Y 1 A GLU 224 ? CG  ? A GLU 224 CG  
18 1 Y 1 A GLU 224 ? CD  ? A GLU 224 CD  
19 1 Y 1 A GLU 224 ? OE1 ? A GLU 224 OE1 
20 1 Y 1 A GLU 224 ? OE2 ? A GLU 224 OE2 
21 1 Y 1 A GLU 238 ? CG  ? A GLU 238 CG  
22 1 Y 1 A GLU 238 ? CD  ? A GLU 238 CD  
23 1 Y 1 A GLU 238 ? OE1 ? A GLU 238 OE1 
24 1 Y 1 A GLU 238 ? OE2 ? A GLU 238 OE2 
25 1 Y 1 B ARG 27  ? CG  ? B ARG 27  CG  
26 1 Y 1 B ARG 27  ? CD  ? B ARG 27  CD  
27 1 Y 1 B ARG 27  ? NE  ? B ARG 27  NE  
28 1 Y 1 B ARG 27  ? CZ  ? B ARG 27  CZ  
29 1 Y 1 B ARG 27  ? NH1 ? B ARG 27  NH1 
30 1 Y 1 B ARG 27  ? NH2 ? B ARG 27  NH2 
31 1 Y 1 B ARG 122 ? CG  ? B ARG 122 CG  
32 1 Y 1 B ARG 122 ? CD  ? B ARG 122 CD  
33 1 Y 1 B ARG 122 ? NE  ? B ARG 122 NE  
34 1 Y 1 B ARG 122 ? CZ  ? B ARG 122 CZ  
35 1 Y 1 B ARG 122 ? NH1 ? B ARG 122 NH1 
36 1 Y 1 B ARG 122 ? NH2 ? B ARG 122 NH2 
37 1 Y 1 B ARG 174 ? CG  ? B ARG 174 CG  
38 1 Y 1 B ARG 174 ? CD  ? B ARG 174 CD  
39 1 Y 1 B ARG 174 ? NE  ? B ARG 174 NE  
40 1 Y 1 B ARG 174 ? CZ  ? B ARG 174 CZ  
41 1 Y 1 B ARG 174 ? NH1 ? B ARG 174 NH1 
42 1 Y 1 B ARG 174 ? NH2 ? B ARG 174 NH2 
43 1 Y 1 B GLU 224 ? CG  ? B GLU 224 CG  
44 1 Y 1 B GLU 224 ? CD  ? B GLU 224 CD  
45 1 Y 1 B GLU 224 ? OE1 ? B GLU 224 OE1 
46 1 Y 1 B GLU 224 ? OE2 ? B GLU 224 OE2 
47 1 Y 1 B GLU 238 ? CG  ? B GLU 238 CG  
48 1 Y 1 B GLU 238 ? CD  ? B GLU 238 CD  
49 1 Y 1 B GLU 238 ? OE1 ? B GLU 238 OE1 
50 1 Y 1 B GLU 238 ? OE2 ? B GLU 238 OE2 
51 1 Y 1 B GLU 313 ? CG  ? B GLU 313 CG  
52 1 Y 1 B GLU 313 ? CD  ? B GLU 313 CD  
53 1 Y 1 B GLU 313 ? OE1 ? B GLU 313 OE1 
54 1 Y 1 B GLU 313 ? OE2 ? B GLU 313 OE2 
# 
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      ? ? ? '(1.19.2_4158: ???)' 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .                    2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .                    3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .                    4 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .                    5 
# 
_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                     8YY7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.970 
_cell.length_a_esd                 ? 
_cell.length_b                     84.970 
_cell.length_b_esd                 ? 
_cell.length_c                     136.220 
_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                         8YY7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                78 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 43' 
_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                   8YY7 
_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             2.71 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.68 
_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              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.1M Bis-Tris pH 5.5
0.2M Ammonium acetate
25% PEG3350
;
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9785 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9785 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YY7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.10 
_reflns.d_resolution_low                               31.61 
_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                                     56291 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_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                                    2.1 
_reflns_shell.d_res_low                                     2.15 
_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                             4167 
_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                                  ? 
_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                                  1.216 
_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                                 8YY7 
_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                            2.10 
_refine.ls_d_res_low                             31.61 
_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                     56241 
_refine.ls_number_reflns_R_free                  2779 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2244 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1945 
_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                    ? 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_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             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_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                            ? 
_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                       2.10 
_refine_hist.d_res_low                        31.61 
_refine_hist.number_atoms_solvent             677 
_refine_hist.number_atoms_total               6811 
_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        6134 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_refine_ls_shell.R_factor_R_free                  0.2550 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2070 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.d_res_high                       2.10 
_refine_ls_shell.d_res_low                        2.175 
_refine_ls_shell.number_reflns_R_free             301 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.number_reflns_all                5629 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.percent_reflns_obs               ? 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
# 
_struct.entry_id                     8YY7 
_struct.title                        'Crystal structure of PtmB in complex with cyclo-(L-Trp-L-Trp) and Hypoxanthine' 
_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        8YY7 
_struct_keywords.text            'P450 oxidoreductase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8YY7 
_struct_ref.pdbx_db_accession          8YY7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_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 8YY7 A 1 ? 412 ? 8YY7 1 ? 412 ? 1 412 
2 1 8YY7 B 1 ? 412 ? 8YY7 1 ? 412 ? 1 412 
# 
_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)' 5810  ? 
1 MORE         -53   ? 
1 'SSA (A^2)'  28890 ? 
# 
_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,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 33  ? GLN A 43  ? PRO A 33  GLN A 43  1 ? 11 
HELX_P HELX_P2  AA2 SER A 61  ? ASP A 71  ? SER A 61  ASP A 71  1 ? 11 
HELX_P HELX_P3  AA3 LEU A 76  ? ASN A 81  ? LEU A 76  ASN A 81  5 ? 6  
HELX_P HELX_P4  AA4 PRO A 93  ? ASN A 98  ? PRO A 93  ASN A 98  1 ? 6  
HELX_P HELX_P5  AA5 ASN A 98  ? ALA A 106 ? ASN A 98  ALA A 106 1 ? 9  
HELX_P HELX_P6  AA6 LEU A 108 ? SER A 117 ? LEU A 108 SER A 117 1 ? 10 
HELX_P HELX_P7  AA7 PRO A 118 ? ASP A 121 ? PRO A 118 ASP A 121 5 ? 4  
HELX_P HELX_P8  AA8 GLU A 123 ? GLY A 143 ? GLU A 123 GLY A 143 1 ? 21 
HELX_P HELX_P9  AA9 PHE A 152 ? GLY A 166 ? PHE A 152 GLY A 166 1 ? 15 
HELX_P HELX_P10 AB1 ASP A 171 ? PHE A 183 ? ASP A 171 PHE A 183 1 ? 13 
HELX_P HELX_P11 AB2 GLU A 191 ? ASN A 209 ? GLU A 191 ASN A 209 1 ? 19 
HELX_P HELX_P12 AB3 GLU A 216 ? ARG A 226 ? GLU A 216 ARG A 226 1 ? 11 
HELX_P HELX_P13 AB4 SER A 236 ? GLN A 269 ? SER A 236 GLN A 269 1 ? 34 
HELX_P HELX_P14 AB5 GLN A 269 ? GLU A 279 ? GLN A 269 GLU A 279 1 ? 11 
HELX_P HELX_P15 AB6 VAL A 282 ? ASN A 294 ? VAL A 282 ASN A 294 1 ? 13 
HELX_P HELX_P16 AB7 LEU A 325 ? TYR A 331 ? LEU A 325 TYR A 331 1 ? 7  
HELX_P HELX_P17 AB8 GLY A 356 ? PHE A 360 ? GLY A 356 PHE A 360 5 ? 5  
HELX_P HELX_P18 AB9 ALA A 363 ? LEU A 382 ? ALA A 363 LEU A 382 1 ? 20 
HELX_P HELX_P19 AC1 PRO A 390 ? LEU A 394 ? PRO A 390 LEU A 394 5 ? 5  
HELX_P HELX_P20 AC2 PRO B 33  ? GLN B 43  ? PRO B 33  GLN B 43  1 ? 11 
HELX_P HELX_P21 AC3 SER B 61  ? GLU B 70  ? SER B 61  GLU B 70  1 ? 10 
HELX_P HELX_P22 AC4 LEU B 76  ? ASN B 81  ? LEU B 76  ASN B 81  5 ? 6  
HELX_P HELX_P23 AC5 PRO B 93  ? ASN B 98  ? PRO B 93  ASN B 98  1 ? 6  
HELX_P HELX_P24 AC6 ASN B 98  ? ALA B 106 ? ASN B 98  ALA B 106 1 ? 9  
HELX_P HELX_P25 AC7 LEU B 108 ? LEU B 116 ? LEU B 108 LEU B 116 1 ? 9  
HELX_P HELX_P26 AC8 GLU B 123 ? GLY B 143 ? GLU B 123 GLY B 143 1 ? 21 
HELX_P HELX_P27 AC9 PHE B 152 ? GLY B 166 ? PHE B 152 GLY B 166 1 ? 15 
HELX_P HELX_P28 AD1 ASP B 171 ? PHE B 183 ? ASP B 171 PHE B 183 1 ? 13 
HELX_P HELX_P29 AD2 GLY B 192 ? ASN B 209 ? GLY B 192 ASN B 209 1 ? 18 
HELX_P HELX_P30 AD3 GLU B 216 ? ARG B 226 ? GLU B 216 ARG B 226 1 ? 11 
HELX_P HELX_P31 AD4 SER B 236 ? GLN B 269 ? SER B 236 GLN B 269 1 ? 34 
HELX_P HELX_P32 AD5 GLN B 269 ? GLU B 279 ? GLN B 269 GLU B 279 1 ? 11 
HELX_P HELX_P33 AD6 VAL B 282 ? ASN B 294 ? VAL B 282 ASN B 294 1 ? 13 
HELX_P HELX_P34 AD7 LEU B 325 ? TYR B 331 ? LEU B 325 TYR B 331 1 ? 7  
HELX_P HELX_P35 AD8 GLY B 356 ? PHE B 360 ? GLY B 356 PHE B 360 5 ? 5  
HELX_P HELX_P36 AD9 ALA B 363 ? LEU B 382 ? ALA B 363 LEU B 382 1 ? 20 
HELX_P HELX_P37 AE1 PRO B 390 ? LEU B 394 ? PRO B 390 LEU B 394 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            metalc1 
_struct_conn.conn_type_id                  metalc 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           H 
_struct_conn.ptnr1_label_comp_id           HEM 
_struct_conn.ptnr1_label_seq_id            . 
_struct_conn.ptnr1_label_atom_id           FE 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           J 
_struct_conn.ptnr2_label_comp_id           HOH 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           O 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            HEM 
_struct_conn.ptnr1_auth_seq_id             503 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            HOH 
_struct_conn.ptnr2_auth_seq_id             765 
_struct_conn.ptnr2_symmetry                1_555 
_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               2.745 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O  ? J HOH . ? B HOH 765 ? 1_555 FE ? H HEM . ? B HEM 503 ? 1_555 NA ? H HEM . ? B HEM 503 ? 1_555 119.5 ? 
2  O  ? J HOH . ? B HOH 765 ? 1_555 FE ? H HEM . ? B HEM 503 ? 1_555 NB ? H HEM . ? B HEM 503 ? 1_555 93.3  ? 
3  NA ? H HEM . ? B HEM 503 ? 1_555 FE ? H HEM . ? B HEM 503 ? 1_555 NB ? H HEM . ? B HEM 503 ? 1_555 87.3  ? 
4  O  ? J HOH . ? B HOH 765 ? 1_555 FE ? H HEM . ? B HEM 503 ? 1_555 NC ? H HEM . ? B HEM 503 ? 1_555 72.4  ? 
5  NA ? H HEM . ? B HEM 503 ? 1_555 FE ? H HEM . ? B HEM 503 ? 1_555 NC ? H HEM . ? B HEM 503 ? 1_555 167.5 ? 
6  NB ? H HEM . ? B HEM 503 ? 1_555 FE ? H HEM . ? B HEM 503 ? 1_555 NC ? H HEM . ? B HEM 503 ? 1_555 88.2  ? 
7  O  ? J HOH . ? B HOH 765 ? 1_555 FE ? H HEM . ? B HEM 503 ? 1_555 ND ? H HEM . ? B HEM 503 ? 1_555 92.2  ? 
8  NA ? H HEM . ? B HEM 503 ? 1_555 FE ? H HEM . ? B HEM 503 ? 1_555 ND ? H HEM . ? B HEM 503 ? 1_555 92.0  ? 
9  NB ? H HEM . ? B HEM 503 ? 1_555 FE ? H HEM . ? B HEM 503 ? 1_555 ND ? H HEM . ? B HEM 503 ? 1_555 173.9 ? 
10 NC ? H HEM . ? B HEM 503 ? 1_555 FE ? H HEM . ? B HEM 503 ? 1_555 ND ? H HEM . ? B HEM 503 ? 1_555 91.1  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 23  A . ? PHE 23  A PRO 24  A ? PRO 24  A 1 5.64  
2 PRO 144 A . ? PRO 144 A PRO 145 A ? PRO 145 A 1 -0.71 
3 PHE 23  B . ? PHE 23  B PRO 24  B ? PRO 24  B 1 3.74  
4 PRO 144 B . ? PRO 144 B PRO 145 B ? PRO 145 B 1 -1.90 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 45  ? ARG A 49  ? VAL A 45  ARG A 49  
AA1 2 GLU A 55  ? VAL A 59  ? GLU A 55  VAL A 59  
AA1 3 LEU A 321 ? VAL A 324 ? LEU A 321 VAL A 324 
AA1 4 LEU A 301 ? ALA A 305 ? LEU A 301 ALA A 305 
AA1 5 PHE A 74  ? SER A 75  ? PHE A 74  SER A 75  
AA2 1 ALA A 146 ? ASP A 147 ? ALA A 146 ASP A 147 
AA2 2 PRO A 409 ? LEU A 411 ? PRO A 409 LEU A 411 
AA2 3 ARG A 386 ? LEU A 387 ? ARG A 386 LEU A 387 
AA3 1 VAL A 309 ? LEU A 311 ? VAL A 309 LEU A 311 
AA3 2 VAL A 314 ? ILE A 316 ? VAL A 314 ILE A 316 
AA4 1 VAL B 45  ? ARG B 49  ? VAL B 45  ARG B 49  
AA4 2 GLU B 55  ? VAL B 59  ? GLU B 55  VAL B 59  
AA4 3 LEU B 321 ? VAL B 324 ? LEU B 321 VAL B 324 
AA4 4 LEU B 301 ? ALA B 305 ? LEU B 301 ALA B 305 
AA4 5 PHE B 74  ? SER B 75  ? PHE B 74  SER B 75  
AA5 1 ALA B 146 ? ASP B 147 ? ALA B 146 ASP B 147 
AA5 2 PRO B 409 ? LEU B 411 ? PRO B 409 LEU B 411 
AA5 3 ARG B 386 ? LEU B 387 ? ARG B 386 LEU B 387 
AA6 1 VAL B 309 ? LEU B 311 ? VAL B 309 LEU B 311 
AA6 2 VAL B 314 ? ILE B 316 ? VAL B 314 ILE B 316 
# 
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 ALA A 46  ? N ALA A 46  O LEU A 58  ? O LEU A 58  
AA1 2 3 N VAL A 59  ? N VAL A 59  O LEU A 323 ? O LEU A 323 
AA1 3 4 O VAL A 322 ? O VAL A 322 N ARG A 303 ? N ARG A 303 
AA1 4 5 O ILE A 304 ? O ILE A 304 N SER A 75  ? N SER A 75  
AA2 1 2 N ALA A 146 ? N ALA A 146 O VAL A 410 ? O VAL A 410 
AA2 2 3 O LEU A 411 ? O LEU A 411 N ARG A 386 ? N ARG A 386 
AA3 1 2 N VAL A 309 ? N VAL A 309 O ILE A 316 ? O ILE A 316 
AA4 1 2 N ALA B 46  ? N ALA B 46  O LEU B 58  ? O LEU B 58  
AA4 2 3 N VAL B 59  ? N VAL B 59  O LEU B 323 ? O LEU B 323 
AA4 3 4 O VAL B 322 ? O VAL B 322 N ARG B 303 ? N ARG B 303 
AA4 4 5 O ILE B 304 ? O ILE B 304 N SER B 75  ? N SER B 75  
AA5 1 2 N ALA B 146 ? N ALA B 146 O VAL B 410 ? O VAL B 410 
AA5 2 3 O LEU B 411 ? O LEU B 411 N ARG B 386 ? N ARG B 386 
AA6 1 2 N LEU B 311 ? N LEU B 311 O VAL B 314 ? O VAL B 314 
# 
_pdbx_entry_details.entry_id                   8YY7 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 26  ? ? 177.95  154.29  
2  1 PHE A 152 ? ? -146.89 -54.75  
3  1 PRO A 212 ? ? -64.81  81.11   
4  1 ASP A 299 ? ? -121.96 -165.60 
5  1 HIS A 338 ? ? 33.85   61.94   
6  1 ASN A 349 ? ? -154.46 66.83   
7  1 SER B 26  ? ? -178.00 130.06  
8  1 ASN B 98  ? ? -96.76  33.91   
9  1 ASP B 121 ? ? -118.15 78.50   
10 1 PHE B 152 ? ? -151.99 -68.08  
11 1 GLU B 191 ? ? -19.90  104.23  
12 1 PRO B 212 ? ? -62.90  79.90   
13 1 GLU B 213 ? ? -33.68  131.97  
14 1 HIS B 338 ? ? 31.53   61.25   
15 1 LEU B 382 ? ? -119.82 68.98   
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 960 ? 5.97 . 
2 1 O ? A HOH 961 ? 6.37 . 
3 1 O ? B HOH 916 ? 6.45 . 
# 
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 THR 2   ? A THR 2   
3  1 Y 1 A THR 3   ? A THR 3   
4  1 Y 1 A THR 4   ? A THR 4   
5  1 Y 1 A ALA 5   ? A ALA 5   
6  1 Y 1 A GLN 6   ? A GLN 6   
7  1 Y 1 A ARG 7   ? A ARG 7   
8  1 Y 1 A ASP 8   ? A ASP 8   
9  1 Y 1 A PRO 9   ? A PRO 9   
10 1 Y 1 A VAL 10  ? A VAL 10  
11 1 Y 1 A LEU 11  ? A LEU 11  
12 1 Y 1 A PRO 12  ? A PRO 12  
13 1 Y 1 A GLY 13  ? A GLY 13  
14 1 Y 1 A THR 14  ? A THR 14  
15 1 Y 1 A ALA 15  ? A ALA 15  
16 1 Y 1 A HIS 16  ? A HIS 16  
17 1 Y 1 A HIS 17  ? A HIS 17  
18 1 Y 1 A PRO 18  ? A PRO 18  
19 1 Y 1 A PRO 229 ? A PRO 229 
20 1 Y 1 A ASP 230 ? A ASP 230 
21 1 Y 1 A VAL 231 ? A VAL 231 
22 1 Y 1 A SER 232 ? A SER 232 
23 1 Y 1 A ASP 233 ? A ASP 233 
24 1 Y 1 A GLN 234 ? A GLN 234 
25 1 Y 1 B MET 1   ? B MET 1   
26 1 Y 1 B THR 2   ? B THR 2   
27 1 Y 1 B THR 3   ? B THR 3   
28 1 Y 1 B THR 4   ? B THR 4   
29 1 Y 1 B ALA 5   ? B ALA 5   
30 1 Y 1 B GLN 6   ? B GLN 6   
31 1 Y 1 B ARG 7   ? B ARG 7   
32 1 Y 1 B ASP 8   ? B ASP 8   
33 1 Y 1 B PRO 9   ? B PRO 9   
34 1 Y 1 B VAL 10  ? B VAL 10  
35 1 Y 1 B LEU 11  ? B LEU 11  
36 1 Y 1 B PRO 12  ? B PRO 12  
37 1 Y 1 B GLY 13  ? B GLY 13  
38 1 Y 1 B THR 14  ? B THR 14  
39 1 Y 1 B ALA 15  ? B ALA 15  
40 1 Y 1 B HIS 16  ? B HIS 16  
41 1 Y 1 B HIS 17  ? B HIS 17  
42 1 Y 1 B PRO 18  ? B PRO 18  
43 1 Y 1 B PRO 229 ? B PRO 229 
44 1 Y 1 B ASP 230 ? B ASP 230 
45 1 Y 1 B VAL 231 ? B VAL 231 
46 1 Y 1 B SER 232 ? B SER 232 
47 1 Y 1 B ASP 233 ? B ASP 233 
48 1 Y 1 B GLN 234 ? B GLN 234 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HEM CHA  C  N N 137 
HEM CHB  C  N N 138 
HEM CHC  C  N N 139 
HEM CHD  C  N N 140 
HEM C1A  C  Y N 141 
HEM C2A  C  Y N 142 
HEM C3A  C  Y N 143 
HEM C4A  C  Y N 144 
HEM CMA  C  N N 145 
HEM CAA  C  N N 146 
HEM CBA  C  N N 147 
HEM CGA  C  N N 148 
HEM O1A  O  N N 149 
HEM O2A  O  N N 150 
HEM C1B  C  N N 151 
HEM C2B  C  N N 152 
HEM C3B  C  N N 153 
HEM C4B  C  N N 154 
HEM CMB  C  N N 155 
HEM CAB  C  N N 156 
HEM CBB  C  N N 157 
HEM C1C  C  Y N 158 
HEM C2C  C  Y N 159 
HEM C3C  C  Y N 160 
HEM C4C  C  Y N 161 
HEM CMC  C  N N 162 
HEM CAC  C  N N 163 
HEM CBC  C  N N 164 
HEM C1D  C  N N 165 
HEM C2D  C  N N 166 
HEM C3D  C  N N 167 
HEM C4D  C  N N 168 
HEM CMD  C  N N 169 
HEM CAD  C  N N 170 
HEM CBD  C  N N 171 
HEM CGD  C  N N 172 
HEM O1D  O  N N 173 
HEM O2D  O  N N 174 
HEM NA   N  Y N 175 
HEM NB   N  N N 176 
HEM NC   N  Y N 177 
HEM ND   N  N N 178 
HEM FE   FE N N 179 
HEM HHB  H  N N 180 
HEM HHC  H  N N 181 
HEM HHD  H  N N 182 
HEM HMA  H  N N 183 
HEM HMAA H  N N 184 
HEM HMAB H  N N 185 
HEM HAA  H  N N 186 
HEM HAAA H  N N 187 
HEM HBA  H  N N 188 
HEM HBAA H  N N 189 
HEM HMB  H  N N 190 
HEM HMBA H  N N 191 
HEM HMBB H  N N 192 
HEM HAB  H  N N 193 
HEM HBB  H  N N 194 
HEM HBBA H  N N 195 
HEM HMC  H  N N 196 
HEM HMCA H  N N 197 
HEM HMCB H  N N 198 
HEM HAC  H  N N 199 
HEM HBC  H  N N 200 
HEM HBCA H  N N 201 
HEM HMD  H  N N 202 
HEM HMDA H  N N 203 
HEM HMDB H  N N 204 
HEM HAD  H  N N 205 
HEM HADA H  N N 206 
HEM HBD  H  N N 207 
HEM HBDA H  N N 208 
HEM H2A  H  N N 209 
HEM H2D  H  N N 210 
HEM HHA  H  N N 211 
HIS N    N  N N 212 
HIS CA   C  N S 213 
HIS C    C  N N 214 
HIS O    O  N N 215 
HIS CB   C  N N 216 
HIS CG   C  Y N 217 
HIS ND1  N  Y N 218 
HIS CD2  C  Y N 219 
HIS CE1  C  Y N 220 
HIS NE2  N  Y N 221 
HIS OXT  O  N N 222 
HIS H    H  N N 223 
HIS H2   H  N N 224 
HIS HA   H  N N 225 
HIS HB2  H  N N 226 
HIS HB3  H  N N 227 
HIS HD1  H  N N 228 
HIS HD2  H  N N 229 
HIS HE1  H  N N 230 
HIS HE2  H  N N 231 
HIS HXT  H  N N 232 
HOH O    O  N N 233 
HOH H1   H  N N 234 
HOH H2   H  N N 235 
HPA N1   N  Y N 236 
HPA C2   C  Y N 237 
HPA N3   N  Y N 238 
HPA C4   C  Y N 239 
HPA C5   C  Y N 240 
HPA C6   C  Y N 241 
HPA O6   O  N N 242 
HPA N7   N  Y N 243 
HPA C8   C  Y N 244 
HPA N9   N  Y N 245 
HPA HN1  H  N N 246 
HPA H2   H  N N 247 
HPA HN7  H  N N 248 
HPA H8   H  N N 249 
ILE N    N  N N 250 
ILE CA   C  N S 251 
ILE C    C  N N 252 
ILE O    O  N N 253 
ILE CB   C  N S 254 
ILE CG1  C  N N 255 
ILE CG2  C  N N 256 
ILE CD1  C  N N 257 
ILE OXT  O  N N 258 
ILE H    H  N N 259 
ILE H2   H  N N 260 
ILE HA   H  N N 261 
ILE HB   H  N N 262 
ILE HG12 H  N N 263 
ILE HG13 H  N N 264 
ILE HG21 H  N N 265 
ILE HG22 H  N N 266 
ILE HG23 H  N N 267 
ILE HD11 H  N N 268 
ILE HD12 H  N N 269 
ILE HD13 H  N N 270 
ILE HXT  H  N N 271 
LEU N    N  N N 272 
LEU CA   C  N S 273 
LEU C    C  N N 274 
LEU O    O  N N 275 
LEU CB   C  N N 276 
LEU CG   C  N N 277 
LEU CD1  C  N N 278 
LEU CD2  C  N N 279 
LEU OXT  O  N N 280 
LEU H    H  N N 281 
LEU H2   H  N N 282 
LEU HA   H  N N 283 
LEU HB2  H  N N 284 
LEU HB3  H  N N 285 
LEU HG   H  N N 286 
LEU HD11 H  N N 287 
LEU HD12 H  N N 288 
LEU HD13 H  N N 289 
LEU HD21 H  N N 290 
LEU HD22 H  N N 291 
LEU HD23 H  N N 292 
LEU HXT  H  N N 293 
LYS N    N  N N 294 
LYS CA   C  N S 295 
LYS C    C  N N 296 
LYS O    O  N N 297 
LYS CB   C  N N 298 
LYS CG   C  N N 299 
LYS CD   C  N N 300 
LYS CE   C  N N 301 
LYS NZ   N  N N 302 
LYS OXT  O  N N 303 
LYS H    H  N N 304 
LYS H2   H  N N 305 
LYS HA   H  N N 306 
LYS HB2  H  N N 307 
LYS HB3  H  N N 308 
LYS HG2  H  N N 309 
LYS HG3  H  N N 310 
LYS HD2  H  N N 311 
LYS HD3  H  N N 312 
LYS HE2  H  N N 313 
LYS HE3  H  N N 314 
LYS HZ1  H  N N 315 
LYS HZ2  H  N N 316 
LYS HZ3  H  N N 317 
LYS HXT  H  N N 318 
MET N    N  N N 319 
MET CA   C  N S 320 
MET C    C  N N 321 
MET O    O  N N 322 
MET CB   C  N N 323 
MET CG   C  N N 324 
MET SD   S  N N 325 
MET CE   C  N N 326 
MET OXT  O  N N 327 
MET H    H  N N 328 
MET H2   H  N N 329 
MET HA   H  N N 330 
MET HB2  H  N N 331 
MET HB3  H  N N 332 
MET HG2  H  N N 333 
MET HG3  H  N N 334 
MET HE1  H  N N 335 
MET HE2  H  N N 336 
MET HE3  H  N N 337 
MET HXT  H  N N 338 
PHE N    N  N N 339 
PHE CA   C  N S 340 
PHE C    C  N N 341 
PHE O    O  N N 342 
PHE CB   C  N N 343 
PHE CG   C  Y N 344 
PHE CD1  C  Y N 345 
PHE CD2  C  Y N 346 
PHE CE1  C  Y N 347 
PHE CE2  C  Y N 348 
PHE CZ   C  Y N 349 
PHE OXT  O  N N 350 
PHE H    H  N N 351 
PHE H2   H  N N 352 
PHE HA   H  N N 353 
PHE HB2  H  N N 354 
PHE HB3  H  N N 355 
PHE HD1  H  N N 356 
PHE HD2  H  N N 357 
PHE HE1  H  N N 358 
PHE HE2  H  N N 359 
PHE HZ   H  N N 360 
PHE HXT  H  N N 361 
PRO N    N  N N 362 
PRO CA   C  N S 363 
PRO C    C  N N 364 
PRO O    O  N N 365 
PRO CB   C  N N 366 
PRO CG   C  N N 367 
PRO CD   C  N N 368 
PRO OXT  O  N N 369 
PRO H    H  N N 370 
PRO HA   H  N N 371 
PRO HB2  H  N N 372 
PRO HB3  H  N N 373 
PRO HG2  H  N N 374 
PRO HG3  H  N N 375 
PRO HD2  H  N N 376 
PRO HD3  H  N N 377 
PRO HXT  H  N N 378 
SER N    N  N N 379 
SER CA   C  N S 380 
SER C    C  N N 381 
SER O    O  N N 382 
SER CB   C  N N 383 
SER OG   O  N N 384 
SER OXT  O  N N 385 
SER H    H  N N 386 
SER H2   H  N N 387 
SER HA   H  N N 388 
SER HB2  H  N N 389 
SER HB3  H  N N 390 
SER HG   H  N N 391 
SER HXT  H  N N 392 
THR N    N  N N 393 
THR CA   C  N S 394 
THR C    C  N N 395 
THR O    O  N N 396 
THR CB   C  N R 397 
THR OG1  O  N N 398 
THR CG2  C  N N 399 
THR OXT  O  N N 400 
THR H    H  N N 401 
THR H2   H  N N 402 
THR HA   H  N N 403 
THR HB   H  N N 404 
THR HG1  H  N N 405 
THR HG21 H  N N 406 
THR HG22 H  N N 407 
THR HG23 H  N N 408 
THR HXT  H  N N 409 
TRP N    N  N N 410 
TRP CA   C  N S 411 
TRP C    C  N N 412 
TRP O    O  N N 413 
TRP CB   C  N N 414 
TRP CG   C  Y N 415 
TRP CD1  C  Y N 416 
TRP CD2  C  Y N 417 
TRP NE1  N  Y N 418 
TRP CE2  C  Y N 419 
TRP CE3  C  Y N 420 
TRP CZ2  C  Y N 421 
TRP CZ3  C  Y N 422 
TRP CH2  C  Y N 423 
TRP OXT  O  N N 424 
TRP H    H  N N 425 
TRP H2   H  N N 426 
TRP HA   H  N N 427 
TRP HB2  H  N N 428 
TRP HB3  H  N N 429 
TRP HD1  H  N N 430 
TRP HE1  H  N N 431 
TRP HE3  H  N N 432 
TRP HZ2  H  N N 433 
TRP HZ3  H  N N 434 
TRP HH2  H  N N 435 
TRP HXT  H  N N 436 
TYR N    N  N N 437 
TYR CA   C  N S 438 
TYR C    C  N N 439 
TYR O    O  N N 440 
TYR CB   C  N N 441 
TYR CG   C  Y N 442 
TYR CD1  C  Y N 443 
TYR CD2  C  Y N 444 
TYR CE1  C  Y N 445 
TYR CE2  C  Y N 446 
TYR CZ   C  Y N 447 
TYR OH   O  N N 448 
TYR OXT  O  N N 449 
TYR H    H  N N 450 
TYR H2   H  N N 451 
TYR HA   H  N N 452 
TYR HB2  H  N N 453 
TYR HB3  H  N N 454 
TYR HD1  H  N N 455 
TYR HD2  H  N N 456 
TYR HE1  H  N N 457 
TYR HE2  H  N N 458 
TYR HH   H  N N 459 
TYR HXT  H  N N 460 
UYM N    N  Y N 461 
UYM C    C  N N 462 
UYM O    O  N N 463 
UYM C1   C  N S 464 
UYM C10  C  Y N 465 
UYM C11  C  N S 466 
UYM C12  C  N N 467 
UYM C15  C  N N 468 
UYM C2   C  N N 469 
UYM C3   C  Y N 470 
UYM C34  C  Y N 471 
UYM C35  C  Y N 472 
UYM C37  C  Y N 473 
UYM C38  C  Y N 474 
UYM C39  C  Y N 475 
UYM C4   C  Y N 476 
UYM C40  C  Y N 477 
UYM C41  C  Y N 478 
UYM C42  C  Y N 479 
UYM C5   C  Y N 480 
UYM C6   C  Y N 481 
UYM C7   C  Y N 482 
UYM C8   C  Y N 483 
UYM C9   C  Y N 484 
UYM N1   N  N N 485 
UYM N2   N  N N 486 
UYM N36  N  Y N 487 
UYM O1   O  N N 488 
UYM H1   H  N N 489 
UYM H2   H  N N 490 
UYM H3   H  N N 491 
UYM H4   H  N N 492 
UYM H5   H  N N 493 
UYM H6   H  N N 494 
UYM H7   H  N N 495 
UYM H8   H  N N 496 
UYM H9   H  N N 497 
UYM H10  H  N N 498 
UYM H11  H  N N 499 
UYM H12  H  N N 500 
UYM H13  H  N N 501 
UYM H14  H  N N 502 
UYM H15  H  N N 503 
UYM H16  H  N N 504 
UYM H17  H  N N 505 
UYM H18  H  N N 506 
UYM H19  H  N N 507 
UYM H20  H  N N 508 
VAL N    N  N N 509 
VAL CA   C  N S 510 
VAL C    C  N N 511 
VAL O    O  N N 512 
VAL CB   C  N N 513 
VAL CG1  C  N N 514 
VAL CG2  C  N N 515 
VAL OXT  O  N N 516 
VAL H    H  N N 517 
VAL H2   H  N N 518 
VAL HA   H  N N 519 
VAL HB   H  N N 520 
VAL HG11 H  N N 521 
VAL HG12 H  N N 522 
VAL HG13 H  N N 523 
VAL HG21 H  N N 524 
VAL HG22 H  N N 525 
VAL HG23 H  N N 526 
VAL HXT  H  N N 527 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HEM CHA C1A  sing N N 129 
HEM CHA C4D  doub N N 130 
HEM CHA HHA  sing N N 131 
HEM CHB C4A  sing N N 132 
HEM CHB C1B  doub N N 133 
HEM CHB HHB  sing N N 134 
HEM CHC C4B  sing N N 135 
HEM CHC C1C  doub N N 136 
HEM CHC HHC  sing N N 137 
HEM CHD C4C  doub N N 138 
HEM CHD C1D  sing N N 139 
HEM CHD HHD  sing N N 140 
HEM C1A C2A  doub Y N 141 
HEM C1A NA   sing Y N 142 
HEM C2A C3A  sing Y N 143 
HEM C2A CAA  sing N N 144 
HEM C3A C4A  doub Y N 145 
HEM C3A CMA  sing N N 146 
HEM C4A NA   sing Y N 147 
HEM CMA HMA  sing N N 148 
HEM CMA HMAA sing N N 149 
HEM CMA HMAB sing N N 150 
HEM CAA CBA  sing N N 151 
HEM CAA HAA  sing N N 152 
HEM CAA HAAA sing N N 153 
HEM CBA CGA  sing N N 154 
HEM CBA HBA  sing N N 155 
HEM CBA HBAA sing N N 156 
HEM CGA O1A  doub N N 157 
HEM CGA O2A  sing N N 158 
HEM C1B C2B  sing N N 159 
HEM C1B NB   sing N N 160 
HEM C2B C3B  doub N N 161 
HEM C2B CMB  sing N N 162 
HEM C3B C4B  sing N N 163 
HEM C3B CAB  sing N N 164 
HEM C4B NB   doub N N 165 
HEM CMB HMB  sing N N 166 
HEM CMB HMBA sing N N 167 
HEM CMB HMBB sing N N 168 
HEM CAB CBB  doub N N 169 
HEM CAB HAB  sing N N 170 
HEM CBB HBB  sing N N 171 
HEM CBB HBBA sing N N 172 
HEM C1C C2C  sing Y N 173 
HEM C1C NC   sing Y N 174 
HEM C2C C3C  doub Y N 175 
HEM C2C CMC  sing N N 176 
HEM C3C C4C  sing Y N 177 
HEM C3C CAC  sing N N 178 
HEM C4C NC   sing Y N 179 
HEM CMC HMC  sing N N 180 
HEM CMC HMCA sing N N 181 
HEM CMC HMCB sing N N 182 
HEM CAC CBC  doub N N 183 
HEM CAC HAC  sing N N 184 
HEM CBC HBC  sing N N 185 
HEM CBC HBCA sing N N 186 
HEM C1D C2D  sing N N 187 
HEM C1D ND   doub N N 188 
HEM C2D C3D  doub N N 189 
HEM C2D CMD  sing N N 190 
HEM C3D C4D  sing N N 191 
HEM C3D CAD  sing N N 192 
HEM C4D ND   sing N N 193 
HEM CMD HMD  sing N N 194 
HEM CMD HMDA sing N N 195 
HEM CMD HMDB sing N N 196 
HEM CAD CBD  sing N N 197 
HEM CAD HAD  sing N N 198 
HEM CAD HADA sing N N 199 
HEM CBD CGD  sing N N 200 
HEM CBD HBD  sing N N 201 
HEM CBD HBDA sing N N 202 
HEM CGD O1D  doub N N 203 
HEM CGD O2D  sing N N 204 
HEM O2A H2A  sing N N 205 
HEM O2D H2D  sing N N 206 
HEM FE  NA   sing N N 207 
HEM FE  NB   sing N N 208 
HEM FE  NC   sing N N 209 
HEM FE  ND   sing N N 210 
HIS N   CA   sing N N 211 
HIS N   H    sing N N 212 
HIS N   H2   sing N N 213 
HIS CA  C    sing N N 214 
HIS CA  CB   sing N N 215 
HIS CA  HA   sing N N 216 
HIS C   O    doub N N 217 
HIS C   OXT  sing N N 218 
HIS CB  CG   sing N N 219 
HIS CB  HB2  sing N N 220 
HIS CB  HB3  sing N N 221 
HIS CG  ND1  sing Y N 222 
HIS CG  CD2  doub Y N 223 
HIS ND1 CE1  doub Y N 224 
HIS ND1 HD1  sing N N 225 
HIS CD2 NE2  sing Y N 226 
HIS CD2 HD2  sing N N 227 
HIS CE1 NE2  sing Y N 228 
HIS CE1 HE1  sing N N 229 
HIS NE2 HE2  sing N N 230 
HIS OXT HXT  sing N N 231 
HOH O   H1   sing N N 232 
HOH O   H2   sing N N 233 
HPA N1  C2   sing Y N 234 
HPA N1  C6   sing Y N 235 
HPA N1  HN1  sing N N 236 
HPA C2  N3   doub Y N 237 
HPA C2  H2   sing N N 238 
HPA N3  C4   sing Y N 239 
HPA C4  C5   doub Y N 240 
HPA C4  N9   sing Y N 241 
HPA C5  C6   sing Y N 242 
HPA C5  N7   sing Y N 243 
HPA C6  O6   doub N N 244 
HPA N7  C8   sing Y N 245 
HPA N7  HN7  sing N N 246 
HPA C8  N9   doub Y N 247 
HPA C8  H8   sing N N 248 
ILE N   CA   sing N N 249 
ILE N   H    sing N N 250 
ILE N   H2   sing N N 251 
ILE CA  C    sing N N 252 
ILE CA  CB   sing N N 253 
ILE CA  HA   sing N N 254 
ILE C   O    doub N N 255 
ILE C   OXT  sing N N 256 
ILE CB  CG1  sing N N 257 
ILE CB  CG2  sing N N 258 
ILE CB  HB   sing N N 259 
ILE CG1 CD1  sing N N 260 
ILE CG1 HG12 sing N N 261 
ILE CG1 HG13 sing N N 262 
ILE CG2 HG21 sing N N 263 
ILE CG2 HG22 sing N N 264 
ILE CG2 HG23 sing N N 265 
ILE CD1 HD11 sing N N 266 
ILE CD1 HD12 sing N N 267 
ILE CD1 HD13 sing N N 268 
ILE OXT HXT  sing N N 269 
LEU N   CA   sing N N 270 
LEU N   H    sing N N 271 
LEU N   H2   sing N N 272 
LEU CA  C    sing N N 273 
LEU CA  CB   sing N N 274 
LEU CA  HA   sing N N 275 
LEU C   O    doub N N 276 
LEU C   OXT  sing N N 277 
LEU CB  CG   sing N N 278 
LEU CB  HB2  sing N N 279 
LEU CB  HB3  sing N N 280 
LEU CG  CD1  sing N N 281 
LEU CG  CD2  sing N N 282 
LEU CG  HG   sing N N 283 
LEU CD1 HD11 sing N N 284 
LEU CD1 HD12 sing N N 285 
LEU CD1 HD13 sing N N 286 
LEU CD2 HD21 sing N N 287 
LEU CD2 HD22 sing N N 288 
LEU CD2 HD23 sing N N 289 
LEU OXT HXT  sing N N 290 
LYS N   CA   sing N N 291 
LYS N   H    sing N N 292 
LYS N   H2   sing N N 293 
LYS CA  C    sing N N 294 
LYS CA  CB   sing N N 295 
LYS CA  HA   sing N N 296 
LYS C   O    doub N N 297 
LYS C   OXT  sing N N 298 
LYS CB  CG   sing N N 299 
LYS CB  HB2  sing N N 300 
LYS CB  HB3  sing N N 301 
LYS CG  CD   sing N N 302 
LYS CG  HG2  sing N N 303 
LYS CG  HG3  sing N N 304 
LYS CD  CE   sing N N 305 
LYS CD  HD2  sing N N 306 
LYS CD  HD3  sing N N 307 
LYS CE  NZ   sing N N 308 
LYS CE  HE2  sing N N 309 
LYS CE  HE3  sing N N 310 
LYS NZ  HZ1  sing N N 311 
LYS NZ  HZ2  sing N N 312 
LYS NZ  HZ3  sing N N 313 
LYS OXT HXT  sing N N 314 
MET N   CA   sing N N 315 
MET N   H    sing N N 316 
MET N   H2   sing N N 317 
MET CA  C    sing N N 318 
MET CA  CB   sing N N 319 
MET CA  HA   sing N N 320 
MET C   O    doub N N 321 
MET C   OXT  sing N N 322 
MET CB  CG   sing N N 323 
MET CB  HB2  sing N N 324 
MET CB  HB3  sing N N 325 
MET CG  SD   sing N N 326 
MET CG  HG2  sing N N 327 
MET CG  HG3  sing N N 328 
MET SD  CE   sing N N 329 
MET CE  HE1  sing N N 330 
MET CE  HE2  sing N N 331 
MET CE  HE3  sing N N 332 
MET OXT HXT  sing N N 333 
PHE N   CA   sing N N 334 
PHE N   H    sing N N 335 
PHE N   H2   sing N N 336 
PHE CA  C    sing N N 337 
PHE CA  CB   sing N N 338 
PHE CA  HA   sing N N 339 
PHE C   O    doub N N 340 
PHE C   OXT  sing N N 341 
PHE CB  CG   sing N N 342 
PHE CB  HB2  sing N N 343 
PHE CB  HB3  sing N N 344 
PHE CG  CD1  doub Y N 345 
PHE CG  CD2  sing Y N 346 
PHE CD1 CE1  sing Y N 347 
PHE CD1 HD1  sing N N 348 
PHE CD2 CE2  doub Y N 349 
PHE CD2 HD2  sing N N 350 
PHE CE1 CZ   doub Y N 351 
PHE CE1 HE1  sing N N 352 
PHE CE2 CZ   sing Y N 353 
PHE CE2 HE2  sing N N 354 
PHE CZ  HZ   sing N N 355 
PHE OXT HXT  sing N N 356 
PRO N   CA   sing N N 357 
PRO N   CD   sing N N 358 
PRO N   H    sing N N 359 
PRO CA  C    sing N N 360 
PRO CA  CB   sing N N 361 
PRO CA  HA   sing N N 362 
PRO C   O    doub N N 363 
PRO C   OXT  sing N N 364 
PRO CB  CG   sing N N 365 
PRO CB  HB2  sing N N 366 
PRO CB  HB3  sing N N 367 
PRO CG  CD   sing N N 368 
PRO CG  HG2  sing N N 369 
PRO CG  HG3  sing N N 370 
PRO CD  HD2  sing N N 371 
PRO CD  HD3  sing N N 372 
PRO OXT HXT  sing N N 373 
SER N   CA   sing N N 374 
SER N   H    sing N N 375 
SER N   H2   sing N N 376 
SER CA  C    sing N N 377 
SER CA  CB   sing N N 378 
SER CA  HA   sing N N 379 
SER C   O    doub N N 380 
SER C   OXT  sing N N 381 
SER CB  OG   sing N N 382 
SER CB  HB2  sing N N 383 
SER CB  HB3  sing N N 384 
SER OG  HG   sing N N 385 
SER OXT HXT  sing N N 386 
THR N   CA   sing N N 387 
THR N   H    sing N N 388 
THR N   H2   sing N N 389 
THR CA  C    sing N N 390 
THR CA  CB   sing N N 391 
THR CA  HA   sing N N 392 
THR C   O    doub N N 393 
THR C   OXT  sing N N 394 
THR CB  OG1  sing N N 395 
THR CB  CG2  sing N N 396 
THR CB  HB   sing N N 397 
THR OG1 HG1  sing N N 398 
THR CG2 HG21 sing N N 399 
THR CG2 HG22 sing N N 400 
THR CG2 HG23 sing N N 401 
THR OXT HXT  sing N N 402 
TRP N   CA   sing N N 403 
TRP N   H    sing N N 404 
TRP N   H2   sing N N 405 
TRP CA  C    sing N N 406 
TRP CA  CB   sing N N 407 
TRP CA  HA   sing N N 408 
TRP C   O    doub N N 409 
TRP C   OXT  sing N N 410 
TRP CB  CG   sing N N 411 
TRP CB  HB2  sing N N 412 
TRP CB  HB3  sing N N 413 
TRP CG  CD1  doub Y N 414 
TRP CG  CD2  sing Y N 415 
TRP CD1 NE1  sing Y N 416 
TRP CD1 HD1  sing N N 417 
TRP CD2 CE2  doub Y N 418 
TRP CD2 CE3  sing Y N 419 
TRP NE1 CE2  sing Y N 420 
TRP NE1 HE1  sing N N 421 
TRP CE2 CZ2  sing Y N 422 
TRP CE3 CZ3  doub Y N 423 
TRP CE3 HE3  sing N N 424 
TRP CZ2 CH2  doub Y N 425 
TRP CZ2 HZ2  sing N N 426 
TRP CZ3 CH2  sing Y N 427 
TRP CZ3 HZ3  sing N N 428 
TRP CH2 HH2  sing N N 429 
TRP OXT HXT  sing N N 430 
TYR N   CA   sing N N 431 
TYR N   H    sing N N 432 
TYR N   H2   sing N N 433 
TYR CA  C    sing N N 434 
TYR CA  CB   sing N N 435 
TYR CA  HA   sing N N 436 
TYR C   O    doub N N 437 
TYR C   OXT  sing N N 438 
TYR CB  CG   sing N N 439 
TYR CB  HB2  sing N N 440 
TYR CB  HB3  sing N N 441 
TYR CG  CD1  doub Y N 442 
TYR CG  CD2  sing Y N 443 
TYR CD1 CE1  sing Y N 444 
TYR CD1 HD1  sing N N 445 
TYR CD2 CE2  doub Y N 446 
TYR CD2 HD2  sing N N 447 
TYR CE1 CZ   doub Y N 448 
TYR CE1 HE1  sing N N 449 
TYR CE2 CZ   sing Y N 450 
TYR CE2 HE2  sing N N 451 
TYR CZ  OH   sing N N 452 
TYR OH  HH   sing N N 453 
TYR OXT HXT  sing N N 454 
UYM C8  C9   doub Y N 455 
UYM C8  C7   sing Y N 456 
UYM C9  C10  sing Y N 457 
UYM C7  C6   doub Y N 458 
UYM C10 C5   doub Y N 459 
UYM C6  C5   sing Y N 460 
UYM C6  C3   sing Y N 461 
UYM C5  N    sing Y N 462 
UYM O   C    doub N N 463 
UYM C3  C2   sing N N 464 
UYM C3  C4   doub Y N 465 
UYM C1  C    sing N N 466 
UYM C1  C2   sing N N 467 
UYM C1  N1   sing N N 468 
UYM N   C4   sing Y N 469 
UYM C   N2   sing N N 470 
UYM N1  C15  sing N N 471 
UYM N2  C11  sing N N 472 
UYM C15 C11  sing N N 473 
UYM C15 O1   doub N N 474 
UYM C11 C12  sing N N 475 
UYM C35 C34  doub Y N 476 
UYM C35 N36  sing Y N 477 
UYM C12 C34  sing N N 478 
UYM C34 C38  sing Y N 479 
UYM N36 C37  sing Y N 480 
UYM C38 C37  doub Y N 481 
UYM C38 C39  sing Y N 482 
UYM C37 C42  sing Y N 483 
UYM C39 C40  doub Y N 484 
UYM C42 C41  doub Y N 485 
UYM C40 C41  sing Y N 486 
UYM N   H1   sing N N 487 
UYM C1  H2   sing N N 488 
UYM C10 H3   sing N N 489 
UYM C11 H4   sing N N 490 
UYM C12 H5   sing N N 491 
UYM C12 H6   sing N N 492 
UYM C2  H7   sing N N 493 
UYM C2  H8   sing N N 494 
UYM C35 H9   sing N N 495 
UYM C39 H10  sing N N 496 
UYM C4  H11  sing N N 497 
UYM C40 H12  sing N N 498 
UYM C41 H13  sing N N 499 
UYM C42 H14  sing N N 500 
UYM C7  H15  sing N N 501 
UYM C8  H16  sing N N 502 
UYM C9  H17  sing N N 503 
UYM N1  H18  sing N N 504 
UYM N2  H19  sing N N 505 
UYM N36 H20  sing N N 506 
VAL N   CA   sing N N 507 
VAL N   H    sing N N 508 
VAL N   H2   sing N N 509 
VAL CA  C    sing N N 510 
VAL CA  CB   sing N N 511 
VAL CA  HA   sing N N 512 
VAL C   O    doub N N 513 
VAL C   OXT  sing N N 514 
VAL CB  CG1  sing N N 515 
VAL CB  CG2  sing N N 516 
VAL CB  HB   sing N N 517 
VAL CG1 HG11 sing N N 518 
VAL CG1 HG12 sing N N 519 
VAL CG1 HG13 sing N N 520 
VAL CG2 HG21 sing N N 521 
VAL CG2 HG22 sing N N 522 
VAL CG2 HG23 sing N N 523 
VAL OXT HXT  sing N N 524 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           31800052 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YY7 
_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]   0.011769 
_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]   0.011769 
_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]   0.007341 
_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  
FE 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . PRO A 1 19  ? 0.107   9.546   -7.148  1.00 81.24 ?  19  PRO A N   1 
ATOM   2    C  CA  . PRO A 1 19  ? -1.251  9.038   -6.889  1.00 68.21 ?  19  PRO A CA  1 
ATOM   3    C  C   . PRO A 1 19  ? -2.287  10.148  -6.746  1.00 54.96 ?  19  PRO A C   1 
ATOM   4    O  O   . PRO A 1 19  ? -2.147  11.034  -5.898  1.00 53.13 ?  19  PRO A O   1 
ATOM   5    C  CB  . PRO A 1 19  ? -1.075  8.257   -5.584  1.00 72.85 ?  19  PRO A CB  1 
ATOM   6    C  CG  . PRO A 1 19  ? 0.026   9.004   -4.861  1.00 78.84 ?  19  PRO A CG  1 
ATOM   7    C  CD  . PRO A 1 19  ? 0.918   9.625   -5.917  1.00 80.87 ?  19  PRO A CD  1 
ATOM   8    N  N   . LEU A 1 20  ? -3.335  10.114  -7.562  1.00 46.28 ?  20  LEU A N   1 
ATOM   9    C  CA  . LEU A 1 20  ? -4.306  11.206  -7.500  1.00 45.99 ?  20  LEU A CA  1 
ATOM   10   C  C   . LEU A 1 20  ? -5.281  10.990  -6.339  1.00 34.92 ?  20  LEU A C   1 
ATOM   11   O  O   . LEU A 1 20  ? -5.731  9.863   -6.103  1.00 34.30 ?  20  LEU A O   1 
ATOM   12   C  CB  . LEU A 1 20  ? -5.087  11.308  -8.808  1.00 32.45 ?  20  LEU A CB  1 
ATOM   13   C  CG  . LEU A 1 20  ? -4.339  11.688  -10.098 1.00 34.97 ?  20  LEU A CG  1 
ATOM   14   C  CD1 . LEU A 1 20  ? -5.271  11.587  -11.297 1.00 30.03 ?  20  LEU A CD1 1 
ATOM   15   C  CD2 . LEU A 1 20  ? -3.714  13.080  -10.025 1.00 33.64 ?  20  LEU A CD2 1 
ATOM   16   N  N   . PRO A 1 21  ? -5.608  12.045  -5.594  1.00 32.57 ?  21  PRO A N   1 
ATOM   17   C  CA  . PRO A 1 21  ? -6.669  11.929  -4.587  1.00 30.23 ?  21  PRO A CA  1 
ATOM   18   C  C   . PRO A 1 21  ? -7.981  11.506  -5.224  1.00 27.86 ?  21  PRO A C   1 
ATOM   19   O  O   . PRO A 1 21  ? -8.291  11.874  -6.360  1.00 26.00 ?  21  PRO A O   1 
ATOM   20   C  CB  . PRO A 1 21  ? -6.762  13.335  -3.980  1.00 28.19 ?  21  PRO A CB  1 
ATOM   21   C  CG  . PRO A 1 21  ? -5.646  14.115  -4.504  1.00 26.27 ?  21  PRO A CG  1 
ATOM   22   C  CD  . PRO A 1 21  ? -4.899  13.333  -5.543  1.00 29.84 ?  21  PRO A CD  1 
ATOM   23   N  N   . ASP A 1 22  ? -8.736  10.693  -4.496  1.00 22.90 ?  22  ASP A N   1 
ATOM   24   C  CA  . ASP A 1 22  ? -10.014 10.210  -4.986  1.00 27.45 ?  22  ASP A CA  1 
ATOM   25   C  C   . ASP A 1 22  ? -11.116 11.200  -4.645  1.00 22.81 ?  22  ASP A C   1 
ATOM   26   O  O   . ASP A 1 22  ? -11.060 11.898  -3.632  1.00 21.12 ?  22  ASP A O   1 
ATOM   27   C  CB  . ASP A 1 22  ? -10.359 8.841   -4.392  1.00 28.37 ?  22  ASP A CB  1 
ATOM   28   C  CG  . ASP A 1 22  ? -9.487  7.735   -4.950  1.00 33.17 ?  22  ASP A CG  1 
ATOM   29   O  OD1 . ASP A 1 22  ? -9.493  7.514   -6.182  1.00 32.33 ?  22  ASP A OD1 1 
ATOM   30   O  OD2 . ASP A 1 22  ? -8.782  7.099   -4.150  1.00 35.00 ?  22  ASP A OD2 1 
ATOM   31   N  N   . PHE A 1 23  ? -12.122 11.250  -5.509  1.00 21.32 ?  23  PHE A N   1 
ATOM   32   C  CA  . PHE A 1 23  ? -13.343 11.985  -5.238  1.00 21.88 ?  23  PHE A CA  1 
ATOM   33   C  C   . PHE A 1 23  ? -14.494 11.053  -5.588  1.00 24.17 ?  23  PHE A C   1 
ATOM   34   O  O   . PHE A 1 23  ? -14.374 10.266  -6.543  1.00 24.11 ?  23  PHE A O   1 
ATOM   35   C  CB  . PHE A 1 23  ? -13.404 13.281  -6.076  1.00 20.71 ?  23  PHE A CB  1 
ATOM   36   C  CG  . PHE A 1 23  ? -14.539 14.199  -5.699  1.00 22.32 ?  23  PHE A CG  1 
ATOM   37   C  CD1 . PHE A 1 23  ? -14.462 14.979  -4.554  1.00 21.15 ?  23  PHE A CD1 1 
ATOM   38   C  CD2 . PHE A 1 23  ? -15.675 14.280  -6.479  1.00 21.56 ?  23  PHE A CD2 1 
ATOM   39   C  CE1 . PHE A 1 23  ? -15.516 15.819  -4.185  1.00 18.12 ?  23  PHE A CE1 1 
ATOM   40   C  CE2 . PHE A 1 23  ? -16.728 15.118  -6.115  1.00 18.40 ?  23  PHE A CE2 1 
ATOM   41   C  CZ  . PHE A 1 23  ? -16.632 15.888  -4.967  1.00 18.52 ?  23  PHE A CZ  1 
ATOM   42   N  N   . PRO A 1 24  ? -15.610 11.085  -4.842  1.00 22.24 ?  24  PRO A N   1 
ATOM   43   C  CA  . PRO A 1 24  ? -16.029 11.964  -3.735  1.00 25.09 ?  24  PRO A CA  1 
ATOM   44   C  C   . PRO A 1 24  ? -15.327 11.660  -2.418  1.00 22.36 ?  24  PRO A C   1 
ATOM   45   O  O   . PRO A 1 24  ? -14.616 10.657  -2.325  1.00 19.79 ?  24  PRO A O   1 
ATOM   46   C  CB  . PRO A 1 24  ? -17.528 11.694  -3.619  1.00 23.06 ?  24  PRO A CB  1 
ATOM   47   C  CG  . PRO A 1 24  ? -17.690 10.295  -4.126  1.00 26.39 ?  24  PRO A CG  1 
ATOM   48   C  CD  . PRO A 1 24  ? -16.604 10.035  -5.124  1.00 24.99 ?  24  PRO A CD  1 
ATOM   49   N  N   . LEU A 1 25  ? -15.558 12.497  -1.401  1.00 24.45 ?  25  LEU A N   1 
ATOM   50   C  CA  . LEU A 1 25  ? -14.647 12.582  -0.261  1.00 24.93 ?  25  LEU A CA  1 
ATOM   51   C  C   . LEU A 1 25  ? -14.912 11.577  0.853   1.00 34.80 ?  25  LEU A C   1 
ATOM   52   O  O   . LEU A 1 25  ? -13.963 10.993  1.394   1.00 43.38 ?  25  LEU A O   1 
ATOM   53   C  CB  . LEU A 1 25  ? -14.673 14.000  0.327   1.00 24.23 ?  25  LEU A CB  1 
ATOM   54   C  CG  . LEU A 1 25  ? -14.132 15.034  -0.650  1.00 28.68 ?  25  LEU A CG  1 
ATOM   55   C  CD1 . LEU A 1 25  ? -14.308 16.436  -0.095  1.00 25.53 ?  25  LEU A CD1 1 
ATOM   56   C  CD2 . LEU A 1 25  ? -12.658 14.750  -0.891  1.00 23.48 ?  25  LEU A CD2 1 
ATOM   57   N  N   . SER A 1 26  ? -16.170 11.401  1.236   1.00 29.61 ?  26  SER A N   1 
ATOM   58   C  CA  . SER A 1 26  ? -16.544 10.606  2.407   1.00 30.79 ?  26  SER A CA  1 
ATOM   59   C  C   . SER A 1 26  ? -18.044 10.772  2.421   1.00 26.82 ?  26  SER A C   1 
ATOM   60   O  O   . SER A 1 26  ? -18.551 11.787  1.926   1.00 23.11 ?  26  SER A O   1 
ATOM   61   C  CB  . SER A 1 26  ? -15.805 10.995  3.689   1.00 30.33 ?  26  SER A CB  1 
ATOM   62   O  OG  . SER A 1 26  ? -16.494 10.448  4.823   1.00 25.35 ?  26  SER A OG  1 
ATOM   63   N  N   . ARG A 1 27  ? -18.745 9.797   3.003   1.00 27.06 ?  27  ARG A N   1 
ATOM   64   C  CA  . ARG A 1 27  ? -20.203 9.764   2.971   1.00 27.05 ?  27  ARG A CA  1 
ATOM   65   C  C   . ARG A 1 27  ? -20.665 10.260  4.330   1.00 24.48 ?  27  ARG A C   1 
ATOM   66   O  O   . ARG A 1 27  ? -21.834 10.651  4.476   1.00 21.99 ?  27  ARG A O   1 
ATOM   67   C  CB  . ARG A 1 27  ? -20.782 8.379   2.692   1.00 24.89 ?  27  ARG A CB  1 
ATOM   68   C  CG  . ARG A 1 27  ? -20.450 7.861   1.312   1.00 29.42 ?  27  ARG A CG  1 
ATOM   69   C  CD  . ARG A 1 27  ? -21.040 8.749   0.216   1.00 32.22 ?  27  ARG A CD  1 
ATOM   70   N  NE  . ARG A 1 27  ? -20.184 9.875   -0.135  1.00 34.51 ?  27  ARG A NE  1 
ATOM   71   C  CZ  . ARG A 1 27  ? -20.600 10.951  -0.788  1.00 30.22 ?  27  ARG A CZ  1 
ATOM   72   N  NH1 . ARG A 1 27  ? -21.851 11.066  -1.204  1.00 28.19 ?  27  ARG A NH1 1 
ATOM   73   N  NH2 . ARG A 1 27  ? -19.741 11.938  -1.020  1.00 25.82 ?  27  ARG A NH2 1 
ATOM   74   N  N   . ARG A 1 28  ? -19.772 10.274  5.311   1.00 20.06 ?  28  ARG A N   1 
ATOM   75   C  CA  . ARG A 1 28  ? -20.141 10.664  6.662   1.00 23.11 ?  28  ARG A CA  1 
ATOM   76   C  C   . ARG A 1 28  ? -20.404 12.162  6.680   1.00 23.00 ?  28  ARG A C   1 
ATOM   77   O  O   . ARG A 1 28  ? -19.537 12.954  6.292   1.00 24.67 ?  28  ARG A O   1 
ATOM   78   C  CB  . ARG A 1 28  ? -19.034 10.289  7.639   1.00 26.10 ?  28  ARG A CB  1 
ATOM   79   C  CG  . ARG A 1 28  ? -19.133 11.022  8.977   1.00 31.12 ?  28  ARG A CG  1 
ATOM   80   C  CD  . ARG A 1 28  ? -18.099 10.503  9.972   1.00 33.78 ?  28  ARG A CD  1 
ATOM   81   N  NE  . ARG A 1 28  ? -18.352 11.017  11.309  1.00 36.74 ?  28  ARG A NE  1 
ATOM   82   C  CZ  . ARG A 1 28  ? -17.661 10.665  12.384  1.00 39.52 ?  28  ARG A CZ  1 
ATOM   83   N  NH1 . ARG A 1 28  ? -16.657 9.806   12.309  1.00 45.44 ?  28  ARG A NH1 1 
ATOM   84   N  NH2 . ARG A 1 28  ? -17.985 11.189  13.561  1.00 36.14 ?  28  ARG A NH2 1 
ATOM   85   N  N   . GLY A 1 29  ? -21.613 12.547  7.084   1.00 21.81 ?  29  GLY A N   1 
ATOM   86   C  CA  . GLY A 1 29  ? -22.058 13.918  6.951   1.00 21.73 ?  29  GLY A CA  1 
ATOM   87   C  C   . GLY A 1 29  ? -22.099 14.733  8.220   1.00 24.12 ?  29  GLY A C   1 
ATOM   88   O  O   . GLY A 1 29  ? -22.621 15.857  8.197   1.00 23.23 ?  29  GLY A O   1 
ATOM   89   N  N   . ASP A 1 30  ? -21.585 14.231  9.336   1.00 21.78 ?  30  ASP A N   1 
ATOM   90   C  CA  . ASP A 1 30  ? -21.761 15.014  10.551  1.00 28.13 ?  30  ASP A CA  1 
ATOM   91   C  C   . ASP A 1 30  ? -20.523 15.799  10.950  1.00 25.13 ?  30  ASP A C   1 
ATOM   92   O  O   . ASP A 1 30  ? -20.619 16.609  11.873  1.00 29.49 ?  30  ASP A O   1 
ATOM   93   C  CB  . ASP A 1 30  ? -22.214 14.126  11.722  1.00 27.92 ?  30  ASP A CB  1 
ATOM   94   C  CG  . ASP A 1 30  ? -21.189 13.101  12.105  1.00 29.78 ?  30  ASP A CG  1 
ATOM   95   O  OD1 . ASP A 1 30  ? -20.893 12.212  11.275  1.00 31.91 ?  30  ASP A OD1 1 
ATOM   96   O  OD2 . ASP A 1 30  ? -20.685 13.182  13.244  1.00 30.60 ?  30  ASP A OD2 1 
ATOM   97   N  N   . ILE A 1 31  ? -19.376 15.578  10.287  1.00 23.99 ?  31  ILE A N   1 
ATOM   98   C  CA  . ILE A 1 31  ? -18.187 16.416  10.423  1.00 26.05 ?  31  ILE A CA  1 
ATOM   99   C  C   . ILE A 1 31  ? -17.552 16.616  9.052   1.00 24.24 ?  31  ILE A C   1 
ATOM   100  O  O   . ILE A 1 31  ? -17.637 15.758  8.169   1.00 19.97 ?  31  ILE A O   1 
ATOM   101  C  CB  . ILE A 1 31  ? -17.132 15.832  11.396  1.00 28.02 ?  31  ILE A CB  1 
ATOM   102  C  CG1 . ILE A 1 31  ? -16.807 14.374  11.035  1.00 28.68 ?  31  ILE A CG1 1 
ATOM   103  C  CG2 . ILE A 1 31  ? -17.604 15.957  12.839  1.00 32.60 ?  31  ILE A CG2 1 
ATOM   104  C  CD1 . ILE A 1 31  ? -15.437 13.904  11.526  1.00 40.50 ?  31  ILE A CD1 1 
ATOM   105  N  N   . LEU A 1 32  ? -16.918 17.759  8.876   1.00 21.93 ?  32  LEU A N   1 
ATOM   106  C  CA  . LEU A 1 32  ? -16.204 18.021  7.632   1.00 23.73 ?  32  LEU A CA  1 
ATOM   107  C  C   . LEU A 1 32  ? -15.186 16.907  7.385   1.00 19.52 ?  32  LEU A C   1 
ATOM   108  O  O   . LEU A 1 32  ? -14.426 16.569  8.294   1.00 24.24 ?  32  LEU A O   1 
ATOM   109  C  CB  . LEU A 1 32  ? -15.491 19.372  7.704   1.00 17.17 ?  32  LEU A CB  1 
ATOM   110  C  CG  . LEU A 1 32  ? -14.759 19.811  6.433   1.00 20.54 ?  32  LEU A CG  1 
ATOM   111  C  CD1 . LEU A 1 32  ? -15.769 20.162  5.361   1.00 17.68 ?  32  LEU A CD1 1 
ATOM   112  C  CD2 . LEU A 1 32  ? -13.896 21.025  6.733   1.00 21.90 ?  32  LEU A CD2 1 
ATOM   113  N  N   . PRO A 1 33  ? -15.161 16.295  6.202   1.00 19.37 ?  33  PRO A N   1 
ATOM   114  C  CA  . PRO A 1 33  ? -14.083 15.339  5.900   1.00 24.18 ?  33  PRO A CA  1 
ATOM   115  C  C   . PRO A 1 33  ? -12.736 16.019  6.065   1.00 24.89 ?  33  PRO A C   1 
ATOM   116  O  O   . PRO A 1 33  ? -12.509 17.110  5.532   1.00 23.48 ?  33  PRO A O   1 
ATOM   117  C  CB  . PRO A 1 33  ? -14.336 14.948  4.439   1.00 20.18 ?  33  PRO A CB  1 
ATOM   118  C  CG  . PRO A 1 33  ? -15.793 15.268  4.195   1.00 27.20 ?  33  PRO A CG  1 
ATOM   119  C  CD  . PRO A 1 33  ? -16.091 16.472  5.071   1.00 20.90 ?  33  PRO A CD  1 
ATOM   120  N  N   . ALA A 1 34  ? -11.850 15.381  6.833   1.00 24.58 ?  34  ALA A N   1 
ATOM   121  C  CA  . ALA A 1 34  ? -10.502 15.915  7.005   1.00 27.39 ?  34  ALA A CA  1 
ATOM   122  C  C   . ALA A 1 34  ? -9.853  16.211  5.661   1.00 29.48 ?  34  ALA A C   1 
ATOM   123  O  O   . ALA A 1 34  ? -9.117  17.194  5.528   1.00 32.90 ?  34  ALA A O   1 
ATOM   124  C  CB  . ALA A 1 34  ? -9.639  14.936  7.811   1.00 28.36 ?  34  ALA A CB  1 
ATOM   125  N  N   . GLU A 1 35  ? -10.149 15.398  4.647   1.00 29.45 ?  35  GLU A N   1 
ATOM   126  C  CA  . GLU A 1 35  ? -9.567  15.609  3.328   1.00 28.58 ?  35  GLU A CA  1 
ATOM   127  C  C   . GLU A 1 35  ? -9.964  16.962  2.738   1.00 30.90 ?  35  GLU A C   1 
ATOM   128  O  O   . GLU A 1 35  ? -9.165  17.584  2.028   1.00 29.43 ?  35  GLU A O   1 
ATOM   129  C  CB  . GLU A 1 35  ? -9.971  14.449  2.409   1.00 29.77 ?  35  GLU A CB  1 
ATOM   130  C  CG  . GLU A 1 35  ? -9.512  14.561  0.966   1.00 34.96 ?  35  GLU A CG  1 
ATOM   131  C  CD  . GLU A 1 35  ? -8.038  14.232  0.778   1.00 38.12 ?  35  GLU A CD  1 
ATOM   132  O  OE1 . GLU A 1 35  ? -7.282  14.303  1.766   1.00 38.06 ?  35  GLU A OE1 1 
ATOM   133  O  OE2 . GLU A 1 35  ? -7.627  13.912  -0.359  1.00 39.62 ?  35  GLU A OE2 1 
ATOM   134  N  N   . ALA A 1 36  ? -11.173 17.447  3.040   1.00 25.84 ?  36  ALA A N   1 
ATOM   135  C  CA  . ALA A 1 36  ? -11.591 18.756  2.538   1.00 33.20 ?  36  ALA A CA  1 
ATOM   136  C  C   . ALA A 1 36  ? -10.697 19.867  3.077   1.00 30.95 ?  36  ALA A C   1 
ATOM   137  O  O   . ALA A 1 36  ? -10.324 20.794  2.344   1.00 29.44 ?  36  ALA A O   1 
ATOM   138  C  CB  . ALA A 1 36  ? -13.055 19.024  2.901   1.00 26.52 ?  36  ALA A CB  1 
ATOM   139  N  N   . GLU A 1 37  ? -10.350 19.801  4.361   1.00 28.78 ?  37  GLU A N   1 
ATOM   140  C  CA  . GLU A 1 37  ? -9.452  20.802  4.925   1.00 29.10 ?  37  GLU A CA  1 
ATOM   141  C  C   . GLU A 1 37  ? -8.039  20.670  4.364   1.00 30.34 ?  37  GLU A C   1 
ATOM   142  O  O   . GLU A 1 37  ? -7.345  21.675  4.182   1.00 29.88 ?  37  GLU A O   1 
ATOM   143  C  CB  . GLU A 1 37  ? -9.445  20.697  6.449   1.00 30.49 ?  37  GLU A CB  1 
ATOM   144  C  CG  . GLU A 1 37  ? -8.594  21.747  7.120   1.00 35.88 ?  37  GLU A CG  1 
ATOM   145  C  CD  . GLU A 1 37  ? -8.642  21.651  8.626   1.00 44.60 ?  37  GLU A CD  1 
ATOM   146  O  OE1 . GLU A 1 37  ? -9.320  20.730  9.128   1.00 43.49 ?  37  GLU A OE1 1 
ATOM   147  O  OE2 . GLU A 1 37  ? -8.000  22.483  9.299   1.00 47.57 ?  37  GLU A OE2 1 
ATOM   148  N  N   . ARG A 1 38  ? -7.591  19.442  4.089   1.00 30.71 ?  38  ARG A N   1 
ATOM   149  C  CA  . ARG A 1 38  ? -6.247  19.263  3.551   1.00 30.56 ?  38  ARG A CA  1 
ATOM   150  C  C   . ARG A 1 38  ? -6.152  19.770  2.116   1.00 27.36 ?  38  ARG A C   1 
ATOM   151  O  O   . ARG A 1 38  ? -5.195  20.463  1.752   1.00 27.57 ?  38  ARG A O   1 
ATOM   152  C  CB  . ARG A 1 38  ? -5.835  17.796  3.618   1.00 30.82 ?  38  ARG A CB  1 
ATOM   153  C  CG  . ARG A 1 38  ? -4.343  17.590  3.403   1.00 31.49 ?  38  ARG A CG  1 
ATOM   154  C  CD  . ARG A 1 38  ? -4.010  16.179  2.966   1.00 36.73 ?  38  ARG A CD  1 
ATOM   155  N  NE  . ARG A 1 38  ? -4.689  15.782  1.735   1.00 37.33 ?  38  ARG A NE  1 
ATOM   156  C  CZ  . ARG A 1 38  ? -4.370  16.233  0.529   1.00 39.28 ?  38  ARG A CZ  1 
ATOM   157  N  NH1 . ARG A 1 38  ? -3.421  17.144  0.358   1.00 32.76 ?  38  ARG A NH1 1 
ATOM   158  N  NH2 . ARG A 1 38  ? -5.023  15.765  -0.534  1.00 38.17 ?  38  ARG A NH2 1 
ATOM   159  N  N   . LEU A 1 39  ? -7.118  19.400  1.277   1.00 29.32 ?  39  LEU A N   1 
ATOM   160  C  CA  . LEU A 1 39  ? -7.159  19.928  -0.085  1.00 28.99 ?  39  LEU A CA  1 
ATOM   161  C  C   . LEU A 1 39  ? -7.145  21.452  -0.085  1.00 28.69 ?  39  LEU A C   1 
ATOM   162  O  O   . LEU A 1 39  ? -6.363  22.079  -0.807  1.00 29.45 ?  39  LEU A O   1 
ATOM   163  C  CB  . LEU A 1 39  ? -8.400  19.405  -0.801  1.00 27.52 ?  39  LEU A CB  1 
ATOM   164  C  CG  . LEU A 1 39  ? -8.455  17.896  -1.036  1.00 27.85 ?  39  LEU A CG  1 
ATOM   165  C  CD1 . LEU A 1 39  ? -9.862  17.505  -1.431  1.00 30.11 ?  39  LEU A CD1 1 
ATOM   166  C  CD2 . LEU A 1 39  ? -7.514  17.529  -2.154  1.00 35.31 ?  39  LEU A CD2 1 
ATOM   167  N  N   . ARG A 1 40  ? -7.996  22.074  0.734   1.00 29.19 ?  40  ARG A N   1 
ATOM   168  C  CA  . ARG A 1 40  ? -8.109  23.527  0.671   1.00 31.72 ?  40  ARG A CA  1 
ATOM   169  C  C   . ARG A 1 40  ? -6.810  24.203  1.081   1.00 33.20 ?  40  ARG A C   1 
ATOM   170  O  O   . ARG A 1 40  ? -6.423  25.225  0.501   1.00 35.43 ?  40  ARG A O   1 
ATOM   171  C  CB  . ARG A 1 40  ? -9.258  24.023  1.545   1.00 27.41 ?  40  ARG A CB  1 
ATOM   172  C  CG  . ARG A 1 40  ? -9.431  25.524  1.434   1.00 28.79 ?  40  ARG A CG  1 
ATOM   173  C  CD  . ARG A 1 40  ? -10.489 26.027  2.370   1.00 25.40 ?  40  ARG A CD  1 
ATOM   174  N  NE  . ARG A 1 40  ? -10.186 25.644  3.741   1.00 30.67 ?  40  ARG A NE  1 
ATOM   175  C  CZ  . ARG A 1 40  ? -10.972 24.881  4.488   1.00 29.53 ?  40  ARG A CZ  1 
ATOM   176  N  NH1 . ARG A 1 40  ? -12.155 24.455  4.045   1.00 20.83 ?  40  ARG A NH1 1 
ATOM   177  N  NH2 . ARG A 1 40  ? -10.575 24.553  5.714   1.00 35.73 ?  40  ARG A NH2 1 
ATOM   178  N  N   . ALA A 1 41  ? -6.113  23.636  2.067   1.00 31.53 ?  41  ALA A N   1 
ATOM   179  C  CA  . ALA A 1 41  ? -4.922  24.276  2.610   1.00 30.48 ?  41  ALA A CA  1 
ATOM   180  C  C   . ALA A 1 41  ? -3.690  24.075  1.733   1.00 35.77 ?  41  ALA A C   1 
ATOM   181  O  O   . ALA A 1 41  ? -2.831  24.962  1.678   1.00 39.95 ?  41  ALA A O   1 
ATOM   182  C  CB  . ALA A 1 41  ? -4.648  23.749  4.020   1.00 34.37 ?  41  ALA A CB  1 
ATOM   183  N  N   . GLU A 1 42  ? -3.583  22.945  1.038   1.00 31.99 ?  42  GLU A N   1 
ATOM   184  C  CA  . GLU A 1 42  ? -2.366  22.600  0.309   1.00 34.43 ?  42  GLU A CA  1 
ATOM   185  C  C   . GLU A 1 42  ? -2.523  22.675  -1.199  1.00 33.63 ?  42  GLU A C   1 
ATOM   186  O  O   . GLU A 1 42  ? -1.575  23.036  -1.893  1.00 35.74 ?  42  GLU A O   1 
ATOM   187  C  CB  . GLU A 1 42  ? -1.901  21.187  0.681   1.00 32.24 ?  42  GLU A CB  1 
ATOM   188  C  CG  . GLU A 1 42  ? -1.612  20.986  2.170   1.00 33.88 ?  42  GLU A CG  1 
ATOM   189  C  CD  . GLU A 1 42  ? -1.369  19.517  2.537   1.00 35.48 ?  42  GLU A CD  1 
ATOM   190  O  OE1 . GLU A 1 42  ? -1.677  18.618  1.725   1.00 34.52 ?  42  GLU A OE1 1 
ATOM   191  O  OE2 . GLU A 1 42  ? -0.864  19.263  3.645   1.00 46.63 ?  42  GLU A OE2 1 
ATOM   192  N  N   . GLN A 1 43  ? -3.686  22.317  -1.734  1.00 29.16 ?  43  GLN A N   1 
ATOM   193  C  CA  . GLN A 1 43  ? -3.919  22.352  -3.177  1.00 28.47 ?  43  GLN A CA  1 
ATOM   194  C  C   . GLN A 1 43  ? -5.369  22.737  -3.444  1.00 24.07 ?  43  GLN A C   1 
ATOM   195  O  O   . GLN A 1 43  ? -6.195  21.908  -3.844  1.00 22.71 ?  43  GLN A O   1 
ATOM   196  C  CB  . GLN A 1 43  ? -3.554  21.016  -3.826  1.00 29.31 ?  43  GLN A CB  1 
ATOM   197  C  CG  . GLN A 1 43  ? -4.393  19.829  -3.389  1.00 37.60 ?  43  GLN A CG  1 
ATOM   198  C  CD  . GLN A 1 43  ? -3.959  18.540  -4.086  1.00 40.66 ?  43  GLN A CD  1 
ATOM   199  O  OE1 . GLN A 1 43  ? -2.837  18.453  -4.594  1.00 41.20 ?  43  GLN A OE1 1 
ATOM   200  N  NE2 . GLN A 1 43  ? -4.840  17.534  -4.103  1.00 42.12 ?  43  GLN A NE2 1 
ATOM   201  N  N   . PRO A 1 44  ? -5.708  24.017  -3.260  1.00 27.12 ?  44  PRO A N   1 
ATOM   202  C  CA  . PRO A 1 44  ? -7.114  24.438  -3.404  1.00 20.72 ?  44  PRO A CA  1 
ATOM   203  C  C   . PRO A 1 44  ? -7.687  24.211  -4.790  1.00 24.14 ?  44  PRO A C   1 
ATOM   204  O  O   . PRO A 1 44  ? -8.915  24.160  -4.925  1.00 23.61 ?  44  PRO A O   1 
ATOM   205  C  CB  . PRO A 1 44  ? -7.071  25.931  -3.040  1.00 23.59 ?  44  PRO A CB  1 
ATOM   206  C  CG  . PRO A 1 44  ? -5.644  26.350  -3.331  1.00 21.14 ?  44  PRO A CG  1 
ATOM   207  C  CD  . PRO A 1 44  ? -4.823  25.145  -2.918  1.00 24.65 ?  44  PRO A CD  1 
ATOM   208  N  N   . VAL A 1 45  ? -6.853  24.092  -5.823  1.00 21.39 ?  45  VAL A N   1 
ATOM   209  C  CA  . VAL A 1 45  ? -7.257  23.543  -7.115  1.00 19.77 ?  45  VAL A CA  1 
ATOM   210  C  C   . VAL A 1 45  ? -6.428  22.286  -7.303  1.00 23.25 ?  45  VAL A C   1 
ATOM   211  O  O   . VAL A 1 45  ? -5.201  22.360  -7.464  1.00 23.71 ?  45  VAL A O   1 
ATOM   212  C  CB  . VAL A 1 45  ? -7.046  24.528  -8.276  1.00 24.31 ?  45  VAL A CB  1 
ATOM   213  C  CG1 . VAL A 1 45  ? -7.551  23.926  -9.594  1.00 18.65 ?  45  VAL A CG1 1 
ATOM   214  C  CG2 . VAL A 1 45  ? -7.763  25.842  -7.998  1.00 24.83 ?  45  VAL A CG2 1 
ATOM   215  N  N   . ALA A 1 46  ? -7.078  21.129  -7.245  1.00 23.23 ?  46  ALA A N   1 
ATOM   216  C  CA  . ALA A 1 46  ? -6.373  19.854  -7.166  1.00 24.13 ?  46  ALA A CA  1 
ATOM   217  C  C   . ALA A 1 46  ? -6.902  18.906  -8.227  1.00 22.71 ?  46  ALA A C   1 
ATOM   218  O  O   . ALA A 1 46  ? -8.117  18.761  -8.374  1.00 22.50 ?  46  ALA A O   1 
ATOM   219  C  CB  . ALA A 1 46  ? -6.545  19.221  -5.777  1.00 23.60 ?  46  ALA A CB  1 
ATOM   220  N  N   . ARG A 1 47  ? -5.994  18.270  -8.966  1.00 22.25 ?  47  ARG A N   1 
ATOM   221  C  CA  . ARG A 1 47  ? -6.388  17.200  -9.866  1.00 24.84 ?  47  ARG A CA  1 
ATOM   222  C  C   . ARG A 1 47  ? -6.791  15.977  -9.050  1.00 24.71 ?  47  ARG A C   1 
ATOM   223  O  O   . ARG A 1 47  ? -6.063  15.552  -8.147  1.00 24.40 ?  47  ARG A O   1 
ATOM   224  C  CB  . ARG A 1 47  ? -5.257  16.855  -10.842 1.00 25.96 ?  47  ARG A CB  1 
ATOM   225  C  CG  . ARG A 1 47  ? -5.721  16.043  -12.071 1.00 28.32 ?  47  ARG A CG  1 
ATOM   226  C  CD  . ARG A 1 47  ? -5.272  16.660  -13.406 1.00 34.80 ?  47  ARG A CD  1 
ATOM   227  N  NE  . ARG A 1 47  ? -3.824  16.871  -13.494 1.00 43.76 ?  47  ARG A NE  1 
ATOM   228  C  CZ  . ARG A 1 47  ? -3.214  17.408  -14.547 1.00 43.70 ?  47  ARG A CZ  1 
ATOM   229  N  NH1 . ARG A 1 47  ? -3.892  17.777  -15.625 1.00 41.25 ?  47  ARG A NH1 1 
ATOM   230  N  NH2 . ARG A 1 47  ? -1.893  17.583  -14.519 1.00 47.44 ?  47  ARG A NH2 1 
ATOM   231  N  N   . VAL A 1 48  ? -7.976  15.439  -9.347  1.00 23.03 ?  48  VAL A N   1 
ATOM   232  C  CA  . VAL A 1 48  ? -8.522  14.296  -8.634  1.00 22.59 ?  48  VAL A CA  1 
ATOM   233  C  C   . VAL A 1 48  ? -9.037  13.282  -9.641  1.00 22.07 ?  48  VAL A C   1 
ATOM   234  O  O   . VAL A 1 48  ? -9.289  13.597  -10.806 1.00 19.28 ?  48  VAL A O   1 
ATOM   235  C  CB  . VAL A 1 48  ? -9.655  14.682  -7.651  1.00 20.94 ?  48  VAL A CB  1 
ATOM   236  C  CG1 . VAL A 1 48  ? -9.151  15.665  -6.594  1.00 18.77 ?  48  VAL A CG1 1 
ATOM   237  C  CG2 . VAL A 1 48  ? -10.865 15.230  -8.396  1.00 17.38 ?  48  VAL A CG2 1 
ATOM   238  N  N   . ARG A 1 49  ? -9.204  12.053  -9.154  1.00 19.66 ?  49  ARG A N   1 
ATOM   239  C  CA  . ARG A 1 49  ? -9.781  10.941  -9.900  1.00 21.36 ?  49  ARG A CA  1 
ATOM   240  C  C   . ARG A 1 49  ? -11.205 10.732  -9.403  1.00 22.08 ?  49  ARG A C   1 
ATOM   241  O  O   . ARG A 1 49  ? -11.412 10.381  -8.239  1.00 19.15 ?  49  ARG A O   1 
ATOM   242  C  CB  . ARG A 1 49  ? -8.950  9.674   -9.703  1.00 23.16 ?  49  ARG A CB  1 
ATOM   243  C  CG  . ARG A 1 49  ? -9.279  8.526   -10.673 1.00 28.45 ?  49  ARG A CG  1 
ATOM   244  C  CD  . ARG A 1 49  ? -8.925  7.168   -10.048 1.00 38.59 ?  49  ARG A CD  1 
ATOM   245  N  NE  . ARG A 1 49  ? -9.559  6.042   -10.728 1.00 43.21 ?  49  ARG A NE  1 
ATOM   246  C  CZ  . ARG A 1 49  ? -10.555 5.332   -10.217 1.00 39.38 ?  49  ARG A CZ  1 
ATOM   247  N  NH1 . ARG A 1 49  ? -11.075 5.623   -9.036  1.00 37.02 ?  49  ARG A NH1 1 
ATOM   248  N  NH2 . ARG A 1 49  ? -11.048 4.312   -10.914 1.00 46.10 ?  49  ARG A NH2 1 
ATOM   249  N  N   . THR A 1 50  ? -12.180 10.964  -10.276 1.00 21.42 ?  50  THR A N   1 
ATOM   250  C  CA  . THR A 1 50  ? -13.574 10.759  -9.913  1.00 22.96 ?  50  THR A CA  1 
ATOM   251  C  C   . THR A 1 50  ? -13.921 9.268   -9.944  1.00 24.56 ?  50  THR A C   1 
ATOM   252  O  O   . THR A 1 50  ? -13.143 8.428   -10.413 1.00 22.21 ?  50  THR A O   1 
ATOM   253  C  CB  . THR A 1 50  ? -14.491 11.512  -10.864 1.00 19.06 ?  50  THR A CB  1 
ATOM   254  O  OG1 . THR A 1 50  ? -14.599 10.751  -12.067 1.00 20.39 ?  50  THR A OG1 1 
ATOM   255  C  CG2 . THR A 1 50  ? -13.936 12.904  -11.175 1.00 18.65 ?  50  THR A CG2 1 
ATOM   256  N  N   . MET A 1 51  ? -15.122 8.942   -9.444  1.00 21.83 ?  51  MET A N   1 
ATOM   257  C  CA  . MET A 1 51  ? -15.546 7.545   -9.375  1.00 22.12 ?  51  MET A CA  1 
ATOM   258  C  C   . MET A 1 51  ? -15.686 6.927   -10.759 1.00 20.20 ?  51  MET A C   1 
ATOM   259  O  O   . MET A 1 51  ? -15.675 5.697   -10.878 1.00 26.71 ?  51  MET A O   1 
ATOM   260  C  CB  . MET A 1 51  ? -16.874 7.414   -8.608  1.00 21.20 ?  51  MET A CB  1 
ATOM   261  C  CG  . MET A 1 51  ? -18.101 7.802   -9.420  1.00 20.93 ?  51  MET A CG  1 
ATOM   262  S  SD  . MET A 1 51  ? -19.668 7.432   -8.583  1.00 21.72 ?  51  MET A SD  1 
ATOM   263  C  CE  . MET A 1 51  ? -19.426 8.493   -7.154  1.00 16.83 ?  51  MET A CE  1 
ATOM   264  N  N   . THR A 1 52  ? -15.813 7.741   -11.812 1.00 21.52 ?  52  THR A N   1 
ATOM   265  C  CA  . THR A 1 52  ? -15.861 7.193   -13.167 1.00 22.13 ?  52  THR A CA  1 
ATOM   266  C  C   . THR A 1 52  ? -14.492 6.765   -13.680 1.00 24.98 ?  52  THR A C   1 
ATOM   267  O  O   . THR A 1 52  ? -14.418 6.095   -14.717 1.00 22.46 ?  52  THR A O   1 
ATOM   268  C  CB  . THR A 1 52  ? -16.435 8.207   -14.159 1.00 24.91 ?  52  THR A CB  1 
ATOM   269  O  OG1 . THR A 1 52  ? -15.497 9.283   -14.334 1.00 21.13 ?  52  THR A OG1 1 
ATOM   270  C  CG2 . THR A 1 52  ? -17.788 8.762   -13.687 1.00 19.99 ?  52  THR A CG2 1 
ATOM   271  N  N   . GLY A 1 53  ? -13.417 7.122   -12.982 1.00 22.54 ?  53  GLY A N   1 
ATOM   272  C  CA  . GLY A 1 53  ? -12.085 7.039   -13.534 1.00 23.14 ?  53  GLY A CA  1 
ATOM   273  C  C   . GLY A 1 53  ? -11.656 8.276   -14.296 1.00 28.77 ?  53  GLY A C   1 
ATOM   274  O  O   . GLY A 1 53  ? -10.476 8.400   -14.626 1.00 21.34 ?  53  GLY A O   1 
ATOM   275  N  N   . ASP A 1 54  ? -12.577 9.188   -14.604 1.00 21.92 ?  54  ASP A N   1 
ATOM   276  C  CA  . ASP A 1 54  ? -12.176 10.441  -15.229 1.00 26.13 ?  54  ASP A CA  1 
ATOM   277  C  C   . ASP A 1 54  ? -11.404 11.308  -14.243 1.00 22.68 ?  54  ASP A C   1 
ATOM   278  O  O   . ASP A 1 54  ? -11.472 11.128  -13.025 1.00 24.77 ?  54  ASP A O   1 
ATOM   279  C  CB  . ASP A 1 54  ? -13.388 11.226  -15.722 1.00 21.80 ?  54  ASP A CB  1 
ATOM   280  C  CG  . ASP A 1 54  ? -14.122 10.523  -16.821 1.00 27.29 ?  54  ASP A CG  1 
ATOM   281  O  OD1 . ASP A 1 54  ? -13.484 9.724   -17.530 1.00 30.98 ?  54  ASP A OD1 1 
ATOM   282  O  OD2 . ASP A 1 54  ? -15.330 10.773  -16.981 1.00 28.35 ?  54  ASP A OD2 1 
ATOM   283  N  N   . GLU A 1 55  ? -10.695 12.291  -14.779 1.00 24.56 ?  55  GLU A N   1 
ATOM   284  C  CA  . GLU A 1 55  ? -10.007 13.255  -13.934 1.00 25.61 ?  55  GLU A CA  1 
ATOM   285  C  C   . GLU A 1 55  ? -10.745 14.587  -13.948 1.00 22.77 ?  55  GLU A C   1 
ATOM   286  O  O   . GLU A 1 55  ? -11.524 14.882  -14.856 1.00 23.52 ?  55  GLU A O   1 
ATOM   287  C  CB  . GLU A 1 55  ? -8.557  13.447  -14.382 1.00 26.84 ?  55  GLU A CB  1 
ATOM   288  C  CG  . GLU A 1 55  ? -7.732  12.173  -14.357 1.00 30.08 ?  55  GLU A CG  1 
ATOM   289  C  CD  . GLU A 1 55  ? -6.262  12.436  -14.654 1.00 37.30 ?  55  GLU A CD  1 
ATOM   290  O  OE1 . GLU A 1 55  ? -5.884  13.627  -14.777 1.00 36.04 ?  55  GLU A OE1 1 
ATOM   291  O  OE2 . GLU A 1 55  ? -5.493  11.457  -14.757 1.00 39.33 ?  55  GLU A OE2 1 
ATOM   292  N  N   . ALA A 1 56  ? -10.486 15.394  -12.921 1.00 21.08 ?  56  ALA A N   1 
ATOM   293  C  CA  . ALA A 1 56  ? -11.166 16.669  -12.764 1.00 19.14 ?  56  ALA A CA  1 
ATOM   294  C  C   . ALA A 1 56  ? -10.299 17.560  -11.907 1.00 21.52 ?  56  ALA A C   1 
ATOM   295  O  O   . ALA A 1 56  ? -9.382  17.088  -11.224 1.00 23.14 ?  56  ALA A O   1 
ATOM   296  C  CB  . ALA A 1 56  ? -12.554 16.508  -12.113 1.00 18.66 ?  56  ALA A CB  1 
ATOM   297  N  N   . TRP A 1 57  ? -10.612 18.856  -11.938 1.00 21.31 ?  57  TRP A N   1 
ATOM   298  C  CA  . TRP A 1 57  ? -10.041 19.829  -11.016 1.00 21.68 ?  57  TRP A CA  1 
ATOM   299  C  C   . TRP A 1 57  ? -11.025 20.086  -9.876  1.00 19.45 ?  57  TRP A C   1 
ATOM   300  O  O   . TRP A 1 57  ? -12.103 20.651  -10.097 1.00 20.93 ?  57  TRP A O   1 
ATOM   301  C  CB  . TRP A 1 57  ? -9.713  21.144  -11.728 1.00 18.97 ?  57  TRP A CB  1 
ATOM   302  C  CG  . TRP A 1 57  ? -8.608  21.044  -12.754 1.00 21.97 ?  57  TRP A CG  1 
ATOM   303  C  CD1 . TRP A 1 57  ? -8.741  21.130  -14.113 1.00 21.39 ?  57  TRP A CD1 1 
ATOM   304  C  CD2 . TRP A 1 57  ? -7.206  20.846  -12.500 1.00 23.97 ?  57  TRP A CD2 1 
ATOM   305  N  NE1 . TRP A 1 57  ? -7.507  21.008  -14.723 1.00 21.88 ?  57  TRP A NE1 1 
ATOM   306  C  CE2 . TRP A 1 57  ? -6.551  20.827  -13.756 1.00 26.03 ?  57  TRP A CE2 1 
ATOM   307  C  CE3 . TRP A 1 57  ? -6.444  20.678  -11.340 1.00 24.18 ?  57  TRP A CE3 1 
ATOM   308  C  CZ2 . TRP A 1 57  ? -5.176  20.646  -13.878 1.00 24.64 ?  57  TRP A CZ2 1 
ATOM   309  C  CZ3 . TRP A 1 57  ? -5.077  20.503  -11.462 1.00 25.75 ?  57  TRP A CZ3 1 
ATOM   310  C  CH2 . TRP A 1 57  ? -4.456  20.484  -12.723 1.00 29.22 ?  57  TRP A CH2 1 
ATOM   311  N  N   . LEU A 1 58  ? -10.641 19.720  -8.662  1.00 19.43 ?  58  LEU A N   1 
ATOM   312  C  CA  . LEU A 1 58  ? -11.472 19.950  -7.482  1.00 18.02 ?  58  LEU A CA  1 
ATOM   313  C  C   . LEU A 1 58  ? -11.075 21.268  -6.826  1.00 20.68 ?  58  LEU A C   1 
ATOM   314  O  O   . LEU A 1 58  ? -9.917  21.445  -6.433  1.00 20.85 ?  58  LEU A O   1 
ATOM   315  C  CB  . LEU A 1 58  ? -11.332 18.797  -6.494  1.00 20.55 ?  58  LEU A CB  1 
ATOM   316  C  CG  . LEU A 1 58  ? -12.214 18.856  -5.246  1.00 20.71 ?  58  LEU A CG  1 
ATOM   317  C  CD1 . LEU A 1 58  ? -13.694 18.737  -5.664  1.00 18.19 ?  58  LEU A CD1 1 
ATOM   318  C  CD2 . LEU A 1 58  ? -11.836 17.736  -4.297  1.00 21.52 ?  58  LEU A CD2 1 
ATOM   319  N  N   . VAL A 1 59  ? -12.032 22.189  -6.716  1.00 17.38 ?  59  VAL A N   1 
ATOM   320  C  CA  . VAL A 1 59  ? -11.787 23.555  -6.262  1.00 19.38 ?  59  VAL A CA  1 
ATOM   321  C  C   . VAL A 1 59  ? -12.375 23.700  -4.868  1.00 17.36 ?  59  VAL A C   1 
ATOM   322  O  O   . VAL A 1 59  ? -13.599 23.629  -4.704  1.00 19.30 ?  59  VAL A O   1 
ATOM   323  C  CB  . VAL A 1 59  ? -12.410 24.578  -7.223  1.00 16.32 ?  59  VAL A CB  1 
ATOM   324  C  CG1 . VAL A 1 59  ? -12.135 26.001  -6.745  1.00 17.40 ?  59  VAL A CG1 1 
ATOM   325  C  CG2 . VAL A 1 59  ? -11.906 24.352  -8.647  1.00 17.65 ?  59  VAL A CG2 1 
ATOM   326  N  N   . SER A 1 60  ? -11.522 23.935  -3.864  1.00 19.64 ?  60  SER A N   1 
ATOM   327  C  CA  . SER A 1 60  ? -11.956 23.765  -2.479  1.00 21.46 ?  60  SER A CA  1 
ATOM   328  C  C   . SER A 1 60  ? -11.768 24.966  -1.561  1.00 22.69 ?  60  SER A C   1 
ATOM   329  O  O   . SER A 1 60  ? -12.147 24.879  -0.389  1.00 21.44 ?  60  SER A O   1 
ATOM   330  C  CB  . SER A 1 60  ? -11.252 22.552  -1.852  1.00 21.90 ?  60  SER A CB  1 
ATOM   331  O  OG  . SER A 1 60  ? -9.842  22.721  -1.873  1.00 27.00 ?  60  SER A OG  1 
ATOM   332  N  N   . SER A 1 61  ? -11.234 26.084  -2.042  1.00 18.55 ?  61  SER A N   1 
ATOM   333  C  CA  . SER A 1 61  ? -11.205 27.293  -1.234  1.00 18.15 ?  61  SER A CA  1 
ATOM   334  C  C   . SER A 1 61  ? -12.343 28.220  -1.637  1.00 18.33 ?  61  SER A C   1 
ATOM   335  O  O   . SER A 1 61  ? -12.833 28.185  -2.771  1.00 19.67 ?  61  SER A O   1 
ATOM   336  C  CB  . SER A 1 61  ? -9.865  28.021  -1.367  1.00 19.11 ?  61  SER A CB  1 
ATOM   337  O  OG  . SER A 1 61  ? -9.787  28.679  -2.618  1.00 23.64 ?  61  SER A OG  1 
ATOM   338  N  N   . TYR A 1 62  ? -12.750 29.070  -0.694  1.00 20.31 ?  62  TYR A N   1 
ATOM   339  C  CA  . TYR A 1 62  ? -13.897 29.942  -0.928  1.00 18.68 ?  62  TYR A CA  1 
ATOM   340  C  C   . TYR A 1 62  ? -13.663 30.855  -2.122  1.00 19.92 ?  62  TYR A C   1 
ATOM   341  O  O   . TYR A 1 62  ? -14.523 30.981  -3.003  1.00 18.04 ?  62  TYR A O   1 
ATOM   342  C  CB  . TYR A 1 62  ? -14.194 30.772  0.321   1.00 21.66 ?  62  TYR A CB  1 
ATOM   343  C  CG  . TYR A 1 62  ? -15.368 31.714  0.140   1.00 21.38 ?  62  TYR A CG  1 
ATOM   344  C  CD1 . TYR A 1 62  ? -15.205 32.974  -0.437  1.00 18.33 ?  62  TYR A CD1 1 
ATOM   345  C  CD2 . TYR A 1 62  ? -16.639 31.339  0.548   1.00 19.39 ?  62  TYR A CD2 1 
ATOM   346  C  CE1 . TYR A 1 62  ? -16.280 33.830  -0.591  1.00 18.42 ?  62  TYR A CE1 1 
ATOM   347  C  CE2 . TYR A 1 62  ? -17.729 32.190  0.404   1.00 19.12 ?  62  TYR A CE2 1 
ATOM   348  C  CZ  . TYR A 1 62  ? -17.546 33.427  -0.167  1.00 22.55 ?  62  TYR A CZ  1 
ATOM   349  O  OH  . TYR A 1 62  ? -18.638 34.253  -0.305  1.00 21.56 ?  62  TYR A OH  1 
ATOM   350  N  N   . GLU A 1 63  ? -12.506 31.514  -2.156  1.00 22.32 ?  63  GLU A N   1 
ATOM   351  C  CA  . GLU A 1 63  ? -12.244 32.520  -3.182  1.00 25.94 ?  63  GLU A CA  1 
ATOM   352  C  C   . GLU A 1 63  ? -12.306 31.908  -4.578  1.00 23.90 ?  63  GLU A C   1 
ATOM   353  O  O   . GLU A 1 63  ? -12.925 32.470  -5.487  1.00 20.22 ?  63  GLU A O   1 
ATOM   354  C  CB  . GLU A 1 63  ? -10.875 33.166  -2.923  1.00 25.43 ?  63  GLU A CB  1 
ATOM   355  C  CG  . GLU A 1 63  ? -10.386 34.129  -4.001  1.00 32.06 ?  63  GLU A CG  1 
ATOM   356  C  CD  . GLU A 1 63  ? -8.863  34.312  -3.981  1.00 36.29 ?  63  GLU A CD  1 
ATOM   357  O  OE1 . GLU A 1 63  ? -8.232  34.004  -2.946  1.00 39.39 ?  63  GLU A OE1 1 
ATOM   358  O  OE2 . GLU A 1 63  ? -8.301  34.748  -5.007  1.00 45.94 ?  63  GLU A OE2 1 
ATOM   359  N  N   . LEU A 1 64  ? -11.673 30.747  -4.763  1.00 18.68 ?  64  LEU A N   1 
ATOM   360  C  CA  . LEU A 1 64  ? -11.642 30.112  -6.073  1.00 20.78 ?  64  LEU A CA  1 
ATOM   361  C  C   . LEU A 1 64  ? -12.959 29.425  -6.409  1.00 19.10 ?  64  LEU A C   1 
ATOM   362  O  O   . LEU A 1 64  ? -13.347 29.394  -7.579  1.00 23.07 ?  64  LEU A O   1 
ATOM   363  C  CB  . LEU A 1 64  ? -10.480 29.122  -6.145  1.00 19.58 ?  64  LEU A CB  1 
ATOM   364  C  CG  . LEU A 1 64  ? -9.112  29.815  -5.950  1.00 26.52 ?  64  LEU A CG  1 
ATOM   365  C  CD1 . LEU A 1 64  ? -7.977  28.805  -5.895  1.00 20.67 ?  64  LEU A CD1 1 
ATOM   366  C  CD2 . LEU A 1 64  ? -8.823  30.894  -7.006  1.00 21.86 ?  64  LEU A CD2 1 
ATOM   367  N  N   . ALA A 1 65  ? -13.651 28.872  -5.409  1.00 18.49 ?  65  ALA A N   1 
ATOM   368  C  CA  . ALA A 1 65  ? -15.001 28.364  -5.623  1.00 16.37 ?  65  ALA A CA  1 
ATOM   369  C  C   . ALA A 1 65  ? -15.909 29.447  -6.195  1.00 19.83 ?  65  ALA A C   1 
ATOM   370  O  O   . ALA A 1 65  ? -16.555 29.253  -7.230  1.00 18.47 ?  65  ALA A O   1 
ATOM   371  C  CB  . ALA A 1 65  ? -15.567 27.833  -4.296  1.00 16.43 ?  65  ALA A CB  1 
ATOM   372  N  N   . LYS A 1 66  ? -15.979 30.595  -5.517  1.00 19.97 ?  66  LYS A N   1 
ATOM   373  C  CA  . LYS A 1 66  ? -16.884 31.656  -5.949  1.00 22.22 ?  66  LYS A CA  1 
ATOM   374  C  C   . LYS A 1 66  ? -16.495 32.165  -7.333  1.00 23.98 ?  66  LYS A C   1 
ATOM   375  O  O   . LYS A 1 66  ? -17.360 32.417  -8.181  1.00 19.47 ?  66  LYS A O   1 
ATOM   376  C  CB  . LYS A 1 66  ? -16.876 32.779  -4.907  1.00 20.39 ?  66  LYS A CB  1 
ATOM   377  C  CG  . LYS A 1 66  ? -17.951 33.857  -5.066  1.00 26.90 ?  66  LYS A CG  1 
ATOM   378  C  CD  . LYS A 1 66  ? -17.907 34.851  -3.886  1.00 32.14 ?  66  LYS A CD  1 
ATOM   379  C  CE  . LYS A 1 66  ? -18.911 36.016  -4.060  1.00 29.49 ?  66  LYS A CE  1 
ATOM   380  N  NZ  . LYS A 1 66  ? -18.349 37.023  -5.000  1.00 40.90 ?  66  LYS A NZ  1 
ATOM   381  N  N   . GLN A 1 67  ? -15.189 32.267  -7.592  1.00 20.67 ?  67  GLN A N   1 
ATOM   382  C  CA  . GLN A 1 67  ? -14.718 32.651  -8.917  1.00 24.52 ?  67  GLN A CA  1 
ATOM   383  C  C   . GLN A 1 67  ? -15.276 31.722  -9.994  1.00 22.23 ?  67  GLN A C   1 
ATOM   384  O  O   . GLN A 1 67  ? -15.812 32.181  -11.009 1.00 19.96 ?  67  GLN A O   1 
ATOM   385  C  CB  . GLN A 1 67  ? -13.191 32.636  -8.939  1.00 27.52 ?  67  GLN A CB  1 
ATOM   386  C  CG  . GLN A 1 67  ? -12.592 33.153  -10.215 1.00 36.98 ?  67  GLN A CG  1 
ATOM   387  C  CD  . GLN A 1 67  ? -11.088 33.278  -10.127 1.00 35.52 ?  67  GLN A CD  1 
ATOM   388  O  OE1 . GLN A 1 67  ? -10.485 33.060  -9.066  1.00 33.76 ?  67  GLN A OE1 1 
ATOM   389  N  NE2 . GLN A 1 67  ? -10.467 33.638  -11.247 1.00 31.38 ?  67  GLN A NE2 1 
ATOM   390  N  N   . VAL A 1 68  ? -15.155 30.404  -9.786  1.00 19.69 ?  68  VAL A N   1 
ATOM   391  C  CA  . VAL A 1 68  ? -15.693 29.445  -10.754 1.00 18.71 ?  68  VAL A CA  1 
ATOM   392  C  C   . VAL A 1 68  ? -17.189 29.655  -10.947 1.00 18.28 ?  68  VAL A C   1 
ATOM   393  O  O   . VAL A 1 68  ? -17.685 29.730  -12.079 1.00 20.21 ?  68  VAL A O   1 
ATOM   394  C  CB  . VAL A 1 68  ? -15.389 28.002  -10.319 1.00 19.14 ?  68  VAL A CB  1 
ATOM   395  C  CG1 . VAL A 1 68  ? -16.116 27.045  -11.226 1.00 16.26 ?  68  VAL A CG1 1 
ATOM   396  C  CG2 . VAL A 1 68  ? -13.878 27.739  -10.357 1.00 16.16 ?  68  VAL A CG2 1 
ATOM   397  N  N   . LEU A 1 69  ? -17.939 29.745  -9.846  1.00 20.41 ?  69  LEU A N   1 
ATOM   398  C  CA  . LEU A 1 69  ? -19.382 29.908  -9.997  1.00 22.95 ?  69  LEU A CA  1 
ATOM   399  C  C   . LEU A 1 69  ? -19.716 31.189  -10.759 1.00 19.05 ?  69  LEU A C   1 
ATOM   400  O  O   . LEU A 1 69  ? -20.688 31.217  -11.517 1.00 17.72 ?  69  LEU A O   1 
ATOM   401  C  CB  . LEU A 1 69  ? -20.073 29.880  -8.622  1.00 22.45 ?  69  LEU A CB  1 
ATOM   402  C  CG  . LEU A 1 69  ? -19.874 28.570  -7.834  1.00 19.10 ?  69  LEU A CG  1 
ATOM   403  C  CD1 . LEU A 1 69  ? -20.657 28.592  -6.526  1.00 17.48 ?  69  LEU A CD1 1 
ATOM   404  C  CD2 . LEU A 1 69  ? -20.282 27.364  -8.688  1.00 16.40 ?  69  LEU A CD2 1 
ATOM   405  N  N   . GLU A 1 70  ? -18.907 32.237  -10.623 1.00 21.14 ?  70  GLU A N   1 
ATOM   406  C  CA  . GLU A 1 70  ? -19.247 33.514  -11.252 1.00 20.69 ?  70  GLU A CA  1 
ATOM   407  C  C   . GLU A 1 70  ? -18.600 33.718  -12.619 1.00 24.56 ?  70  GLU A C   1 
ATOM   408  O  O   . GLU A 1 70  ? -18.858 34.736  -13.266 1.00 27.77 ?  70  GLU A O   1 
ATOM   409  C  CB  . GLU A 1 70  ? -18.882 34.668  -10.321 1.00 24.01 ?  70  GLU A CB  1 
ATOM   410  C  CG  . GLU A 1 70  ? -19.958 34.922  -9.257  1.00 28.26 ?  70  GLU A CG  1 
ATOM   411  C  CD  . GLU A 1 70  ? -19.447 35.793  -8.152  1.00 33.36 ?  70  GLU A CD  1 
ATOM   412  O  OE1 . GLU A 1 70  ? -18.266 36.184  -8.232  1.00 34.41 ?  70  GLU A OE1 1 
ATOM   413  O  OE2 . GLU A 1 70  ? -20.203 36.062  -7.195  1.00 36.52 ?  70  GLU A OE2 1 
ATOM   414  N  N   . ASP A 1 71  ? -17.799 32.771  -13.087 1.00 23.53 ?  71  ASP A N   1 
ATOM   415  C  CA  . ASP A 1 71  ? -17.159 32.848  -14.397 1.00 22.02 ?  71  ASP A CA  1 
ATOM   416  C  C   . ASP A 1 71  ? -17.890 31.899  -15.340 1.00 24.24 ?  71  ASP A C   1 
ATOM   417  O  O   . ASP A 1 71  ? -17.764 30.677  -15.216 1.00 23.06 ?  71  ASP A O   1 
ATOM   418  C  CB  . ASP A 1 71  ? -15.680 32.491  -14.265 1.00 20.53 ?  71  ASP A CB  1 
ATOM   419  C  CG  . ASP A 1 71  ? -14.914 32.607  -15.570 1.00 21.65 ?  71  ASP A CG  1 
ATOM   420  O  OD1 . ASP A 1 71  ? -15.513 32.623  -16.671 1.00 19.83 ?  71  ASP A OD1 1 
ATOM   421  O  OD2 . ASP A 1 71  ? -13.676 32.657  -15.476 1.00 26.14 ?  71  ASP A OD2 1 
ATOM   422  N  N   . ASP A 1 72  ? -18.624 32.454  -16.308 1.00 21.30 ?  72  ASP A N   1 
ATOM   423  C  CA  . ASP A 1 72  ? -19.486 31.626  -17.151 1.00 21.57 ?  72  ASP A CA  1 
ATOM   424  C  C   . ASP A 1 72  ? -18.748 30.917  -18.275 1.00 24.38 ?  72  ASP A C   1 
ATOM   425  O  O   . ASP A 1 72  ? -19.398 30.269  -19.105 1.00 26.30 ?  72  ASP A O   1 
ATOM   426  C  CB  . ASP A 1 72  ? -20.618 32.461  -17.746 1.00 27.69 ?  72  ASP A CB  1 
ATOM   427  C  CG  . ASP A 1 72  ? -21.709 32.719  -16.750 1.00 26.42 ?  72  ASP A CG  1 
ATOM   428  O  OD1 . ASP A 1 72  ? -21.871 31.888  -15.828 1.00 30.62 ?  72  ASP A OD1 1 
ATOM   429  O  OD2 . ASP A 1 72  ? -22.390 33.753  -16.870 1.00 28.98 ?  72  ASP A OD2 1 
ATOM   430  N  N   . ARG A 1 73  ? -17.425 31.006  -18.336 1.00 23.35 ?  73  ARG A N   1 
ATOM   431  C  CA  . ARG A 1 73  ? -16.717 30.073  -19.199 1.00 26.55 ?  73  ARG A CA  1 
ATOM   432  C  C   . ARG A 1 73  ? -16.474 28.741  -18.511 1.00 24.66 ?  73  ARG A C   1 
ATOM   433  O  O   . ARG A 1 73  ? -15.868 27.858  -19.119 1.00 22.63 ?  73  ARG A O   1 
ATOM   434  C  CB  . ARG A 1 73  ? -15.411 30.687  -19.690 1.00 24.49 ?  73  ARG A CB  1 
ATOM   435  C  CG  . ARG A 1 73  ? -15.595 32.131  -20.086 1.00 29.38 ?  73  ARG A CG  1 
ATOM   436  C  CD  . ARG A 1 73  ? -14.278 32.721  -20.327 1.00 27.62 ?  73  ARG A CD  1 
ATOM   437  N  NE  . ARG A 1 73  ? -13.624 33.045  -19.070 1.00 26.07 ?  73  ARG A NE  1 
ATOM   438  C  CZ  . ARG A 1 73  ? -12.332 33.319  -18.997 1.00 26.78 ?  73  ARG A CZ  1 
ATOM   439  N  NH1 . ARG A 1 73  ? -11.576 33.328  -20.085 1.00 28.42 ?  73  ARG A NH1 1 
ATOM   440  N  NH2 . ARG A 1 73  ? -11.778 33.550  -17.807 1.00 25.18 ?  73  ARG A NH2 1 
ATOM   441  N  N   . PHE A 1 74  ? -16.915 28.595  -17.254 1.00 18.98 ?  74  PHE A N   1 
ATOM   442  C  CA  . PHE A 1 74  ? -17.125 27.293  -16.633 1.00 19.24 ?  74  PHE A CA  1 
ATOM   443  C  C   . PHE A 1 74  ? -18.612 26.995  -16.752 1.00 23.37 ?  74  PHE A C   1 
ATOM   444  O  O   . PHE A 1 74  ? -19.430 27.621  -16.072 1.00 24.89 ?  74  PHE A O   1 
ATOM   445  C  CB  . PHE A 1 74  ? -16.657 27.288  -15.185 1.00 18.63 ?  74  PHE A CB  1 
ATOM   446  C  CG  . PHE A 1 74  ? -15.198 27.586  -15.029 1.00 20.51 ?  74  PHE A CG  1 
ATOM   447  C  CD1 . PHE A 1 74  ? -14.245 26.651  -15.386 1.00 23.25 ?  74  PHE A CD1 1 
ATOM   448  C  CD2 . PHE A 1 74  ? -14.775 28.802  -14.536 1.00 19.39 ?  74  PHE A CD2 1 
ATOM   449  C  CE1 . PHE A 1 74  ? -12.889 26.927  -15.243 1.00 23.43 ?  74  PHE A CE1 1 
ATOM   450  C  CE2 . PHE A 1 74  ? -13.426 29.084  -14.411 1.00 22.75 ?  74  PHE A CE2 1 
ATOM   451  C  CZ  . PHE A 1 74  ? -12.485 28.148  -14.759 1.00 19.75 ?  74  PHE A CZ  1 
ATOM   452  N  N   . SER A 1 75  ? -18.958 26.061  -17.630 1.00 17.76 ?  75  SER A N   1 
ATOM   453  C  CA  . SER A 1 75  ? -20.326 25.867  -18.094 1.00 22.76 ?  75  SER A CA  1 
ATOM   454  C  C   . SER A 1 75  ? -20.982 24.665  -17.431 1.00 19.02 ?  75  SER A C   1 
ATOM   455  O  O   . SER A 1 75  ? -20.426 23.565  -17.450 1.00 18.25 ?  75  SER A O   1 
ATOM   456  C  CB  . SER A 1 75  ? -20.342 25.655  -19.606 1.00 21.85 ?  75  SER A CB  1 
ATOM   457  O  OG  . SER A 1 75  ? -21.666 25.419  -20.063 1.00 23.90 ?  75  SER A OG  1 
ATOM   458  N  N   . LEU A 1 76  ? -22.197 24.867  -16.913 1.00 21.73 ?  76  LEU A N   1 
ATOM   459  C  CA  . LEU A 1 76  ? -22.956 23.780  -16.309 1.00 19.98 ?  76  LEU A CA  1 
ATOM   460  C  C   . LEU A 1 76  ? -23.603 22.908  -17.383 1.00 22.64 ?  76  LEU A C   1 
ATOM   461  O  O   . LEU A 1 76  ? -23.499 21.677  -17.347 1.00 19.18 ?  76  LEU A O   1 
ATOM   462  C  CB  . LEU A 1 76  ? -24.024 24.347  -15.358 1.00 18.08 ?  76  LEU A CB  1 
ATOM   463  C  CG  . LEU A 1 76  ? -25.046 23.320  -14.839 1.00 21.00 ?  76  LEU A CG  1 
ATOM   464  C  CD1 . LEU A 1 76  ? -24.326 22.323  -13.954 1.00 17.93 ?  76  LEU A CD1 1 
ATOM   465  C  CD2 . LEU A 1 76  ? -26.221 23.972  -14.071 1.00 20.92 ?  76  LEU A CD2 1 
ATOM   466  N  N   . LYS A 1 77  ? -24.273 23.515  -18.352 1.00 20.30 ?  77  LYS A N   1 
ATOM   467  C  CA  . LYS A 1 77  ? -25.016 22.746  -19.380 1.00 23.19 ?  77  LYS A CA  1 
ATOM   468  C  C   . LYS A 1 77  ? -24.096 21.743  -20.085 1.00 24.36 ?  77  LYS A C   1 
ATOM   469  O  O   . LYS A 1 77  ? -24.523 20.614  -20.327 1.00 23.40 ?  77  LYS A O   1 
ATOM   470  C  CB  . LYS A 1 77  ? -25.602 23.733  -20.390 1.00 30.21 ?  77  LYS A CB  1 
ATOM   471  C  CG  . LYS A 1 77  ? -25.783 23.251  -21.818 1.00 34.08 ?  77  LYS A CG  1 
ATOM   472  C  CD  . LYS A 1 77  ? -25.976 24.410  -22.787 1.00 38.18 ?  77  LYS A CD  1 
ATOM   473  C  CE  . LYS A 1 77  ? -27.048 24.147  -23.793 1.00 42.72 ?  77  LYS A CE  1 
ATOM   474  N  NZ  . LYS A 1 77  ? -26.620 23.190  -24.814 1.00 49.46 ?  77  LYS A NZ  1 
ATOM   475  N  N   . ASP A 1 78  ? -22.861 22.147  -20.348 1.00 23.98 ?  78  ASP A N   1 
ATOM   476  C  CA  . ASP A 1 78  ? -21.983 21.273  -21.115 1.00 24.89 ?  78  ASP A CA  1 
ATOM   477  C  C   . ASP A 1 78  ? -21.493 20.062  -20.331 1.00 24.82 ?  78  ASP A C   1 
ATOM   478  O  O   . ASP A 1 78  ? -20.933 19.140  -20.949 1.00 23.82 ?  78  ASP A O   1 
ATOM   479  C  CB  . ASP A 1 78  ? -20.798 22.083  -21.640 1.00 21.44 ?  78  ASP A CB  1 
ATOM   480  C  CG  . ASP A 1 78  ? -21.230 23.110  -22.662 1.00 28.37 ?  78  ASP A CG  1 
ATOM   481  O  OD1 . ASP A 1 78  ? -21.652 22.696  -23.749 1.00 35.44 ?  78  ASP A OD1 1 
ATOM   482  O  OD2 . ASP A 1 78  ? -21.190 24.318  -22.369 1.00 33.06 ?  78  ASP A OD2 1 
ATOM   483  N  N   . THR A 1 79  ? -21.709 20.016  -19.008 1.00 19.06 ?  79  THR A N   1 
ATOM   484  C  CA  . THR A 1 79  ? -21.305 18.823  -18.260 1.00 19.49 ?  79  THR A CA  1 
ATOM   485  C  C   . THR A 1 79  ? -22.065 17.584  -18.700 1.00 22.32 ?  79  THR A C   1 
ATOM   486  O  O   . THR A 1 79  ? -21.598 16.463  -18.450 1.00 21.41 ?  79  THR A O   1 
ATOM   487  C  CB  . THR A 1 79  ? -21.514 18.995  -16.757 1.00 18.70 ?  79  THR A CB  1 
ATOM   488  O  OG1 . THR A 1 79  ? -22.897 19.244  -16.498 1.00 19.95 ?  79  THR A OG1 1 
ATOM   489  C  CG2 . THR A 1 79  ? -20.667 20.119  -16.212 1.00 17.96 ?  79  THR A CG2 1 
ATOM   490  N  N   . ALA A 1 80  ? -23.231 17.764  -19.319 1.00 21.99 ?  80  ALA A N   1 
ATOM   491  C  CA  . ALA A 1 80  ? -24.086 16.681  -19.792 1.00 24.28 ?  80  ALA A CA  1 
ATOM   492  C  C   . ALA A 1 80  ? -23.735 16.205  -21.202 1.00 26.21 ?  80  ALA A C   1 
ATOM   493  O  O   . ALA A 1 80  ? -24.373 15.266  -21.699 1.00 30.45 ?  80  ALA A O   1 
ATOM   494  C  CB  . ALA A 1 80  ? -25.551 17.135  -19.765 1.00 19.17 ?  80  ALA A CB  1 
ATOM   495  N  N   . ASN A 1 81  ? -22.769 16.839  -21.863 1.00 25.05 ?  81  ASN A N   1 
ATOM   496  C  CA  . ASN A 1 81  ? -22.470 16.516  -23.253 1.00 30.66 ?  81  ASN A CA  1 
ATOM   497  C  C   . ASN A 1 81  ? -21.895 15.104  -23.370 1.00 32.37 ?  81  ASN A C   1 
ATOM   498  O  O   . ASN A 1 81  ? -21.167 14.646  -22.482 1.00 28.48 ?  81  ASN A O   1 
ATOM   499  C  CB  . ASN A 1 81  ? -21.471 17.514  -23.839 1.00 30.34 ?  81  ASN A CB  1 
ATOM   500  C  CG  . ASN A 1 81  ? -22.066 18.891  -24.031 1.00 32.58 ?  81  ASN A CG  1 
ATOM   501  O  OD1 . ASN A 1 81  ? -23.286 19.067  -23.998 1.00 26.00 ?  81  ASN A OD1 1 
ATOM   502  N  ND2 . ASN A 1 81  ? -21.202 19.880  -24.239 1.00 33.64 ?  81  ASN A ND2 1 
ATOM   503  N  N   . PRO A 1 82  ? -22.196 14.401  -24.467 1.00 34.95 ?  82  PRO A N   1 
ATOM   504  C  CA  . PRO A 1 82  ? -21.558 13.102  -24.701 1.00 34.76 ?  82  PRO A CA  1 
ATOM   505  C  C   . PRO A 1 82  ? -20.044 13.240  -24.686 1.00 31.06 ?  82  PRO A C   1 
ATOM   506  O  O   . PRO A 1 82  ? -19.481 14.187  -25.242 1.00 31.20 ?  82  PRO A O   1 
ATOM   507  C  CB  . PRO A 1 82  ? -22.063 12.692  -26.091 1.00 35.21 ?  82  PRO A CB  1 
ATOM   508  C  CG  . PRO A 1 82  ? -23.115 13.660  -26.469 1.00 33.51 ?  82  PRO A CG  1 
ATOM   509  C  CD  . PRO A 1 82  ? -22.988 14.865  -25.620 1.00 33.42 ?  82  PRO A CD  1 
ATOM   510  N  N   . GLY A 1 83  ? -19.384 12.302  -24.020 1.00 27.04 ?  83  GLY A N   1 
ATOM   511  C  CA  . GLY A 1 83  ? -17.944 12.230  -24.109 1.00 29.80 ?  83  GLY A CA  1 
ATOM   512  C  C   . GLY A 1 83  ? -17.156 13.233  -23.292 1.00 30.55 ?  83  GLY A C   1 
ATOM   513  O  O   . GLY A 1 83  ? -15.923 13.233  -23.389 1.00 33.02 ?  83  GLY A O   1 
ATOM   514  N  N   . VAL A 1 84  ? -17.794 14.093  -22.500 1.00 26.70 ?  84  VAL A N   1 
ATOM   515  C  CA  . VAL A 1 84  ? -17.014 14.961  -21.608 1.00 25.32 ?  84  VAL A CA  1 
ATOM   516  C  C   . VAL A 1 84  ? -16.637 14.164  -20.364 1.00 26.40 ?  84  VAL A C   1 
ATOM   517  O  O   . VAL A 1 84  ? -17.303 13.172  -20.047 1.00 26.96 ?  84  VAL A O   1 
ATOM   518  C  CB  . VAL A 1 84  ? -17.770 16.252  -21.223 1.00 25.42 ?  84  VAL A CB  1 
ATOM   519  C  CG1 . VAL A 1 84  ? -18.135 17.082  -22.460 1.00 25.09 ?  84  VAL A CG1 1 
ATOM   520  C  CG2 . VAL A 1 84  ? -18.988 15.949  -20.360 1.00 20.43 ?  84  VAL A CG2 1 
ATOM   521  N  N   . PRO A 1 85  ? -15.589 14.539  -19.637 1.00 24.65 ?  85  PRO A N   1 
ATOM   522  C  CA  . PRO A 1 85  ? -15.319 13.879  -18.353 1.00 23.39 ?  85  PRO A CA  1 
ATOM   523  C  C   . PRO A 1 85  ? -16.459 14.120  -17.369 1.00 28.68 ?  85  PRO A C   1 
ATOM   524  O  O   . PRO A 1 85  ? -17.148 15.145  -17.418 1.00 22.52 ?  85  PRO A O   1 
ATOM   525  C  CB  . PRO A 1 85  ? -14.008 14.525  -17.879 1.00 22.20 ?  85  PRO A CB  1 
ATOM   526  C  CG  . PRO A 1 85  ? -13.817 15.749  -18.761 1.00 26.25 ?  85  PRO A CG  1 
ATOM   527  C  CD  . PRO A 1 85  ? -14.523 15.470  -20.037 1.00 21.85 ?  85  PRO A CD  1 
ATOM   528  N  N   . ARG A 1 86  ? -16.655 13.150  -16.470 1.00 24.22 ?  86  ARG A N   1 
ATOM   529  C  CA  . ARG A 1 86  ? -17.807 13.113  -15.574 1.00 28.43 ?  86  ARG A CA  1 
ATOM   530  C  C   . ARG A 1 86  ? -17.377 12.725  -14.167 1.00 24.61 ?  86  ARG A C   1 
ATOM   531  O  O   . ARG A 1 86  ? -16.458 11.923  -13.990 1.00 22.05 ?  86  ARG A O   1 
ATOM   532  C  CB  . ARG A 1 86  ? -18.845 12.089  -16.030 1.00 26.10 ?  86  ARG A CB  1 
ATOM   533  C  CG  . ARG A 1 86  ? -19.172 12.139  -17.479 1.00 29.16 ?  86  ARG A CG  1 
ATOM   534  C  CD  . ARG A 1 86  ? -20.614 11.731  -17.669 1.00 35.92 ?  86  ARG A CD  1 
ATOM   535  N  NE  . ARG A 1 86  ? -21.478 12.439  -16.734 1.00 32.73 ?  86  ARG A NE  1 
ATOM   536  C  CZ  . ARG A 1 86  ? -22.268 13.436  -17.096 1.00 32.69 ?  86  ARG A CZ  1 
ATOM   537  N  NH1 . ARG A 1 86  ? -22.303 13.860  -18.349 1.00 33.49 ?  86  ARG A NH1 1 
ATOM   538  N  NH2 . ARG A 1 86  ? -23.033 14.024  -16.184 1.00 41.96 ?  86  ARG A NH2 1 
ATOM   539  N  N   . GLN A 1 87  ? -18.062 13.289  -13.163 1.00 21.64 ?  87  GLN A N   1 
ATOM   540  C  CA  . GLN A 1 87  ? -17.933 12.785  -11.800 1.00 18.37 ?  87  GLN A CA  1 
ATOM   541  C  C   . GLN A 1 87  ? -18.828 11.570  -11.544 1.00 20.13 ?  87  GLN A C   1 
ATOM   542  O  O   . GLN A 1 87  ? -18.542 10.780  -10.637 1.00 16.82 ?  87  GLN A O   1 
ATOM   543  C  CB  . GLN A 1 87  ? -18.234 13.891  -10.777 1.00 22.46 ?  87  GLN A CB  1 
ATOM   544  C  CG  . GLN A 1 87  ? -19.617 14.549  -10.910 1.00 16.87 ?  87  GLN A CG  1 
ATOM   545  C  CD  . GLN A 1 87  ? -19.966 15.438  -9.720  1.00 20.69 ?  87  GLN A CD  1 
ATOM   546  O  OE1 . GLN A 1 87  ? -19.384 15.313  -8.629  1.00 19.80 ?  87  GLN A OE1 1 
ATOM   547  N  NE2 . GLN A 1 87  ? -20.932 16.337  -9.920  1.00 15.68 ?  87  GLN A NE2 1 
ATOM   548  N  N   . TYR A 1 88  ? -19.886 11.386  -12.326 1.00 21.19 ?  88  TYR A N   1 
ATOM   549  C  CA  . TYR A 1 88  ? -20.673 10.159  -12.258 1.00 19.47 ?  88  TYR A CA  1 
ATOM   550  C  C   . TYR A 1 88  ? -21.561 10.118  -13.485 1.00 22.55 ?  88  TYR A C   1 
ATOM   551  O  O   . TYR A 1 88  ? -21.718 11.125  -14.180 1.00 22.00 ?  88  TYR A O   1 
ATOM   552  C  CB  . TYR A 1 88  ? -21.513 10.062  -10.972 1.00 20.58 ?  88  TYR A CB  1 
ATOM   553  C  CG  . TYR A 1 88  ? -22.218 11.338  -10.559 1.00 17.69 ?  88  TYR A CG  1 
ATOM   554  C  CD1 . TYR A 1 88  ? -23.385 11.763  -11.205 1.00 20.31 ?  88  TYR A CD1 1 
ATOM   555  C  CD2 . TYR A 1 88  ? -21.741 12.096  -9.494  1.00 17.41 ?  88  TYR A CD2 1 
ATOM   556  C  CE1 . TYR A 1 88  ? -24.046 12.918  -10.808 1.00 18.26 ?  88  TYR A CE1 1 
ATOM   557  C  CE2 . TYR A 1 88  ? -22.390 13.258  -9.089  1.00 18.21 ?  88  TYR A CE2 1 
ATOM   558  C  CZ  . TYR A 1 88  ? -23.534 13.666  -9.750  1.00 19.44 ?  88  TYR A CZ  1 
ATOM   559  O  OH  . TYR A 1 88  ? -24.165 14.818  -9.344  1.00 23.04 ?  88  TYR A OH  1 
ATOM   560  N  N   . ALA A 1 89  ? -22.130 8.940   -13.749 1.00 20.82 ?  89  ALA A N   1 
ATOM   561  C  CA  . ALA A 1 89  ? -22.959 8.755   -14.935 1.00 25.49 ?  89  ALA A CA  1 
ATOM   562  C  C   . ALA A 1 89  ? -24.155 9.700   -14.939 1.00 25.64 ?  89  ALA A C   1 
ATOM   563  O  O   . ALA A 1 89  ? -24.767 9.966   -13.903 1.00 25.32 ?  89  ALA A O   1 
ATOM   564  C  CB  . ALA A 1 89  ? -23.455 7.306   -15.022 1.00 23.77 ?  89  ALA A CB  1 
ATOM   565  N  N   . LEU A 1 90  ? -24.482 10.207  -16.125 1.00 28.24 ?  90  LEU A N   1 
ATOM   566  C  CA  . LEU A 1 90  ? -25.753 10.881  -16.339 1.00 28.15 ?  90  LEU A CA  1 
ATOM   567  C  C   . LEU A 1 90  ? -26.893 9.926   -16.045 1.00 29.33 ?  90  LEU A C   1 
ATOM   568  O  O   . LEU A 1 90  ? -26.924 8.813   -16.575 1.00 29.07 ?  90  LEU A O   1 
ATOM   569  C  CB  . LEU A 1 90  ? -25.855 11.368  -17.787 1.00 32.78 ?  90  LEU A CB  1 
ATOM   570  C  CG  . LEU A 1 90  ? -27.134 12.044  -18.258 1.00 35.34 ?  90  LEU A CG  1 
ATOM   571  C  CD1 . LEU A 1 90  ? -27.351 13.325  -17.479 1.00 32.82 ?  90  LEU A CD1 1 
ATOM   572  C  CD2 . LEU A 1 90  ? -27.074 12.323  -19.752 1.00 33.03 ?  90  LEU A CD2 1 
ATOM   573  N  N   . THR A 1 91  ? -27.837 10.364  -15.211 1.00 29.89 ?  91  THR A N   1 
ATOM   574  C  CA  . THR A 1 91  ? -29.047 9.603   -14.922 1.00 27.92 ?  91  THR A CA  1 
ATOM   575  C  C   . THR A 1 91  ? -30.322 10.263  -15.431 1.00 26.66 ?  91  THR A C   1 
ATOM   576  O  O   . THR A 1 91  ? -31.412 9.739   -15.184 1.00 27.84 ?  91  THR A O   1 
ATOM   577  C  CB  . THR A 1 91  ? -29.185 9.379   -13.416 1.00 29.69 ?  91  THR A CB  1 
ATOM   578  O  OG1 . THR A 1 91  ? -29.338 10.649  -12.775 1.00 26.50 ?  91  THR A OG1 1 
ATOM   579  C  CG2 . THR A 1 91  ? -27.969 8.655   -12.863 1.00 27.93 ?  91  THR A CG2 1 
ATOM   580  N  N   . ILE A 1 92  ? -30.224 11.401  -16.109 1.00 30.68 ?  92  ILE A N   1 
ATOM   581  C  CA  . ILE A 1 92  ? -31.386 12.068  -16.689 1.00 35.92 ?  92  ILE A CA  1 
ATOM   582  C  C   . ILE A 1 92  ? -31.048 12.423  -18.131 1.00 38.75 ?  92  ILE A C   1 
ATOM   583  O  O   . ILE A 1 92  ? -29.872 12.396  -18.525 1.00 36.57 ?  92  ILE A O   1 
ATOM   584  C  CB  . ILE A 1 92  ? -31.783 13.327  -15.884 1.00 30.94 ?  92  ILE A CB  1 
ATOM   585  C  CG1 . ILE A 1 92  ? -30.639 14.345  -15.879 1.00 31.03 ?  92  ILE A CG1 1 
ATOM   586  C  CG2 . ILE A 1 92  ? -32.210 12.938  -14.477 1.00 38.26 ?  92  ILE A CG2 1 
ATOM   587  C  CD1 . ILE A 1 92  ? -31.005 15.717  -15.294 1.00 35.98 ?  92  ILE A CD1 1 
ATOM   588  N  N   . PRO A 1 93  ? -32.049 12.747  -18.949 1.00 39.73 ?  93  PRO A N   1 
ATOM   589  C  CA  . PRO A 1 93  ? -31.747 13.277  -20.285 1.00 37.42 ?  93  PRO A CA  1 
ATOM   590  C  C   . PRO A 1 93  ? -30.839 14.482  -20.160 1.00 35.51 ?  93  PRO A C   1 
ATOM   591  O  O   . PRO A 1 93  ? -30.997 15.288  -19.229 1.00 34.61 ?  93  PRO A O   1 
ATOM   592  C  CB  . PRO A 1 93  ? -33.120 13.664  -20.866 1.00 35.26 ?  93  PRO A CB  1 
ATOM   593  C  CG  . PRO A 1 93  ? -34.139 13.070  -19.979 1.00 39.63 ?  93  PRO A CG  1 
ATOM   594  C  CD  . PRO A 1 93  ? -33.489 12.516  -18.744 1.00 34.46 ?  93  PRO A CD  1 
ATOM   595  N  N   . PRO A 1 94  ? -29.845 14.611  -21.041 1.00 37.05 ?  94  PRO A N   1 
ATOM   596  C  CA  . PRO A 1 94  ? -28.865 15.699  -20.879 1.00 34.82 ?  94  PRO A CA  1 
ATOM   597  C  C   . PRO A 1 94  ? -29.486 17.088  -20.885 1.00 33.31 ?  94  PRO A C   1 
ATOM   598  O  O   . PRO A 1 94  ? -28.927 18.006  -20.265 1.00 29.56 ?  94  PRO A O   1 
ATOM   599  C  CB  . PRO A 1 94  ? -27.914 15.490  -22.070 1.00 33.23 ?  94  PRO A CB  1 
ATOM   600  C  CG  . PRO A 1 94  ? -28.698 14.641  -23.049 1.00 38.08 ?  94  PRO A CG  1 
ATOM   601  C  CD  . PRO A 1 94  ? -29.520 13.738  -22.181 1.00 37.16 ?  94  PRO A CD  1 
ATOM   602  N  N   . GLU A 1 95  ? -30.626 17.270  -21.565 1.00 31.92 ?  95  GLU A N   1 
ATOM   603  C  CA  . GLU A 1 95  ? -31.274 18.579  -21.584 1.00 36.14 ?  95  GLU A CA  1 
ATOM   604  C  C   . GLU A 1 95  ? -31.691 19.015  -20.185 1.00 35.66 ?  95  GLU A C   1 
ATOM   605  O  O   . GLU A 1 95  ? -31.753 20.217  -19.902 1.00 34.35 ?  95  GLU A O   1 
ATOM   606  C  CB  . GLU A 1 95  ? -32.498 18.562  -22.505 1.00 37.00 ?  95  GLU A CB  1 
ATOM   607  C  CG  . GLU A 1 95  ? -32.193 18.336  -23.981 1.00 46.82 ?  95  GLU A CG  1 
ATOM   608  C  CD  . GLU A 1 95  ? -32.077 16.857  -24.339 1.00 43.76 ?  95  GLU A CD  1 
ATOM   609  O  OE1 . GLU A 1 95  ? -32.174 15.991  -23.443 1.00 48.96 ?  95  GLU A OE1 1 
ATOM   610  O  OE2 . GLU A 1 95  ? -31.875 16.561  -25.525 1.00 43.85 ?  95  GLU A OE2 1 
ATOM   611  N  N   . VAL A 1 96  ? -31.965 18.056  -19.296 1.00 33.92 ?  96  VAL A N   1 
ATOM   612  C  CA  . VAL A 1 96  ? -32.497 18.384  -17.975 1.00 31.27 ?  96  VAL A CA  1 
ATOM   613  C  C   . VAL A 1 96  ? -31.436 19.023  -17.086 1.00 33.72 ?  96  VAL A C   1 
ATOM   614  O  O   . VAL A 1 96  ? -31.767 19.770  -16.161 1.00 36.15 ?  96  VAL A O   1 
ATOM   615  C  CB  . VAL A 1 96  ? -33.098 17.123  -17.337 1.00 33.96 ?  96  VAL A CB  1 
ATOM   616  C  CG1 . VAL A 1 96  ? -33.746 17.450  -15.995 1.00 36.42 ?  96  VAL A CG1 1 
ATOM   617  C  CG2 . VAL A 1 96  ? -34.104 16.504  -18.288 1.00 31.01 ?  96  VAL A CG2 1 
ATOM   618  N  N   . VAL A 1 97  ? -30.152 18.758  -17.338 1.00 32.88 ?  97  VAL A N   1 
ATOM   619  C  CA  . VAL A 1 97  ? -29.114 19.485  -16.608 1.00 35.38 ?  97  VAL A CA  1 
ATOM   620  C  C   . VAL A 1 97  ? -29.203 20.976  -16.916 1.00 34.27 ?  97  VAL A C   1 
ATOM   621  O  O   . VAL A 1 97  ? -28.854 21.821  -16.081 1.00 33.22 ?  97  VAL A O   1 
ATOM   622  C  CB  . VAL A 1 97  ? -27.720 18.912  -16.940 1.00 29.99 ?  97  VAL A CB  1 
ATOM   623  C  CG1 . VAL A 1 97  ? -26.639 19.649  -16.156 1.00 27.30 ?  97  VAL A CG1 1 
ATOM   624  C  CG2 . VAL A 1 97  ? -27.674 17.422  -16.622 1.00 28.49 ?  97  VAL A CG2 1 
ATOM   625  N  N   . ASN A 1 98  ? -29.688 21.317  -18.111 1.00 34.81 ?  98  ASN A N   1 
ATOM   626  C  CA  . ASN A 1 98  ? -29.983 22.683  -18.526 1.00 37.15 ?  98  ASN A CA  1 
ATOM   627  C  C   . ASN A 1 98  ? -31.425 23.087  -18.213 1.00 34.46 ?  98  ASN A C   1 
ATOM   628  O  O   . ASN A 1 98  ? -32.004 23.903  -18.937 1.00 39.67 ?  98  ASN A O   1 
ATOM   629  C  CB  . ASN A 1 98  ? -29.696 22.829  -20.022 1.00 34.90 ?  98  ASN A CB  1 
ATOM   630  C  CG  . ASN A 1 98  ? -29.439 24.265  -20.437 1.00 41.13 ?  98  ASN A CG  1 
ATOM   631  O  OD1 . ASN A 1 98  ? -28.963 25.080  -19.645 1.00 42.69 ?  98  ASN A OD1 1 
ATOM   632  N  ND2 . ASN A 1 98  ? -29.758 24.583  -21.689 1.00 41.04 ?  98  ASN A ND2 1 
ATOM   633  N  N   . ASN A 1 99  ? -32.016 22.519  -17.157 1.00 34.22 ?  99  ASN A N   1 
ATOM   634  C  CA  . ASN A 1 99  ? -33.413 22.768  -16.810 1.00 37.37 ?  99  ASN A CA  1 
ATOM   635  C  C   . ASN A 1 99  ? -33.763 24.250  -16.880 1.00 37.41 ?  99  ASN A C   1 
ATOM   636  O  O   . ASN A 1 99  ? -34.674 24.657  -17.612 1.00 36.10 ?  99  ASN A O   1 
ATOM   637  C  CB  . ASN A 1 99  ? -33.693 22.217  -15.409 1.00 34.47 ?  99  ASN A CB  1 
ATOM   638  C  CG  . ASN A 1 99  ? -35.165 21.987  -15.148 1.00 38.53 ?  99  ASN A CG  1 
ATOM   639  O  OD1 . ASN A 1 99  ? -35.972 21.879  -16.080 1.00 38.35 ?  99  ASN A OD1 1 
ATOM   640  N  ND2 . ASN A 1 99  ? -35.534 21.936  -13.865 1.00 37.63 ?  99  ASN A ND2 1 
ATOM   641  N  N   . MET A 1 100 ? -33.040 25.079  -16.130 1.00 36.14 ?  100 MET A N   1 
ATOM   642  C  CA  . MET A 1 100 ? -33.396 26.491  -16.101 1.00 38.37 ?  100 MET A CA  1 
ATOM   643  C  C   . MET A 1 100 ? -33.211 27.146  -17.461 1.00 38.17 ?  100 MET A C   1 
ATOM   644  O  O   . MET A 1 100 ? -33.989 28.033  -17.826 1.00 39.59 ?  100 MET A O   1 
ATOM   645  C  CB  . MET A 1 100 ? -32.591 27.217  -15.025 1.00 36.97 ?  100 MET A CB  1 
ATOM   646  C  CG  . MET A 1 100 ? -33.171 26.989  -13.640 1.00 38.73 ?  100 MET A CG  1 
ATOM   647  S  SD  . MET A 1 100 ? -34.713 27.858  -13.261 1.00 46.10 ?  100 MET A SD  1 
ATOM   648  C  CE  . MET A 1 100 ? -34.769 29.166  -14.495 1.00 45.95 ?  100 MET A CE  1 
ATOM   649  N  N   . GLY A 1 101 ? -32.201 26.720  -18.224 1.00 40.50 ?  101 GLY A N   1 
ATOM   650  C  CA  . GLY A 1 101 ? -32.063 27.204  -19.588 1.00 37.48 ?  101 GLY A CA  1 
ATOM   651  C  C   . GLY A 1 101 ? -33.292 26.917  -20.425 1.00 41.51 ?  101 GLY A C   1 
ATOM   652  O  O   . GLY A 1 101 ? -33.849 27.816  -21.058 1.00 40.43 ?  101 GLY A O   1 
ATOM   653  N  N   . ASN A 1 102 ? -33.748 25.660  -20.418 1.00 40.52 ?  102 ASN A N   1 
ATOM   654  C  CA  . ASN A 1 102 ? -34.948 25.306  -21.171 1.00 38.98 ?  102 ASN A CA  1 
ATOM   655  C  C   . ASN A 1 102 ? -36.164 26.073  -20.665 1.00 44.05 ?  102 ASN A C   1 
ATOM   656  O  O   . ASN A 1 102 ? -37.030 26.473  -21.454 1.00 41.08 ?  102 ASN A O   1 
ATOM   657  C  CB  . ASN A 1 102 ? -35.198 23.797  -21.093 1.00 39.15 ?  102 ASN A CB  1 
ATOM   658  C  CG  . ASN A 1 102 ? -33.949 22.971  -21.397 1.00 44.61 ?  102 ASN A CG  1 
ATOM   659  O  OD1 . ASN A 1 102 ? -33.154 23.317  -22.274 1.00 45.45 ?  102 ASN A OD1 1 
ATOM   660  N  ND2 . ASN A 1 102 ? -33.787 21.856  -20.680 1.00 43.33 ?  102 ASN A ND2 1 
ATOM   661  N  N   . ILE A 1 103 ? -36.243 26.292  -19.350 1.00 44.04 ?  103 ILE A N   1 
ATOM   662  C  CA  . ILE A 1 103 ? -37.373 27.017  -18.777 1.00 39.11 ?  103 ILE A CA  1 
ATOM   663  C  C   . ILE A 1 103 ? -37.397 28.454  -19.284 1.00 42.76 ?  103 ILE A C   1 
ATOM   664  O  O   . ILE A 1 103 ? -38.453 28.973  -19.670 1.00 41.84 ?  103 ILE A O   1 
ATOM   665  C  CB  . ILE A 1 103 ? -37.310 26.958  -17.240 1.00 36.07 ?  103 ILE A CB  1 
ATOM   666  C  CG1 . ILE A 1 103 ? -37.642 25.548  -16.749 1.00 34.23 ?  103 ILE A CG1 1 
ATOM   667  C  CG2 . ILE A 1 103 ? -38.239 27.997  -16.603 1.00 33.47 ?  103 ILE A CG2 1 
ATOM   668  C  CD1 . ILE A 1 103 ? -37.053 25.232  -15.371 1.00 31.99 ?  103 ILE A CD1 1 
ATOM   669  N  N   . ASN A 1 104 ? -36.232 29.109  -19.312 1.00 40.12 ?  104 ASN A N   1 
ATOM   670  C  CA  . ASN A 1 104 ? -36.167 30.504  -19.740 1.00 44.58 ?  104 ASN A CA  1 
ATOM   671  C  C   . ASN A 1 104 ? -36.477 30.670  -21.223 1.00 43.42 ?  104 ASN A C   1 
ATOM   672  O  O   . ASN A 1 104 ? -37.089 31.668  -21.613 1.00 46.00 ?  104 ASN A O   1 
ATOM   673  C  CB  . ASN A 1 104 ? -34.791 31.084  -19.420 1.00 40.31 ?  104 ASN A CB  1 
ATOM   674  C  CG  . ASN A 1 104 ? -34.575 31.273  -17.938 1.00 39.97 ?  104 ASN A CG  1 
ATOM   675  O  OD1 . ASN A 1 104 ? -35.527 31.292  -17.164 1.00 39.54 ?  104 ASN A OD1 1 
ATOM   676  N  ND2 . ASN A 1 104 ? -33.322 31.394  -17.530 1.00 44.33 ?  104 ASN A ND2 1 
ATOM   677  N  N   . SER A 1 105 ? -36.070 29.716  -22.063 1.00 45.89 ?  105 SER A N   1 
ATOM   678  C  CA  . SER A 1 105 ? -36.239 29.887  -23.502 1.00 46.34 ?  105 SER A CA  1 
ATOM   679  C  C   . SER A 1 105 ? -37.638 29.511  -23.963 1.00 47.25 ?  105 SER A C   1 
ATOM   680  O  O   . SER A 1 105 ? -38.102 30.011  -24.995 1.00 48.29 ?  105 SER A O   1 
ATOM   681  C  CB  . SER A 1 105 ? -35.204 29.056  -24.264 1.00 44.07 ?  105 SER A CB  1 
ATOM   682  O  OG  . SER A 1 105 ? -35.412 27.669  -24.060 1.00 46.44 ?  105 SER A OG  1 
ATOM   683  N  N   . ALA A 1 106 ? -38.320 28.636  -23.231 1.00 43.86 ?  106 ALA A N   1 
ATOM   684  C  CA  . ALA A 1 106 ? -39.649 28.192  -23.613 1.00 45.78 ?  106 ALA A CA  1 
ATOM   685  C  C   . ALA A 1 106 ? -40.750 29.073  -23.042 1.00 43.94 ?  106 ALA A C   1 
ATOM   686  O  O   . ALA A 1 106 ? -41.922 28.689  -23.099 1.00 46.31 ?  106 ALA A O   1 
ATOM   687  C  CB  . ALA A 1 106 ? -39.860 26.737  -23.182 1.00 44.65 ?  106 ALA A CB  1 
ATOM   688  N  N   . GLY A 1 107 ? -40.405 30.239  -22.494 1.00 43.01 ?  107 GLY A N   1 
ATOM   689  C  CA  . GLY A 1 107 ? -41.402 31.107  -21.897 1.00 39.52 ?  107 GLY A CA  1 
ATOM   690  C  C   . GLY A 1 107 ? -42.039 30.571  -20.632 1.00 45.97 ?  107 GLY A C   1 
ATOM   691  O  O   . GLY A 1 107 ? -43.115 31.036  -20.249 1.00 47.29 ?  107 GLY A O   1 
ATOM   692  N  N   . LEU A 1 108 ? -41.403 29.599  -19.973 1.00 43.83 ?  108 LEU A N   1 
ATOM   693  C  CA  . LEU A 1 108 ? -41.920 28.987  -18.753 1.00 44.73 ?  108 LEU A CA  1 
ATOM   694  C  C   . LEU A 1 108 ? -41.426 29.673  -17.482 1.00 37.49 ?  108 LEU A C   1 
ATOM   695  O  O   . LEU A 1 108 ? -41.839 29.285  -16.383 1.00 36.99 ?  108 LEU A O   1 
ATOM   696  C  CB  . LEU A 1 108 ? -41.538 27.501  -18.709 1.00 40.79 ?  108 LEU A CB  1 
ATOM   697  C  CG  . LEU A 1 108 ? -42.011 26.605  -19.855 1.00 43.11 ?  108 LEU A CG  1 
ATOM   698  C  CD1 . LEU A 1 108 ? -41.698 25.154  -19.555 1.00 42.18 ?  108 LEU A CD1 1 
ATOM   699  C  CD2 . LEU A 1 108 ? -43.503 26.780  -20.097 1.00 44.36 ?  108 LEU A CD2 1 
ATOM   700  N  N   . ARG A 1 109 ? -40.569 30.687  -17.603 1.00 37.29 ?  109 ARG A N   1 
ATOM   701  C  CA  . ARG A 1 109 ? -39.911 31.247  -16.427 1.00 39.75 ?  109 ARG A CA  1 
ATOM   702  C  C   . ARG A 1 109 ? -40.911 31.871  -15.457 1.00 42.29 ?  109 ARG A C   1 
ATOM   703  O  O   . ARG A 1 109 ? -40.812 31.665  -14.241 1.00 40.37 ?  109 ARG A O   1 
ATOM   704  C  CB  . ARG A 1 109 ? -38.867 32.277  -16.853 1.00 43.88 ?  109 ARG A CB  1 
ATOM   705  C  CG  . ARG A 1 109 ? -37.977 32.732  -15.723 1.00 50.67 ?  109 ARG A CG  1 
ATOM   706  C  CD  . ARG A 1 109 ? -37.028 33.828  -16.165 1.00 50.74 ?  109 ARG A CD  1 
ATOM   707  N  NE  . ARG A 1 109 ? -36.358 34.459  -15.033 1.00 53.50 ?  109 ARG A NE  1 
ATOM   708  C  CZ  . ARG A 1 109 ? -35.450 33.868  -14.266 1.00 54.70 ?  109 ARG A CZ  1 
ATOM   709  N  NH1 . ARG A 1 109 ? -35.070 32.616  -14.474 1.00 55.18 ?  109 ARG A NH1 1 
ATOM   710  N  NH2 . ARG A 1 109 ? -34.908 34.550  -13.261 1.00 58.87 ?  109 ARG A NH2 1 
ATOM   711  N  N   . ASN A 1 110 ? -41.879 32.634  -15.973 1.00 39.80 ?  110 ASN A N   1 
ATOM   712  C  CA  . ASN A 1 110 ? -42.832 33.315  -15.100 1.00 39.26 ?  110 ASN A CA  1 
ATOM   713  C  C   . ASN A 1 110 ? -43.610 32.317  -14.253 1.00 36.15 ?  110 ASN A C   1 
ATOM   714  O  O   . ASN A 1 110 ? -43.744 32.492  -13.036 1.00 35.76 ?  110 ASN A O   1 
ATOM   715  C  CB  . ASN A 1 110 ? -43.796 34.168  -15.930 1.00 42.70 ?  110 ASN A CB  1 
ATOM   716  C  CG  . ASN A 1 110 ? -43.223 35.526  -16.272 1.00 52.25 ?  110 ASN A CG  1 
ATOM   717  O  OD1 . ASN A 1 110 ? -42.007 35.729  -16.224 1.00 52.13 ?  110 ASN A OD1 1 
ATOM   718  N  ND2 . ASN A 1 110 ? -44.093 36.461  -16.641 1.00 60.88 ?  110 ASN A ND2 1 
ATOM   719  N  N   . ALA A 1 111 ? -44.148 31.272  -14.893 1.00 30.20 ?  111 ALA A N   1 
ATOM   720  C  CA  . ALA A 1 111 ? -44.872 30.230  -14.168 1.00 29.33 ?  111 ALA A CA  1 
ATOM   721  C  C   . ALA A 1 111 ? -43.981 29.573  -13.120 1.00 30.07 ?  111 ALA A C   1 
ATOM   722  O  O   . ALA A 1 111 ? -44.395 29.379  -11.971 1.00 32.47 ?  111 ALA A O   1 
ATOM   723  C  CB  . ALA A 1 111 ? -45.404 29.183  -15.152 1.00 28.00 ?  111 ALA A CB  1 
ATOM   724  N  N   . VAL A 1 112 ? -42.750 29.226  -13.503 1.00 28.68 ?  112 VAL A N   1 
ATOM   725  C  CA  . VAL A 1 112 ? -41.833 28.553  -12.582 1.00 29.67 ?  112 VAL A CA  1 
ATOM   726  C  C   . VAL A 1 112 ? -41.501 29.459  -11.397 1.00 29.64 ?  112 VAL A C   1 
ATOM   727  O  O   . VAL A 1 112 ? -41.646 29.072  -10.234 1.00 27.85 ?  112 VAL A O   1 
ATOM   728  C  CB  . VAL A 1 112 ? -40.560 28.100  -13.329 1.00 26.06 ?  112 VAL A CB  1 
ATOM   729  C  CG1 . VAL A 1 112 ? -39.425 27.835  -12.350 1.00 30.39 ?  112 VAL A CG1 1 
ATOM   730  C  CG2 . VAL A 1 112 ? -40.839 26.857  -14.172 1.00 22.40 ?  112 VAL A CG2 1 
ATOM   731  N  N   . MET A 1 113 ? -41.052 30.681  -11.671 1.00 28.57 ?  113 MET A N   1 
ATOM   732  C  CA  . MET A 1 113 ? -40.637 31.556  -10.578 1.00 34.76 ?  113 MET A CA  1 
ATOM   733  C  C   . MET A 1 113 ? -41.808 31.901  -9.664  1.00 34.70 ?  113 MET A C   1 
ATOM   734  O  O   . MET A 1 113 ? -41.640 32.013  -8.441  1.00 34.62 ?  113 MET A O   1 
ATOM   735  C  CB  . MET A 1 113 ? -39.990 32.822  -11.139 1.00 36.64 ?  113 MET A CB  1 
ATOM   736  C  CG  . MET A 1 113 ? -38.740 32.526  -11.976 1.00 42.28 ?  113 MET A CG  1 
ATOM   737  S  SD  . MET A 1 113 ? -37.239 31.845  -11.187 1.00 50.59 ?  113 MET A SD  1 
ATOM   738  C  CE  . MET A 1 113 ? -37.461 32.131  -9.432  1.00 48.98 ?  113 MET A CE  1 
ATOM   739  N  N   . LYS A 1 114 ? -43.009 32.065  -10.232 1.00 35.87 ?  114 LYS A N   1 
ATOM   740  C  CA  . LYS A 1 114 ? -44.180 32.310  -9.394  1.00 34.97 ?  114 LYS A CA  1 
ATOM   741  C  C   . LYS A 1 114 ? -44.429 31.130  -8.467  1.00 30.73 ?  114 LYS A C   1 
ATOM   742  O  O   . LYS A 1 114 ? -44.786 31.311  -7.297  1.00 32.20 ?  114 LYS A O   1 
ATOM   743  C  CB  . LYS A 1 114 ? -45.408 32.574  -10.269 1.00 36.70 ?  114 LYS A CB  1 
ATOM   744  C  CG  . LYS A 1 114 ? -45.563 34.029  -10.732 1.00 45.85 ?  114 LYS A CG  1 
ATOM   745  C  CD  . LYS A 1 114 ? -46.544 34.813  -9.862  1.00 45.75 ?  114 LYS A CD  1 
ATOM   746  C  CE  . LYS A 1 114 ? -47.806 34.006  -9.596  1.00 52.27 ?  114 LYS A CE  1 
ATOM   747  N  NZ  . LYS A 1 114 ? -48.698 34.667  -8.596  1.00 57.37 ?  114 LYS A NZ  1 
ATOM   748  N  N   . THR A 1 115 ? -44.228 29.912  -8.973  1.00 29.26 ?  115 THR A N   1 
ATOM   749  C  CA  . THR A 1 115 ? -44.401 28.708  -8.164  1.00 28.39 ?  115 THR A CA  1 
ATOM   750  C  C   . THR A 1 115 ? -43.356 28.634  -7.053  1.00 31.02 ?  115 THR A C   1 
ATOM   751  O  O   . THR A 1 115 ? -43.665 28.235  -5.925  1.00 30.82 ?  115 THR A O   1 
ATOM   752  C  CB  . THR A 1 115 ? -44.321 27.470  -9.072  1.00 32.79 ?  115 THR A CB  1 
ATOM   753  O  OG1 . THR A 1 115 ? -45.458 27.440  -9.941  1.00 33.11 ?  115 THR A OG1 1 
ATOM   754  C  CG2 . THR A 1 115 ? -44.298 26.173  -8.252  1.00 27.73 ?  115 THR A CG2 1 
ATOM   755  N  N   . LEU A 1 116 ? -42.115 29.023  -7.344  1.00 31.83 ?  116 LEU A N   1 
ATOM   756  C  CA  . LEU A 1 116 ? -41.063 28.922  -6.341  1.00 30.62 ?  116 LEU A CA  1 
ATOM   757  C  C   . LEU A 1 116 ? -41.081 30.066  -5.336  1.00 34.93 ?  116 LEU A C   1 
ATOM   758  O  O   . LEU A 1 116 ? -40.383 29.983  -4.325  1.00 34.65 ?  116 LEU A O   1 
ATOM   759  C  CB  . LEU A 1 116 ? -39.695 28.859  -7.017  1.00 28.86 ?  116 LEU A CB  1 
ATOM   760  C  CG  . LEU A 1 116 ? -39.516 27.698  -7.992  1.00 28.51 ?  116 LEU A CG  1 
ATOM   761  C  CD1 . LEU A 1 116 ? -38.177 27.810  -8.724  1.00 26.25 ?  116 LEU A CD1 1 
ATOM   762  C  CD2 . LEU A 1 116 ? -39.619 26.374  -7.241  1.00 26.44 ?  116 LEU A CD2 1 
ATOM   763  N  N   . SER A 1 117 ? -41.865 31.120  -5.579  1.00 40.24 ?  117 SER A N   1 
ATOM   764  C  CA  . SER A 1 117 ? -41.947 32.260  -4.672  1.00 38.73 ?  117 SER A CA  1 
ATOM   765  C  C   . SER A 1 117 ? -42.858 31.969  -3.483  1.00 40.01 ?  117 SER A C   1 
ATOM   766  O  O   . SER A 1 117 ? -44.077 31.842  -3.657  1.00 36.84 ?  117 SER A O   1 
ATOM   767  C  CB  . SER A 1 117 ? -42.446 33.497  -5.414  1.00 36.83 ?  117 SER A CB  1 
ATOM   768  O  OG  . SER A 1 117 ? -42.441 34.614  -4.541  1.00 48.03 ?  117 SER A OG  1 
ATOM   769  N  N   . PRO A 1 118 ? -42.310 31.859  -2.265  1.00 37.68 ?  118 PRO A N   1 
ATOM   770  C  CA  . PRO A 1 118 ? -43.176 31.682  -1.086  1.00 41.55 ?  118 PRO A CA  1 
ATOM   771  C  C   . PRO A 1 118 ? -44.190 32.797  -0.914  1.00 44.70 ?  118 PRO A C   1 
ATOM   772  O  O   . PRO A 1 118 ? -45.266 32.564  -0.346  1.00 43.19 ?  118 PRO A O   1 
ATOM   773  C  CB  . PRO A 1 118 ? -42.176 31.647  0.080   1.00 40.25 ?  118 PRO A CB  1 
ATOM   774  C  CG  . PRO A 1 118 ? -40.891 31.181  -0.544  1.00 36.43 ?  118 PRO A CG  1 
ATOM   775  C  CD  . PRO A 1 118 ? -40.881 31.813  -1.910  1.00 34.67 ?  118 PRO A CD  1 
ATOM   776  N  N   . GLN A 1 119 ? -43.879 34.002  -1.400  1.00 45.42 ?  119 GLN A N   1 
ATOM   777  C  CA  . GLN A 1 119 ? -44.801 35.124  -1.274  1.00 45.82 ?  119 GLN A CA  1 
ATOM   778  C  C   . GLN A 1 119 ? -46.018 34.971  -2.180  1.00 47.60 ?  119 GLN A C   1 
ATOM   779  O  O   . GLN A 1 119 ? -47.094 35.487  -1.856  1.00 50.41 ?  119 GLN A O   1 
ATOM   780  C  CB  . GLN A 1 119 ? -44.067 36.422  -1.585  1.00 49.32 ?  119 GLN A CB  1 
ATOM   781  N  N   . ALA A 1 120 ? -45.876 34.275  -3.310  1.00 40.94 ?  120 ALA A N   1 
ATOM   782  C  CA  . ALA A 1 120 ? -47.006 34.087  -4.213  1.00 37.35 ?  120 ALA A CA  1 
ATOM   783  C  C   . ALA A 1 120 ? -48.051 33.133  -3.648  1.00 40.50 ?  120 ALA A C   1 
ATOM   784  O  O   . ALA A 1 120 ? -49.175 33.094  -4.163  1.00 42.19 ?  120 ALA A O   1 
ATOM   785  C  CB  . ALA A 1 120 ? -46.513 33.581  -5.567  1.00 31.40 ?  120 ALA A CB  1 
ATOM   786  N  N   . ASP A 1 121 ? -47.710 32.365  -2.614  1.00 37.40 ?  121 ASP A N   1 
ATOM   787  C  CA  . ASP A 1 121 ? -48.628 31.431  -1.957  1.00 33.84 ?  121 ASP A CA  1 
ATOM   788  C  C   . ASP A 1 121 ? -48.831 31.939  -0.532  1.00 38.58 ?  121 ASP A C   1 
ATOM   789  O  O   . ASP A 1 121 ? -48.192 31.479  0.415   1.00 34.80 ?  121 ASP A O   1 
ATOM   790  C  CB  . ASP A 1 121 ? -48.058 29.984  -2.000  1.00 35.75 ?  121 ASP A CB  1 
ATOM   791  C  CG  . ASP A 1 121 ? -48.993 28.943  -1.368  1.00 36.27 ?  121 ASP A CG  1 
ATOM   792  O  OD1 . ASP A 1 121 ? -49.925 29.312  -0.628  1.00 33.84 ?  121 ASP A OD1 1 
ATOM   793  O  OD2 . ASP A 1 121 ? -48.784 27.733  -1.605  1.00 38.25 ?  121 ASP A OD2 1 
ATOM   794  N  N   . ARG A 1 122 ? -49.750 32.901  -0.385  1.00 39.21 ?  122 ARG A N   1 
ATOM   795  C  CA  . ARG A 1 122 ? -49.944 33.590  0.889   1.00 40.81 ?  122 ARG A CA  1 
ATOM   796  C  C   . ARG A 1 122 ? -50.272 32.628  2.031   1.00 37.06 ?  122 ARG A C   1 
ATOM   797  O  O   . ARG A 1 122 ? -50.007 32.944  3.196   1.00 36.64 ?  122 ARG A O   1 
ATOM   798  C  CB  . ARG A 1 122 ? -51.043 34.649  0.724   1.00 43.72 ?  122 ARG A CB  1 
ATOM   799  N  N   . GLU A 1 123 ? -50.815 31.453  1.719   1.00 38.45 ?  123 GLU A N   1 
ATOM   800  C  CA  . GLU A 1 123 ? -51.123 30.429  2.706   1.00 38.12 ?  123 GLU A CA  1 
ATOM   801  C  C   . GLU A 1 123 ? -49.955 29.504  3.027   1.00 31.00 ?  123 GLU A C   1 
ATOM   802  O  O   . GLU A 1 123 ? -50.067 28.715  3.969   1.00 27.38 ?  123 GLU A O   1 
ATOM   803  C  CB  . GLU A 1 123 ? -52.287 29.567  2.217   1.00 38.47 ?  123 GLU A CB  1 
ATOM   804  C  CG  . GLU A 1 123 ? -53.566 30.324  2.095   1.00 48.72 ?  123 GLU A CG  1 
ATOM   805  C  CD  . GLU A 1 123 ? -53.938 30.929  3.408   1.00 48.24 ?  123 GLU A CD  1 
ATOM   806  O  OE1 . GLU A 1 123 ? -53.743 30.234  4.430   1.00 51.72 ?  123 GLU A OE1 1 
ATOM   807  O  OE2 . GLU A 1 123 ? -54.440 32.077  3.416   1.00 50.34 ?  123 GLU A OE2 1 
ATOM   808  N  N   . LEU A 1 124 ? -48.858 29.559  2.268   1.00 32.01 ?  124 LEU A N   1 
ATOM   809  C  CA  . LEU A 1 124 ? -47.854 28.497  2.359   1.00 27.95 ?  124 LEU A CA  1 
ATOM   810  C  C   . LEU A 1 124 ? -47.292 28.371  3.771   1.00 25.53 ?  124 LEU A C   1 
ATOM   811  O  O   . LEU A 1 124 ? -47.179 27.258  4.302   1.00 20.91 ?  124 LEU A O   1 
ATOM   812  C  CB  . LEU A 1 124 ? -46.735 28.740  1.350   1.00 29.65 ?  124 LEU A CB  1 
ATOM   813  C  CG  . LEU A 1 124 ? -45.590 27.724  1.464   1.00 29.22 ?  124 LEU A CG  1 
ATOM   814  C  CD1 . LEU A 1 124 ? -46.052 26.320  1.073   1.00 25.84 ?  124 LEU A CD1 1 
ATOM   815  C  CD2 . LEU A 1 124 ? -44.392 28.162  0.641   1.00 24.64 ?  124 LEU A CD2 1 
ATOM   816  N  N   . GLY A 1 125 ? -46.985 29.503  4.414   1.00 23.79 ?  125 GLY A N   1 
ATOM   817  C  CA  . GLY A 1 125 ? -46.417 29.464  5.754   1.00 20.30 ?  125 GLY A CA  1 
ATOM   818  C  C   . GLY A 1 125 ? -47.288 28.745  6.773   1.00 28.10 ?  125 GLY A C   1 
ATOM   819  O  O   . GLY A 1 125 ? -46.829 27.836  7.479   1.00 24.46 ?  125 GLY A O   1 
ATOM   820  N  N   . GLY A 1 126 ? -48.548 29.165  6.902   1.00 25.59 ?  126 GLY A N   1 
ATOM   821  C  CA  . GLY A 1 126 ? -49.426 28.487  7.847   1.00 20.91 ?  126 GLY A CA  1 
ATOM   822  C  C   . GLY A 1 126 ? -49.616 27.016  7.510   1.00 23.23 ?  126 GLY A C   1 
ATOM   823  O  O   . GLY A 1 126 ? -49.698 26.163  8.399   1.00 24.25 ?  126 GLY A O   1 
ATOM   824  N  N   . TRP A 1 127 ? -49.687 26.696  6.219   1.00 22.74 ?  127 TRP A N   1 
ATOM   825  C  CA  . TRP A 1 127 ? -49.894 25.307  5.812   1.00 23.41 ?  127 TRP A CA  1 
ATOM   826  C  C   . TRP A 1 127 ? -48.670 24.445  6.129   1.00 22.37 ?  127 TRP A C   1 
ATOM   827  O  O   . TRP A 1 127 ? -48.803 23.321  6.624   1.00 21.14 ?  127 TRP A O   1 
ATOM   828  C  CB  . TRP A 1 127 ? -50.228 25.247  4.320   1.00 21.98 ?  127 TRP A CB  1 
ATOM   829  C  CG  . TRP A 1 127 ? -50.411 23.860  3.753   1.00 24.74 ?  127 TRP A CG  1 
ATOM   830  C  CD1 . TRP A 1 127 ? -51.576 23.144  3.681   1.00 32.50 ?  127 TRP A CD1 1 
ATOM   831  C  CD2 . TRP A 1 127 ? -49.402 23.041  3.154   1.00 25.68 ?  127 TRP A CD2 1 
ATOM   832  N  NE1 . TRP A 1 127 ? -51.349 21.928  3.083   1.00 33.88 ?  127 TRP A NE1 1 
ATOM   833  C  CE2 . TRP A 1 127 ? -50.021 21.838  2.754   1.00 28.44 ?  127 TRP A CE2 1 
ATOM   834  C  CE3 . TRP A 1 127 ? -48.028 23.200  2.932   1.00 27.59 ?  127 TRP A CE3 1 
ATOM   835  C  CZ2 . TRP A 1 127 ? -49.315 20.802  2.129   1.00 27.67 ?  127 TRP A CZ2 1 
ATOM   836  C  CZ3 . TRP A 1 127 ? -47.329 22.169  2.314   1.00 25.95 ?  127 TRP A CZ3 1 
ATOM   837  C  CH2 . TRP A 1 127 ? -47.976 20.990  1.916   1.00 25.60 ?  127 TRP A CH2 1 
ATOM   838  N  N   . LEU A 1 128 ? -47.468 24.946  5.823   1.00 21.47 ?  128 LEU A N   1 
ATOM   839  C  CA  . LEU A 1 128 ? -46.247 24.218  6.177   1.00 21.12 ?  128 LEU A CA  1 
ATOM   840  C  C   . LEU A 1 128 ? -46.143 24.001  7.682   1.00 21.25 ?  128 LEU A C   1 
ATOM   841  O  O   . LEU A 1 128 ? -45.765 22.912  8.133   1.00 18.69 ?  128 LEU A O   1 
ATOM   842  C  CB  . LEU A 1 128 ? -45.009 24.966  5.676   1.00 19.07 ?  128 LEU A CB  1 
ATOM   843  C  CG  . LEU A 1 128 ? -44.592 24.760  4.222   1.00 24.86 ?  128 LEU A CG  1 
ATOM   844  C  CD1 . LEU A 1 128 ? -43.450 25.719  3.859   1.00 21.77 ?  128 LEU A CD1 1 
ATOM   845  C  CD2 . LEU A 1 128 ? -44.191 23.298  3.962   1.00 20.04 ?  128 LEU A CD2 1 
ATOM   846  N  N   . GLU A 1 129 ? -46.461 25.029  8.478   1.00 21.99 ?  129 GLU A N   1 
ATOM   847  C  CA  . GLU A 1 129 ? -46.452 24.847  9.929   1.00 24.42 ?  129 GLU A CA  1 
ATOM   848  C  C   . GLU A 1 129 ? -47.389 23.723  10.345  1.00 21.68 ?  129 GLU A C   1 
ATOM   849  O  O   . GLU A 1 129 ? -47.050 22.903  11.208  1.00 21.26 ?  129 GLU A O   1 
ATOM   850  C  CB  . GLU A 1 129 ? -46.837 26.148  10.646  1.00 22.86 ?  129 GLU A CB  1 
ATOM   851  C  CG  . GLU A 1 129 ? -46.573 26.073  12.145  1.00 27.13 ?  129 GLU A CG  1 
ATOM   852  C  CD  . GLU A 1 129 ? -46.967 27.341  12.905  1.00 36.70 ?  129 GLU A CD  1 
ATOM   853  O  OE1 . GLU A 1 129 ? -47.392 28.331  12.277  1.00 34.71 ?  129 GLU A OE1 1 
ATOM   854  O  OE2 . GLU A 1 129 ? -46.816 27.347  14.142  1.00 41.03 ?  129 GLU A OE2 1 
ATOM   855  N  N   . ALA A 1 130 ? -48.574 23.669  9.744   1.00 22.18 ?  130 ALA A N   1 
ATOM   856  C  CA  . ALA A 1 130 ? -49.553 22.667  10.154  1.00 22.37 ?  130 ALA A CA  1 
ATOM   857  C  C   . ALA A 1 130 ? -49.131 21.268  9.711   1.00 21.91 ?  130 ALA A C   1 
ATOM   858  O  O   . ALA A 1 130 ? -49.321 20.298  10.458  1.00 18.90 ?  130 ALA A O   1 
ATOM   859  C  CB  . ALA A 1 130 ? -50.939 23.033  9.604   1.00 21.14 ?  130 ALA A CB  1 
ATOM   860  N  N   . GLN A 1 131 ? -48.547 21.142  8.507   1.00 22.97 ?  131 GLN A N   1 
ATOM   861  C  CA  . GLN A 1 131 ? -47.976 19.856  8.085   1.00 23.45 ?  131 GLN A CA  1 
ATOM   862  C  C   . GLN A 1 131 ? -46.907 19.378  9.064   1.00 23.09 ?  131 GLN A C   1 
ATOM   863  O  O   . GLN A 1 131 ? -46.878 18.200  9.445   1.00 21.16 ?  131 GLN A O   1 
ATOM   864  C  CB  . GLN A 1 131 ? -47.364 19.961  6.681   1.00 22.98 ?  131 GLN A CB  1 
ATOM   865  C  CG  . GLN A 1 131 ? -48.350 20.241  5.560   1.00 30.47 ?  131 GLN A CG  1 
ATOM   866  C  CD  . GLN A 1 131 ? -49.228 19.047  5.204   1.00 33.01 ?  131 GLN A CD  1 
ATOM   867  O  OE1 . GLN A 1 131 ? -48.766 17.903  5.150   1.00 31.58 ?  131 GLN A OE1 1 
ATOM   868  N  NE2 . GLN A 1 131 ? -50.516 19.315  4.968   1.00 34.87 ?  131 GLN A NE2 1 
ATOM   869  N  N   . ALA A 1 132 ? -45.996 20.276  9.463   1.00 16.77 ?  132 ALA A N   1 
ATOM   870  C  CA  . ALA A 1 132 ? -44.913 19.859  10.347  1.00 18.80 ?  132 ALA A CA  1 
ATOM   871  C  C   . ALA A 1 132 ? -45.465 19.396  11.684  1.00 17.61 ?  132 ALA A C   1 
ATOM   872  O  O   . ALA A 1 132 ? -45.012 18.389  12.236  1.00 15.75 ?  132 ALA A O   1 
ATOM   873  C  CB  . ALA A 1 132 ? -43.913 21.004  10.545  1.00 19.12 ?  132 ALA A CB  1 
ATOM   874  N  N   . HIS A 1 133 ? -46.473 20.105  12.199  1.00 17.67 ?  133 HIS A N   1 
ATOM   875  C  CA  . HIS A 1 133 ? -47.053 19.751  13.490  1.00 21.14 ?  133 HIS A CA  1 
ATOM   876  C  C   . HIS A 1 133 ? -47.806 18.423  13.422  1.00 20.26 ?  133 HIS A C   1 
ATOM   877  O  O   . HIS A 1 133 ? -47.756 17.626  14.369  1.00 21.13 ?  133 HIS A O   1 
ATOM   878  C  CB  . HIS A 1 133 ? -47.978 20.870  13.971  1.00 21.34 ?  133 HIS A CB  1 
ATOM   879  C  CG  . HIS A 1 133 ? -47.279 21.954  14.733  1.00 22.55 ?  133 HIS A CG  1 
ATOM   880  N  ND1 . HIS A 1 133 ? -46.597 22.980  14.117  1.00 28.02 ?  133 HIS A ND1 1 
ATOM   881  C  CD2 . HIS A 1 133 ? -47.167 22.174  16.062  1.00 23.96 ?  133 HIS A CD2 1 
ATOM   882  C  CE1 . HIS A 1 133 ? -46.080 23.775  15.034  1.00 27.35 ?  133 HIS A CE1 1 
ATOM   883  N  NE2 . HIS A 1 133 ? -46.417 23.313  16.223  1.00 28.75 ?  133 HIS A NE2 1 
ATOM   884  N  N   . GLN A 1 134 ? -48.514 18.157  12.317  1.00 20.61 ?  134 GLN A N   1 
ATOM   885  C  CA  . GLN A 1 134 ? -49.258 16.897  12.238  1.00 20.95 ?  134 GLN A CA  1 
ATOM   886  C  C   . GLN A 1 134 ? -48.305 15.716  12.251  1.00 18.82 ?  134 GLN A C   1 
ATOM   887  O  O   . GLN A 1 134 ? -48.555 14.708  12.922  1.00 18.55 ?  134 GLN A O   1 
ATOM   888  C  CB  . GLN A 1 134 ? -50.131 16.853  10.978  1.00 24.90 ?  134 GLN A CB  1 
ATOM   889  C  CG  . GLN A 1 134 ? -51.428 17.630  11.089  1.00 28.02 ?  134 GLN A CG  1 
ATOM   890  C  CD  . GLN A 1 134 ? -52.494 17.149  10.114  1.00 29.82 ?  134 GLN A CD  1 
ATOM   891  O  OE1 . GLN A 1 134 ? -52.263 16.245  9.310   1.00 34.10 ?  134 GLN A OE1 1 
ATOM   892  N  NE2 . GLN A 1 134 ? -53.693 17.715  10.229  1.00 35.97 ?  134 GLN A NE2 1 
ATOM   893  N  N   . LEU A 1 135 ? -47.185 15.841  11.536  1.00 19.24 ?  135 LEU A N   1 
ATOM   894  C  CA  . LEU A 1 135 ? -46.188 14.773  11.515  1.00 20.05 ?  135 LEU A CA  1 
ATOM   895  C  C   . LEU A 1 135 ? -45.535 14.592  12.883  1.00 18.94 ?  135 LEU A C   1 
ATOM   896  O  O   . LEU A 1 135 ? -45.286 13.464  13.310  1.00 18.50 ?  135 LEU A O   1 
ATOM   897  C  CB  . LEU A 1 135 ? -45.138 15.081  10.459  1.00 18.81 ?  135 LEU A CB  1 
ATOM   898  C  CG  . LEU A 1 135 ? -45.668 15.086  9.018   1.00 20.68 ?  135 LEU A CG  1 
ATOM   899  C  CD1 . LEU A 1 135 ? -44.683 15.802  8.081   1.00 17.19 ?  135 LEU A CD1 1 
ATOM   900  C  CD2 . LEU A 1 135 ? -45.943 13.652  8.553   1.00 17.35 ?  135 LEU A CD2 1 
ATOM   901  N  N   . LEU A 1 136 ? -45.235 15.688  13.575  1.00 17.58 ?  136 LEU A N   1 
ATOM   902  C  CA  . LEU A 1 136 ? -44.620 15.560  14.894  1.00 18.94 ?  136 LEU A CA  1 
ATOM   903  C  C   . LEU A 1 136 ? -45.616 15.021  15.921  1.00 17.62 ?  136 LEU A C   1 
ATOM   904  O  O   . LEU A 1 136 ? -45.251 14.216  16.787  1.00 18.50 ?  136 LEU A O   1 
ATOM   905  C  CB  . LEU A 1 136 ? -44.059 16.913  15.336  1.00 16.67 ?  136 LEU A CB  1 
ATOM   906  C  CG  . LEU A 1 136 ? -42.831 17.409  14.560  1.00 20.41 ?  136 LEU A CG  1 
ATOM   907  C  CD1 . LEU A 1 136 ? -42.558 18.912  14.834  1.00 18.25 ?  136 LEU A CD1 1 
ATOM   908  C  CD2 . LEU A 1 136 ? -41.603 16.551  14.888  1.00 16.78 ?  136 LEU A CD2 1 
ATOM   909  N  N   . ASP A 1 137 ? -46.876 15.456  15.845  1.00 17.34 ?  137 ASP A N   1 
ATOM   910  C  CA  . ASP A 1 137 ? -47.889 14.953  16.777  1.00 21.76 ?  137 ASP A CA  1 
ATOM   911  C  C   . ASP A 1 137 ? -48.081 13.444  16.610  1.00 23.07 ?  137 ASP A C   1 
ATOM   912  O  O   . ASP A 1 137 ? -48.240 12.709  17.597  1.00 21.12 ?  137 ASP A O   1 
ATOM   913  C  CB  . ASP A 1 137 ? -49.216 15.704  16.559  1.00 18.75 ?  137 ASP A CB  1 
ATOM   914  C  CG  . ASP A 1 137 ? -49.216 17.106  17.189  1.00 23.42 ?  137 ASP A CG  1 
ATOM   915  O  OD1 . ASP A 1 137 ? -48.542 17.301  18.213  1.00 25.66 ?  137 ASP A OD1 1 
ATOM   916  O  OD2 . ASP A 1 137 ? -49.872 18.020  16.649  1.00 25.02 ?  137 ASP A OD2 1 
ATOM   917  N  N   . ARG A 1 138 ? -48.087 12.971  15.358  1.00 21.48 ?  138 ARG A N   1 
ATOM   918  C  CA  . ARG A 1 138 ? -48.133 11.533  15.103  1.00 26.04 ?  138 ARG A CA  1 
ATOM   919  C  C   . ARG A 1 138 ? -46.974 10.813  15.779  1.00 20.21 ?  138 ARG A C   1 
ATOM   920  O  O   . ARG A 1 138 ? -47.161 9.750   16.372  1.00 19.08 ?  138 ARG A O   1 
ATOM   921  C  CB  . ARG A 1 138 ? -48.114 11.269  13.598  1.00 26.67 ?  138 ARG A CB  1 
ATOM   922  C  CG  . ARG A 1 138 ? -48.289 9.801   13.194  1.00 32.86 ?  138 ARG A CG  1 
ATOM   923  C  CD  . ARG A 1 138 ? -48.307 9.694   11.662  1.00 37.19 ?  138 ARG A CD  1 
ATOM   924  N  NE  . ARG A 1 138 ? -48.075 8.340   11.170  1.00 43.94 ?  138 ARG A NE  1 
ATOM   925  C  CZ  . ARG A 1 138 ? -49.007 7.398   11.095  1.00 52.56 ?  138 ARG A CZ  1 
ATOM   926  N  NH1 . ARG A 1 138 ? -50.259 7.630   11.472  1.00 44.45 ?  138 ARG A NH1 1 
ATOM   927  N  NH2 . ARG A 1 138 ? -48.676 6.194   10.628  1.00 48.71 ?  138 ARG A NH2 1 
ATOM   928  N  N   . LEU A 1 139 ? -45.763 11.374  15.706  1.00 20.53 ?  139 LEU A N   1 
ATOM   929  C  CA  . LEU A 1 139 ? -44.639 10.707  16.365  1.00 18.30 ?  139 LEU A CA  1 
ATOM   930  C  C   . LEU A 1 139 ? -44.772 10.787  17.879  1.00 19.93 ?  139 LEU A C   1 
ATOM   931  O  O   . LEU A 1 139 ? -44.414 9.841   18.584  1.00 17.59 ?  139 LEU A O   1 
ATOM   932  C  CB  . LEU A 1 139 ? -43.308 11.305  15.900  1.00 18.24 ?  139 LEU A CB  1 
ATOM   933  C  CG  . LEU A 1 139 ? -43.045 11.186  14.396  1.00 21.78 ?  139 LEU A CG  1 
ATOM   934  C  CD1 . LEU A 1 139 ? -41.840 12.011  13.972  1.00 22.92 ?  139 LEU A CD1 1 
ATOM   935  C  CD2 . LEU A 1 139 ? -42.872 9.704   13.958  1.00 19.69 ?  139 LEU A CD2 1 
ATOM   936  N  N   . ILE A 1 140 ? -45.303 11.901  18.400  1.00 20.87 ?  140 ILE A N   1 
ATOM   937  C  CA  . ILE A 1 140 ? -45.537 11.996  19.842  1.00 18.04 ?  140 ILE A CA  1 
ATOM   938  C  C   . ILE A 1 140 ? -46.570 10.964  20.281  1.00 21.13 ?  140 ILE A C   1 
ATOM   939  O  O   . ILE A 1 140 ? -46.394 10.285  21.302  1.00 20.43 ?  140 ILE A O   1 
ATOM   940  C  CB  . ILE A 1 140 ? -45.951 13.431  20.227  1.00 21.78 ?  140 ILE A CB  1 
ATOM   941  C  CG1 . ILE A 1 140 ? -44.752 14.374  20.078  1.00 22.38 ?  140 ILE A CG1 1 
ATOM   942  C  CG2 . ILE A 1 140 ? -46.512 13.501  21.680  1.00 19.32 ?  140 ILE A CG2 1 
ATOM   943  C  CD1 . ILE A 1 140 ? -45.132 15.824  19.803  1.00 17.85 ?  140 ILE A CD1 1 
ATOM   944  N  N   . GLU A 1 141 ? -47.652 10.817  19.503  1.00 24.23 ?  141 GLU A N   1 
ATOM   945  C  CA  . GLU A 1 141 ? -48.645 9.768   19.746  1.00 25.07 ?  141 GLU A CA  1 
ATOM   946  C  C   . GLU A 1 141 ? -47.985 8.415   19.981  1.00 25.21 ?  141 GLU A C   1 
ATOM   947  O  O   . GLU A 1 141 ? -48.261 7.736   20.976  1.00 20.93 ?  141 GLU A O   1 
ATOM   948  C  CB  . GLU A 1 141 ? -49.608 9.689   18.555  1.00 24.52 ?  141 GLU A CB  1 
ATOM   949  C  CG  . GLU A 1 141 ? -50.724 8.651   18.661  1.00 31.32 ?  141 GLU A CG  1 
ATOM   950  C  CD  . GLU A 1 141 ? -51.343 8.336   17.298  1.00 29.11 ?  141 GLU A CD  1 
ATOM   951  O  OE1 . GLU A 1 141 ? -51.485 9.276   16.492  1.00 34.41 ?  141 GLU A OE1 1 
ATOM   952  O  OE2 . GLU A 1 141 ? -51.679 7.165   17.025  1.00 35.31 ?  141 GLU A OE2 1 
ATOM   953  N  N   . GLN A 1 142 ? -47.073 8.029   19.089  1.00 23.24 ?  142 GLN A N   1 
ATOM   954  C  CA  . GLN A 1 142 ? -46.493 6.694   19.149  1.00 23.46 ?  142 GLN A CA  1 
ATOM   955  C  C   . GLN A 1 142 ? -45.387 6.595   20.192  1.00 23.25 ?  142 GLN A C   1 
ATOM   956  O  O   . GLN A 1 142 ? -45.131 5.505   20.722  1.00 21.43 ?  142 GLN A O   1 
ATOM   957  C  CB  . GLN A 1 142 ? -45.958 6.313   17.767  1.00 25.60 ?  142 GLN A CB  1 
ATOM   958  C  CG  . GLN A 1 142 ? -47.034 6.260   16.688  1.00 32.00 ?  142 GLN A CG  1 
ATOM   959  C  CD  . GLN A 1 142 ? -46.455 6.128   15.287  1.00 38.07 ?  142 GLN A CD  1 
ATOM   960  O  OE1 . GLN A 1 142 ? -45.258 5.855   15.113  1.00 34.01 ?  142 GLN A OE1 1 
ATOM   961  N  NE2 . GLN A 1 142 ? -47.301 6.317   14.279  1.00 42.44 ?  142 GLN A NE2 1 
ATOM   962  N  N   . GLY A 1 143 ? -44.691 7.696   20.477  1.00 21.36 ?  143 GLY A N   1 
ATOM   963  C  CA  . GLY A 1 143 ? -43.662 7.681   21.498  1.00 20.74 ?  143 GLY A CA  1 
ATOM   964  C  C   . GLY A 1 143 ? -42.278 7.411   20.935  1.00 20.20 ?  143 GLY A C   1 
ATOM   965  O  O   . GLY A 1 143 ? -42.126 6.858   19.851  1.00 19.57 ?  143 GLY A O   1 
ATOM   966  N  N   . PRO A 1 144 ? -41.236 7.779   21.672  1.00 22.92 ?  144 PRO A N   1 
ATOM   967  C  CA  . PRO A 1 144 ? -39.865 7.624   21.148  1.00 20.82 ?  144 PRO A CA  1 
ATOM   968  C  C   . PRO A 1 144 ? -39.382 6.190   21.294  1.00 23.05 ?  144 PRO A C   1 
ATOM   969  O  O   . PRO A 1 144 ? -39.928 5.421   22.102  1.00 21.91 ?  144 PRO A O   1 
ATOM   970  C  CB  . PRO A 1 144 ? -39.053 8.597   22.017  1.00 22.05 ?  144 PRO A CB  1 
ATOM   971  C  CG  . PRO A 1 144 ? -39.780 8.598   23.341  1.00 23.64 ?  144 PRO A CG  1 
ATOM   972  C  CD  . PRO A 1 144 ? -41.265 8.437   22.989  1.00 22.05 ?  144 PRO A CD  1 
ATOM   973  N  N   . PRO A 1 145 ? -38.368 5.767   20.509  1.00 21.07 ?  145 PRO A N   1 
ATOM   974  C  CA  . PRO A 1 145 ? -37.680 6.564   19.498  1.00 20.83 ?  145 PRO A CA  1 
ATOM   975  C  C   . PRO A 1 145 ? -38.467 6.658   18.200  1.00 23.60 ?  145 PRO A C   1 
ATOM   976  O  O   . PRO A 1 145 ? -39.480 5.973   17.996  1.00 22.10 ?  145 PRO A O   1 
ATOM   977  C  CB  . PRO A 1 145 ? -36.381 5.795   19.273  1.00 20.72 ?  145 PRO A CB  1 
ATOM   978  C  CG  . PRO A 1 145 ? -36.801 4.359   19.454  1.00 22.40 ?  145 PRO A CG  1 
ATOM   979  C  CD  . PRO A 1 145 ? -37.873 4.378   20.531  1.00 18.25 ?  145 PRO A CD  1 
ATOM   980  N  N   . ALA A 1 146 ? -37.992 7.520   17.314  1.00 21.31 ?  146 ALA A N   1 
ATOM   981  C  CA  . ALA A 1 146 ? -38.585 7.599   15.994  1.00 19.48 ?  146 ALA A CA  1 
ATOM   982  C  C   . ALA A 1 146 ? -37.487 7.927   14.998  1.00 19.63 ?  146 ALA A C   1 
ATOM   983  O  O   . ALA A 1 146 ? -36.406 8.401   15.367  1.00 18.72 ?  146 ALA A O   1 
ATOM   984  C  CB  . ALA A 1 146 ? -39.699 8.642   15.935  1.00 16.82 ?  146 ALA A CB  1 
ATOM   985  N  N   . ASP A 1 147 ? -37.775 7.640   13.731  1.00 14.38 ?  147 ASP A N   1 
ATOM   986  C  CA  . ASP A 1 147 ? -36.899 7.980   12.620  1.00 14.88 ?  147 ASP A CA  1 
ATOM   987  C  C   . ASP A 1 147 ? -37.428 9.272   12.000  1.00 17.94 ?  147 ASP A C   1 
ATOM   988  O  O   . ASP A 1 147 ? -38.489 9.276   11.360  1.00 21.09 ?  147 ASP A O   1 
ATOM   989  C  CB  . ASP A 1 147 ? -36.864 6.819   11.624  1.00 17.05 ?  147 ASP A CB  1 
ATOM   990  C  CG  . ASP A 1 147 ? -36.201 7.177   10.313  1.00 19.34 ?  147 ASP A CG  1 
ATOM   991  O  OD1 . ASP A 1 147 ? -35.346 8.093   10.283  1.00 17.69 ?  147 ASP A OD1 1 
ATOM   992  O  OD2 . ASP A 1 147 ? -36.556 6.524   9.309   1.00 19.85 ?  147 ASP A OD2 1 
ATOM   993  N  N   . LEU A 1 148 ? -36.697 10.373  12.199  1.00 18.73 ?  148 LEU A N   1 
ATOM   994  C  CA  . LEU A 1 148 ? -37.156 11.660  11.693  1.00 19.00 ?  148 LEU A CA  1 
ATOM   995  C  C   . LEU A 1 148 ? -36.960 11.814  10.193  1.00 17.88 ?  148 LEU A C   1 
ATOM   996  O  O   . LEU A 1 148 ? -37.419 12.807  9.627   1.00 20.06 ?  148 LEU A O   1 
ATOM   997  C  CB  . LEU A 1 148 ? -36.445 12.814  12.411  1.00 17.43 ?  148 LEU A CB  1 
ATOM   998  C  CG  . LEU A 1 148 ? -36.876 12.998  13.874  1.00 21.79 ?  148 LEU A CG  1 
ATOM   999  C  CD1 . LEU A 1 148 ? -36.381 14.311  14.477  1.00 16.19 ?  148 LEU A CD1 1 
ATOM   1000 C  CD2 . LEU A 1 148 ? -38.368 12.874  13.990  1.00 19.56 ?  148 LEU A CD2 1 
ATOM   1001 N  N   . ARG A 1 149 ? -36.282 10.885  9.534   1.00 19.75 ?  149 ARG A N   1 
ATOM   1002 C  CA  . ARG A 1 149 ? -36.261 10.942  8.077   1.00 17.51 ?  149 ARG A CA  1 
ATOM   1003 C  C   . ARG A 1 149 ? -37.579 10.424  7.512   1.00 17.10 ?  149 ARG A C   1 
ATOM   1004 O  O   . ARG A 1 149 ? -38.328 11.168  6.870   1.00 18.40 ?  149 ARG A O   1 
ATOM   1005 C  CB  . ARG A 1 149 ? -35.080 10.145  7.515   1.00 18.70 ?  149 ARG A CB  1 
ATOM   1006 C  CG  . ARG A 1 149 ? -35.158 10.012  5.998   1.00 18.85 ?  149 ARG A CG  1 
ATOM   1007 C  CD  . ARG A 1 149 ? -33.882 9.472   5.368   1.00 20.21 ?  149 ARG A CD  1 
ATOM   1008 N  NE  . ARG A 1 149 ? -34.014 9.431   3.913   1.00 23.39 ?  149 ARG A NE  1 
ATOM   1009 C  CZ  . ARG A 1 149 ? -34.774 8.556   3.263   1.00 25.29 ?  149 ARG A CZ  1 
ATOM   1010 N  NH1 . ARG A 1 149 ? -35.447 7.609   3.905   1.00 28.45 ?  149 ARG A NH1 1 
ATOM   1011 N  NH2 . ARG A 1 149 ? -34.846 8.616   1.939   1.00 29.03 ?  149 ARG A NH2 1 
ATOM   1012 N  N   . ASP A 1 150 ? -37.897 9.152   7.766   1.00 18.71 ?  150 ASP A N   1 
ATOM   1013 C  CA  . ASP A 1 150 ? -39.149 8.606   7.250   1.00 20.48 ?  150 ASP A CA  1 
ATOM   1014 C  C   . ASP A 1 150 ? -40.363 9.228   7.933   1.00 19.35 ?  150 ASP A C   1 
ATOM   1015 O  O   . ASP A 1 150 ? -41.398 9.423   7.291   1.00 20.22 ?  150 ASP A O   1 
ATOM   1016 C  CB  . ASP A 1 150 ? -39.188 7.082   7.422   1.00 20.38 ?  150 ASP A CB  1 
ATOM   1017 C  CG  . ASP A 1 150 ? -40.486 6.476   6.897   1.00 19.59 ?  150 ASP A CG  1 
ATOM   1018 O  OD1 . ASP A 1 150 ? -40.703 6.547   5.678   1.00 27.81 ?  150 ASP A OD1 1 
ATOM   1019 O  OD2 . ASP A 1 150 ? -41.303 5.953   7.688   1.00 22.60 ?  150 ASP A OD2 1 
ATOM   1020 N  N   . GLY A 1 151 ? -40.260 9.544   9.223   1.00 17.91 ?  151 GLY A N   1 
ATOM   1021 C  CA  . GLY A 1 151 ? -41.390 10.112  9.932   1.00 17.24 ?  151 GLY A CA  1 
ATOM   1022 C  C   . GLY A 1 151 ? -41.525 11.613  9.861   1.00 21.53 ?  151 GLY A C   1 
ATOM   1023 O  O   . GLY A 1 151 ? -42.509 12.160  10.360  1.00 24.28 ?  151 GLY A O   1 
ATOM   1024 N  N   . PHE A 1 152 ? -40.568 12.318  9.264   1.00 18.86 ?  152 PHE A N   1 
ATOM   1025 C  CA  . PHE A 1 152 ? -40.643 13.770  9.297   1.00 19.13 ?  152 PHE A CA  1 
ATOM   1026 C  C   . PHE A 1 152 ? -40.101 14.514  8.083   1.00 19.81 ?  152 PHE A C   1 
ATOM   1027 O  O   . PHE A 1 152 ? -40.838 15.313  7.505   1.00 20.85 ?  152 PHE A O   1 
ATOM   1028 C  CB  . PHE A 1 152 ? -39.920 14.308  10.543  1.00 17.58 ?  152 PHE A CB  1 
ATOM   1029 C  CG  . PHE A 1 152 ? -40.061 15.800  10.752  1.00 19.50 ?  152 PHE A CG  1 
ATOM   1030 C  CD1 . PHE A 1 152 ? -41.312 16.393  10.830  1.00 20.17 ?  152 PHE A CD1 1 
ATOM   1031 C  CD2 . PHE A 1 152 ? -38.935 16.599  10.916  1.00 17.90 ?  152 PHE A CD2 1 
ATOM   1032 C  CE1 . PHE A 1 152 ? -41.446 17.768  11.043  1.00 19.90 ?  152 PHE A CE1 1 
ATOM   1033 C  CE2 . PHE A 1 152 ? -39.055 17.973  11.137  1.00 22.04 ?  152 PHE A CE2 1 
ATOM   1034 C  CZ  . PHE A 1 152 ? -40.324 18.564  11.201  1.00 18.92 ?  152 PHE A CZ  1 
ATOM   1035 N  N   . THR A 1 153 ? -38.843 14.286  7.672   1.00 16.97 ?  153 THR A N   1 
ATOM   1036 C  CA  . THR A 1 153 ? -38.252 15.191  6.674   1.00 18.96 ?  153 THR A CA  1 
ATOM   1037 C  C   . THR A 1 153 ? -38.751 14.729  5.304   1.00 20.48 ?  153 THR A C   1 
ATOM   1038 O  O   . THR A 1 153 ? -39.013 15.564  4.426   1.00 15.32 ?  153 THR A O   1 
ATOM   1039 C  CB  . THR A 1 153 ? -36.718 15.202  6.685   1.00 17.97 ?  153 THR A CB  1 
ATOM   1040 O  OG1 . THR A 1 153 ? -36.241 13.946  6.208   1.00 16.16 ?  153 THR A OG1 1 
ATOM   1041 C  CG2 . THR A 1 153 ? -36.178 15.417  8.104   1.00 16.77 ?  153 THR A CG2 1 
ATOM   1042 N  N   . GLU A 1 154 ? -38.844 13.404  5.082   1.00 20.84 ?  154 GLU A N   1 
ATOM   1043 C  CA  . GLU A 1 154 ? -39.361 12.885  3.811   1.00 20.42 ?  154 GLU A CA  1 
ATOM   1044 C  C   . GLU A 1 154 ? -40.821 13.265  3.576   1.00 18.43 ?  154 GLU A C   1 
ATOM   1045 O  O   . GLU A 1 154 ? -41.110 13.951  2.577   1.00 17.68 ?  154 GLU A O   1 
ATOM   1046 C  CB  . GLU A 1 154 ? -39.157 11.366  3.740   1.00 17.02 ?  154 GLU A CB  1 
ATOM   1047 C  CG  . GLU A 1 154 ? -37.703 10.908  3.524   1.00 22.49 ?  154 GLU A CG  1 
ATOM   1048 C  CD  . GLU A 1 154 ? -37.180 11.261  2.134   1.00 23.38 ?  154 GLU A CD  1 
ATOM   1049 O  OE1 . GLU A 1 154 ? -37.520 10.560  1.159   1.00 19.78 ?  154 GLU A OE1 1 
ATOM   1050 O  OE2 . GLU A 1 154 ? -36.415 12.227  2.016   1.00 22.57 ?  154 GLU A OE2 1 
ATOM   1051 N  N   . PRO A 1 155 ? -41.777 12.881  4.433   1.00 15.44 ?  155 PRO A N   1 
ATOM   1052 C  CA  . PRO A 1 155 ? -43.178 13.256  4.158   1.00 19.44 ?  155 PRO A CA  1 
ATOM   1053 C  C   . PRO A 1 155 ? -43.408 14.757  4.098   1.00 16.95 ?  155 PRO A C   1 
ATOM   1054 O  O   . PRO A 1 155 ? -44.229 15.219  3.290   1.00 21.27 ?  155 PRO A O   1 
ATOM   1055 C  CB  . PRO A 1 155 ? -43.956 12.619  5.327   1.00 21.00 ?  155 PRO A CB  1 
ATOM   1056 C  CG  . PRO A 1 155 ? -42.933 12.450  6.419   1.00 20.63 ?  155 PRO A CG  1 
ATOM   1057 C  CD  . PRO A 1 155 ? -41.646 12.138  5.699   1.00 17.84 ?  155 PRO A CD  1 
ATOM   1058 N  N   . TYR A 1 156 ? -42.692 15.532  4.925   1.00 16.88 ?  156 TYR A N   1 
ATOM   1059 C  CA  . TYR A 1 156 ? -42.831 16.989  4.923   1.00 16.94 ?  156 TYR A CA  1 
ATOM   1060 C  C   . TYR A 1 156 ? -42.332 17.593  3.614   1.00 17.06 ?  156 TYR A C   1 
ATOM   1061 O  O   . TYR A 1 156 ? -42.992 18.455  3.019   1.00 19.07 ?  156 TYR A O   1 
ATOM   1062 C  CB  . TYR A 1 156 ? -42.063 17.555  6.114   1.00 16.24 ?  156 TYR A CB  1 
ATOM   1063 C  CG  . TYR A 1 156 ? -41.953 19.062  6.217   1.00 16.67 ?  156 TYR A CG  1 
ATOM   1064 C  CD1 . TYR A 1 156 ? -43.039 19.836  6.658   1.00 17.84 ?  156 TYR A CD1 1 
ATOM   1065 C  CD2 . TYR A 1 156 ? -40.751 19.713  5.912   1.00 17.41 ?  156 TYR A CD2 1 
ATOM   1066 C  CE1 . TYR A 1 156 ? -42.932 21.237  6.787   1.00 17.62 ?  156 TYR A CE1 1 
ATOM   1067 C  CE2 . TYR A 1 156 ? -40.625 21.113  6.035   1.00 17.16 ?  156 TYR A CE2 1 
ATOM   1068 C  CZ  . TYR A 1 156 ? -41.723 21.865  6.478   1.00 18.86 ?  156 TYR A CZ  1 
ATOM   1069 O  OH  . TYR A 1 156 ? -41.601 23.231  6.610   1.00 17.50 ?  156 TYR A OH  1 
ATOM   1070 N  N   . SER A 1 157 ? -41.162 17.149  3.141   1.00 16.43 ?  157 SER A N   1 
ATOM   1071 C  CA  . SER A 1 157 ? -40.631 17.661  1.877   1.00 14.30 ?  157 SER A CA  1 
ATOM   1072 C  C   . SER A 1 157 ? -41.479 17.231  0.679   1.00 15.25 ?  157 SER A C   1 
ATOM   1073 O  O   . SER A 1 157 ? -41.600 17.976  -0.300  1.00 17.79 ?  157 SER A O   1 
ATOM   1074 C  CB  . SER A 1 157 ? -39.183 17.183  1.692   1.00 15.70 ?  157 SER A CB  1 
ATOM   1075 O  OG  . SER A 1 157 ? -38.380 17.561  2.806   1.00 14.54 ?  157 SER A OG  1 
ATOM   1076 N  N   . ALA A 1 158 ? -42.004 16.002  0.700   1.00 15.14 ?  158 ALA A N   1 
ATOM   1077 C  CA  . ALA A 1 158 ? -42.844 15.545  -0.398  1.00 18.04 ?  158 ALA A CA  1 
ATOM   1078 C  C   . ALA A 1 158 ? -44.165 16.299  -0.425  1.00 19.60 ?  158 ALA A C   1 
ATOM   1079 O  O   . ALA A 1 158 ? -44.662 16.649  -1.503  1.00 22.21 ?  158 ALA A O   1 
ATOM   1080 C  CB  . ALA A 1 158 ? -43.095 14.045  -0.278  1.00 18.68 ?  158 ALA A CB  1 
ATOM   1081 N  N   . ALA A 1 159 ? -44.746 16.546  0.755   1.00 17.41 ?  159 ALA A N   1 
ATOM   1082 C  CA  . ALA A 1 159 ? -45.957 17.352  0.846   1.00 19.54 ?  159 ALA A CA  1 
ATOM   1083 C  C   . ALA A 1 159 ? -45.749 18.710  0.192   1.00 19.74 ?  159 ALA A C   1 
ATOM   1084 O  O   . ALA A 1 159 ? -46.549 19.131  -0.652  1.00 23.75 ?  159 ALA A O   1 
ATOM   1085 C  CB  . ALA A 1 159 ? -46.370 17.521  2.313   1.00 18.15 ?  159 ALA A CB  1 
ATOM   1086 N  N   . LEU A 1 160 ? -44.657 19.397  0.549   1.00 20.61 ?  160 LEU A N   1 
ATOM   1087 C  CA  . LEU A 1 160 ? -44.392 20.717  -0.028  1.00 23.18 ?  160 LEU A CA  1 
ATOM   1088 C  C   . LEU A 1 160 ? -44.308 20.646  -1.546  1.00 21.84 ?  160 LEU A C   1 
ATOM   1089 O  O   . LEU A 1 160 ? -44.887 21.478  -2.254  1.00 20.93 ?  160 LEU A O   1 
ATOM   1090 C  CB  . LEU A 1 160 ? -43.096 21.311  0.540   1.00 17.63 ?  160 LEU A CB  1 
ATOM   1091 C  CG  . LEU A 1 160 ? -42.558 22.510  -0.265  1.00 23.91 ?  160 LEU A CG  1 
ATOM   1092 C  CD1 . LEU A 1 160 ? -43.523 23.670  -0.212  1.00 21.59 ?  160 LEU A CD1 1 
ATOM   1093 C  CD2 . LEU A 1 160 ? -41.165 22.947  0.221   1.00 26.84 ?  160 LEU A CD2 1 
ATOM   1094 N  N   . HIS A 1 161 ? -43.586 19.657  -2.071  1.00 21.15 ?  161 HIS A N   1 
ATOM   1095 C  CA  . HIS A 1 161 ? -43.377 19.642  -3.512  1.00 19.81 ?  161 HIS A CA  1 
ATOM   1096 C  C   . HIS A 1 161 ? -44.585 19.096  -4.262  1.00 19.17 ?  161 HIS A C   1 
ATOM   1097 O  O   . HIS A 1 161 ? -44.790 19.452  -5.428  1.00 18.08 ?  161 HIS A O   1 
ATOM   1098 C  CB  . HIS A 1 161 ? -42.079 18.897  -3.823  1.00 18.44 ?  161 HIS A CB  1 
ATOM   1099 C  CG  . HIS A 1 161 ? -40.876 19.683  -3.405  1.00 18.64 ?  161 HIS A CG  1 
ATOM   1100 N  ND1 . HIS A 1 161 ? -40.442 19.725  -2.099  1.00 17.34 ?  161 HIS A ND1 1 
ATOM   1101 C  CD2 . HIS A 1 161 ? -40.087 20.544  -4.092  1.00 19.47 ?  161 HIS A CD2 1 
ATOM   1102 C  CE1 . HIS A 1 161 ? -39.412 20.550  -2.004  1.00 16.60 ?  161 HIS A CE1 1 
ATOM   1103 N  NE2 . HIS A 1 161 ? -39.180 21.064  -3.198  1.00 21.45 ?  161 HIS A NE2 1 
ATOM   1104 N  N   . CYS A 1 162 ? -45.413 18.289  -3.606  1.00 19.36 ?  162 CYS A N   1 
ATOM   1105 C  CA  . CYS A 1 162 ? -46.717 17.968  -4.174  1.00 21.39 ?  162 CYS A CA  1 
ATOM   1106 C  C   . CYS A 1 162 ? -47.559 19.225  -4.313  1.00 23.83 ?  162 CYS A C   1 
ATOM   1107 O  O   . CYS A 1 162 ? -48.162 19.470  -5.365  1.00 22.15 ?  162 CYS A O   1 
ATOM   1108 C  CB  . CYS A 1 162 ? -47.431 16.940  -3.302  1.00 21.95 ?  162 CYS A CB  1 
ATOM   1109 S  SG  . CYS A 1 162 ? -46.790 15.279  -3.556  1.00 22.58 ?  162 CYS A SG  1 
ATOM   1110 N  N   . ARG A 1 163 ? -47.597 20.038  -3.252  1.00 21.32 ?  163 ARG A N   1 
ATOM   1111 C  CA  . ARG A 1 163 ? -48.324 21.308  -3.285  1.00 26.84 ?  163 ARG A CA  1 
ATOM   1112 C  C   . ARG A 1 163 ? -47.765 22.254  -4.347  1.00 22.22 ?  163 ARG A C   1 
ATOM   1113 O  O   . ARG A 1 163 ? -48.525 22.926  -5.053  1.00 25.12 ?  163 ARG A O   1 
ATOM   1114 C  CB  . ARG A 1 163 ? -48.270 21.964  -1.899  1.00 24.01 ?  163 ARG A CB  1 
ATOM   1115 C  CG  . ARG A 1 163 ? -49.012 23.298  -1.791  1.00 28.44 ?  163 ARG A CG  1 
ATOM   1116 C  CD  . ARG A 1 163 ? -48.915 23.861  -0.373  1.00 24.26 ?  163 ARG A CD  1 
ATOM   1117 N  NE  . ARG A 1 163 ? -49.463 25.211  -0.276  1.00 30.74 ?  163 ARG A NE  1 
ATOM   1118 C  CZ  . ARG A 1 163 ? -50.699 25.494  0.114   1.00 30.32 ?  163 ARG A CZ  1 
ATOM   1119 N  NH1 . ARG A 1 163 ? -51.565 24.542  0.406   1.00 25.74 ?  163 ARG A NH1 1 
ATOM   1120 N  NH2 . ARG A 1 163 ? -51.072 26.767  0.221   1.00 31.31 ?  163 ARG A NH2 1 
ATOM   1121 N  N   . LEU A 1 164 ? -46.438 22.327  -4.469  1.00 21.96 ?  164 LEU A N   1 
ATOM   1122 C  CA  . LEU A 1 164 ? -45.820 23.154  -5.509  1.00 22.05 ?  164 LEU A CA  1 
ATOM   1123 C  C   . LEU A 1 164 ? -46.317 22.775  -6.900  1.00 23.99 ?  164 LEU A C   1 
ATOM   1124 O  O   . LEU A 1 164 ? -46.589 23.648  -7.733  1.00 24.56 ?  164 LEU A O   1 
ATOM   1125 C  CB  . LEU A 1 164 ? -44.299 23.003  -5.466  1.00 24.93 ?  164 LEU A CB  1 
ATOM   1126 C  CG  . LEU A 1 164 ? -43.464 23.719  -4.400  1.00 29.85 ?  164 LEU A CG  1 
ATOM   1127 C  CD1 . LEU A 1 164 ? -42.041 23.805  -4.910  1.00 28.23 ?  164 LEU A CD1 1 
ATOM   1128 C  CD2 . LEU A 1 164 ? -44.013 25.102  -4.062  1.00 28.78 ?  164 LEU A CD2 1 
ATOM   1129 N  N   . LEU A 1 165 ? -46.413 21.472  -7.179  1.00 24.88 ?  165 LEU A N   1 
ATOM   1130 C  CA  . LEU A 1 165 ? -46.811 21.006  -8.507  1.00 27.16 ?  165 LEU A CA  1 
ATOM   1131 C  C   . LEU A 1 165 ? -48.321 21.055  -8.712  1.00 25.44 ?  165 LEU A C   1 
ATOM   1132 O  O   . LEU A 1 165 ? -48.774 21.180  -9.852  1.00 23.77 ?  165 LEU A O   1 
ATOM   1133 C  CB  . LEU A 1 165 ? -46.318 19.575  -8.742  1.00 20.49 ?  165 LEU A CB  1 
ATOM   1134 C  CG  . LEU A 1 165 ? -44.806 19.359  -8.830  1.00 24.04 ?  165 LEU A CG  1 
ATOM   1135 C  CD1 . LEU A 1 165 ? -44.502 18.013  -9.453  1.00 24.42 ?  165 LEU A CD1 1 
ATOM   1136 C  CD2 . LEU A 1 165 ? -44.169 20.463  -9.637  1.00 30.62 ?  165 LEU A CD2 1 
ATOM   1137 N  N   . GLY A 1 166 ? -49.106 20.965  -7.639  1.00 26.91 ?  166 GLY A N   1 
ATOM   1138 C  CA  . GLY A 1 166 ? -50.548 20.875  -7.769  1.00 29.37 ?  166 GLY A CA  1 
ATOM   1139 C  C   . GLY A 1 166 ? -51.053 19.458  -7.887  1.00 32.46 ?  166 GLY A C   1 
ATOM   1140 O  O   . GLY A 1 166 ? -52.000 19.202  -8.641  1.00 31.72 ?  166 GLY A O   1 
ATOM   1141 N  N   . ILE A 1 167 ? -50.421 18.516  -7.203  1.00 31.08 ?  167 ILE A N   1 
ATOM   1142 C  CA  . ILE A 1 167 ? -50.802 17.110  -7.292  1.00 28.85 ?  167 ILE A CA  1 
ATOM   1143 C  C   . ILE A 1 167 ? -51.103 16.636  -5.878  1.00 28.61 ?  167 ILE A C   1 
ATOM   1144 O  O   . ILE A 1 167 ? -50.675 17.262  -4.891  1.00 25.71 ?  167 ILE A O   1 
ATOM   1145 C  CB  . ILE A 1 167 ? -49.710 16.262  -7.989  1.00 29.38 ?  167 ILE A CB  1 
ATOM   1146 C  CG1 . ILE A 1 167 ? -48.446 16.168  -7.126  1.00 26.28 ?  167 ILE A CG1 1 
ATOM   1147 C  CG2 . ILE A 1 167 ? -49.352 16.847  -9.361  1.00 27.58 ?  167 ILE A CG2 1 
ATOM   1148 C  CD1 . ILE A 1 167 ? -47.398 15.236  -7.694  1.00 22.95 ?  167 ILE A CD1 1 
ATOM   1149 N  N   . PRO A 1 168 ? -51.887 15.572  -5.730  1.00 31.48 ?  168 PRO A N   1 
ATOM   1150 C  CA  . PRO A 1 168 ? -52.159 15.056  -4.389  1.00 31.32 ?  168 PRO A CA  1 
ATOM   1151 C  C   . PRO A 1 168 ? -50.883 14.487  -3.805  1.00 28.96 ?  168 PRO A C   1 
ATOM   1152 O  O   . PRO A 1 168 ? -49.881 14.320  -4.497  1.00 31.34 ?  168 PRO A O   1 
ATOM   1153 C  CB  . PRO A 1 168 ? -53.214 13.965  -4.599  1.00 29.82 ?  168 PRO A CB  1 
ATOM   1154 C  CG  . PRO A 1 168 ? -53.633 14.066  -6.021  1.00 34.08 ?  168 PRO A CG  1 
ATOM   1155 C  CD  . PRO A 1 168 ? -52.561 14.781  -6.774  1.00 34.53 ?  168 PRO A CD  1 
ATOM   1156 N  N   . THR A 1 169 ? -50.924 14.211  -2.505  1.00 31.69 ?  169 THR A N   1 
ATOM   1157 C  CA  . THR A 1 169 ? -49.822 13.550  -1.825  1.00 29.29 ?  169 THR A CA  1 
ATOM   1158 C  C   . THR A 1 169 ? -50.006 12.046  -1.732  1.00 28.86 ?  169 THR A C   1 
ATOM   1159 O  O   . THR A 1 169 ? -49.216 11.390  -1.051  1.00 33.28 ?  169 THR A O   1 
ATOM   1160 C  CB  . THR A 1 169 ? -49.638 14.108  -0.413  1.00 33.13 ?  169 THR A CB  1 
ATOM   1161 O  OG1 . THR A 1 169 ? -50.841 13.890  0.337   1.00 31.52 ?  169 THR A OG1 1 
ATOM   1162 C  CG2 . THR A 1 169 ? -49.293 15.600  -0.441  1.00 25.36 ?  169 THR A CG2 1 
ATOM   1163 N  N   . ASP A 1 170 ? -51.022 11.488  -2.399  1.00 31.77 ?  170 ASP A N   1 
ATOM   1164 C  CA  . ASP A 1 170 ? -51.362 10.077  -2.214  1.00 28.29 ?  170 ASP A CA  1 
ATOM   1165 C  C   . ASP A 1 170 ? -50.168 9.161   -2.456  1.00 29.92 ?  170 ASP A C   1 
ATOM   1166 O  O   . ASP A 1 170 ? -49.963 8.188   -1.717  1.00 33.31 ?  170 ASP A O   1 
ATOM   1167 C  CB  . ASP A 1 170 ? -52.494 9.675   -3.159  1.00 33.90 ?  170 ASP A CB  1 
ATOM   1168 C  CG  . ASP A 1 170 ? -53.719 10.554  -3.030  1.00 40.21 ?  170 ASP A CG  1 
ATOM   1169 O  OD1 . ASP A 1 170 ? -53.733 11.493  -2.200  1.00 38.78 ?  170 ASP A OD1 1 
ATOM   1170 O  OD2 . ASP A 1 170 ? -54.666 10.310  -3.796  1.00 45.18 ?  170 ASP A OD2 1 
ATOM   1171 N  N   . ASP A 1 171 ? -49.380 9.440   -3.494  1.00 26.15 ?  171 ASP A N   1 
ATOM   1172 C  CA  . ASP A 1 171 ? -48.306 8.555   -3.928  1.00 29.86 ?  171 ASP A CA  1 
ATOM   1173 C  C   . ASP A 1 171 ? -46.922 9.049   -3.515  1.00 26.44 ?  171 ASP A C   1 
ATOM   1174 O  O   . ASP A 1 171 ? -45.941 8.794   -4.220  1.00 27.43 ?  171 ASP A O   1 
ATOM   1175 C  CB  . ASP A 1 171 ? -48.373 8.374   -5.441  1.00 26.52 ?  171 ASP A CB  1 
ATOM   1176 C  CG  . ASP A 1 171 ? -49.748 7.966   -5.901  1.00 30.13 ?  171 ASP A CG  1 
ATOM   1177 O  OD1 . ASP A 1 171 ? -50.254 6.934   -5.409  1.00 30.73 ?  171 ASP A OD1 1 
ATOM   1178 O  OD2 . ASP A 1 171 ? -50.327 8.686   -6.734  1.00 28.94 ?  171 ASP A OD2 1 
ATOM   1179 N  N   . TRP A 1 172 ? -46.810 9.722   -2.370  1.00 25.61 ?  172 TRP A N   1 
ATOM   1180 C  CA  . TRP A 1 172 ? -45.544 10.372  -2.052  1.00 25.69 ?  172 TRP A CA  1 
ATOM   1181 C  C   . TRP A 1 172 ? -44.425 9.360   -1.807  1.00 22.26 ?  172 TRP A C   1 
ATOM   1182 O  O   . TRP A 1 172 ? -43.271 9.636   -2.145  1.00 23.93 ?  172 TRP A O   1 
ATOM   1183 C  CB  . TRP A 1 172 ? -45.719 11.310  -0.853  1.00 23.77 ?  172 TRP A CB  1 
ATOM   1184 C  CG  . TRP A 1 172 ? -45.939 10.619  0.470   1.00 23.53 ?  172 TRP A CG  1 
ATOM   1185 C  CD1 . TRP A 1 172 ? -47.143 10.269  1.021   1.00 24.59 ?  172 TRP A CD1 1 
ATOM   1186 C  CD2 . TRP A 1 172 ? -44.935 10.223  1.417   1.00 21.51 ?  172 TRP A CD2 1 
ATOM   1187 N  NE1 . TRP A 1 172 ? -46.946 9.679   2.239   1.00 22.74 ?  172 TRP A NE1 1 
ATOM   1188 C  CE2 . TRP A 1 172 ? -45.602 9.638   2.509   1.00 23.94 ?  172 TRP A CE2 1 
ATOM   1189 C  CE3 . TRP A 1 172 ? -43.537 10.298  1.439   1.00 22.42 ?  172 TRP A CE3 1 
ATOM   1190 C  CZ2 . TRP A 1 172 ? -44.924 9.121   3.607   1.00 23.27 ?  172 TRP A CZ2 1 
ATOM   1191 C  CZ3 . TRP A 1 172 ? -42.864 9.796   2.541   1.00 22.34 ?  172 TRP A CZ3 1 
ATOM   1192 C  CH2 . TRP A 1 172 ? -43.557 9.208   3.606   1.00 23.61 ?  172 TRP A CH2 1 
ATOM   1193 N  N   . ARG A 1 173 ? -44.731 8.189   -1.239  1.00 22.34 ?  173 ARG A N   1 
ATOM   1194 C  CA  . ARG A 1 173 ? -43.686 7.180   -1.044  1.00 22.28 ?  173 ARG A CA  1 
ATOM   1195 C  C   . ARG A 1 173 ? -43.128 6.707   -2.383  1.00 20.13 ?  173 ARG A C   1 
ATOM   1196 O  O   . ARG A 1 173 ? -41.907 6.610   -2.563  1.00 20.96 ?  173 ARG A O   1 
ATOM   1197 C  CB  . ARG A 1 173 ? -44.226 5.998   -0.235  1.00 23.56 ?  173 ARG A CB  1 
ATOM   1198 C  CG  . ARG A 1 173 ? -44.772 6.369   1.133   1.00 23.73 ?  173 ARG A CG  1 
ATOM   1199 C  CD  . ARG A 1 173 ? -44.774 5.177   2.072   1.00 22.99 ?  173 ARG A CD  1 
ATOM   1200 N  NE  . ARG A 1 173 ? -44.900 5.602   3.461   1.00 27.29 ?  173 ARG A NE  1 
ATOM   1201 C  CZ  . ARG A 1 173 ? -43.872 5.723   4.287   1.00 27.71 ?  173 ARG A CZ  1 
ATOM   1202 N  NH1 . ARG A 1 173 ? -42.633 5.484   3.886   1.00 24.09 ?  173 ARG A NH1 1 
ATOM   1203 N  NH2 . ARG A 1 173 ? -44.089 6.102   5.543   1.00 26.89 ?  173 ARG A NH2 1 
ATOM   1204 N  N   . ARG A 1 174 ? -44.013 6.431   -3.347  1.00 20.87 ?  174 ARG A N   1 
ATOM   1205 C  CA  . ARG A 1 174 ? -43.571 6.078   -4.698  1.00 23.13 ?  174 ARG A CA  1 
ATOM   1206 C  C   . ARG A 1 174 ? -42.702 7.182   -5.294  1.00 24.11 ?  174 ARG A C   1 
ATOM   1207 O  O   . ARG A 1 174 ? -41.637 6.914   -5.864  1.00 24.55 ?  174 ARG A O   1 
ATOM   1208 C  CB  . ARG A 1 174 ? -44.795 5.800   -5.587  1.00 26.79 ?  174 ARG A CB  1 
ATOM   1209 N  N   . LEU A 1 175 ? -43.134 8.442   -5.157  1.00 21.72 ?  175 LEU A N   1 
ATOM   1210 C  CA  . LEU A 1 175 ? -42.371 9.549   -5.741  1.00 21.27 ?  175 LEU A CA  1 
ATOM   1211 C  C   . LEU A 1 175 ? -41.018 9.719   -5.053  1.00 19.11 ?  175 LEU A C   1 
ATOM   1212 O  O   . LEU A 1 175 ? -39.987 9.883   -5.715  1.00 18.01 ?  175 LEU A O   1 
ATOM   1213 C  CB  . LEU A 1 175 ? -43.173 10.850  -5.667  1.00 22.21 ?  175 LEU A CB  1 
ATOM   1214 C  CG  . LEU A 1 175 ? -44.402 10.918  -6.582  1.00 25.69 ?  175 LEU A CG  1 
ATOM   1215 C  CD1 . LEU A 1 175 ? -45.299 12.098  -6.219  1.00 27.12 ?  175 LEU A CD1 1 
ATOM   1216 C  CD2 . LEU A 1 175 ? -43.983 10.985  -8.043  1.00 22.48 ?  175 LEU A CD2 1 
ATOM   1217 N  N   . MET A 1 176 ? -41.001 9.673   -3.724  1.00 20.75 ?  176 MET A N   1 
ATOM   1218 C  CA  . MET A 1 176 ? -39.740 9.733   -2.993  1.00 18.84 ?  176 MET A CA  1 
ATOM   1219 C  C   . MET A 1 176 ? -38.834 8.551   -3.346  1.00 21.77 ?  176 MET A C   1 
ATOM   1220 O  O   . MET A 1 176 ? -37.599 8.680   -3.362  1.00 17.54 ?  176 MET A O   1 
ATOM   1221 C  CB  . MET A 1 176 ? -40.053 9.739   -1.508  1.00 19.32 ?  176 MET A CB  1 
ATOM   1222 C  CG  . MET A 1 176 ? -40.524 11.088  -0.978  1.00 20.34 ?  176 MET A CG  1 
ATOM   1223 S  SD  . MET A 1 176 ? -40.024 12.605  -1.824  1.00 23.94 ?  176 MET A SD  1 
ATOM   1224 C  CE  . MET A 1 176 ? -38.550 12.868  -0.877  1.00 20.08 ?  176 MET A CE  1 
ATOM   1225 N  N   . SER A 1 177 ? -39.427 7.396   -3.645  1.00 19.14 ?  177 SER A N   1 
ATOM   1226 C  CA  . SER A 1 177 ? -38.625 6.243   -4.034  1.00 21.16 ?  177 SER A CA  1 
ATOM   1227 C  C   . SER A 1 177 ? -38.033 6.419   -5.430  1.00 17.74 ?  177 SER A C   1 
ATOM   1228 O  O   . SER A 1 177 ? -36.949 5.905   -5.706  1.00 19.52 ?  177 SER A O   1 
ATOM   1229 C  CB  . SER A 1 177 ? -39.466 4.961   -3.969  1.00 25.14 ?  177 SER A CB  1 
ATOM   1230 O  OG  . SER A 1 177 ? -38.696 3.839   -4.411  1.00 24.52 ?  177 SER A OG  1 
ATOM   1231 N  N   . GLY A 1 178 ? -38.726 7.135   -6.325  1.00 21.61 ?  178 GLY A N   1 
ATOM   1232 C  CA  . GLY A 1 178 ? -38.111 7.497   -7.597  1.00 20.57 ?  178 GLY A CA  1 
ATOM   1233 C  C   . GLY A 1 178 ? -36.859 8.339   -7.403  1.00 18.44 ?  178 GLY A C   1 
ATOM   1234 O  O   . GLY A 1 178 ? -35.879 8.205   -8.145  1.00 19.69 ?  178 GLY A O   1 
ATOM   1235 N  N   . ILE A 1 179 ? -36.875 9.207   -6.391  1.00 18.09 ?  179 ILE A N   1 
ATOM   1236 C  CA  . ILE A 1 179 ? -35.695 9.990   -6.024  1.00 18.54 ?  179 ILE A CA  1 
ATOM   1237 C  C   . ILE A 1 179 ? -34.549 9.069   -5.595  1.00 16.17 ?  179 ILE A C   1 
ATOM   1238 O  O   . ILE A 1 179 ? -33.375 9.332   -5.889  1.00 16.58 ?  179 ILE A O   1 
ATOM   1239 C  CB  . ILE A 1 179 ? -36.087 11.008  -4.925  1.00 14.72 ?  179 ILE A CB  1 
ATOM   1240 C  CG1 . ILE A 1 179 ? -36.779 12.244  -5.552  1.00 19.41 ?  179 ILE A CG1 1 
ATOM   1241 C  CG2 . ILE A 1 179 ? -34.914 11.399  -4.081  1.00 18.15 ?  179 ILE A CG2 1 
ATOM   1242 C  CD1 . ILE A 1 179 ? -37.547 13.113  -4.558  1.00 19.74 ?  179 ILE A CD1 1 
ATOM   1243 N  N   . ASP A 1 180 ? -34.869 7.960   -4.925  1.00 17.44 ?  180 ASP A N   1 
ATOM   1244 C  CA  . ASP A 1 180 ? -33.830 7.041   -4.456  1.00 16.15 ?  180 ASP A CA  1 
ATOM   1245 C  C   . ASP A 1 180 ? -33.026 6.434   -5.607  1.00 21.30 ?  180 ASP A C   1 
ATOM   1246 O  O   . ASP A 1 180 ? -31.906 5.944   -5.387  1.00 21.34 ?  180 ASP A O   1 
ATOM   1247 C  CB  . ASP A 1 180 ? -34.471 5.942   -3.613  1.00 14.44 ?  180 ASP A CB  1 
ATOM   1248 C  CG  . ASP A 1 180 ? -34.893 6.438   -2.234  1.00 20.10 ?  180 ASP A CG  1 
ATOM   1249 O  OD1 . ASP A 1 180 ? -34.380 7.488   -1.782  1.00 20.35 ?  180 ASP A OD1 1 
ATOM   1250 O  OD2 . ASP A 1 180 ? -35.727 5.771   -1.592  1.00 22.89 ?  180 ASP A OD2 1 
ATOM   1251 N  N   . VAL A 1 181 ? -33.579 6.431   -6.816  1.00 18.41 ?  181 VAL A N   1 
ATOM   1252 C  CA  . VAL A 1 181 ? -32.876 5.941   -7.991  1.00 17.85 ?  181 VAL A CA  1 
ATOM   1253 C  C   . VAL A 1 181 ? -32.348 7.088   -8.839  1.00 16.78 ?  181 VAL A C   1 
ATOM   1254 O  O   . VAL A 1 181 ? -31.226 7.021   -9.344  1.00 15.34 ?  181 VAL A O   1 
ATOM   1255 C  CB  . VAL A 1 181 ? -33.784 5.009   -8.829  1.00 21.47 ?  181 VAL A CB  1 
ATOM   1256 C  CG1 . VAL A 1 181 ? -33.123 4.682   -10.176 1.00 17.87 ?  181 VAL A CG1 1 
ATOM   1257 C  CG2 . VAL A 1 181 ? -34.115 3.710   -8.065  1.00 21.08 ?  181 VAL A CG2 1 
ATOM   1258 N  N   . ALA A 1 182 ? -33.133 8.164   -8.971  1.00 17.17 ?  182 ALA A N   1 
ATOM   1259 C  CA  . ALA A 1 182 ? -32.749 9.254   -9.870  1.00 15.46 ?  182 ALA A CA  1 
ATOM   1260 C  C   . ALA A 1 182 ? -31.425 9.890   -9.477  1.00 15.33 ?  182 ALA A C   1 
ATOM   1261 O  O   . ALA A 1 182 ? -30.665 10.311  -10.354 1.00 19.53 ?  182 ALA A O   1 
ATOM   1262 C  CB  . ALA A 1 182 ? -33.843 10.329  -9.906  1.00 14.47 ?  182 ALA A CB  1 
ATOM   1263 N  N   . PHE A 1 183 ? -31.135 9.980   -8.174  1.00 16.47 ?  183 PHE A N   1 
ATOM   1264 C  CA  . PHE A 1 183 ? -30.008 10.757  -7.674  1.00 17.45 ?  183 PHE A CA  1 
ATOM   1265 C  C   . PHE A 1 183 ? -28.830 9.878   -7.265  1.00 17.96 ?  183 PHE A C   1 
ATOM   1266 O  O   . PHE A 1 183 ? -27.945 10.339  -6.531  1.00 16.69 ?  183 PHE A O   1 
ATOM   1267 C  CB  . PHE A 1 183 ? -30.475 11.658  -6.520  1.00 16.12 ?  183 PHE A CB  1 
ATOM   1268 C  CG  . PHE A 1 183 ? -31.335 12.812  -6.991  1.00 19.18 ?  183 PHE A CG  1 
ATOM   1269 C  CD1 . PHE A 1 183 ? -32.704 12.637  -7.196  1.00 17.49 ?  183 PHE A CD1 1 
ATOM   1270 C  CD2 . PHE A 1 183 ? -30.770 14.047  -7.291  1.00 19.53 ?  183 PHE A CD2 1 
ATOM   1271 C  CE1 . PHE A 1 183 ? -33.506 13.697  -7.652  1.00 20.30 ?  183 PHE A CE1 1 
ATOM   1272 C  CE2 . PHE A 1 183 ? -31.558 15.101  -7.758  1.00 19.64 ?  183 PHE A CE2 1 
ATOM   1273 C  CZ  . PHE A 1 183 ? -32.927 14.925  -7.938  1.00 18.55 ?  183 PHE A CZ  1 
ATOM   1274 N  N   . ILE A 1 184 ? -28.812 8.625   -7.738  1.00 17.74 ?  184 ILE A N   1 
ATOM   1275 C  CA  . ILE A 1 184 ? -27.690 7.712   -7.542  1.00 18.86 ?  184 ILE A CA  1 
ATOM   1276 C  C   . ILE A 1 184 ? -26.472 8.204   -8.320  1.00 18.27 ?  184 ILE A C   1 
ATOM   1277 O  O   . ILE A 1 184 ? -26.584 8.678   -9.456  1.00 17.75 ?  184 ILE A O   1 
ATOM   1278 C  CB  . ILE A 1 184 ? -28.092 6.291   -7.990  1.00 16.16 ?  184 ILE A CB  1 
ATOM   1279 C  CG1 . ILE A 1 184 ? -28.989 5.610   -6.944  1.00 18.32 ?  184 ILE A CG1 1 
ATOM   1280 C  CG2 . ILE A 1 184 ? -26.859 5.422   -8.246  1.00 16.57 ?  184 ILE A CG2 1 
ATOM   1281 C  CD1 . ILE A 1 184 ? -29.493 4.203   -7.394  1.00 21.45 ?  184 ILE A CD1 1 
ATOM   1282 N  N   . THR A 1 185 ? -25.296 8.099   -7.709  1.00 17.68 ?  185 THR A N   1 
ATOM   1283 C  CA  . THR A 1 185 ? -24.034 8.363   -8.389  1.00 17.57 ?  185 THR A CA  1 
ATOM   1284 C  C   . THR A 1 185 ? -23.409 7.022   -8.750  1.00 17.98 ?  185 THR A C   1 
ATOM   1285 O  O   . THR A 1 185 ? -23.073 6.243   -7.860  1.00 17.94 ?  185 THR A O   1 
ATOM   1286 C  CB  . THR A 1 185 ? -23.080 9.165   -7.505  1.00 17.53 ?  185 THR A CB  1 
ATOM   1287 O  OG1 . THR A 1 185 ? -22.806 8.401   -6.315  1.00 20.11 ?  185 THR A OG1 1 
ATOM   1288 C  CG2 . THR A 1 185 ? -23.703 10.520  -7.120  1.00 17.64 ?  185 THR A CG2 1 
ATOM   1289 N  N   . SER A 1 186 ? -23.273 6.751   -10.050 1.00 18.46 ?  186 SER A N   1 
ATOM   1290 C  CA  . SER A 1 186 ? -22.743 5.489   -10.560 1.00 20.61 ?  186 SER A CA  1 
ATOM   1291 C  C   . SER A 1 186 ? -21.519 5.731   -11.436 1.00 19.77 ?  186 SER A C   1 
ATOM   1292 O  O   . SER A 1 186 ? -21.506 6.690   -12.212 1.00 22.19 ?  186 SER A O   1 
ATOM   1293 C  CB  . SER A 1 186 ? -23.804 4.747   -11.390 1.00 20.60 ?  186 SER A CB  1 
ATOM   1294 O  OG  . SER A 1 186 ? -23.340 3.460   -11.765 1.00 24.07 ?  186 SER A OG  1 
ATOM   1295 N  N   . PRO A 1 187 ? -20.489 4.877   -11.343 1.00 22.28 ?  187 PRO A N   1 
ATOM   1296 C  CA  . PRO A 1 187 ? -19.351 4.971   -12.277 1.00 21.87 ?  187 PRO A CA  1 
ATOM   1297 C  C   . PRO A 1 187 ? -19.753 4.935   -13.739 1.00 24.34 ?  187 PRO A C   1 
ATOM   1298 O  O   . PRO A 1 187 ? -19.162 5.649   -14.559 1.00 23.36 ?  187 PRO A O   1 
ATOM   1299 C  CB  . PRO A 1 187 ? -18.500 3.739   -11.918 1.00 21.66 ?  187 PRO A CB  1 
ATOM   1300 C  CG  . PRO A 1 187 ? -18.878 3.430   -10.482 1.00 23.69 ?  187 PRO A CG  1 
ATOM   1301 C  CD  . PRO A 1 187 ? -20.332 3.767   -10.381 1.00 25.09 ?  187 PRO A CD  1 
ATOM   1302 N  N   . ARG A 1 188 ? -20.751 4.119   -14.082 1.00 23.40 ?  188 ARG A N   1 
ATOM   1303 C  CA  . ARG A 1 188 ? -21.196 3.947   -15.459 1.00 24.00 ?  188 ARG A CA  1 
ATOM   1304 C  C   . ARG A 1 188 ? -22.710 3.992   -15.480 1.00 22.75 ?  188 ARG A C   1 
ATOM   1305 O  O   . ARG A 1 188 ? -23.366 3.798   -14.450 1.00 19.20 ?  188 ARG A O   1 
ATOM   1306 C  CB  . ARG A 1 188 ? -20.738 2.614   -16.074 1.00 25.63 ?  188 ARG A CB  1 
ATOM   1307 C  CG  . ARG A 1 188 ? -19.246 2.361   -16.037 1.00 28.45 ?  188 ARG A CG  1 
ATOM   1308 C  CD  . ARG A 1 188 ? -18.602 2.823   -17.322 1.00 31.43 ?  188 ARG A CD  1 
ATOM   1309 N  NE  . ARG A 1 188 ? -17.951 4.103   -17.096 1.00 41.54 ?  188 ARG A NE  1 
ATOM   1310 C  CZ  . ARG A 1 188 ? -16.685 4.238   -16.724 1.00 43.74 ?  188 ARG A CZ  1 
ATOM   1311 N  NH1 . ARG A 1 188 ? -15.866 3.198   -16.668 1.00 44.10 ?  188 ARG A NH1 1 
ATOM   1312 N  NH2 . ARG A 1 188 ? -16.231 5.446   -16.398 1.00 43.43 ?  188 ARG A NH2 1 
ATOM   1313 N  N   . THR A 1 189 ? -23.266 4.217   -16.670 1.00 20.28 ?  189 THR A N   1 
ATOM   1314 C  CA  . THR A 1 189 ? -24.717 4.241   -16.786 1.00 23.65 ?  189 THR A CA  1 
ATOM   1315 C  C   . THR A 1 189 ? -25.292 2.880   -16.420 1.00 21.33 ?  189 THR A C   1 
ATOM   1316 O  O   . THR A 1 189 ? -24.673 1.838   -16.655 1.00 25.29 ?  189 THR A O   1 
ATOM   1317 C  CB  . THR A 1 189 ? -25.156 4.659   -18.195 1.00 24.45 ?  189 THR A CB  1 
ATOM   1318 O  OG1 . THR A 1 189 ? -24.849 3.620   -19.128 1.00 32.24 ?  189 THR A OG1 1 
ATOM   1319 C  CG2 . THR A 1 189 ? -24.445 5.896   -18.600 1.00 28.69 ?  189 THR A CG2 1 
ATOM   1320 N  N   . PHE A 1 190 ? -26.475 2.932   -15.816 1.00 22.58 ?  190 PHE A N   1 
ATOM   1321 C  CA  . PHE A 1 190 ? -27.200 1.717   -15.369 1.00 23.56 ?  190 PHE A CA  1 
ATOM   1322 C  C   . PHE A 1 190 ? -28.610 1.737   -15.959 1.00 23.93 ?  190 PHE A C   1 
ATOM   1323 O  O   . PHE A 1 190 ? -29.196 2.817   -16.084 1.00 21.88 ?  190 PHE A O   1 
ATOM   1324 C  CB  . PHE A 1 190 ? -27.201 1.638   -13.841 1.00 21.06 ?  190 PHE A CB  1 
ATOM   1325 C  CG  . PHE A 1 190 ? -27.807 2.792   -13.059 1.00 19.60 ?  190 PHE A CG  1 
ATOM   1326 C  CD1 . PHE A 1 190 ? -27.058 3.921   -12.758 1.00 19.54 ?  190 PHE A CD1 1 
ATOM   1327 C  CD2 . PHE A 1 190 ? -29.110 2.722   -12.587 1.00 23.18 ?  190 PHE A CD2 1 
ATOM   1328 C  CE1 . PHE A 1 190 ? -27.608 4.960   -12.032 1.00 17.44 ?  190 PHE A CE1 1 
ATOM   1329 C  CE2 . PHE A 1 190 ? -29.654 3.763   -11.860 1.00 21.49 ?  190 PHE A CE2 1 
ATOM   1330 C  CZ  . PHE A 1 190 ? -28.903 4.879   -11.585 1.00 18.04 ?  190 PHE A CZ  1 
ATOM   1331 N  N   . GLU A 1 191 ? -29.139 0.564   -16.290 1.00 21.18 ?  191 GLU A N   1 
ATOM   1332 C  CA  . GLU A 1 191 ? -30.472 0.442   -16.940 1.00 22.84 ?  191 GLU A CA  1 
ATOM   1333 C  C   . GLU A 1 191 ? -31.597 1.142   -16.159 1.00 22.75 ?  191 GLU A C   1 
ATOM   1334 O  O   . GLU A 1 191 ? -32.496 1.689   -16.791 1.00 24.49 ?  191 GLU A O   1 
ATOM   1335 C  CB  . GLU A 1 191 ? -30.796 -1.043  -17.070 1.00 23.77 ?  191 GLU A CB  1 
ATOM   1336 C  CG  . GLU A 1 191 ? -31.832 -1.353  -18.143 1.00 25.59 ?  191 GLU A CG  1 
ATOM   1337 C  CD  . GLU A 1 191 ? -32.331 -2.785  -18.115 1.00 23.42 ?  191 GLU A CD  1 
ATOM   1338 O  OE1 . GLU A 1 191 ? -31.718 -3.622  -17.429 1.00 22.26 ?  191 GLU A OE1 1 
ATOM   1339 O  OE2 . GLU A 1 191 ? -33.338 -3.058  -18.784 1.00 24.51 ?  191 GLU A OE2 1 
ATOM   1340 N  N   . GLY A 1 192 ? -31.536 1.129   -14.838 1.00 18.78 ?  192 GLY A N   1 
ATOM   1341 C  CA  . GLY A 1 192 ? -32.650 1.683   -14.053 1.00 34.34 ?  192 GLY A CA  1 
ATOM   1342 C  C   . GLY A 1 192 ? -32.889 3.164   -14.263 1.00 22.76 ?  192 GLY A C   1 
ATOM   1343 O  O   . GLY A 1 192 ? -34.042 3.556   -14.152 1.00 22.65 ?  192 GLY A O   1 
ATOM   1344 N  N   . SER A 1 193 ? -31.854 3.930   -14.596 1.00 20.17 ?  193 SER A N   1 
ATOM   1345 C  CA  . SER A 1 193 ? -31.967 5.408   -14.641 1.00 22.63 ?  193 SER A CA  1 
ATOM   1346 C  C   . SER A 1 193 ? -33.046 5.833   -15.646 1.00 21.64 ?  193 SER A C   1 
ATOM   1347 O  O   . SER A 1 193 ? -33.979 6.541   -15.268 1.00 20.33 ?  193 SER A O   1 
ATOM   1348 C  CB  . SER A 1 193 ? -30.624 6.031   -14.908 1.00 20.96 ?  193 SER A CB  1 
ATOM   1349 O  OG  . SER A 1 193 ? -30.198 5.833   -16.244 1.00 29.05 ?  193 SER A OG  1 
ATOM   1350 N  N   . ALA A 1 194 ? -32.928 5.344   -16.865 1.00 20.68 ?  194 ALA A N   1 
ATOM   1351 C  CA  . ALA A 1 194 ? -33.881 5.763   -17.894 1.00 20.07 ?  194 ALA A CA  1 
ATOM   1352 C  C   . ALA A 1 194 ? -35.281 5.202   -17.640 1.00 22.32 ?  194 ALA A C   1 
ATOM   1353 O  O   . ALA A 1 194 ? -36.268 5.925   -17.808 1.00 20.71 ?  194 ALA A O   1 
ATOM   1354 C  CB  . ALA A 1 194 ? -33.387 5.356   -19.285 1.00 26.77 ?  194 ALA A CB  1 
ATOM   1355 N  N   . VAL A 1 195 ? -35.398 3.917   -17.254 1.00 19.39 ?  195 VAL A N   1 
ATOM   1356 C  CA  . VAL A 1 195 ? -36.705 3.366   -16.869 1.00 20.68 ?  195 VAL A CA  1 
ATOM   1357 C  C   . VAL A 1 195 ? -37.322 4.198   -15.751 1.00 22.80 ?  195 VAL A C   1 
ATOM   1358 O  O   . VAL A 1 195 ? -38.510 4.538   -15.780 1.00 18.91 ?  195 VAL A O   1 
ATOM   1359 C  CB  . VAL A 1 195 ? -36.593 1.889   -16.438 1.00 21.00 ?  195 VAL A CB  1 
ATOM   1360 C  CG1 . VAL A 1 195 ? -37.944 1.366   -16.009 1.00 22.19 ?  195 VAL A CG1 1 
ATOM   1361 C  CG2 . VAL A 1 195 ? -36.026 0.989   -17.557 1.00 21.00 ?  195 VAL A CG2 1 
ATOM   1362 N  N   . ASN A 1 196 ? -36.526 4.502   -14.728 1.00 20.93 ?  196 ASN A N   1 
ATOM   1363 C  CA  . ASN A 1 196 ? -37.018 5.303   -13.612 1.00 20.59 ?  196 ASN A CA  1 
ATOM   1364 C  C   . ASN A 1 196 ? -37.486 6.679   -14.078 1.00 20.66 ?  196 ASN A C   1 
ATOM   1365 O  O   . ASN A 1 196 ? -38.551 7.163   -13.661 1.00 23.00 ?  196 ASN A O   1 
ATOM   1366 C  CB  . ASN A 1 196 ? -35.916 5.443   -12.565 1.00 19.16 ?  196 ASN A CB  1 
ATOM   1367 C  CG  . ASN A 1 196 ? -36.422 6.030   -11.280 1.00 24.76 ?  196 ASN A CG  1 
ATOM   1368 O  OD1 . ASN A 1 196 ? -37.254 5.419   -10.603 1.00 23.74 ?  196 ASN A OD1 1 
ATOM   1369 N  ND2 . ASN A 1 196 ? -35.931 7.225   -10.931 1.00 17.07 ?  196 ASN A ND2 1 
ATOM   1370 N  N   . TRP A 1 197 ? -36.703 7.320   -14.945 1.00 18.68 ?  197 TRP A N   1 
ATOM   1371 C  CA  . TRP A 1 197 ? -37.041 8.667   -15.390 1.00 24.60 ?  197 TRP A CA  1 
ATOM   1372 C  C   . TRP A 1 197 ? -38.375 8.682   -16.132 1.00 23.91 ?  197 TRP A C   1 
ATOM   1373 O  O   . TRP A 1 197 ? -39.294 9.421   -15.768 1.00 24.10 ?  197 TRP A O   1 
ATOM   1374 C  CB  . TRP A 1 197 ? -35.922 9.221   -16.274 1.00 23.76 ?  197 TRP A CB  1 
ATOM   1375 C  CG  . TRP A 1 197 ? -36.313 10.522  -16.871 1.00 28.37 ?  197 TRP A CG  1 
ATOM   1376 C  CD1 . TRP A 1 197 ? -36.835 10.735  -18.117 1.00 30.13 ?  197 TRP A CD1 1 
ATOM   1377 C  CD2 . TRP A 1 197 ? -36.282 11.800  -16.223 1.00 26.48 ?  197 TRP A CD2 1 
ATOM   1378 N  NE1 . TRP A 1 197 ? -37.107 12.072  -18.289 1.00 30.66 ?  197 TRP A NE1 1 
ATOM   1379 C  CE2 . TRP A 1 197 ? -36.778 12.745  -17.141 1.00 27.14 ?  197 TRP A CE2 1 
ATOM   1380 C  CE3 . TRP A 1 197 ? -35.881 12.236  -14.955 1.00 28.54 ?  197 TRP A CE3 1 
ATOM   1381 C  CZ2 . TRP A 1 197 ? -36.882 14.098  -16.831 1.00 30.90 ?  197 TRP A CZ2 1 
ATOM   1382 C  CZ3 . TRP A 1 197 ? -35.980 13.588  -14.651 1.00 25.14 ?  197 TRP A CZ3 1 
ATOM   1383 C  CH2 . TRP A 1 197 ? -36.472 14.498  -15.585 1.00 28.33 ?  197 TRP A CH2 1 
ATOM   1384 N  N   . TYR A 1 198 ? -38.517 7.832   -17.154 1.00 26.80 ?  198 TYR A N   1 
ATOM   1385 C  CA  . TYR A 1 198 ? -39.752 7.823   -17.933 1.00 27.95 ?  198 TYR A CA  1 
ATOM   1386 C  C   . TYR A 1 198 ? -40.938 7.334   -17.115 1.00 22.56 ?  198 TYR A C   1 
ATOM   1387 O  O   . TYR A 1 198 ? -42.081 7.703   -17.406 1.00 26.08 ?  198 TYR A O   1 
ATOM   1388 C  CB  . TYR A 1 198 ? -39.554 6.986   -19.197 1.00 25.21 ?  198 TYR A CB  1 
ATOM   1389 C  CG  . TYR A 1 198 ? -38.578 7.658   -20.134 1.00 30.23 ?  198 TYR A CG  1 
ATOM   1390 C  CD1 . TYR A 1 198 ? -38.873 8.894   -20.702 1.00 31.51 ?  198 TYR A CD1 1 
ATOM   1391 C  CD2 . TYR A 1 198 ? -37.347 7.090   -20.411 1.00 34.36 ?  198 TYR A CD2 1 
ATOM   1392 C  CE1 . TYR A 1 198 ? -37.974 9.531   -21.543 1.00 34.78 ?  198 TYR A CE1 1 
ATOM   1393 C  CE2 . TYR A 1 198 ? -36.443 7.719   -21.251 1.00 35.47 ?  198 TYR A CE2 1 
ATOM   1394 C  CZ  . TYR A 1 198 ? -36.762 8.937   -21.811 1.00 37.89 ?  198 TYR A CZ  1 
ATOM   1395 O  OH  . TYR A 1 198 ? -35.856 9.559   -22.644 1.00 50.56 ?  198 TYR A OH  1 
ATOM   1396 N  N   . LYS A 1 199 ? -40.697 6.518   -16.090 1.00 22.97 ?  199 LYS A N   1 
ATOM   1397 C  CA  . LYS A 1 199 ? -41.787 6.124   -15.204 1.00 23.01 ?  199 LYS A CA  1 
ATOM   1398 C  C   . LYS A 1 199 ? -42.453 7.352   -14.577 1.00 22.74 ?  199 LYS A C   1 
ATOM   1399 O  O   . LYS A 1 199 ? -43.668 7.551   -14.694 1.00 22.78 ?  199 LYS A O   1 
ATOM   1400 C  CB  . LYS A 1 199 ? -41.262 5.168   -14.130 1.00 22.33 ?  199 LYS A CB  1 
ATOM   1401 C  CG  . LYS A 1 199 ? -42.242 4.897   -12.975 1.00 23.92 ?  199 LYS A CG  1 
ATOM   1402 C  CD  . LYS A 1 199 ? -41.601 3.966   -11.939 1.00 22.83 ?  199 LYS A CD  1 
ATOM   1403 C  CE  . LYS A 1 199 ? -42.449 3.852   -10.672 1.00 27.72 ?  199 LYS A CE  1 
ATOM   1404 N  NZ  . LYS A 1 199 ? -41.918 2.817   -9.725  1.00 21.44 ?  199 LYS A NZ  1 
ATOM   1405 N  N   . ASP A 1 200 ? -41.671 8.208   -13.934 1.00 23.18 ?  200 ASP A N   1 
ATOM   1406 C  CA  . ASP A 1 200 ? -42.279 9.352   -13.271 1.00 19.87 ?  200 ASP A CA  1 
ATOM   1407 C  C   . ASP A 1 200 ? -42.544 10.518  -14.212 1.00 20.52 ?  200 ASP A C   1 
ATOM   1408 O  O   . ASP A 1 200 ? -43.396 11.354  -13.902 1.00 22.65 ?  200 ASP A O   1 
ATOM   1409 C  CB  . ASP A 1 200 ? -41.407 9.772   -12.097 1.00 23.27 ?  200 ASP A CB  1 
ATOM   1410 C  CG  . ASP A 1 200 ? -41.588 8.850   -10.908 1.00 25.73 ?  200 ASP A CG  1 
ATOM   1411 O  OD1 . ASP A 1 200 ? -42.580 8.075   -10.915 1.00 23.86 ?  200 ASP A OD1 1 
ATOM   1412 O  OD2 . ASP A 1 200 ? -40.750 8.885   -9.984  1.00 22.85 ?  200 ASP A OD2 1 
ATOM   1413 N  N   . LEU A 1 201 ? -41.844 10.600  -15.348 1.00 22.67 ?  201 LEU A N   1 
ATOM   1414 C  CA  . LEU A 1 201 ? -42.288 11.508  -16.400 1.00 21.86 ?  201 LEU A CA  1 
ATOM   1415 C  C   . LEU A 1 201 ? -43.728 11.207  -16.787 1.00 25.93 ?  201 LEU A C   1 
ATOM   1416 O  O   . LEU A 1 201 ? -44.545 12.124  -16.938 1.00 25.90 ?  201 LEU A O   1 
ATOM   1417 C  CB  . LEU A 1 201 ? -41.394 11.394  -17.627 1.00 25.68 ?  201 LEU A CB  1 
ATOM   1418 C  CG  . LEU A 1 201 ? -41.557 12.450  -18.726 1.00 25.90 ?  201 LEU A CG  1 
ATOM   1419 C  CD1 . LEU A 1 201 ? -41.155 13.848  -18.236 1.00 22.35 ?  201 LEU A CD1 1 
ATOM   1420 C  CD2 . LEU A 1 201 ? -40.733 12.041  -19.942 1.00 31.46 ?  201 LEU A CD2 1 
ATOM   1421 N  N   . GLY A 1 202 ? -44.054 9.922   -16.946 1.00 23.18 ?  202 GLY A N   1 
ATOM   1422 C  CA  . GLY A 1 202 ? -45.411 9.559   -17.317 1.00 23.81 ?  202 GLY A CA  1 
ATOM   1423 C  C   . GLY A 1 202 ? -46.405 9.872   -16.216 1.00 25.48 ?  202 GLY A C   1 
ATOM   1424 O  O   . GLY A 1 202 ? -47.528 10.304  -16.490 1.00 27.78 ?  202 GLY A O   1 
ATOM   1425 N  N   . TYR A 1 203 ? -46.004 9.673   -14.958 1.00 22.54 ?  203 TYR A N   1 
ATOM   1426 C  CA  . TYR A 1 203 ? -46.841 10.091  -13.835 1.00 23.63 ?  203 TYR A CA  1 
ATOM   1427 C  C   . TYR A 1 203 ? -47.194 11.574  -13.940 1.00 25.62 ?  203 TYR A C   1 
ATOM   1428 O  O   . TYR A 1 203 ? -48.355 11.969  -13.767 1.00 26.68 ?  203 TYR A O   1 
ATOM   1429 C  CB  . TYR A 1 203 ? -46.123 9.796   -12.517 1.00 26.57 ?  203 TYR A CB  1 
ATOM   1430 C  CG  . TYR A 1 203 ? -46.965 10.019  -11.276 1.00 25.95 ?  203 TYR A CG  1 
ATOM   1431 C  CD1 . TYR A 1 203 ? -47.042 11.281  -10.677 1.00 29.55 ?  203 TYR A CD1 1 
ATOM   1432 C  CD2 . TYR A 1 203 ? -47.671 8.973   -10.698 1.00 24.21 ?  203 TYR A CD2 1 
ATOM   1433 C  CE1 . TYR A 1 203 ? -47.796 11.491  -9.535  1.00 25.50 ?  203 TYR A CE1 1 
ATOM   1434 C  CE2 . TYR A 1 203 ? -48.431 9.168   -9.552  1.00 27.57 ?  203 TYR A CE2 1 
ATOM   1435 C  CZ  . TYR A 1 203 ? -48.491 10.431  -8.978  1.00 31.18 ?  203 TYR A CZ  1 
ATOM   1436 O  OH  . TYR A 1 203 ? -49.258 10.634  -7.849  1.00 29.69 ?  203 TYR A OH  1 
ATOM   1437 N  N   . MET A 1 204 ? -46.199 12.410  -14.236 1.00 24.58 ?  204 MET A N   1 
ATOM   1438 C  CA  . MET A 1 204 ? -46.443 13.844  -14.308 1.00 24.30 ?  204 MET A CA  1 
ATOM   1439 C  C   . MET A 1 204 ? -47.298 14.189  -15.523 1.00 27.88 ?  204 MET A C   1 
ATOM   1440 O  O   . MET A 1 204 ? -48.176 15.055  -15.446 1.00 25.22 ?  204 MET A O   1 
ATOM   1441 C  CB  . MET A 1 204 ? -45.115 14.602  -14.358 1.00 25.40 ?  204 MET A CB  1 
ATOM   1442 C  CG  . MET A 1 204 ? -44.352 14.667  -13.031 1.00 25.22 ?  204 MET A CG  1 
ATOM   1443 S  SD  . MET A 1 204 ? -45.304 14.995  -11.544 1.00 24.37 ?  204 MET A SD  1 
ATOM   1444 C  CE  . MET A 1 204 ? -44.129 14.432  -10.316 1.00 29.06 ?  204 MET A CE  1 
ATOM   1445 N  N   . VAL A 1 205 ? -47.037 13.535  -16.662 1.00 23.08 ?  205 VAL A N   1 
ATOM   1446 C  CA  . VAL A 1 205 ? -47.893 13.687  -17.840 1.00 27.34 ?  205 VAL A CA  1 
ATOM   1447 C  C   . VAL A 1 205 ? -49.331 13.321  -17.501 1.00 26.35 ?  205 VAL A C   1 
ATOM   1448 O  O   . VAL A 1 205 ? -50.274 14.017  -17.897 1.00 30.28 ?  205 VAL A O   1 
ATOM   1449 C  CB  . VAL A 1 205 ? -47.357 12.831  -19.009 1.00 26.51 ?  205 VAL A CB  1 
ATOM   1450 C  CG1 . VAL A 1 205 ? -48.432 12.627  -20.069 1.00 31.45 ?  205 VAL A CG1 1 
ATOM   1451 C  CG2 . VAL A 1 205 ? -46.154 13.479  -19.633 1.00 25.32 ?  205 VAL A CG2 1 
ATOM   1452 N  N   . ASP A 1 206 ? -49.522 12.216  -16.774 1.00 25.10 ?  206 ASP A N   1 
ATOM   1453 C  CA  . ASP A 1 206 ? -50.869 11.794  -16.401 1.00 26.94 ?  206 ASP A CA  1 
ATOM   1454 C  C   . ASP A 1 206 ? -51.572 12.871  -15.587 1.00 31.28 ?  206 ASP A C   1 
ATOM   1455 O  O   . ASP A 1 206 ? -52.751 13.167  -15.822 1.00 36.88 ?  206 ASP A O   1 
ATOM   1456 C  CB  . ASP A 1 206 ? -50.817 10.487  -15.605 1.00 30.93 ?  206 ASP A CB  1 
ATOM   1457 C  CG  . ASP A 1 206 ? -50.443 9.273   -16.463 1.00 35.93 ?  206 ASP A CG  1 
ATOM   1458 O  OD1 . ASP A 1 206 ? -50.542 9.332   -17.708 1.00 33.57 ?  206 ASP A OD1 1 
ATOM   1459 O  OD2 . ASP A 1 206 ? -50.030 8.256   -15.876 1.00 40.15 ?  206 ASP A OD2 1 
ATOM   1460 N  N   . ARG A 1 207 ? -50.872 13.466  -14.616 1.00 29.10 ?  207 ARG A N   1 
ATOM   1461 C  CA  . ARG A 1 207 ? -51.497 14.518  -13.821 1.00 31.85 ?  207 ARG A CA  1 
ATOM   1462 C  C   . ARG A 1 207 ? -51.801 15.743  -14.674 1.00 32.45 ?  207 ARG A C   1 
ATOM   1463 O  O   . ARG A 1 207 ? -52.868 16.346  -14.539 1.00 32.97 ?  207 ARG A O   1 
ATOM   1464 C  CB  . ARG A 1 207 ? -50.612 14.909  -12.633 1.00 29.57 ?  207 ARG A CB  1 
ATOM   1465 C  CG  . ARG A 1 207 ? -50.042 13.752  -11.838 1.00 33.47 ?  207 ARG A CG  1 
ATOM   1466 C  CD  . ARG A 1 207 ? -51.021 13.229  -10.789 1.00 35.91 ?  207 ARG A CD  1 
ATOM   1467 N  NE  . ARG A 1 207 ? -51.916 12.196  -11.310 1.00 39.75 ?  207 ARG A NE  1 
ATOM   1468 C  CZ  . ARG A 1 207 ? -51.551 11.002  -11.776 1.00 42.71 ?  207 ARG A CZ  1 
ATOM   1469 N  NH1 . ARG A 1 207 ? -50.282 10.627  -11.830 1.00 36.53 ?  207 ARG A NH1 1 
ATOM   1470 N  NH2 . ARG A 1 207 ? -52.491 10.155  -12.196 1.00 45.31 ?  207 ARG A NH2 1 
ATOM   1471 N  N   . LEU A 1 208 ? -50.878 16.121  -15.559 1.00 31.06 ?  208 LEU A N   1 
ATOM   1472 C  CA  . LEU A 1 208 ? -51.076 17.318  -16.372 1.00 32.84 ?  208 LEU A CA  1 
ATOM   1473 C  C   . LEU A 1 208 ? -52.273 17.168  -17.305 1.00 36.71 ?  208 LEU A C   1 
ATOM   1474 O  O   . LEU A 1 208 ? -52.994 18.141  -17.558 1.00 38.87 ?  208 LEU A O   1 
ATOM   1475 C  CB  . LEU A 1 208 ? -49.800 17.619  -17.159 1.00 33.13 ?  208 LEU A CB  1 
ATOM   1476 C  CG  . LEU A 1 208 ? -49.781 18.694  -18.247 1.00 37.94 ?  208 LEU A CG  1 
ATOM   1477 C  CD1 . LEU A 1 208 ? -49.579 20.074  -17.661 1.00 34.89 ?  208 LEU A CD1 1 
ATOM   1478 C  CD2 . LEU A 1 208 ? -48.680 18.401  -19.239 1.00 34.88 ?  208 LEU A CD2 1 
ATOM   1479 N  N   . ASN A 1 209 ? -52.517 15.956  -17.809 1.00 31.46 ?  209 ASN A N   1 
ATOM   1480 C  CA  . ASN A 1 209 ? -53.569 15.712  -18.784 1.00 36.90 ?  209 ASN A CA  1 
ATOM   1481 C  C   . ASN A 1 209 ? -54.808 15.062  -18.174 1.00 39.70 ?  209 ASN A C   1 
ATOM   1482 O  O   . ASN A 1 209 ? -55.573 14.412  -18.893 1.00 43.44 ?  209 ASN A O   1 
ATOM   1483 C  CB  . ASN A 1 209 ? -53.044 14.841  -19.926 1.00 33.14 ?  209 ASN A CB  1 
ATOM   1484 C  CG  . ASN A 1 209 ? -52.026 15.556  -20.780 1.00 34.16 ?  209 ASN A CG  1 
ATOM   1485 O  OD1 . ASN A 1 209 ? -51.984 16.786  -20.825 1.00 33.20 ?  209 ASN A OD1 1 
ATOM   1486 N  ND2 . ASN A 1 209 ? -51.202 14.786  -21.475 1.00 35.03 ?  209 ASN A ND2 1 
ATOM   1487 N  N   . ALA A 1 210 ? -55.023 15.218  -16.873 1.00 40.33 ?  210 ALA A N   1 
ATOM   1488 C  CA  . ALA A 1 210 ? -56.211 14.653  -16.250 1.00 45.97 ?  210 ALA A CA  1 
ATOM   1489 C  C   . ALA A 1 210 ? -57.466 15.307  -16.823 1.00 48.08 ?  210 ALA A C   1 
ATOM   1490 O  O   . ALA A 1 210 ? -57.439 16.456  -17.278 1.00 50.41 ?  210 ALA A O   1 
ATOM   1491 C  CB  . ALA A 1 210 ? -56.148 14.832  -14.732 1.00 42.03 ?  210 ALA A CB  1 
ATOM   1492 N  N   . ASP A 1 211 ? -58.574 14.550  -16.824 1.00 49.54 ?  211 ASP A N   1 
ATOM   1493 C  CA  . ASP A 1 211 ? -59.816 15.066  -17.407 1.00 56.64 ?  211 ASP A CA  1 
ATOM   1494 C  C   . ASP A 1 211 ? -60.340 16.273  -16.641 1.00 58.19 ?  211 ASP A C   1 
ATOM   1495 O  O   . ASP A 1 211 ? -60.544 17.332  -17.261 1.00 65.40 ?  211 ASP A O   1 
ATOM   1496 C  CB  . ASP A 1 211 ? -60.867 13.956  -17.523 1.00 58.62 ?  211 ASP A CB  1 
ATOM   1497 C  CG  . ASP A 1 211 ? -62.065 14.371  -18.379 1.00 60.39 ?  211 ASP A CG  1 
ATOM   1498 O  OD1 . ASP A 1 211 ? -62.279 15.588  -18.587 1.00 55.22 ?  211 ASP A OD1 1 
ATOM   1499 O  OD2 . ASP A 1 211 ? -62.802 13.474  -18.843 1.00 64.55 ?  211 ASP A OD2 1 
ATOM   1500 N  N   . PRO A 1 212 ? -60.574 16.208  -15.328 1.00 54.36 ?  212 PRO A N   1 
ATOM   1501 C  CA  . PRO A 1 212 ? -60.628 17.476  -14.597 1.00 54.34 ?  212 PRO A CA  1 
ATOM   1502 C  C   . PRO A 1 212 ? -59.280 18.176  -14.615 1.00 50.65 ?  212 PRO A C   1 
ATOM   1503 O  O   . PRO A 1 212 ? -58.487 18.033  -13.681 1.00 51.26 ?  212 PRO A O   1 
ATOM   1504 C  CB  . PRO A 1 212 ? -61.047 17.087  -13.175 1.00 51.22 ?  212 PRO A CB  1 
ATOM   1505 C  CG  . PRO A 1 212 ? -60.925 15.607  -13.087 1.00 55.45 ?  212 PRO A CG  1 
ATOM   1506 C  CD  . PRO A 1 212 ? -60.625 15.034  -14.437 1.00 52.31 ?  212 PRO A CD  1 
ATOM   1507 N  N   . GLU A 1 213 ? -58.993 18.867  -15.714 1.00 50.13 ?  213 GLU A N   1 
ATOM   1508 C  CA  . GLU A 1 213 ? -57.681 19.470  -15.911 1.00 46.42 ?  213 GLU A CA  1 
ATOM   1509 C  C   . GLU A 1 213 ? -57.137 20.147  -14.649 1.00 46.57 ?  213 GLU A C   1 
ATOM   1510 O  O   . GLU A 1 213 ? -57.900 20.773  -13.902 1.00 48.44 ?  213 GLU A O   1 
ATOM   1511 C  CB  . GLU A 1 213 ? -57.749 20.458  -17.081 1.00 52.76 ?  213 GLU A CB  1 
ATOM   1512 C  CG  . GLU A 1 213 ? -56.442 21.132  -17.475 1.00 50.92 ?  213 GLU A CG  1 
ATOM   1513 C  CD  . GLU A 1 213 ? -55.403 20.156  -18.013 1.00 55.12 ?  213 GLU A CD  1 
ATOM   1514 O  OE1 . GLU A 1 213 ? -55.779 18.998  -18.312 1.00 50.16 ?  213 GLU A OE1 1 
ATOM   1515 O  OE2 . GLU A 1 213 ? -54.212 20.532  -18.104 1.00 48.94 ?  213 GLU A OE2 1 
ATOM   1516 N  N   . PRO A 1 214 ? -55.844 20.016  -14.356 1.00 44.21 ?  214 PRO A N   1 
ATOM   1517 C  CA  . PRO A 1 214 ? -55.322 20.586  -13.105 1.00 42.78 ?  214 PRO A CA  1 
ATOM   1518 C  C   . PRO A 1 214 ? -55.493 22.095  -13.053 1.00 42.49 ?  214 PRO A C   1 
ATOM   1519 O  O   . PRO A 1 214 ? -55.168 22.816  -13.999 1.00 37.81 ?  214 PRO A O   1 
ATOM   1520 C  CB  . PRO A 1 214 ? -53.836 20.202  -13.110 1.00 44.40 ?  214 PRO A CB  1 
ATOM   1521 C  CG  . PRO A 1 214 ? -53.605 19.341  -14.284 1.00 41.54 ?  214 PRO A CG  1 
ATOM   1522 C  CD  . PRO A 1 214 ? -54.806 19.352  -15.167 1.00 46.19 ?  214 PRO A CD  1 
ATOM   1523 N  N   . THR A 1 215 ? -55.880 22.584  -11.873 1.00 39.69 ?  215 THR A N   1 
ATOM   1524 C  CA  . THR A 1 215 ? -56.138 24.025  -11.691 1.00 37.54 ?  215 THR A CA  1 
ATOM   1525 C  C   . THR A 1 215 ? -55.170 24.645  -10.722 1.00 46.34 ?  215 THR A C   1 
ATOM   1526 O  O   . THR A 1 215 ? -55.089 25.879  -10.689 1.00 53.59 ?  215 THR A O   1 
ATOM   1527 C  CB  . THR A 1 215 ? -57.555 24.216  -11.160 1.00 45.03 ?  215 THR A CB  1 
ATOM   1528 O  OG1 . THR A 1 215 ? -57.498 23.930  -9.768  1.00 44.84 ?  215 THR A OG1 1 
ATOM   1529 C  CG2 . THR A 1 215 ? -58.555 23.276  -11.803 1.00 44.93 ?  215 THR A CG2 1 
ATOM   1530 N  N   . GLU A 1 216 ? -54.479 23.847  -9.928  1.00 44.44 ?  216 GLU A N   1 
ATOM   1531 C  CA  . GLU A 1 216 ? -53.638 24.453  -8.875  1.00 40.32 ?  216 GLU A CA  1 
ATOM   1532 C  C   . GLU A 1 216 ? -52.158 24.209  -9.143  1.00 37.07 ?  216 GLU A C   1 
ATOM   1533 O  O   . GLU A 1 216 ? -51.809 23.235  -9.826  1.00 35.03 ?  216 GLU A O   1 
ATOM   1534 C  CB  . GLU A 1 216 ? -53.941 23.854  -7.502  1.00 45.19 ?  216 GLU A CB  1 
ATOM   1535 C  CG  . GLU A 1 216 ? -55.377 24.072  -7.042  1.00 47.08 ?  216 GLU A CG  1 
ATOM   1536 C  CD  . GLU A 1 216 ? -55.670 25.544  -6.839  1.00 52.35 ?  216 GLU A CD  1 
ATOM   1537 O  OE1 . GLU A 1 216 ? -56.445 26.114  -7.635  1.00 61.51 ?  216 GLU A OE1 1 
ATOM   1538 O  OE2 . GLU A 1 216 ? -55.107 26.118  -5.889  1.00 56.44 ?  216 GLU A OE2 1 
ATOM   1539 N  N   . GLY A 1 217 ? -51.325 25.098  -8.630  1.00 31.93 ?  217 GLY A N   1 
ATOM   1540 C  CA  . GLY A 1 217 ? -49.890 24.845  -8.721  1.00 27.21 ?  217 GLY A CA  1 
ATOM   1541 C  C   . GLY A 1 217 ? -49.232 25.013  -10.064 1.00 29.71 ?  217 GLY A C   1 
ATOM   1542 O  O   . GLY A 1 217 ? -49.783 25.724  -10.913 1.00 28.68 ?  217 GLY A O   1 
ATOM   1543 N  N   . LEU A 1 218 ? -48.192 24.239  -10.303 1.00 23.82 ?  218 LEU A N   1 
ATOM   1544 C  CA  . LEU A 1 218 ? -47.280 24.452  -11.420 1.00 27.61 ?  218 LEU A CA  1 
ATOM   1545 C  C   . LEU A 1 218 ? -48.035 23.828  -12.581 1.00 26.00 ?  218 LEU A C   1 
ATOM   1546 O  O   . LEU A 1 218 ? -48.049 24.380  -13.687 1.00 27.57 ?  218 LEU A O   1 
ATOM   1547 C  CB  . LEU A 1 218 ? -45.904 23.799  -11.269 1.00 26.36 ?  218 LEU A CB  1 
ATOM   1548 C  CG  . LEU A 1 218 ? -44.961 24.105  -12.447 1.00 24.92 ?  218 LEU A CG  1 
ATOM   1549 C  CD1 . LEU A 1 218 ? -44.311 25.472  -12.291 1.00 26.85 ?  218 LEU A CD1 1 
ATOM   1550 C  CD2 . LEU A 1 218 ? -43.906 23.029  -12.592 1.00 25.16 ?  218 LEU A CD2 1 
ATOM   1551 N  N   . LEU A 1 219 ? -48.660 22.670  -12.355 1.00 24.94 ?  219 LEU A N   1 
ATOM   1552 C  CA  . LEU A 1 219 ? -49.397 22.016  -13.434 1.00 28.61 ?  219 LEU A CA  1 
ATOM   1553 C  C   . LEU A 1 219 ? -50.655 22.794  -13.807 1.00 32.69 ?  219 LEU A C   1 
ATOM   1554 O  O   . LEU A 1 219 ? -51.086 22.750  -14.966 1.00 37.50 ?  219 LEU A O   1 
ATOM   1555 C  CB  . LEU A 1 219 ? -49.755 20.586  -13.037 1.00 28.44 ?  219 LEU A CB  1 
ATOM   1556 C  CG  . LEU A 1 219 ? -48.570 19.624  -12.855 1.00 27.53 ?  219 LEU A CG  1 
ATOM   1557 C  CD1 . LEU A 1 219 ? -49.069 18.211  -12.757 1.00 23.58 ?  219 LEU A CD1 1 
ATOM   1558 C  CD2 . LEU A 1 219 ? -47.543 19.767  -13.988 1.00 26.84 ?  219 LEU A CD2 1 
ATOM   1559 N  N   . GLY A 1 220 ? -51.261 23.494  -12.843 1.00 29.36 ?  220 GLY A N   1 
ATOM   1560 C  CA  . GLY A 1 220 ? -52.340 24.410  -13.174 1.00 33.98 ?  220 GLY A CA  1 
ATOM   1561 C  C   . GLY A 1 220 ? -51.859 25.565  -14.034 1.00 36.57 ?  220 GLY A C   1 
ATOM   1562 O  O   . GLY A 1 220 ? -52.474 25.898  -15.051 1.00 38.83 ?  220 GLY A O   1 
ATOM   1563 N  N   . ARG A 1 221 ? -50.735 26.179  -13.649 1.00 30.14 ?  221 ARG A N   1 
ATOM   1564 C  CA  . ARG A 1 221 ? -50.153 27.226  -14.483 1.00 33.70 ?  221 ARG A CA  1 
ATOM   1565 C  C   . ARG A 1 221 ? -49.744 26.686  -15.848 1.00 35.76 ?  221 ARG A C   1 
ATOM   1566 O  O   . ARG A 1 221 ? -49.862 27.398  -16.850 1.00 38.97 ?  221 ARG A O   1 
ATOM   1567 C  CB  . ARG A 1 221 ? -48.956 27.872  -13.782 1.00 28.30 ?  221 ARG A CB  1 
ATOM   1568 C  CG  . ARG A 1 221 ? -49.348 28.917  -12.759 1.00 28.11 ?  221 ARG A CG  1 
ATOM   1569 C  CD  . ARG A 1 221 ? -48.292 29.100  -11.685 1.00 30.59 ?  221 ARG A CD  1 
ATOM   1570 N  NE  . ARG A 1 221 ? -48.784 29.937  -10.593 1.00 33.79 ?  221 ARG A NE  1 
ATOM   1571 C  CZ  . ARG A 1 221 ? -48.655 29.649  -9.304  1.00 41.22 ?  221 ARG A CZ  1 
ATOM   1572 N  NH1 . ARG A 1 221 ? -48.001 28.569  -8.896  1.00 37.49 ?  221 ARG A NH1 1 
ATOM   1573 N  NH2 . ARG A 1 221 ? -49.185 30.473  -8.399  1.00 44.22 ?  221 ARG A NH2 1 
ATOM   1574 N  N   . PHE A 1 222 ? -49.278 25.430  -15.914 1.00 33.62 ?  222 PHE A N   1 
ATOM   1575 C  CA  . PHE A 1 222 ? -48.915 24.849  -17.206 1.00 38.62 ?  222 PHE A CA  1 
ATOM   1576 C  C   . PHE A 1 222 ? -50.153 24.598  -18.065 1.00 39.89 ?  222 PHE A C   1 
ATOM   1577 O  O   . PHE A 1 222 ? -50.156 24.902  -19.264 1.00 39.78 ?  222 PHE A O   1 
ATOM   1578 C  CB  . PHE A 1 222 ? -48.127 23.542  -17.017 1.00 31.21 ?  222 PHE A CB  1 
ATOM   1579 C  CG  . PHE A 1 222 ? -46.666 23.740  -16.667 1.00 27.95 ?  222 PHE A CG  1 
ATOM   1580 C  CD1 . PHE A 1 222 ? -46.123 25.011  -16.573 1.00 29.71 ?  222 PHE A CD1 1 
ATOM   1581 C  CD2 . PHE A 1 222 ? -45.847 22.648  -16.417 1.00 29.68 ?  222 PHE A CD2 1 
ATOM   1582 C  CE1 . PHE A 1 222 ? -44.783 25.200  -16.246 1.00 30.17 ?  222 PHE A CE1 1 
ATOM   1583 C  CE2 . PHE A 1 222 ? -44.504 22.815  -16.086 1.00 26.02 ?  222 PHE A CE2 1 
ATOM   1584 C  CZ  . PHE A 1 222 ? -43.966 24.094  -16.005 1.00 28.39 ?  222 PHE A CZ  1 
ATOM   1585 N  N   . ALA A 1 223 ? -51.211 24.036  -17.474 1.00 35.32 ?  223 ALA A N   1 
ATOM   1586 C  CA  . ALA A 1 223 ? -52.417 23.749  -18.246 1.00 41.52 ?  223 ALA A CA  1 
ATOM   1587 C  C   . ALA A 1 223 ? -52.994 25.017  -18.866 1.00 48.95 ?  223 ALA A C   1 
ATOM   1588 O  O   . ALA A 1 223 ? -53.521 24.984  -19.985 1.00 51.06 ?  223 ALA A O   1 
ATOM   1589 C  CB  . ALA A 1 223 ? -53.452 23.053  -17.361 1.00 44.00 ?  223 ALA A CB  1 
ATOM   1590 N  N   . GLU A 1 224 ? -52.894 26.147  -18.159 1.00 46.65 ?  224 GLU A N   1 
ATOM   1591 C  CA  . GLU A 1 224 ? -53.305 27.423  -18.735 1.00 52.52 ?  224 GLU A CA  1 
ATOM   1592 C  C   . GLU A 1 224 ? -52.354 27.865  -19.837 1.00 52.71 ?  224 GLU A C   1 
ATOM   1593 O  O   . GLU A 1 224 ? -52.796 28.358  -20.881 1.00 54.85 ?  224 GLU A O   1 
ATOM   1594 C  CB  . GLU A 1 224 ? -53.385 28.499  -17.650 1.00 51.34 ?  224 GLU A CB  1 
ATOM   1595 N  N   . LEU A 1 225 ? -51.048 27.690  -19.621 1.00 53.03 ?  225 LEU A N   1 
ATOM   1596 C  CA  . LEU A 1 225 ? -50.048 28.167  -20.571 1.00 53.69 ?  225 LEU A CA  1 
ATOM   1597 C  C   . LEU A 1 225 ? -50.294 27.619  -21.972 1.00 59.87 ?  225 LEU A C   1 
ATOM   1598 O  O   . LEU A 1 225 ? -50.240 28.365  -22.957 1.00 70.43 ?  225 LEU A O   1 
ATOM   1599 C  CB  . LEU A 1 225 ? -48.648 27.789  -20.090 1.00 55.16 ?  225 LEU A CB  1 
ATOM   1600 C  CG  . LEU A 1 225 ? -47.477 28.379  -20.875 1.00 56.46 ?  225 LEU A CG  1 
ATOM   1601 C  CD1 . LEU A 1 225 ? -46.282 28.650  -19.965 1.00 55.29 ?  225 LEU A CD1 1 
ATOM   1602 C  CD2 . LEU A 1 225 ? -47.090 27.456  -22.021 1.00 62.42 ?  225 LEU A CD2 1 
ATOM   1603 N  N   . ARG A 1 226 ? -50.565 26.319  -22.087 1.00 59.63 ?  226 ARG A N   1 
ATOM   1604 C  CA  . ARG A 1 226 ? -50.717 25.728  -23.412 1.00 64.91 ?  226 ARG A CA  1 
ATOM   1605 C  C   . ARG A 1 226 ? -52.086 25.983  -24.036 1.00 67.79 ?  226 ARG A C   1 
ATOM   1606 O  O   . ARG A 1 226 ? -52.335 25.492  -25.142 1.00 70.45 ?  226 ARG A O   1 
ATOM   1607 C  CB  . ARG A 1 226 ? -50.436 24.223  -23.369 1.00 60.61 ?  226 ARG A CB  1 
ATOM   1608 C  CG  . ARG A 1 226 ? -51.185 23.471  -22.305 1.00 54.43 ?  226 ARG A CG  1 
ATOM   1609 C  CD  . ARG A 1 226 ? -50.869 21.980  -22.353 1.00 47.91 ?  226 ARG A CD  1 
ATOM   1610 N  NE  . ARG A 1 226 ? -51.906 21.222  -21.667 1.00 43.57 ?  226 ARG A NE  1 
ATOM   1611 C  CZ  . ARG A 1 226 ? -51.839 19.930  -21.387 1.00 43.00 ?  226 ARG A CZ  1 
ATOM   1612 N  NH1 . ARG A 1 226 ? -50.782 19.205  -21.715 1.00 38.22 ?  226 ARG A NH1 1 
ATOM   1613 N  NH2 . ARG A 1 226 ? -52.861 19.351  -20.760 1.00 42.14 ?  226 ARG A NH2 1 
ATOM   1614 N  N   . ARG A 1 227 ? -52.972 26.731  -23.368 1.00 65.79 ?  227 ARG A N   1 
ATOM   1615 C  CA  . ARG A 1 227 ? -54.186 27.236  -24.000 1.00 67.22 ?  227 ARG A CA  1 
ATOM   1616 C  C   . ARG A 1 227 ? -53.969 28.574  -24.696 1.00 76.42 ?  227 ARG A C   1 
ATOM   1617 O  O   . ARG A 1 227 ? -54.769 28.943  -25.563 1.00 77.94 ?  227 ARG A O   1 
ATOM   1618 C  CB  . ARG A 1 227 ? -55.315 27.380  -22.971 1.00 65.05 ?  227 ARG A CB  1 
ATOM   1619 C  CG  . ARG A 1 227 ? -55.864 26.064  -22.433 1.00 60.42 ?  227 ARG A CG  1 
ATOM   1620 C  CD  . ARG A 1 227 ? -56.620 26.272  -21.128 1.00 61.98 ?  227 ARG A CD  1 
ATOM   1621 N  NE  . ARG A 1 227 ? -56.629 25.069  -20.301 1.00 66.59 ?  227 ARG A NE  1 
ATOM   1622 C  CZ  . ARG A 1 227 ? -57.182 24.988  -19.098 1.00 63.60 ?  227 ARG A CZ  1 
ATOM   1623 N  NH1 . ARG A 1 227 ? -57.766 26.034  -18.534 1.00 67.82 ?  227 ARG A NH1 1 
ATOM   1624 N  NH2 . ARG A 1 227 ? -57.130 23.834  -18.436 1.00 54.86 ?  227 ARG A NH2 1 
ATOM   1625 N  N   . SER A 1 228 ? -52.904 29.298  -24.336 1.00 74.56 ?  228 SER A N   1 
ATOM   1626 C  CA  . SER A 1 228 ? -52.574 30.568  -24.963 1.00 81.13 ?  228 SER A CA  1 
ATOM   1627 C  C   . SER A 1 228 ? -52.291 30.376  -26.456 1.00 88.13 ?  228 SER A C   1 
ATOM   1628 O  O   . SER A 1 228 ? -51.970 29.271  -26.900 1.00 88.19 ?  228 SER A O   1 
ATOM   1629 C  CB  . SER A 1 228 ? -51.371 31.190  -24.248 1.00 81.36 ?  228 SER A CB  1 
ATOM   1630 O  OG  . SER A 1 228 ? -50.965 32.412  -24.837 1.00 91.52 ?  228 SER A OG  1 
ATOM   1631 N  N   . VAL A 1 235 ? -44.029 24.502  -26.909 1.00 82.36 ?  235 VAL A N   1 
ATOM   1632 C  CA  . VAL A 1 235 ? -43.803 23.812  -25.606 1.00 63.82 ?  235 VAL A CA  1 
ATOM   1633 C  C   . VAL A 1 235 ? -44.650 22.531  -25.640 1.00 56.49 ?  235 VAL A C   1 
ATOM   1634 O  O   . VAL A 1 235 ? -45.843 22.640  -25.937 1.00 65.84 ?  235 VAL A O   1 
ATOM   1635 C  CB  . VAL A 1 235 ? -44.154 24.738  -24.429 1.00 60.49 ?  235 VAL A CB  1 
ATOM   1636 C  CG1 . VAL A 1 235 ? -45.618 25.143  -24.390 1.00 66.04 ?  235 VAL A CG1 1 
ATOM   1637 C  CG2 . VAL A 1 235 ? -43.710 24.153  -23.099 1.00 58.02 ?  235 VAL A CG2 1 
ATOM   1638 N  N   . SER A 1 236 ? -44.060 21.360  -25.410 1.00 43.72 ?  236 SER A N   1 
ATOM   1639 C  CA  . SER A 1 236 ? -44.776 20.098  -25.501 1.00 40.05 ?  236 SER A CA  1 
ATOM   1640 C  C   . SER A 1 236 ? -45.141 19.579  -24.118 1.00 35.79 ?  236 SER A C   1 
ATOM   1641 O  O   . SER A 1 236 ? -44.668 20.070  -23.091 1.00 35.08 ?  236 SER A O   1 
ATOM   1642 C  CB  . SER A 1 236 ? -43.937 19.045  -26.233 1.00 36.80 ?  236 SER A CB  1 
ATOM   1643 O  OG  . SER A 1 236 ? -42.892 18.563  -25.402 1.00 39.68 ?  236 SER A OG  1 
ATOM   1644 N  N   . ASP A 1 237 ? -45.985 18.546  -24.116 1.00 33.36 ?  237 ASP A N   1 
ATOM   1645 C  CA  . ASP A 1 237 ? -46.304 17.852  -22.876 1.00 34.68 ?  237 ASP A CA  1 
ATOM   1646 C  C   . ASP A 1 237 ? -45.049 17.314  -22.208 1.00 37.43 ?  237 ASP A C   1 
ATOM   1647 O  O   . ASP A 1 237 ? -44.942 17.316  -20.973 1.00 29.83 ?  237 ASP A O   1 
ATOM   1648 C  CB  . ASP A 1 237 ? -47.283 16.711  -23.148 1.00 35.52 ?  237 ASP A CB  1 
ATOM   1649 C  CG  . ASP A 1 237 ? -48.714 17.184  -23.238 1.00 37.37 ?  237 ASP A CG  1 
ATOM   1650 O  OD1 . ASP A 1 237 ? -48.929 18.396  -23.468 1.00 39.59 ?  237 ASP A OD1 1 
ATOM   1651 O  OD2 . ASP A 1 237 ? -49.620 16.348  -23.041 1.00 36.71 ?  237 ASP A OD2 1 
ATOM   1652 N  N   . GLU A 1 238 ? -44.090 16.842  -23.011 1.00 36.45 ?  238 GLU A N   1 
ATOM   1653 C  CA  . GLU A 1 238 ? -42.886 16.227  -22.464 1.00 39.92 ?  238 GLU A CA  1 
ATOM   1654 C  C   . GLU A 1 238 ? -42.052 17.250  -21.703 1.00 33.01 ?  238 GLU A C   1 
ATOM   1655 O  O   . GLU A 1 238 ? -41.609 16.998  -20.575 1.00 30.92 ?  238 GLU A O   1 
ATOM   1656 C  CB  . GLU A 1 238 ? -42.064 15.595  -23.593 1.00 40.27 ?  238 GLU A CB  1 
ATOM   1657 N  N   . LEU A 1 239 ? -41.817 18.411  -22.316 1.00 32.28 ?  239 LEU A N   1 
ATOM   1658 C  CA  . LEU A 1 239 ? -41.051 19.449  -21.643 1.00 30.94 ?  239 LEU A CA  1 
ATOM   1659 C  C   . LEU A 1 239 ? -41.751 19.907  -20.372 1.00 29.72 ?  239 LEU A C   1 
ATOM   1660 O  O   . LEU A 1 239 ? -41.108 20.093  -19.331 1.00 24.58 ?  239 LEU A O   1 
ATOM   1661 C  CB  . LEU A 1 239 ? -40.819 20.625  -22.586 1.00 32.43 ?  239 LEU A CB  1 
ATOM   1662 C  CG  . LEU A 1 239 ? -40.270 21.874  -21.895 1.00 34.71 ?  239 LEU A CG  1 
ATOM   1663 C  CD1 . LEU A 1 239 ? -38.847 21.623  -21.435 1.00 37.19 ?  239 LEU A CD1 1 
ATOM   1664 C  CD2 . LEU A 1 239 ? -40.299 23.059  -22.832 1.00 39.76 ?  239 LEU A CD2 1 
ATOM   1665 N  N   . LEU A 1 240 ? -43.074 20.064  -20.434 1.00 29.84 ?  240 LEU A N   1 
ATOM   1666 C  CA  . LEU A 1 240 ? -43.830 20.501  -19.268 1.00 25.25 ?  240 LEU A CA  1 
ATOM   1667 C  C   . LEU A 1 240 ? -43.688 19.500  -18.127 1.00 24.24 ?  240 LEU A C   1 
ATOM   1668 O  O   . LEU A 1 240 ? -43.384 19.869  -16.984 1.00 26.83 ?  240 LEU A O   1 
ATOM   1669 C  CB  . LEU A 1 240 ? -45.298 20.687  -19.658 1.00 27.72 ?  240 LEU A CB  1 
ATOM   1670 C  CG  . LEU A 1 240 ? -45.592 21.914  -20.538 1.00 31.00 ?  240 LEU A CG  1 
ATOM   1671 C  CD1 . LEU A 1 240 ? -47.073 21.989  -20.878 1.00 34.06 ?  240 LEU A CD1 1 
ATOM   1672 C  CD2 . LEU A 1 240 ? -45.122 23.211  -19.864 1.00 27.72 ?  240 LEU A CD2 1 
ATOM   1673 N  N   . ALA A 1 241 ? -43.886 18.221  -18.429 1.00 23.69 ?  241 ALA A N   1 
ATOM   1674 C  CA  . ALA A 1 241 ? -43.736 17.188  -17.416 1.00 26.05 ?  241 ALA A CA  1 
ATOM   1675 C  C   . ALA A 1 241 ? -42.295 17.078  -16.935 1.00 24.63 ?  241 ALA A C   1 
ATOM   1676 O  O   . ALA A 1 241 ? -42.058 16.751  -15.764 1.00 25.11 ?  241 ALA A O   1 
ATOM   1677 C  CB  . ALA A 1 241 ? -44.221 15.853  -17.969 1.00 25.61 ?  241 ALA A CB  1 
ATOM   1678 N  N   . THR A 1 242 ? -41.332 17.370  -17.810 1.00 22.72 ?  242 THR A N   1 
ATOM   1679 C  CA  . THR A 1 242 ? -39.925 17.280  -17.429 1.00 23.77 ?  242 THR A CA  1 
ATOM   1680 C  C   . THR A 1 242 ? -39.580 18.327  -16.381 1.00 26.09 ?  242 THR A C   1 
ATOM   1681 O  O   . THR A 1 242 ? -38.906 18.026  -15.389 1.00 21.62 ?  242 THR A O   1 
ATOM   1682 C  CB  . THR A 1 242 ? -39.038 17.444  -18.670 1.00 24.04 ?  242 THR A CB  1 
ATOM   1683 O  OG1 . THR A 1 242 ? -39.204 16.314  -19.526 1.00 23.97 ?  242 THR A OG1 1 
ATOM   1684 C  CG2 . THR A 1 242 ? -37.571 17.553  -18.296 1.00 26.63 ?  242 THR A CG2 1 
ATOM   1685 N  N   . VAL A 1 243 ? -40.052 19.557  -16.582 1.00 23.59 ?  243 VAL A N   1 
ATOM   1686 C  CA  . VAL A 1 243 ? -39.847 20.616  -15.602 1.00 21.16 ?  243 VAL A CA  1 
ATOM   1687 C  C   . VAL A 1 243 ? -40.479 20.239  -14.272 1.00 20.85 ?  243 VAL A C   1 
ATOM   1688 O  O   . VAL A 1 243 ? -39.872 20.412  -13.210 1.00 22.31 ?  243 VAL A O   1 
ATOM   1689 C  CB  . VAL A 1 243 ? -40.411 21.948  -16.139 1.00 23.20 ?  243 VAL A CB  1 
ATOM   1690 C  CG1 . VAL A 1 243 ? -40.337 23.051  -15.065 1.00 21.27 ?  243 VAL A CG1 1 
ATOM   1691 C  CG2 . VAL A 1 243 ? -39.668 22.364  -17.377 1.00 22.68 ?  243 VAL A CG2 1 
ATOM   1692 N  N   . ALA A 1 244 ? -41.719 19.740  -14.308 1.00 22.69 ?  244 ALA A N   1 
ATOM   1693 C  CA  . ALA A 1 244 ? -42.392 19.325  -13.083 1.00 22.14 ?  244 ALA A CA  1 
ATOM   1694 C  C   . ALA A 1 244 ? -41.594 18.249  -12.356 1.00 23.34 ?  244 ALA A C   1 
ATOM   1695 O  O   . ALA A 1 244 ? -41.334 18.358  -11.153 1.00 24.25 ?  244 ALA A O   1 
ATOM   1696 C  CB  . ALA A 1 244 ? -43.801 18.817  -13.402 1.00 23.08 ?  244 ALA A CB  1 
ATOM   1697 N  N   . LEU A 1 245 ? -41.197 17.199  -13.073 1.00 23.25 ?  245 LEU A N   1 
ATOM   1698 C  CA  . LEU A 1 245 ? -40.483 16.104  -12.424 1.00 20.25 ?  245 LEU A CA  1 
ATOM   1699 C  C   . LEU A 1 245 ? -39.119 16.551  -11.906 1.00 22.93 ?  245 LEU A C   1 
ATOM   1700 O  O   . LEU A 1 245 ? -38.705 16.148  -10.812 1.00 21.59 ?  245 LEU A O   1 
ATOM   1701 C  CB  . LEU A 1 245 ? -40.327 14.936  -13.398 1.00 24.58 ?  245 LEU A CB  1 
ATOM   1702 C  CG  . LEU A 1 245 ? -39.509 13.743  -12.898 1.00 26.03 ?  245 LEU A CG  1 
ATOM   1703 C  CD1 . LEU A 1 245 ? -40.056 13.242  -11.550 1.00 22.38 ?  245 LEU A CD1 1 
ATOM   1704 C  CD2 . LEU A 1 245 ? -39.495 12.631  -13.960 1.00 22.76 ?  245 LEU A CD2 1 
ATOM   1705 N  N   . SER A 1 246 ? -38.392 17.369  -12.680 1.00 19.57 ?  246 SER A N   1 
ATOM   1706 C  CA  . SER A 1 246 ? -37.062 17.758  -12.230 1.00 24.95 ?  246 SER A CA  1 
ATOM   1707 C  C   . SER A 1 246 ? -37.145 18.660  -11.005 1.00 22.07 ?  246 SER A C   1 
ATOM   1708 O  O   . SER A 1 246 ? -36.310 18.556  -10.103 1.00 21.35 ?  246 SER A O   1 
ATOM   1709 C  CB  . SER A 1 246 ? -36.284 18.437  -13.359 1.00 23.56 ?  246 SER A CB  1 
ATOM   1710 O  OG  . SER A 1 246 ? -36.903 19.636  -13.736 1.00 35.57 ?  246 SER A OG  1 
ATOM   1711 N  N   . LEU A 1 247 ? -38.168 19.524  -10.944 1.00 20.09 ?  247 LEU A N   1 
ATOM   1712 C  CA  . LEU A 1 247 ? -38.329 20.430  -9.810  1.00 22.59 ?  247 LEU A CA  1 
ATOM   1713 C  C   . LEU A 1 247 ? -38.793 19.677  -8.571  1.00 23.07 ?  247 LEU A C   1 
ATOM   1714 O  O   . LEU A 1 247 ? -38.319 19.947  -7.462  1.00 20.47 ?  247 LEU A O   1 
ATOM   1715 C  CB  . LEU A 1 247 ? -39.324 21.545  -10.156 1.00 21.83 ?  247 LEU A CB  1 
ATOM   1716 C  CG  . LEU A 1 247 ? -38.883 22.647  -11.127 1.00 32.51 ?  247 LEU A CG  1 
ATOM   1717 C  CD1 . LEU A 1 247 ? -40.049 23.598  -11.414 1.00 25.01 ?  247 LEU A CD1 1 
ATOM   1718 C  CD2 . LEU A 1 247 ? -37.651 23.414  -10.608 1.00 22.31 ?  247 LEU A CD2 1 
ATOM   1719 N  N   . PHE A 1 248 ? -39.734 18.741  -8.734  1.00 20.08 ?  248 PHE A N   1 
ATOM   1720 C  CA  . PHE A 1 248 ? -40.101 17.884  -7.614  1.00 22.01 ?  248 PHE A CA  1 
ATOM   1721 C  C   . PHE A 1 248 ? -38.877 17.160  -7.082  1.00 21.49 ?  248 PHE A C   1 
ATOM   1722 O  O   . PHE A 1 248 ? -38.568 17.224  -5.889  1.00 22.18 ?  248 PHE A O   1 
ATOM   1723 C  CB  . PHE A 1 248 ? -41.160 16.867  -8.038  1.00 22.33 ?  248 PHE A CB  1 
ATOM   1724 C  CG  . PHE A 1 248 ? -41.618 15.978  -6.912  1.00 22.41 ?  248 PHE A CG  1 
ATOM   1725 C  CD1 . PHE A 1 248 ? -40.895 14.838  -6.560  1.00 18.18 ?  248 PHE A CD1 1 
ATOM   1726 C  CD2 . PHE A 1 248 ? -42.776 16.276  -6.217  1.00 17.70 ?  248 PHE A CD2 1 
ATOM   1727 C  CE1 . PHE A 1 248 ? -41.316 14.029  -5.525  1.00 18.51 ?  248 PHE A CE1 1 
ATOM   1728 C  CE2 . PHE A 1 248 ? -43.207 15.470  -5.183  1.00 19.22 ?  248 PHE A CE2 1 
ATOM   1729 C  CZ  . PHE A 1 248 ? -42.473 14.343  -4.828  1.00 18.69 ?  248 PHE A CZ  1 
ATOM   1730 N  N   . GLY A 1 249 ? -38.165 16.469  -7.969  1.00 20.78 ?  249 GLY A N   1 
ATOM   1731 C  CA  . GLY A 1 249 ? -37.085 15.603  -7.530  1.00 20.07 ?  249 GLY A CA  1 
ATOM   1732 C  C   . GLY A 1 249 ? -35.965 16.386  -6.885  1.00 18.84 ?  249 GLY A C   1 
ATOM   1733 O  O   . GLY A 1 249 ? -35.577 16.113  -5.744  1.00 17.51 ?  249 GLY A O   1 
ATOM   1734 N  N   . ALA A 1 250 ? -35.456 17.401  -7.593  1.00 19.01 ?  250 ALA A N   1 
ATOM   1735 C  CA  . ALA A 1 250 ? -34.380 18.220  -7.042  1.00 21.30 ?  250 ALA A CA  1 
ATOM   1736 C  C   . ALA A 1 250 ? -34.797 18.900  -5.732  1.00 20.39 ?  250 ALA A C   1 
ATOM   1737 O  O   . ALA A 1 250 ? -34.032 18.920  -4.757  1.00 20.44 ?  250 ALA A O   1 
ATOM   1738 C  CB  . ALA A 1 250 ? -33.936 19.257  -8.077  1.00 21.70 ?  250 ALA A CB  1 
ATOM   1739 N  N   . GLY A 1 251 ? -35.993 19.499  -5.703  1.00 20.34 ?  251 GLY A N   1 
ATOM   1740 C  CA  . GLY A 1 251 ? -36.425 20.214  -4.506  1.00 16.75 ?  251 GLY A CA  1 
ATOM   1741 C  C   . GLY A 1 251 ? -36.674 19.300  -3.315  1.00 16.42 ?  251 GLY A C   1 
ATOM   1742 O  O   . GLY A 1 251 ? -36.182 19.550  -2.209  1.00 19.68 ?  251 GLY A O   1 
ATOM   1743 N  N   . ALA A 1 252 ? -37.429 18.221  -3.519  1.00 16.59 ?  252 ALA A N   1 
ATOM   1744 C  CA  . ALA A 1 252 ? -37.683 17.291  -2.412  1.00 17.78 ?  252 ALA A CA  1 
ATOM   1745 C  C   . ALA A 1 252 ? -36.386 16.707  -1.859  1.00 18.32 ?  252 ALA A C   1 
ATOM   1746 O  O   . ALA A 1 252 ? -36.159 16.711  -0.646  1.00 16.02 ?  252 ALA A O   1 
ATOM   1747 C  CB  . ALA A 1 252 ? -38.612 16.164  -2.853  1.00 17.13 ?  252 ALA A CB  1 
ATOM   1748 N  N   . VAL A 1 253 ? -35.515 16.193  -2.732  1.00 18.55 ?  253 VAL A N   1 
ATOM   1749 C  CA  . VAL A 1 253 ? -34.309 15.547  -2.218  1.00 16.28 ?  253 VAL A CA  1 
ATOM   1750 C  C   . VAL A 1 253 ? -33.420 16.550  -1.494  1.00 17.77 ?  253 VAL A C   1 
ATOM   1751 O  O   . VAL A 1 253 ? -32.791 16.212  -0.484  1.00 15.77 ?  253 VAL A O   1 
ATOM   1752 C  CB  . VAL A 1 253 ? -33.542 14.824  -3.339  1.00 17.18 ?  253 VAL A CB  1 
ATOM   1753 C  CG1 . VAL A 1 253 ? -33.038 15.813  -4.418  1.00 15.70 ?  253 VAL A CG1 1 
ATOM   1754 C  CG2 . VAL A 1 253 ? -32.377 14.035  -2.727  1.00 13.52 ?  253 VAL A CG2 1 
ATOM   1755 N  N   . SER A 1 254 ? -33.364 17.808  -1.982  1.00 14.92 ?  254 SER A N   1 
ATOM   1756 C  CA  . SER A 1 254 ? -32.433 18.781  -1.406  1.00 16.89 ?  254 SER A CA  1 
ATOM   1757 C  C   . SER A 1 254 ? -32.941 19.343  -0.084  1.00 16.08 ?  254 SER A C   1 
ATOM   1758 O  O   . SER A 1 254 ? -32.159 19.510  0.854   1.00 13.40 ?  254 SER A O   1 
ATOM   1759 C  CB  . SER A 1 254 ? -32.156 19.929  -2.387  1.00 16.47 ?  254 SER A CB  1 
ATOM   1760 O  OG  . SER A 1 254 ? -31.547 19.459  -3.580  1.00 15.74 ?  254 SER A OG  1 
ATOM   1761 N  N   . THR A 1 255 ? -34.240 19.649  0.012   1.00 17.54 ?  255 THR A N   1 
ATOM   1762 C  CA  . THR A 1 255 ? -34.781 20.128  1.285   1.00 14.92 ?  255 THR A CA  1 
ATOM   1763 C  C   . THR A 1 255 ? -34.818 19.011  2.327   1.00 15.58 ?  255 THR A C   1 
ATOM   1764 O  O   . THR A 1 255 ? -34.467 19.234  3.485   1.00 16.94 ?  255 THR A O   1 
ATOM   1765 C  CB  . THR A 1 255 ? -36.179 20.724  1.089   1.00 16.40 ?  255 THR A CB  1 
ATOM   1766 O  OG1 . THR A 1 255 ? -37.021 19.768  0.441   1.00 15.96 ?  255 THR A OG1 1 
ATOM   1767 C  CG2 . THR A 1 255 ? -36.113 21.997  0.235   1.00 13.81 ?  255 THR A CG2 1 
ATOM   1768 N  N   . SER A 1 256 ? -35.221 17.798  1.934   1.00 15.19 ?  256 SER A N   1 
ATOM   1769 C  CA  . SER A 1 256 ? -35.192 16.672  2.870   1.00 17.35 ?  256 SER A CA  1 
ATOM   1770 C  C   . SER A 1 256 ? -33.788 16.414  3.414   1.00 16.16 ?  256 SER A C   1 
ATOM   1771 O  O   . SER A 1 256 ? -33.617 16.164  4.614   1.00 15.24 ?  256 SER A O   1 
ATOM   1772 C  CB  . SER A 1 256 ? -35.712 15.405  2.195   1.00 14.95 ?  256 SER A CB  1 
ATOM   1773 O  OG  . SER A 1 256 ? -35.688 14.331  3.125   1.00 19.15 ?  256 SER A OG  1 
ATOM   1774 N  N   . ALA A 1 257 ? -32.772 16.427  2.543   1.00 17.71 ?  257 ALA A N   1 
ATOM   1775 C  CA  . ALA A 1 257 ? -31.423 16.111  3.010   1.00 16.73 ?  257 ALA A CA  1 
ATOM   1776 C  C   . ALA A 1 257 ? -30.853 17.228  3.878   1.00 17.17 ?  257 ALA A C   1 
ATOM   1777 O  O   . ALA A 1 257 ? -30.224 16.958  4.906   1.00 15.25 ?  257 ALA A O   1 
ATOM   1778 C  CB  . ALA A 1 257 ? -30.495 15.835  1.823   1.00 13.24 ?  257 ALA A CB  1 
ATOM   1779 N  N   . PHE A 1 258 ? -31.016 18.487  3.465   1.00 16.70 ?  258 PHE A N   1 
ATOM   1780 C  CA  . PHE A 1 258 ? -30.574 19.583  4.323   1.00 18.53 ?  258 PHE A CA  1 
ATOM   1781 C  C   . PHE A 1 258 ? -31.246 19.525  5.689   1.00 16.77 ?  258 PHE A C   1 
ATOM   1782 O  O   . PHE A 1 258 ? -30.589 19.690  6.721   1.00 18.72 ?  258 PHE A O   1 
ATOM   1783 C  CB  . PHE A 1 258 ? -30.857 20.945  3.681   1.00 17.02 ?  258 PHE A CB  1 
ATOM   1784 C  CG  . PHE A 1 258 ? -30.720 22.098  4.655   1.00 20.67 ?  258 PHE A CG  1 
ATOM   1785 C  CD1 . PHE A 1 258 ? -29.576 22.221  5.444   1.00 16.44 ?  258 PHE A CD1 1 
ATOM   1786 C  CD2 . PHE A 1 258 ? -31.728 23.053  4.782   1.00 16.98 ?  258 PHE A CD2 1 
ATOM   1787 C  CE1 . PHE A 1 258 ? -29.443 23.268  6.378   1.00 19.76 ?  258 PHE A CE1 1 
ATOM   1788 C  CE2 . PHE A 1 258 ? -31.602 24.110  5.691   1.00 19.73 ?  258 PHE A CE2 1 
ATOM   1789 C  CZ  . PHE A 1 258 ? -30.461 24.219  6.495   1.00 17.30 ?  258 PHE A CZ  1 
ATOM   1790 N  N   . LEU A 1 259 ? -32.569 19.339  5.717   1.00 17.03 ?  259 LEU A N   1 
ATOM   1791 C  CA  . LEU A 1 259 ? -33.274 19.357  6.998   1.00 17.54 ?  259 LEU A CA  1 
ATOM   1792 C  C   . LEU A 1 259 ? -32.759 18.260  7.918   1.00 18.63 ?  259 LEU A C   1 
ATOM   1793 O  O   . LEU A 1 259 ? -32.653 18.463  9.136   1.00 17.90 ?  259 LEU A O   1 
ATOM   1794 C  CB  . LEU A 1 259 ? -34.783 19.223  6.779   1.00 15.39 ?  259 LEU A CB  1 
ATOM   1795 C  CG  . LEU A 1 259 ? -35.669 19.210  8.029   1.00 19.03 ?  259 LEU A CG  1 
ATOM   1796 C  CD1 . LEU A 1 259 ? -35.392 20.402  8.919   1.00 16.65 ?  259 LEU A CD1 1 
ATOM   1797 C  CD2 . LEU A 1 259 ? -37.119 19.231  7.602   1.00 19.66 ?  259 LEU A CD2 1 
ATOM   1798 N  N   . GLN A 1 260 ? -32.395 17.100  7.350   1.00 17.22 ?  260 GLN A N   1 
ATOM   1799 C  CA  . GLN A 1 260 ? -31.857 16.022  8.180   1.00 18.45 ?  260 GLN A CA  1 
ATOM   1800 C  C   . GLN A 1 260 ? -30.543 16.447  8.813   1.00 18.64 ?  260 GLN A C   1 
ATOM   1801 O  O   . GLN A 1 260 ? -30.258 16.093  9.962   1.00 22.52 ?  260 GLN A O   1 
ATOM   1802 C  CB  . GLN A 1 260 ? -31.644 14.742  7.356   1.00 18.61 ?  260 GLN A CB  1 
ATOM   1803 C  CG  . GLN A 1 260 ? -32.922 14.060  6.799   1.00 18.89 ?  260 GLN A CG  1 
ATOM   1804 C  CD  . GLN A 1 260 ? -32.605 12.935  5.787   1.00 26.39 ?  260 GLN A CD  1 
ATOM   1805 O  OE1 . GLN A 1 260 ? -31.932 11.953  6.119   1.00 26.58 ?  260 GLN A OE1 1 
ATOM   1806 N  NE2 . GLN A 1 260 ? -33.084 13.090  4.539   1.00 28.65 ?  260 GLN A NE2 1 
ATOM   1807 N  N   . HIS A 1 261 ? -29.719 17.197  8.064   1.00 15.92 ?  261 HIS A N   1 
ATOM   1808 C  CA  . HIS A 1 261 ? -28.445 17.680  8.598   1.00 16.66 ?  261 HIS A CA  1 
ATOM   1809 C  C   . HIS A 1 261 ? -28.671 18.705  9.706   1.00 15.99 ?  261 HIS A C   1 
ATOM   1810 O  O   . HIS A 1 261 ? -28.045 18.637  10.773  1.00 15.34 ?  261 HIS A O   1 
ATOM   1811 C  CB  . HIS A 1 261 ? -27.599 18.269  7.458   1.00 16.13 ?  261 HIS A CB  1 
ATOM   1812 C  CG  . HIS A 1 261 ? -26.875 17.230  6.644   1.00 18.79 ?  261 HIS A CG  1 
ATOM   1813 N  ND1 . HIS A 1 261 ? -25.528 16.976  6.787   1.00 19.19 ?  261 HIS A ND1 1 
ATOM   1814 C  CD2 . HIS A 1 261 ? -27.321 16.360  5.702   1.00 17.61 ?  261 HIS A CD2 1 
ATOM   1815 C  CE1 . HIS A 1 261 ? -25.170 16.008  5.957   1.00 21.17 ?  261 HIS A CE1 1 
ATOM   1816 N  NE2 . HIS A 1 261 ? -26.241 15.612  5.291   1.00 18.73 ?  261 HIS A NE2 1 
ATOM   1817 N  N   . ALA A 1 262 ? -29.592 19.638  9.484   1.00 16.62 ?  262 ALA A N   1 
ATOM   1818 C  CA  . ALA A 1 262 ? -29.930 20.615  10.519  1.00 15.38 ?  262 ALA A CA  1 
ATOM   1819 C  C   . ALA A 1 262 ? -30.460 19.940  11.788  1.00 17.73 ?  262 ALA A C   1 
ATOM   1820 O  O   . ALA A 1 262 ? -30.143 20.366  12.907  1.00 19.73 ?  262 ALA A O   1 
ATOM   1821 C  CB  . ALA A 1 262 ? -30.944 21.613  9.953   1.00 14.30 ?  262 ALA A CB  1 
ATOM   1822 N  N   . ILE A 1 263 ? -31.243 18.868  11.644  1.00 17.19 ?  263 ILE A N   1 
ATOM   1823 C  CA  . ILE A 1 263 ? -31.767 18.171  12.824  1.00 17.02 ?  263 ILE A CA  1 
ATOM   1824 C  C   . ILE A 1 263 ? -30.628 17.557  13.637  1.00 17.88 ?  263 ILE A C   1 
ATOM   1825 O  O   . ILE A 1 263 ? -30.544 17.726  14.867  1.00 20.44 ?  263 ILE A O   1 
ATOM   1826 C  CB  . ILE A 1 263 ? -32.803 17.114  12.395  1.00 19.42 ?  263 ILE A CB  1 
ATOM   1827 C  CG1 . ILE A 1 263 ? -34.107 17.821  11.986  1.00 20.55 ?  263 ILE A CG1 1 
ATOM   1828 C  CG2 . ILE A 1 263 ? -33.021 16.071  13.519  1.00 15.63 ?  263 ILE A CG2 1 
ATOM   1829 C  CD1 . ILE A 1 263 ? -35.121 16.936  11.237  1.00 17.04 ?  263 ILE A CD1 1 
ATOM   1830 N  N   . ILE A 1 264 ? -29.729 16.836  12.956  1.00 16.16 ?  264 ILE A N   1 
ATOM   1831 C  CA  . ILE A 1 264 ? -28.536 16.304  13.608  1.00 16.24 ?  264 ILE A CA  1 
ATOM   1832 C  C   . ILE A 1 264 ? -27.847 17.405  14.415  1.00 20.09 ?  264 ILE A C   1 
ATOM   1833 O  O   . ILE A 1 264 ? -27.533 17.230  15.599  1.00 16.75 ?  264 ILE A O   1 
ATOM   1834 C  CB  . ILE A 1 264 ? -27.593 15.677  12.563  1.00 17.78 ?  264 ILE A CB  1 
ATOM   1835 C  CG1 . ILE A 1 264 ? -28.174 14.332  12.087  1.00 18.34 ?  264 ILE A CG1 1 
ATOM   1836 C  CG2 . ILE A 1 264 ? -26.200 15.488  13.157  1.00 18.45 ?  264 ILE A CG2 1 
ATOM   1837 C  CD1 . ILE A 1 264 ? -27.597 13.785  10.807  1.00 16.83 ?  264 ILE A CD1 1 
ATOM   1838 N  N   . ALA A 1 265 ? -27.656 18.577  13.798  1.00 16.97 ?  265 ALA A N   1 
ATOM   1839 C  CA  . ALA A 1 265 ? -26.985 19.680  14.490  1.00 17.56 ?  265 ALA A CA  1 
ATOM   1840 C  C   . ALA A 1 265 ? -27.743 20.097  15.753  1.00 16.27 ?  265 ALA A C   1 
ATOM   1841 O  O   . ALA A 1 265 ? -27.141 20.271  16.818  1.00 19.71 ?  265 ALA A O   1 
ATOM   1842 C  CB  . ALA A 1 265 ? -26.799 20.865  13.533  1.00 17.49 ?  265 ALA A CB  1 
ATOM   1843 N  N   . LEU A 1 266 ? -29.069 20.227  15.667  1.00 15.59 ?  266 LEU A N   1 
ATOM   1844 C  CA  . LEU A 1 266 ? -29.857 20.589  16.850  1.00 16.79 ?  266 LEU A CA  1 
ATOM   1845 C  C   . LEU A 1 266 ? -29.893 19.470  17.890  1.00 19.53 ?  266 LEU A C   1 
ATOM   1846 O  O   . LEU A 1 266 ? -29.988 19.749  19.091  1.00 19.20 ?  266 LEU A O   1 
ATOM   1847 C  CB  . LEU A 1 266 ? -31.285 20.937  16.451  1.00 18.94 ?  266 LEU A CB  1 
ATOM   1848 C  CG  . LEU A 1 266 ? -31.463 22.132  15.514  1.00 19.14 ?  266 LEU A CG  1 
ATOM   1849 C  CD1 . LEU A 1 266 ? -32.928 22.525  15.495  1.00 18.02 ?  266 LEU A CD1 1 
ATOM   1850 C  CD2 . LEU A 1 266 ? -30.625 23.315  15.965  1.00 17.86 ?  266 LEU A CD2 1 
ATOM   1851 N  N   . ALA A 1 267 ? -29.854 18.206  17.455  1.00 19.12 ?  267 ALA A N   1 
ATOM   1852 C  CA  . ALA A 1 267 ? -29.829 17.101  18.409  1.00 19.87 ?  267 ALA A CA  1 
ATOM   1853 C  C   . ALA A 1 267 ? -28.477 16.998  19.084  1.00 21.05 ?  267 ALA A C   1 
ATOM   1854 O  O   . ALA A 1 267 ? -28.397 16.712  20.280  1.00 21.24 ?  267 ALA A O   1 
ATOM   1855 C  CB  . ALA A 1 267 ? -30.155 15.780  17.721  1.00 17.43 ?  267 ALA A CB  1 
ATOM   1856 N  N   . GLN A 1 268 ? -27.402 17.216  18.329  1.00 21.02 ?  268 GLN A N   1 
ATOM   1857 C  CA  . GLN A 1 268 ? -26.059 17.106  18.877  1.00 20.41 ?  268 GLN A CA  1 
ATOM   1858 C  C   . GLN A 1 268 ? -25.688 18.312  19.733  1.00 22.83 ?  268 GLN A C   1 
ATOM   1859 O  O   . GLN A 1 268 ? -24.815 18.210  20.602  1.00 22.02 ?  268 GLN A O   1 
ATOM   1860 C  CB  . GLN A 1 268 ? -25.047 16.950  17.742  1.00 19.21 ?  268 GLN A CB  1 
ATOM   1861 C  CG  . GLN A 1 268 ? -25.013 15.555  17.129  1.00 23.54 ?  268 GLN A CG  1 
ATOM   1862 C  CD  . GLN A 1 268 ? -24.410 14.520  18.077  1.00 28.95 ?  268 GLN A CD  1 
ATOM   1863 O  OE1 . GLN A 1 268 ? -25.099 13.946  18.931  1.00 29.94 ?  268 GLN A OE1 1 
ATOM   1864 N  NE2 . GLN A 1 268 ? -23.118 14.288  17.933  1.00 28.70 ?  268 GLN A NE2 1 
ATOM   1865 N  N   . GLN A 1 269 ? -26.301 19.463  19.482  1.00 19.29 ?  269 GLN A N   1 
ATOM   1866 C  CA  . GLN A 1 269 ? -25.941 20.711  20.152  1.00 19.11 ?  269 GLN A CA  1 
ATOM   1867 C  C   . GLN A 1 269 ? -27.216 21.340  20.684  1.00 19.05 ?  269 GLN A C   1 
ATOM   1868 O  O   . GLN A 1 269 ? -27.719 22.322  20.127  1.00 17.88 ?  269 GLN A O   1 
ATOM   1869 C  CB  . GLN A 1 269 ? -25.210 21.659  19.204  1.00 19.22 ?  269 GLN A CB  1 
ATOM   1870 C  CG  . GLN A 1 269 ? -23.930 21.088  18.636  1.00 21.70 ?  269 GLN A CG  1 
ATOM   1871 C  CD  . GLN A 1 269 ? -23.058 22.158  18.022  1.00 21.29 ?  269 GLN A CD  1 
ATOM   1872 O  OE1 . GLN A 1 269 ? -22.912 23.261  18.564  1.00 23.21 ?  269 GLN A OE1 1 
ATOM   1873 N  NE2 . GLN A 1 269 ? -22.475 21.843  16.891  1.00 18.88 ?  269 GLN A NE2 1 
ATOM   1874 N  N   . PRO A 1 270 ? -27.767 20.787  21.771  1.00 19.55 ?  270 PRO A N   1 
ATOM   1875 C  CA  . PRO A 1 270 ? -29.063 21.269  22.274  1.00 17.46 ?  270 PRO A CA  1 
ATOM   1876 C  C   . PRO A 1 270 ? -29.053 22.720  22.722  1.00 20.22 ?  270 PRO A C   1 
ATOM   1877 O  O   . PRO A 1 270 ? -30.130 23.324  22.814  1.00 18.82 ?  270 PRO A O   1 
ATOM   1878 C  CB  . PRO A 1 270 ? -29.357 20.318  23.444  1.00 19.52 ?  270 PRO A CB  1 
ATOM   1879 C  CG  . PRO A 1 270 ? -28.016 19.768  23.834  1.00 19.18 ?  270 PRO A CG  1 
ATOM   1880 C  CD  . PRO A 1 270 ? -27.253 19.653  22.557  1.00 19.27 ?  270 PRO A CD  1 
ATOM   1881 N  N   . GLU A 1 271 ? -27.882 23.311  22.995  1.00 16.72 ?  271 GLU A N   1 
ATOM   1882 C  CA  . GLU A 1 271 ? -27.865 24.746  23.274  1.00 19.72 ?  271 GLU A CA  1 
ATOM   1883 C  C   . GLU A 1 271 ? -28.488 25.536  22.123  1.00 19.64 ?  271 GLU A C   1 
ATOM   1884 O  O   . GLU A 1 271 ? -29.154 26.549  22.364  1.00 19.87 ?  271 GLU A O   1 
ATOM   1885 C  CB  . GLU A 1 271 ? -26.441 25.234  23.567  1.00 18.99 ?  271 GLU A CB  1 
ATOM   1886 C  CG  . GLU A 1 271 ? -25.466 25.242  22.367  1.00 20.09 ?  271 GLU A CG  1 
ATOM   1887 C  CD  . GLU A 1 271 ? -24.744 23.898  22.140  1.00 18.99 ?  271 GLU A CD  1 
ATOM   1888 O  OE1 . GLU A 1 271 ? -25.216 22.851  22.627  1.00 18.51 ?  271 GLU A OE1 1 
ATOM   1889 O  OE2 . GLU A 1 271 ? -23.689 23.888  21.465  1.00 22.79 ?  271 GLU A OE2 1 
ATOM   1890 N  N   . LEU A 1 272 ? -28.333 25.052  20.878  1.00 16.13 ?  272 LEU A N   1 
ATOM   1891 C  CA  . LEU A 1 272 ? -28.920 25.715  19.707  1.00 18.61 ?  272 LEU A CA  1 
ATOM   1892 C  C   . LEU A 1 272 ? -30.442 25.680  19.746  1.00 17.79 ?  272 LEU A C   1 
ATOM   1893 O  O   . LEU A 1 272 ? -31.107 26.659  19.382  1.00 15.15 ?  272 LEU A O   1 
ATOM   1894 C  CB  . LEU A 1 272 ? -28.427 25.042  18.414  1.00 14.41 ?  272 LEU A CB  1 
ATOM   1895 C  CG  . LEU A 1 272 ? -26.911 24.972  18.185  1.00 14.54 ?  272 LEU A CG  1 
ATOM   1896 C  CD1 . LEU A 1 272 ? -26.607 24.229  16.864  1.00 16.06 ?  272 LEU A CD1 1 
ATOM   1897 C  CD2 . LEU A 1 272 ? -26.342 26.366  18.101  1.00 15.84 ?  272 LEU A CD2 1 
ATOM   1898 N  N   . ALA A 1 273 ? -31.004 24.538  20.137  1.00 15.37 ?  273 ALA A N   1 
ATOM   1899 C  CA  . ALA A 1 273 ? -32.445 24.415  20.274  1.00 18.02 ?  273 ALA A CA  1 
ATOM   1900 C  C   . ALA A 1 273 ? -32.957 25.303  21.407  1.00 20.70 ?  273 ALA A C   1 
ATOM   1901 O  O   . ALA A 1 273 ? -34.018 25.922  21.289  1.00 18.90 ?  273 ALA A O   1 
ATOM   1902 C  CB  . ALA A 1 273 ? -32.809 22.946  20.512  1.00 15.36 ?  273 ALA A CB  1 
ATOM   1903 N  N   . ASP A 1 274 ? -32.210 25.380  22.509  1.00 18.64 ?  274 ASP A N   1 
ATOM   1904 C  CA  . ASP A 1 274 ? -32.546 26.331  23.567  1.00 19.67 ?  274 ASP A CA  1 
ATOM   1905 C  C   . ASP A 1 274 ? -32.552 27.767  23.044  1.00 19.97 ?  274 ASP A C   1 
ATOM   1906 O  O   . ASP A 1 274 ? -33.404 28.568  23.436  1.00 19.97 ?  274 ASP A O   1 
ATOM   1907 C  CB  . ASP A 1 274 ? -31.568 26.179  24.735  1.00 18.28 ?  274 ASP A CB  1 
ATOM   1908 C  CG  . ASP A 1 274 ? -32.046 25.157  25.764  1.00 26.46 ?  274 ASP A CG  1 
ATOM   1909 O  OD1 . ASP A 1 274 ? -33.178 24.638  25.611  1.00 24.31 ?  274 ASP A OD1 1 
ATOM   1910 O  OD2 . ASP A 1 274 ? -31.296 24.888  26.730  1.00 23.50 ?  274 ASP A OD2 1 
ATOM   1911 N  N   . ARG A 1 275 ? -31.607 28.113  22.163  1.00 20.08 ?  275 ARG A N   1 
ATOM   1912 C  CA  . ARG A 1 275 ? -31.592 29.459  21.588  1.00 18.10 ?  275 ARG A CA  1 
ATOM   1913 C  C   . ARG A 1 275 ? -32.837 29.721  20.746  1.00 21.88 ?  275 ARG A C   1 
ATOM   1914 O  O   . ARG A 1 275 ? -33.430 30.808  20.813  1.00 19.80 ?  275 ARG A O   1 
ATOM   1915 C  CB  . ARG A 1 275 ? -30.338 29.661  20.737  1.00 20.35 ?  275 ARG A CB  1 
ATOM   1916 C  CG  . ARG A 1 275 ? -30.333 30.990  19.963  1.00 19.80 ?  275 ARG A CG  1 
ATOM   1917 C  CD  . ARG A 1 275 ? -30.079 32.195  20.880  1.00 20.87 ?  275 ARG A CD  1 
ATOM   1918 N  NE  . ARG A 1 275 ? -29.961 33.462  20.161  1.00 20.40 ?  275 ARG A NE  1 
ATOM   1919 C  CZ  . ARG A 1 275 ? -28.873 33.866  19.520  1.00 20.09 ?  275 ARG A CZ  1 
ATOM   1920 N  NH1 . ARG A 1 275 ? -27.831 33.066  19.354  1.00 18.35 ?  275 ARG A NH1 1 
ATOM   1921 N  NH2 . ARG A 1 275 ? -28.823 35.109  19.041  1.00 18.42 ?  275 ARG A NH2 1 
ATOM   1922 N  N   . LEU A 1 276 ? -33.254 28.732  19.952  1.00 17.29 ?  276 LEU A N   1 
ATOM   1923 C  CA  . LEU A 1 276 ? -34.411 28.921  19.090  1.00 18.58 ?  276 LEU A CA  1 
ATOM   1924 C  C   . LEU A 1 276 ? -35.693 29.010  19.902  1.00 20.58 ?  276 LEU A C   1 
ATOM   1925 O  O   . LEU A 1 276 ? -36.591 29.785  19.562  1.00 20.43 ?  276 LEU A O   1 
ATOM   1926 C  CB  . LEU A 1 276 ? -34.493 27.789  18.064  1.00 17.46 ?  276 LEU A CB  1 
ATOM   1927 C  CG  . LEU A 1 276 ? -33.373 27.858  17.014  1.00 19.09 ?  276 LEU A CG  1 
ATOM   1928 C  CD1 . LEU A 1 276 ? -33.341 26.572  16.183  1.00 17.30 ?  276 LEU A CD1 1 
ATOM   1929 C  CD2 . LEU A 1 276 ? -33.609 29.067  16.109  1.00 19.61 ?  276 LEU A CD2 1 
ATOM   1930 N  N   . ARG A 1 277 ? -35.786 28.244  20.990  1.00 17.43 ?  277 ARG A N   1 
ATOM   1931 C  CA  . ARG A 1 277 ? -36.922 28.386  21.891  1.00 19.63 ?  277 ARG A CA  1 
ATOM   1932 C  C   . ARG A 1 277 ? -36.941 29.765  22.544  1.00 21.37 ?  277 ARG A C   1 
ATOM   1933 O  O   . ARG A 1 277 ? -37.988 30.420  22.594  1.00 20.63 ?  277 ARG A O   1 
ATOM   1934 C  CB  . ARG A 1 277 ? -36.885 27.298  22.959  1.00 19.77 ?  277 ARG A CB  1 
ATOM   1935 C  CG  . ARG A 1 277 ? -37.647 26.028  22.604  1.00 21.62 ?  277 ARG A CG  1 
ATOM   1936 C  CD  . ARG A 1 277 ? -37.396 24.949  23.685  1.00 21.51 ?  277 ARG A CD  1 
ATOM   1937 N  NE  . ARG A 1 277 ? -36.994 23.738  23.001  1.00 34.25 ?  277 ARG A NE  1 
ATOM   1938 C  CZ  . ARG A 1 277 ? -35.787 23.201  22.990  1.00 25.69 ?  277 ARG A CZ  1 
ATOM   1939 N  NH1 . ARG A 1 277 ? -34.846 23.567  23.846  1.00 23.34 ?  277 ARG A NH1 1 
ATOM   1940 N  NH2 . ARG A 1 277 ? -35.520 22.266  22.094  1.00 26.37 ?  277 ARG A NH2 1 
ATOM   1941 N  N   . ALA A 1 278 ? -35.796 30.212  23.074  1.00 19.21 ?  278 ALA A N   1 
ATOM   1942 C  CA  . ALA A 1 278 ? -35.763 31.485  23.795  1.00 21.23 ?  278 ALA A CA  1 
ATOM   1943 C  C   . ALA A 1 278 ? -35.960 32.681  22.866  1.00 20.72 ?  278 ALA A C   1 
ATOM   1944 O  O   . ALA A 1 278 ? -36.477 33.714  23.298  1.00 26.55 ?  278 ALA A O   1 
ATOM   1945 C  CB  . ALA A 1 278 ? -34.446 31.633  24.563  1.00 17.69 ?  278 ALA A CB  1 
ATOM   1946 N  N   . GLU A 1 279 ? -35.581 32.566  21.594  1.00 22.53 ?  279 GLU A N   1 
ATOM   1947 C  CA  . GLU A 1 279 ? -35.578 33.703  20.672  1.00 22.82 ?  279 GLU A CA  1 
ATOM   1948 C  C   . GLU A 1 279 ? -35.998 33.235  19.286  1.00 21.83 ?  279 GLU A C   1 
ATOM   1949 O  O   . GLU A 1 279 ? -35.182 33.166  18.370  1.00 20.56 ?  279 GLU A O   1 
ATOM   1950 C  CB  . GLU A 1 279 ? -34.193 34.360  20.631  1.00 25.71 ?  279 GLU A CB  1 
ATOM   1951 C  CG  . GLU A 1 279 ? -34.173 35.704  19.911  1.00 27.14 ?  279 GLU A CG  1 
ATOM   1952 C  CD  . GLU A 1 279 ? -32.818 36.398  19.949  1.00 40.62 ?  279 GLU A CD  1 
ATOM   1953 O  OE1 . GLU A 1 279 ? -31.899 35.917  20.661  1.00 39.76 ?  279 GLU A OE1 1 
ATOM   1954 O  OE2 . GLU A 1 279 ? -32.697 37.455  19.289  1.00 39.38 ?  279 GLU A OE2 1 
ATOM   1955 N  N   . PRO A 1 280 ? -37.288 32.939  19.094  1.00 23.84 ?  280 PRO A N   1 
ATOM   1956 C  CA  . PRO A 1 280 ? -37.730 32.351  17.818  1.00 23.32 ?  280 PRO A CA  1 
ATOM   1957 C  C   . PRO A 1 280 ? -37.449 33.206  16.596  1.00 23.58 ?  280 PRO A C   1 
ATOM   1958 O  O   . PRO A 1 280 ? -37.348 32.660  15.493  1.00 22.94 ?  280 PRO A O   1 
ATOM   1959 C  CB  . PRO A 1 280 ? -39.245 32.157  18.011  1.00 23.88 ?  280 PRO A CB  1 
ATOM   1960 C  CG  . PRO A 1 280 ? -39.523 32.349  19.438  1.00 22.54 ?  280 PRO A CG  1 
ATOM   1961 C  CD  . PRO A 1 280 ? -38.360 33.002  20.108  1.00 24.11 ?  280 PRO A CD  1 
ATOM   1962 N  N   . ALA A 1 281 ? -37.337 34.528  16.744  1.00 22.32 ?  281 ALA A N   1 
ATOM   1963 C  CA  . ALA A 1 281 ? -37.053 35.390  15.604  1.00 22.11 ?  281 ALA A CA  1 
ATOM   1964 C  C   . ALA A 1 281 ? -35.659 35.177  15.026  1.00 25.99 ?  281 ALA A C   1 
ATOM   1965 O  O   . ALA A 1 281 ? -35.384 35.668  13.927  1.00 24.25 ?  281 ALA A O   1 
ATOM   1966 C  CB  . ALA A 1 281 ? -37.216 36.857  16.000  1.00 25.43 ?  281 ALA A CB  1 
ATOM   1967 N  N   . VAL A 1 282 ? -34.770 34.472  15.733  1.00 22.54 ?  282 VAL A N   1 
ATOM   1968 C  CA  . VAL A 1 282 ? -33.455 34.177  15.163  1.00 24.19 ?  282 VAL A CA  1 
ATOM   1969 C  C   . VAL A 1 282 ? -33.492 32.991  14.209  1.00 22.45 ?  282 VAL A C   1 
ATOM   1970 O  O   . VAL A 1 282 ? -32.436 32.569  13.713  1.00 20.87 ?  282 VAL A O   1 
ATOM   1971 C  CB  . VAL A 1 282 ? -32.436 33.952  16.307  1.00 25.78 ?  282 VAL A CB  1 
ATOM   1972 C  CG1 . VAL A 1 282 ? -32.802 32.754  17.150  1.00 24.18 ?  282 VAL A CG1 1 
ATOM   1973 C  CG2 . VAL A 1 282 ? -31.010 33.818  15.771  1.00 30.75 ?  282 VAL A CG2 1 
ATOM   1974 N  N   . ILE A 1 283 ? -34.677 32.428  13.930  1.00 19.53 ?  283 ILE A N   1 
ATOM   1975 C  CA  . ILE A 1 283 ? -34.726 31.216  13.108  1.00 17.76 ?  283 ILE A CA  1 
ATOM   1976 C  C   . ILE A 1 283 ? -34.119 31.467  11.724  1.00 19.78 ?  283 ILE A C   1 
ATOM   1977 O  O   . ILE A 1 283 ? -33.483 30.578  11.150  1.00 22.84 ?  283 ILE A O   1 
ATOM   1978 C  CB  . ILE A 1 283 ? -36.176 30.683  13.012  1.00 22.14 ?  283 ILE A CB  1 
ATOM   1979 C  CG1 . ILE A 1 283 ? -36.225 29.277  12.391  1.00 20.07 ?  283 ILE A CG1 1 
ATOM   1980 C  CG2 . ILE A 1 283 ? -37.055 31.626  12.170  1.00 22.82 ?  283 ILE A CG2 1 
ATOM   1981 C  CD1 . ILE A 1 283 ? -35.576 28.142  13.208  1.00 15.50 ?  283 ILE A CD1 1 
ATOM   1982 N  N   . GLY A 1 284 ? -34.276 32.675  11.178  1.00 20.61 ?  284 GLY A N   1 
ATOM   1983 C  CA  . GLY A 1 284 ? -33.745 32.948  9.850   1.00 23.13 ?  284 GLY A CA  1 
ATOM   1984 C  C   . GLY A 1 284 ? -32.224 32.936  9.816   1.00 22.71 ?  284 GLY A C   1 
ATOM   1985 O  O   . GLY A 1 284 ? -31.614 32.304  8.945   1.00 20.48 ?  284 GLY A O   1 
ATOM   1986 N  N   . ARG A 1 285 ? -31.593 33.651  10.751  1.00 18.29 ?  285 ARG A N   1 
ATOM   1987 C  CA  . ARG A 1 285 ? -30.136 33.623  10.845  1.00 21.33 ?  285 ARG A CA  1 
ATOM   1988 C  C   . ARG A 1 285 ? -29.641 32.223  11.158  1.00 19.75 ?  285 ARG A C   1 
ATOM   1989 O  O   . ARG A 1 285 ? -28.623 31.783  10.609  1.00 21.28 ?  285 ARG A O   1 
ATOM   1990 C  CB  . ARG A 1 285 ? -29.646 34.595  11.930  1.00 28.53 ?  285 ARG A CB  1 
ATOM   1991 C  CG  . ARG A 1 285 ? -29.321 36.010  11.483  1.00 32.80 ?  285 ARG A CG  1 
ATOM   1992 C  CD  . ARG A 1 285 ? -28.394 36.681  12.526  1.00 39.16 ?  285 ARG A CD  1 
ATOM   1993 N  NE  . ARG A 1 285 ? -29.055 36.737  13.828  1.00 46.20 ?  285 ARG A NE  1 
ATOM   1994 C  CZ  . ARG A 1 285 ? -28.535 37.243  14.945  1.00 47.99 ?  285 ARG A CZ  1 
ATOM   1995 N  NH1 . ARG A 1 285 ? -27.307 37.743  14.984  1.00 46.35 ?  285 ARG A NH1 1 
ATOM   1996 N  NH2 . ARG A 1 285 ? -29.270 37.253  16.054  1.00 46.21 ?  285 ARG A NH2 1 
ATOM   1997 N  N   . ALA A 1 286 ? -30.324 31.532  12.078  1.00 18.66 ?  286 ALA A N   1 
ATOM   1998 C  CA  . ALA A 1 286 ? -29.929 30.177  12.462  1.00 21.32 ?  286 ALA A CA  1 
ATOM   1999 C  C   . ALA A 1 286 ? -29.868 29.266  11.245  1.00 18.11 ?  286 ALA A C   1 
ATOM   2000 O  O   . ALA A 1 286 ? -28.865 28.580  11.020  1.00 19.72 ?  286 ALA A O   1 
ATOM   2001 C  CB  . ALA A 1 286 ? -30.907 29.606  13.498  1.00 19.37 ?  286 ALA A CB  1 
ATOM   2002 N  N   . VAL A 1 287 ? -30.934 29.264  10.441  1.00 19.77 ?  287 VAL A N   1 
ATOM   2003 C  CA  . VAL A 1 287 ? -30.975 28.437  9.233   1.00 19.17 ?  287 VAL A CA  1 
ATOM   2004 C  C   . VAL A 1 287 ? -29.907 28.867  8.234   1.00 18.64 ?  287 VAL A C   1 
ATOM   2005 O  O   . VAL A 1 287 ? -29.318 28.025  7.536   1.00 17.60 ?  287 VAL A O   1 
ATOM   2006 C  CB  . VAL A 1 287 ? -32.378 28.471  8.601   1.00 19.04 ?  287 VAL A CB  1 
ATOM   2007 C  CG1 . VAL A 1 287 ? -32.318 27.941  7.155   1.00 21.83 ?  287 VAL A CG1 1 
ATOM   2008 C  CG2 . VAL A 1 287 ? -33.350 27.632  9.437   1.00 21.34 ?  287 VAL A CG2 1 
ATOM   2009 N  N   . ASP A 1 288 ? -29.652 30.180  8.125   1.00 17.30 ?  288 ASP A N   1 
ATOM   2010 C  CA  . ASP A 1 288 ? -28.552 30.634  7.276   1.00 18.38 ?  288 ASP A CA  1 
ATOM   2011 C  C   . ASP A 1 288 ? -27.238 29.988  7.707   1.00 19.57 ?  288 ASP A C   1 
ATOM   2012 O  O   . ASP A 1 288 ? -26.442 29.542  6.866   1.00 19.54 ?  288 ASP A O   1 
ATOM   2013 C  CB  . ASP A 1 288 ? -28.440 32.163  7.317   1.00 20.06 ?  288 ASP A CB  1 
ATOM   2014 C  CG  . ASP A 1 288 ? -27.813 32.732  6.059   1.00 25.84 ?  288 ASP A CG  1 
ATOM   2015 O  OD1 . ASP A 1 288 ? -28.123 32.227  4.952   1.00 22.04 ?  288 ASP A OD1 1 
ATOM   2016 O  OD2 . ASP A 1 288 ? -27.001 33.682  6.178   1.00 28.09 ?  288 ASP A OD2 1 
ATOM   2017 N  N   . GLU A 1 289 ? -27.010 29.892  9.012   1.00 15.74 ?  289 GLU A N   1 
ATOM   2018 C  CA  . GLU A 1 289 ? -25.759 29.312  9.486   1.00 17.18 ?  289 GLU A CA  1 
ATOM   2019 C  C   . GLU A 1 289 ? -25.763 27.794  9.335   1.00 19.43 ?  289 GLU A C   1 
ATOM   2020 O  O   . GLU A 1 289 ? -24.754 27.204  8.924   1.00 17.96 ?  289 GLU A O   1 
ATOM   2021 C  CB  . GLU A 1 289 ? -25.512 29.732  10.942  1.00 17.11 ?  289 GLU A CB  1 
ATOM   2022 C  CG  . GLU A 1 289 ? -24.418 28.946  11.671  1.00 15.72 ?  289 GLU A CG  1 
ATOM   2023 C  CD  . GLU A 1 289 ? -23.020 29.267  11.155  1.00 18.17 ?  289 GLU A CD  1 
ATOM   2024 O  OE1 . GLU A 1 289 ? -22.874 29.868  10.052  1.00 14.10 ?  289 GLU A OE1 1 
ATOM   2025 O  OE2 . GLU A 1 289 ? -22.068 28.903  11.867  1.00 17.60 ?  289 GLU A OE2 1 
ATOM   2026 N  N   . LEU A 1 290 ? -26.897 27.145  9.628   1.00 17.88 ?  290 LEU A N   1 
ATOM   2027 C  CA  . LEU A 1 290 ? -26.996 25.711  9.380   1.00 18.72 ?  290 LEU A CA  1 
ATOM   2028 C  C   . LEU A 1 290 ? -26.770 25.392  7.900   1.00 18.60 ?  290 LEU A C   1 
ATOM   2029 O  O   . LEU A 1 290 ? -26.201 24.341  7.564   1.00 18.51 ?  290 LEU A O   1 
ATOM   2030 C  CB  . LEU A 1 290 ? -28.361 25.198  9.863   1.00 16.82 ?  290 LEU A CB  1 
ATOM   2031 C  CG  . LEU A 1 290 ? -28.573 25.358  11.380  1.00 18.61 ?  290 LEU A CG  1 
ATOM   2032 C  CD1 . LEU A 1 290 ? -30.001 24.983  11.880  1.00 17.77 ?  290 LEU A CD1 1 
ATOM   2033 C  CD2 . LEU A 1 290 ? -27.517 24.572  12.153  1.00 20.58 ?  290 LEU A CD2 1 
ATOM   2034 N  N   . LEU A 1 291 ? -27.169 26.302  7.004   1.00 19.54 ?  291 LEU A N   1 
ATOM   2035 C  CA  . LEU A 1 291 ? -26.940 26.090  5.577   1.00 19.95 ?  291 LEU A CA  1 
ATOM   2036 C  C   . LEU A 1 291 ? -25.450 26.119  5.266   1.00 19.05 ?  291 LEU A C   1 
ATOM   2037 O  O   . LEU A 1 291 ? -24.931 25.240  4.567   1.00 17.51 ?  291 LEU A O   1 
ATOM   2038 C  CB  . LEU A 1 291 ? -27.702 27.141  4.759   1.00 18.27 ?  291 LEU A CB  1 
ATOM   2039 C  CG  . LEU A 1 291 ? -29.179 26.834  4.454   1.00 19.84 ?  291 LEU A CG  1 
ATOM   2040 C  CD1 . LEU A 1 291 ? -29.921 28.119  4.081   1.00 20.91 ?  291 LEU A CD1 1 
ATOM   2041 C  CD2 . LEU A 1 291 ? -29.318 25.780  3.329   1.00 15.66 ?  291 LEU A CD2 1 
ATOM   2042 N  N   . ARG A 1 292 ? -24.732 27.101  5.817   1.00 18.55 ?  292 ARG A N   1 
ATOM   2043 C  CA  . ARG A 1 292 ? -23.286 27.122  5.632   1.00 18.12 ?  292 ARG A CA  1 
ATOM   2044 C  C   . ARG A 1 292 ? -22.664 25.830  6.130   1.00 18.56 ?  292 ARG A C   1 
ATOM   2045 O  O   . ARG A 1 292 ? -21.799 25.243  5.470   1.00 20.50 ?  292 ARG A O   1 
ATOM   2046 C  CB  . ARG A 1 292 ? -22.650 28.298  6.377   1.00 19.12 ?  292 ARG A CB  1 
ATOM   2047 C  CG  . ARG A 1 292 ? -21.116 28.279  6.246   1.00 17.28 ?  292 ARG A CG  1 
ATOM   2048 C  CD  . ARG A 1 292 ? -20.447 29.222  7.232   1.00 19.05 ?  292 ARG A CD  1 
ATOM   2049 N  NE  . ARG A 1 292 ? -20.608 28.778  8.611   1.00 18.30 ?  292 ARG A NE  1 
ATOM   2050 C  CZ  . ARG A 1 292 ? -19.785 27.943  9.229   1.00 18.96 ?  292 ARG A CZ  1 
ATOM   2051 N  NH1 . ARG A 1 292 ? -18.717 27.450  8.617   1.00 20.78 ?  292 ARG A NH1 1 
ATOM   2052 N  NH2 . ARG A 1 292 ? -20.036 27.596  10.491  1.00 14.87 ?  292 ARG A NH2 1 
ATOM   2053 N  N   . TYR A 1 293 ? -23.085 25.390  7.314   1.00 17.87 ?  293 TYR A N   1 
ATOM   2054 C  CA  . TYR A 1 293 ? -22.486 24.236  7.972   1.00 16.81 ?  293 TYR A CA  1 
ATOM   2055 C  C   . TYR A 1 293 ? -22.793 22.930  7.255   1.00 19.19 ?  293 TYR A C   1 
ATOM   2056 O  O   . TYR A 1 293 ? -21.989 21.992  7.314   1.00 21.58 ?  293 TYR A O   1 
ATOM   2057 C  CB  . TYR A 1 293 ? -23.013 24.155  9.399   1.00 19.68 ?  293 TYR A CB  1 
ATOM   2058 C  CG  . TYR A 1 293 ? -22.131 23.421  10.376  1.00 19.26 ?  293 TYR A CG  1 
ATOM   2059 C  CD1 . TYR A 1 293 ? -20.924 23.958  10.764  1.00 15.32 ?  293 TYR A CD1 1 
ATOM   2060 C  CD2 . TYR A 1 293 ? -22.540 22.219  10.958  1.00 19.78 ?  293 TYR A CD2 1 
ATOM   2061 C  CE1 . TYR A 1 293 ? -20.122 23.325  11.671  1.00 18.05 ?  293 TYR A CE1 1 
ATOM   2062 C  CE2 . TYR A 1 293 ? -21.723 21.563  11.881  1.00 21.05 ?  293 TYR A CE2 1 
ATOM   2063 C  CZ  . TYR A 1 293 ? -20.518 22.137  12.229  1.00 19.86 ?  293 TYR A CZ  1 
ATOM   2064 O  OH  . TYR A 1 293 ? -19.672 21.536  13.138  1.00 26.15 ?  293 TYR A OH  1 
ATOM   2065 N  N   . ASN A 1 294 ? -23.948 22.845  6.596   1.00 17.99 ?  294 ASN A N   1 
ATOM   2066 C  CA  . ASN A 1 294 ? -24.524 21.549  6.264   1.00 19.11 ?  294 ASN A CA  1 
ATOM   2067 C  C   . ASN A 1 294 ? -23.723 20.863  5.168   1.00 17.68 ?  294 ASN A C   1 
ATOM   2068 O  O   . ASN A 1 294 ? -23.216 21.509  4.248   1.00 15.70 ?  294 ASN A O   1 
ATOM   2069 C  CB  . ASN A 1 294 ? -25.998 21.707  5.841   1.00 17.36 ?  294 ASN A CB  1 
ATOM   2070 C  CG  . ASN A 1 294 ? -26.156 22.521  4.569   1.00 19.93 ?  294 ASN A CG  1 
ATOM   2071 O  OD1 . ASN A 1 294 ? -25.313 22.462  3.676   1.00 22.06 ?  294 ASN A OD1 1 
ATOM   2072 N  ND2 . ASN A 1 294 ? -27.237 23.287  4.480   1.00 17.63 ?  294 ASN A ND2 1 
ATOM   2073 N  N   . LEU A 1 295 ? -23.621 19.533  5.279   1.00 19.15 ?  295 LEU A N   1 
ATOM   2074 C  CA  . LEU A 1 295 ? -22.825 18.701  4.389   1.00 17.48 ?  295 LEU A CA  1 
ATOM   2075 C  C   . LEU A 1 295 ? -23.693 17.856  3.464   1.00 17.91 ?  295 LEU A C   1 
ATOM   2076 O  O   . LEU A 1 295 ? -23.257 16.809  2.989   1.00 17.63 ?  295 LEU A O   1 
ATOM   2077 C  CB  . LEU A 1 295 ? -21.891 17.816  5.209   1.00 16.35 ?  295 LEU A CB  1 
ATOM   2078 C  CG  . LEU A 1 295 ? -20.906 18.617  6.062   1.00 18.96 ?  295 LEU A CG  1 
ATOM   2079 C  CD1 . LEU A 1 295 ? -20.037 17.717  6.940   1.00 15.51 ?  295 LEU A CD1 1 
ATOM   2080 C  CD2 . LEU A 1 295 ? -20.052 19.470  5.165   1.00 16.66 ?  295 LEU A CD2 1 
ATOM   2081 N  N   . SER A 1 296 ? -24.920 18.312  3.182   1.00 19.70 ?  296 SER A N   1 
ATOM   2082 C  CA  . SER A 1 296 ? -25.858 17.493  2.418   1.00 15.78 ?  296 SER A CA  1 
ATOM   2083 C  C   . SER A 1 296 ? -25.428 17.345  0.958   1.00 16.61 ?  296 SER A C   1 
ATOM   2084 O  O   . SER A 1 296 ? -25.683 16.302  0.346   1.00 18.68 ?  296 SER A O   1 
ATOM   2085 C  CB  . SER A 1 296 ? -27.271 18.083  2.513   1.00 16.80 ?  296 SER A CB  1 
ATOM   2086 O  OG  . SER A 1 296 ? -27.368 19.297  1.765   1.00 14.76 ?  296 SER A OG  1 
ATOM   2087 N  N   . ILE A 1 297 ? -24.750 18.342  0.394   1.00 17.38 ?  297 ILE A N   1 
ATOM   2088 C  CA  . ILE A 1 297 ? -24.203 18.198  -0.957  1.00 18.28 ?  297 ILE A CA  1 
ATOM   2089 C  C   . ILE A 1 297 ? -23.061 17.188  -0.886  1.00 18.22 ?  297 ILE A C   1 
ATOM   2090 O  O   . ILE A 1 297 ? -22.008 17.470  -0.307  1.00 19.32 ?  297 ILE A O   1 
ATOM   2091 C  CB  . ILE A 1 297 ? -23.724 19.536  -1.534  1.00 19.51 ?  297 ILE A CB  1 
ATOM   2092 C  CG1 . ILE A 1 297 ? -24.868 20.533  -1.645  1.00 18.12 ?  297 ILE A CG1 1 
ATOM   2093 C  CG2 . ILE A 1 297 ? -23.071 19.344  -2.932  1.00 17.43 ?  297 ILE A CG2 1 
ATOM   2094 C  CD1 . ILE A 1 297 ? -24.398 21.929  -2.096  1.00 18.07 ?  297 ILE A CD1 1 
ATOM   2095 N  N   . GLY A 1 298 ? -23.276 16.003  -1.450  1.00 15.82 ?  298 GLY A N   1 
ATOM   2096 C  CA  . GLY A 1 298 ? -22.336 14.905  -1.358  1.00 16.61 ?  298 GLY A CA  1 
ATOM   2097 C  C   . GLY A 1 298 ? -21.433 14.718  -2.565  1.00 22.76 ?  298 GLY A C   1 
ATOM   2098 O  O   . GLY A 1 298 ? -20.579 13.824  -2.555  1.00 20.60 ?  298 GLY A O   1 
ATOM   2099 N  N   . ASP A 1 299 ? -21.621 15.521  -3.611  1.00 18.36 ?  299 ASP A N   1 
ATOM   2100 C  CA  . ASP A 1 299 ? -20.739 15.581  -4.772  1.00 21.75 ?  299 ASP A CA  1 
ATOM   2101 C  C   . ASP A 1 299 ? -20.298 17.037  -4.816  1.00 20.58 ?  299 ASP A C   1 
ATOM   2102 O  O   . ASP A 1 299 ? -20.496 17.773  -3.846  1.00 22.45 ?  299 ASP A O   1 
ATOM   2103 C  CB  . ASP A 1 299 ? -21.510 15.291  -6.070  1.00 17.16 ?  299 ASP A CB  1 
ATOM   2104 C  CG  . ASP A 1 299 ? -22.644 16.294  -6.324  1.00 23.00 ?  299 ASP A CG  1 
ATOM   2105 O  OD1 . ASP A 1 299 ? -23.039 16.994  -5.365  1.00 22.26 ?  299 ASP A OD1 1 
ATOM   2106 O  OD2 . ASP A 1 299 ? -23.141 16.381  -7.481  1.00 20.75 ?  299 ASP A OD2 1 
ATOM   2107 N  N   . ALA A 1 300 ? -19.722 17.465  -5.930  1.00 20.15 ?  300 ALA A N   1 
ATOM   2108 C  CA  . ALA A 1 300 ? -19.413 18.866  -6.153  1.00 19.99 ?  300 ALA A CA  1 
ATOM   2109 C  C   . ALA A 1 300 ? -20.193 19.447  -7.316  1.00 19.77 ?  300 ALA A C   1 
ATOM   2110 O  O   . ALA A 1 300 ? -20.784 18.708  -8.107  1.00 19.92 ?  300 ALA A O   1 
ATOM   2111 C  CB  . ALA A 1 300 ? -17.908 18.965  -6.413  1.00 18.57 ?  300 ALA A CB  1 
ATOM   2112 N  N   . LEU A 1 301 ? -20.195 20.774  -7.422  1.00 15.18 ?  301 LEU A N   1 
ATOM   2113 C  CA  . LEU A 1 301 ? -20.908 21.421  -8.524  1.00 16.23 ?  301 LEU A CA  1 
ATOM   2114 C  C   . LEU A 1 301 ? -20.060 21.329  -9.787  1.00 17.35 ?  301 LEU A C   1 
ATOM   2115 O  O   . LEU A 1 301 ? -18.932 21.837  -9.803  1.00 18.65 ?  301 LEU A O   1 
ATOM   2116 C  CB  . LEU A 1 301 ? -21.226 22.884  -8.198  1.00 15.41 ?  301 LEU A CB  1 
ATOM   2117 C  CG  . LEU A 1 301 ? -21.910 23.162  -6.849  1.00 20.38 ?  301 LEU A CG  1 
ATOM   2118 C  CD1 . LEU A 1 301 ? -22.498 24.570  -6.812  1.00 20.02 ?  301 LEU A CD1 1 
ATOM   2119 C  CD2 . LEU A 1 301 ? -22.991 22.121  -6.499  1.00 20.62 ?  301 LEU A CD2 1 
ATOM   2120 N  N   . PRO A 1 302 ? -20.541 20.681  -10.845 1.00 19.88 ?  302 PRO A N   1 
ATOM   2121 C  CA  . PRO A 1 302 ? -19.688 20.424  -12.011 1.00 19.02 ?  302 PRO A CA  1 
ATOM   2122 C  C   . PRO A 1 302 ? -19.761 21.530  -13.055 1.00 20.88 ?  302 PRO A C   1 
ATOM   2123 O  O   . PRO A 1 302 ? -20.809 22.135  -13.291 1.00 16.27 ?  302 PRO A O   1 
ATOM   2124 C  CB  . PRO A 1 302 ? -20.274 19.125  -12.574 1.00 16.62 ?  302 PRO A CB  1 
ATOM   2125 C  CG  . PRO A 1 302 ? -21.779 19.249  -12.265 1.00 21.60 ?  302 PRO A CG  1 
ATOM   2126 C  CD  . PRO A 1 302 ? -21.889 20.083  -10.992 1.00 20.91 ?  302 PRO A CD  1 
ATOM   2127 N  N   . ARG A 1 303 ? -18.619 21.787  -13.689 1.00 17.07 ?  303 ARG A N   1 
ATOM   2128 C  CA  . ARG A 1 303 ? -18.541 22.674  -14.842 1.00 16.71 ?  303 ARG A CA  1 
ATOM   2129 C  C   . ARG A 1 303 ? -17.521 22.103  -15.824 1.00 18.43 ?  303 ARG A C   1 
ATOM   2130 O  O   . ARG A 1 303 ? -16.540 21.462  -15.422 1.00 17.46 ?  303 ARG A O   1 
ATOM   2131 C  CB  . ARG A 1 303 ? -18.139 24.114  -14.450 1.00 20.74 ?  303 ARG A CB  1 
ATOM   2132 C  CG  . ARG A 1 303 ? -19.005 24.795  -13.367 1.00 17.11 ?  303 ARG A CG  1 
ATOM   2133 C  CD  . ARG A 1 303 ? -20.375 25.195  -13.919 1.00 17.98 ?  303 ARG A CD  1 
ATOM   2134 N  NE  . ARG A 1 303 ? -21.143 26.052  -13.016 1.00 19.59 ?  303 ARG A NE  1 
ATOM   2135 C  CZ  . ARG A 1 303 ? -22.023 25.622  -12.119 1.00 20.04 ?  303 ARG A CZ  1 
ATOM   2136 N  NH1 . ARG A 1 303 ? -22.190 24.325  -11.872 1.00 14.70 ?  303 ARG A NH1 1 
ATOM   2137 N  NH2 . ARG A 1 303 ? -22.767 26.516  -11.460 1.00 19.19 ?  303 ARG A NH2 1 
ATOM   2138 N  N   . ILE A 1 304 ? -17.778 22.313  -17.113 1.00 18.75 ?  304 ILE A N   1 
ATOM   2139 C  CA  . ILE A 1 304 ? -16.797 22.081  -18.171 1.00 17.95 ?  304 ILE A CA  1 
ATOM   2140 C  C   . ILE A 1 304 ? -16.210 23.427  -18.585 1.00 20.53 ?  304 ILE A C   1 
ATOM   2141 O  O   . ILE A 1 304 ? -16.948 24.373  -18.877 1.00 22.30 ?  304 ILE A O   1 
ATOM   2142 C  CB  . ILE A 1 304 ? -17.419 21.373  -19.386 1.00 19.79 ?  304 ILE A CB  1 
ATOM   2143 C  CG1 . ILE A 1 304 ? -18.056 20.028  -18.998 1.00 24.13 ?  304 ILE A CG1 1 
ATOM   2144 C  CG2 . ILE A 1 304 ? -16.364 21.215  -20.521 1.00 24.14 ?  304 ILE A CG2 1 
ATOM   2145 C  CD1 . ILE A 1 304 ? -17.079 18.956  -18.511 1.00 18.92 ?  304 ILE A CD1 1 
ATOM   2146 N  N   . ALA A 1 305 ? -14.885 23.515  -18.611 1.00 23.15 ?  305 ALA A N   1 
ATOM   2147 C  CA  . ALA A 1 305 ? -14.221 24.730  -19.066 1.00 24.73 ?  305 ALA A CA  1 
ATOM   2148 C  C   . ALA A 1 305 ? -14.418 24.921  -20.568 1.00 25.81 ?  305 ALA A C   1 
ATOM   2149 O  O   . ALA A 1 305 ? -14.095 24.034  -21.364 1.00 19.53 ?  305 ALA A O   1 
ATOM   2150 C  CB  . ALA A 1 305 ? -12.735 24.665  -18.735 1.00 22.70 ?  305 ALA A CB  1 
ATOM   2151 N  N   . LEU A 1 306 ? -14.951 26.085  -20.958 1.00 23.31 ?  306 LEU A N   1 
ATOM   2152 C  CA  . LEU A 1 306 ? -15.145 26.388  -22.372 1.00 25.00 ?  306 LEU A CA  1 
ATOM   2153 C  C   . LEU A 1 306 ? -13.914 27.006  -23.007 1.00 25.36 ?  306 LEU A C   1 
ATOM   2154 O  O   . LEU A 1 306 ? -13.803 27.018  -24.235 1.00 30.31 ?  306 LEU A O   1 
ATOM   2155 C  CB  . LEU A 1 306 ? -16.337 27.332  -22.562 1.00 22.73 ?  306 LEU A CB  1 
ATOM   2156 C  CG  . LEU A 1 306 ? -17.691 26.831  -22.064 1.00 26.13 ?  306 LEU A CG  1 
ATOM   2157 C  CD1 . LEU A 1 306 ? -18.759 27.870  -22.363 1.00 29.10 ?  306 LEU A CD1 1 
ATOM   2158 C  CD2 . LEU A 1 306 ? -18.052 25.481  -22.687 1.00 26.55 ?  306 LEU A CD2 1 
ATOM   2159 N  N   . ALA A 1 307 ? -13.006 27.532  -22.198 1.00 26.43 ?  307 ALA A N   1 
ATOM   2160 C  CA  . ALA A 1 307 ? -11.755 28.082  -22.675 1.00 26.47 ?  307 ALA A CA  1 
ATOM   2161 C  C   . ALA A 1 307 ? -10.724 27.787  -21.606 1.00 27.76 ?  307 ALA A C   1 
ATOM   2162 O  O   . ALA A 1 307 ? -11.071 27.378  -20.497 1.00 25.05 ?  307 ALA A O   1 
ATOM   2163 C  CB  . ALA A 1 307 ? -11.871 29.588  -22.957 1.00 28.17 ?  307 ALA A CB  1 
ATOM   2164 N  N   . ASP A 1 308 ? -9.450  27.978  -21.948 1.00 26.76 ?  308 ASP A N   1 
ATOM   2165 C  CA  . ASP A 1 308 ? -8.394  27.845  -20.956 1.00 28.85 ?  308 ASP A CA  1 
ATOM   2166 C  C   . ASP A 1 308 ? -8.520  28.982  -19.957 1.00 28.55 ?  308 ASP A C   1 
ATOM   2167 O  O   . ASP A 1 308 ? -8.757  30.130  -20.336 1.00 25.40 ?  308 ASP A O   1 
ATOM   2168 C  CB  . ASP A 1 308 ? -7.012  27.890  -21.603 1.00 33.03 ?  308 ASP A CB  1 
ATOM   2169 C  CG  . ASP A 1 308 ? -6.877  26.941  -22.771 1.00 34.04 ?  308 ASP A CG  1 
ATOM   2170 O  OD1 . ASP A 1 308 ? -6.885  25.719  -22.586 1.00 33.90 ?  308 ASP A OD1 1 
ATOM   2171 O  OD2 . ASP A 1 308 ? -6.787  27.436  -23.903 1.00 46.93 ?  308 ASP A OD2 1 
ATOM   2172 N  N   . VAL A 1 309 ? -8.365  28.668  -18.676 1.00 26.19 ?  309 VAL A N   1 
ATOM   2173 C  CA  . VAL A 1 309 ? -8.574  29.646  -17.613 1.00 27.52 ?  309 VAL A CA  1 
ATOM   2174 C  C   . VAL A 1 309 ? -7.541  29.414  -16.525 1.00 24.55 ?  309 VAL A C   1 
ATOM   2175 O  O   . VAL A 1 309 ? -7.353  28.284  -16.071 1.00 25.58 ?  309 VAL A O   1 
ATOM   2176 C  CB  . VAL A 1 309 ? -10.000 29.563  -17.032 1.00 24.52 ?  309 VAL A CB  1 
ATOM   2177 C  CG1 . VAL A 1 309 ? -10.124 30.435  -15.786 1.00 24.96 ?  309 VAL A CG1 1 
ATOM   2178 C  CG2 . VAL A 1 309 ? -11.021 29.970  -18.072 1.00 24.59 ?  309 VAL A CG2 1 
ATOM   2179 N  N   . ARG A 1 310 ? -6.856  30.474  -16.117 1.00 30.25 ?  310 ARG A N   1 
ATOM   2180 C  CA  . ARG A 1 310 ? -5.931  30.399  -14.994 1.00 25.65 ?  310 ARG A CA  1 
ATOM   2181 C  C   . ARG A 1 310 ? -6.733  30.592  -13.714 1.00 28.94 ?  310 ARG A C   1 
ATOM   2182 O  O   . ARG A 1 310 ? -7.242  31.688  -13.457 1.00 29.46 ?  310 ARG A O   1 
ATOM   2183 C  CB  . ARG A 1 310 ? -4.830  31.446  -15.110 1.00 30.11 ?  310 ARG A CB  1 
ATOM   2184 C  CG  . ARG A 1 310 ? -3.780  31.289  -14.038 1.00 32.66 ?  310 ARG A CG  1 
ATOM   2185 C  CD  . ARG A 1 310 ? -2.494  31.980  -14.458 1.00 45.82 ?  310 ARG A CD  1 
ATOM   2186 N  NE  . ARG A 1 310 ? -1.629  31.161  -15.307 1.00 42.27 ?  310 ARG A NE  1 
ATOM   2187 C  CZ  . ARG A 1 310 ? -1.023  30.042  -14.932 1.00 40.06 ?  310 ARG A CZ  1 
ATOM   2188 N  NH1 . ARG A 1 310 ? -1.173  29.543  -13.717 1.00 44.49 ?  310 ARG A NH1 1 
ATOM   2189 N  NH2 . ARG A 1 310 ? -0.224  29.420  -15.793 1.00 41.35 ?  310 ARG A NH2 1 
ATOM   2190 N  N   . LEU A 1 311 ? -6.855  29.527  -12.922 1.00 23.35 ?  311 LEU A N   1 
ATOM   2191 C  CA  . LEU A 1 311 ? -7.599  29.546  -11.670 1.00 22.36 ?  311 LEU A CA  1 
ATOM   2192 C  C   . LEU A 1 311 ? -6.628  29.241  -10.546 1.00 26.72 ?  311 LEU A C   1 
ATOM   2193 O  O   . LEU A 1 311 ? -6.062  28.139  -10.494 1.00 24.23 ?  311 LEU A O   1 
ATOM   2194 C  CB  . LEU A 1 311 ? -8.742  28.526  -11.682 1.00 24.35 ?  311 LEU A CB  1 
ATOM   2195 C  CG  . LEU A 1 311 ? -9.606  28.485  -10.421 1.00 25.92 ?  311 LEU A CG  1 
ATOM   2196 C  CD1 . LEU A 1 311 ? -10.616 29.643  -10.432 1.00 25.76 ?  311 LEU A CD1 1 
ATOM   2197 C  CD2 . LEU A 1 311 ? -10.315 27.119  -10.284 1.00 22.13 ?  311 LEU A CD2 1 
ATOM   2198 N  N   . GLY A 1 312 ? -6.449  30.207  -9.643  1.00 23.08 ?  312 GLY A N   1 
ATOM   2199 C  CA  . GLY A 1 312 ? -5.391  30.068  -8.660  1.00 26.35 ?  312 GLY A CA  1 
ATOM   2200 C  C   . GLY A 1 312 ? -4.132  29.841  -9.461  1.00 29.66 ?  312 GLY A C   1 
ATOM   2201 O  O   . GLY A 1 312 ? -3.947  30.420  -10.535 1.00 26.14 ?  312 GLY A O   1 
ATOM   2202 N  N   . GLU A 1 313 ? -3.281  28.944  -8.977  1.00 28.05 ?  313 GLU A N   1 
ATOM   2203 C  CA  . GLU A 1 313 ? -2.050  28.597  -9.669  1.00 34.46 ?  313 GLU A CA  1 
ATOM   2204 C  C   . GLU A 1 313 ? -2.192  27.646  -10.848 1.00 34.40 ?  313 GLU A C   1 
ATOM   2205 O  O   . GLU A 1 313 ? -1.190  27.339  -11.504 1.00 30.44 ?  313 GLU A O   1 
ATOM   2206 C  CB  . GLU A 1 313 ? -1.076  28.007  -8.645  1.00 34.38 ?  313 GLU A CB  1 
ATOM   2207 C  CG  . GLU A 1 313 ? -0.839  28.934  -7.467  1.00 45.02 ?  313 GLU A CG  1 
ATOM   2208 C  CD  . GLU A 1 313 ? 0.279   28.452  -6.572  1.00 55.59 ?  313 GLU A CD  1 
ATOM   2209 O  OE1 . GLU A 1 313 ? 0.964   29.303  -5.958  1.00 55.49 ?  313 GLU A OE1 1 
ATOM   2210 O  OE2 . GLU A 1 313 ? 0.470   27.216  -6.491  1.00 59.62 ?  313 GLU A OE2 1 
ATOM   2211 N  N   . VAL A 1 314 ? -3.399  27.172  -11.140 1.00 28.13 ?  314 VAL A N   1 
ATOM   2212 C  CA  . VAL A 1 314 ? -3.599  26.084  -12.092 1.00 27.82 ?  314 VAL A CA  1 
ATOM   2213 C  C   . VAL A 1 314 ? -4.146  26.646  -13.396 1.00 24.84 ?  314 VAL A C   1 
ATOM   2214 O  O   . VAL A 1 314 ? -5.145  27.381  -13.400 1.00 26.34 ?  314 VAL A O   1 
ATOM   2215 C  CB  . VAL A 1 314 ? -4.541  25.009  -11.522 1.00 29.81 ?  314 VAL A CB  1 
ATOM   2216 C  CG1 . VAL A 1 314 ? -4.926  23.995  -12.605 1.00 23.33 ?  314 VAL A CG1 1 
ATOM   2217 C  CG2 . VAL A 1 314 ? -3.894  24.312  -10.345 1.00 25.48 ?  314 VAL A CG2 1 
ATOM   2218 N  N   . GLU A 1 315 ? -3.507  26.283  -14.504 1.00 25.96 ?  315 GLU A N   1 
ATOM   2219 C  CA  . GLU A 1 315 ? -4.057  26.553  -15.830 1.00 27.17 ?  315 GLU A CA  1 
ATOM   2220 C  C   . GLU A 1 315 ? -5.026  25.434  -16.183 1.00 28.09 ?  315 GLU A C   1 
ATOM   2221 O  O   . GLU A 1 315 ? -4.610  24.299  -16.433 1.00 30.62 ?  315 GLU A O   1 
ATOM   2222 C  CB  . GLU A 1 315 ? -2.946  26.661  -16.869 1.00 31.75 ?  315 GLU A CB  1 
ATOM   2223 C  CG  . GLU A 1 315 ? -3.391  27.257  -18.193 1.00 38.46 ?  315 GLU A CG  1 
ATOM   2224 C  CD  . GLU A 1 315 ? -3.842  28.699  -18.073 1.00 38.82 ?  315 GLU A CD  1 
ATOM   2225 O  OE1 . GLU A 1 315 ? -3.294  29.420  -17.210 1.00 36.59 ?  315 GLU A OE1 1 
ATOM   2226 O  OE2 . GLU A 1 315 ? -4.724  29.119  -18.859 1.00 44.09 ?  315 GLU A OE2 1 
ATOM   2227 N  N   . ILE A 1 316 ? -6.310  25.744  -16.213 1.00 25.85 ?  316 ILE A N   1 
ATOM   2228 C  CA  . ILE A 1 316 ? -7.325  24.771  -16.585 1.00 27.13 ?  316 ILE A CA  1 
ATOM   2229 C  C   . ILE A 1 316 ? -7.548  24.834  -18.090 1.00 27.02 ?  316 ILE A C   1 
ATOM   2230 O  O   . ILE A 1 316 ? -7.655  25.919  -18.674 1.00 25.18 ?  316 ILE A O   1 
ATOM   2231 C  CB  . ILE A 1 316 ? -8.626  25.015  -15.796 1.00 23.46 ?  316 ILE A CB  1 
ATOM   2232 C  CG1 . ILE A 1 316 ? -8.392  24.746  -14.311 1.00 24.05 ?  316 ILE A CG1 1 
ATOM   2233 C  CG2 . ILE A 1 316 ? -9.731  24.148  -16.317 1.00 20.90 ?  316 ILE A CG2 1 
ATOM   2234 C  CD1 . ILE A 1 316 ? -9.532  25.184  -13.414 1.00 25.77 ?  316 ILE A CD1 1 
ATOM   2235 N  N   . ARG A 1 317 ? -7.624  23.670  -18.726 1.00 26.63 ?  317 ARG A N   1 
ATOM   2236 C  CA  . ARG A 1 317 ? -7.717  23.607  -20.174 1.00 26.94 ?  317 ARG A CA  1 
ATOM   2237 C  C   . ARG A 1 317 ? -9.157  23.442  -20.634 1.00 27.68 ?  317 ARG A C   1 
ATOM   2238 O  O   . ARG A 1 317 ? -9.967  22.770  -19.990 1.00 25.13 ?  317 ARG A O   1 
ATOM   2239 C  CB  . ARG A 1 317 ? -6.864  22.465  -20.726 1.00 28.22 ?  317 ARG A CB  1 
ATOM   2240 C  CG  . ARG A 1 317 ? -5.391  22.547  -20.316 1.00 31.15 ?  317 ARG A CG  1 
ATOM   2241 C  CD  . ARG A 1 317 ? -4.619  23.493  -21.215 1.00 42.09 ?  317 ARG A CD  1 
ATOM   2242 N  NE  . ARG A 1 317 ? -3.398  23.988  -20.585 1.00 43.56 ?  317 ARG A NE  1 
ATOM   2243 C  CZ  . ARG A 1 317 ? -2.841  25.166  -20.834 1.00 41.80 ?  317 ARG A CZ  1 
ATOM   2244 N  NH1 . ARG A 1 317 ? -3.394  26.031  -21.671 1.00 45.61 ?  317 ARG A NH1 1 
ATOM   2245 N  NH2 . ARG A 1 317 ? -1.692  25.478  -20.238 1.00 46.36 ?  317 ARG A NH2 1 
ATOM   2246 N  N   . ALA A 1 318 ? -9.459  24.059  -21.774 1.00 24.58 ?  318 ALA A N   1 
ATOM   2247 C  CA  . ALA A 1 318 ? -10.753 23.878  -22.416 1.00 27.94 ?  318 ALA A CA  1 
ATOM   2248 C  C   . ALA A 1 318 ? -11.103 22.396  -22.470 1.00 24.90 ?  318 ALA A C   1 
ATOM   2249 O  O   . ALA A 1 318 ? -10.246 21.556  -22.754 1.00 28.27 ?  318 ALA A O   1 
ATOM   2250 C  CB  . ALA A 1 318 ? -10.724 24.475  -23.829 1.00 20.82 ?  318 ALA A CB  1 
ATOM   2251 N  N   . GLY A 1 319 ? -12.358 22.079  -22.141 1.00 24.98 ?  319 GLY A N   1 
ATOM   2252 C  CA  . GLY A 1 319 ? -12.863 20.717  -22.172 1.00 23.61 ?  319 GLY A CA  1 
ATOM   2253 C  C   . GLY A 1 319 ? -12.710 19.932  -20.884 1.00 24.82 ?  319 GLY A C   1 
ATOM   2254 O  O   . GLY A 1 319 ? -13.270 18.833  -20.774 1.00 22.60 ?  319 GLY A O   1 
ATOM   2255 N  N   . GLU A 1 320 ? -11.975 20.447  -19.911 1.00 23.55 ?  320 GLU A N   1 
ATOM   2256 C  CA  . GLU A 1 320 ? -11.717 19.710  -18.684 1.00 26.57 ?  320 GLU A CA  1 
ATOM   2257 C  C   . GLU A 1 320 ? -12.838 19.927  -17.671 1.00 22.36 ?  320 GLU A C   1 
ATOM   2258 O  O   . GLU A 1 320 ? -13.532 20.946  -17.686 1.00 21.91 ?  320 GLU A O   1 
ATOM   2259 C  CB  . GLU A 1 320 ? -10.370 20.125  -18.089 1.00 22.95 ?  320 GLU A CB  1 
ATOM   2260 C  CG  . GLU A 1 320 ? -9.182  19.643  -18.928 1.00 22.68 ?  320 GLU A CG  1 
ATOM   2261 C  CD  . GLU A 1 320 ? -7.853  19.953  -18.273 1.00 26.12 ?  320 GLU A CD  1 
ATOM   2262 O  OE1 . GLU A 1 320 ? -7.743  21.001  -17.612 1.00 26.53 ?  320 GLU A OE1 1 
ATOM   2263 O  OE2 . GLU A 1 320 ? -6.917  19.142  -18.406 1.00 31.78 ?  320 GLU A OE2 1 
ATOM   2264 N  N   . LEU A 1 321 ? -13.000 18.959  -16.779 1.00 22.99 ?  321 LEU A N   1 
ATOM   2265 C  CA  . LEU A 1 321 ? -14.034 19.026  -15.755 1.00 21.43 ?  321 LEU A CA  1 
ATOM   2266 C  C   . LEU A 1 321 ? -13.531 19.757  -14.514 1.00 20.20 ?  321 LEU A C   1 
ATOM   2267 O  O   . LEU A 1 321 ? -12.404 19.547  -14.052 1.00 21.52 ?  321 LEU A O   1 
ATOM   2268 C  CB  . LEU A 1 321 ? -14.503 17.619  -15.382 1.00 20.18 ?  321 LEU A CB  1 
ATOM   2269 C  CG  . LEU A 1 321 ? -15.549 17.445  -14.282 1.00 19.52 ?  321 LEU A CG  1 
ATOM   2270 C  CD1 . LEU A 1 321 ? -16.854 18.174  -14.618 1.00 17.66 ?  321 LEU A CD1 1 
ATOM   2271 C  CD2 . LEU A 1 321 ? -15.783 15.930  -14.039 1.00 21.68 ?  321 LEU A CD2 1 
ATOM   2272 N  N   . VAL A 1 322 ? -14.382 20.624  -13.985 1.00 18.91 ?  322 VAL A N   1 
ATOM   2273 C  CA  . VAL A 1 322 ? -14.105 21.421  -12.799 1.00 16.17 ?  322 VAL A CA  1 
ATOM   2274 C  C   . VAL A 1 322 ? -15.183 21.097  -11.776 1.00 19.02 ?  322 VAL A C   1 
ATOM   2275 O  O   . VAL A 1 322 ? -16.374 21.067  -12.115 1.00 22.47 ?  322 VAL A O   1 
ATOM   2276 C  CB  . VAL A 1 322 ? -14.093 22.922  -13.136 1.00 17.17 ?  322 VAL A CB  1 
ATOM   2277 C  CG1 . VAL A 1 322 ? -13.799 23.759  -11.895 1.00 19.55 ?  322 VAL A CG1 1 
ATOM   2278 C  CG2 . VAL A 1 322 ? -13.060 23.193  -14.222 1.00 21.09 ?  322 VAL A CG2 1 
ATOM   2279 N  N   . LEU A 1 323 ? -14.771 20.858  -10.530 1.00 20.79 ?  323 LEU A N   1 
ATOM   2280 C  CA  . LEU A 1 323 ? -15.686 20.459  -9.467  1.00 19.71 ?  323 LEU A CA  1 
ATOM   2281 C  C   . LEU A 1 323 ? -15.549 21.427  -8.301  1.00 16.83 ?  323 LEU A C   1 
ATOM   2282 O  O   . LEU A 1 323 ? -14.476 21.517  -7.685  1.00 18.43 ?  323 LEU A O   1 
ATOM   2283 C  CB  . LEU A 1 323 ? -15.407 19.021  -9.007  1.00 13.39 ?  323 LEU A CB  1 
ATOM   2284 C  CG  . LEU A 1 323 ? -15.642 17.924  -10.052 1.00 24.74 ?  323 LEU A CG  1 
ATOM   2285 C  CD1 . LEU A 1 323 ? -15.187 16.560  -9.522  1.00 19.81 ?  323 LEU A CD1 1 
ATOM   2286 C  CD2 . LEU A 1 323 ? -17.107 17.861  -10.457 1.00 19.58 ?  323 LEU A CD2 1 
ATOM   2287 N  N   . VAL A 1 324 ? -16.638 22.119  -7.980  1.00 17.42 ?  324 VAL A N   1 
ATOM   2288 C  CA  . VAL A 1 324 ? -16.636 23.099  -6.897  1.00 18.46 ?  324 VAL A CA  1 
ATOM   2289 C  C   . VAL A 1 324 ? -17.086 22.416  -5.610  1.00 19.70 ?  324 VAL A C   1 
ATOM   2290 O  O   . VAL A 1 324 ? -18.239 21.979  -5.492  1.00 19.56 ?  324 VAL A O   1 
ATOM   2291 C  CB  . VAL A 1 324 ? -17.535 24.301  -7.225  1.00 18.81 ?  324 VAL A CB  1 
ATOM   2292 C  CG1 . VAL A 1 324 ? -17.515 25.290  -6.059  1.00 17.53 ?  324 VAL A CG1 1 
ATOM   2293 C  CG2 . VAL A 1 324 ? -17.063 24.965  -8.505  1.00 15.08 ?  324 VAL A CG2 1 
ATOM   2294 N  N   . LEU A 1 325 ? -16.176 22.338  -4.638  1.00 18.83 ?  325 LEU A N   1 
ATOM   2295 C  CA  . LEU A 1 325 ? -16.438 21.663  -3.367  1.00 19.77 ?  325 LEU A CA  1 
ATOM   2296 C  C   . LEU A 1 325 ? -17.028 22.677  -2.399  1.00 18.64 ?  325 LEU A C   1 
ATOM   2297 O  O   . LEU A 1 325 ? -16.301 23.443  -1.761  1.00 20.94 ?  325 LEU A O   1 
ATOM   2298 C  CB  . LEU A 1 325 ? -15.159 21.057  -2.804  1.00 18.98 ?  325 LEU A CB  1 
ATOM   2299 C  CG  . LEU A 1 325 ? -15.375 20.159  -1.594  1.00 21.00 ?  325 LEU A CG  1 
ATOM   2300 C  CD1 . LEU A 1 325 ? -15.909 18.798  -2.087  1.00 21.12 ?  325 LEU A CD1 1 
ATOM   2301 C  CD2 . LEU A 1 325 ? -14.067 19.993  -0.843  1.00 17.56 ?  325 LEU A CD2 1 
ATOM   2302 N  N   . ILE A 1 326 ? -18.352 22.670  -2.285  1.00 18.64 ?  326 ILE A N   1 
ATOM   2303 C  CA  . ILE A 1 326 ? -19.053 23.694  -1.518  1.00 17.54 ?  326 ILE A CA  1 
ATOM   2304 C  C   . ILE A 1 326 ? -18.602 23.695  -0.059  1.00 18.60 ?  326 ILE A C   1 
ATOM   2305 O  O   . ILE A 1 326 ? -18.347 24.754  0.528   1.00 20.41 ?  326 ILE A O   1 
ATOM   2306 C  CB  . ILE A 1 326 ? -20.572 23.490  -1.666  1.00 18.07 ?  326 ILE A CB  1 
ATOM   2307 C  CG1 . ILE A 1 326 ? -20.979 23.786  -3.117  1.00 19.23 ?  326 ILE A CG1 1 
ATOM   2308 C  CG2 . ILE A 1 326 ? -21.366 24.407  -0.700  1.00 17.22 ?  326 ILE A CG2 1 
ATOM   2309 C  CD1 . ILE A 1 326 ? -20.818 25.269  -3.488  1.00 17.44 ?  326 ILE A CD1 1 
ATOM   2310 N  N   . GLU A 1 327 ? -18.474 22.518  0.549   1.00 18.86 ?  327 GLU A N   1 
ATOM   2311 C  CA  . GLU A 1 327 ? -18.095 22.492  1.961   1.00 18.79 ?  327 GLU A CA  1 
ATOM   2312 C  C   . GLU A 1 327 ? -16.657 22.959  2.176   1.00 20.09 ?  327 GLU A C   1 
ATOM   2313 O  O   . GLU A 1 327 ? -16.327 23.488  3.246   1.00 17.84 ?  327 GLU A O   1 
ATOM   2314 C  CB  . GLU A 1 327 ? -18.297 21.090  2.542   1.00 20.50 ?  327 GLU A CB  1 
ATOM   2315 C  CG  . GLU A 1 327 ? -17.353 20.051  2.016   1.00 18.14 ?  327 GLU A CG  1 
ATOM   2316 C  CD  . GLU A 1 327 ? -18.038 19.148  1.036   1.00 26.90 ?  327 GLU A CD  1 
ATOM   2317 O  OE1 . GLU A 1 327 ? -18.786 19.664  0.166   1.00 28.70 ?  327 GLU A OE1 1 
ATOM   2318 O  OE2 . GLU A 1 327 ? -17.857 17.922  1.155   1.00 29.23 ?  327 GLU A OE2 1 
ATOM   2319 N  N   . GLY A 1 328 ? -15.784 22.771  1.191   1.00 19.21 ?  328 GLY A N   1 
ATOM   2320 C  CA  . GLY A 1 328 ? -14.476 23.394  1.292   1.00 21.49 ?  328 GLY A CA  1 
ATOM   2321 C  C   . GLY A 1 328 ? -14.588 24.902  1.404   1.00 18.69 ?  328 GLY A C   1 
ATOM   2322 O  O   . GLY A 1 328 ? -13.968 25.524  2.267   1.00 20.58 ?  328 GLY A O   1 
ATOM   2323 N  N   . ALA A 1 329 ? -15.409 25.504  0.539   1.00 19.76 ?  329 ALA A N   1 
ATOM   2324 C  CA  . ALA A 1 329 ? -15.591 26.954  0.552   1.00 18.07 ?  329 ALA A CA  1 
ATOM   2325 C  C   . ALA A 1 329 ? -16.307 27.422  1.820   1.00 16.40 ?  329 ALA A C   1 
ATOM   2326 O  O   . ALA A 1 329 ? -15.927 28.433  2.421   1.00 18.28 ?  329 ALA A O   1 
ATOM   2327 C  CB  . ALA A 1 329 ? -16.370 27.378  -0.691  1.00 18.16 ?  329 ALA A CB  1 
ATOM   2328 N  N   . ASN A 1 330 ? -17.327 26.693  2.255   1.00 16.73 ?  330 ASN A N   1 
ATOM   2329 C  CA  . ASN A 1 330 ? -18.144 27.144  3.377   1.00 18.21 ?  330 ASN A CA  1 
ATOM   2330 C  C   . ASN A 1 330 ? -17.460 26.970  4.718   1.00 20.26 ?  330 ASN A C   1 
ATOM   2331 O  O   . ASN A 1 330 ? -17.922 27.550  5.710   1.00 16.04 ?  330 ASN A O   1 
ATOM   2332 C  CB  . ASN A 1 330 ? -19.472 26.398  3.383   1.00 13.71 ?  330 ASN A CB  1 
ATOM   2333 C  CG  . ASN A 1 330 ? -20.461 27.005  2.432   1.00 18.49 ?  330 ASN A CG  1 
ATOM   2334 O  OD1 . ASN A 1 330 ? -20.203 28.058  1.846   1.00 15.70 ?  330 ASN A OD1 1 
ATOM   2335 N  ND2 . ASN A 1 330 ? -21.599 26.353  2.268   1.00 19.55 ?  330 ASN A ND2 1 
ATOM   2336 N  N   . TYR A 1 331 ? -16.370 26.204  4.767   1.00 17.25 ?  331 TYR A N   1 
ATOM   2337 C  CA  . TYR A 1 331 ? -15.581 26.034  5.978   1.00 18.35 ?  331 TYR A CA  1 
ATOM   2338 C  C   . TYR A 1 331 ? -14.224 26.722  5.865   1.00 21.25 ?  331 TYR A C   1 
ATOM   2339 O  O   . TYR A 1 331 ? -13.318 26.432  6.653   1.00 17.77 ?  331 TYR A O   1 
ATOM   2340 C  CB  . TYR A 1 331 ? -15.393 24.551  6.290   1.00 18.25 ?  331 TYR A CB  1 
ATOM   2341 C  CG  . TYR A 1 331 ? -16.587 23.834  6.917   1.00 19.72 ?  331 TYR A CG  1 
ATOM   2342 C  CD1 . TYR A 1 331 ? -17.728 23.551  6.180   1.00 18.66 ?  331 TYR A CD1 1 
ATOM   2343 C  CD2 . TYR A 1 331 ? -16.535 23.385  8.236   1.00 19.38 ?  331 TYR A CD2 1 
ATOM   2344 C  CE1 . TYR A 1 331 ? -18.807 22.867  6.758   1.00 16.76 ?  331 TYR A CE1 1 
ATOM   2345 C  CE2 . TYR A 1 331 ? -17.594 22.701  8.812   1.00 18.31 ?  331 TYR A CE2 1 
ATOM   2346 C  CZ  . TYR A 1 331 ? -18.731 22.454  8.077   1.00 19.12 ?  331 TYR A CZ  1 
ATOM   2347 O  OH  . TYR A 1 331 ? -19.769 21.762  8.672   1.00 17.02 ?  331 TYR A OH  1 
ATOM   2348 N  N   . ASP A 1 332 ? -14.080 27.638  4.912   1.00 19.00 ?  332 ASP A N   1 
ATOM   2349 C  CA  . ASP A 1 332 ? -12.809 28.320  4.684   1.00 20.13 ?  332 ASP A CA  1 
ATOM   2350 C  C   . ASP A 1 332 ? -12.571 29.358  5.777   1.00 20.67 ?  332 ASP A C   1 
ATOM   2351 O  O   . ASP A 1 332 ? -13.335 30.325  5.871   1.00 19.47 ?  332 ASP A O   1 
ATOM   2352 C  CB  . ASP A 1 332 ? -12.814 28.980  3.308   1.00 20.60 ?  332 ASP A CB  1 
ATOM   2353 C  CG  . ASP A 1 332 ? -11.436 29.454  2.877   1.00 21.81 ?  332 ASP A CG  1 
ATOM   2354 O  OD1 . ASP A 1 332 ? -10.641 29.838  3.761   1.00 19.95 ?  332 ASP A OD1 1 
ATOM   2355 O  OD2 . ASP A 1 332 ? -11.150 29.430  1.654   1.00 19.78 ?  332 ASP A OD2 1 
ATOM   2356 N  N   . PRO A 1 333 ? -11.540 29.200  6.616   1.00 20.51 ?  333 PRO A N   1 
ATOM   2357 C  CA  . PRO A 1 333 ? -11.305 30.187  7.690   1.00 18.46 ?  333 PRO A CA  1 
ATOM   2358 C  C   . PRO A 1 333 ? -10.851 31.549  7.175   1.00 25.88 ?  333 PRO A C   1 
ATOM   2359 O  O   . PRO A 1 333 ? -10.911 32.527  7.932   1.00 24.39 ?  333 PRO A O   1 
ATOM   2360 C  CB  . PRO A 1 333 ? -10.213 29.527  8.551   1.00 26.50 ?  333 PRO A CB  1 
ATOM   2361 C  CG  . PRO A 1 333 ? -9.459  28.605  7.572   1.00 23.99 ?  333 PRO A CG  1 
ATOM   2362 C  CD  . PRO A 1 333 ? -10.553 28.100  6.619   1.00 18.97 ?  333 PRO A CD  1 
ATOM   2363 N  N   . ALA A 1 334 ? -10.396 31.651  5.919   1.00 18.89 ?  334 ALA A N   1 
ATOM   2364 C  CA  . ALA A 1 334 ? -10.133 32.972  5.357   1.00 26.95 ?  334 ALA A CA  1 
ATOM   2365 C  C   . ALA A 1 334 ? -11.401 33.807  5.313   1.00 27.67 ?  334 ALA A C   1 
ATOM   2366 O  O   . ALA A 1 334 ? -11.338 35.044  5.351   1.00 24.95 ?  334 ALA A O   1 
ATOM   2367 C  CB  . ALA A 1 334 ? -9.534  32.858  3.949   1.00 20.38 ?  334 ALA A CB  1 
ATOM   2368 N  N   . VAL A 1 335 ? -12.562 33.158  5.242   1.00 22.79 ?  335 VAL A N   1 
ATOM   2369 C  CA  . VAL A 1 335 ? -13.832 33.852  5.141   1.00 21.48 ?  335 VAL A CA  1 
ATOM   2370 C  C   . VAL A 1 335 ? -14.656 33.698  6.410   1.00 21.78 ?  335 VAL A C   1 
ATOM   2371 O  O   . VAL A 1 335 ? -15.269 34.661  6.875   1.00 19.75 ?  335 VAL A O   1 
ATOM   2372 C  CB  . VAL A 1 335 ? -14.618 33.368  3.904   1.00 23.15 ?  335 VAL A CB  1 
ATOM   2373 C  CG1 . VAL A 1 335 ? -15.979 34.063  3.818   1.00 22.07 ?  335 VAL A CG1 1 
ATOM   2374 C  CG2 . VAL A 1 335 ? -13.794 33.624  2.641   1.00 24.92 ?  335 VAL A CG2 1 
ATOM   2375 N  N   . PHE A 1 336 ? -14.664 32.506  6.994   1.00 21.71 ?  336 PHE A N   1 
ATOM   2376 C  CA  . PHE A 1 336 ? -15.542 32.198  8.119   1.00 21.54 ?  336 PHE A CA  1 
ATOM   2377 C  C   . PHE A 1 336 ? -14.675 31.870  9.326   1.00 22.25 ?  336 PHE A C   1 
ATOM   2378 O  O   . PHE A 1 336 ? -14.108 30.766  9.404   1.00 23.39 ?  336 PHE A O   1 
ATOM   2379 C  CB  . PHE A 1 336 ? -16.477 31.033  7.770   1.00 20.34 ?  336 PHE A CB  1 
ATOM   2380 C  CG  . PHE A 1 336 ? -17.292 31.253  6.511   1.00 23.57 ?  336 PHE A CG  1 
ATOM   2381 C  CD1 . PHE A 1 336 ? -18.506 31.955  6.557   1.00 19.49 ?  336 PHE A CD1 1 
ATOM   2382 C  CD2 . PHE A 1 336 ? -16.860 30.747  5.284   1.00 21.17 ?  336 PHE A CD2 1 
ATOM   2383 C  CE1 . PHE A 1 336 ? -19.268 32.160  5.398   1.00 17.64 ?  336 PHE A CE1 1 
ATOM   2384 C  CE2 . PHE A 1 336 ? -17.607 30.948  4.123   1.00 20.01 ?  336 PHE A CE2 1 
ATOM   2385 C  CZ  . PHE A 1 336 ? -18.826 31.658  4.185   1.00 20.00 ?  336 PHE A CZ  1 
ATOM   2386 N  N   . PRO A 1 337 ? -14.522 32.788  10.285  1.00 22.57 ?  337 PRO A N   1 
ATOM   2387 C  CA  . PRO A 1 337 ? -13.799 32.442  11.511  1.00 22.07 ?  337 PRO A CA  1 
ATOM   2388 C  C   . PRO A 1 337 ? -14.477 31.281  12.221  1.00 24.46 ?  337 PRO A C   1 
ATOM   2389 O  O   . PRO A 1 337 ? -15.696 31.093  12.125  1.00 23.48 ?  337 PRO A O   1 
ATOM   2390 C  CB  . PRO A 1 337 ? -13.859 33.726  12.346  1.00 25.24 ?  337 PRO A CB  1 
ATOM   2391 C  CG  . PRO A 1 337 ? -14.989 34.517  11.775  1.00 27.66 ?  337 PRO A CG  1 
ATOM   2392 C  CD  . PRO A 1 337 ? -15.071 34.153  10.322  1.00 19.15 ?  337 PRO A CD  1 
ATOM   2393 N  N   . HIS A 1 338 ? -13.664 30.514  12.953  1.00 20.92 ?  338 HIS A N   1 
ATOM   2394 C  CA  . HIS A 1 338 ? -14.031 29.256  13.591  1.00 21.21 ?  338 HIS A CA  1 
ATOM   2395 C  C   . HIS A 1 338 ? -15.054 28.505  12.735  1.00 20.72 ?  338 HIS A C   1 
ATOM   2396 O  O   . HIS A 1 338 ? -16.175 28.239  13.188  1.00 21.41 ?  338 HIS A O   1 
ATOM   2397 C  CB  . HIS A 1 338 ? -14.537 29.483  15.026  1.00 20.63 ?  338 HIS A CB  1 
ATOM   2398 C  CG  . HIS A 1 338 ? -15.559 30.576  15.179  1.00 21.39 ?  338 HIS A CG  1 
ATOM   2399 N  ND1 . HIS A 1 338 ? -15.215 31.897  15.374  1.00 21.92 ?  338 HIS A ND1 1 
ATOM   2400 C  CD2 . HIS A 1 338 ? -16.914 30.530  15.233  1.00 20.45 ?  338 HIS A CD2 1 
ATOM   2401 C  CE1 . HIS A 1 338 ? -16.316 32.624  15.495  1.00 21.88 ?  338 HIS A CE1 1 
ATOM   2402 N  NE2 . HIS A 1 338 ? -17.361 31.818  15.419  1.00 19.32 ?  338 HIS A NE2 1 
ATOM   2403 N  N   . PRO A 1 339 ? -14.693 28.123  11.505  1.00 19.41 ?  339 PRO A N   1 
ATOM   2404 C  CA  . PRO A 1 339 ? -15.699 27.549  10.600  1.00 19.17 ?  339 PRO A CA  1 
ATOM   2405 C  C   . PRO A 1 339 ? -16.284 26.248  11.113  1.00 19.20 ?  339 PRO A C   1 
ATOM   2406 O  O   . PRO A 1 339 ? -17.420 25.910  10.756  1.00 16.79 ?  339 PRO A O   1 
ATOM   2407 C  CB  . PRO A 1 339 ? -14.923 27.319  9.296   1.00 21.12 ?  339 PRO A CB  1 
ATOM   2408 C  CG  . PRO A 1 339 ? -13.473 27.294  9.680   1.00 18.58 ?  339 PRO A CG  1 
ATOM   2409 C  CD  . PRO A 1 339 ? -13.315 27.971  11.004  1.00 19.27 ?  339 PRO A CD  1 
ATOM   2410 N  N   . GLU A 1 340 ? -15.537 25.518  11.943  1.00 15.97 ?  340 GLU A N   1 
ATOM   2411 C  CA  . GLU A 1 340 ? -15.974 24.233  12.480  1.00 23.05 ?  340 GLU A CA  1 
ATOM   2412 C  C   . GLU A 1 340 ? -16.992 24.369  13.611  1.00 21.16 ?  340 GLU A C   1 
ATOM   2413 O  O   . GLU A 1 340 ? -17.518 23.355  14.071  1.00 22.21 ?  340 GLU A O   1 
ATOM   2414 C  CB  . GLU A 1 340 ? -14.755 23.439  12.968  1.00 22.01 ?  340 GLU A CB  1 
ATOM   2415 C  CG  . GLU A 1 340 ? -14.296 23.787  14.397  1.00 26.55 ?  340 GLU A CG  1 
ATOM   2416 C  CD  . GLU A 1 340 ? -13.403 25.036  14.497  1.00 24.44 ?  340 GLU A CD  1 
ATOM   2417 O  OE1 . GLU A 1 340 ? -13.156 25.721  13.479  1.00 25.90 ?  340 GLU A OE1 1 
ATOM   2418 O  OE2 . GLU A 1 340 ? -12.939 25.334  15.618  1.00 25.79 ?  340 GLU A OE2 1 
ATOM   2419 N  N   . ARG A 1 341 ? -17.300 25.586  14.055  1.00 20.50 ?  341 ARG A N   1 
ATOM   2420 C  CA  . ARG A 1 341 ? -18.210 25.815  15.172  1.00 21.13 ?  341 ARG A CA  1 
ATOM   2421 C  C   . ARG A 1 341 ? -19.450 26.543  14.661  1.00 20.95 ?  341 ARG A C   1 
ATOM   2422 O  O   . ARG A 1 341 ? -19.349 27.660  14.139  1.00 20.11 ?  341 ARG A O   1 
ATOM   2423 C  CB  . ARG A 1 341 ? -17.525 26.628  16.270  1.00 19.97 ?  341 ARG A CB  1 
ATOM   2424 C  CG  . ARG A 1 341 ? -16.188 26.063  16.736  1.00 21.94 ?  341 ARG A CG  1 
ATOM   2425 C  CD  . ARG A 1 341 ? -15.656 26.798  17.976  1.00 18.06 ?  341 ARG A CD  1 
ATOM   2426 N  NE  . ARG A 1 341 ? -16.564 26.654  19.104  1.00 19.14 ?  341 ARG A NE  1 
ATOM   2427 C  CZ  . ARG A 1 341 ? -16.653 25.559  19.843  1.00 21.36 ?  341 ARG A CZ  1 
ATOM   2428 N  NH1 . ARG A 1 341 ? -15.853 24.521  19.639  1.00 23.14 ?  341 ARG A NH1 1 
ATOM   2429 N  NH2 . ARG A 1 341 ? -17.582 25.489  20.791  1.00 21.32 ?  341 ARG A NH2 1 
ATOM   2430 N  N   . ILE A 1 342 ? -20.612 25.906  14.808  1.00 16.47 ?  342 ILE A N   1 
ATOM   2431 C  CA  . ILE A 1 342 ? -21.874 26.566  14.502  1.00 17.60 ?  342 ILE A CA  1 
ATOM   2432 C  C   . ILE A 1 342 ? -22.026 27.838  15.330  1.00 20.31 ?  342 ILE A C   1 
ATOM   2433 O  O   . ILE A 1 342 ? -21.726 27.870  16.536  1.00 19.16 ?  342 ILE A O   1 
ATOM   2434 C  CB  . ILE A 1 342 ? -23.040 25.596  14.751  1.00 18.60 ?  342 ILE A CB  1 
ATOM   2435 C  CG1 . ILE A 1 342 ? -23.058 24.500  13.682  1.00 20.51 ?  342 ILE A CG1 1 
ATOM   2436 C  CG2 . ILE A 1 342 ? -24.350 26.339  14.758  1.00 19.79 ?  342 ILE A CG2 1 
ATOM   2437 C  CD1 . ILE A 1 342 ? -24.015 23.347  14.031  1.00 17.54 ?  342 ILE A CD1 1 
ATOM   2438 N  N   . ASP A 1 343 ? -22.491 28.902  14.680  1.00 17.38 ?  343 ASP A N   1 
ATOM   2439 C  CA  . ASP A 1 343 ? -22.515 30.221  15.310  1.00 19.60 ?  343 ASP A CA  1 
ATOM   2440 C  C   . ASP A 1 343 ? -23.651 31.013  14.674  1.00 21.38 ?  343 ASP A C   1 
ATOM   2441 O  O   . ASP A 1 343 ? -23.547 31.417  13.511  1.00 20.30 ?  343 ASP A O   1 
ATOM   2442 C  CB  . ASP A 1 343 ? -21.173 30.920  15.117  1.00 19.16 ?  343 ASP A CB  1 
ATOM   2443 C  CG  . ASP A 1 343 ? -21.088 32.271  15.821  1.00 20.02 ?  343 ASP A CG  1 
ATOM   2444 O  OD1 . ASP A 1 343 ? -22.111 32.819  16.297  1.00 21.22 ?  343 ASP A OD1 1 
ATOM   2445 O  OD2 . ASP A 1 343 ? -19.960 32.793  15.871  1.00 22.19 ?  343 ASP A OD2 1 
ATOM   2446 N  N   . PHE A 1 344 ? -24.727 31.225  15.434  1.00 20.72 ?  344 PHE A N   1 
ATOM   2447 C  CA  . PHE A 1 344 ? -25.893 31.955  14.959  1.00 23.86 ?  344 PHE A CA  1 
ATOM   2448 C  C   . PHE A 1 344 ? -25.691 33.469  14.959  1.00 25.98 ?  344 PHE A C   1 
ATOM   2449 O  O   . PHE A 1 344 ? -26.597 34.203  14.544  1.00 25.78 ?  344 PHE A O   1 
ATOM   2450 C  CB  . PHE A 1 344 ? -27.125 31.610  15.818  1.00 24.27 ?  344 PHE A CB  1 
ATOM   2451 C  CG  . PHE A 1 344 ? -27.628 30.179  15.650  1.00 22.50 ?  344 PHE A CG  1 
ATOM   2452 C  CD1 . PHE A 1 344 ? -27.159 29.370  14.628  1.00 20.73 ?  344 PHE A CD1 1 
ATOM   2453 C  CD2 . PHE A 1 344 ? -28.558 29.655  16.533  1.00 18.56 ?  344 PHE A CD2 1 
ATOM   2454 C  CE1 . PHE A 1 344 ? -27.627 28.071  14.468  1.00 19.66 ?  344 PHE A CE1 1 
ATOM   2455 C  CE2 . PHE A 1 344 ? -29.025 28.360  16.386  1.00 18.46 ?  344 PHE A CE2 1 
ATOM   2456 C  CZ  . PHE A 1 344 ? -28.554 27.564  15.352  1.00 20.53 ?  344 PHE A CZ  1 
ATOM   2457 N  N   . ASP A 1 345 ? -24.535 33.967  15.388  1.00 23.07 ?  345 ASP A N   1 
ATOM   2458 C  CA  . ASP A 1 345 ? -24.368 35.404  15.561  1.00 20.80 ?  345 ASP A CA  1 
ATOM   2459 C  C   . ASP A 1 345 ? -23.184 35.950  14.764  1.00 24.39 ?  345 ASP A C   1 
ATOM   2460 O  O   . ASP A 1 345 ? -22.514 36.891  15.199  1.00 21.97 ?  345 ASP A O   1 
ATOM   2461 C  CB  . ASP A 1 345 ? -24.246 35.726  17.049  1.00 24.14 ?  345 ASP A CB  1 
ATOM   2462 C  CG  . ASP A 1 345 ? -25.482 35.298  17.831  1.00 25.91 ?  345 ASP A CG  1 
ATOM   2463 O  OD1 . ASP A 1 345 ? -26.558 35.900  17.627  1.00 28.31 ?  345 ASP A OD1 1 
ATOM   2464 O  OD2 . ASP A 1 345 ? -25.384 34.344  18.624  1.00 22.36 ?  345 ASP A OD2 1 
ATOM   2465 N  N   . ARG A 1 346 ? -22.930 35.385  13.584  1.00 25.25 ?  346 ARG A N   1 
ATOM   2466 C  CA  . ARG A 1 346 ? -21.836 35.861  12.747  1.00 21.93 ?  346 ARG A CA  1 
ATOM   2467 C  C   . ARG A 1 346 ? -22.174 37.226  12.169  1.00 22.79 ?  346 ARG A C   1 
ATOM   2468 O  O   . ARG A 1 346 ? -23.313 37.478  11.771  1.00 23.52 ?  346 ARG A O   1 
ATOM   2469 C  CB  . ARG A 1 346 ? -21.548 34.866  11.616  1.00 24.23 ?  346 ARG A CB  1 
ATOM   2470 C  CG  . ARG A 1 346 ? -20.957 33.542  12.110  1.00 18.34 ?  346 ARG A CG  1 
ATOM   2471 C  CD  . ARG A 1 346 ? -20.961 32.427  11.035  1.00 17.09 ?  346 ARG A CD  1 
ATOM   2472 N  NE  . ARG A 1 346 ? -20.332 31.223  11.573  1.00 19.77 ?  346 ARG A NE  1 
ATOM   2473 C  CZ  . ARG A 1 346 ? -19.019 31.087  11.733  1.00 23.11 ?  346 ARG A CZ  1 
ATOM   2474 N  NH1 . ARG A 1 346 ? -18.171 32.015  11.304  1.00 18.09 ?  346 ARG A NH1 1 
ATOM   2475 N  NH2 . ARG A 1 346 ? -18.543 29.990  12.327  1.00 16.09 ?  346 ARG A NH2 1 
ATOM   2476 N  N   . GLU A 1 347 ? -21.182 38.123  12.172  1.00 22.18 ?  347 GLU A N   1 
ATOM   2477 C  CA  . GLU A 1 347 ? -21.347 39.445  11.565  1.00 28.37 ?  347 GLU A CA  1 
ATOM   2478 C  C   . GLU A 1 347 ? -21.774 39.329  10.110  1.00 26.19 ?  347 GLU A C   1 
ATOM   2479 O  O   . GLU A 1 347 ? -22.627 40.082  9.630   1.00 25.40 ?  347 GLU A O   1 
ATOM   2480 C  CB  . GLU A 1 347 ? -20.023 40.212  11.636  1.00 30.53 ?  347 GLU A CB  1 
ATOM   2481 C  CG  . GLU A 1 347 ? -19.551 40.600  13.014  1.00 44.48 ?  347 GLU A CG  1 
ATOM   2482 C  CD  . GLU A 1 347 ? -18.203 41.284  12.951  1.00 51.61 ?  347 GLU A CD  1 
ATOM   2483 O  OE1 . GLU A 1 347 ? -17.588 41.267  11.864  1.00 50.36 ?  347 GLU A OE1 1 
ATOM   2484 O  OE2 . GLU A 1 347 ? -17.764 41.850  13.976  1.00 66.54 ?  347 GLU A OE2 1 
ATOM   2485 N  N   . SER A 1 348 ? -21.166 38.397  9.394   1.00 28.64 ?  348 SER A N   1 
ATOM   2486 C  CA  . SER A 1 348 ? -21.349 38.201  7.967   1.00 27.91 ?  348 SER A CA  1 
ATOM   2487 C  C   . SER A 1 348 ? -21.484 36.708  7.727   1.00 29.40 ?  348 SER A C   1 
ATOM   2488 O  O   . SER A 1 348 ? -20.940 35.906  8.486   1.00 32.67 ?  348 SER A O   1 
ATOM   2489 C  CB  . SER A 1 348 ? -20.141 38.748  7.189   1.00 29.27 ?  348 SER A CB  1 
ATOM   2490 O  OG  . SER A 1 348 ? -20.396 38.802  5.799   1.00 46.21 ?  348 SER A OG  1 
ATOM   2491 N  N   . ASN A 1 349 ? -22.183 36.319  6.662   1.00 22.01 ?  349 ASN A N   1 
ATOM   2492 C  CA  . ASN A 1 349 ? -22.292 34.903  6.314   1.00 27.16 ?  349 ASN A CA  1 
ATOM   2493 C  C   . ASN A 1 349 ? -22.556 34.721  4.829   1.00 18.81 ?  349 ASN A C   1 
ATOM   2494 O  O   . ASN A 1 349 ? -23.609 34.216  4.426   1.00 24.53 ?  349 ASN A O   1 
ATOM   2495 C  CB  . ASN A 1 349 ? -23.376 34.227  7.150   1.00 23.97 ?  349 ASN A CB  1 
ATOM   2496 C  CG  . ASN A 1 349 ? -23.095 32.760  7.345   1.00 22.85 ?  349 ASN A CG  1 
ATOM   2497 O  OD1 . ASN A 1 349 ? -22.206 32.212  6.690   1.00 24.08 ?  349 ASN A OD1 1 
ATOM   2498 N  ND2 . ASN A 1 349 ? -23.799 32.127  8.278   1.00 22.28 ?  349 ASN A ND2 1 
ATOM   2499 N  N   . PRO A 1 350 ? -21.569 35.078  3.958   1.00 18.38 ?  350 PRO A N   1 
ATOM   2500 C  CA  . PRO A 1 350 ? -21.735 34.961  2.509   1.00 20.60 ?  350 PRO A CA  1 
ATOM   2501 C  C   . PRO A 1 350 ? -21.341 33.555  2.056   1.00 16.53 ?  350 PRO A C   1 
ATOM   2502 O  O   . PRO A 1 350 ? -20.359 33.366  1.335   1.00 17.21 ?  350 PRO A O   1 
ATOM   2503 C  CB  . PRO A 1 350 ? -20.723 35.986  1.971   1.00 26.22 ?  350 PRO A CB  1 
ATOM   2504 C  CG  . PRO A 1 350 ? -19.592 35.878  2.939   1.00 22.27 ?  350 PRO A CG  1 
ATOM   2505 C  CD  . PRO A 1 350 ? -20.226 35.580  4.307   1.00 24.09 ?  350 PRO A CD  1 
ATOM   2506 N  N   . HIS A 1 351 ? -22.144 32.569  2.450   1.00 15.56 ?  351 HIS A N   1 
ATOM   2507 C  CA  . HIS A 1 351 ? -21.857 31.156  2.215   1.00 19.57 ?  351 HIS A CA  1 
ATOM   2508 C  C   . HIS A 1 351 ? -22.387 30.792  0.827   1.00 20.18 ?  351 HIS A C   1 
ATOM   2509 O  O   . HIS A 1 351 ? -23.257 31.463  0.270   1.00 18.99 ?  351 HIS A O   1 
ATOM   2510 C  CB  . HIS A 1 351 ? -22.521 30.257  3.270   1.00 17.25 ?  351 HIS A CB  1 
ATOM   2511 C  CG  . HIS A 1 351 ? -24.023 30.354  3.287   1.00 20.01 ?  351 HIS A CG  1 
ATOM   2512 N  ND1 . HIS A 1 351 ? -24.815 29.856  2.273   1.00 18.79 ?  351 HIS A ND1 1 
ATOM   2513 C  CD2 . HIS A 1 351 ? -24.873 30.908  4.189   1.00 19.30 ?  351 HIS A CD2 1 
ATOM   2514 C  CE1 . HIS A 1 351 ? -26.086 30.096  2.546   1.00 18.83 ?  351 HIS A CE1 1 
ATOM   2515 N  NE2 . HIS A 1 351 ? -26.149 30.736  3.702   1.00 20.85 ?  351 HIS A NE2 1 
ATOM   2516 N  N   . LEU A 1 352 ? -21.890 29.666  0.303   1.00 18.94 ?  352 LEU A N   1 
ATOM   2517 C  CA  . LEU A 1 352 ? -22.211 29.178  -1.036  1.00 19.44 ?  352 LEU A CA  1 
ATOM   2518 C  C   . LEU A 1 352 ? -23.154 27.969  -1.032  1.00 18.51 ?  352 LEU A C   1 
ATOM   2519 O  O   . LEU A 1 352 ? -23.118 27.156  -1.959  1.00 19.88 ?  352 LEU A O   1 
ATOM   2520 C  CB  . LEU A 1 352 ? -20.918 28.820  -1.774  1.00 19.97 ?  352 LEU A CB  1 
ATOM   2521 C  CG  . LEU A 1 352 ? -19.809 29.871  -1.793  1.00 20.44 ?  352 LEU A CG  1 
ATOM   2522 C  CD1 . LEU A 1 352 ? -18.656 29.440  -2.735  1.00 17.98 ?  352 LEU A CD1 1 
ATOM   2523 C  CD2 . LEU A 1 352 ? -20.358 31.240  -2.182  1.00 19.67 ?  352 LEU A CD2 1 
ATOM   2524 N  N   . ALA A 1 353 ? -23.994 27.819  0.004   1.00 19.01 ?  353 ALA A N   1 
ATOM   2525 C  CA  . ALA A 1 353 ? -24.829 26.619  0.128   1.00 18.15 ?  353 ALA A CA  1 
ATOM   2526 C  C   . ALA A 1 353 ? -25.850 26.504  -1.001  1.00 20.42 ?  353 ALA A C   1 
ATOM   2527 O  O   . ALA A 1 353 ? -26.311 25.396  -1.320  1.00 16.72 ?  353 ALA A O   1 
ATOM   2528 C  CB  . ALA A 1 353 ? -25.563 26.613  1.475   1.00 16.49 ?  353 ALA A CB  1 
ATOM   2529 N  N   . PHE A 1 354 ? -26.240 27.633  -1.578  1.00 17.20 ?  354 PHE A N   1 
ATOM   2530 C  CA  . PHE A 1 354 ? -27.094 27.695  -2.754  1.00 19.67 ?  354 PHE A CA  1 
ATOM   2531 C  C   . PHE A 1 354 ? -26.305 27.936  -4.033  1.00 17.81 ?  354 PHE A C   1 
ATOM   2532 O  O   . PHE A 1 354 ? -26.904 28.196  -5.077  1.00 17.31 ?  354 PHE A O   1 
ATOM   2533 C  CB  . PHE A 1 354 ? -28.141 28.790  -2.566  1.00 17.11 ?  354 PHE A CB  1 
ATOM   2534 C  CG  . PHE A 1 354 ? -29.166 28.467  -1.509  1.00 20.04 ?  354 PHE A CG  1 
ATOM   2535 C  CD1 . PHE A 1 354 ? -30.019 27.374  -1.656  1.00 18.67 ?  354 PHE A CD1 1 
ATOM   2536 C  CD2 . PHE A 1 354 ? -29.269 29.249  -0.364  1.00 18.83 ?  354 PHE A CD2 1 
ATOM   2537 C  CE1 . PHE A 1 354 ? -30.977 27.086  -0.676  1.00 22.16 ?  354 PHE A CE1 1 
ATOM   2538 C  CE2 . PHE A 1 354 ? -30.219 28.969  0.615   1.00 19.32 ?  354 PHE A CE2 1 
ATOM   2539 C  CZ  . PHE A 1 354 ? -31.072 27.898  0.466   1.00 15.31 ?  354 PHE A CZ  1 
ATOM   2540 N  N   . GLY A 1 355 ? -24.978 27.862  -3.968  1.00 18.28 ?  355 GLY A N   1 
ATOM   2541 C  CA  . GLY A 1 355 ? -24.172 28.106  -5.138  1.00 18.06 ?  355 GLY A CA  1 
ATOM   2542 C  C   . GLY A 1 355 ? -23.864 29.587  -5.302  1.00 22.32 ?  355 GLY A C   1 
ATOM   2543 O  O   . GLY A 1 355 ? -23.811 30.344  -4.337  1.00 20.99 ?  355 GLY A O   1 
ATOM   2544 N  N   . GLY A 1 356 ? -23.663 30.001  -6.549  1.00 20.41 ?  356 GLY A N   1 
ATOM   2545 C  CA  . GLY A 1 356 ? -23.385 31.402  -6.810  1.00 22.08 ?  356 GLY A CA  1 
ATOM   2546 C  C   . GLY A 1 356 ? -23.424 31.671  -8.297  1.00 21.45 ?  356 GLY A C   1 
ATOM   2547 O  O   . GLY A 1 356 ? -23.477 30.748  -9.111  1.00 19.54 ?  356 GLY A O   1 
ATOM   2548 N  N   . GLY A 1 357 ? -23.416 32.956  -8.644  1.00 20.90 ?  357 GLY A N   1 
ATOM   2549 C  CA  . GLY A 1 357 ? -23.412 33.292  -10.066 1.00 17.59 ?  357 GLY A CA  1 
ATOM   2550 C  C   . GLY A 1 357 ? -24.700 32.906  -10.771 1.00 21.47 ?  357 GLY A C   1 
ATOM   2551 O  O   . GLY A 1 357 ? -25.781 32.910  -10.185 1.00 19.86 ?  357 GLY A O   1 
ATOM   2552 N  N   . GLN A 1 358 ? -24.584 32.547  -12.058 1.00 19.91 ?  358 GLN A N   1 
ATOM   2553 C  CA  . GLN A 1 358 ? -25.783 32.442  -12.884 1.00 21.70 ?  358 GLN A CA  1 
ATOM   2554 C  C   . GLN A 1 358 ? -26.683 31.271  -12.483 1.00 21.19 ?  358 GLN A C   1 
ATOM   2555 O  O   . GLN A 1 358 ? -27.897 31.337  -12.694 1.00 19.90 ?  358 GLN A O   1 
ATOM   2556 C  CB  . GLN A 1 358 ? -25.404 32.362  -14.363 1.00 26.59 ?  358 GLN A CB  1 
ATOM   2557 C  CG  . GLN A 1 358 ? -26.520 32.389  -15.361 1.00 30.12 ?  358 GLN A CG  1 
ATOM   2558 C  CD  . GLN A 1 358 ? -26.008 32.475  -16.797 1.00 30.39 ?  358 GLN A CD  1 
ATOM   2559 O  OE1 . GLN A 1 358 ? -24.800 32.608  -17.027 1.00 31.84 ?  358 GLN A OE1 1 
ATOM   2560 N  NE2 . GLN A 1 358 ? -26.907 32.342  -17.763 1.00 33.17 ?  358 GLN A NE2 1 
ATOM   2561 N  N   . HIS A 1 359 ? -26.138 30.225  -11.862 1.00 21.63 ?  359 HIS A N   1 
ATOM   2562 C  CA  . HIS A 1 359 ? -26.949 29.067  -11.504 1.00 22.04 ?  359 HIS A CA  1 
ATOM   2563 C  C   . HIS A 1 359 ? -27.312 29.034  -10.020 1.00 19.52 ?  359 HIS A C   1 
ATOM   2564 O  O   . HIS A 1 359 ? -27.724 27.981  -9.513  1.00 23.05 ?  359 HIS A O   1 
ATOM   2565 C  CB  . HIS A 1 359 ? -26.236 27.774  -11.928 1.00 17.85 ?  359 HIS A CB  1 
ATOM   2566 C  CG  . HIS A 1 359 ? -26.046 27.657  -13.412 1.00 18.62 ?  359 HIS A CG  1 
ATOM   2567 N  ND1 . HIS A 1 359 ? -27.091 27.413  -14.280 1.00 21.02 ?  359 HIS A ND1 1 
ATOM   2568 C  CD2 . HIS A 1 359 ? -24.940 27.781  -14.182 1.00 18.51 ?  359 HIS A CD2 1 
ATOM   2569 C  CE1 . HIS A 1 359 ? -26.631 27.370  -15.519 1.00 21.97 ?  359 HIS A CE1 1 
ATOM   2570 N  NE2 . HIS A 1 359 ? -25.329 27.596  -15.487 1.00 22.15 ?  359 HIS A NE2 1 
ATOM   2571 N  N   . PHE A 1 360 ? -27.154 30.156  -9.313  1.00 20.51 ?  360 PHE A N   1 
ATOM   2572 C  CA  . PHE A 1 360 ? -27.611 30.265  -7.927  1.00 20.67 ?  360 PHE A CA  1 
ATOM   2573 C  C   . PHE A 1 360 ? -29.024 29.717  -7.812  1.00 19.74 ?  360 PHE A C   1 
ATOM   2574 O  O   . PHE A 1 360 ? -29.864 29.946  -8.685  1.00 17.68 ?  360 PHE A O   1 
ATOM   2575 C  CB  . PHE A 1 360 ? -27.570 31.730  -7.466  1.00 20.35 ?  360 PHE A CB  1 
ATOM   2576 C  CG  . PHE A 1 360 ? -27.938 31.947  -6.012  1.00 24.35 ?  360 PHE A CG  1 
ATOM   2577 C  CD1 . PHE A 1 360 ? -26.975 31.839  -5.006  1.00 19.76 ?  360 PHE A CD1 1 
ATOM   2578 C  CD2 . PHE A 1 360 ? -29.233 32.313  -5.654  1.00 22.35 ?  360 PHE A CD2 1 
ATOM   2579 C  CE1 . PHE A 1 360 ? -27.296 32.073  -3.668  1.00 21.89 ?  360 PHE A CE1 1 
ATOM   2580 C  CE2 . PHE A 1 360 ? -29.565 32.548  -4.308  1.00 20.71 ?  360 PHE A CE2 1 
ATOM   2581 C  CZ  . PHE A 1 360 ? -28.596 32.421  -3.316  1.00 22.56 ?  360 PHE A CZ  1 
ATOM   2582 N  N   . CYS A 1 361 ? -29.270 28.967  -6.746  1.00 21.48 ?  361 CYS A N   1 
ATOM   2583 C  CA  . CYS A 1 361 ? -30.509 28.219  -6.645  1.00 19.74 ?  361 CYS A CA  1 
ATOM   2584 C  C   . CYS A 1 361 ? -31.707 29.158  -6.799  1.00 21.85 ?  361 CYS A C   1 
ATOM   2585 O  O   . CYS A 1 361 ? -31.807 30.151  -6.063  1.00 22.50 ?  361 CYS A O   1 
ATOM   2586 C  CB  . CYS A 1 361 ? -30.563 27.478  -5.314  1.00 20.40 ?  361 CYS A CB  1 
ATOM   2587 S  SG  . CYS A 1 361 ? -32.200 26.859  -4.915  1.00 19.76 ?  361 CYS A SG  1 
ATOM   2588 N  N   . PRO A 1 362 ? -32.597 28.919  -7.767  1.00 20.95 ?  362 PRO A N   1 
ATOM   2589 C  CA  . PRO A 1 362 ? -33.780 29.780  -7.934  1.00 20.24 ?  362 PRO A CA  1 
ATOM   2590 C  C   . PRO A 1 362 ? -34.819 29.605  -6.846  1.00 21.67 ?  362 PRO A C   1 
ATOM   2591 O  O   . PRO A 1 362 ? -35.816 30.338  -6.836  1.00 24.75 ?  362 PRO A O   1 
ATOM   2592 C  CB  . PRO A 1 362 ? -34.341 29.330  -9.290  1.00 18.96 ?  362 PRO A CB  1 
ATOM   2593 C  CG  . PRO A 1 362 ? -34.024 27.882  -9.316  1.00 21.14 ?  362 PRO A CG  1 
ATOM   2594 C  CD  . PRO A 1 362 ? -32.610 27.794  -8.712  1.00 19.85 ?  362 PRO A CD  1 
ATOM   2595 N  N   . ALA A 1 363 ? -34.618 28.677  -5.922  1.00 18.06 ?  363 ALA A N   1 
ATOM   2596 C  CA  . ALA A 1 363 ? -35.605 28.402  -4.894  1.00 21.51 ?  363 ALA A CA  1 
ATOM   2597 C  C   . ALA A 1 363 ? -35.045 28.624  -3.490  1.00 17.56 ?  363 ALA A C   1 
ATOM   2598 O  O   . ALA A 1 363 ? -35.549 28.043  -2.522  1.00 20.85 ?  363 ALA A O   1 
ATOM   2599 C  CB  . ALA A 1 363 ? -36.145 26.981  -5.046  1.00 20.97 ?  363 ALA A CB  1 
ATOM   2600 N  N   . SER A 1 364 ? -34.015 29.470  -3.357  1.00 19.73 ?  364 SER A N   1 
ATOM   2601 C  CA  . SER A 1 364 ? -33.370 29.642  -2.050  1.00 21.15 ?  364 SER A CA  1 
ATOM   2602 C  C   . SER A 1 364 ? -34.371 30.069  -0.980  1.00 20.34 ?  364 SER A C   1 
ATOM   2603 O  O   . SER A 1 364 ? -34.345 29.552  0.140   1.00 23.54 ?  364 SER A O   1 
ATOM   2604 C  CB  . SER A 1 364 ? -32.227 30.655  -2.132  1.00 20.94 ?  364 SER A CB  1 
ATOM   2605 O  OG  . SER A 1 364 ? -32.687 31.932  -2.546  1.00 22.93 ?  364 SER A OG  1 
ATOM   2606 N  N   . ALA A 1 365 ? -35.274 30.993  -1.309  1.00 23.14 ?  365 ALA A N   1 
ATOM   2607 C  CA  . ALA A 1 365 ? -36.222 31.471  -0.304  1.00 19.86 ?  365 ALA A CA  1 
ATOM   2608 C  C   . ALA A 1 365 ? -37.162 30.353  0.143   1.00 18.27 ?  365 ALA A C   1 
ATOM   2609 O  O   . ALA A 1 365 ? -37.482 30.238  1.331   1.00 21.14 ?  365 ALA A O   1 
ATOM   2610 C  CB  . ALA A 1 365 ? -36.992 32.668  -0.857  1.00 19.05 ?  365 ALA A CB  1 
ATOM   2611 N  N   . LEU A 1 366 ? -37.584 29.502  -0.792  1.00 19.73 ?  366 LEU A N   1 
ATOM   2612 C  CA  . LEU A 1 366 ? -38.428 28.357  -0.458  1.00 20.04 ?  366 LEU A CA  1 
ATOM   2613 C  C   . LEU A 1 366 ? -37.679 27.354  0.404   1.00 19.87 ?  366 LEU A C   1 
ATOM   2614 O  O   . LEU A 1 366 ? -38.222 26.833  1.386   1.00 19.02 ?  366 LEU A O   1 
ATOM   2615 C  CB  . LEU A 1 366 ? -38.908 27.679  -1.740  1.00 24.54 ?  366 LEU A CB  1 
ATOM   2616 C  CG  . LEU A 1 366 ? -39.954 26.583  -1.544  1.00 28.02 ?  366 LEU A CG  1 
ATOM   2617 C  CD1 . LEU A 1 366 ? -41.235 27.185  -1.000  1.00 29.91 ?  366 LEU A CD1 1 
ATOM   2618 C  CD2 . LEU A 1 366 ? -40.216 25.900  -2.850  1.00 27.40 ?  366 LEU A CD2 1 
ATOM   2619 N  N   . GLY A 1 367 ? -36.429 27.062  0.045   1.00 17.89 ?  367 GLY A N   1 
ATOM   2620 C  CA  . GLY A 1 367 ? -35.631 26.172  0.865   1.00 16.85 ?  367 GLY A CA  1 
ATOM   2621 C  C   . GLY A 1 367 ? -35.478 26.680  2.287   1.00 20.11 ?  367 GLY A C   1 
ATOM   2622 O  O   . GLY A 1 367 ? -35.558 25.902  3.237   1.00 19.82 ?  367 GLY A O   1 
ATOM   2623 N  N   . ARG A 1 368 ? -35.245 27.994  2.450   1.00 20.30 ?  368 ARG A N   1 
ATOM   2624 C  CA  . ARG A 1 368 ? -35.134 28.570  3.789   1.00 21.51 ?  368 ARG A CA  1 
ATOM   2625 C  C   . ARG A 1 368 ? -36.447 28.434  4.553   1.00 20.47 ?  368 ARG A C   1 
ATOM   2626 O  O   . ARG A 1 368 ? -36.468 28.002  5.715   1.00 22.29 ?  368 ARG A O   1 
ATOM   2627 C  CB  . ARG A 1 368 ? -34.724 30.046  3.715   1.00 21.03 ?  368 ARG A CB  1 
ATOM   2628 C  CG  . ARG A 1 368 ? -33.376 30.358  3.036   1.00 25.48 ?  368 ARG A CG  1 
ATOM   2629 C  CD  . ARG A 1 368 ? -33.184 31.892  2.871   1.00 28.79 ?  368 ARG A CD  1 
ATOM   2630 N  NE  . ARG A 1 368 ? -31.876 32.246  2.325   1.00 25.57 ?  368 ARG A NE  1 
ATOM   2631 C  CZ  . ARG A 1 368 ? -30.753 32.209  3.028   1.00 26.00 ?  368 ARG A CZ  1 
ATOM   2632 N  NH1 . ARG A 1 368 ? -30.754 31.860  4.303   1.00 22.04 ?  368 ARG A NH1 1 
ATOM   2633 N  NH2 . ARG A 1 368 ? -29.601 32.514  2.434   1.00 27.23 ?  368 ARG A NH2 1 
ATOM   2634 N  N   . THR A 1 369 ? -37.555 28.810  3.914   1.00 20.52 ?  369 THR A N   1 
ATOM   2635 C  CA  . THR A 1 369 ? -38.857 28.733  4.566   1.00 22.69 ?  369 THR A CA  1 
ATOM   2636 C  C   . THR A 1 369 ? -39.166 27.310  4.996   1.00 20.42 ?  369 THR A C   1 
ATOM   2637 O  O   . THR A 1 369 ? -39.608 27.067  6.126   1.00 20.89 ?  369 THR A O   1 
ATOM   2638 C  CB  . THR A 1 369 ? -39.944 29.231  3.621   1.00 25.82 ?  369 THR A CB  1 
ATOM   2639 O  OG1 . THR A 1 369 ? -39.605 30.542  3.171   1.00 29.60 ?  369 THR A OG1 1 
ATOM   2640 C  CG2 . THR A 1 369 ? -41.285 29.250  4.330   1.00 23.19 ?  369 THR A CG2 1 
ATOM   2641 N  N   . HIS A 1 370 ? -38.951 26.363  4.083   1.00 18.22 ?  370 HIS A N   1 
ATOM   2642 C  CA  . HIS A 1 370 ? -39.148 24.948  4.364   1.00 17.73 ?  370 HIS A CA  1 
ATOM   2643 C  C   . HIS A 1 370 ? -38.446 24.557  5.653   1.00 19.70 ?  370 HIS A C   1 
ATOM   2644 O  O   . HIS A 1 370 ? -39.063 23.994  6.567   1.00 18.71 ?  370 HIS A O   1 
ATOM   2645 C  CB  . HIS A 1 370 ? -38.630 24.140  3.171   1.00 17.46 ?  370 HIS A CB  1 
ATOM   2646 C  CG  . HIS A 1 370 ? -38.910 22.668  3.233   1.00 17.30 ?  370 HIS A CG  1 
ATOM   2647 N  ND1 . HIS A 1 370 ? -38.144 21.785  3.965   1.00 19.14 ?  370 HIS A ND1 1 
ATOM   2648 C  CD2 . HIS A 1 370 ? -39.850 21.921  2.605   1.00 15.40 ?  370 HIS A CD2 1 
ATOM   2649 C  CE1 . HIS A 1 370 ? -38.617 20.558  3.805   1.00 18.70 ?  370 HIS A CE1 1 
ATOM   2650 N  NE2 . HIS A 1 370 ? -39.653 20.615  2.984   1.00 18.18 ?  370 HIS A NE2 1 
ATOM   2651 N  N   . ALA A 1 371 ? -37.154 24.891  5.760   1.00 18.43 ?  371 ALA A N   1 
ATOM   2652 C  CA  . ALA A 1 371 ? -36.367 24.443  6.904   1.00 16.17 ?  371 ALA A CA  1 
ATOM   2653 C  C   . ALA A 1 371 ? -36.708 25.236  8.158   1.00 18.85 ?  371 ALA A C   1 
ATOM   2654 O  O   . ALA A 1 371 ? -36.789 24.667  9.251   1.00 15.25 ?  371 ALA A O   1 
ATOM   2655 C  CB  . ALA A 1 371 ? -34.876 24.562  6.598   1.00 17.27 ?  371 ALA A CB  1 
ATOM   2656 N  N   . GLU A 1 372 ? -36.889 26.554  8.020   1.00 17.68 ?  372 GLU A N   1 
ATOM   2657 C  CA  . GLU A 1 372 ? -37.225 27.382  9.173   1.00 19.40 ?  372 GLU A CA  1 
ATOM   2658 C  C   . GLU A 1 372 ? -38.490 26.888  9.854   1.00 16.64 ?  372 GLU A C   1 
ATOM   2659 O  O   . GLU A 1 372 ? -38.536 26.734  11.080  1.00 18.78 ?  372 GLU A O   1 
ATOM   2660 C  CB  . GLU A 1 372 ? -37.398 28.845  8.753   1.00 18.26 ?  372 GLU A CB  1 
ATOM   2661 C  CG  . GLU A 1 372 ? -36.099 29.511  8.311   1.00 18.95 ?  372 GLU A CG  1 
ATOM   2662 C  CD  . GLU A 1 372 ? -36.323 30.861  7.651   1.00 24.64 ?  372 GLU A CD  1 
ATOM   2663 O  OE1 . GLU A 1 372 ? -37.425 31.406  7.801   1.00 32.20 ?  372 GLU A OE1 1 
ATOM   2664 O  OE2 . GLU A 1 372 ? -35.397 31.375  6.994   1.00 22.75 ?  372 GLU A OE2 1 
ATOM   2665 N  N   . ILE A 1 373 ? -39.536 26.646  9.077   1.00 19.80 ?  373 ILE A N   1 
ATOM   2666 C  CA  . ILE A 1 373 ? -40.805 26.290  9.689   1.00 18.87 ?  373 ILE A CA  1 
ATOM   2667 C  C   . ILE A 1 373 ? -40.707 24.915  10.345  1.00 19.87 ?  373 ILE A C   1 
ATOM   2668 O  O   . ILE A 1 373 ? -41.149 24.728  11.485  1.00 17.86 ?  373 ILE A O   1 
ATOM   2669 C  CB  . ILE A 1 373 ? -41.928 26.390  8.642   1.00 23.04 ?  373 ILE A CB  1 
ATOM   2670 C  CG1 . ILE A 1 373 ? -42.172 27.875  8.317   1.00 21.95 ?  373 ILE A CG1 1 
ATOM   2671 C  CG2 . ILE A 1 373 ? -43.190 25.722  9.143   1.00 21.78 ?  373 ILE A CG2 1 
ATOM   2672 C  CD1 . ILE A 1 373 ? -43.120 28.137  7.172   1.00 21.67 ?  373 ILE A CD1 1 
ATOM   2673 N  N   . ALA A 1 374 ? -40.076 23.949  9.664   1.00 17.33 ?  374 ALA A N   1 
ATOM   2674 C  CA  . ALA A 1 374 ? -39.903 22.613  10.244  1.00 18.88 ?  374 ALA A CA  1 
ATOM   2675 C  C   . ALA A 1 374 ? -39.114 22.664  11.551  1.00 16.17 ?  374 ALA A C   1 
ATOM   2676 O  O   . ALA A 1 374 ? -39.495 22.027  12.547  1.00 16.48 ?  374 ALA A O   1 
ATOM   2677 C  CB  . ALA A 1 374 ? -39.195 21.688  9.239   1.00 15.50 ?  374 ALA A CB  1 
ATOM   2678 N  N   . LEU A 1 375 ? -38.011 23.414  11.572  1.00 16.00 ?  375 LEU A N   1 
ATOM   2679 C  CA  . LEU A 1 375 ? -37.153 23.430  12.759  1.00 15.90 ?  375 LEU A CA  1 
ATOM   2680 C  C   . LEU A 1 375 ? -37.791 24.195  13.917  1.00 18.14 ?  375 LEU A C   1 
ATOM   2681 O  O   . LEU A 1 375 ? -37.600 23.822  15.079  1.00 15.77 ?  375 LEU A O   1 
ATOM   2682 C  CB  . LEU A 1 375 ? -35.793 24.020  12.411  1.00 16.48 ?  375 LEU A CB  1 
ATOM   2683 C  CG  . LEU A 1 375 ? -34.954 23.141  11.476  1.00 15.47 ?  375 LEU A CG  1 
ATOM   2684 C  CD1 . LEU A 1 375 ? -33.732 23.920  10.948  1.00 18.21 ?  375 LEU A CD1 1 
ATOM   2685 C  CD2 . LEU A 1 375 ? -34.523 21.852  12.160  1.00 16.32 ?  375 LEU A CD2 1 
ATOM   2686 N  N   . THR A 1 376 ? -38.559 25.248  13.621  1.00 17.93 ?  376 THR A N   1 
ATOM   2687 C  CA  . THR A 1 376 ? -39.327 25.927  14.662  1.00 18.21 ?  376 THR A CA  1 
ATOM   2688 C  C   . THR A 1 376 ? -40.331 24.973  15.304  1.00 20.25 ?  376 THR A C   1 
ATOM   2689 O  O   . THR A 1 376 ? -40.412 24.870  16.533  1.00 17.89 ?  376 THR A O   1 
ATOM   2690 C  CB  . THR A 1 376 ? -40.036 27.152  14.076  1.00 18.13 ?  376 THR A CB  1 
ATOM   2691 O  OG1 . THR A 1 376 ? -39.069 28.126  13.656  1.00 20.20 ?  376 THR A OG1 1 
ATOM   2692 C  CG2 . THR A 1 376 ? -40.961 27.788  15.109  1.00 23.22 ?  376 THR A CG2 1 
ATOM   2693 N  N   . ALA A 1 377 ? -41.091 24.245  14.480  1.00 18.07 ?  377 ALA A N   1 
ATOM   2694 C  CA  . ALA A 1 377 ? -42.005 23.243  15.017  1.00 17.92 ?  377 ALA A CA  1 
ATOM   2695 C  C   . ALA A 1 377 ? -41.254 22.179  15.808  1.00 18.37 ?  377 ALA A C   1 
ATOM   2696 O  O   . ALA A 1 377 ? -41.721 21.724  16.860  1.00 19.85 ?  377 ALA A O   1 
ATOM   2697 C  CB  . ALA A 1 377 ? -42.804 22.607  13.876  1.00 17.89 ?  377 ALA A CB  1 
ATOM   2698 N  N   . LEU A 1 378 ? -40.072 21.782  15.328  1.00 17.98 ?  378 LEU A N   1 
ATOM   2699 C  CA  . LEU A 1 378 ? -39.347 20.684  15.965  1.00 15.81 ?  378 LEU A CA  1 
ATOM   2700 C  C   . LEU A 1 378 ? -38.895 21.050  17.374  1.00 17.68 ?  378 LEU A C   1 
ATOM   2701 O  O   . LEU A 1 378 ? -39.044 20.252  18.305  1.00 17.49 ?  378 LEU A O   1 
ATOM   2702 C  CB  . LEU A 1 378 ? -38.140 20.282  15.105  1.00 16.69 ?  378 LEU A CB  1 
ATOM   2703 C  CG  . LEU A 1 378 ? -37.294 19.121  15.632  1.00 17.55 ?  378 LEU A CG  1 
ATOM   2704 C  CD1 . LEU A 1 378 ? -38.018 17.802  15.492  1.00 19.93 ?  378 LEU A CD1 1 
ATOM   2705 C  CD2 . LEU A 1 378 ? -35.984 19.068  14.875  1.00 16.12 ?  378 LEU A CD2 1 
ATOM   2706 N  N   . VAL A 1 379 ? -38.290 22.230  17.548  1.00 17.04 ?  379 VAL A N   1 
ATOM   2707 C  CA  . VAL A 1 379 ? -37.762 22.548  18.873  1.00 19.18 ?  379 VAL A CA  1 
ATOM   2708 C  C   . VAL A 1 379 ? -38.907 22.862  19.838  1.00 17.06 ?  379 VAL A C   1 
ATOM   2709 O  O   . VAL A 1 379 ? -38.774 22.657  21.051  1.00 16.32 ?  379 VAL A O   1 
ATOM   2710 C  CB  . VAL A 1 379 ? -36.725 23.692  18.822  1.00 18.26 ?  379 VAL A CB  1 
ATOM   2711 C  CG1 . VAL A 1 379 ? -35.525 23.351  17.878  1.00 16.77 ?  379 VAL A CG1 1 
ATOM   2712 C  CG2 . VAL A 1 379 ? -37.377 25.027  18.472  1.00 20.60 ?  379 VAL A CG2 1 
ATOM   2713 N  N   . GLU A 1 380 ? -40.058 23.305  19.326  1.00 16.83 ?  380 GLU A N   1 
ATOM   2714 C  CA  . GLU A 1 380 ? -41.221 23.476  20.199  1.00 21.53 ?  380 GLU A CA  1 
ATOM   2715 C  C   . GLU A 1 380 ? -41.774 22.122  20.644  1.00 19.39 ?  380 GLU A C   1 
ATOM   2716 O  O   . GLU A 1 380 ? -42.026 21.904  21.836  1.00 21.20 ?  380 GLU A O   1 
ATOM   2717 C  CB  . GLU A 1 380 ? -42.302 24.306  19.497  1.00 22.69 ?  380 GLU A CB  1 
ATOM   2718 C  CG  . GLU A 1 380 ? -41.963 25.817  19.345  1.00 32.20 ?  380 GLU A CG  1 
ATOM   2719 C  CD  . GLU A 1 380 ? -42.953 26.566  18.436  1.00 38.81 ?  380 GLU A CD  1 
ATOM   2720 O  OE1 . GLU A 1 380 ? -43.954 25.941  18.010  1.00 35.81 ?  380 GLU A OE1 1 
ATOM   2721 O  OE2 . GLU A 1 380 ? -42.752 27.780  18.181  1.00 37.63 ?  380 GLU A OE2 1 
ATOM   2722 N  N   . LYS A 1 381 ? -41.959 21.196  19.697  1.00 21.31 ?  381 LYS A N   1 
ATOM   2723 C  CA  . LYS A 1 381 ? -42.688 19.961  19.976  1.00 18.05 ?  381 LYS A CA  1 
ATOM   2724 C  C   . LYS A 1 381 ? -41.818 18.898  20.618  1.00 21.38 ?  381 LYS A C   1 
ATOM   2725 O  O   . LYS A 1 381 ? -42.339 18.037  21.327  1.00 18.85 ?  381 LYS A O   1 
ATOM   2726 C  CB  . LYS A 1 381 ? -43.282 19.389  18.690  1.00 18.71 ?  381 LYS A CB  1 
ATOM   2727 C  CG  . LYS A 1 381 ? -44.277 20.316  18.007  1.00 26.42 ?  381 LYS A CG  1 
ATOM   2728 C  CD  . LYS A 1 381 ? -45.493 20.534  18.899  1.00 28.05 ?  381 LYS A CD  1 
ATOM   2729 C  CE  . LYS A 1 381 ? -46.523 21.391  18.209  1.00 32.01 ?  381 LYS A CE  1 
ATOM   2730 N  NZ  . LYS A 1 381 ? -47.715 21.645  19.062  1.00 33.62 ?  381 LYS A NZ  1 
ATOM   2731 N  N   . LEU A 1 382 ? -40.508 18.918  20.372  1.00 17.20 ?  382 LEU A N   1 
ATOM   2732 C  CA  . LEU A 1 382 ? -39.601 17.888  20.883  1.00 18.53 ?  382 LEU A CA  1 
ATOM   2733 C  C   . LEU A 1 382 ? -38.479 18.556  21.665  1.00 26.49 ?  382 LEU A C   1 
ATOM   2734 O  O   . LEU A 1 382 ? -37.302 18.444  21.298  1.00 20.57 ?  382 LEU A O   1 
ATOM   2735 C  CB  . LEU A 1 382 ? -39.030 17.037  19.744  1.00 20.11 ?  382 LEU A CB  1 
ATOM   2736 C  CG  . LEU A 1 382 ? -39.983 16.372  18.732  1.00 22.51 ?  382 LEU A CG  1 
ATOM   2737 C  CD1 . LEU A 1 382 ? -39.227 15.387  17.815  1.00 17.89 ?  382 LEU A CD1 1 
ATOM   2738 C  CD2 . LEU A 1 382 ? -41.119 15.664  19.429  1.00 18.52 ?  382 LEU A CD2 1 
ATOM   2739 N  N   . PRO A 1 383 ? -38.805 19.245  22.769  1.00 22.18 ?  383 PRO A N   1 
ATOM   2740 C  CA  . PRO A 1 383 ? -37.784 20.064  23.437  1.00 22.65 ?  383 PRO A CA  1 
ATOM   2741 C  C   . PRO A 1 383 ? -36.577 19.271  23.932  1.00 22.12 ?  383 PRO A C   1 
ATOM   2742 O  O   . PRO A 1 383 ? -35.495 19.860  24.065  1.00 22.51 ?  383 PRO A O   1 
ATOM   2743 C  CB  . PRO A 1 383 ? -38.551 20.720  24.602  1.00 22.96 ?  383 PRO A CB  1 
ATOM   2744 C  CG  . PRO A 1 383 ? -39.703 19.827  24.866  1.00 22.92 ?  383 PRO A CG  1 
ATOM   2745 C  CD  . PRO A 1 383 ? -40.083 19.248  23.505  1.00 21.48 ?  383 PRO A CD  1 
ATOM   2746 N  N   . ALA A 1 384 ? -36.708 17.967  24.188  1.00 18.99 ?  384 ALA A N   1 
ATOM   2747 C  CA  . ALA A 1 384 ? -35.576 17.172  24.649  1.00 22.30 ?  384 ALA A CA  1 
ATOM   2748 C  C   . ALA A 1 384 ? -34.929 16.341  23.532  1.00 18.94 ?  384 ALA A C   1 
ATOM   2749 O  O   . ALA A 1 384 ? -34.176 15.399  23.821  1.00 17.91 ?  384 ALA A O   1 
ATOM   2750 C  CB  . ALA A 1 384 ? -35.996 16.275  25.818  1.00 22.42 ?  384 ALA A CB  1 
ATOM   2751 N  N   . LEU A 1 385 ? -35.193 16.686  22.271  1.00 18.63 ?  385 LEU A N   1 
ATOM   2752 C  CA  . LEU A 1 385 ? -34.616 16.014  21.108  1.00 21.03 ?  385 LEU A CA  1 
ATOM   2753 C  C   . LEU A 1 385 ? -33.132 15.699  21.291  1.00 19.71 ?  385 LEU A C   1 
ATOM   2754 O  O   . LEU A 1 385 ? -32.340 16.568  21.651  1.00 17.92 ?  385 LEU A O   1 
ATOM   2755 C  CB  . LEU A 1 385 ? -34.788 16.902  19.872  1.00 16.86 ?  385 LEU A CB  1 
ATOM   2756 C  CG  . LEU A 1 385 ? -34.294 16.313  18.542  1.00 22.57 ?  385 LEU A CG  1 
ATOM   2757 C  CD1 . LEU A 1 385 ? -35.296 15.302  18.028  1.00 20.12 ?  385 LEU A CD1 1 
ATOM   2758 C  CD2 . LEU A 1 385 ? -34.067 17.417  17.498  1.00 19.48 ?  385 LEU A CD2 1 
ATOM   2759 N  N   . ARG A 1 386 ? -32.769 14.451  21.009  1.00 18.10 ?  386 ARG A N   1 
ATOM   2760 C  CA  . ARG A 1 386 ? -31.394 13.962  21.024  1.00 20.68 ?  386 ARG A CA  1 
ATOM   2761 C  C   . ARG A 1 386 ? -31.362 12.712  20.163  1.00 19.02 ?  386 ARG A C   1 
ATOM   2762 O  O   . ARG A 1 386 ? -32.405 12.099  19.914  1.00 17.90 ?  386 ARG A O   1 
ATOM   2763 C  CB  . ARG A 1 386 ? -30.908 13.638  22.447  1.00 18.92 ?  386 ARG A CB  1 
ATOM   2764 C  CG  . ARG A 1 386 ? -31.742 12.571  23.166  1.00 18.85 ?  386 ARG A CG  1 
ATOM   2765 C  CD  . ARG A 1 386 ? -31.515 12.650  24.685  1.00 24.44 ?  386 ARG A CD  1 
ATOM   2766 N  NE  . ARG A 1 386 ? -32.194 11.587  25.414  1.00 24.17 ?  386 ARG A NE  1 
ATOM   2767 C  CZ  . ARG A 1 386 ? -33.457 11.633  25.820  1.00 23.86 ?  386 ARG A CZ  1 
ATOM   2768 N  NH1 . ARG A 1 386 ? -34.226 12.688  25.582  1.00 26.46 ?  386 ARG A NH1 1 
ATOM   2769 N  NH2 . ARG A 1 386 ? -33.960 10.596  26.485  1.00 26.62 ?  386 ARG A NH2 1 
ATOM   2770 N  N   . LEU A 1 387 ? -30.157 12.335  19.719  1.00 18.43 ?  387 LEU A N   1 
ATOM   2771 C  CA  . LEU A 1 387 ? -29.990 11.109  18.945  1.00 17.32 ?  387 LEU A CA  1 
ATOM   2772 C  C   . LEU A 1 387 ? -30.162 9.906   19.857  1.00 20.93 ?  387 LEU A C   1 
ATOM   2773 O  O   . LEU A 1 387 ? -29.810 9.948   21.038  1.00 21.66 ?  387 LEU A O   1 
ATOM   2774 C  CB  . LEU A 1 387 ? -28.603 11.036  18.282  1.00 16.72 ?  387 LEU A CB  1 
ATOM   2775 C  CG  . LEU A 1 387 ? -28.236 12.069  17.204  1.00 22.59 ?  387 LEU A CG  1 
ATOM   2776 C  CD1 . LEU A 1 387 ? -26.892 11.705  16.570  1.00 19.78 ?  387 LEU A CD1 1 
ATOM   2777 C  CD2 . LEU A 1 387 ? -29.336 12.186  16.129  1.00 18.02 ?  387 LEU A CD2 1 
ATOM   2778 N  N   . ALA A 1 388 ? -30.693 8.815   19.283  1.00 18.95 ?  388 ALA A N   1 
ATOM   2779 C  CA  . ALA A 1 388 ? -30.991 7.600   20.022  1.00 20.50 ?  388 ALA A CA  1 
ATOM   2780 C  C   . ALA A 1 388 ? -29.756 6.742   20.274  1.00 22.10 ?  388 ALA A C   1 
ATOM   2781 O  O   . ALA A 1 388 ? -29.810 5.847   21.115  1.00 15.75 ?  388 ALA A O   1 
ATOM   2782 C  CB  . ALA A 1 388 ? -32.036 6.773   19.266  1.00 18.25 ?  388 ALA A CB  1 
ATOM   2783 N  N   . LEU A 1 389 ? -28.671 6.987   19.553  1.00 19.72 ?  389 LEU A N   1 
ATOM   2784 C  CA  . LEU A 1 389 ? -27.421 6.249   19.676  1.00 20.88 ?  389 LEU A CA  1 
ATOM   2785 C  C   . LEU A 1 389 ? -26.311 7.226   19.314  1.00 21.02 ?  389 LEU A C   1 
ATOM   2786 O  O   . LEU A 1 389 ? -26.591 8.349   18.888  1.00 20.19 ?  389 LEU A O   1 
ATOM   2787 C  CB  . LEU A 1 389 ? -27.424 5.005   18.771  1.00 22.86 ?  389 LEU A CB  1 
ATOM   2788 C  CG  . LEU A 1 389 ? -27.537 5.103   17.238  1.00 27.83 ?  389 LEU A CG  1 
ATOM   2789 C  CD1 . LEU A 1 389 ? -26.187 5.451   16.632  1.00 24.71 ?  389 LEU A CD1 1 
ATOM   2790 C  CD2 . LEU A 1 389 ? -28.067 3.848   16.589  1.00 23.41 ?  389 LEU A CD2 1 
ATOM   2791 N  N   . PRO A 1 390 ? -25.040 6.862   19.521  1.00 23.60 ?  390 PRO A N   1 
ATOM   2792 C  CA  . PRO A 1 390 ? -23.967 7.825   19.209  1.00 18.89 ?  390 PRO A CA  1 
ATOM   2793 C  C   . PRO A 1 390 ? -23.960 8.209   17.731  1.00 22.92 ?  390 PRO A C   1 
ATOM   2794 O  O   . PRO A 1 390 ? -24.230 7.382   16.860  1.00 17.01 ?  390 PRO A O   1 
ATOM   2795 C  CB  . PRO A 1 390 ? -22.682 7.075   19.601  1.00 23.24 ?  390 PRO A CB  1 
ATOM   2796 C  CG  . PRO A 1 390 ? -23.117 6.070   20.625  1.00 23.16 ?  390 PRO A CG  1 
ATOM   2797 C  CD  . PRO A 1 390 ? -24.504 5.650   20.177  1.00 22.85 ?  390 PRO A CD  1 
ATOM   2798 N  N   . VAL A 1 391 ? -23.628 9.481   17.457  1.00 19.18 ?  391 VAL A N   1 
ATOM   2799 C  CA  . VAL A 1 391 ? -23.690 10.003  16.086  1.00 20.65 ?  391 VAL A CA  1 
ATOM   2800 C  C   . VAL A 1 391 ? -22.832 9.165   15.136  1.00 22.20 ?  391 VAL A C   1 
ATOM   2801 O  O   . VAL A 1 391 ? -23.209 8.949   13.979  1.00 20.31 ?  391 VAL A O   1 
ATOM   2802 C  CB  . VAL A 1 391 ? -23.281 11.493  16.062  1.00 25.48 ?  391 VAL A CB  1 
ATOM   2803 C  CG1 . VAL A 1 391 ? -21.785 11.674  16.381  1.00 22.04 ?  391 VAL A CG1 1 
ATOM   2804 C  CG2 . VAL A 1 391 ? -23.646 12.159  14.730  1.00 17.94 ?  391 VAL A CG2 1 
ATOM   2805 N  N   . GLU A 1 392 ? -21.684 8.655   15.614  1.00 21.05 ?  392 GLU A N   1 
ATOM   2806 C  CA  . GLU A 1 392 ? -20.789 7.863   14.764  1.00 24.97 ?  392 GLU A CA  1 
ATOM   2807 C  C   . GLU A 1 392 ? -21.426 6.581   14.259  1.00 22.99 ?  392 GLU A C   1 
ATOM   2808 O  O   . GLU A 1 392 ? -20.851 5.936   13.381  1.00 24.06 ?  392 GLU A O   1 
ATOM   2809 C  CB  . GLU A 1 392 ? -19.500 7.446   15.495  1.00 23.24 ?  392 GLU A CB  1 
ATOM   2810 C  CG  . GLU A 1 392 ? -18.587 8.563   15.894  1.00 33.28 ?  392 GLU A CG  1 
ATOM   2811 C  CD  . GLU A 1 392 ? -18.985 9.169   17.227  1.00 32.62 ?  392 GLU A CD  1 
ATOM   2812 O  OE1 . GLU A 1 392 ? -20.015 8.749   17.813  1.00 39.35 ?  392 GLU A OE1 1 
ATOM   2813 O  OE2 . GLU A 1 392 ? -18.277 10.089  17.667  1.00 30.38 ?  392 GLU A OE2 1 
ATOM   2814 N  N   . GLN A 1 393 ? -22.551 6.153   14.828  1.00 20.46 ?  393 GLN A N   1 
ATOM   2815 C  CA  . GLN A 1 393 ? -23.164 4.898   14.413  1.00 23.47 ?  393 GLN A CA  1 
ATOM   2816 C  C   . GLN A 1 393 ? -24.354 5.121   13.499  1.00 22.14 ?  393 GLN A C   1 
ATOM   2817 O  O   . GLN A 1 393 ? -25.050 4.161   13.156  1.00 22.27 ?  393 GLN A O   1 
ATOM   2818 C  CB  . GLN A 1 393 ? -23.549 4.056   15.641  1.00 23.75 ?  393 GLN A CB  1 
ATOM   2819 C  CG  . GLN A 1 393 ? -22.313 3.609   16.447  1.00 25.40 ?  393 GLN A CG  1 
ATOM   2820 C  CD  . GLN A 1 393 ? -22.635 3.048   17.828  1.00 25.10 ?  393 GLN A CD  1 
ATOM   2821 O  OE1 . GLN A 1 393 ? -21.967 3.379   18.815  1.00 23.74 ?  393 GLN A OE1 1 
ATOM   2822 N  NE2 . GLN A 1 393 ? -23.650 2.197   17.903  1.00 22.25 ?  393 GLN A NE2 1 
ATOM   2823 N  N   . LEU A 1 394 ? -24.602 6.369   13.097  1.00 20.22 ?  394 LEU A N   1 
ATOM   2824 C  CA  . LEU A 1 394 ? -25.551 6.617   12.020  1.00 18.13 ?  394 LEU A CA  1 
ATOM   2825 C  C   . LEU A 1 394 ? -25.052 5.948   10.751  1.00 20.31 ?  394 LEU A C   1 
ATOM   2826 O  O   . LEU A 1 394 ? -23.849 5.923   10.477  1.00 18.84 ?  394 LEU A O   1 
ATOM   2827 C  CB  . LEU A 1 394 ? -25.715 8.115   11.765  1.00 19.53 ?  394 LEU A CB  1 
ATOM   2828 C  CG  . LEU A 1 394 ? -26.423 8.920   12.851  1.00 20.39 ?  394 LEU A CG  1 
ATOM   2829 C  CD1 . LEU A 1 394 ? -26.290 10.402  12.554  1.00 18.03 ?  394 LEU A CD1 1 
ATOM   2830 C  CD2 . LEU A 1 394 ? -27.885 8.489   12.911  1.00 23.69 ?  394 LEU A CD2 1 
ATOM   2831 N  N   . ALA A 1 395 ? -25.984 5.422   9.968   1.00 17.99 ?  395 ALA A N   1 
ATOM   2832 C  CA  . ALA A 1 395 ? -25.674 4.832   8.674   1.00 18.51 ?  395 ALA A CA  1 
ATOM   2833 C  C   . ALA A 1 395 ? -25.775 5.924   7.618   1.00 19.00 ?  395 ALA A C   1 
ATOM   2834 O  O   . ALA A 1 395 ? -26.868 6.427   7.348   1.00 22.85 ?  395 ALA A O   1 
ATOM   2835 C  CB  . ALA A 1 395 ? -26.643 3.692   8.367   1.00 17.30 ?  395 ALA A CB  1 
ATOM   2836 N  N   . TRP A 1 396 ? -24.653 6.284   7.007   1.00 19.39 ?  396 TRP A N   1 
ATOM   2837 C  CA  . TRP A 1 396 ? -24.666 7.285   5.949   1.00 18.82 ?  396 TRP A CA  1 
ATOM   2838 C  C   . TRP A 1 396 ? -24.850 6.594   4.600   1.00 21.49 ?  396 TRP A C   1 
ATOM   2839 O  O   . TRP A 1 396 ? -24.165 5.612   4.302   1.00 22.71 ?  396 TRP A O   1 
ATOM   2840 C  CB  . TRP A 1 396 ? -23.383 8.117   5.998   1.00 18.58 ?  396 TRP A CB  1 
ATOM   2841 C  CG  . TRP A 1 396 ? -23.383 8.998   7.225   1.00 16.71 ?  396 TRP A CG  1 
ATOM   2842 C  CD1 . TRP A 1 396 ? -22.849 8.712   8.450   1.00 21.02 ?  396 TRP A CD1 1 
ATOM   2843 C  CD2 . TRP A 1 396 ? -24.022 10.271  7.359   1.00 22.39 ?  396 TRP A CD2 1 
ATOM   2844 N  NE1 . TRP A 1 396 ? -23.094 9.748   9.333   1.00 20.12 ?  396 TRP A NE1 1 
ATOM   2845 C  CE2 . TRP A 1 396 ? -23.814 10.713  8.686   1.00 21.63 ?  396 TRP A CE2 1 
ATOM   2846 C  CE3 . TRP A 1 396 ? -24.738 11.088  6.482   1.00 20.64 ?  396 TRP A CE3 1 
ATOM   2847 C  CZ2 . TRP A 1 396 ? -24.285 11.937  9.146   1.00 23.57 ?  396 TRP A CZ2 1 
ATOM   2848 C  CZ3 . TRP A 1 396 ? -25.210 12.298  6.944   1.00 20.64 ?  396 TRP A CZ3 1 
ATOM   2849 C  CH2 . TRP A 1 396 ? -24.985 12.710  8.265   1.00 19.88 ?  396 TRP A CH2 1 
ATOM   2850 N  N   . ARG A 1 397 ? -25.789 7.094   3.806   1.00 17.25 ?  397 ARG A N   1 
ATOM   2851 C  CA  . ARG A 1 397 ? -26.105 6.471   2.525   1.00 19.31 ?  397 ARG A CA  1 
ATOM   2852 C  C   . ARG A 1 397 ? -24.922 6.556   1.557   1.00 19.38 ?  397 ARG A C   1 
ATOM   2853 O  O   . ARG A 1 397 ? -24.356 7.645   1.374   1.00 17.49 ?  397 ARG A O   1 
ATOM   2854 C  CB  . ARG A 1 397 ? -27.320 7.130   1.888   1.00 15.35 ?  397 ARG A CB  1 
ATOM   2855 C  CG  . ARG A 1 397 ? -27.641 6.530   0.526   1.00 15.77 ?  397 ARG A CG  1 
ATOM   2856 C  CD  . ARG A 1 397 ? -28.874 7.162   -0.127  1.00 15.89 ?  397 ARG A CD  1 
ATOM   2857 N  NE  . ARG A 1 397 ? -30.120 6.845   0.571   1.00 19.38 ?  397 ARG A NE  1 
ATOM   2858 C  CZ  . ARG A 1 397 ? -31.331 7.120   0.097   1.00 21.35 ?  397 ARG A CZ  1 
ATOM   2859 N  NH1 . ARG A 1 397 ? -31.502 7.636   -1.113  1.00 21.44 ?  397 ARG A NH1 1 
ATOM   2860 N  NH2 . ARG A 1 397 ? -32.397 6.878   0.856   1.00 16.84 ?  397 ARG A NH2 1 
ATOM   2861 N  N   . PRO A 1 398 ? -24.537 5.449   0.909   1.00 19.04 ?  398 PRO A N   1 
ATOM   2862 C  CA  . PRO A 1 398 ? -23.482 5.489   -0.110  1.00 17.56 ?  398 PRO A CA  1 
ATOM   2863 C  C   . PRO A 1 398 ? -24.049 5.723   -1.502  1.00 17.60 ?  398 PRO A C   1 
ATOM   2864 O  O   . PRO A 1 398 ? -25.239 5.513   -1.762  1.00 20.54 ?  398 PRO A O   1 
ATOM   2865 C  CB  . PRO A 1 398 ? -22.871 4.083   -0.031  1.00 17.83 ?  398 PRO A CB  1 
ATOM   2866 C  CG  . PRO A 1 398 ? -24.125 3.203   0.213   1.00 20.09 ?  398 PRO A CG  1 
ATOM   2867 C  CD  . PRO A 1 398 ? -25.012 4.066   1.160   1.00 17.77 ?  398 PRO A CD  1 
ATOM   2868 N  N   . GLY A 1 399 ? -23.166 6.164   -2.398  1.00 20.04 ?  399 GLY A N   1 
ATOM   2869 C  CA  . GLY A 1 399 ? -23.484 6.193   -3.826  1.00 15.49 ?  399 GLY A CA  1 
ATOM   2870 C  C   . GLY A 1 399 ? -24.692 7.036   -4.169  1.00 15.38 ?  399 GLY A C   1 
ATOM   2871 O  O   . GLY A 1 399 ? -25.510 6.640   -5.010  1.00 17.40 ?  399 GLY A O   1 
ATOM   2872 N  N   . PHE A 1 400 ? -24.812 8.203   -3.540  1.00 14.70 ?  400 PHE A N   1 
ATOM   2873 C  CA  . PHE A 1 400 ? -25.943 9.100   -3.717  1.00 17.33 ?  400 PHE A CA  1 
ATOM   2874 C  C   . PHE A 1 400 ? -25.415 10.523  -3.868  1.00 17.63 ?  400 PHE A C   1 
ATOM   2875 O  O   . PHE A 1 400 ? -24.362 10.861  -3.326  1.00 16.96 ?  400 PHE A O   1 
ATOM   2876 C  CB  . PHE A 1 400 ? -26.896 8.995   -2.516  1.00 15.82 ?  400 PHE A CB  1 
ATOM   2877 C  CG  . PHE A 1 400 ? -28.322 9.367   -2.821  1.00 17.21 ?  400 PHE A CG  1 
ATOM   2878 C  CD1 . PHE A 1 400 ? -29.020 8.728   -3.835  1.00 18.24 ?  400 PHE A CD1 1 
ATOM   2879 C  CD2 . PHE A 1 400 ? -28.967 10.355  -2.075  1.00 16.32 ?  400 PHE A CD2 1 
ATOM   2880 C  CE1 . PHE A 1 400 ? -30.345 9.066   -4.105  1.00 18.35 ?  400 PHE A CE1 1 
ATOM   2881 C  CE2 . PHE A 1 400 ? -30.288 10.703  -2.340  1.00 15.94 ?  400 PHE A CE2 1 
ATOM   2882 C  CZ  . PHE A 1 400 ? -30.979 10.055  -3.355  1.00 17.21 ?  400 PHE A CZ  1 
ATOM   2883 N  N   . ILE A 1 401 ? -26.145 11.355  -4.613  1.00 15.73 ?  401 ILE A N   1 
ATOM   2884 C  CA  . ILE A 1 401 ? -25.717 12.744  -4.802  1.00 15.91 ?  401 ILE A CA  1 
ATOM   2885 C  C   . ILE A 1 401 ? -25.695 13.491  -3.471  1.00 17.73 ?  401 ILE A C   1 
ATOM   2886 O  O   . ILE A 1 401 ? -24.796 14.303  -3.210  1.00 17.64 ?  401 ILE A O   1 
ATOM   2887 C  CB  . ILE A 1 401 ? -26.612 13.442  -5.847  1.00 19.19 ?  401 ILE A CB  1 
ATOM   2888 C  CG1 . ILE A 1 401 ? -26.176 13.036  -7.254  1.00 17.01 ?  401 ILE A CG1 1 
ATOM   2889 C  CG2 . ILE A 1 401 ? -26.549 14.957  -5.699  1.00 14.88 ?  401 ILE A CG2 1 
ATOM   2890 C  CD1 . ILE A 1 401 ? -27.212 13.323  -8.345  1.00 18.28 ?  401 ILE A CD1 1 
ATOM   2891 N  N   . LYS A 1 402 ? -26.667 13.220  -2.602  1.00 17.23 ?  402 LYS A N   1 
ATOM   2892 C  CA  . LYS A 1 402 ? -26.691 13.798  -1.264  1.00 16.81 ?  402 LYS A CA  1 
ATOM   2893 C  C   . LYS A 1 402 ? -26.024 12.885  -0.238  1.00 16.65 ?  402 LYS A C   1 
ATOM   2894 O  O   . LYS A 1 402 ? -26.117 11.659  -0.322  1.00 18.20 ?  402 LYS A O   1 
ATOM   2895 C  CB  . LYS A 1 402 ? -28.135 14.087  -0.824  1.00 16.42 ?  402 LYS A CB  1 
ATOM   2896 C  CG  . LYS A 1 402 ? -28.923 14.966  -1.827  1.00 12.67 ?  402 LYS A CG  1 
ATOM   2897 C  CD  . LYS A 1 402 ? -28.430 16.417  -1.788  1.00 16.60 ?  402 LYS A CD  1 
ATOM   2898 C  CE  . LYS A 1 402 ? -29.218 17.311  -2.733  1.00 15.29 ?  402 LYS A CE  1 
ATOM   2899 N  NZ  . LYS A 1 402 ? -28.605 18.659  -2.800  1.00 21.23 ?  402 LYS A NZ  1 
ATOM   2900 N  N   . ARG A 1 403 ? -25.363 13.497  0.744   1.00 17.99 ?  403 ARG A N   1 
ATOM   2901 C  CA  . ARG A 1 403 ? -25.093 12.833  2.014   1.00 18.90 ?  403 ARG A CA  1 
ATOM   2902 C  C   . ARG A 1 403 ? -26.344 12.873  2.874   1.00 19.37 ?  403 ARG A C   1 
ATOM   2903 O  O   . ARG A 1 403 ? -26.942 13.940  3.042   1.00 18.13 ?  403 ARG A O   1 
ATOM   2904 C  CB  . ARG A 1 403 ? -23.962 13.528  2.772   1.00 21.36 ?  403 ARG A CB  1 
ATOM   2905 C  CG  . ARG A 1 403 ? -22.578 13.261  2.251   1.00 16.31 ?  403 ARG A CG  1 
ATOM   2906 C  CD  . ARG A 1 403 ? -21.578 13.759  3.251   1.00 19.51 ?  403 ARG A CD  1 
ATOM   2907 N  NE  . ARG A 1 403 ? -20.256 13.915  2.655   1.00 24.35 ?  403 ARG A NE  1 
ATOM   2908 C  CZ  . ARG A 1 403 ? -19.787 15.044  2.149   1.00 21.31 ?  403 ARG A CZ  1 
ATOM   2909 N  NH1 . ARG A 1 403 ? -20.522 16.153  2.127   1.00 20.72 ?  403 ARG A NH1 1 
ATOM   2910 N  NH2 . ARG A 1 403 ? -18.549 15.068  1.663   1.00 25.17 ?  403 ARG A NH2 1 
ATOM   2911 N  N   . LEU A 1 404 ? -26.728 11.726  3.438   1.00 15.55 ?  404 LEU A N   1 
ATOM   2912 C  CA  . LEU A 1 404 ? -27.899 11.681  4.304   1.00 19.12 ?  404 LEU A CA  1 
ATOM   2913 C  C   . LEU A 1 404 ? -27.820 10.436  5.170   1.00 20.53 ?  404 LEU A C   1 
ATOM   2914 O  O   . LEU A 1 404 ? -27.274 9.415   4.734   1.00 19.54 ?  404 LEU A O   1 
ATOM   2915 C  CB  . LEU A 1 404 ? -29.206 11.680  3.493   1.00 21.60 ?  404 LEU A CB  1 
ATOM   2916 C  CG  . LEU A 1 404 ? -29.454 10.510  2.548   1.00 24.08 ?  404 LEU A CG  1 
ATOM   2917 C  CD1 . LEU A 1 404 ? -29.958 9.336   3.345   1.00 23.92 ?  404 LEU A CD1 1 
ATOM   2918 C  CD2 . LEU A 1 404 ? -30.477 10.905  1.494   1.00 24.02 ?  404 LEU A CD2 1 
ATOM   2919 N  N   . PRO A 1 405 ? -28.354 10.484  6.387   1.00 18.80 ?  405 PRO A N   1 
ATOM   2920 C  CA  . PRO A 1 405 ? -28.490 9.259   7.176   1.00 20.06 ?  405 PRO A CA  1 
ATOM   2921 C  C   . PRO A 1 405 ? -29.662 8.441   6.655   1.00 21.87 ?  405 PRO A C   1 
ATOM   2922 O  O   . PRO A 1 405 ? -30.725 8.984   6.340   1.00 22.29 ?  405 PRO A O   1 
ATOM   2923 C  CB  . PRO A 1 405 ? -28.737 9.775   8.602   1.00 19.06 ?  405 PRO A CB  1 
ATOM   2924 C  CG  . PRO A 1 405 ? -29.303 11.166  8.420   1.00 22.64 ?  405 PRO A CG  1 
ATOM   2925 C  CD  . PRO A 1 405 ? -28.841 11.687  7.092   1.00 22.10 ?  405 PRO A CD  1 
ATOM   2926 N  N   . GLU A 1 406 ? -29.440 7.128   6.516   1.00 19.08 ?  406 GLU A N   1 
ATOM   2927 C  CA  . GLU A 1 406 ? -30.502 6.238   6.040   1.00 18.57 ?  406 GLU A CA  1 
ATOM   2928 C  C   . GLU A 1 406 ? -31.700 6.270   6.984   1.00 20.08 ?  406 GLU A C   1 
ATOM   2929 O  O   . GLU A 1 406 ? -32.860 6.304   6.547   1.00 16.39 ?  406 GLU A O   1 
ATOM   2930 C  CB  . GLU A 1 406 ? -29.963 4.813   5.916   1.00 17.69 ?  406 GLU A CB  1 
ATOM   2931 C  CG  . GLU A 1 406 ? -28.719 4.720   5.036   1.00 19.11 ?  406 GLU A CG  1 
ATOM   2932 C  CD  . GLU A 1 406 ? -29.068 4.516   3.573   1.00 20.59 ?  406 GLU A CD  1 
ATOM   2933 O  OE1 . GLU A 1 406 ? -30.156 4.993   3.172   1.00 19.17 ?  406 GLU A OE1 1 
ATOM   2934 O  OE2 . GLU A 1 406 ? -28.269 3.878   2.840   1.00 16.23 ?  406 GLU A OE2 1 
ATOM   2935 N  N   . ARG A 1 407 ? -31.420 6.252   8.288   1.00 19.49 ?  407 ARG A N   1 
ATOM   2936 C  CA  . ARG A 1 407 ? -32.383 6.436   9.357   1.00 17.77 ?  407 ARG A CA  1 
ATOM   2937 C  C   . ARG A 1 407 ? -31.850 7.535   10.259  1.00 19.04 ?  407 ARG A C   1 
ATOM   2938 O  O   . ARG A 1 407 ? -30.631 7.711   10.372  1.00 17.38 ?  407 ARG A O   1 
ATOM   2939 C  CB  . ARG A 1 407 ? -32.578 5.145   10.170  1.00 15.37 ?  407 ARG A CB  1 
ATOM   2940 C  CG  . ARG A 1 407 ? -33.361 4.082   9.446   1.00 17.23 ?  407 ARG A CG  1 
ATOM   2941 C  CD  . ARG A 1 407 ? -32.881 2.684   9.831   1.00 19.97 ?  407 ARG A CD  1 
ATOM   2942 N  NE  . ARG A 1 407 ? -31.452 2.482   9.588   1.00 18.81 ?  407 ARG A NE  1 
ATOM   2943 C  CZ  . ARG A 1 407 ? -30.942 2.043   8.441   1.00 21.71 ?  407 ARG A CZ  1 
ATOM   2944 N  NH1 . ARG A 1 407 ? -31.693 1.895   7.359   1.00 21.17 ?  407 ARG A NH1 1 
ATOM   2945 N  NH2 . ARG A 1 407 ? -29.644 1.749   8.376   1.00 19.57 ?  407 ARG A NH2 1 
ATOM   2946 N  N   . LEU A 1 408 ? -32.758 8.277   10.901  1.00 17.07 ?  408 LEU A N   1 
ATOM   2947 C  CA  . LEU A 1 408 ? -32.378 9.368   11.800  1.00 17.52 ?  408 LEU A CA  1 
ATOM   2948 C  C   . LEU A 1 408 ? -33.076 9.088   13.124  1.00 18.05 ?  408 LEU A C   1 
ATOM   2949 O  O   . LEU A 1 408 ? -34.105 9.706   13.442  1.00 15.86 ?  408 LEU A O   1 
ATOM   2950 C  CB  . LEU A 1 408 ? -32.744 10.734  11.204  1.00 16.26 ?  408 LEU A CB  1 
ATOM   2951 C  CG  . LEU A 1 408 ? -32.491 12.007  12.023  1.00 19.57 ?  408 LEU A CG  1 
ATOM   2952 C  CD1 . LEU A 1 408 ? -30.996 12.184  12.290  1.00 19.27 ?  408 LEU A CD1 1 
ATOM   2953 C  CD2 . LEU A 1 408 ? -33.054 13.269  11.347  1.00 15.43 ?  408 LEU A CD2 1 
ATOM   2954 N  N   . PRO A 1 409 ? -32.584 8.117   13.899  1.00 19.56 ?  409 PRO A N   1 
ATOM   2955 C  CA  . PRO A 1 409 ? -33.301 7.716   15.120  1.00 20.25 ?  409 PRO A CA  1 
ATOM   2956 C  C   . PRO A 1 409 ? -33.009 8.675   16.270  1.00 19.88 ?  409 PRO A C   1 
ATOM   2957 O  O   . PRO A 1 409 ? -31.851 8.940   16.613  1.00 16.74 ?  409 PRO A O   1 
ATOM   2958 C  CB  . PRO A 1 409 ? -32.777 6.301   15.410  1.00 16.95 ?  409 PRO A CB  1 
ATOM   2959 C  CG  . PRO A 1 409 ? -31.504 6.175   14.669  1.00 21.97 ?  409 PRO A CG  1 
ATOM   2960 C  CD  . PRO A 1 409 ? -31.434 7.244   13.605  1.00 20.38 ?  409 PRO A CD  1 
ATOM   2961 N  N   . VAL A 1 410 ? -34.078 9.205   16.857  1.00 18.78 ?  410 VAL A N   1 
ATOM   2962 C  CA  . VAL A 1 410 ? -33.975 10.198  17.914  1.00 17.38 ?  410 VAL A CA  1 
ATOM   2963 C  C   . VAL A 1 410 ? -34.863 9.800   19.080  1.00 19.02 ?  410 VAL A C   1 
ATOM   2964 O  O   . VAL A 1 410 ? -35.795 8.999   18.947  1.00 17.31 ?  410 VAL A O   1 
ATOM   2965 C  CB  . VAL A 1 410 ? -34.368 11.601  17.425  1.00 18.03 ?  410 VAL A CB  1 
ATOM   2966 C  CG1 . VAL A 1 410 ? -33.596 11.940  16.160  1.00 17.37 ?  410 VAL A CG1 1 
ATOM   2967 C  CG2 . VAL A 1 410 ? -35.885 11.655  17.205  1.00 18.93 ?  410 VAL A CG2 1 
ATOM   2968 N  N   . LEU A 1 411 ? -34.554 10.391  20.232  1.00 19.98 ?  411 LEU A N   1 
ATOM   2969 C  CA  . LEU A 1 411 ? -35.358 10.322  21.438  1.00 24.76 ?  411 LEU A CA  1 
ATOM   2970 C  C   . LEU A 1 411 ? -35.786 11.731  21.825  1.00 21.83 ?  411 LEU A C   1 
ATOM   2971 O  O   . LEU A 1 411 ? -35.166 12.719  21.420  1.00 20.74 ?  411 LEU A O   1 
ATOM   2972 C  CB  . LEU A 1 411 ? -34.572 9.708   22.599  1.00 19.67 ?  411 LEU A CB  1 
ATOM   2973 C  CG  . LEU A 1 411 ? -34.089 8.262   22.472  1.00 22.04 ?  411 LEU A CG  1 
ATOM   2974 C  CD1 . LEU A 1 411 ? -33.106 7.935   23.606  1.00 18.19 ?  411 LEU A CD1 1 
ATOM   2975 C  CD2 . LEU A 1 411 ? -35.284 7.315   22.497  1.00 19.49 ?  411 LEU A CD2 1 
ATOM   2976 N  N   . TRP A 1 412 ? -36.818 11.809  22.659  1.00 21.14 ?  412 TRP A N   1 
ATOM   2977 C  CA  . TRP A 1 412 ? -37.250 13.077  23.235  1.00 21.61 ?  412 TRP A CA  1 
ATOM   2978 C  C   . TRP A 1 412 ? -38.021 12.840  24.540  1.00 24.29 ?  412 TRP A C   1 
ATOM   2979 O  O   . TRP A 1 412 ? -38.144 11.690  24.972  1.00 25.20 ?  412 TRP A O   1 
ATOM   2980 C  CB  . TRP A 1 412 ? -38.113 13.845  22.239  1.00 17.61 ?  412 TRP A CB  1 
ATOM   2981 C  CG  . TRP A 1 412 ? -39.391 13.151  21.901  1.00 20.19 ?  412 TRP A CG  1 
ATOM   2982 C  CD1 . TRP A 1 412 ? -40.602 13.284  22.549  1.00 21.04 ?  412 TRP A CD1 1 
ATOM   2983 C  CD2 . TRP A 1 412 ? -39.608 12.227  20.831  1.00 18.48 ?  412 TRP A CD2 1 
ATOM   2984 N  NE1 . TRP A 1 412 ? -41.550 12.500  21.936  1.00 23.04 ?  412 TRP A NE1 1 
ATOM   2985 C  CE2 . TRP A 1 412 ? -40.971 11.841  20.882  1.00 19.47 ?  412 TRP A CE2 1 
ATOM   2986 C  CE3 . TRP A 1 412 ? -38.791 11.687  19.834  1.00 16.81 ?  412 TRP A CE3 1 
ATOM   2987 C  CZ2 . TRP A 1 412 ? -41.528 10.934  19.971  1.00 18.83 ?  412 TRP A CZ2 1 
ATOM   2988 C  CZ3 . TRP A 1 412 ? -39.349 10.782  18.929  1.00 18.30 ?  412 TRP A CZ3 1 
ATOM   2989 C  CH2 . TRP A 1 412 ? -40.703 10.415  19.008  1.00 19.49 ?  412 TRP A CH2 1 
ATOM   2990 N  N   . PRO B 1 19  ? -1.445  -9.501  15.420  1.00 84.15 ?  19  PRO B N   1 
ATOM   2991 C  CA  . PRO B 1 19  ? -2.689  -8.761  15.155  1.00 77.33 ?  19  PRO B CA  1 
ATOM   2992 C  C   . PRO B 1 19  ? -3.917  -9.661  15.087  1.00 66.58 ?  19  PRO B C   1 
ATOM   2993 O  O   . PRO B 1 19  ? -3.956  -10.615 14.301  1.00 64.01 ?  19  PRO B O   1 
ATOM   2994 C  CB  . PRO B 1 19  ? -2.404  -8.091  13.806  1.00 75.25 ?  19  PRO B CB  1 
ATOM   2995 C  CG  . PRO B 1 19  ? -1.481  -9.054  13.112  1.00 79.99 ?  19  PRO B CG  1 
ATOM   2996 C  CD  . PRO B 1 19  ? -0.688  -9.775  14.183  1.00 81.54 ?  19  PRO B CD  1 
ATOM   2997 N  N   . LEU B 1 20  ? -4.942  -9.360  15.902  1.00 54.09 ?  20  LEU B N   1 
ATOM   2998 C  CA  . LEU B 1 20  ? -6.135  -10.206 15.942  1.00 50.53 ?  20  LEU B CA  1 
ATOM   2999 C  C   . LEU B 1 20  ? -7.099  -9.813  14.823  1.00 46.50 ?  20  LEU B C   1 
ATOM   3000 O  O   . LEU B 1 20  ? -7.366  -8.619  14.638  1.00 45.90 ?  20  LEU B O   1 
ATOM   3001 C  CB  . LEU B 1 20  ? -6.834  -10.083 17.291  1.00 43.67 ?  20  LEU B CB  1 
ATOM   3002 C  CG  . LEU B 1 20  ? -6.078  -10.588 18.526  1.00 42.12 ?  20  LEU B CG  1 
ATOM   3003 C  CD1 . LEU B 1 20  ? -6.824  -10.273 19.819  1.00 36.13 ?  20  LEU B CD1 1 
ATOM   3004 C  CD2 . LEU B 1 20  ? -5.780  -12.077 18.431  1.00 42.05 ?  20  LEU B CD2 1 
ATOM   3005 N  N   . PRO B 1 21  ? -7.616  -10.770 14.050  1.00 40.11 ?  21  PRO B N   1 
ATOM   3006 C  CA  . PRO B 1 21  ? -8.605  -10.427 13.016  1.00 40.78 ?  21  PRO B CA  1 
ATOM   3007 C  C   . PRO B 1 21  ? -9.865  -9.827  13.625  1.00 40.45 ?  21  PRO B C   1 
ATOM   3008 O  O   . PRO B 1 21  ? -10.284 -10.182 14.730  1.00 34.11 ?  21  PRO B O   1 
ATOM   3009 C  CB  . PRO B 1 21  ? -8.908  -11.764 12.330  1.00 37.82 ?  21  PRO B CB  1 
ATOM   3010 C  CG  . PRO B 1 21  ? -8.018  -12.787 12.941  1.00 39.57 ?  21  PRO B CG  1 
ATOM   3011 C  CD  . PRO B 1 21  ? -7.169  -12.172 13.996  1.00 41.80 ?  21  PRO B CD  1 
ATOM   3012 N  N   . ASP B 1 22  ? -10.473 -8.907  12.885  1.00 34.29 ?  22  ASP B N   1 
ATOM   3013 C  CA  . ASP B 1 22  ? -11.665 -8.227  13.360  1.00 36.00 ?  22  ASP B CA  1 
ATOM   3014 C  C   . ASP B 1 22  ? -12.920 -9.030  13.035  1.00 30.09 ?  22  ASP B C   1 
ATOM   3015 O  O   . ASP B 1 22  ? -12.992 -9.739  12.026  1.00 32.52 ?  22  ASP B O   1 
ATOM   3016 C  CB  . ASP B 1 22  ? -11.771 -6.832  12.750  1.00 36.15 ?  22  ASP B CB  1 
ATOM   3017 C  CG  . ASP B 1 22  ? -10.679 -5.904  13.238  1.00 39.65 ?  22  ASP B CG  1 
ATOM   3018 O  OD1 . ASP B 1 22  ? -10.516 -5.759  14.470  1.00 39.83 ?  22  ASP B OD1 1 
ATOM   3019 O  OD2 . ASP B 1 22  ? -9.995  -5.310  12.384  1.00 43.60 ?  22  ASP B OD2 1 
ATOM   3020 N  N   . PHE B 1 23  ? -13.897 -8.936  13.930  1.00 27.57 ?  23  PHE B N   1 
ATOM   3021 C  CA  . PHE B 1 23  ? -15.240 -9.438  13.712  1.00 28.26 ?  23  PHE B CA  1 
ATOM   3022 C  C   . PHE B 1 23  ? -16.219 -8.326  14.068  1.00 30.98 ?  23  PHE B C   1 
ATOM   3023 O  O   . PHE B 1 23  ? -15.970 -7.575  15.024  1.00 31.42 ?  23  PHE B O   1 
ATOM   3024 C  CB  . PHE B 1 23  ? -15.514 -10.685 14.569  1.00 25.67 ?  23  PHE B CB  1 
ATOM   3025 C  CG  . PHE B 1 23  ? -16.767 -11.417 14.180  1.00 25.60 ?  23  PHE B CG  1 
ATOM   3026 C  CD1 . PHE B 1 23  ? -16.789 -12.237 13.068  1.00 26.20 ?  23  PHE B CD1 1 
ATOM   3027 C  CD2 . PHE B 1 23  ? -17.930 -11.256 14.914  1.00 26.69 ?  23  PHE B CD2 1 
ATOM   3028 C  CE1 . PHE B 1 23  ? -17.950 -12.896 12.685  1.00 24.30 ?  23  PHE B CE1 1 
ATOM   3029 C  CE2 . PHE B 1 23  ? -19.097 -11.916 14.545  1.00 27.97 ?  23  PHE B CE2 1 
ATOM   3030 C  CZ  . PHE B 1 23  ? -19.101 -12.735 13.423  1.00 25.21 ?  23  PHE B CZ  1 
ATOM   3031 N  N   . PRO B 1 24  ? -17.342 -8.080  13.339  1.00 27.63 ?  24  PRO B N   1 
ATOM   3032 C  CA  . PRO B 1 24  ? -17.771 -8.887  12.202  1.00 29.66 ?  24  PRO B CA  1 
ATOM   3033 C  C   . PRO B 1 24  ? -16.997 -8.823  10.888  1.00 29.46 ?  24  PRO B C   1 
ATOM   3034 O  O   . PRO B 1 24  ? -16.113 -7.977  10.768  1.00 24.66 ?  24  PRO B O   1 
ATOM   3035 C  CB  . PRO B 1 24  ? -19.226 -8.445  12.014  1.00 31.57 ?  24  PRO B CB  1 
ATOM   3036 C  CG  . PRO B 1 24  ? -19.198 -6.988  12.359  1.00 34.06 ?  24  PRO B CG  1 
ATOM   3037 C  CD  . PRO B 1 24  ? -18.308 -6.994  13.575  1.00 28.49 ?  24  PRO B CD  1 
ATOM   3038 N  N   . LEU B 1 25  ? -17.403 -9.636  9.910   1.00 31.37 ?  25  LEU B N   1 
ATOM   3039 C  CA  . LEU B 1 25  ? -16.629 -9.818  8.654   1.00 33.12 ?  25  LEU B CA  1 
ATOM   3040 C  C   . LEU B 1 25  ? -16.837 -8.763  7.552   1.00 39.87 ?  25  LEU B C   1 
ATOM   3041 O  O   . LEU B 1 25  ? -15.805 -8.297  7.054   1.00 48.34 ?  25  LEU B O   1 
ATOM   3042 C  CB  . LEU B 1 25  ? -16.967 -11.214 8.137   1.00 32.16 ?  25  LEU B CB  1 
ATOM   3043 C  CG  . LEU B 1 25  ? -16.135 -12.350 8.733   1.00 34.02 ?  25  LEU B CG  1 
ATOM   3044 C  CD1 . LEU B 1 25  ? -16.433 -12.497 10.208  1.00 27.88 ?  25  LEU B CD1 1 
ATOM   3045 C  CD2 . LEU B 1 25  ? -16.414 -13.645 7.994   1.00 28.04 ?  25  LEU B CD2 1 
ATOM   3046 N  N   . SER B 1 26  ? -18.051 -8.510  7.098   1.00 30.19 ?  26  SER B N   1 
ATOM   3047 C  CA  . SER B 1 26  ? -18.280 -7.586  5.953   1.00 29.96 ?  26  SER B CA  1 
ATOM   3048 C  C   . SER B 1 26  ? -19.783 -7.489  5.732   1.00 23.25 ?  26  SER B C   1 
ATOM   3049 O  O   . SER B 1 26  ? -20.417 -8.534  5.651   1.00 26.84 ?  26  SER B O   1 
ATOM   3050 C  CB  . SER B 1 26  ? -17.608 -7.974  4.669   1.00 30.00 ?  26  SER B CB  1 
ATOM   3051 O  OG  . SER B 1 26  ? -18.110 -9.203  4.165   1.00 30.00 ?  26  SER B OG  1 
ATOM   3052 N  N   . ARG B 1 27  ? -20.315 -6.270  5.636   1.00 24.82 ?  27  ARG B N   1 
ATOM   3053 C  CA  . ARG B 1 27  ? -21.783 -6.094  5.486   1.00 24.92 ?  27  ARG B CA  1 
ATOM   3054 C  C   . ARG B 1 27  ? -22.195 -6.474  4.054   1.00 25.30 ?  27  ARG B C   1 
ATOM   3055 O  O   . ARG B 1 27  ? -23.409 -6.644  3.813   1.00 19.13 ?  27  ARG B O   1 
ATOM   3056 C  CB  . ARG B 1 27  ? -22.172 -4.659  5.860   1.00 23.67 ?  27  ARG B CB  1 
ATOM   3057 N  N   . ARG B 1 28  ? -21.218 -6.624  3.151   1.00 20.88 ?  28  ARG B N   1 
ATOM   3058 C  CA  . ARG B 1 28  ? -21.542 -7.038  1.764   1.00 22.17 ?  28  ARG B CA  1 
ATOM   3059 C  C   . ARG B 1 28  ? -22.135 -8.445  1.838   1.00 21.60 ?  28  ARG B C   1 
ATOM   3060 O  O   . ARG B 1 28  ? -21.458 -9.353  2.321   1.00 23.69 ?  28  ARG B O   1 
ATOM   3061 C  CB  . ARG B 1 28  ? -20.347 -6.903  0.818   1.00 24.85 ?  28  ARG B CB  1 
ATOM   3062 C  CG  . ARG B 1 28  ? -20.592 -7.578  -0.523  1.00 33.53 ?  28  ARG B CG  1 
ATOM   3063 C  CD  . ARG B 1 28  ? -19.553 -7.262  -1.580  1.00 31.22 ?  28  ARG B CD  1 
ATOM   3064 N  NE  . ARG B 1 28  ? -20.143 -7.376  -2.918  1.00 44.13 ?  28  ARG B NE  1 
ATOM   3065 C  CZ  . ARG B 1 28  ? -19.454 -7.503  -4.040  1.00 33.47 ?  28  ARG B CZ  1 
ATOM   3066 N  NH1 . ARG B 1 28  ? -18.157 -7.273  -4.044  1.00 39.79 ?  28  ARG B NH1 1 
ATOM   3067 N  NH2 . ARG B 1 28  ? -20.064 -7.862  -5.151  1.00 33.82 ?  28  ARG B NH2 1 
ATOM   3068 N  N   . GLY B 1 29  ? -23.358 -8.590  1.361   1.00 23.66 ?  29  GLY B N   1 
ATOM   3069 C  CA  . GLY B 1 29  ? -24.060 -9.844  1.503   1.00 21.29 ?  29  GLY B CA  1 
ATOM   3070 C  C   . GLY B 1 29  ? -24.310 -10.633 0.235   1.00 21.93 ?  29  GLY B C   1 
ATOM   3071 O  O   . GLY B 1 29  ? -25.009 -11.644 0.288   1.00 25.01 ?  29  GLY B O   1 
ATOM   3072 N  N   . ASP B 1 30  ? -23.768 -10.208 -0.903  1.00 24.35 ?  30  ASP B N   1 
ATOM   3073 C  CA  . ASP B 1 30  ? -24.054 -10.896 -2.156  1.00 27.77 ?  30  ASP B CA  1 
ATOM   3074 C  C   . ASP B 1 30  ? -22.966 -11.876 -2.578  1.00 27.62 ?  30  ASP B C   1 
ATOM   3075 O  O   . ASP B 1 30  ? -23.168 -12.595 -3.560  1.00 27.63 ?  30  ASP B O   1 
ATOM   3076 C  CB  . ASP B 1 30  ? -24.287 -9.883  -3.283  1.00 27.43 ?  30  ASP B CB  1 
ATOM   3077 C  CG  . ASP B 1 30  ? -23.051 -9.113  -3.631  1.00 29.91 ?  30  ASP B CG  1 
ATOM   3078 O  OD1 . ASP B 1 30  ? -22.672 -8.220  -2.850  1.00 34.05 ?  30  ASP B OD1 1 
ATOM   3079 O  OD2 . ASP B 1 30  ? -22.457 -9.399  -4.696  1.00 34.00 ?  30  ASP B OD2 1 
ATOM   3080 N  N   . ILE B 1 31  ? -21.815 -11.900 -1.892  1.00 25.62 ?  31  ILE B N   1 
ATOM   3081 C  CA  . ILE B 1 31  ? -20.823 -12.960 -2.048  1.00 24.96 ?  31  ILE B CA  1 
ATOM   3082 C  C   . ILE B 1 31  ? -20.256 -13.298 -0.675  1.00 23.11 ?  31  ILE B C   1 
ATOM   3083 O  O   . ILE B 1 31  ? -20.286 -12.486 0.251   1.00 23.05 ?  31  ILE B O   1 
ATOM   3084 C  CB  . ILE B 1 31  ? -19.664 -12.585 -2.998  1.00 24.99 ?  31  ILE B CB  1 
ATOM   3085 C  CG1 . ILE B 1 31  ? -18.952 -11.324 -2.502  1.00 29.65 ?  31  ILE B CG1 1 
ATOM   3086 C  CG2 . ILE B 1 31  ? -20.166 -12.412 -4.411  1.00 37.88 ?  31  ILE B CG2 1 
ATOM   3087 C  CD1 . ILE B 1 31  ? -17.502 -11.199 -2.964  1.00 38.46 ?  31  ILE B CD1 1 
ATOM   3088 N  N   . LEU B 1 32  ? -19.721 -14.506 -0.556  1.00 23.49 ?  32  LEU B N   1 
ATOM   3089 C  CA  . LEU B 1 32  ? -19.093 -14.907 0.698   1.00 25.99 ?  32  LEU B CA  1 
ATOM   3090 C  C   . LEU B 1 32  ? -17.891 -14.002 0.964   1.00 23.21 ?  32  LEU B C   1 
ATOM   3091 O  O   . LEU B 1 32  ? -17.093 -13.764 0.053   1.00 24.35 ?  32  LEU B O   1 
ATOM   3092 C  CB  . LEU B 1 32  ? -18.655 -16.376 0.650   1.00 21.61 ?  32  LEU B CB  1 
ATOM   3093 C  CG  . LEU B 1 32  ? -17.984 -16.913 1.924   1.00 24.84 ?  32  LEU B CG  1 
ATOM   3094 C  CD1 . LEU B 1 32  ? -19.027 -17.111 3.024   1.00 24.09 ?  32  LEU B CD1 1 
ATOM   3095 C  CD2 . LEU B 1 32  ? -17.236 -18.219 1.648   1.00 29.13 ?  32  LEU B CD2 1 
ATOM   3096 N  N   . PRO B 1 33  ? -17.752 -13.443 2.162   1.00 26.52 ?  33  PRO B N   1 
ATOM   3097 C  CA  . PRO B 1 33  ? -16.537 -12.682 2.463   1.00 24.71 ?  33  PRO B CA  1 
ATOM   3098 C  C   . PRO B 1 33  ? -15.317 -13.576 2.287   1.00 24.49 ?  33  PRO B C   1 
ATOM   3099 O  O   . PRO B 1 33  ? -15.262 -14.682 2.824   1.00 26.73 ?  33  PRO B O   1 
ATOM   3100 C  CB  . PRO B 1 33  ? -16.731 -12.261 3.926   1.00 28.86 ?  33  PRO B CB  1 
ATOM   3101 C  CG  . PRO B 1 33  ? -18.213 -12.280 4.132   1.00 27.04 ?  33  PRO B CG  1 
ATOM   3102 C  CD  . PRO B 1 33  ? -18.715 -13.414 3.274   1.00 26.37 ?  33  PRO B CD  1 
ATOM   3103 N  N   . ALA B 1 34  ? -14.346 -13.095 1.504   1.00 32.14 ?  34  ALA B N   1 
ATOM   3104 C  CA  . ALA B 1 34  ? -13.078 -13.811 1.347   1.00 29.95 ?  34  ALA B CA  1 
ATOM   3105 C  C   . ALA B 1 34  ? -12.509 -14.228 2.695   1.00 29.96 ?  34  ALA B C   1 
ATOM   3106 O  O   . ALA B 1 34  ? -11.991 -15.340 2.848   1.00 28.88 ?  34  ALA B O   1 
ATOM   3107 C  CB  . ALA B 1 34  ? -12.070 -12.934 0.607   1.00 27.57 ?  34  ALA B CB  1 
ATOM   3108 N  N   . GLU B 1 35  ? -12.630 -13.354 3.695   1.00 33.10 ?  35  GLU B N   1 
ATOM   3109 C  CA  . GLU B 1 35  ? -12.074 -13.651 5.011   1.00 33.88 ?  35  GLU B CA  1 
ATOM   3110 C  C   . GLU B 1 35  ? -12.716 -14.881 5.640   1.00 32.34 ?  35  GLU B C   1 
ATOM   3111 O  O   . GLU B 1 35  ? -12.060 -15.602 6.400   1.00 31.63 ?  35  GLU B O   1 
ATOM   3112 C  CB  . GLU B 1 35  ? -12.221 -12.425 5.919   1.00 33.11 ?  35  GLU B CB  1 
ATOM   3113 C  CG  . GLU B 1 35  ? -11.806 -12.652 7.361   1.00 40.09 ?  35  GLU B CG  1 
ATOM   3114 C  CD  . GLU B 1 35  ? -10.297 -12.672 7.558   1.00 40.12 ?  35  GLU B CD  1 
ATOM   3115 O  OE1 . GLU B 1 35  ? -9.558  -12.795 6.548   1.00 39.61 ?  35  GLU B OE1 1 
ATOM   3116 O  OE2 . GLU B 1 35  ? -9.855  -12.584 8.731   1.00 40.49 ?  35  GLU B OE2 1 
ATOM   3117 N  N   . ALA B 1 36  ? -13.993 -15.139 5.348   1.00 29.87 ?  36  ALA B N   1 
ATOM   3118 C  CA  . ALA B 1 36  ? -14.620 -16.351 5.866   1.00 31.46 ?  36  ALA B CA  1 
ATOM   3119 C  C   . ALA B 1 36  ? -13.938 -17.595 5.307   1.00 33.18 ?  36  ALA B C   1 
ATOM   3120 O  O   . ALA B 1 36  ? -13.673 -18.558 6.039   1.00 32.25 ?  36  ALA B O   1 
ATOM   3121 C  CB  . ALA B 1 36  ? -16.114 -16.365 5.533   1.00 25.92 ?  36  ALA B CB  1 
ATOM   3122 N  N   . GLU B 1 37  ? -13.645 -17.592 4.009   1.00 31.77 ?  37  GLU B N   1 
ATOM   3123 C  CA  . GLU B 1 37  ? -12.949 -18.726 3.418   1.00 31.21 ?  37  GLU B CA  1 
ATOM   3124 C  C   . GLU B 1 37  ? -11.548 -18.869 3.994   1.00 32.27 ?  37  GLU B C   1 
ATOM   3125 O  O   . GLU B 1 37  ? -11.122 -19.979 4.317   1.00 34.94 ?  37  GLU B O   1 
ATOM   3126 C  CB  . GLU B 1 37  ? -12.906 -18.576 1.894   1.00 34.82 ?  37  GLU B CB  1 
ATOM   3127 C  CG  . GLU B 1 37  ? -12.605 -19.875 1.156   1.00 39.76 ?  37  GLU B CG  1 
ATOM   3128 C  CD  . GLU B 1 37  ? -12.547 -19.704 -0.359  1.00 48.10 ?  37  GLU B CD  1 
ATOM   3129 O  OE1 . GLU B 1 37  ? -13.157 -18.743 -0.886  1.00 47.37 ?  37  GLU B OE1 1 
ATOM   3130 O  OE2 . GLU B 1 37  ? -11.878 -20.534 -1.019  1.00 52.70 ?  37  GLU B OE2 1 
ATOM   3131 N  N   . ARG B 1 38  ? -10.816 -17.759 4.141   1.00 34.71 ?  38  ARG B N   1 
ATOM   3132 C  CA  . ARG B 1 38  ? -9.465  -17.851 4.685   1.00 37.26 ?  38  ARG B CA  1 
ATOM   3133 C  C   . ARG B 1 38  ? -9.487  -18.331 6.129   1.00 38.55 ?  38  ARG B C   1 
ATOM   3134 O  O   . ARG B 1 38  ? -8.627  -19.120 6.537   1.00 38.35 ?  38  ARG B O   1 
ATOM   3135 C  CB  . ARG B 1 38  ? -8.744  -16.505 4.593   1.00 39.44 ?  38  ARG B CB  1 
ATOM   3136 C  CG  . ARG B 1 38  ? -7.313  -16.570 5.113   1.00 40.58 ?  38  ARG B CG  1 
ATOM   3137 C  CD  . ARG B 1 38  ? -6.751  -15.210 5.532   1.00 42.82 ?  38  ARG B CD  1 
ATOM   3138 N  NE  . ARG B 1 38  ? -7.325  -14.691 6.766   1.00 43.21 ?  38  ARG B NE  1 
ATOM   3139 C  CZ  . ARG B 1 38  ? -7.036  -15.139 7.981   1.00 44.88 ?  38  ARG B CZ  1 
ATOM   3140 N  NH1 . ARG B 1 38  ? -6.199  -16.146 8.166   1.00 43.57 ?  38  ARG B NH1 1 
ATOM   3141 N  NH2 . ARG B 1 38  ? -7.606  -14.566 9.037   1.00 43.79 ?  38  ARG B NH2 1 
ATOM   3142 N  N   . LEU B 1 39  ? -10.466 -17.871 6.912   1.00 34.77 ?  39  LEU B N   1 
ATOM   3143 C  CA  . LEU B 1 39  ? -10.570 -18.306 8.303   1.00 36.88 ?  39  LEU B CA  1 
ATOM   3144 C  C   . LEU B 1 39  ? -10.804 -19.810 8.391   1.00 33.95 ?  39  LEU B C   1 
ATOM   3145 O  O   . LEU B 1 39  ? -10.161 -20.504 9.181   1.00 33.15 ?  39  LEU B O   1 
ATOM   3146 C  CB  . LEU B 1 39  ? -11.696 -17.550 9.007   1.00 30.68 ?  39  LEU B CB  1 
ATOM   3147 C  CG  . LEU B 1 39  ? -11.364 -16.120 9.442   1.00 30.55 ?  39  LEU B CG  1 
ATOM   3148 C  CD1 . LEU B 1 39  ? -12.640 -15.313 9.527   1.00 33.93 ?  39  LEU B CD1 1 
ATOM   3149 C  CD2 . LEU B 1 39  ? -10.639 -16.105 10.779  1.00 34.09 ?  39  LEU B CD2 1 
ATOM   3150 N  N   . ARG B 1 40  ? -11.721 -20.332 7.578   1.00 33.89 ?  40  ARG B N   1 
ATOM   3151 C  CA  . ARG B 1 40  ? -12.058 -21.748 7.679   1.00 34.01 ?  40  ARG B CA  1 
ATOM   3152 C  C   . ARG B 1 40  ? -10.894 -22.626 7.242   1.00 39.46 ?  40  ARG B C   1 
ATOM   3153 O  O   . ARG B 1 40  ? -10.664 -23.696 7.823   1.00 38.18 ?  40  ARG B O   1 
ATOM   3154 C  CB  . ARG B 1 40  ? -13.305 -22.060 6.850   1.00 29.14 ?  40  ARG B CB  1 
ATOM   3155 C  CG  . ARG B 1 40  ? -13.714 -23.518 6.928   1.00 34.26 ?  40  ARG B CG  1 
ATOM   3156 C  CD  . ARG B 1 40  ? -14.766 -23.844 5.894   1.00 31.22 ?  40  ARG B CD  1 
ATOM   3157 N  NE  . ARG B 1 40  ? -14.349 -23.417 4.561   1.00 35.60 ?  40  ARG B NE  1 
ATOM   3158 C  CZ  . ARG B 1 40  ? -15.005 -22.535 3.814   1.00 33.56 ?  40  ARG B CZ  1 
ATOM   3159 N  NH1 . ARG B 1 40  ? -16.150 -21.994 4.217   1.00 29.09 ?  40  ARG B NH1 1 
ATOM   3160 N  NH2 . ARG B 1 40  ? -14.499 -22.180 2.636   1.00 36.07 ?  40  ARG B NH2 1 
ATOM   3161 N  N   . ALA B 1 41  ? -10.140 -22.181 6.236   1.00 37.46 ?  41  ALA B N   1 
ATOM   3162 C  CA  . ALA B 1 41  ? -9.070  -22.998 5.680   1.00 36.32 ?  41  ALA B CA  1 
ATOM   3163 C  C   . ALA B 1 41  ? -7.821  -22.980 6.544   1.00 40.59 ?  41  ALA B C   1 
ATOM   3164 O  O   . ALA B 1 41  ? -7.128  -23.999 6.635   1.00 39.45 ?  41  ALA B O   1 
ATOM   3165 C  CB  . ALA B 1 41  ? -8.730  -22.520 4.270   1.00 43.81 ?  41  ALA B CB  1 
ATOM   3166 N  N   . GLU B 1 42  ? -7.526  -21.849 7.187   1.00 40.72 ?  42  GLU B N   1 
ATOM   3167 C  CA  . GLU B 1 42  ? -6.292  -21.638 7.937   1.00 42.40 ?  42  GLU B CA  1 
ATOM   3168 C  C   . GLU B 1 42  ? -6.451  -21.799 9.445   1.00 40.49 ?  42  GLU B C   1 
ATOM   3169 O  O   . GLU B 1 42  ? -5.585  -22.397 10.090  1.00 38.99 ?  42  GLU B O   1 
ATOM   3170 C  CB  . GLU B 1 42  ? -5.729  -20.244 7.634   1.00 42.10 ?  42  GLU B CB  1 
ATOM   3171 C  CG  . GLU B 1 42  ? -5.385  -20.049 6.172   1.00 43.67 ?  42  GLU B CG  1 
ATOM   3172 C  CD  . GLU B 1 42  ? -4.731  -18.716 5.886   1.00 47.55 ?  42  GLU B CD  1 
ATOM   3173 O  OE1 . GLU B 1 42  ? -4.674  -17.871 6.802   1.00 45.67 ?  42  GLU B OE1 1 
ATOM   3174 O  OE2 . GLU B 1 42  ? -4.268  -18.521 4.738   1.00 46.80 ?  42  GLU B OE2 1 
ATOM   3175 N  N   . GLN B 1 43  ? -7.524  -21.273 10.035  1.00 34.03 ?  43  GLN B N   1 
ATOM   3176 C  CA  . GLN B 1 43  ? -7.715  -21.325 11.486  1.00 36.31 ?  43  GLN B CA  1 
ATOM   3177 C  C   . GLN B 1 43  ? -9.202  -21.442 11.784  1.00 33.35 ?  43  GLN B C   1 
ATOM   3178 O  O   . GLN B 1 43  ? -9.842  -20.486 12.238  1.00 31.95 ?  43  GLN B O   1 
ATOM   3179 C  CB  . GLN B 1 43  ? -7.105  -20.096 12.163  1.00 36.40 ?  43  GLN B CB  1 
ATOM   3180 C  CG  . GLN B 1 43  ? -7.762  -18.774 11.777  1.00 43.47 ?  43  GLN B CG  1 
ATOM   3181 C  CD  . GLN B 1 43  ? -7.134  -17.561 12.467  1.00 48.12 ?  43  GLN B CD  1 
ATOM   3182 O  OE1 . GLN B 1 43  ? -5.994  -17.617 12.949  1.00 49.21 ?  43  GLN B OE1 1 
ATOM   3183 N  NE2 . GLN B 1 43  ? -7.872  -16.455 12.503  1.00 40.28 ?  43  GLN B NE2 1 
ATOM   3184 N  N   . PRO B 1 44  ? -9.785  -22.625 11.552  1.00 32.73 ?  44  PRO B N   1 
ATOM   3185 C  CA  . PRO B 1 44  ? -11.237 -22.793 11.749  1.00 30.97 ?  44  PRO B CA  1 
ATOM   3186 C  C   . PRO B 1 44  ? -11.708 -22.568 13.172  1.00 30.04 ?  44  PRO B C   1 
ATOM   3187 O  O   . PRO B 1 44  ? -12.921 -22.540 13.393  1.00 31.68 ?  44  PRO B O   1 
ATOM   3188 C  CB  . PRO B 1 44  ? -11.493 -24.242 11.294  1.00 29.68 ?  44  PRO B CB  1 
ATOM   3189 C  CG  . PRO B 1 44  ? -10.154 -24.918 11.380  1.00 31.40 ?  44  PRO B CG  1 
ATOM   3190 C  CD  . PRO B 1 44  ? -9.155  -23.854 11.031  1.00 32.04 ?  44  PRO B CD  1 
ATOM   3191 N  N   . VAL B 1 45  ? -10.806 -22.424 14.140  1.00 32.73 ?  45  VAL B N   1 
ATOM   3192 C  CA  . VAL B 1 45  ? -11.132 -21.907 15.469  1.00 30.65 ?  45  VAL B CA  1 
ATOM   3193 C  C   . VAL B 1 45  ? -10.141 -20.777 15.707  1.00 32.07 ?  45  VAL B C   1 
ATOM   3194 O  O   . VAL B 1 45  ? -8.969  -21.025 16.007  1.00 36.60 ?  45  VAL B O   1 
ATOM   3195 C  CB  . VAL B 1 45  ? -11.047 -22.968 16.573  1.00 34.23 ?  45  VAL B CB  1 
ATOM   3196 C  CG1 . VAL B 1 45  ? -11.620 -22.429 17.868  1.00 28.97 ?  45  VAL B CG1 1 
ATOM   3197 C  CG2 . VAL B 1 45  ? -11.792 -24.221 16.163  1.00 30.10 ?  45  VAL B CG2 1 
ATOM   3198 N  N   . ALA B 1 46  ? -10.596 -19.536 15.561  1.00 30.08 ?  46  ALA B N   1 
ATOM   3199 C  CA  . ALA B 1 46  ? -9.704  -18.386 15.486  1.00 33.01 ?  46  ALA B CA  1 
ATOM   3200 C  C   . ALA B 1 46  ? -10.041 -17.392 16.586  1.00 29.51 ?  46  ALA B C   1 
ATOM   3201 O  O   . ALA B 1 46  ? -11.217 -17.094 16.822  1.00 29.03 ?  46  ALA B O   1 
ATOM   3202 C  CB  . ALA B 1 46  ? -9.802  -17.712 14.115  1.00 32.56 ?  46  ALA B CB  1 
ATOM   3203 N  N   . ARG B 1 47  ? -9.015  -16.902 17.274  1.00 33.12 ?  47  ARG B N   1 
ATOM   3204 C  CA  . ARG B 1 47  ? -9.217  -15.796 18.198  1.00 34.82 ?  47  ARG B CA  1 
ATOM   3205 C  C   . ARG B 1 47  ? -9.411  -14.512 17.408  1.00 32.91 ?  47  ARG B C   1 
ATOM   3206 O  O   . ARG B 1 47  ? -8.577  -14.162 16.570  1.00 31.28 ?  47  ARG B O   1 
ATOM   3207 C  CB  . ARG B 1 47  ? -8.032  -15.664 19.158  1.00 35.78 ?  47  ARG B CB  1 
ATOM   3208 C  CG  . ARG B 1 47  ? -8.346  -14.830 20.390  1.00 39.68 ?  47  ARG B CG  1 
ATOM   3209 C  CD  . ARG B 1 47  ? -8.612  -15.702 21.600  1.00 43.43 ?  47  ARG B CD  1 
ATOM   3210 N  NE  . ARG B 1 47  ? -7.382  -16.102 22.281  1.00 50.51 ?  47  ARG B NE  1 
ATOM   3211 C  CZ  . ARG B 1 47  ? -7.335  -16.553 23.528  1.00 52.91 ?  47  ARG B CZ  1 
ATOM   3212 N  NH1 . ARG B 1 47  ? -8.437  -16.712 24.249  1.00 52.54 ?  47  ARG B NH1 1 
ATOM   3213 N  NH2 . ARG B 1 47  ? -6.155  -16.854 24.067  1.00 52.20 ?  47  ARG B NH2 1 
ATOM   3214 N  N   . VAL B 1 48  ? -10.530 -13.825 17.657  1.00 32.03 ?  48  VAL B N   1 
ATOM   3215 C  CA  . VAL B 1 48  ? -10.880 -12.598 16.949  1.00 30.20 ?  48  VAL B CA  1 
ATOM   3216 C  C   . VAL B 1 48  ? -11.226 -11.517 17.964  1.00 29.17 ?  48  VAL B C   1 
ATOM   3217 O  O   . VAL B 1 48  ? -11.629 -11.800 19.091  1.00 27.65 ?  48  VAL B O   1 
ATOM   3218 C  CB  . VAL B 1 48  ? -12.071 -12.787 15.983  1.00 25.34 ?  48  VAL B CB  1 
ATOM   3219 C  CG1 . VAL B 1 48  ? -11.761 -13.849 14.928  1.00 25.14 ?  48  VAL B CG1 1 
ATOM   3220 C  CG2 . VAL B 1 48  ? -13.339 -13.138 16.779  1.00 23.05 ?  48  VAL B CG2 1 
ATOM   3221 N  N   . ARG B 1 49  ? -11.106 -10.264 17.527  1.00 29.35 ?  49  ARG B N   1 
ATOM   3222 C  CA  . ARG B 1 49  ? -11.546 -9.107  18.303  1.00 26.83 ?  49  ARG B CA  1 
ATOM   3223 C  C   . ARG B 1 49  ? -12.922 -8.673  17.804  1.00 26.93 ?  49  ARG B C   1 
ATOM   3224 O  O   . ARG B 1 49  ? -13.076 -8.322  16.631  1.00 24.72 ?  49  ARG B O   1 
ATOM   3225 C  CB  . ARG B 1 49  ? -10.548 -7.957  18.178  1.00 28.35 ?  49  ARG B CB  1 
ATOM   3226 C  CG  . ARG B 1 49  ? -10.812 -6.781  19.122  1.00 33.71 ?  49  ARG B CG  1 
ATOM   3227 C  CD  . ARG B 1 49  ? -10.097 -5.518  18.624  1.00 41.34 ?  49  ARG B CD  1 
ATOM   3228 N  NE  . ARG B 1 49  ? -10.470 -4.326  19.384  1.00 50.87 ?  49  ARG B NE  1 
ATOM   3229 C  CZ  . ARG B 1 49  ? -11.450 -3.491  19.062  1.00 47.26 ?  49  ARG B CZ  1 
ATOM   3230 N  NH1 . ARG B 1 49  ? -12.155 -3.644  17.949  1.00 39.88 ?  49  ARG B NH1 1 
ATOM   3231 N  NH2 . ARG B 1 49  ? -11.732 -2.476  19.878  1.00 46.65 ?  49  ARG B NH2 1 
ATOM   3232 N  N   . THR B 1 50  ? -13.915 -8.715  18.688  1.00 25.82 ?  50  THR B N   1 
ATOM   3233 C  CA  . THR B 1 50  ? -15.249 -8.237  18.371  1.00 27.75 ?  50  THR B CA  1 
ATOM   3234 C  C   . THR B 1 50  ? -15.288 -6.707  18.409  1.00 28.60 ?  50  THR B C   1 
ATOM   3235 O  O   . THR B 1 50  ? -14.355 -6.042  18.871  1.00 28.97 ?  50  THR B O   1 
ATOM   3236 C  CB  . THR B 1 50  ? -16.279 -8.803  19.354  1.00 26.28 ?  50  THR B CB  1 
ATOM   3237 O  OG1 . THR B 1 50  ? -16.143 -8.142  20.622  1.00 27.40 ?  50  THR B OG1 1 
ATOM   3238 C  CG2 . THR B 1 50  ? -16.113 -10.321 19.529  1.00 23.84 ?  50  THR B CG2 1 
ATOM   3239 N  N   . MET B 1 51  ? -16.412 -6.152  17.942  1.00 27.17 ?  51  MET B N   1 
ATOM   3240 C  CA  . MET B 1 51  ? -16.587 -4.700  17.904  1.00 32.79 ?  51  MET B CA  1 
ATOM   3241 C  C   . MET B 1 51  ? -16.647 -4.077  19.297  1.00 26.79 ?  51  MET B C   1 
ATOM   3242 O  O   . MET B 1 51  ? -16.452 -2.865  19.430  1.00 27.40 ?  51  MET B O   1 
ATOM   3243 C  CB  . MET B 1 51  ? -17.836 -4.368  17.077  1.00 27.17 ?  51  MET B CB  1 
ATOM   3244 C  CG  . MET B 1 51  ? -19.154 -4.734  17.743  1.00 32.22 ?  51  MET B CG  1 
ATOM   3245 S  SD  . MET B 1 51  ? -20.560 -3.888  16.962  1.00 27.47 ?  51  MET B SD  1 
ATOM   3246 C  CE  . MET B 1 51  ? -20.725 -5.047  15.581  1.00 26.03 ?  51  MET B CE  1 
ATOM   3247 N  N   . THR B 1 52  ? -16.890 -4.868  20.338  1.00 29.01 ?  52  THR B N   1 
ATOM   3248 C  CA  . THR B 1 52  ? -16.832 -4.336  21.697  1.00 29.53 ?  52  THR B CA  1 
ATOM   3249 C  C   . THR B 1 52  ? -15.408 -4.197  22.211  1.00 32.02 ?  52  THR B C   1 
ATOM   3250 O  O   . THR B 1 52  ? -15.199 -3.539  23.236  1.00 29.54 ?  52  THR B O   1 
ATOM   3251 C  CB  . THR B 1 52  ? -17.573 -5.238  22.677  1.00 29.43 ?  52  THR B CB  1 
ATOM   3252 O  OG1 . THR B 1 52  ? -16.879 -6.492  22.738  1.00 32.74 ?  52  THR B OG1 1 
ATOM   3253 C  CG2 . THR B 1 52  ? -19.012 -5.463  22.246  1.00 27.38 ?  52  THR B CG2 1 
ATOM   3254 N  N   . GLY B 1 53  ? -14.435 -4.810  21.536  1.00 30.55 ?  53  GLY B N   1 
ATOM   3255 C  CA  . GLY B 1 53  ? -13.095 -4.946  22.061  1.00 29.47 ?  53  GLY B CA  1 
ATOM   3256 C  C   . GLY B 1 53  ? -12.841 -6.261  22.769  1.00 32.40 ?  53  GLY B C   1 
ATOM   3257 O  O   . GLY B 1 53  ? -11.678 -6.600  23.007  1.00 29.84 ?  53  GLY B O   1 
ATOM   3258 N  N   . ASP B 1 54  ? -13.892 -6.997  23.124  1.00 29.52 ?  54  ASP B N   1 
ATOM   3259 C  CA  . ASP B 1 54  ? -13.740 -8.304  23.742  1.00 32.27 ?  54  ASP B CA  1 
ATOM   3260 C  C   . ASP B 1 54  ? -13.157 -9.300  22.744  1.00 34.28 ?  54  ASP B C   1 
ATOM   3261 O  O   . ASP B 1 54  ? -13.201 -9.106  21.527  1.00 32.09 ?  54  ASP B O   1 
ATOM   3262 C  CB  . ASP B 1 54  ? -15.087 -8.823  24.259  1.00 29.41 ?  54  ASP B CB  1 
ATOM   3263 C  CG  . ASP B 1 54  ? -15.650 -7.981  25.411  1.00 35.21 ?  54  ASP B CG  1 
ATOM   3264 O  OD1 . ASP B 1 54  ? -14.871 -7.233  26.042  1.00 33.72 ?  54  ASP B OD1 1 
ATOM   3265 O  OD2 . ASP B 1 54  ? -16.872 -8.074  25.690  1.00 30.14 ?  54  ASP B OD2 1 
ATOM   3266 N  N   . GLU B 1 55  ? -12.620 -10.390 23.273  1.00 35.79 ?  55  GLU B N   1 
ATOM   3267 C  CA  . GLU B 1 55  ? -12.065 -11.445 22.445  1.00 36.12 ?  55  GLU B CA  1 
ATOM   3268 C  C   . GLU B 1 55  ? -13.009 -12.636 22.433  1.00 32.48 ?  55  GLU B C   1 
ATOM   3269 O  O   . GLU B 1 55  ? -13.762 -12.865 23.385  1.00 29.87 ?  55  GLU B O   1 
ATOM   3270 C  CB  . GLU B 1 55  ? -10.690 -11.870 22.946  1.00 38.12 ?  55  GLU B CB  1 
ATOM   3271 C  CG  . GLU B 1 55  ? -9.639  -10.816 22.761  1.00 39.12 ?  55  GLU B CG  1 
ATOM   3272 C  CD  . GLU B 1 55  ? -8.269  -11.298 23.190  1.00 50.18 ?  55  GLU B CD  1 
ATOM   3273 O  OE1 . GLU B 1 55  ? -8.139  -12.506 23.489  1.00 50.29 ?  55  GLU B OE1 1 
ATOM   3274 O  OE2 . GLU B 1 55  ? -7.327  -10.475 23.215  1.00 52.43 ?  55  GLU B OE2 1 
ATOM   3275 N  N   . ALA B 1 56  ? -12.966 -13.388 21.337  1.00 34.21 ?  56  ALA B N   1 
ATOM   3276 C  CA  . ALA B 1 56  ? -13.818 -14.555 21.174  1.00 30.55 ?  56  ALA B CA  1 
ATOM   3277 C  C   . ALA B 1 56  ? -13.120 -15.549 20.259  1.00 28.61 ?  56  ALA B C   1 
ATOM   3278 O  O   . ALA B 1 56  ? -12.187 -15.200 19.533  1.00 27.05 ?  56  ALA B O   1 
ATOM   3279 C  CB  . ALA B 1 56  ? -15.193 -14.179 20.601  1.00 24.65 ?  56  ALA B CB  1 
ATOM   3280 N  N   . TRP B 1 57  ? -13.591 -16.797 20.301  1.00 26.34 ?  57  TRP B N   1 
ATOM   3281 C  CA  . TRP B 1 57  ? -13.214 -17.818 19.331  1.00 27.74 ?  57  TRP B CA  1 
ATOM   3282 C  C   . TRP B 1 57  ? -14.267 -17.862 18.228  1.00 23.46 ?  57  TRP B C   1 
ATOM   3283 O  O   . TRP B 1 57  ? -15.438 -18.145 18.497  1.00 27.16 ?  57  TRP B O   1 
ATOM   3284 C  CB  . TRP B 1 57  ? -13.086 -19.198 19.986  1.00 30.07 ?  57  TRP B CB  1 
ATOM   3285 C  CG  . TRP B 1 57  ? -12.014 -19.286 21.036  1.00 33.89 ?  57  TRP B CG  1 
ATOM   3286 C  CD1 . TRP B 1 57  ? -12.195 -19.380 22.390  1.00 33.06 ?  57  TRP B CD1 1 
ATOM   3287 C  CD2 . TRP B 1 57  ? -10.598 -19.292 20.818  1.00 36.63 ?  57  TRP B CD2 1 
ATOM   3288 N  NE1 . TRP B 1 57  ? -10.975 -19.439 23.027  1.00 37.89 ?  57  TRP B NE1 1 
ATOM   3289 C  CE2 . TRP B 1 57  ? -9.979  -19.387 22.086  1.00 38.77 ?  57  TRP B CE2 1 
ATOM   3290 C  CE3 . TRP B 1 57  ? -9.792  -19.230 19.678  1.00 35.21 ?  57  TRP B CE3 1 
ATOM   3291 C  CZ2 . TRP B 1 57  ? -8.593  -19.417 22.241  1.00 38.57 ?  57  TRP B CZ2 1 
ATOM   3292 C  CZ3 . TRP B 1 57  ? -8.412  -19.261 19.835  1.00 38.27 ?  57  TRP B CZ3 1 
ATOM   3293 C  CH2 . TRP B 1 57  ? -7.829  -19.354 21.107  1.00 42.29 ?  57  TRP B CH2 1 
ATOM   3294 N  N   . LEU B 1 58  ? -13.842 -17.613 16.995  1.00 23.94 ?  58  LEU B N   1 
ATOM   3295 C  CA  . LEU B 1 58  ? -14.707 -17.692 15.824  1.00 23.03 ?  58  LEU B CA  1 
ATOM   3296 C  C   . LEU B 1 58  ? -14.560 -19.070 15.178  1.00 24.64 ?  58  LEU B C   1 
ATOM   3297 O  O   . LEU B 1 58  ? -13.452 -19.464 14.791  1.00 24.02 ?  58  LEU B O   1 
ATOM   3298 C  CB  . LEU B 1 58  ? -14.347 -16.587 14.831  1.00 20.22 ?  58  LEU B CB  1 
ATOM   3299 C  CG  . LEU B 1 58  ? -15.263 -16.465 13.614  1.00 26.42 ?  58  LEU B CG  1 
ATOM   3300 C  CD1 . LEU B 1 58  ? -16.683 -16.035 14.043  1.00 20.45 ?  58  LEU B CD1 1 
ATOM   3301 C  CD2 . LEU B 1 58  ? -14.662 -15.495 12.615  1.00 26.47 ?  58  LEU B CD2 1 
ATOM   3302 N  N   . VAL B 1 59  ? -15.669 -19.797 15.070  1.00 24.11 ?  59  VAL B N   1 
ATOM   3303 C  CA  . VAL B 1 59  ? -15.687 -21.182 14.595  1.00 25.29 ?  59  VAL B CA  1 
ATOM   3304 C  C   . VAL B 1 59  ? -16.266 -21.207 13.186  1.00 20.99 ?  59  VAL B C   1 
ATOM   3305 O  O   . VAL B 1 59  ? -17.449 -20.911 13.005  1.00 21.93 ?  59  VAL B O   1 
ATOM   3306 C  CB  . VAL B 1 59  ? -16.507 -22.078 15.534  1.00 21.74 ?  59  VAL B CB  1 
ATOM   3307 C  CG1 . VAL B 1 59  ? -16.545 -23.521 15.015  1.00 20.17 ?  59  VAL B CG1 1 
ATOM   3308 C  CG2 . VAL B 1 59  ? -15.933 -22.029 16.938  1.00 21.89 ?  59  VAL B CG2 1 
ATOM   3309 N  N   . SER B 1 60  ? -15.449 -21.602 12.189  1.00 25.68 ?  60  SER B N   1 
ATOM   3310 C  CA  . SER B 1 60  ? -15.787 -21.378 10.780  1.00 23.36 ?  60  SER B CA  1 
ATOM   3311 C  C   . SER B 1 60  ? -15.849 -22.621 9.890   1.00 28.30 ?  60  SER B C   1 
ATOM   3312 O  O   . SER B 1 60  ? -16.260 -22.502 8.729   1.00 25.86 ?  60  SER B O   1 
ATOM   3313 C  CB  . SER B 1 60  ? -14.807 -20.367 10.159  1.00 26.31 ?  60  SER B CB  1 
ATOM   3314 O  OG  . SER B 1 60  ? -13.453 -20.750 10.319  1.00 30.46 ?  60  SER B OG  1 
ATOM   3315 N  N   . SER B 1 61  ? -15.480 -23.798 10.376  1.00 25.50 ?  61  SER B N   1 
ATOM   3316 C  CA  . SER B 1 61  ? -15.671 -25.006 9.587   1.00 27.68 ?  61  SER B CA  1 
ATOM   3317 C  C   . SER B 1 61  ? -17.005 -25.641 9.933   1.00 26.40 ?  61  SER B C   1 
ATOM   3318 O  O   . SER B 1 61  ? -17.528 -25.463 11.038  1.00 22.40 ?  61  SER B O   1 
ATOM   3319 C  CB  . SER B 1 61  ? -14.552 -26.015 9.824   1.00 25.50 ?  61  SER B CB  1 
ATOM   3320 O  OG  . SER B 1 61  ? -14.726 -26.644 11.079  1.00 21.86 ?  61  SER B OG  1 
ATOM   3321 N  N   . TYR B 1 62  ? -17.547 -26.402 8.978   1.00 24.24 ?  62  TYR B N   1 
ATOM   3322 C  CA  . TYR B 1 62  ? -18.830 -27.063 9.201   1.00 23.14 ?  62  TYR B CA  1 
ATOM   3323 C  C   . TYR B 1 62  ? -18.763 -28.018 10.387  1.00 25.66 ?  62  TYR B C   1 
ATOM   3324 O  O   . TYR B 1 62  ? -19.656 -28.029 11.242  1.00 23.00 ?  62  TYR B O   1 
ATOM   3325 C  CB  . TYR B 1 62  ? -19.275 -27.813 7.943   1.00 19.89 ?  62  TYR B CB  1 
ATOM   3326 C  CG  . TYR B 1 62  ? -20.604 -28.533 8.115   1.00 26.09 ?  62  TYR B CG  1 
ATOM   3327 C  CD1 . TYR B 1 62  ? -20.671 -29.804 8.695   1.00 28.14 ?  62  TYR B CD1 1 
ATOM   3328 C  CD2 . TYR B 1 62  ? -21.790 -27.941 7.723   1.00 21.17 ?  62  TYR B CD2 1 
ATOM   3329 C  CE1 . TYR B 1 62  ? -21.878 -30.457 8.871   1.00 20.99 ?  62  TYR B CE1 1 
ATOM   3330 C  CE2 . TYR B 1 62  ? -23.007 -28.601 7.884   1.00 25.42 ?  62  TYR B CE2 1 
ATOM   3331 C  CZ  . TYR B 1 62  ? -23.038 -29.865 8.460   1.00 26.61 ?  62  TYR B CZ  1 
ATOM   3332 O  OH  . TYR B 1 62  ? -24.249 -30.526 8.618   1.00 23.38 ?  62  TYR B OH  1 
ATOM   3333 N  N   . GLU B 1 63  ? -17.720 -28.848 10.441  1.00 27.49 ?  63  GLU B N   1 
ATOM   3334 C  CA  . GLU B 1 63  ? -17.677 -29.888 11.463  1.00 30.63 ?  63  GLU B CA  1 
ATOM   3335 C  C   . GLU B 1 63  ? -17.573 -29.274 12.852  1.00 29.43 ?  63  GLU B C   1 
ATOM   3336 O  O   . GLU B 1 63  ? -18.281 -29.686 13.778  1.00 27.75 ?  63  GLU B O   1 
ATOM   3337 C  CB  . GLU B 1 63  ? -16.506 -30.835 11.208  1.00 29.58 ?  63  GLU B CB  1 
ATOM   3338 C  CG  . GLU B 1 63  ? -16.435 -31.997 12.195  1.00 41.70 ?  63  GLU B CG  1 
ATOM   3339 C  CD  . GLU B 1 63  ? -15.295 -32.967 11.910  1.00 46.20 ?  63  GLU B CD  1 
ATOM   3340 O  OE1 . GLU B 1 63  ? -14.515 -32.732 10.960  1.00 51.32 ?  63  GLU B OE1 1 
ATOM   3341 O  OE2 . GLU B 1 63  ? -15.185 -33.971 12.641  1.00 52.78 ?  63  GLU B OE2 1 
ATOM   3342 N  N   . LEU B 1 64  ? -16.719 -28.262 13.006  1.00 25.08 ?  64  LEU B N   1 
ATOM   3343 C  CA  . LEU B 1 64  ? -16.551 -27.637 14.312  1.00 28.54 ?  64  LEU B CA  1 
ATOM   3344 C  C   . LEU B 1 64  ? -17.753 -26.769 14.668  1.00 28.81 ?  64  LEU B C   1 
ATOM   3345 O  O   . LEU B 1 64  ? -18.150 -26.708 15.836  1.00 29.06 ?  64  LEU B O   1 
ATOM   3346 C  CB  . LEU B 1 64  ? -15.250 -26.835 14.330  1.00 27.25 ?  64  LEU B CB  1 
ATOM   3347 C  CG  . LEU B 1 64  ? -14.022 -27.753 14.183  1.00 33.01 ?  64  LEU B CG  1 
ATOM   3348 C  CD1 . LEU B 1 64  ? -12.713 -26.984 14.136  1.00 31.61 ?  64  LEU B CD1 1 
ATOM   3349 C  CD2 . LEU B 1 64  ? -13.977 -28.793 15.300  1.00 36.09 ?  64  LEU B CD2 1 
ATOM   3350 N  N   . ALA B 1 65  ? -18.344 -26.091 13.676  1.00 26.29 ?  65  ALA B N   1 
ATOM   3351 C  CA  . ALA B 1 65  ? -19.574 -25.338 13.901  1.00 28.96 ?  65  ALA B CA  1 
ATOM   3352 C  C   . ALA B 1 65  ? -20.675 -26.242 14.436  1.00 26.84 ?  65  ALA B C   1 
ATOM   3353 O  O   . ALA B 1 65  ? -21.265 -25.970 15.488  1.00 24.10 ?  65  ALA B O   1 
ATOM   3354 C  CB  . ALA B 1 65  ? -20.031 -24.661 12.603  1.00 23.04 ?  65  ALA B CB  1 
ATOM   3355 N  N   . LYS B 1 66  ? -20.977 -27.319 13.699  1.00 24.94 ?  66  LYS B N   1 
ATOM   3356 C  CA  . LYS B 1 66  ? -22.008 -28.263 14.123  1.00 25.65 ?  66  LYS B CA  1 
ATOM   3357 C  C   . LYS B 1 66  ? -21.715 -28.794 15.517  1.00 29.03 ?  66  LYS B C   1 
ATOM   3358 O  O   . LYS B 1 66  ? -22.612 -28.882 16.358  1.00 29.75 ?  66  LYS B O   1 
ATOM   3359 C  CB  . LYS B 1 66  ? -22.103 -29.421 13.121  1.00 29.81 ?  66  LYS B CB  1 
ATOM   3360 C  CG  . LYS B 1 66  ? -23.255 -30.406 13.364  1.00 33.57 ?  66  LYS B CG  1 
ATOM   3361 C  CD  . LYS B 1 66  ? -23.188 -31.589 12.390  1.00 38.01 ?  66  LYS B CD  1 
ATOM   3362 C  CE  . LYS B 1 66  ? -24.337 -32.579 12.596  1.00 42.36 ?  66  LYS B CE  1 
ATOM   3363 N  NZ  . LYS B 1 66  ? -25.649 -32.016 12.136  1.00 48.28 ?  66  LYS B NZ  1 
ATOM   3364 N  N   . GLN B 1 67  ? -20.448 -29.109 15.786  1.00 30.85 ?  67  GLN B N   1 
ATOM   3365 C  CA  . GLN B 1 67  ? -20.049 -29.616 17.093  1.00 31.41 ?  67  GLN B CA  1 
ATOM   3366 C  C   . GLN B 1 67  ? -20.430 -28.646 18.211  1.00 32.43 ?  67  GLN B C   1 
ATOM   3367 O  O   . GLN B 1 67  ? -21.010 -29.054 19.223  1.00 31.96 ?  67  GLN B O   1 
ATOM   3368 C  CB  . GLN B 1 67  ? -18.544 -29.876 17.087  1.00 35.16 ?  67  GLN B CB  1 
ATOM   3369 C  CG  . GLN B 1 67  ? -18.011 -30.537 18.328  1.00 44.24 ?  67  GLN B CG  1 
ATOM   3370 C  CD  . GLN B 1 67  ? -16.562 -30.909 18.172  1.00 41.87 ?  67  GLN B CD  1 
ATOM   3371 O  OE1 . GLN B 1 67  ? -15.986 -30.751 17.097  1.00 44.53 ?  67  GLN B OE1 1 
ATOM   3372 N  NE2 . GLN B 1 67  ? -15.950 -31.390 19.250  1.00 49.18 ?  67  GLN B NE2 1 
ATOM   3373 N  N   . VAL B 1 68  ? -20.106 -27.355 18.050  1.00 29.57 ?  68  VAL B N   1 
ATOM   3374 C  CA  . VAL B 1 68  ? -20.432 -26.363 19.081  1.00 28.79 ?  68  VAL B CA  1 
ATOM   3375 C  C   . VAL B 1 68  ? -21.933 -26.335 19.349  1.00 29.63 ?  68  VAL B C   1 
ATOM   3376 O  O   . VAL B 1 68  ? -22.382 -26.356 20.503  1.00 29.33 ?  68  VAL B O   1 
ATOM   3377 C  CB  . VAL B 1 68  ? -19.926 -24.970 18.670  1.00 29.73 ?  68  VAL B CB  1 
ATOM   3378 C  CG1 . VAL B 1 68  ? -20.594 -23.892 19.536  1.00 28.27 ?  68  VAL B CG1 1 
ATOM   3379 C  CG2 . VAL B 1 68  ? -18.430 -24.894 18.810  1.00 24.76 ?  68  VAL B CG2 1 
ATOM   3380 N  N   . LEU B 1 69  ? -22.729 -26.272 18.282  1.00 25.52 ?  69  LEU B N   1 
ATOM   3381 C  CA  . LEU B 1 69  ? -24.171 -26.118 18.410  1.00 26.02 ?  69  LEU B CA  1 
ATOM   3382 C  C   . LEU B 1 69  ? -24.832 -27.326 19.059  1.00 27.13 ?  69  LEU B C   1 
ATOM   3383 O  O   . LEU B 1 69  ? -25.915 -27.184 19.636  1.00 26.43 ?  69  LEU B O   1 
ATOM   3384 C  CB  . LEU B 1 69  ? -24.794 -25.879 17.031  1.00 27.73 ?  69  LEU B CB  1 
ATOM   3385 C  CG  . LEU B 1 69  ? -24.371 -24.610 16.282  1.00 26.46 ?  69  LEU B CG  1 
ATOM   3386 C  CD1 . LEU B 1 69  ? -25.037 -24.561 14.910  1.00 26.63 ?  69  LEU B CD1 1 
ATOM   3387 C  CD2 . LEU B 1 69  ? -24.677 -23.346 17.089  1.00 24.48 ?  69  LEU B CD2 1 
ATOM   3388 N  N   . GLU B 1 70  ? -24.216 -28.504 18.966  1.00 28.28 ?  70  GLU B N   1 
ATOM   3389 C  CA  . GLU B 1 70  ? -24.777 -29.731 19.515  1.00 29.37 ?  70  GLU B CA  1 
ATOM   3390 C  C   . GLU B 1 70  ? -24.168 -30.112 20.859  1.00 32.21 ?  70  GLU B C   1 
ATOM   3391 O  O   . GLU B 1 70  ? -24.500 -31.170 21.402  1.00 30.74 ?  70  GLU B O   1 
ATOM   3392 C  CB  . GLU B 1 70  ? -24.599 -30.878 18.518  1.00 29.36 ?  70  GLU B CB  1 
ATOM   3393 C  CG  . GLU B 1 70  ? -25.523 -30.767 17.331  1.00 32.55 ?  70  GLU B CG  1 
ATOM   3394 C  CD  . GLU B 1 70  ? -25.273 -31.817 16.268  1.00 31.83 ?  70  GLU B CD  1 
ATOM   3395 O  OE1 . GLU B 1 70  ? -24.319 -32.608 16.408  1.00 35.01 ?  70  GLU B OE1 1 
ATOM   3396 O  OE2 . GLU B 1 70  ? -26.041 -31.841 15.288  1.00 36.83 ?  70  GLU B OE2 1 
ATOM   3397 N  N   . ASP B 1 71  ? -23.300 -29.271 21.406  1.00 31.14 ?  71  ASP B N   1 
ATOM   3398 C  CA  . ASP B 1 71  ? -22.563 -29.535 22.638  1.00 33.97 ?  71  ASP B CA  1 
ATOM   3399 C  C   . ASP B 1 71  ? -23.046 -28.523 23.670  1.00 36.75 ?  71  ASP B C   1 
ATOM   3400 O  O   . ASP B 1 71  ? -22.617 -27.365 23.653  1.00 33.43 ?  71  ASP B O   1 
ATOM   3401 C  CB  . ASP B 1 71  ? -21.059 -29.422 22.402  1.00 31.04 ?  71  ASP B CB  1 
ATOM   3402 C  CG  . ASP B 1 71  ? -20.236 -29.750 23.643  1.00 36.09 ?  71  ASP B CG  1 
ATOM   3403 O  OD1 . ASP B 1 71  ? -20.825 -29.907 24.736  1.00 32.47 ?  71  ASP B OD1 1 
ATOM   3404 O  OD2 . ASP B 1 71  ? -18.994 -29.839 23.524  1.00 36.95 ?  71  ASP B OD2 1 
ATOM   3405 N  N   . ASP B 1 72  ? -23.915 -28.965 24.583  1.00 40.25 ?  72  ASP B N   1 
ATOM   3406 C  CA  . ASP B 1 72  ? -24.567 -28.037 25.503  1.00 42.26 ?  72  ASP B CA  1 
ATOM   3407 C  C   . ASP B 1 72  ? -23.637 -27.487 26.584  1.00 39.10 ?  72  ASP B C   1 
ATOM   3408 O  O   . ASP B 1 72  ? -24.105 -26.705 27.420  1.00 40.59 ?  72  ASP B O   1 
ATOM   3409 C  CB  . ASP B 1 72  ? -25.784 -28.698 26.159  1.00 44.39 ?  72  ASP B CB  1 
ATOM   3410 C  CG  . ASP B 1 72  ? -27.032 -28.586 25.304  1.00 52.26 ?  72  ASP B CG  1 
ATOM   3411 O  OD1 . ASP B 1 72  ? -27.210 -27.533 24.643  1.00 47.92 ?  72  ASP B OD1 1 
ATOM   3412 O  OD2 . ASP B 1 72  ? -27.819 -29.564 25.261  1.00 57.51 ?  72  ASP B OD2 1 
ATOM   3413 N  N   . ARG B 1 73  ? -22.351 -27.850 26.603  1.00 35.67 ?  73  ARG B N   1 
ATOM   3414 C  CA  . ARG B 1 73  ? -21.426 -27.077 27.423  1.00 34.95 ?  73  ARG B CA  1 
ATOM   3415 C  C   . ARG B 1 73  ? -21.089 -25.726 26.805  1.00 35.78 ?  73  ARG B C   1 
ATOM   3416 O  O   . ARG B 1 73  ? -20.301 -24.973 27.393  1.00 33.27 ?  73  ARG B O   1 
ATOM   3417 C  CB  . ARG B 1 73  ? -20.135 -27.849 27.680  1.00 35.67 ?  73  ARG B CB  1 
ATOM   3418 C  CG  . ARG B 1 73  ? -20.320 -29.322 27.959  1.00 43.43 ?  73  ARG B CG  1 
ATOM   3419 C  CD  . ARG B 1 73  ? -18.976 -30.020 28.010  1.00 39.27 ?  73  ARG B CD  1 
ATOM   3420 N  NE  . ARG B 1 73  ? -18.534 -30.422 26.678  1.00 38.83 ?  73  ARG B NE  1 
ATOM   3421 C  CZ  . ARG B 1 73  ? -17.317 -30.866 26.402  1.00 41.13 ?  73  ARG B CZ  1 
ATOM   3422 N  NH1 . ARG B 1 73  ? -16.399 -30.995 27.346  1.00 43.24 ?  73  ARG B NH1 1 
ATOM   3423 N  NH2 . ARG B 1 73  ? -17.010 -31.185 25.147  1.00 41.15 ?  73  ARG B NH2 1 
ATOM   3424 N  N   . PHE B 1 74  ? -21.636 -25.437 25.622  1.00 34.30 ?  74  PHE B N   1 
ATOM   3425 C  CA  . PHE B 1 74  ? -21.606 -24.111 25.011  1.00 30.38 ?  74  PHE B CA  1 
ATOM   3426 C  C   . PHE B 1 74  ? -23.015 -23.540 25.160  1.00 30.78 ?  74  PHE B C   1 
ATOM   3427 O  O   . PHE B 1 74  ? -23.966 -24.078 24.585  1.00 33.35 ?  74  PHE B O   1 
ATOM   3428 C  CB  . PHE B 1 74  ? -21.187 -24.209 23.541  1.00 29.37 ?  74  PHE B CB  1 
ATOM   3429 C  CG  . PHE B 1 74  ? -19.760 -24.663 23.339  1.00 30.30 ?  74  PHE B CG  1 
ATOM   3430 C  CD1 . PHE B 1 74  ? -18.695 -23.835 23.659  1.00 30.55 ?  74  PHE B CD1 1 
ATOM   3431 C  CD2 . PHE B 1 74  ? -19.486 -25.924 22.841  1.00 29.42 ?  74  PHE B CD2 1 
ATOM   3432 C  CE1 . PHE B 1 74  ? -17.386 -24.259 23.468  1.00 26.00 ?  74  PHE B CE1 1 
ATOM   3433 C  CE2 . PHE B 1 74  ? -18.187 -26.348 22.659  1.00 28.03 ?  74  PHE B CE2 1 
ATOM   3434 C  CZ  . PHE B 1 74  ? -17.138 -25.522 22.978  1.00 26.39 ?  74  PHE B CZ  1 
ATOM   3435 N  N   . SER B 1 75  ? -23.158 -22.467 25.943  1.00 27.70 ?  75  SER B N   1 
ATOM   3436 C  CA  . SER B 1 75  ? -24.463 -22.021 26.422  1.00 28.28 ?  75  SER B CA  1 
ATOM   3437 C  C   . SER B 1 75  ? -24.900 -20.722 25.752  1.00 25.39 ?  75  SER B C   1 
ATOM   3438 O  O   . SER B 1 75  ? -24.163 -19.732 25.765  1.00 26.02 ?  75  SER B O   1 
ATOM   3439 C  CB  . SER B 1 75  ? -24.449 -21.820 27.940  1.00 30.31 ?  75  SER B CB  1 
ATOM   3440 O  OG  . SER B 1 75  ? -25.576 -21.065 28.357  1.00 28.12 ?  75  SER B OG  1 
ATOM   3441 N  N   . LEU B 1 76  ? -26.126 -20.712 25.225  1.00 27.92 ?  76  LEU B N   1 
ATOM   3442 C  CA  . LEU B 1 76  ? -26.686 -19.491 24.651  1.00 27.86 ?  76  LEU B CA  1 
ATOM   3443 C  C   . LEU B 1 76  ? -27.190 -18.552 25.743  1.00 31.34 ?  76  LEU B C   1 
ATOM   3444 O  O   . LEU B 1 76  ? -26.919 -17.344 25.710  1.00 28.91 ?  76  LEU B O   1 
ATOM   3445 C  CB  . LEU B 1 76  ? -27.818 -19.832 23.673  1.00 24.00 ?  76  LEU B CB  1 
ATOM   3446 C  CG  . LEU B 1 76  ? -28.637 -18.643 23.170  1.00 29.27 ?  76  LEU B CG  1 
ATOM   3447 C  CD1 . LEU B 1 76  ? -27.753 -17.673 22.374  1.00 29.76 ?  76  LEU B CD1 1 
ATOM   3448 C  CD2 . LEU B 1 76  ? -29.817 -19.109 22.328  1.00 34.30 ?  76  LEU B CD2 1 
ATOM   3449 N  N   . LYS B 1 77  ? -27.910 -19.101 26.728  1.00 30.01 ?  77  LYS B N   1 
ATOM   3450 C  CA  . LYS B 1 77  ? -28.480 -18.290 27.802  1.00 30.80 ?  77  LYS B CA  1 
ATOM   3451 C  C   . LYS B 1 77  ? -27.437 -17.380 28.447  1.00 32.64 ?  77  LYS B C   1 
ATOM   3452 O  O   . LYS B 1 77  ? -27.690 -16.194 28.690  1.00 29.63 ?  77  LYS B O   1 
ATOM   3453 C  CB  . LYS B 1 77  ? -29.107 -19.203 28.853  1.00 36.51 ?  77  LYS B CB  1 
ATOM   3454 C  CG  . LYS B 1 77  ? -29.790 -18.442 29.976  1.00 45.52 ?  77  LYS B CG  1 
ATOM   3455 C  CD  . LYS B 1 77  ? -30.453 -19.371 30.991  1.00 46.91 ?  77  LYS B CD  1 
ATOM   3456 C  CE  . LYS B 1 77  ? -31.114 -18.613 32.125  1.00 47.57 ?  77  LYS B CE  1 
ATOM   3457 N  NZ  . LYS B 1 77  ? -31.743 -19.576 33.081  1.00 54.26 ?  77  LYS B NZ  1 
ATOM   3458 N  N   . ASP B 1 78  ? -26.252 -17.923 28.729  1.00 30.66 ?  78  ASP B N   1 
ATOM   3459 C  CA  . ASP B 1 78  ? -25.252 -17.213 29.513  1.00 31.29 ?  78  ASP B CA  1 
ATOM   3460 C  C   . ASP B 1 78  ? -24.541 -16.109 28.729  1.00 34.75 ?  78  ASP B C   1 
ATOM   3461 O  O   . ASP B 1 78  ? -23.754 -15.368 29.331  1.00 27.60 ?  78  ASP B O   1 
ATOM   3462 C  CB  . ASP B 1 78  ? -24.231 -18.219 30.060  1.00 32.70 ?  78  ASP B CB  1 
ATOM   3463 C  CG  . ASP B 1 78  ? -24.815 -19.113 31.167  1.00 33.02 ?  78  ASP B CG  1 
ATOM   3464 O  OD1 . ASP B 1 78  ? -25.885 -18.799 31.713  1.00 33.44 ?  78  ASP B OD1 1 
ATOM   3465 O  OD2 . ASP B 1 78  ? -24.207 -20.145 31.480  1.00 38.95 ?  78  ASP B OD2 1 
ATOM   3466 N  N   . THR B 1 79  ? -24.787 -15.978 27.416  1.00 28.75 ?  79  THR B N   1 
ATOM   3467 C  CA  . THR B 1 79  ? -24.194 -14.873 26.663  1.00 28.46 ?  79  THR B CA  1 
ATOM   3468 C  C   . THR B 1 79  ? -24.739 -13.528 27.111  1.00 30.72 ?  79  THR B C   1 
ATOM   3469 O  O   . THR B 1 79  ? -24.074 -12.504 26.904  1.00 28.51 ?  79  THR B O   1 
ATOM   3470 C  CB  . THR B 1 79  ? -24.440 -15.025 25.154  1.00 27.60 ?  79  THR B CB  1 
ATOM   3471 O  OG1 . THR B 1 79  ? -25.850 -15.117 24.896  1.00 28.61 ?  79  THR B OG1 1 
ATOM   3472 C  CG2 . THR B 1 79  ? -23.721 -16.245 24.603  1.00 22.61 ?  79  THR B CG2 1 
ATOM   3473 N  N   . ALA B 1 80  ? -25.942 -13.518 27.690  1.00 32.56 ?  80  ALA B N   1 
ATOM   3474 C  CA  . ALA B 1 80  ? -26.621 -12.335 28.201  1.00 31.84 ?  80  ALA B CA  1 
ATOM   3475 C  C   . ALA B 1 80  ? -26.283 -12.028 29.656  1.00 36.04 ?  80  ALA B C   1 
ATOM   3476 O  O   . ALA B 1 80  ? -26.866 -11.100 30.218  1.00 40.32 ?  80  ALA B O   1 
ATOM   3477 C  CB  . ALA B 1 80  ? -28.136 -12.507 28.071  1.00 31.95 ?  80  ALA B CB  1 
ATOM   3478 N  N   . ASN B 1 81  ? -25.358 -12.781 30.287  1.00 34.36 ?  81  ASN B N   1 
ATOM   3479 C  CA  . ASN B 1 81  ? -25.042 -12.527 31.685  1.00 38.11 ?  81  ASN B CA  1 
ATOM   3480 C  C   . ASN B 1 81  ? -24.163 -11.282 31.826  1.00 39.33 ?  81  ASN B C   1 
ATOM   3481 O  O   . ASN B 1 81  ? -23.366 -10.971 30.938  1.00 40.28 ?  81  ASN B O   1 
ATOM   3482 C  CB  . ASN B 1 81  ? -24.330 -13.730 32.312  1.00 36.26 ?  81  ASN B CB  1 
ATOM   3483 C  CG  . ASN B 1 81  ? -25.238 -14.944 32.477  1.00 41.69 ?  81  ASN B CG  1 
ATOM   3484 O  OD1 . ASN B 1 81  ? -26.460 -14.861 32.332  1.00 38.59 ?  81  ASN B OD1 1 
ATOM   3485 N  ND2 . ASN B 1 81  ? -24.632 -16.084 32.802  1.00 38.75 ?  81  ASN B ND2 1 
ATOM   3486 N  N   . PRO B 1 82  ? -24.287 -10.560 32.938  1.00 41.12 ?  82  PRO B N   1 
ATOM   3487 C  CA  . PRO B 1 82  ? -23.430 -9.384  33.159  1.00 37.57 ?  82  PRO B CA  1 
ATOM   3488 C  C   . PRO B 1 82  ? -21.954 -9.756  33.167  1.00 37.50 ?  82  PRO B C   1 
ATOM   3489 O  O   . PRO B 1 82  ? -21.543 -10.734 33.794  1.00 38.17 ?  82  PRO B O   1 
ATOM   3490 C  CB  . PRO B 1 82  ? -23.871 -8.864  34.534  1.00 37.33 ?  82  PRO B CB  1 
ATOM   3491 C  CG  . PRO B 1 82  ? -25.126 -9.578  34.885  1.00 42.83 ?  82  PRO B CG  1 
ATOM   3492 C  CD  . PRO B 1 82  ? -25.277 -10.774 34.010  1.00 40.87 ?  82  PRO B CD  1 
ATOM   3493 N  N   . GLY B 1 83  ? -21.150 -8.956  32.475  1.00 41.86 ?  83  GLY B N   1 
ATOM   3494 C  CA  . GLY B 1 83  ? -19.712 -9.080  32.579  1.00 37.78 ?  83  GLY B CA  1 
ATOM   3495 C  C   . GLY B 1 83  ? -19.063 -10.166 31.745  1.00 35.87 ?  83  GLY B C   1 
ATOM   3496 O  O   . GLY B 1 83  ? -17.834 -10.277 31.770  1.00 36.99 ?  83  GLY B O   1 
ATOM   3497 N  N   . VAL B 1 84  ? -19.827 -10.976 31.015  1.00 34.45 ?  84  VAL B N   1 
ATOM   3498 C  CA  . VAL B 1 84  ? -19.228 -11.939 30.083  1.00 32.04 ?  84  VAL B CA  1 
ATOM   3499 C  C   . VAL B 1 84  ? -18.786 -11.204 28.822  1.00 33.63 ?  84  VAL B C   1 
ATOM   3500 O  O   . VAL B 1 84  ? -19.342 -10.142 28.505  1.00 34.74 ?  84  VAL B O   1 
ATOM   3501 C  CB  . VAL B 1 84  ? -20.203 -13.071 29.728  1.00 33.62 ?  84  VAL B CB  1 
ATOM   3502 C  CG1 . VAL B 1 84  ? -20.673 -13.802 30.998  1.00 32.34 ?  84  VAL B CG1 1 
ATOM   3503 C  CG2 . VAL B 1 84  ? -21.385 -12.518 28.920  1.00 30.75 ?  84  VAL B CG2 1 
ATOM   3504 N  N   . PRO B 1 85  ? -17.800 -11.713 28.079  1.00 32.63 ?  85  PRO B N   1 
ATOM   3505 C  CA  . PRO B 1 85  ? -17.441 -11.068 26.810  1.00 31.08 ?  85  PRO B CA  1 
ATOM   3506 C  C   . PRO B 1 85  ? -18.605 -11.109 25.824  1.00 28.61 ?  85  PRO B C   1 
ATOM   3507 O  O   . PRO B 1 85  ? -19.429 -12.027 25.835  1.00 29.60 ?  85  PRO B O   1 
ATOM   3508 C  CB  . PRO B 1 85  ? -16.237 -11.883 26.314  1.00 31.98 ?  85  PRO B CB  1 
ATOM   3509 C  CG  . PRO B 1 85  ? -16.223 -13.139 27.146  1.00 32.50 ?  85  PRO B CG  1 
ATOM   3510 C  CD  . PRO B 1 85  ? -16.877 -12.804 28.441  1.00 29.85 ?  85  PRO B CD  1 
ATOM   3511 N  N   . ARG B 1 86  ? -18.678 -10.077 24.978  1.00 29.20 ?  86  ARG B N   1 
ATOM   3512 C  CA  . ARG B 1 86  ? -19.820 -9.847  24.100  1.00 28.14 ?  86  ARG B CA  1 
ATOM   3513 C  C   . ARG B 1 86  ? -19.344 -9.551  22.690  1.00 26.95 ?  86  ARG B C   1 
ATOM   3514 O  O   . ARG B 1 86  ? -18.332 -8.868  22.506  1.00 25.62 ?  86  ARG B O   1 
ATOM   3515 C  CB  . ARG B 1 86  ? -20.663 -8.650  24.541  1.00 30.53 ?  86  ARG B CB  1 
ATOM   3516 C  CG  . ARG B 1 86  ? -21.016 -8.553  25.999  1.00 36.61 ?  86  ARG B CG  1 
ATOM   3517 C  CD  . ARG B 1 86  ? -22.329 -7.816  26.109  1.00 36.76 ?  86  ARG B CD  1 
ATOM   3518 N  NE  . ARG B 1 86  ? -23.299 -8.379  25.174  1.00 38.59 ?  86  ARG B NE  1 
ATOM   3519 C  CZ  . ARG B 1 86  ? -24.125 -9.371  25.477  1.00 39.37 ?  86  ARG B CZ  1 
ATOM   3520 N  NH1 . ARG B 1 86  ? -24.139 -9.909  26.686  1.00 40.39 ?  86  ARG B NH1 1 
ATOM   3521 N  NH2 . ARG B 1 86  ? -24.960 -9.829  24.550  1.00 41.96 ?  86  ARG B NH2 1 
ATOM   3522 N  N   . GLN B 1 87  ? -20.103 -10.016 21.694  1.00 28.11 ?  87  GLN B N   1 
ATOM   3523 C  CA  . GLN B 1 87  ? -19.822 -9.567  20.332  1.00 27.64 ?  87  GLN B CA  1 
ATOM   3524 C  C   . GLN B 1 87  ? -20.392 -8.176  20.057  1.00 25.26 ?  87  GLN B C   1 
ATOM   3525 O  O   . GLN B 1 87  ? -19.834 -7.445  19.236  1.00 28.47 ?  87  GLN B O   1 
ATOM   3526 C  CB  . GLN B 1 87  ? -20.334 -10.579 19.299  1.00 25.48 ?  87  GLN B CB  1 
ATOM   3527 C  CG  . GLN B 1 87  ? -21.785 -11.010 19.424  1.00 24.56 ?  87  GLN B CG  1 
ATOM   3528 C  CD  . GLN B 1 87  ? -22.223 -11.816 18.218  1.00 24.52 ?  87  GLN B CD  1 
ATOM   3529 O  OE1 . GLN B 1 87  ? -21.622 -11.709 17.144  1.00 24.80 ?  87  GLN B OE1 1 
ATOM   3530 N  NE2 . GLN B 1 87  ? -23.285 -12.607 18.372  1.00 23.54 ?  87  GLN B NE2 1 
ATOM   3531 N  N   . TYR B 1 88  ? -21.482 -7.792  20.721  1.00 24.85 ?  88  TYR B N   1 
ATOM   3532 C  CA  . TYR B 1 88  ? -22.008 -6.429  20.668  1.00 22.68 ?  88  TYR B CA  1 
ATOM   3533 C  C   . TYR B 1 88  ? -22.900 -6.228  21.886  1.00 30.26 ?  88  TYR B C   1 
ATOM   3534 O  O   . TYR B 1 88  ? -23.220 -7.176  22.603  1.00 27.15 ?  88  TYR B O   1 
ATOM   3535 C  CB  . TYR B 1 88  ? -22.777 -6.138  19.364  1.00 20.90 ?  88  TYR B CB  1 
ATOM   3536 C  CG  . TYR B 1 88  ? -23.685 -7.260  18.935  1.00 26.41 ?  88  TYR B CG  1 
ATOM   3537 C  CD1 . TYR B 1 88  ? -24.904 -7.481  19.576  1.00 24.65 ?  88  TYR B CD1 1 
ATOM   3538 C  CD2 . TYR B 1 88  ? -23.319 -8.109  17.897  1.00 23.08 ?  88  TYR B CD2 1 
ATOM   3539 C  CE1 . TYR B 1 88  ? -25.734 -8.510  19.185  1.00 25.39 ?  88  TYR B CE1 1 
ATOM   3540 C  CE2 . TYR B 1 88  ? -24.140 -9.138  17.501  1.00 22.67 ?  88  TYR B CE2 1 
ATOM   3541 C  CZ  . TYR B 1 88  ? -25.338 -9.334  18.142  1.00 24.79 ?  88  TYR B CZ  1 
ATOM   3542 O  OH  . TYR B 1 88  ? -26.136 -10.367 17.740  1.00 22.36 ?  88  TYR B OH  1 
ATOM   3543 N  N   . ALA B 1 89  ? -23.292 -4.975  22.116  1.00 23.23 ?  89  ALA B N   1 
ATOM   3544 C  CA  . ALA B 1 89  ? -24.037 -4.646  23.323  1.00 29.28 ?  89  ALA B CA  1 
ATOM   3545 C  C   . ALA B 1 89  ? -25.394 -5.334  23.336  1.00 29.58 ?  89  ALA B C   1 
ATOM   3546 O  O   . ALA B 1 89  ? -26.056 -5.458  22.305  1.00 29.96 ?  89  ALA B O   1 
ATOM   3547 C  CB  . ALA B 1 89  ? -24.232 -3.128  23.441  1.00 25.89 ?  89  ALA B CB  1 
ATOM   3548 N  N   . LEU B 1 90  ? -25.798 -5.789  24.521  1.00 32.21 ?  90  LEU B N   1 
ATOM   3549 C  CA  . LEU B 1 90  ? -27.166 -6.239  24.739  1.00 33.84 ?  90  LEU B CA  1 
ATOM   3550 C  C   . LEU B 1 90  ? -28.130 -5.101  24.452  1.00 31.98 ?  90  LEU B C   1 
ATOM   3551 O  O   . LEU B 1 90  ? -27.920 -3.975  24.910  1.00 35.70 ?  90  LEU B O   1 
ATOM   3552 C  CB  . LEU B 1 90  ? -27.336 -6.699  26.190  1.00 36.16 ?  90  LEU B CB  1 
ATOM   3553 C  CG  . LEU B 1 90  ? -28.682 -7.161  26.731  1.00 39.57 ?  90  LEU B CG  1 
ATOM   3554 C  CD1 . LEU B 1 90  ? -29.125 -8.413  25.972  1.00 39.91 ?  90  LEU B CD1 1 
ATOM   3555 C  CD2 . LEU B 1 90  ? -28.624 -7.419  28.232  1.00 35.89 ?  90  LEU B CD2 1 
ATOM   3556 N  N   . THR B 1 91  ? -29.195 -5.388  23.704  1.00 34.99 ?  91  THR B N   1 
ATOM   3557 C  CA  . THR B 1 91  ? -30.220 -4.388  23.431  1.00 37.65 ?  91  THR B CA  1 
ATOM   3558 C  C   . THR B 1 91  ? -31.587 -4.790  23.956  1.00 35.99 ?  91  THR B C   1 
ATOM   3559 O  O   . THR B 1 91  ? -32.544 -4.020  23.807  1.00 34.95 ?  91  THR B O   1 
ATOM   3560 C  CB  . THR B 1 91  ? -30.321 -4.110  21.926  1.00 35.26 ?  91  THR B CB  1 
ATOM   3561 O  OG1 . THR B 1 91  ? -30.605 -5.330  21.235  1.00 35.82 ?  91  THR B OG1 1 
ATOM   3562 C  CG2 . THR B 1 91  ? -28.997 -3.553  21.407  1.00 32.97 ?  91  THR B CG2 1 
ATOM   3563 N  N   . ILE B 1 92  ? -31.706 -5.968  24.557  1.00 34.76 ?  92  ILE B N   1 
ATOM   3564 C  CA  . ILE B 1 92  ? -32.952 -6.460  25.136  1.00 36.16 ?  92  ILE B CA  1 
ATOM   3565 C  C   . ILE B 1 92  ? -32.633 -6.902  26.560  1.00 42.73 ?  92  ILE B C   1 
ATOM   3566 O  O   . ILE B 1 92  ? -31.449 -7.043  26.902  1.00 36.57 ?  92  ILE B O   1 
ATOM   3567 C  CB  . ILE B 1 92  ? -33.541 -7.617  24.311  1.00 39.24 ?  92  ILE B CB  1 
ATOM   3568 C  CG1 . ILE B 1 92  ? -32.562 -8.799  24.274  1.00 41.12 ?  92  ILE B CG1 1 
ATOM   3569 C  CG2 . ILE B 1 92  ? -33.895 -7.148  22.918  1.00 38.26 ?  92  ILE B CG2 1 
ATOM   3570 C  CD1 . ILE B 1 92  ? -33.143 -10.068 23.665  1.00 43.92 ?  92  ILE B CD1 1 
ATOM   3571 N  N   . PRO B 1 93  ? -33.624 -7.112  27.423  1.00 46.69 ?  93  PRO B N   1 
ATOM   3572 C  CA  . PRO B 1 93  ? -33.336 -7.672  28.755  1.00 46.80 ?  93  PRO B CA  1 
ATOM   3573 C  C   . PRO B 1 93  ? -32.687 -9.039  28.637  1.00 47.87 ?  93  PRO B C   1 
ATOM   3574 O  O   . PRO B 1 93  ? -33.063 -9.846  27.771  1.00 46.08 ?  93  PRO B O   1 
ATOM   3575 C  CB  . PRO B 1 93  ? -34.721 -7.761  29.417  1.00 46.77 ?  93  PRO B CB  1 
ATOM   3576 C  CG  . PRO B 1 93  ? -35.551 -6.741  28.709  1.00 44.29 ?  93  PRO B CG  1 
ATOM   3577 C  CD  . PRO B 1 93  ? -35.029 -6.687  27.291  1.00 43.19 ?  93  PRO B CD  1 
ATOM   3578 N  N   . PRO B 1 94  ? -31.695 -9.326  29.483  1.00 48.96 ?  94  PRO B N   1 
ATOM   3579 C  CA  . PRO B 1 94  ? -30.961 -10.596 29.362  1.00 46.88 ?  94  PRO B CA  1 
ATOM   3580 C  C   . PRO B 1 94  ? -31.838 -11.830 29.394  1.00 49.28 ?  94  PRO B C   1 
ATOM   3581 O  O   . PRO B 1 94  ? -31.452 -12.861 28.825  1.00 45.20 ?  94  PRO B O   1 
ATOM   3582 C  CB  . PRO B 1 94  ? -29.993 -10.553 30.558  1.00 48.47 ?  94  PRO B CB  1 
ATOM   3583 C  CG  . PRO B 1 94  ? -30.454 -9.390  31.416  1.00 52.91 ?  94  PRO B CG  1 
ATOM   3584 C  CD  . PRO B 1 94  ? -31.063 -8.426  30.460  1.00 49.35 ?  94  PRO B CD  1 
ATOM   3585 N  N   . GLU B 1 95  ? -33.010 -11.766 30.032  1.00 49.08 ?  95  GLU B N   1 
ATOM   3586 C  CA  . GLU B 1 95  ? -33.906 -12.919 30.018  1.00 52.93 ?  95  GLU B CA  1 
ATOM   3587 C  C   . GLU B 1 95  ? -34.412 -13.221 28.617  1.00 49.32 ?  95  GLU B C   1 
ATOM   3588 O  O   . GLU B 1 95  ? -34.675 -14.384 28.294  1.00 52.53 ?  95  GLU B O   1 
ATOM   3589 C  CB  . GLU B 1 95  ? -35.098 -12.695 30.957  1.00 54.60 ?  95  GLU B CB  1 
ATOM   3590 C  CG  . GLU B 1 95  ? -34.746 -12.626 32.429  1.00 58.87 ?  95  GLU B CG  1 
ATOM   3591 C  CD  . GLU B 1 95  ? -34.476 -11.200 32.884  1.00 69.98 ?  95  GLU B CD  1 
ATOM   3592 O  OE1 . GLU B 1 95  ? -35.210 -10.279 32.442  1.00 64.74 ?  95  GLU B OE1 1 
ATOM   3593 O  OE2 . GLU B 1 95  ? -33.537 -11.000 33.695  1.00 71.21 ?  95  GLU B OE2 1 
ATOM   3594 N  N   . VAL B 1 96  ? -34.552 -12.197 27.771  1.00 47.68 ?  96  VAL B N   1 
ATOM   3595 C  CA  . VAL B 1 96  ? -35.133 -12.418 26.449  1.00 47.04 ?  96  VAL B CA  1 
ATOM   3596 C  C   . VAL B 1 96  ? -34.228 -13.285 25.584  1.00 44.35 ?  96  VAL B C   1 
ATOM   3597 O  O   . VAL B 1 96  ? -34.721 -14.087 24.779  1.00 43.33 ?  96  VAL B O   1 
ATOM   3598 C  CB  . VAL B 1 96  ? -35.456 -11.080 25.762  1.00 42.18 ?  96  VAL B CB  1 
ATOM   3599 C  CG1 . VAL B 1 96  ? -35.941 -11.331 24.348  1.00 42.34 ?  96  VAL B CG1 1 
ATOM   3600 C  CG2 . VAL B 1 96  ? -36.524 -10.345 26.541  1.00 40.26 ?  96  VAL B CG2 1 
ATOM   3601 N  N   . VAL B 1 97  ? -32.904 -13.162 25.737  1.00 41.99 ?  97  VAL B N   1 
ATOM   3602 C  CA  . VAL B 1 97  ? -31.990 -14.073 25.046  1.00 44.01 ?  97  VAL B CA  1 
ATOM   3603 C  C   . VAL B 1 97  ? -32.329 -15.526 25.364  1.00 46.88 ?  97  VAL B C   1 
ATOM   3604 O  O   . VAL B 1 97  ? -32.103 -16.425 24.540  1.00 43.22 ?  97  VAL B O   1 
ATOM   3605 C  CB  . VAL B 1 97  ? -30.526 -13.741 25.408  1.00 42.82 ?  97  VAL B CB  1 
ATOM   3606 C  CG1 . VAL B 1 97  ? -29.575 -14.659 24.665  1.00 35.73 ?  97  VAL B CG1 1 
ATOM   3607 C  CG2 . VAL B 1 97  ? -30.214 -12.281 25.086  1.00 38.70 ?  97  VAL B CG2 1 
ATOM   3608 N  N   . ASN B 1 98  ? -32.891 -15.777 26.550  1.00 45.94 ?  98  ASN B N   1 
ATOM   3609 C  CA  . ASN B 1 98  ? -33.388 -17.090 26.946  1.00 47.77 ?  98  ASN B CA  1 
ATOM   3610 C  C   . ASN B 1 98  ? -34.892 -17.226 26.718  1.00 50.38 ?  98  ASN B C   1 
ATOM   3611 O  O   . ASN B 1 98  ? -35.582 -17.896 27.498  1.00 52.35 ?  98  ASN B O   1 
ATOM   3612 C  CB  . ASN B 1 98  ? -33.047 -17.361 28.414  1.00 49.89 ?  98  ASN B CB  1 
ATOM   3613 C  CG  . ASN B 1 98  ? -33.159 -18.833 28.781  1.00 52.95 ?  98  ASN B CG  1 
ATOM   3614 O  OD1 . ASN B 1 98  ? -32.929 -19.714 27.949  1.00 54.42 ?  98  ASN B OD1 1 
ATOM   3615 N  ND2 . ASN B 1 98  ? -33.543 -19.104 30.024  1.00 50.08 ?  98  ASN B ND2 1 
ATOM   3616 N  N   . ASN B 1 99  ? -35.410 -16.585 25.665  1.00 47.56 ?  99  ASN B N   1 
ATOM   3617 C  CA  . ASN B 1 99  ? -36.828 -16.660 25.315  1.00 47.86 ?  99  ASN B CA  1 
ATOM   3618 C  C   . ASN B 1 99  ? -37.377 -18.078 25.415  1.00 52.08 ?  99  ASN B C   1 
ATOM   3619 O  O   . ASN B 1 99  ? -38.433 -18.313 26.014  1.00 49.96 ?  99  ASN B O   1 
ATOM   3620 C  CB  . ASN B 1 99  ? -37.029 -16.127 23.894  1.00 45.91 ?  99  ASN B CB  1 
ATOM   3621 C  CG  . ASN B 1 99  ? -38.319 -15.355 23.736  1.00 50.24 ?  99  ASN B CG  1 
ATOM   3622 O  OD1 . ASN B 1 99  ? -38.864 -14.832 24.713  1.00 53.65 ?  99  ASN B OD1 1 
ATOM   3623 N  ND2 . ASN B 1 99  ? -38.818 -15.272 22.500  1.00 45.16 ?  99  ASN B ND2 1 
ATOM   3624 N  N   . MET B 1 100 ? -36.647 -19.037 24.836  1.00 49.07 ?  100 MET B N   1 
ATOM   3625 C  CA  . MET B 1 100 ? -37.142 -20.405 24.739  1.00 51.36 ?  100 MET B CA  1 
ATOM   3626 C  C   . MET B 1 100 ? -37.096 -21.109 26.084  1.00 50.33 ?  100 MET B C   1 
ATOM   3627 O  O   . MET B 1 100 ? -37.967 -21.933 26.385  1.00 52.28 ?  100 MET B O   1 
ATOM   3628 C  CB  . MET B 1 100 ? -36.332 -21.171 23.701  1.00 47.47 ?  100 MET B CB  1 
ATOM   3629 C  CG  . MET B 1 100 ? -36.840 -20.951 22.304  1.00 48.54 ?  100 MET B CG  1 
ATOM   3630 S  SD  . MET B 1 100 ? -38.629 -20.943 22.289  1.00 62.17 ?  100 MET B SD  1 
ATOM   3631 C  CE  . MET B 1 100 ? -38.886 -22.613 21.754  1.00 49.55 ?  100 MET B CE  1 
ATOM   3632 N  N   . GLY B 1 101 ? -36.081 -20.812 26.897  1.00 54.19 ?  101 GLY B N   1 
ATOM   3633 C  CA  . GLY B 1 101 ? -36.083 -21.301 28.265  1.00 51.74 ?  101 GLY B CA  1 
ATOM   3634 C  C   . GLY B 1 101 ? -37.288 -20.806 29.043  1.00 54.13 ?  101 GLY B C   1 
ATOM   3635 O  O   . GLY B 1 101 ? -38.014 -21.593 29.658  1.00 55.94 ?  101 GLY B O   1 
ATOM   3636 N  N   . ASN B 1 102 ? -37.527 -19.488 29.010  1.00 55.08 ?  102 ASN B N   1 
ATOM   3637 C  CA  . ASN B 1 102 ? -38.663 -18.912 29.729  1.00 56.59 ?  102 ASN B CA  1 
ATOM   3638 C  C   . ASN B 1 102 ? -39.998 -19.418 29.190  1.00 52.93 ?  102 ASN B C   1 
ATOM   3639 O  O   . ASN B 1 102 ? -40.950 -19.591 29.960  1.00 55.75 ?  102 ASN B O   1 
ATOM   3640 C  CB  . ASN B 1 102 ? -38.616 -17.381 29.663  1.00 55.48 ?  102 ASN B CB  1 
ATOM   3641 C  CG  . ASN B 1 102 ? -37.251 -16.819 30.025  1.00 54.33 ?  102 ASN B CG  1 
ATOM   3642 O  OD1 . ASN B 1 102 ? -36.620 -17.257 30.988  1.00 56.20 ?  102 ASN B OD1 1 
ATOM   3643 N  ND2 . ASN B 1 102 ? -36.785 -15.848 29.246  1.00 54.33 ?  102 ASN B ND2 1 
ATOM   3644 N  N   . ILE B 1 103 ? -40.093 -19.651 27.878  1.00 52.43 ?  103 ILE B N   1 
ATOM   3645 C  CA  . ILE B 1 103 ? -41.333 -20.168 27.309  1.00 50.11 ?  103 ILE B CA  1 
ATOM   3646 C  C   . ILE B 1 103 ? -41.594 -21.590 27.794  1.00 56.78 ?  103 ILE B C   1 
ATOM   3647 O  O   . ILE B 1 103 ? -42.755 -21.995 27.973  1.00 53.09 ?  103 ILE B O   1 
ATOM   3648 C  CB  . ILE B 1 103 ? -41.272 -20.079 25.771  1.00 50.68 ?  103 ILE B CB  1 
ATOM   3649 C  CG1 . ILE B 1 103 ? -41.463 -18.631 25.318  1.00 43.93 ?  103 ILE B CG1 1 
ATOM   3650 C  CG2 . ILE B 1 103 ? -42.300 -20.994 25.117  1.00 48.11 ?  103 ILE B CG2 1 
ATOM   3651 C  CD1 . ILE B 1 103 ? -41.237 -18.410 23.831  1.00 41.48 ?  103 ILE B CD1 1 
ATOM   3652 N  N   . ASN B 1 104 ? -40.530 -22.361 28.034  1.00 54.53 ?  104 ASN B N   1 
ATOM   3653 C  CA  . ASN B 1 104 ? -40.703 -23.731 28.496  1.00 56.78 ?  104 ASN B CA  1 
ATOM   3654 C  C   . ASN B 1 104 ? -41.159 -23.759 29.952  1.00 54.28 ?  104 ASN B C   1 
ATOM   3655 O  O   . ASN B 1 104 ? -42.185 -24.367 30.282  1.00 57.51 ?  104 ASN B O   1 
ATOM   3656 C  CB  . ASN B 1 104 ? -39.397 -24.505 28.323  1.00 56.28 ?  104 ASN B CB  1 
ATOM   3657 C  CG  . ASN B 1 104 ? -39.138 -24.887 26.878  1.00 61.89 ?  104 ASN B CG  1 
ATOM   3658 O  OD1 . ASN B 1 104 ? -39.960 -24.618 26.000  1.00 53.17 ?  104 ASN B OD1 1 
ATOM   3659 N  ND2 . ASN B 1 104 ? -37.993 -25.515 26.622  1.00 61.76 ?  104 ASN B ND2 1 
ATOM   3660 N  N   . SER B 1 105 ? -40.422 -23.079 30.833  1.00 52.96 ?  105 SER B N   1 
ATOM   3661 C  CA  . SER B 1 105 ? -40.654 -23.184 32.270  1.00 56.71 ?  105 SER B CA  1 
ATOM   3662 C  C   . SER B 1 105 ? -41.965 -22.548 32.724  1.00 56.17 ?  105 SER B C   1 
ATOM   3663 O  O   . SER B 1 105 ? -42.361 -22.753 33.875  1.00 54.06 ?  105 SER B O   1 
ATOM   3664 C  CB  . SER B 1 105 ? -39.484 -22.553 33.028  1.00 57.85 ?  105 SER B CB  1 
ATOM   3665 O  OG  . SER B 1 105 ? -39.395 -21.162 32.764  1.00 62.57 ?  105 SER B OG  1 
ATOM   3666 N  N   . ALA B 1 106 ? -42.645 -21.789 31.867  1.00 54.78 ?  106 ALA B N   1 
ATOM   3667 C  CA  . ALA B 1 106 ? -43.875 -21.110 32.253  1.00 50.85 ?  106 ALA B CA  1 
ATOM   3668 C  C   . ALA B 1 106 ? -45.117 -21.739 31.639  1.00 49.59 ?  106 ALA B C   1 
ATOM   3669 O  O   . ALA B 1 106 ? -46.186 -21.122 31.668  1.00 51.10 ?  106 ALA B O   1 
ATOM   3670 C  CB  . ALA B 1 106 ? -43.806 -19.628 31.878  1.00 55.03 ?  106 ALA B CB  1 
ATOM   3671 N  N   . GLY B 1 107 ? -45.014 -22.950 31.095  1.00 51.84 ?  107 GLY B N   1 
ATOM   3672 C  CA  . GLY B 1 107 ? -46.165 -23.549 30.446  1.00 53.24 ?  107 GLY B CA  1 
ATOM   3673 C  C   . GLY B 1 107 ? -46.595 -22.835 29.185  1.00 54.11 ?  107 GLY B C   1 
ATOM   3674 O  O   . GLY B 1 107 ? -47.740 -22.987 28.751  1.00 47.62 ?  107 GLY B O   1 
ATOM   3675 N  N   . LEU B 1 108 ? -45.702 -22.044 28.591  1.00 51.89 ?  108 LEU B N   1 
ATOM   3676 C  CA  . LEU B 1 108 ? -45.991 -21.278 27.392  1.00 48.14 ?  108 LEU B CA  1 
ATOM   3677 C  C   . LEU B 1 108 ? -45.621 -22.024 26.119  1.00 46.29 ?  108 LEU B C   1 
ATOM   3678 O  O   . LEU B 1 108 ? -45.995 -21.579 25.029  1.00 47.80 ?  108 LEU B O   1 
ATOM   3679 C  CB  . LEU B 1 108 ? -45.243 -19.939 27.443  1.00 49.33 ?  108 LEU B CB  1 
ATOM   3680 C  CG  . LEU B 1 108 ? -45.648 -18.953 28.543  1.00 46.30 ?  108 LEU B CG  1 
ATOM   3681 C  CD1 . LEU B 1 108 ? -44.727 -17.741 28.560  1.00 42.76 ?  108 LEU B CD1 1 
ATOM   3682 C  CD2 . LEU B 1 108 ? -47.100 -18.514 28.387  1.00 51.00 ?  108 LEU B CD2 1 
ATOM   3683 N  N   . ARG B 1 109 ? -44.923 -23.158 26.236  1.00 49.25 ?  109 ARG B N   1 
ATOM   3684 C  CA  . ARG B 1 109 ? -44.427 -23.876 25.063  1.00 48.43 ?  109 ARG B CA  1 
ATOM   3685 C  C   . ARG B 1 109 ? -45.551 -24.296 24.127  1.00 48.29 ?  109 ARG B C   1 
ATOM   3686 O  O   . ARG B 1 109 ? -45.423 -24.188 22.899  1.00 44.73 ?  109 ARG B O   1 
ATOM   3687 C  CB  . ARG B 1 109 ? -43.640 -25.106 25.500  1.00 53.52 ?  109 ARG B CB  1 
ATOM   3688 C  CG  . ARG B 1 109 ? -42.993 -25.834 24.340  1.00 56.16 ?  109 ARG B CG  1 
ATOM   3689 C  CD  . ARG B 1 109 ? -42.157 -26.974 24.853  1.00 60.10 ?  109 ARG B CD  1 
ATOM   3690 N  NE  . ARG B 1 109 ? -41.523 -27.732 23.782  1.00 63.81 ?  109 ARG B NE  1 
ATOM   3691 C  CZ  . ARG B 1 109 ? -40.391 -27.377 23.196  1.00 66.25 ?  109 ARG B CZ  1 
ATOM   3692 N  NH1 . ARG B 1 109 ? -39.747 -26.282 23.556  1.00 68.33 ?  109 ARG B NH1 1 
ATOM   3693 N  NH2 . ARG B 1 109 ? -39.913 -28.119 22.203  1.00 67.11 ?  109 ARG B NH2 1 
ATOM   3694 N  N   . ASN B 1 110 ? -46.650 -24.802 24.682  1.00 42.82 ?  110 ASN B N   1 
ATOM   3695 C  CA  . ASN B 1 110 ? -47.740 -25.266 23.835  1.00 49.79 ?  110 ASN B CA  1 
ATOM   3696 C  C   . ASN B 1 110 ? -48.269 -24.142 22.958  1.00 45.21 ?  110 ASN B C   1 
ATOM   3697 O  O   . ASN B 1 110 ? -48.356 -24.286 21.732  1.00 47.35 ?  110 ASN B O   1 
ATOM   3698 C  CB  . ASN B 1 110 ? -48.862 -25.852 24.688  1.00 54.27 ?  110 ASN B CB  1 
ATOM   3699 C  CG  . ASN B 1 110 ? -49.873 -26.602 23.860  1.00 62.72 ?  110 ASN B CG  1 
ATOM   3700 O  OD1 . ASN B 1 110 ? -49.535 -27.182 22.825  1.00 66.29 ?  110 ASN B OD1 1 
ATOM   3701 N  ND2 . ASN B 1 110 ? -51.120 -26.617 24.317  1.00 65.32 ?  110 ASN B ND2 1 
ATOM   3702 N  N   . ALA B 1 111 ? -48.623 -23.007 23.575  1.00 40.57 ?  111 ALA B N   1 
ATOM   3703 C  CA  . ALA B 1 111 ? -49.147 -21.872 22.820  1.00 40.33 ?  111 ALA B CA  1 
ATOM   3704 C  C   . ALA B 1 111 ? -48.164 -21.422 21.744  1.00 34.93 ?  111 ALA B C   1 
ATOM   3705 O  O   . ALA B 1 111 ? -48.544 -21.220 20.586  1.00 36.44 ?  111 ALA B O   1 
ATOM   3706 C  CB  . ALA B 1 111 ? -49.470 -20.720 23.770  1.00 40.95 ?  111 ALA B CB  1 
ATOM   3707 N  N   . VAL B 1 112 ? -46.891 -21.272 22.113  1.00 37.37 ?  112 VAL B N   1 
ATOM   3708 C  CA  . VAL B 1 112 ? -45.868 -20.853 21.153  1.00 39.46 ?  112 VAL B CA  1 
ATOM   3709 C  C   . VAL B 1 112 ? -45.742 -21.880 20.031  1.00 37.42 ?  112 VAL B C   1 
ATOM   3710 O  O   . VAL B 1 112 ? -45.888 -21.553 18.848  1.00 37.63 ?  112 VAL B O   1 
ATOM   3711 C  CB  . VAL B 1 112 ? -44.524 -20.626 21.868  1.00 36.84 ?  112 VAL B CB  1 
ATOM   3712 C  CG1 . VAL B 1 112 ? -43.411 -20.391 20.860  1.00 36.85 ?  112 VAL B CG1 1 
ATOM   3713 C  CG2 . VAL B 1 112 ? -44.627 -19.460 22.842  1.00 34.22 ?  112 VAL B CG2 1 
ATOM   3714 N  N   . MET B 1 113 ? -45.502 -23.146 20.396  1.00 41.75 ?  113 MET B N   1 
ATOM   3715 C  CA  . MET B 1 113 ? -45.319 -24.199 19.395  1.00 42.10 ?  113 MET B CA  1 
ATOM   3716 C  C   . MET B 1 113 ? -46.504 -24.300 18.446  1.00 41.85 ?  113 MET B C   1 
ATOM   3717 O  O   . MET B 1 113 ? -46.323 -24.449 17.233  1.00 42.84 ?  113 MET B O   1 
ATOM   3718 C  CB  . MET B 1 113 ? -45.074 -25.541 20.083  1.00 50.86 ?  113 MET B CB  1 
ATOM   3719 C  CG  . MET B 1 113 ? -43.802 -25.567 20.881  1.00 50.71 ?  113 MET B CG  1 
ATOM   3720 S  SD  . MET B 1 113 ? -42.409 -25.332 19.755  1.00 62.55 ?  113 MET B SD  1 
ATOM   3721 C  CE  . MET B 1 113 ? -42.012 -23.634 20.074  1.00 51.29 ?  113 MET B CE  1 
ATOM   3722 N  N   . LYS B 1 114 ? -47.726 -24.233 18.971  1.00 45.72 ?  114 LYS B N   1 
ATOM   3723 C  CA  . LYS B 1 114 ? -48.886 -24.279 18.088  1.00 42.51 ?  114 LYS B CA  1 
ATOM   3724 C  C   . LYS B 1 114 ? -48.901 -23.081 17.148  1.00 42.81 ?  114 LYS B C   1 
ATOM   3725 O  O   . LYS B 1 114 ? -49.266 -23.203 15.974  1.00 43.89 ?  114 LYS B O   1 
ATOM   3726 C  CB  . LYS B 1 114 ? -50.174 -24.340 18.911  1.00 50.01 ?  114 LYS B CB  1 
ATOM   3727 C  CG  . LYS B 1 114 ? -50.879 -25.699 18.862  1.00 61.74 ?  114 LYS B CG  1 
ATOM   3728 C  CD  . LYS B 1 114 ? -51.951 -25.824 19.951  1.00 67.12 ?  114 LYS B CD  1 
ATOM   3729 C  CE  . LYS B 1 114 ? -53.012 -26.873 19.606  1.00 71.09 ?  114 LYS B CE  1 
ATOM   3730 N  NZ  . LYS B 1 114 ? -54.183 -26.809 20.539  1.00 68.81 ?  114 LYS B NZ  1 
ATOM   3731 N  N   . THR B 1 115 ? -48.494 -21.914 17.646  1.00 43.27 ?  115 THR B N   1 
ATOM   3732 C  CA  . THR B 1 115 ? -48.495 -20.712 16.821  1.00 41.37 ?  115 THR B CA  1 
ATOM   3733 C  C   . THR B 1 115 ? -47.448 -20.810 15.716  1.00 43.14 ?  115 THR B C   1 
ATOM   3734 O  O   . THR B 1 115 ? -47.676 -20.355 14.587  1.00 38.92 ?  115 THR B O   1 
ATOM   3735 C  CB  . THR B 1 115 ? -48.255 -19.488 17.713  1.00 39.99 ?  115 THR B CB  1 
ATOM   3736 O  OG1 . THR B 1 115 ? -49.428 -19.235 18.496  1.00 40.24 ?  115 THR B OG1 1 
ATOM   3737 C  CG2 . THR B 1 115 ? -47.939 -18.266 16.896  1.00 31.22 ?  115 THR B CG2 1 
ATOM   3738 N  N   . LEU B 1 116 ? -46.307 -21.427 16.014  1.00 39.56 ?  116 LEU B N   1 
ATOM   3739 C  CA  . LEU B 1 116 ? -45.241 -21.592 15.032  1.00 43.95 ?  116 LEU B CA  1 
ATOM   3740 C  C   . LEU B 1 116 ? -45.454 -22.826 14.160  1.00 46.16 ?  116 LEU B C   1 
ATOM   3741 O  O   . LEU B 1 116 ? -44.488 -23.425 13.680  1.00 54.84 ?  116 LEU B O   1 
ATOM   3742 C  CB  . LEU B 1 116 ? -43.891 -21.680 15.742  1.00 35.82 ?  116 LEU B CB  1 
ATOM   3743 C  CG  . LEU B 1 116 ? -43.538 -20.477 16.623  1.00 31.53 ?  116 LEU B CG  1 
ATOM   3744 C  CD1 . LEU B 1 116 ? -42.200 -20.684 17.279  1.00 31.78 ?  116 LEU B CD1 1 
ATOM   3745 C  CD2 . LEU B 1 116 ? -43.524 -19.212 15.797  1.00 30.60 ?  116 LEU B CD2 1 
ATOM   3746 N  N   . SER B 1 117 ? -46.699 -23.226 13.951  1.00 49.31 ?  117 SER B N   1 
ATOM   3747 C  CA  . SER B 1 117 ? -47.010 -24.373 13.099  1.00 53.37 ?  117 SER B CA  1 
ATOM   3748 C  C   . SER B 1 117 ? -47.744 -23.899 11.855  1.00 54.29 ?  117 SER B C   1 
ATOM   3749 O  O   . SER B 1 117 ? -48.915 -23.485 11.957  1.00 54.56 ?  117 SER B O   1 
ATOM   3750 C  CB  . SER B 1 117 ? -47.858 -25.393 13.855  1.00 49.66 ?  117 SER B CB  1 
ATOM   3751 O  OG  . SER B 1 117 ? -47.297 -25.656 15.125  1.00 50.93 ?  117 SER B OG  1 
ATOM   3752 N  N   . PRO B 1 118 ? -47.117 -23.932 10.662  1.00 54.27 ?  118 PRO B N   1 
ATOM   3753 C  CA  . PRO B 1 118 ? -47.868 -23.658 9.426   1.00 51.78 ?  118 PRO B CA  1 
ATOM   3754 C  C   . PRO B 1 118 ? -49.094 -24.553 9.304   1.00 56.02 ?  118 PRO B C   1 
ATOM   3755 O  O   . PRO B 1 118 ? -50.066 -24.214 8.618   1.00 56.08 ?  118 PRO B O   1 
ATOM   3756 C  CB  . PRO B 1 118 ? -46.844 -23.954 8.319   1.00 47.98 ?  118 PRO B CB  1 
ATOM   3757 C  CG  . PRO B 1 118 ? -45.515 -23.741 8.971   1.00 44.41 ?  118 PRO B CG  1 
ATOM   3758 C  CD  . PRO B 1 118 ? -45.691 -24.197 10.397  1.00 45.34 ?  118 PRO B CD  1 
ATOM   3759 N  N   . GLN B 1 119 ? -49.048 -25.697 9.999   1.00 54.55 ?  119 GLN B N   1 
ATOM   3760 C  CA  . GLN B 1 119 ? -50.103 -26.700 9.936   1.00 57.62 ?  119 GLN B CA  1 
ATOM   3761 C  C   . GLN B 1 119 ? -51.282 -26.368 10.847  1.00 57.09 ?  119 GLN B C   1 
ATOM   3762 O  O   . GLN B 1 119 ? -52.416 -26.761 10.551  1.00 60.51 ?  119 GLN B O   1 
ATOM   3763 C  CB  . GLN B 1 119 ? -49.524 -28.067 10.303  1.00 60.64 ?  119 GLN B CB  1 
ATOM   3764 C  CG  . GLN B 1 119 ? -48.852 -28.792 9.150   1.00 65.74 ?  119 GLN B CG  1 
ATOM   3765 C  CD  . GLN B 1 119 ? -47.414 -28.335 8.933   1.00 68.08 ?  119 GLN B CD  1 
ATOM   3766 O  OE1 . GLN B 1 119 ? -46.670 -28.108 9.890   1.00 66.76 ?  119 GLN B OE1 1 
ATOM   3767 N  NE2 . GLN B 1 119 ? -47.012 -28.219 7.668   1.00 67.34 ?  119 GLN B NE2 1 
ATOM   3768 N  N   . ALA B 1 120 ? -51.041 -25.666 11.958  1.00 55.48 ?  120 ALA B N   1 
ATOM   3769 C  CA  . ALA B 1 120 ? -52.125 -25.252 12.842  1.00 54.32 ?  120 ALA B CA  1 
ATOM   3770 C  C   . ALA B 1 120 ? -52.940 -24.086 12.289  1.00 53.67 ?  120 ALA B C   1 
ATOM   3771 O  O   . ALA B 1 120 ? -53.989 -23.761 12.856  1.00 55.92 ?  120 ALA B O   1 
ATOM   3772 C  CB  . ALA B 1 120 ? -51.570 -24.879 14.216  1.00 46.54 ?  120 ALA B CB  1 
ATOM   3773 N  N   . ASP B 1 121 ? -52.488 -23.448 11.210  1.00 54.07 ?  121 ASP B N   1 
ATOM   3774 C  CA  . ASP B 1 121 ? -53.213 -22.369 10.537  1.00 46.72 ?  121 ASP B CA  1 
ATOM   3775 C  C   . ASP B 1 121 ? -53.506 -22.849 9.120   1.00 47.06 ?  121 ASP B C   1 
ATOM   3776 O  O   . ASP B 1 121 ? -52.837 -22.463 8.158   1.00 44.21 ?  121 ASP B O   1 
ATOM   3777 C  CB  . ASP B 1 121 ? -52.393 -21.052 10.556  1.00 42.87 ?  121 ASP B CB  1 
ATOM   3778 C  CG  . ASP B 1 121 ? -53.166 -19.855 10.001  1.00 41.18 ?  121 ASP B CG  1 
ATOM   3779 O  OD1 . ASP B 1 121 ? -54.193 -20.041 9.310   1.00 40.60 ?  121 ASP B OD1 1 
ATOM   3780 O  OD2 . ASP B 1 121 ? -52.728 -18.712 10.245  1.00 44.58 ?  121 ASP B OD2 1 
ATOM   3781 N  N   . ARG B 1 122 ? -54.528 -23.696 8.996   1.00 51.60 ?  122 ARG B N   1 
ATOM   3782 C  CA  . ARG B 1 122 ? -54.839 -24.336 7.722   1.00 51.93 ?  122 ARG B CA  1 
ATOM   3783 C  C   . ARG B 1 122 ? -55.052 -23.321 6.600   1.00 50.01 ?  122 ARG B C   1 
ATOM   3784 O  O   . ARG B 1 122 ? -54.881 -23.664 5.425   1.00 45.67 ?  122 ARG B O   1 
ATOM   3785 C  CB  . ARG B 1 122 ? -56.066 -25.240 7.917   1.00 62.12 ?  122 ARG B CB  1 
ATOM   3786 N  N   . GLU B 1 123 ? -55.376 -22.069 6.933   1.00 45.70 ?  123 GLU B N   1 
ATOM   3787 C  CA  . GLU B 1 123 ? -55.535 -21.023 5.929   1.00 46.51 ?  123 GLU B CA  1 
ATOM   3788 C  C   . GLU B 1 123 ? -54.253 -20.243 5.645   1.00 36.03 ?  123 GLU B C   1 
ATOM   3789 O  O   . GLU B 1 123 ? -54.241 -19.431 4.715   1.00 31.67 ?  123 GLU B O   1 
ATOM   3790 C  CB  . GLU B 1 123 ? -56.619 -20.035 6.366   1.00 43.35 ?  123 GLU B CB  1 
ATOM   3791 C  CG  . GLU B 1 123 ? -58.007 -20.632 6.449   1.00 51.02 ?  123 GLU B CG  1 
ATOM   3792 C  CD  . GLU B 1 123 ? -58.451 -21.223 5.132   1.00 58.51 ?  123 GLU B CD  1 
ATOM   3793 O  OE1 . GLU B 1 123 ? -58.173 -20.610 4.076   1.00 61.69 ?  123 GLU B OE1 1 
ATOM   3794 O  OE2 . GLU B 1 123 ? -59.067 -22.313 5.159   1.00 64.51 ?  123 GLU B OE2 1 
ATOM   3795 N  N   . LEU B 1 124 ? -53.188 -20.459 6.417   1.00 39.04 ?  124 LEU B N   1 
ATOM   3796 C  CA  . LEU B 1 124 ? -52.025 -19.578 6.344   1.00 34.77 ?  124 LEU B CA  1 
ATOM   3797 C  C   . LEU B 1 124 ? -51.453 -19.531 4.934   1.00 31.87 ?  124 LEU B C   1 
ATOM   3798 O  O   . LEU B 1 124 ? -51.193 -18.447 4.399   1.00 32.65 ?  124 LEU B O   1 
ATOM   3799 C  CB  . LEU B 1 124 ? -50.961 -20.029 7.342   1.00 37.60 ?  124 LEU B CB  1 
ATOM   3800 C  CG  . LEU B 1 124 ? -49.603 -19.347 7.209   1.00 34.33 ?  124 LEU B CG  1 
ATOM   3801 C  CD1 . LEU B 1 124 ? -49.692 -17.916 7.722   1.00 31.64 ?  124 LEU B CD1 1 
ATOM   3802 C  CD2 . LEU B 1 124 ? -48.544 -20.148 7.955   1.00 36.55 ?  124 LEU B CD2 1 
ATOM   3803 N  N   . GLY B 1 125 ? -51.280 -20.698 4.304   1.00 32.54 ?  125 GLY B N   1 
ATOM   3804 C  CA  . GLY B 1 125 ? -50.664 -20.737 2.984   1.00 27.70 ?  125 GLY B CA  1 
ATOM   3805 C  C   . GLY B 1 125 ? -51.405 -19.898 1.958   1.00 33.49 ?  125 GLY B C   1 
ATOM   3806 O  O   . GLY B 1 125 ? -50.809 -19.077 1.254   1.00 32.64 ?  125 GLY B O   1 
ATOM   3807 N  N   . GLY B 1 126 ? -52.720 -20.096 1.853   1.00 29.50 ?  126 GLY B N   1 
ATOM   3808 C  CA  . GLY B 1 126 ? -53.496 -19.299 0.922   1.00 27.77 ?  126 GLY B CA  1 
ATOM   3809 C  C   . GLY B 1 126 ? -53.495 -17.827 1.280   1.00 30.70 ?  126 GLY B C   1 
ATOM   3810 O  O   . GLY B 1 126 ? -53.564 -16.966 0.399   1.00 32.89 ?  126 GLY B O   1 
ATOM   3811 N  N   . TRP B 1 127 ? -53.399 -17.514 2.573   1.00 28.56 ?  127 TRP B N   1 
ATOM   3812 C  CA  . TRP B 1 127 ? -53.411 -16.118 2.995   1.00 31.05 ?  127 TRP B CA  1 
ATOM   3813 C  C   . TRP B 1 127 ? -52.093 -15.425 2.654   1.00 29.20 ?  127 TRP B C   1 
ATOM   3814 O  O   . TRP B 1 127 ? -52.091 -14.294 2.149   1.00 29.37 ?  127 TRP B O   1 
ATOM   3815 C  CB  . TRP B 1 127 ? -53.697 -16.038 4.493   1.00 30.99 ?  127 TRP B CB  1 
ATOM   3816 C  CG  . TRP B 1 127 ? -53.735 -14.637 4.998   1.00 32.18 ?  127 TRP B CG  1 
ATOM   3817 C  CD1 . TRP B 1 127 ? -54.802 -13.781 4.974   1.00 33.05 ?  127 TRP B CD1 1 
ATOM   3818 C  CD2 . TRP B 1 127 ? -52.650 -13.912 5.577   1.00 31.38 ?  127 TRP B CD2 1 
ATOM   3819 N  NE1 . TRP B 1 127 ? -54.445 -12.568 5.518   1.00 35.45 ?  127 TRP B NE1 1 
ATOM   3820 C  CE2 . TRP B 1 127 ? -53.130 -12.625 5.897   1.00 29.95 ?  127 TRP B CE2 1 
ATOM   3821 C  CE3 . TRP B 1 127 ? -51.317 -14.229 5.864   1.00 32.19 ?  127 TRP B CE3 1 
ATOM   3822 C  CZ2 . TRP B 1 127 ? -52.328 -11.661 6.493   1.00 34.15 ?  127 TRP B CZ2 1 
ATOM   3823 C  CZ3 . TRP B 1 127 ? -50.522 -13.270 6.455   1.00 33.37 ?  127 TRP B CZ3 1 
ATOM   3824 C  CH2 . TRP B 1 127 ? -51.027 -11.999 6.761   1.00 33.18 ?  127 TRP B CH2 1 
ATOM   3825 N  N   . LEU B 1 128 ? -50.964 -16.088 2.928   1.00 25.26 ?  128 LEU B N   1 
ATOM   3826 C  CA  . LEU B 1 128 ? -49.667 -15.536 2.541   1.00 23.60 ?  128 LEU B CA  1 
ATOM   3827 C  C   . LEU B 1 128 ? -49.592 -15.335 1.034   1.00 23.99 ?  128 LEU B C   1 
ATOM   3828 O  O   . LEU B 1 128 ? -49.099 -14.302 0.560   1.00 23.22 ?  128 LEU B O   1 
ATOM   3829 C  CB  . LEU B 1 128 ? -48.546 -16.459 3.015   1.00 24.78 ?  128 LEU B CB  1 
ATOM   3830 C  CG  . LEU B 1 128 ? -48.177 -16.451 4.506   1.00 27.59 ?  128 LEU B CG  1 
ATOM   3831 C  CD1 . LEU B 1 128 ? -47.132 -17.520 4.856   1.00 22.31 ?  128 LEU B CD1 1 
ATOM   3832 C  CD2 . LEU B 1 128 ? -47.694 -15.081 4.948   1.00 27.28 ?  128 LEU B CD2 1 
ATOM   3833 N  N   . GLU B 1 129 ? -50.109 -16.305 0.269   1.00 24.20 ?  129 GLU B N   1 
ATOM   3834 C  CA  . GLU B 1 129 ? -50.179 -16.192 -1.185  1.00 26.60 ?  129 GLU B CA  1 
ATOM   3835 C  C   . GLU B 1 129 ? -50.913 -14.929 -1.615  1.00 28.24 ?  129 GLU B C   1 
ATOM   3836 O  O   . GLU B 1 129 ? -50.462 -14.211 -2.516  1.00 24.53 ?  129 GLU B O   1 
ATOM   3837 C  CB  . GLU B 1 129 ? -50.869 -17.433 -1.771  1.00 28.58 ?  129 GLU B CB  1 
ATOM   3838 C  CG  . GLU B 1 129 ? -50.819 -17.494 -3.290  1.00 45.33 ?  129 GLU B CG  1 
ATOM   3839 C  CD  . GLU B 1 129 ? -51.432 -18.759 -3.890  1.00 46.06 ?  129 GLU B CD  1 
ATOM   3840 O  OE1 . GLU B 1 129 ? -51.423 -18.883 -5.128  1.00 49.71 ?  129 GLU B OE1 1 
ATOM   3841 O  OE2 . GLU B 1 129 ? -51.909 -19.624 -3.139  1.00 52.44 ?  129 GLU B OE2 1 
ATOM   3842 N  N   . ALA B 1 130 ? -52.078 -14.671 -1.012  1.00 26.32 ?  130 ALA B N   1 
ATOM   3843 C  CA  . ALA B 1 130 ? -52.826 -13.459 -1.330  1.00 30.76 ?  130 ALA B CA  1 
ATOM   3844 C  C   . ALA B 1 130 ? -52.058 -12.211 -0.910  1.00 25.48 ?  130 ALA B C   1 
ATOM   3845 O  O   . ALA B 1 130 ? -52.063 -11.203 -1.627  1.00 28.85 ?  130 ALA B O   1 
ATOM   3846 C  CB  . ALA B 1 130 ? -54.204 -13.497 -0.654  1.00 27.06 ?  130 ALA B CB  1 
ATOM   3847 N  N   . GLN B 1 131 ? -51.395 -12.252 0.253   1.00 25.11 ?  131 GLN B N   1 
ATOM   3848 C  CA  . GLN B 1 131 ? -50.569 -11.115 0.664   1.00 26.09 ?  131 GLN B CA  1 
ATOM   3849 C  C   . GLN B 1 131 ? -49.472 -10.841 -0.364  1.00 27.70 ?  131 GLN B C   1 
ATOM   3850 O  O   . GLN B 1 131 ? -49.299 -9.704  -0.823  1.00 27.25 ?  131 GLN B O   1 
ATOM   3851 C  CB  . GLN B 1 131 ? -49.955 -11.369 2.042   1.00 27.51 ?  131 GLN B CB  1 
ATOM   3852 C  CG  . GLN B 1 131 ? -50.960 -11.373 3.179   1.00 32.64 ?  131 GLN B CG  1 
ATOM   3853 C  CD  . GLN B 1 131 ? -51.555 -10.006 3.407   1.00 34.95 ?  131 GLN B CD  1 
ATOM   3854 O  OE1 . GLN B 1 131 ? -50.866 -8.990  3.298   1.00 36.15 ?  131 GLN B OE1 1 
ATOM   3855 N  NE2 . GLN B 1 131 ? -52.846 -9.967  3.691   1.00 38.58 ?  131 GLN B NE2 1 
ATOM   3856 N  N   . ALA B 1 132 ? -48.728 -11.886 -0.742  1.00 24.08 ?  132 ALA B N   1 
ATOM   3857 C  CA  . ALA B 1 132 ? -47.697 -11.766 -1.770  1.00 22.52 ?  132 ALA B CA  1 
ATOM   3858 C  C   . ALA B 1 132 ? -48.245 -11.151 -3.049  1.00 24.05 ?  132 ALA B C   1 
ATOM   3859 O  O   . ALA B 1 132 ? -47.657 -10.215 -3.605  1.00 22.12 ?  132 ALA B O   1 
ATOM   3860 C  CB  . ALA B 1 132 ? -47.099 -13.142 -2.071  1.00 22.51 ?  132 ALA B CB  1 
ATOM   3861 N  N   . HIS B 1 133 ? -49.369 -11.684 -3.542  1.00 26.24 ?  133 HIS B N   1 
ATOM   3862 C  CA  . HIS B 1 133 ? -49.892 -11.237 -4.829  1.00 24.61 ?  133 HIS B CA  1 
ATOM   3863 C  C   . HIS B 1 133 ? -50.435 -9.819  -4.755  1.00 23.96 ?  133 HIS B C   1 
ATOM   3864 O  O   . HIS B 1 133 ? -50.320 -9.055  -5.724  1.00 27.32 ?  133 HIS B O   1 
ATOM   3865 C  CB  . HIS B 1 133 ? -50.988 -12.187 -5.317  1.00 30.46 ?  133 HIS B CB  1 
ATOM   3866 C  CG  . HIS B 1 133 ? -50.453 -13.436 -5.943  1.00 33.83 ?  133 HIS B CG  1 
ATOM   3867 N  ND1 . HIS B 1 133 ? -50.102 -13.508 -7.273  1.00 37.10 ?  133 HIS B ND1 1 
ATOM   3868 C  CD2 . HIS B 1 133 ? -50.193 -14.655 -5.418  1.00 32.50 ?  133 HIS B CD2 1 
ATOM   3869 C  CE1 . HIS B 1 133 ? -49.649 -14.721 -7.540  1.00 39.56 ?  133 HIS B CE1 1 
ATOM   3870 N  NE2 . HIS B 1 133 ? -49.693 -15.435 -6.430  1.00 33.94 ?  133 HIS B NE2 1 
ATOM   3871 N  N   . GLN B 1 134 ? -51.077 -9.458  -3.643  1.00 23.86 ?  134 GLN B N   1 
ATOM   3872 C  CA  . GLN B 1 134 ? -51.550 -8.084  -3.526  1.00 26.77 ?  134 GLN B CA  1 
ATOM   3873 C  C   . GLN B 1 134 ? -50.388 -7.101  -3.585  1.00 21.61 ?  134 GLN B C   1 
ATOM   3874 O  O   . GLN B 1 134 ? -50.467 -6.079  -4.275  1.00 22.85 ?  134 GLN B O   1 
ATOM   3875 C  CB  . GLN B 1 134 ? -52.349 -7.904  -2.241  1.00 29.36 ?  134 GLN B CB  1 
ATOM   3876 C  CG  . GLN B 1 134 ? -52.915 -6.515  -2.087  1.00 40.98 ?  134 GLN B CG  1 
ATOM   3877 C  CD  . GLN B 1 134 ? -53.953 -6.448  -0.995  1.00 52.92 ?  134 GLN B CD  1 
ATOM   3878 O  OE1 . GLN B 1 134 ? -54.020 -7.334  -0.136  1.00 51.52 ?  134 GLN B OE1 1 
ATOM   3879 N  NE2 . GLN B 1 134 ? -54.786 -5.404  -1.025  1.00 52.72 ?  134 GLN B NE2 1 
ATOM   3880 N  N   . LEU B 1 135 ? -49.290 -7.405  -2.885  1.00 24.92 ?  135 LEU B N   1 
ATOM   3881 C  CA  . LEU B 1 135 ? -48.144 -6.498  -2.895  1.00 25.40 ?  135 LEU B CA  1 
ATOM   3882 C  C   . LEU B 1 135 ? -47.537 -6.389  -4.290  1.00 23.82 ?  135 LEU B C   1 
ATOM   3883 O  O   . LEU B 1 135 ? -47.214 -5.286  -4.744  1.00 26.20 ?  135 LEU B O   1 
ATOM   3884 C  CB  . LEU B 1 135 ? -47.093 -6.958  -1.884  1.00 25.18 ?  135 LEU B CB  1 
ATOM   3885 C  CG  . LEU B 1 135 ? -47.512 -6.841  -0.413  1.00 26.86 ?  135 LEU B CG  1 
ATOM   3886 C  CD1 . LEU B 1 135 ? -46.606 -7.697  0.477   1.00 22.09 ?  135 LEU B CD1 1 
ATOM   3887 C  CD2 . LEU B 1 135 ? -47.521 -5.376  0.057   1.00 23.95 ?  135 LEU B CD2 1 
ATOM   3888 N  N   . LEU B 1 136 ? -47.410 -7.515  -5.005  1.00 22.96 ?  136 LEU B N   1 
ATOM   3889 C  CA  . LEU B 1 136 ? -46.770 -7.476  -6.321  1.00 23.52 ?  136 LEU B CA  1 
ATOM   3890 C  C   . LEU B 1 136 ? -47.669 -6.814  -7.366  1.00 25.86 ?  136 LEU B C   1 
ATOM   3891 O  O   . LEU B 1 136 ? -47.171 -6.099  -8.245  1.00 24.70 ?  136 LEU B O   1 
ATOM   3892 C  CB  . LEU B 1 136 ? -46.357 -8.889  -6.748  1.00 23.62 ?  136 LEU B CB  1 
ATOM   3893 C  CG  . LEU B 1 136 ? -45.213 -9.497  -5.915  1.00 22.93 ?  136 LEU B CG  1 
ATOM   3894 C  CD1 . LEU B 1 136 ? -45.222 -11.016 -6.009  1.00 24.47 ?  136 LEU B CD1 1 
ATOM   3895 C  CD2 . LEU B 1 136 ? -43.854 -8.960  -6.334  1.00 22.46 ?  136 LEU B CD2 1 
ATOM   3896 N  N   . ASP B 1 137 ? -48.997 -7.007  -7.269  1.00 22.11 ?  137 ASP B N   1 
ATOM   3897 C  CA  . ASP B 1 137 ? -49.920 -6.321  -8.178  1.00 23.49 ?  137 ASP B CA  1 
ATOM   3898 C  C   . ASP B 1 137 ? -49.777 -4.810  -8.071  1.00 25.16 ?  137 ASP B C   1 
ATOM   3899 O  O   . ASP B 1 137 ? -49.884 -4.093  -9.072  1.00 25.81 ?  137 ASP B O   1 
ATOM   3900 C  CB  . ASP B 1 137 ? -51.370 -6.714  -7.874  1.00 26.52 ?  137 ASP B CB  1 
ATOM   3901 C  CG  . ASP B 1 137 ? -51.704 -8.128  -8.313  1.00 28.21 ?  137 ASP B CG  1 
ATOM   3902 O  OD1 . ASP B 1 137 ? -51.015 -8.627  -9.210  1.00 30.76 ?  137 ASP B OD1 1 
ATOM   3903 O  OD2 . ASP B 1 137 ? -52.649 -8.733  -7.756  1.00 29.37 ?  137 ASP B OD2 1 
ATOM   3904 N  N   . ARG B 1 138 ? -49.560 -4.306  -6.856  1.00 26.25 ?  138 ARG B N   1 
ATOM   3905 C  CA  . ARG B 1 138 ? -49.380 -2.869  -6.659  1.00 29.60 ?  138 ARG B CA  1 
ATOM   3906 C  C   . ARG B 1 138 ? -48.116 -2.380  -7.358  1.00 27.68 ?  138 ARG B C   1 
ATOM   3907 O  O   . ARG B 1 138 ? -48.140 -1.385  -8.094  1.00 30.92 ?  138 ARG B O   1 
ATOM   3908 C  CB  . ARG B 1 138 ? -49.330 -2.569  -5.160  1.00 31.13 ?  138 ARG B CB  1 
ATOM   3909 C  CG  . ARG B 1 138 ? -49.342 -1.097  -4.780  1.00 41.71 ?  138 ARG B CG  1 
ATOM   3910 C  CD  . ARG B 1 138 ? -49.841 -0.910  -3.336  1.00 46.00 ?  138 ARG B CD  1 
ATOM   3911 N  NE  . ARG B 1 138 ? -50.054 -2.183  -2.648  1.00 47.33 ?  138 ARG B NE  1 
ATOM   3912 C  CZ  . ARG B 1 138 ? -51.123 -2.483  -1.917  1.00 57.09 ?  138 ARG B CZ  1 
ATOM   3913 N  NH1 . ARG B 1 138 ? -52.109 -1.614  -1.739  1.00 60.86 ?  138 ARG B NH1 1 
ATOM   3914 N  NH2 . ARG B 1 138 ? -51.204 -3.683  -1.344  1.00 53.54 ?  138 ARG B NH2 1 
ATOM   3915 N  N   . LEU B 1 139 ? -46.996 -3.077  -7.140  1.00 24.86 ?  139 LEU B N   1 
ATOM   3916 C  CA  . LEU B 1 139 ? -45.760 -2.732  -7.838  1.00 23.96 ?  139 LEU B CA  1 
ATOM   3917 C  C   . LEU B 1 139 ? -45.947 -2.791  -9.345  1.00 22.39 ?  139 LEU B C   1 
ATOM   3918 O  O   . LEU B 1 139 ? -45.446 -1.927  -10.074 1.00 22.31 ?  139 LEU B O   1 
ATOM   3919 C  CB  . LEU B 1 139 ? -44.638 -3.677  -7.404  1.00 24.53 ?  139 LEU B CB  1 
ATOM   3920 C  CG  . LEU B 1 139 ? -44.333 -3.612  -5.905  1.00 28.21 ?  139 LEU B CG  1 
ATOM   3921 C  CD1 . LEU B 1 139 ? -43.341 -4.683  -5.495  1.00 29.01 ?  139 LEU B CD1 1 
ATOM   3922 C  CD2 . LEU B 1 139 ? -43.814 -2.218  -5.553  1.00 27.35 ?  139 LEU B CD2 1 
ATOM   3923 N  N   . ILE B 1 140 ? -46.672 -3.802  -9.832  1.00 22.52 ?  140 ILE B N   1 
ATOM   3924 C  CA  . ILE B 1 140 ? -46.894 -3.915  -11.272 1.00 26.33 ?  140 ILE B CA  1 
ATOM   3925 C  C   . ILE B 1 140 ? -47.696 -2.719  -11.777 1.00 23.82 ?  140 ILE B C   1 
ATOM   3926 O  O   . ILE B 1 140 ? -47.382 -2.154  -12.830 1.00 19.98 ?  140 ILE B O   1 
ATOM   3927 C  CB  . ILE B 1 140 ? -47.574 -5.258  -11.622 1.00 24.41 ?  140 ILE B CB  1 
ATOM   3928 C  CG1 . ILE B 1 140 ? -46.614 -6.443  -11.427 1.00 24.19 ?  140 ILE B CG1 1 
ATOM   3929 C  CG2 . ILE B 1 140 ? -48.086 -5.260  -13.066 1.00 29.92 ?  140 ILE B CG2 1 
ATOM   3930 C  CD1 . ILE B 1 140 ? -47.316 -7.821  -11.383 1.00 21.87 ?  140 ILE B CD1 1 
ATOM   3931 N  N   . GLU B 1 141 ? -48.733 -2.308  -11.026 1.00 28.97 ?  141 GLU B N   1 
ATOM   3932 C  CA  . GLU B 1 141 ? -49.522 -1.123  -11.383 1.00 29.01 ?  141 GLU B CA  1 
ATOM   3933 C  C   . GLU B 1 141 ? -48.624 0.088   -11.614 1.00 25.55 ?  141 GLU B C   1 
ATOM   3934 O  O   . GLU B 1 141 ? -48.737 0.788   -12.626 1.00 25.59 ?  141 GLU B O   1 
ATOM   3935 C  CB  . GLU B 1 141 ? -50.525 -0.782  -10.268 1.00 32.57 ?  141 GLU B CB  1 
ATOM   3936 C  CG  . GLU B 1 141 ? -51.791 -1.647  -10.131 1.00 43.50 ?  141 GLU B CG  1 
ATOM   3937 C  CD  . GLU B 1 141 ? -52.515 -1.398  -8.786  1.00 47.61 ?  141 GLU B CD  1 
ATOM   3938 O  OE1 . GLU B 1 141 ? -52.566 -0.217  -8.365  1.00 46.21 ?  141 GLU B OE1 1 
ATOM   3939 O  OE2 . GLU B 1 141 ? -53.022 -2.366  -8.153  1.00 43.72 ?  141 GLU B OE2 1 
ATOM   3940 N  N   . GLN B 1 142 ? -47.733 0.365   -10.669 1.00 26.36 ?  142 GLN B N   1 
ATOM   3941 C  CA  . GLN B 1 142 ? -46.855 1.558   -10.749 1.00 26.44 ?  142 GLN B CA  1 
ATOM   3942 C  C   . GLN B 1 142 ? -45.795 1.383   -11.842 1.00 25.27 ?  142 GLN B C   1 
ATOM   3943 O  O   . GLN B 1 142 ? -45.365 2.394   -12.404 1.00 26.49 ?  142 GLN B O   1 
ATOM   3944 C  CB  . GLN B 1 142 ? -46.253 1.767   -9.360  1.00 27.81 ?  142 GLN B CB  1 
ATOM   3945 C  CG  . GLN B 1 142 ? -47.290 2.179   -8.322  1.00 38.37 ?  142 GLN B CG  1 
ATOM   3946 C  CD  . GLN B 1 142 ? -46.825 2.063   -6.887  1.00 43.33 ?  142 GLN B CD  1 
ATOM   3947 O  OE1 . GLN B 1 142 ? -45.647 1.831   -6.603  1.00 39.13 ?  142 GLN B OE1 1 
ATOM   3948 N  NE2 . GLN B 1 142 ? -47.758 2.230   -5.962  1.00 44.09 ?  142 GLN B NE2 1 
ATOM   3949 N  N   . GLY B 1 143 ? -45.395 0.145   -12.129 1.00 26.92 ?  143 GLY B N   1 
ATOM   3950 C  CA  . GLY B 1 143 ? -44.341 -0.071  -13.099 1.00 22.26 ?  143 GLY B CA  1 
ATOM   3951 C  C   . GLY B 1 143 ? -42.949 0.011   -12.488 1.00 25.75 ?  143 GLY B C   1 
ATOM   3952 O  O   . GLY B 1 143 ? -42.754 0.567   -11.401 1.00 23.82 ?  143 GLY B O   1 
ATOM   3953 N  N   . PRO B 1 144 ? -41.952 -0.535  -13.190 1.00 25.32 ?  144 PRO B N   1 
ATOM   3954 C  CA  . PRO B 1 144 ? -40.584 -0.587  -12.655 1.00 22.51 ?  144 PRO B CA  1 
ATOM   3955 C  C   . PRO B 1 144 ? -39.865 0.743   -12.823 1.00 24.23 ?  144 PRO B C   1 
ATOM   3956 O  O   . PRO B 1 144 ? -40.245 1.568   -13.671 1.00 20.20 ?  144 PRO B O   1 
ATOM   3957 C  CB  . PRO B 1 144 ? -39.923 -1.686  -13.510 1.00 21.30 ?  144 PRO B CB  1 
ATOM   3958 C  CG  . PRO B 1 144 ? -40.613 -1.520  -14.863 1.00 22.83 ?  144 PRO B CG  1 
ATOM   3959 C  CD  . PRO B 1 144 ? -42.052 -1.174  -14.522 1.00 22.70 ?  144 PRO B CD  1 
ATOM   3960 N  N   . PRO B 1 145 ? -38.791 0.986   -12.046 1.00 23.83 ?  145 PRO B N   1 
ATOM   3961 C  CA  . PRO B 1 145 ? -38.262 0.091   -11.008 1.00 21.76 ?  145 PRO B CA  1 
ATOM   3962 C  C   . PRO B 1 145 ? -39.052 0.172   -9.725  1.00 24.75 ?  145 PRO B C   1 
ATOM   3963 O  O   . PRO B 1 145 ? -39.879 1.087   -9.564  1.00 23.70 ?  145 PRO B O   1 
ATOM   3964 C  CB  . PRO B 1 145 ? -36.848 0.612   -10.778 1.00 19.09 ?  145 PRO B CB  1 
ATOM   3965 C  CG  . PRO B 1 145 ? -36.959 2.080   -11.070 1.00 20.79 ?  145 PRO B CG  1 
ATOM   3966 C  CD  . PRO B 1 145 ? -37.946 2.184   -12.213 1.00 20.56 ?  145 PRO B CD  1 
ATOM   3967 N  N   . ALA B 1 146 ? -38.805 -0.770  -8.818  1.00 18.85 ?  146 ALA B N   1 
ATOM   3968 C  CA  . ALA B 1 146 ? -39.380 -0.685  -7.488  1.00 19.91 ?  146 ALA B CA  1 
ATOM   3969 C  C   . ALA B 1 146 ? -38.374 -1.238  -6.500  1.00 19.75 ?  146 ALA B C   1 
ATOM   3970 O  O   . ALA B 1 146 ? -37.444 -1.950  -6.872  1.00 21.83 ?  146 ALA B O   1 
ATOM   3971 C  CB  . ALA B 1 146 ? -40.709 -1.444  -7.371  1.00 21.50 ?  146 ALA B CB  1 
ATOM   3972 N  N   . ASP B 1 147 ? -38.595 -0.918  -5.228  1.00 18.68 ?  147 ASP B N   1 
ATOM   3973 C  CA  . ASP B 1 147 ? -37.753 -1.364  -4.129  1.00 20.10 ?  147 ASP B CA  1 
ATOM   3974 C  C   . ASP B 1 147 ? -38.438 -2.556  -3.480  1.00 22.09 ?  147 ASP B C   1 
ATOM   3975 O  O   . ASP B 1 147 ? -39.452 -2.387  -2.797  1.00 19.66 ?  147 ASP B O   1 
ATOM   3976 C  CB  . ASP B 1 147 ? -37.558 -0.230  -3.126  1.00 21.62 ?  147 ASP B CB  1 
ATOM   3977 C  CG  . ASP B 1 147 ? -37.010 -0.703  -1.802  1.00 21.65 ?  147 ASP B CG  1 
ATOM   3978 O  OD1 . ASP B 1 147 ? -36.336 -1.750  -1.763  1.00 19.16 ?  147 ASP B OD1 1 
ATOM   3979 O  OD2 . ASP B 1 147 ? -37.232 0.005   -0.801  1.00 27.05 ?  147 ASP B OD2 1 
ATOM   3980 N  N   . LEU B 1 148 ? -37.889 -3.758  -3.682  1.00 20.21 ?  148 LEU B N   1 
ATOM   3981 C  CA  . LEU B 1 148 ? -38.578 -4.946  -3.168  1.00 20.59 ?  148 LEU B CA  1 
ATOM   3982 C  C   . LEU B 1 148 ? -38.457 -5.099  -1.659  1.00 18.46 ?  148 LEU B C   1 
ATOM   3983 O  O   . LEU B 1 148 ? -39.136 -5.955  -1.079  1.00 23.25 ?  148 LEU B O   1 
ATOM   3984 C  CB  . LEU B 1 148 ? -38.057 -6.210  -3.848  1.00 17.37 ?  148 LEU B CB  1 
ATOM   3985 C  CG  . LEU B 1 148 ? -38.452 -6.314  -5.319  1.00 23.43 ?  148 LEU B CG  1 
ATOM   3986 C  CD1 . LEU B 1 148 ? -38.161 -7.709  -5.845  1.00 19.91 ?  148 LEU B CD1 1 
ATOM   3987 C  CD2 . LEU B 1 148 ? -39.924 -5.934  -5.538  1.00 22.07 ?  148 LEU B CD2 1 
ATOM   3988 N  N   . ARG B 1 149 ? -37.619 -4.310  -1.004  1.00 19.59 ?  149 ARG B N   1 
ATOM   3989 C  CA  . ARG B 1 149 ? -37.611 -4.354  0.452   1.00 21.73 ?  149 ARG B CA  1 
ATOM   3990 C  C   . ARG B 1 149 ? -38.844 -3.650  1.010   1.00 24.33 ?  149 ARG B C   1 
ATOM   3991 O  O   . ARG B 1 149 ? -39.703 -4.287  1.632   1.00 21.96 ?  149 ARG B O   1 
ATOM   3992 C  CB  . ARG B 1 149 ? -36.325 -3.730  0.997   1.00 20.48 ?  149 ARG B CB  1 
ATOM   3993 C  CG  . ARG B 1 149 ? -36.263 -3.750  2.506   1.00 20.67 ?  149 ARG B CG  1 
ATOM   3994 C  CD  . ARG B 1 149 ? -34.893 -3.336  3.040   1.00 23.99 ?  149 ARG B CD  1 
ATOM   3995 N  NE  . ARG B 1 149 ? -34.920 -3.348  4.495   1.00 28.82 ?  149 ARG B NE  1 
ATOM   3996 C  CZ  . ARG B 1 149 ? -35.596 -2.467  5.228   1.00 31.05 ?  149 ARG B CZ  1 
ATOM   3997 N  NH1 . ARG B 1 149 ? -36.203 -1.423  4.677   1.00 32.29 ?  149 ARG B NH1 1 
ATOM   3998 N  NH2 . ARG B 1 149 ? -35.665 -2.634  6.544   1.00 31.30 ?  149 ARG B NH2 1 
ATOM   3999 N  N   . ASP B 1 150 ? -38.966 -2.335  0.759   1.00 20.69 ?  150 ASP B N   1 
ATOM   4000 C  CA  . ASP B 1 150 ? -40.117 -1.582  1.261   1.00 22.88 ?  150 ASP B CA  1 
ATOM   4001 C  C   . ASP B 1 150 ? -41.411 -2.009  0.572   1.00 23.57 ?  150 ASP B C   1 
ATOM   4002 O  O   . ASP B 1 150 ? -42.481 -1.985  1.189   1.00 25.06 ?  150 ASP B O   1 
ATOM   4003 C  CB  . ASP B 1 150 ? -39.894 -0.075  1.081   1.00 21.31 ?  150 ASP B CB  1 
ATOM   4004 C  CG  . ASP B 1 150 ? -41.008 0.774   1.714   1.00 23.24 ?  150 ASP B CG  1 
ATOM   4005 O  OD1 . ASP B 1 150 ? -41.181 0.696   2.942   1.00 24.77 ?  150 ASP B OD1 1 
ATOM   4006 O  OD2 . ASP B 1 150 ? -41.705 1.529   0.991   1.00 24.02 ?  150 ASP B OD2 1 
ATOM   4007 N  N   . GLY B 1 151 ? -41.337 -2.417  -0.687  1.00 21.32 ?  151 GLY B N   1 
ATOM   4008 C  CA  . GLY B 1 151 ? -42.547 -2.759  -1.446  1.00 22.61 ?  151 GLY B CA  1 
ATOM   4009 C  C   . GLY B 1 151 ? -42.951 -4.216  -1.347  1.00 24.24 ?  151 GLY B C   1 
ATOM   4010 O  O   . GLY B 1 151 ? -43.989 -4.562  -1.911  1.00 25.30 ?  151 GLY B O   1 
ATOM   4011 N  N   . PHE B 1 152 ? -42.171 -5.038  -0.650  1.00 22.80 ?  152 PHE B N   1 
ATOM   4012 C  CA  . PHE B 1 152 ? -42.515 -6.473  -0.660  1.00 21.72 ?  152 PHE B CA  1 
ATOM   4013 C  C   . PHE B 1 152 ? -42.059 -7.174  0.605   1.00 22.72 ?  152 PHE B C   1 
ATOM   4014 O  O   . PHE B 1 152 ? -42.938 -7.427  1.409   1.00 20.41 ?  152 PHE B O   1 
ATOM   4015 C  CB  . PHE B 1 152 ? -41.935 -7.116  -1.931  1.00 22.90 ?  152 PHE B CB  1 
ATOM   4016 C  CG  . PHE B 1 152 ? -42.342 -8.566  -2.169  1.00 22.54 ?  152 PHE B CG  1 
ATOM   4017 C  CD1 . PHE B 1 152 ? -43.678 -8.927  -2.273  1.00 22.62 ?  152 PHE B CD1 1 
ATOM   4018 C  CD2 . PHE B 1 152 ? -41.386 -9.566  -2.288  1.00 19.55 ?  152 PHE B CD2 1 
ATOM   4019 C  CE1 . PHE B 1 152 ? -44.043 -10.245 -2.493  1.00 25.32 ?  152 PHE B CE1 1 
ATOM   4020 C  CE2 . PHE B 1 152 ? -41.756 -10.882 -2.506  1.00 22.35 ?  152 PHE B CE2 1 
ATOM   4021 C  CZ  . PHE B 1 152 ? -43.084 -11.220 -2.609  1.00 20.95 ?  152 PHE B CZ  1 
ATOM   4022 N  N   . THR B 1 153 ? -40.753 -7.329  0.840   1.00 19.68 ?  153 THR B N   1 
ATOM   4023 C  CA  . THR B 1 153 ? -40.333 -8.261  1.887   1.00 19.13 ?  153 THR B CA  1 
ATOM   4024 C  C   . THR B 1 153 ? -40.747 -7.662  3.230   1.00 23.39 ?  153 THR B C   1 
ATOM   4025 O  O   . THR B 1 153 ? -41.213 -8.392  4.116   1.00 22.87 ?  153 THR B O   1 
ATOM   4026 C  CB  . THR B 1 153 ? -38.827 -8.568  1.879   1.00 17.45 ?  153 THR B CB  1 
ATOM   4027 O  OG1 . THR B 1 153 ? -38.094 -7.418  2.303   1.00 19.52 ?  153 THR B OG1 1 
ATOM   4028 C  CG2 . THR B 1 153 ? -38.342 -9.001  0.475   1.00 15.58 ?  153 THR B CG2 1 
ATOM   4029 N  N   . GLU B 1 154 ? -40.604 -6.345  3.404   1.00 19.47 ?  154 GLU B N   1 
ATOM   4030 C  CA  . GLU B 1 154 ? -40.960 -5.744  4.690   1.00 23.17 ?  154 GLU B CA  1 
ATOM   4031 C  C   . GLU B 1 154 ? -42.445 -5.892  5.004   1.00 21.84 ?  154 GLU B C   1 
ATOM   4032 O  O   . GLU B 1 154 ? -42.776 -6.477  6.049   1.00 21.68 ?  154 GLU B O   1 
ATOM   4033 C  CB  . GLU B 1 154 ? -40.488 -4.285  4.725   1.00 23.82 ?  154 GLU B CB  1 
ATOM   4034 C  CG  . GLU B 1 154 ? -38.983 -4.133  4.948   1.00 22.90 ?  154 GLU B CG  1 
ATOM   4035 C  CD  . GLU B 1 154 ? -38.528 -4.563  6.338   1.00 28.41 ?  154 GLU B CD  1 
ATOM   4036 O  OE1 . GLU B 1 154 ? -38.586 -3.722  7.260   1.00 31.13 ?  154 GLU B OE1 1 
ATOM   4037 O  OE2 . GLU B 1 154 ? -38.047 -5.703  6.511   1.00 24.89 ?  154 GLU B OE2 1 
ATOM   4038 N  N   . PRO B 1 155 ? -43.379 -5.413  4.169   1.00 18.05 ?  155 PRO B N   1 
ATOM   4039 C  CA  . PRO B 1 155 ? -44.803 -5.603  4.500   1.00 19.93 ?  155 PRO B CA  1 
ATOM   4040 C  C   . PRO B 1 155 ? -45.230 -7.058  4.510   1.00 23.69 ?  155 PRO B C   1 
ATOM   4041 O  O   . PRO B 1 155 ? -46.144 -7.423  5.267   1.00 22.80 ?  155 PRO B O   1 
ATOM   4042 C  CB  . PRO B 1 155 ? -45.535 -4.832  3.389   1.00 16.96 ?  155 PRO B CB  1 
ATOM   4043 C  CG  . PRO B 1 155 ? -44.561 -4.841  2.235   1.00 20.94 ?  155 PRO B CG  1 
ATOM   4044 C  CD  . PRO B 1 155 ? -43.211 -4.720  2.874   1.00 16.38 ?  155 PRO B CD  1 
ATOM   4045 N  N   . TYR B 1 156 ? -44.626 -7.896  3.665   1.00 20.35 ?  156 TYR B N   1 
ATOM   4046 C  CA  . TYR B 1 156 ? -45.006 -9.304  3.649   1.00 19.19 ?  156 TYR B CA  1 
ATOM   4047 C  C   . TYR B 1 156 ? -44.628 -9.983  4.958   1.00 19.63 ?  156 TYR B C   1 
ATOM   4048 O  O   . TYR B 1 156 ? -45.437 -10.721 5.538   1.00 22.74 ?  156 TYR B O   1 
ATOM   4049 C  CB  . TYR B 1 156 ? -44.347 -9.991  2.456   1.00 20.16 ?  156 TYR B CB  1 
ATOM   4050 C  CG  . TYR B 1 156 ? -44.558 -11.483 2.321   1.00 21.62 ?  156 TYR B CG  1 
ATOM   4051 C  CD1 . TYR B 1 156 ? -45.758 -12.012 1.828   1.00 24.99 ?  156 TYR B CD1 1 
ATOM   4052 C  CD2 . TYR B 1 156 ? -43.535 -12.363 2.626   1.00 22.36 ?  156 TYR B CD2 1 
ATOM   4053 C  CE1 . TYR B 1 156 ? -45.921 -13.412 1.670   1.00 23.64 ?  156 TYR B CE1 1 
ATOM   4054 C  CE2 . TYR B 1 156 ? -43.686 -13.731 2.472   1.00 24.31 ?  156 TYR B CE2 1 
ATOM   4055 C  CZ  . TYR B 1 156 ? -44.867 -14.253 2.003   1.00 21.33 ?  156 TYR B CZ  1 
ATOM   4056 O  OH  . TYR B 1 156 ? -44.953 -15.626 1.869   1.00 23.53 ?  156 TYR B OH  1 
ATOM   4057 N  N   . SER B 1 157 ? -43.406 -9.733  5.445   1.00 21.29 ?  157 SER B N   1 
ATOM   4058 C  CA  . SER B 1 157 ? -42.968 -10.319 6.709   1.00 21.13 ?  157 SER B CA  1 
ATOM   4059 C  C   . SER B 1 157 ? -43.729 -9.730  7.890   1.00 22.96 ?  157 SER B C   1 
ATOM   4060 O  O   . SER B 1 157 ? -44.022 -10.441 8.862   1.00 21.64 ?  157 SER B O   1 
ATOM   4061 C  CB  . SER B 1 157 ? -41.457 -10.121 6.884   1.00 24.91 ?  157 SER B CB  1 
ATOM   4062 O  OG  . SER B 1 157 ? -40.733 -10.643 5.771   1.00 21.10 ?  157 SER B OG  1 
ATOM   4063 N  N   . ALA B 1 158 ? -44.050 -8.432  7.830   1.00 20.43 ?  158 ALA B N   1 
ATOM   4064 C  CA  . ALA B 1 158 ? -44.819 -7.805  8.905   1.00 22.14 ?  158 ALA B CA  1 
ATOM   4065 C  C   . ALA B 1 158 ? -46.225 -8.375  8.959   1.00 25.27 ?  158 ALA B C   1 
ATOM   4066 O  O   . ALA B 1 158 ? -46.740 -8.683  10.040  1.00 26.95 ?  158 ALA B O   1 
ATOM   4067 C  CB  . ALA B 1 158 ? -44.870 -6.284  8.713   1.00 21.00 ?  158 ALA B CB  1 
ATOM   4068 N  N   . ALA B 1 159 ? -46.862 -8.516  7.797   1.00 23.99 ?  159 ALA B N   1 
ATOM   4069 C  CA  . ALA B 1 159 ? -48.181 -9.134  7.748   1.00 26.04 ?  159 ALA B CA  1 
ATOM   4070 C  C   . ALA B 1 159 ? -48.158 -10.518 8.381   1.00 25.67 ?  159 ALA B C   1 
ATOM   4071 O  O   . ALA B 1 159 ? -49.029 -10.857 9.190   1.00 28.37 ?  159 ALA B O   1 
ATOM   4072 C  CB  . ALA B 1 159 ? -48.674 -9.210  6.302   1.00 25.67 ?  159 ALA B CB  1 
ATOM   4073 N  N   . LEU B 1 160 ? -47.154 -11.329 8.046   1.00 21.56 ?  160 LEU B N   1 
ATOM   4074 C  CA  . LEU B 1 160 ? -47.130 -12.688 8.580   1.00 27.32 ?  160 LEU B CA  1 
ATOM   4075 C  C   . LEU B 1 160 ? -47.071 -12.670 10.098  1.00 28.63 ?  160 LEU B C   1 
ATOM   4076 O  O   . LEU B 1 160 ? -47.815 -13.395 10.767  1.00 23.60 ?  160 LEU B O   1 
ATOM   4077 C  CB  . LEU B 1 160 ? -45.953 -13.489 8.020   1.00 24.62 ?  160 LEU B CB  1 
ATOM   4078 C  CG  . LEU B 1 160 ? -45.634 -14.734 8.858   1.00 30.72 ?  160 LEU B CG  1 
ATOM   4079 C  CD1 . LEU B 1 160 ? -46.806 -15.738 8.820   1.00 30.93 ?  160 LEU B CD1 1 
ATOM   4080 C  CD2 . LEU B 1 160 ? -44.344 -15.414 8.407   1.00 28.34 ?  160 LEU B CD2 1 
ATOM   4081 N  N   . HIS B 1 161 ? -46.177 -11.857 10.660  1.00 23.46 ?  161 HIS B N   1 
ATOM   4082 C  CA  . HIS B 1 161 ? -46.010 -11.867 12.098  1.00 26.03 ?  161 HIS B CA  1 
ATOM   4083 C  C   . HIS B 1 161 ? -47.112 -11.102 12.816  1.00 25.14 ?  161 HIS B C   1 
ATOM   4084 O  O   . HIS B 1 161 ? -47.373 -11.382 13.987  1.00 24.02 ?  161 HIS B O   1 
ATOM   4085 C  CB  . HIS B 1 161 ? -44.612 -11.349 12.436  1.00 27.72 ?  161 HIS B CB  1 
ATOM   4086 C  CG  . HIS B 1 161 ? -43.549 -12.313 12.026  1.00 25.85 ?  161 HIS B CG  1 
ATOM   4087 N  ND1 . HIS B 1 161 ? -43.122 -12.425 10.721  1.00 22.29 ?  161 HIS B ND1 1 
ATOM   4088 C  CD2 . HIS B 1 161 ? -42.922 -13.294 12.715  1.00 24.83 ?  161 HIS B CD2 1 
ATOM   4089 C  CE1 . HIS B 1 161 ? -42.231 -13.395 10.637  1.00 23.35 ?  161 HIS B CE1 1 
ATOM   4090 N  NE2 . HIS B 1 161 ? -42.094 -13.940 11.832  1.00 23.39 ?  161 HIS B NE2 1 
ATOM   4091 N  N   . CYS B 1 162 ? -47.794 -10.180 12.135  1.00 23.56 ?  162 CYS B N   1 
ATOM   4092 C  CA  . CYS B 1 162 ? -49.022 -9.645  12.708  1.00 28.46 ?  162 CYS B CA  1 
ATOM   4093 C  C   . CYS B 1 162 ? -50.075 -10.743 12.835  1.00 28.79 ?  162 CYS B C   1 
ATOM   4094 O  O   . CYS B 1 162 ? -50.773 -10.836 13.852  1.00 28.54 ?  162 CYS B O   1 
ATOM   4095 C  CB  . CYS B 1 162 ? -49.533 -8.481  11.862  1.00 27.00 ?  162 CYS B CB  1 
ATOM   4096 S  SG  . CYS B 1 162 ? -48.605 -6.935  12.082  1.00 28.26 ?  162 CYS B SG  1 
ATOM   4097 N  N   . ARG B 1 163 ? -50.170 -11.616 11.832  1.00 25.00 ?  163 ARG B N   1 
ATOM   4098 C  CA  . ARG B 1 163 ? -51.138 -12.706 11.905  1.00 26.71 ?  163 ARG B CA  1 
ATOM   4099 C  C   . ARG B 1 163 ? -50.733 -13.723 12.962  1.00 27.45 ?  163 ARG B C   1 
ATOM   4100 O  O   . ARG B 1 163 ? -51.584 -14.251 13.683  1.00 30.12 ?  163 ARG B O   1 
ATOM   4101 C  CB  . ARG B 1 163 ? -51.274 -13.370 10.542  1.00 29.12 ?  163 ARG B CB  1 
ATOM   4102 C  CG  . ARG B 1 163 ? -52.291 -14.501 10.492  1.00 34.21 ?  163 ARG B CG  1 
ATOM   4103 C  CD  . ARG B 1 163 ? -52.300 -15.111 9.103   1.00 31.87 ?  163 ARG B CD  1 
ATOM   4104 N  NE  . ARG B 1 163 ? -53.150 -16.287 8.988   1.00 35.38 ?  163 ARG B NE  1 
ATOM   4105 C  CZ  . ARG B 1 163 ? -54.414 -16.262 8.591   1.00 35.68 ?  163 ARG B CZ  1 
ATOM   4106 N  NH1 . ARG B 1 163 ? -55.045 -15.122 8.361   1.00 28.10 ?  163 ARG B NH1 1 
ATOM   4107 N  NH2 . ARG B 1 163 ? -55.060 -17.412 8.414   1.00 39.63 ?  163 ARG B NH2 1 
ATOM   4108 N  N   . LEU B 1 164 ? -49.432 -13.993 13.074  1.00 25.40 ?  164 LEU B N   1 
ATOM   4109 C  CA  . LEU B 1 164 ? -48.924 -14.898 14.097  1.00 25.99 ?  164 LEU B CA  1 
ATOM   4110 C  C   . LEU B 1 164 ? -49.360 -14.463 15.490  1.00 32.17 ?  164 LEU B C   1 
ATOM   4111 O  O   . LEU B 1 164 ? -49.708 -15.299 16.330  1.00 30.51 ?  164 LEU B O   1 
ATOM   4112 C  CB  . LEU B 1 164 ? -47.395 -14.952 14.018  1.00 26.01 ?  164 LEU B CB  1 
ATOM   4113 C  CG  . LEU B 1 164 ? -46.750 -16.330 14.101  1.00 38.68 ?  164 LEU B CG  1 
ATOM   4114 C  CD1 . LEU B 1 164 ? -47.387 -17.263 13.074  1.00 36.43 ?  164 LEU B CD1 1 
ATOM   4115 C  CD2 . LEU B 1 164 ? -45.242 -16.233 13.859  1.00 35.07 ?  164 LEU B CD2 1 
ATOM   4116 N  N   . LEU B 1 165 ? -49.352 -13.154 15.749  1.00 27.87 ?  165 LEU B N   1 
ATOM   4117 C  CA  . LEU B 1 165 ? -49.661 -12.653 17.078  1.00 30.79 ?  165 LEU B CA  1 
ATOM   4118 C  C   . LEU B 1 165 ? -51.156 -12.496 17.285  1.00 30.64 ?  165 LEU B C   1 
ATOM   4119 O  O   . LEU B 1 165 ? -51.626 -12.532 18.429  1.00 32.54 ?  165 LEU B O   1 
ATOM   4120 C  CB  . LEU B 1 165 ? -48.963 -11.313 17.307  1.00 26.71 ?  165 LEU B CB  1 
ATOM   4121 C  CG  . LEU B 1 165 ? -47.458 -11.369 17.540  1.00 27.42 ?  165 LEU B CG  1 
ATOM   4122 C  CD1 . LEU B 1 165 ? -46.941 -10.032 18.075  1.00 30.44 ?  165 LEU B CD1 1 
ATOM   4123 C  CD2 . LEU B 1 165 ? -47.088 -12.485 18.474  1.00 34.03 ?  165 LEU B CD2 1 
ATOM   4124 N  N   . GLY B 1 166 ? -51.905 -12.339 16.199  1.00 30.20 ?  166 GLY B N   1 
ATOM   4125 C  CA  . GLY B 1 166 ? -53.304 -11.984 16.274  1.00 28.47 ?  166 GLY B CA  1 
ATOM   4126 C  C   . GLY B 1 166 ? -53.554 -10.507 16.455  1.00 36.00 ?  166 GLY B C   1 
ATOM   4127 O  O   . GLY B 1 166 ? -54.431 -10.128 17.236  1.00 40.63 ?  166 GLY B O   1 
ATOM   4128 N  N   . ILE B 1 167 ? -52.794 -9.658  15.771  1.00 33.91 ?  167 ILE B N   1 
ATOM   4129 C  CA  . ILE B 1 167 ? -52.973 -8.208  15.832  1.00 30.90 ?  167 ILE B CA  1 
ATOM   4130 C  C   . ILE B 1 167 ? -53.170 -7.721  14.405  1.00 31.19 ?  167 ILE B C   1 
ATOM   4131 O  O   . ILE B 1 167 ? -52.798 -8.415  13.447  1.00 31.16 ?  167 ILE B O   1 
ATOM   4132 C  CB  . ILE B 1 167 ? -51.776 -7.507  16.518  1.00 25.36 ?  167 ILE B CB  1 
ATOM   4133 C  CG1 . ILE B 1 167 ? -50.494 -7.674  15.697  1.00 31.49 ?  167 ILE B CG1 1 
ATOM   4134 C  CG2 . ILE B 1 167 ? -51.567 -8.059  17.915  1.00 30.09 ?  167 ILE B CG2 1 
ATOM   4135 C  CD1 . ILE B 1 167 ? -49.312 -6.886  16.233  1.00 25.87 ?  167 ILE B CD1 1 
ATOM   4136 N  N   . PRO B 1 168 ? -53.786 -6.552  14.217  1.00 29.12 ?  168 PRO B N   1 
ATOM   4137 C  CA  . PRO B 1 168 ? -53.926 -6.008  12.861  1.00 34.33 ?  168 PRO B CA  1 
ATOM   4138 C  C   . PRO B 1 168 ? -52.572 -5.594  12.297  1.00 30.29 ?  168 PRO B C   1 
ATOM   4139 O  O   . PRO B 1 168 ? -51.575 -5.474  13.008  1.00 30.77 ?  168 PRO B O   1 
ATOM   4140 C  CB  . PRO B 1 168 ? -54.859 -4.801  13.037  1.00 32.64 ?  168 PRO B CB  1 
ATOM   4141 C  CG  . PRO B 1 168 ? -55.436 -4.916  14.405  1.00 30.89 ?  168 PRO B CG  1 
ATOM   4142 C  CD  . PRO B 1 168 ? -54.484 -5.736  15.222  1.00 34.60 ?  168 PRO B CD  1 
ATOM   4143 N  N   . THR B 1 169 ? -52.546 -5.375  10.987  1.00 33.87 ?  169 THR B N   1 
ATOM   4144 C  CA  . THR B 1 169 ? -51.337 -4.918  10.317  1.00 32.13 ?  169 THR B CA  1 
ATOM   4145 C  C   . THR B 1 169 ? -51.245 -3.402  10.219  1.00 30.27 ?  169 THR B C   1 
ATOM   4146 O  O   . THR B 1 169 ? -50.284 -2.899  9.629   1.00 32.15 ?  169 THR B O   1 
ATOM   4147 C  CB  . THR B 1 169 ? -51.246 -5.524  8.916   1.00 33.18 ?  169 THR B CB  1 
ATOM   4148 O  OG1 . THR B 1 169 ? -52.328 -5.030  8.110   1.00 30.11 ?  169 THR B OG1 1 
ATOM   4149 C  CG2 . THR B 1 169 ? -51.313 -7.038  8.995   1.00 29.15 ?  169 THR B CG2 1 
ATOM   4150 N  N   . ASP B 1 170 ? -52.204 -2.670  10.806  1.00 33.55 ?  170 ASP B N   1 
ATOM   4151 C  CA  . ASP B 1 170 ? -52.286 -1.215  10.636  1.00 34.50 ?  170 ASP B CA  1 
ATOM   4152 C  C   . ASP B 1 170 ? -50.979 -0.496  10.958  1.00 31.94 ?  170 ASP B C   1 
ATOM   4153 O  O   . ASP B 1 170 ? -50.637 0.498   10.306  1.00 34.92 ?  170 ASP B O   1 
ATOM   4154 C  CB  . ASP B 1 170 ? -53.389 -0.637  11.520  1.00 33.99 ?  170 ASP B CB  1 
ATOM   4155 C  CG  . ASP B 1 170 ? -54.759 -1.190  11.195  1.00 39.44 ?  170 ASP B CG  1 
ATOM   4156 O  OD1 . ASP B 1 170 ? -54.854 -2.174  10.437  1.00 40.71 ?  170 ASP B OD1 1 
ATOM   4157 O  OD2 . ASP B 1 170 ? -55.741 -0.613  11.697  1.00 39.95 ?  170 ASP B OD2 1 
ATOM   4158 N  N   . ASP B 1 171 ? -50.258 -0.948  11.986  1.00 26.39 ?  171 ASP B N   1 
ATOM   4159 C  CA  . ASP B 1 171 ? -49.078 -0.245  12.479  1.00 30.68 ?  171 ASP B CA  1 
ATOM   4160 C  C   . ASP B 1 171 ? -47.775 -0.903  12.038  1.00 26.70 ?  171 ASP B C   1 
ATOM   4161 O  O   . ASP B 1 171 ? -46.754 -0.791  12.730  1.00 24.54 ?  171 ASP B O   1 
ATOM   4162 C  CB  . ASP B 1 171 ? -49.126 -0.148  14.003  1.00 24.32 ?  171 ASP B CB  1 
ATOM   4163 C  CG  . ASP B 1 171 ? -50.429 0.430   14.498  1.00 28.58 ?  171 ASP B CG  1 
ATOM   4164 O  OD1 . ASP B 1 171 ? -50.889 1.408   13.888  1.00 27.52 ?  171 ASP B OD1 1 
ATOM   4165 O  OD2 . ASP B 1 171 ? -50.982 -0.081  15.493  1.00 28.54 ?  171 ASP B OD2 1 
ATOM   4166 N  N   . TRP B 1 172 ? -47.785 -1.587  10.895  1.00 24.48 ?  172 TRP B N   1 
ATOM   4167 C  CA  . TRP B 1 172 ? -46.619 -2.382  10.531  1.00 25.12 ?  172 TRP B CA  1 
ATOM   4168 C  C   . TRP B 1 172 ? -45.393 -1.509  10.310  1.00 22.70 ?  172 TRP B C   1 
ATOM   4169 O  O   . TRP B 1 172 ? -44.277 -1.913  10.653  1.00 23.99 ?  172 TRP B O   1 
ATOM   4170 C  CB  . TRP B 1 172 ? -46.920 -3.240  9.298   1.00 23.04 ?  172 TRP B CB  1 
ATOM   4171 C  CG  . TRP B 1 172 ? -47.064 -2.483  8.027   1.00 22.59 ?  172 TRP B CG  1 
ATOM   4172 C  CD1 . TRP B 1 172 ? -48.209 -1.932  7.520   1.00 21.57 ?  172 TRP B CD1 1 
ATOM   4173 C  CD2 . TRP B 1 172 ? -46.036 -2.231  7.066   1.00 24.73 ?  172 TRP B CD2 1 
ATOM   4174 N  NE1 . TRP B 1 172 ? -47.945 -1.326  6.310   1.00 19.60 ?  172 TRP B NE1 1 
ATOM   4175 C  CE2 . TRP B 1 172 ? -46.623 -1.506  6.003   1.00 23.69 ?  172 TRP B CE2 1 
ATOM   4176 C  CE3 . TRP B 1 172 ? -44.673 -2.545  7.000   1.00 23.59 ?  172 TRP B CE3 1 
ATOM   4177 C  CZ2 . TRP B 1 172 ? -45.894 -1.083  4.895   1.00 22.83 ?  172 TRP B CZ2 1 
ATOM   4178 C  CZ3 . TRP B 1 172 ? -43.952 -2.128  5.893   1.00 23.34 ?  172 TRP B CZ3 1 
ATOM   4179 C  CH2 . TRP B 1 172 ? -44.566 -1.396  4.859   1.00 22.51 ?  172 TRP B CH2 1 
ATOM   4180 N  N   . ARG B 1 173 ? -45.569 -0.309  9.746   1.00 22.46 ?  173 ARG B N   1 
ATOM   4181 C  CA  . ARG B 1 173 ? -44.402 0.549   9.528   1.00 24.00 ?  173 ARG B CA  1 
ATOM   4182 C  C   . ARG B 1 173 ? -43.727 0.885   10.849  1.00 22.87 ?  173 ARG B C   1 
ATOM   4183 O  O   . ARG B 1 173 ? -42.499 0.788   10.972  1.00 24.43 ?  173 ARG B O   1 
ATOM   4184 C  CB  . ARG B 1 173 ? -44.782 1.824   8.773   1.00 20.75 ?  173 ARG B CB  1 
ATOM   4185 C  CG  . ARG B 1 173 ? -45.223 1.573   7.335   1.00 24.12 ?  173 ARG B CG  1 
ATOM   4186 C  CD  . ARG B 1 173 ? -44.915 2.767   6.415   1.00 23.55 ?  173 ARG B CD  1 
ATOM   4187 N  NE  . ARG B 1 173 ? -45.116 2.412   5.013   1.00 27.25 ?  173 ARG B NE  1 
ATOM   4188 C  CZ  . ARG B 1 173 ? -44.145 2.050   4.186   1.00 27.94 ?  173 ARG B CZ  1 
ATOM   4189 N  NH1 . ARG B 1 173 ? -42.883 2.027   4.573   1.00 26.57 ?  173 ARG B NH1 1 
ATOM   4190 N  NH2 . ARG B 1 173 ? -44.450 1.691   2.942   1.00 30.13 ?  173 ARG B NH2 1 
ATOM   4191 N  N   . ARG B 1 174 ? -44.523 1.241   11.864  1.00 23.36 ?  174 ARG B N   1 
ATOM   4192 C  CA  . ARG B 1 174 ? -43.968 1.532   13.186  1.00 22.86 ?  174 ARG B CA  1 
ATOM   4193 C  C   . ARG B 1 174 ? -43.276 0.309   13.787  1.00 23.69 ?  174 ARG B C   1 
ATOM   4194 O  O   . ARG B 1 174 ? -42.195 0.424   14.377  1.00 24.12 ?  174 ARG B O   1 
ATOM   4195 C  CB  . ARG B 1 174 ? -45.078 2.042   14.116  1.00 22.54 ?  174 ARG B CB  1 
ATOM   4196 N  N   . LEU B 1 175 ? -43.892 -0.867  13.671  1.00 22.63 ?  175 LEU B N   1 
ATOM   4197 C  CA  . LEU B 1 175 ? -43.311 -2.061  14.283  1.00 17.20 ?  175 LEU B CA  1 
ATOM   4198 C  C   . LEU B 1 175 ? -42.007 -2.463  13.593  1.00 21.70 ?  175 LEU B C   1 
ATOM   4199 O  O   . LEU B 1 175 ? -41.025 -2.814  14.256  1.00 21.68 ?  175 LEU B O   1 
ATOM   4200 C  CB  . LEU B 1 175 ? -44.324 -3.212  14.242  1.00 23.14 ?  175 LEU B CB  1 
ATOM   4201 C  CG  . LEU B 1 175 ? -45.599 -3.036  15.085  1.00 26.67 ?  175 LEU B CG  1 
ATOM   4202 C  CD1 . LEU B 1 175 ? -46.667 -4.093  14.786  1.00 21.21 ?  175 LEU B CD1 1 
ATOM   4203 C  CD2 . LEU B 1 175 ? -45.244 -3.061  16.565  1.00 24.58 ?  175 LEU B CD2 1 
ATOM   4204 N  N   . MET B 1 176 ? -41.974 -2.424  12.264  1.00 20.75 ?  176 MET B N   1 
ATOM   4205 C  CA  . MET B 1 176 ? -40.711 -2.692  11.591  1.00 22.54 ?  176 MET B CA  1 
ATOM   4206 C  C   . MET B 1 176 ? -39.676 -1.615  11.907  1.00 22.84 ?  176 MET B C   1 
ATOM   4207 O  O   . MET B 1 176 ? -38.472 -1.899  11.897  1.00 20.94 ?  176 MET B O   1 
ATOM   4208 C  CB  . MET B 1 176 ? -40.930 -2.851  10.080  1.00 20.25 ?  176 MET B CB  1 
ATOM   4209 C  CG  . MET B 1 176 ? -41.986 -3.926  9.742   1.00 20.22 ?  176 MET B CG  1 
ATOM   4210 S  SD  . MET B 1 176 ? -41.487 -5.591  10.275  1.00 21.86 ?  176 MET B SD  1 
ATOM   4211 C  CE  . MET B 1 176 ? -40.019 -5.888  9.265   1.00 22.39 ?  176 MET B CE  1 
ATOM   4212 N  N   . SER B 1 177 ? -40.110 -0.387  12.221  1.00 20.28 ?  177 SER B N   1 
ATOM   4213 C  CA  . SER B 1 177 ? -39.142 0.619   12.643  1.00 21.83 ?  177 SER B CA  1 
ATOM   4214 C  C   . SER B 1 177 ? -38.548 0.277   14.006  1.00 22.31 ?  177 SER B C   1 
ATOM   4215 O  O   . SER B 1 177 ? -37.377 0.564   14.260  1.00 19.54 ?  177 SER B O   1 
ATOM   4216 C  CB  . SER B 1 177 ? -39.776 2.021   12.680  1.00 26.79 ?  177 SER B CB  1 
ATOM   4217 O  OG  . SER B 1 177 ? -38.774 2.975   13.059  1.00 24.85 ?  177 SER B OG  1 
ATOM   4218 N  N   . GLY B 1 178 ? -39.328 -0.354  14.889  1.00 27.08 ?  178 GLY B N   1 
ATOM   4219 C  CA  . GLY B 1 178 ? -38.759 -0.818  16.144  1.00 20.73 ?  178 GLY B CA  1 
ATOM   4220 C  C   . GLY B 1 178 ? -37.661 -1.842  15.923  1.00 21.13 ?  178 GLY B C   1 
ATOM   4221 O  O   . GLY B 1 178 ? -36.633 -1.835  16.610  1.00 21.33 ?  178 GLY B O   1 
ATOM   4222 N  N   . ILE B 1 179 ? -37.855 -2.721  14.944  1.00 18.45 ?  179 ILE B N   1 
ATOM   4223 C  CA  . ILE B 1 179 ? -36.822 -3.692  14.589  1.00 19.50 ?  179 ILE B CA  1 
ATOM   4224 C  C   . ILE B 1 179 ? -35.553 -2.985  14.122  1.00 18.54 ?  179 ILE B C   1 
ATOM   4225 O  O   . ILE B 1 179 ? -34.432 -3.416  14.432  1.00 22.23 ?  179 ILE B O   1 
ATOM   4226 C  CB  . ILE B 1 179 ? -37.376 -4.653  13.526  1.00 22.55 ?  179 ILE B CB  1 
ATOM   4227 C  CG1 . ILE B 1 179 ? -38.302 -5.685  14.182  1.00 22.46 ?  179 ILE B CG1 1 
ATOM   4228 C  CG2 . ILE B 1 179 ? -36.264 -5.320  12.750  1.00 22.08 ?  179 ILE B CG2 1 
ATOM   4229 C  CD1 . ILE B 1 179 ? -39.189 -6.408  13.163  1.00 21.32 ?  179 ILE B CD1 1 
ATOM   4230 N  N   . ASP B 1 180 ? -35.707 -1.872  13.395  1.00 18.95 ?  180 ASP B N   1 
ATOM   4231 C  CA  . ASP B 1 180 ? -34.546 -1.110  12.920  1.00 18.43 ?  180 ASP B CA  1 
ATOM   4232 C  C   . ASP B 1 180 ? -33.649 -0.648  14.066  1.00 22.89 ?  180 ASP B C   1 
ATOM   4233 O  O   . ASP B 1 180 ? -32.452 -0.395  13.863  1.00 23.07 ?  180 ASP B O   1 
ATOM   4234 C  CB  . ASP B 1 180 ? -35.020 0.099   12.121  1.00 15.59 ?  180 ASP B CB  1 
ATOM   4235 C  CG  . ASP B 1 180 ? -35.412 -0.267  10.710  1.00 20.58 ?  180 ASP B CG  1 
ATOM   4236 O  OD1 . ASP B 1 180 ? -34.996 -1.356  10.230  1.00 24.19 ?  180 ASP B OD1 1 
ATOM   4237 O  OD2 . ASP B 1 180 ? -36.118 0.537   10.079  1.00 20.21 ?  180 ASP B OD2 1 
ATOM   4238 N  N   . VAL B 1 181 ? -34.211 -0.497  15.259  1.00 22.16 ?  181 VAL B N   1 
ATOM   4239 C  CA  . VAL B 1 181 ? -33.448 -0.135  16.449  1.00 18.60 ?  181 VAL B CA  1 
ATOM   4240 C  C   . VAL B 1 181 ? -33.088 -1.357  17.283  1.00 18.13 ?  181 VAL B C   1 
ATOM   4241 O  O   . VAL B 1 181 ? -31.951 -1.478  17.744  1.00 16.84 ?  181 VAL B O   1 
ATOM   4242 C  CB  . VAL B 1 181 ? -34.238 0.884   17.294  1.00 21.99 ?  181 VAL B CB  1 
ATOM   4243 C  CG1 . VAL B 1 181 ? -33.484 1.174   18.602  1.00 22.18 ?  181 VAL B CG1 1 
ATOM   4244 C  CG2 . VAL B 1 181 ? -34.485 2.162   16.495  1.00 21.09 ?  181 VAL B CG2 1 
ATOM   4245 N  N   . ALA B 1 182 ? -34.048 -2.278  17.477  1.00 18.96 ?  182 ALA B N   1 
ATOM   4246 C  CA  . ALA B 1 182 ? -33.819 -3.424  18.362  1.00 21.35 ?  182 ALA B CA  1 
ATOM   4247 C  C   . ALA B 1 182 ? -32.636 -4.284  17.922  1.00 18.52 ?  182 ALA B C   1 
ATOM   4248 O  O   . ALA B 1 182 ? -31.931 -4.839  18.773  1.00 23.13 ?  182 ALA B O   1 
ATOM   4249 C  CB  . ALA B 1 182 ? -35.074 -4.298  18.454  1.00 18.77 ?  182 ALA B CB  1 
ATOM   4250 N  N   . PHE B 1 183 ? -32.400 -4.425  16.612  1.00 20.22 ?  183 PHE B N   1 
ATOM   4251 C  CA  . PHE B 1 183 ? -31.386 -5.363  16.132  1.00 19.04 ?  183 PHE B CA  1 
ATOM   4252 C  C   . PHE B 1 183 ? -30.095 -4.665  15.699  1.00 18.96 ?  183 PHE B C   1 
ATOM   4253 O  O   . PHE B 1 183 ? -29.295 -5.239  14.948  1.00 21.16 ?  183 PHE B O   1 
ATOM   4254 C  CB  . PHE B 1 183 ? -31.965 -6.241  15.020  1.00 18.70 ?  183 PHE B CB  1 
ATOM   4255 C  CG  . PHE B 1 183 ? -33.022 -7.197  15.516  1.00 23.20 ?  183 PHE B CG  1 
ATOM   4256 C  CD1 . PHE B 1 183 ? -34.330 -6.766  15.714  1.00 24.32 ?  183 PHE B CD1 1 
ATOM   4257 C  CD2 . PHE B 1 183 ? -32.703 -8.506  15.828  1.00 24.65 ?  183 PHE B CD2 1 
ATOM   4258 C  CE1 . PHE B 1 183 ? -35.307 -7.634  16.193  1.00 24.90 ?  183 PHE B CE1 1 
ATOM   4259 C  CE2 . PHE B 1 183 ? -33.670 -9.373  16.310  1.00 29.03 ?  183 PHE B CE2 1 
ATOM   4260 C  CZ  . PHE B 1 183 ? -34.978 -8.929  16.493  1.00 26.86 ?  183 PHE B CZ  1 
ATOM   4261 N  N   . ILE B 1 184 ? -29.856 -3.461  16.215  1.00 20.10 ?  184 ILE B N   1 
ATOM   4262 C  CA  . ILE B 1 184 ? -28.598 -2.757  16.009  1.00 20.20 ?  184 ILE B CA  1 
ATOM   4263 C  C   . ILE B 1 184 ? -27.477 -3.460  16.766  1.00 20.94 ?  184 ILE B C   1 
ATOM   4264 O  O   . ILE B 1 184 ? -27.659 -3.899  17.907  1.00 18.46 ?  184 ILE B O   1 
ATOM   4265 C  CB  . ILE B 1 184 ? -28.763 -1.301  16.484  1.00 22.18 ?  184 ILE B CB  1 
ATOM   4266 C  CG1 . ILE B 1 184 ? -29.547 -0.479  15.452  1.00 17.19 ?  184 ILE B CG1 1 
ATOM   4267 C  CG2 . ILE B 1 184 ? -27.414 -0.646  16.835  1.00 15.17 ?  184 ILE B CG2 1 
ATOM   4268 C  CD1 . ILE B 1 184 ? -29.702 0.985   15.886  1.00 17.65 ?  184 ILE B CD1 1 
ATOM   4269 N  N   . THR B 1 185 ? -26.307 -3.578  16.134  1.00 19.75 ?  185 THR B N   1 
ATOM   4270 C  CA  . THR B 1 185 ? -25.098 -4.046  16.807  1.00 20.15 ?  185 THR B CA  1 
ATOM   4271 C  C   . THR B 1 185 ? -24.263 -2.831  17.199  1.00 21.06 ?  185 THR B C   1 
ATOM   4272 O  O   . THR B 1 185 ? -23.830 -2.063  16.332  1.00 21.47 ?  185 THR B O   1 
ATOM   4273 C  CB  . THR B 1 185 ? -24.279 -4.989  15.925  1.00 22.22 ?  185 THR B CB  1 
ATOM   4274 O  OG1 . THR B 1 185 ? -23.836 -4.284  14.763  1.00 23.00 ?  185 THR B OG1 1 
ATOM   4275 C  CG2 . THR B 1 185 ? -25.123 -6.192  15.482  1.00 22.25 ?  185 THR B CG2 1 
ATOM   4276 N  N   . SER B 1 186 ? -24.043 -2.664  18.501  1.00 20.08 ?  186 SER B N   1 
ATOM   4277 C  CA  . SER B 1 186 ? -23.358 -1.509  19.064  1.00 23.31 ?  186 SER B CA  1 
ATOM   4278 C  C   . SER B 1 186 ? -22.204 -1.951  19.954  1.00 23.77 ?  186 SER B C   1 
ATOM   4279 O  O   . SER B 1 186 ? -22.346 -2.905  20.729  1.00 25.10 ?  186 SER B O   1 
ATOM   4280 C  CB  . SER B 1 186 ? -24.332 -0.635  19.880  1.00 22.40 ?  186 SER B CB  1 
ATOM   4281 O  OG  . SER B 1 186 ? -23.734 0.607   20.219  1.00 21.53 ?  186 SER B OG  1 
ATOM   4282 N  N   . PRO B 1 187 ? -21.040 -1.293  19.842  1.00 22.76 ?  187 PRO B N   1 
ATOM   4283 C  CA  . PRO B 1 187 ? -19.930 -1.577  20.775  1.00 25.13 ?  187 PRO B CA  1 
ATOM   4284 C  C   . PRO B 1 187 ? -20.303 -1.445  22.247  1.00 28.40 ?  187 PRO B C   1 
ATOM   4285 O  O   . PRO B 1 187 ? -19.924 -2.288  23.070  1.00 31.59 ?  187 PRO B O   1 
ATOM   4286 C  CB  . PRO B 1 187 ? -18.883 -0.532  20.369  1.00 25.35 ?  187 PRO B CB  1 
ATOM   4287 C  CG  . PRO B 1 187 ? -19.133 -0.321  18.927  1.00 30.60 ?  187 PRO B CG  1 
ATOM   4288 C  CD  . PRO B 1 187 ? -20.630 -0.387  18.762  1.00 22.73 ?  187 PRO B CD  1 
ATOM   4289 N  N   . ARG B 1 188 ? -21.012 -0.382  22.599  1.00 25.94 ?  188 ARG B N   1 
ATOM   4290 C  CA  . ARG B 1 188 ? -21.478 -0.127  23.953  1.00 29.34 ?  188 ARG B CA  1 
ATOM   4291 C  C   . ARG B 1 188 ? -22.989 0.051   23.928  1.00 26.11 ?  188 ARG B C   1 
ATOM   4292 O  O   . ARG B 1 188 ? -23.575 0.369   22.887  1.00 22.08 ?  188 ARG B O   1 
ATOM   4293 C  CB  . ARG B 1 188 ? -20.814 1.121   24.544  1.00 29.71 ?  188 ARG B CB  1 
ATOM   4294 C  CG  . ARG B 1 188 ? -19.314 1.010   24.671  1.00 29.97 ?  188 ARG B CG  1 
ATOM   4295 C  CD  . ARG B 1 188 ? -18.922 0.039   25.769  1.00 38.89 ?  188 ARG B CD  1 
ATOM   4296 N  NE  . ARG B 1 188 ? -17.484 0.073   26.006  1.00 50.92 ?  188 ARG B NE  1 
ATOM   4297 C  CZ  . ARG B 1 188 ? -16.599 -0.664  25.347  1.00 52.29 ?  188 ARG B CZ  1 
ATOM   4298 N  NH1 . ARG B 1 188 ? -16.975 -1.522  24.409  1.00 41.28 ?  188 ARG B NH1 1 
ATOM   4299 N  NH2 . ARG B 1 188 ? -15.304 -0.533  25.631  1.00 55.62 ?  188 ARG B NH2 1 
ATOM   4300 N  N   . THR B 1 189 ? -23.622 -0.152  25.082  1.00 26.16 ?  189 THR B N   1 
ATOM   4301 C  CA  . THR B 1 189 ? -25.063 0.057   25.153  1.00 24.00 ?  189 THR B CA  1 
ATOM   4302 C  C   . THR B 1 189 ? -25.391 1.518   24.858  1.00 26.45 ?  189 THR B C   1 
ATOM   4303 O  O   . THR B 1 189 ? -24.589 2.423   25.107  1.00 31.24 ?  189 THR B O   1 
ATOM   4304 C  CB  . THR B 1 189 ? -25.612 -0.344  26.526  1.00 29.48 ?  189 THR B CB  1 
ATOM   4305 O  OG1 . THR B 1 189 ? -25.248 0.639   27.493  1.00 33.04 ?  189 THR B OG1 1 
ATOM   4306 C  CG2 . THR B 1 189 ? -25.062 -1.680  26.958  1.00 35.63 ?  189 THR B CG2 1 
ATOM   4307 N  N   . PHE B 1 190 ? -26.581 1.739   24.293  1.00 24.65 ?  190 PHE B N   1 
ATOM   4308 C  CA  . PHE B 1 190 ? -26.998 3.121   23.932  1.00 24.74 ?  190 PHE B CA  1 
ATOM   4309 C  C   . PHE B 1 190 ? -28.403 3.617   24.269  1.00 21.98 ?  190 PHE B C   1 
ATOM   4310 O  O   . PHE B 1 190 ? -29.367 3.286   23.542  1.00 21.77 ?  190 PHE B O   1 
ATOM   4311 C  CB  . PHE B 1 190 ? -26.989 3.305   22.410  1.00 22.96 ?  190 PHE B CB  1 
ATOM   4312 C  CG  . PHE B 1 190 ? -27.868 2.347   21.615  1.00 23.26 ?  190 PHE B CG  1 
ATOM   4313 C  CD1 . PHE B 1 190 ? -27.411 1.082   21.262  1.00 21.08 ?  190 PHE B CD1 1 
ATOM   4314 C  CD2 . PHE B 1 190 ? -29.145 2.718   21.211  1.00 23.54 ?  190 PHE B CD2 1 
ATOM   4315 C  CE1 . PHE B 1 190 ? -28.213 0.215   20.537  1.00 22.56 ?  190 PHE B CE1 1 
ATOM   4316 C  CE2 . PHE B 1 190 ? -29.942 1.848   20.484  1.00 23.91 ?  190 PHE B CE2 1 
ATOM   4317 C  CZ  . PHE B 1 190 ? -29.475 0.600   20.149  1.00 20.74 ?  190 PHE B CZ  1 
ATOM   4318 N  N   . GLU B 1 191 ? -28.523 4.382   25.357  1.00 30.00 ?  191 GLU B N   1 
ATOM   4319 C  CA  . GLU B 1 191 ? -29.839 4.960   25.730  1.00 30.00 ?  191 GLU B CA  1 
ATOM   4320 C  C   . GLU B 1 191 ? -30.856 5.022   24.583  1.00 30.00 ?  191 GLU B C   1 
ATOM   4321 O  O   . GLU B 1 191 ? -30.701 5.902   23.717  1.00 30.00 ?  191 GLU B O   1 
ATOM   4322 C  CB  . GLU B 1 191 ? -29.726 6.304   26.448  1.00 30.00 ?  191 GLU B CB  1 
ATOM   4323 C  CG  . GLU B 1 191 ? -31.070 6.850   26.918  1.00 30.00 ?  191 GLU B CG  1 
ATOM   4324 C  CD  . GLU B 1 191 ? -31.248 8.338   26.681  1.00 30.00 ?  191 GLU B CD  1 
ATOM   4325 O  OE1 . GLU B 1 191 ? -30.605 8.875   25.755  1.00 30.00 ?  191 GLU B OE1 1 
ATOM   4326 O  OE2 . GLU B 1 191 ? -32.033 8.960   27.426  1.00 30.00 ?  191 GLU B OE2 1 
ATOM   4327 N  N   . GLY B 1 192 ? -31.843 4.122   24.577  1.00 16.38 ?  192 GLY B N   1 
ATOM   4328 C  CA  . GLY B 1 192 ? -32.828 4.069   23.479  1.00 35.25 ?  192 GLY B CA  1 
ATOM   4329 C  C   . GLY B 1 192 ? -33.210 2.632   23.199  1.00 22.86 ?  192 GLY B C   1 
ATOM   4330 O  O   . GLY B 1 192 ? -34.400 2.388   22.974  1.00 24.82 ?  192 GLY B O   1 
ATOM   4331 N  N   . SER B 1 193 ? -32.241 1.717   23.199  1.00 25.17 ?  193 SER B N   1 
ATOM   4332 C  CA  . SER B 1 193 ? -32.496 0.275   23.011  1.00 25.51 ?  193 SER B CA  1 
ATOM   4333 C  C   . SER B 1 193 ? -33.586 -0.029  24.049  1.00 23.68 ?  193 SER B C   1 
ATOM   4334 O  O   . SER B 1 193 ? -34.591 -0.650  23.705  1.00 23.26 ?  193 SER B O   1 
ATOM   4335 C  CB  . SER B 1 193 ? -31.259 -0.550  23.234  1.00 25.20 ?  193 SER B CB  1 
ATOM   4336 O  OG  . SER B 1 193 ? -30.889 -0.618  24.601  1.00 29.05 ?  193 SER B OG  1 
ATOM   4337 N  N   . ALA B 1 194 ? -33.424 0.517   25.254  1.00 24.10 ?  194 ALA B N   1 
ATOM   4338 C  CA  . ALA B 1 194 ? -34.360 0.200   26.354  1.00 23.47 ?  194 ALA B CA  1 
ATOM   4339 C  C   . ALA B 1 194 ? -35.630 1.011   26.086  1.00 21.90 ?  194 ALA B C   1 
ATOM   4340 O  O   . ALA B 1 194 ? -36.717 0.446   26.173  1.00 24.65 ?  194 ALA B O   1 
ATOM   4341 C  CB  . ALA B 1 194 ? -33.759 0.507   27.693  1.00 23.74 ?  194 ALA B CB  1 
ATOM   4342 N  N   . VAL B 1 195 ? -35.484 2.290   25.745  1.00 22.99 ?  195 VAL B N   1 
ATOM   4343 C  CA  . VAL B 1 195 ? -36.697 3.036   25.415  1.00 20.66 ?  195 VAL B CA  1 
ATOM   4344 C  C   . VAL B 1 195 ? -37.461 2.329   24.305  1.00 22.69 ?  195 VAL B C   1 
ATOM   4345 O  O   . VAL B 1 195 ? -38.685 2.167   24.369  1.00 20.99 ?  195 VAL B O   1 
ATOM   4346 C  CB  . VAL B 1 195 ? -36.359 4.482   25.012  1.00 24.80 ?  195 VAL B CB  1 
ATOM   4347 C  CG1 . VAL B 1 195 ? -37.614 5.201   24.560  1.00 19.01 ?  195 VAL B CG1 1 
ATOM   4348 C  CG2 . VAL B 1 195 ? -35.662 5.240   26.170  1.00 23.14 ?  195 VAL B CG2 1 
ATOM   4349 N  N   . ASN B 1 196 ? -36.749 1.923   23.250  1.00 23.89 ?  196 ASN B N   1 
ATOM   4350 C  CA  . ASN B 1 196 ? -37.402 1.246   22.134  1.00 21.00 ?  196 ASN B CA  1 
ATOM   4351 C  C   . ASN B 1 196 ? -38.059 -0.056  22.589  1.00 22.04 ?  196 ASN B C   1 
ATOM   4352 O  O   . ASN B 1 196 ? -39.171 -0.383  22.162  1.00 20.26 ?  196 ASN B O   1 
ATOM   4353 C  CB  . ASN B 1 196 ? -36.372 0.986   21.029  1.00 20.48 ?  196 ASN B CB  1 
ATOM   4354 C  CG  . ASN B 1 196 ? -36.986 0.378   19.778  1.00 22.72 ?  196 ASN B CG  1 
ATOM   4355 O  OD1 . ASN B 1 196 ? -37.791 1.011   19.088  1.00 22.48 ?  196 ASN B OD1 1 
ATOM   4356 N  ND2 . ASN B 1 196 ? -36.599 -0.862  19.478  1.00 21.28 ?  196 ASN B ND2 1 
ATOM   4357 N  N   . TRP B 1 197 ? -37.391 -0.810  23.464  1.00 24.01 ?  197 TRP B N   1 
ATOM   4358 C  CA  . TRP B 1 197 ? -37.974 -2.065  23.931  1.00 25.12 ?  197 TRP B CA  1 
ATOM   4359 C  C   . TRP B 1 197 ? -39.289 -1.823  24.670  1.00 24.83 ?  197 TRP B C   1 
ATOM   4360 O  O   . TRP B 1 197 ? -40.315 -2.424  24.340  1.00 23.33 ?  197 TRP B O   1 
ATOM   4361 C  CB  . TRP B 1 197 ? -36.986 -2.813  24.825  1.00 24.33 ?  197 TRP B CB  1 
ATOM   4362 C  CG  . TRP B 1 197 ? -37.588 -4.082  25.407  1.00 31.75 ?  197 TRP B CG  1 
ATOM   4363 C  CD1 . TRP B 1 197 ? -38.122 -4.245  26.657  1.00 28.64 ?  197 TRP B CD1 1 
ATOM   4364 C  CD2 . TRP B 1 197 ? -37.724 -5.352  24.743  1.00 30.77 ?  197 TRP B CD2 1 
ATOM   4365 N  NE1 . TRP B 1 197 ? -38.579 -5.540  26.811  1.00 29.53 ?  197 TRP B NE1 1 
ATOM   4366 C  CE2 . TRP B 1 197 ? -38.343 -6.237  25.653  1.00 32.50 ?  197 TRP B CE2 1 
ATOM   4367 C  CE3 . TRP B 1 197 ? -37.378 -5.824  23.470  1.00 31.03 ?  197 TRP B CE3 1 
ATOM   4368 C  CZ2 . TRP B 1 197 ? -38.636 -7.563  25.323  1.00 34.75 ?  197 TRP B CZ2 1 
ATOM   4369 C  CZ3 . TRP B 1 197 ? -37.667 -7.145  23.142  1.00 33.12 ?  197 TRP B CZ3 1 
ATOM   4370 C  CH2 . TRP B 1 197 ? -38.293 -7.996  24.064  1.00 32.76 ?  197 TRP B CH2 1 
ATOM   4371 N  N   . TYR B 1 198 ? -39.278 -0.946  25.674  1.00 23.01 ?  198 TYR B N   1 
ATOM   4372 C  CA  . TYR B 1 198 ? -40.489 -0.723  26.456  1.00 26.64 ?  198 TYR B CA  1 
ATOM   4373 C  C   . TYR B 1 198 ? -41.568 -0.045  25.632  1.00 27.49 ?  198 TYR B C   1 
ATOM   4374 O  O   . TYR B 1 198 ? -42.757 -0.201  25.933  1.00 25.18 ?  198 TYR B O   1 
ATOM   4375 C  CB  . TYR B 1 198 ? -40.158 0.083   27.720  1.00 25.65 ?  198 TYR B CB  1 
ATOM   4376 C  CG  . TYR B 1 198 ? -39.264 -0.695  28.666  1.00 31.47 ?  198 TYR B CG  1 
ATOM   4377 C  CD1 . TYR B 1 198 ? -39.666 -1.930  29.171  1.00 31.05 ?  198 TYR B CD1 1 
ATOM   4378 C  CD2 . TYR B 1 198 ? -37.999 -0.223  29.021  1.00 30.99 ?  198 TYR B CD2 1 
ATOM   4379 C  CE1 . TYR B 1 198 ? -38.842 -2.668  30.009  1.00 33.29 ?  198 TYR B CE1 1 
ATOM   4380 C  CE2 . TYR B 1 198 ? -37.171 -0.955  29.868  1.00 32.74 ?  198 TYR B CE2 1 
ATOM   4381 C  CZ  . TYR B 1 198 ? -37.598 -2.179  30.354  1.00 36.54 ?  198 TYR B CZ  1 
ATOM   4382 O  OH  . TYR B 1 198 ? -36.791 -2.915  31.201  1.00 40.96 ?  198 TYR B OH  1 
ATOM   4383 N  N   . LYS B 1 199 ? -41.176 0.673   24.573  1.00 28.11 ?  199 LYS B N   1 
ATOM   4384 C  CA  . LYS B 1 199 ? -42.156 1.229   23.647  1.00 23.72 ?  199 LYS B CA  1 
ATOM   4385 C  C   . LYS B 1 199 ? -43.024 0.127   23.048  1.00 24.12 ?  199 LYS B C   1 
ATOM   4386 O  O   . LYS B 1 199 ? -44.257 0.190   23.087  1.00 23.25 ?  199 LYS B O   1 
ATOM   4387 C  CB  . LYS B 1 199 ? -41.438 2.009   22.540  1.00 22.47 ?  199 LYS B CB  1 
ATOM   4388 C  CG  . LYS B 1 199 ? -42.389 2.582   21.463  1.00 25.37 ?  199 LYS B CG  1 
ATOM   4389 C  CD  . LYS B 1 199 ? -41.609 3.142   20.269  1.00 22.47 ?  199 LYS B CD  1 
ATOM   4390 C  CE  . LYS B 1 199 ? -42.561 3.651   19.195  1.00 24.72 ?  199 LYS B CE  1 
ATOM   4391 N  NZ  . LYS B 1 199 ? -41.868 4.347   18.067  1.00 20.22 ?  199 LYS B NZ  1 
ATOM   4392 N  N   . ASP B 1 200 ? -42.402 -0.898  22.482  1.00 23.74 ?  200 ASP B N   1 
ATOM   4393 C  CA  . ASP B 1 200 ? -43.206 -1.889  21.788  1.00 22.90 ?  200 ASP B CA  1 
ATOM   4394 C  C   . ASP B 1 200 ? -43.702 -2.984  22.709  1.00 21.85 ?  200 ASP B C   1 
ATOM   4395 O  O   . ASP B 1 200 ? -44.695 -3.638  22.383  1.00 24.30 ?  200 ASP B O   1 
ATOM   4396 C  CB  . ASP B 1 200 ? -42.419 -2.456  20.603  1.00 21.32 ?  200 ASP B CB  1 
ATOM   4397 C  CG  . ASP B 1 200 ? -42.425 -1.496  19.421  1.00 25.63 ?  200 ASP B CG  1 
ATOM   4398 O  OD1 . ASP B 1 200 ? -43.277 -0.573  19.433  1.00 21.39 ?  200 ASP B OD1 1 
ATOM   4399 O  OD2 . ASP B 1 200 ? -41.591 -1.645  18.504  1.00 24.01 ?  200 ASP B OD2 1 
ATOM   4400 N  N   . LEU B 1 201 ? -43.061 -3.165  23.863  1.00 23.07 ?  201 LEU B N   1 
ATOM   4401 C  CA  . LEU B 1 201 ? -43.656 -3.971  24.920  1.00 24.06 ?  201 LEU B CA  1 
ATOM   4402 C  C   . LEU B 1 201 ? -45.002 -3.395  25.334  1.00 25.20 ?  201 LEU B C   1 
ATOM   4403 O  O   . LEU B 1 201 ? -45.994 -4.122  25.442  1.00 28.63 ?  201 LEU B O   1 
ATOM   4404 C  CB  . LEU B 1 201 ? -42.717 -4.038  26.119  1.00 26.16 ?  201 LEU B CB  1 
ATOM   4405 C  CG  . LEU B 1 201 ? -43.127 -5.043  27.197  1.00 29.22 ?  201 LEU B CG  1 
ATOM   4406 C  CD1 . LEU B 1 201 ? -42.892 -6.467  26.699  1.00 27.91 ?  201 LEU B CD1 1 
ATOM   4407 C  CD2 . LEU B 1 201 ? -42.401 -4.770  28.502  1.00 28.88 ?  201 LEU B CD2 1 
ATOM   4408 N  N   . GLY B 1 202 ? -45.053 -2.080  25.561  1.00 24.51 ?  202 GLY B N   1 
ATOM   4409 C  CA  . GLY B 1 202 ? -46.319 -1.441  25.883  1.00 25.10 ?  202 GLY B CA  1 
ATOM   4410 C  C   . GLY B 1 202 ? -47.358 -1.649  24.801  1.00 26.79 ?  202 GLY B C   1 
ATOM   4411 O  O   . GLY B 1 202 ? -48.518 -1.945  25.092  1.00 27.77 ?  202 GLY B O   1 
ATOM   4412 N  N   . TYR B 1 203 ? -46.951 -1.516  23.537  1.00 23.90 ?  203 TYR B N   1 
ATOM   4413 C  CA  . TYR B 1 203 ? -47.847 -1.829  22.427  1.00 25.41 ?  203 TYR B CA  1 
ATOM   4414 C  C   . TYR B 1 203 ? -48.413 -3.241  22.546  1.00 23.31 ?  203 TYR B C   1 
ATOM   4415 O  O   . TYR B 1 203 ? -49.602 -3.459  22.318  1.00 25.28 ?  203 TYR B O   1 
ATOM   4416 C  CB  . TYR B 1 203 ? -47.099 -1.671  21.099  1.00 26.50 ?  203 TYR B CB  1 
ATOM   4417 C  CG  . TYR B 1 203 ? -47.958 -1.836  19.854  1.00 27.42 ?  203 TYR B CG  1 
ATOM   4418 C  CD1 . TYR B 1 203 ? -48.229 -3.101  19.328  1.00 23.36 ?  203 TYR B CD1 1 
ATOM   4419 C  CD2 . TYR B 1 203 ? -48.480 -0.718  19.191  1.00 23.20 ?  203 TYR B CD2 1 
ATOM   4420 C  CE1 . TYR B 1 203 ? -49.005 -3.249  18.181  1.00 24.87 ?  203 TYR B CE1 1 
ATOM   4421 C  CE2 . TYR B 1 203 ? -49.247 -0.854  18.055  1.00 24.47 ?  203 TYR B CE2 1 
ATOM   4422 C  CZ  . TYR B 1 203 ? -49.508 -2.124  17.550  1.00 27.40 ?  203 TYR B CZ  1 
ATOM   4423 O  OH  . TYR B 1 203 ? -50.272 -2.256  16.414  1.00 26.86 ?  203 TYR B OH  1 
ATOM   4424 N  N   . MET B 1 204 ? -47.566 -4.219  22.867  1.00 26.90 ?  204 MET B N   1 
ATOM   4425 C  CA  . MET B 1 204 ? -48.022 -5.603  22.928  1.00 29.19 ?  204 MET B CA  1 
ATOM   4426 C  C   . MET B 1 204 ? -48.917 -5.828  24.143  1.00 30.37 ?  204 MET B C   1 
ATOM   4427 O  O   . MET B 1 204 ? -49.895 -6.579  24.067  1.00 28.77 ?  204 MET B O   1 
ATOM   4428 C  CB  . MET B 1 204 ? -46.820 -6.551  22.962  1.00 26.18 ?  204 MET B CB  1 
ATOM   4429 C  CG  . MET B 1 204 ? -45.956 -6.576  21.696  1.00 24.40 ?  204 MET B CG  1 
ATOM   4430 S  SD  . MET B 1 204 ? -46.739 -7.063  20.137  1.00 27.84 ?  204 MET B SD  1 
ATOM   4431 C  CE  . MET B 1 204 ? -47.080 -8.783  20.519  1.00 27.75 ?  204 MET B CE  1 
ATOM   4432 N  N   . VAL B 1 205 ? -48.592 -5.191  25.272  1.00 28.18 ?  205 VAL B N   1 
ATOM   4433 C  CA  . VAL B 1 205 ? -49.442 -5.290  26.463  1.00 32.80 ?  205 VAL B CA  1 
ATOM   4434 C  C   . VAL B 1 205 ? -50.847 -4.784  26.156  1.00 30.07 ?  205 VAL B C   1 
ATOM   4435 O  O   . VAL B 1 205 ? -51.848 -5.400  26.535  1.00 31.35 ?  205 VAL B O   1 
ATOM   4436 C  CB  . VAL B 1 205 ? -48.815 -4.510  27.634  1.00 30.45 ?  205 VAL B CB  1 
ATOM   4437 C  CG1 . VAL B 1 205 ? -49.853 -4.240  28.706  1.00 37.81 ?  205 VAL B CG1 1 
ATOM   4438 C  CG2 . VAL B 1 205 ? -47.670 -5.277  28.218  1.00 26.53 ?  205 VAL B CG2 1 
ATOM   4439 N  N   . ASP B 1 206 ? -50.933 -3.668  25.432  1.00 30.52 ?  206 ASP B N   1 
ATOM   4440 C  CA  . ASP B 1 206 ? -52.214 -3.057  25.100  1.00 28.56 ?  206 ASP B CA  1 
ATOM   4441 C  C   . ASP B 1 206 ? -53.053 -3.946  24.189  1.00 32.30 ?  206 ASP B C   1 
ATOM   4442 O  O   . ASP B 1 206 ? -54.276 -4.038  24.357  1.00 36.35 ?  206 ASP B O   1 
ATOM   4443 C  CB  . ASP B 1 206 ? -51.961 -1.709  24.438  1.00 30.70 ?  206 ASP B CB  1 
ATOM   4444 C  CG  . ASP B 1 206 ? -51.716 -0.601  25.442  1.00 40.08 ?  206 ASP B CG  1 
ATOM   4445 O  OD1 . ASP B 1 206 ? -51.489 -0.898  26.643  1.00 33.91 ?  206 ASP B OD1 1 
ATOM   4446 O  OD2 . ASP B 1 206 ? -51.723 0.573   25.015  1.00 43.65 ?  206 ASP B OD2 1 
ATOM   4447 N  N   . ARG B 1 207 ? -52.429 -4.581  23.193  1.00 27.48 ?  207 ARG B N   1 
ATOM   4448 C  CA  . ARG B 1 207 ? -53.187 -5.477  22.321  1.00 33.27 ?  207 ARG B CA  1 
ATOM   4449 C  C   . ARG B 1 207 ? -53.710 -6.678  23.094  1.00 29.90 ?  207 ARG B C   1 
ATOM   4450 O  O   . ARG B 1 207 ? -54.801 -7.176  22.805  1.00 35.76 ?  207 ARG B O   1 
ATOM   4451 C  CB  . ARG B 1 207 ? -52.323 -5.949  21.142  1.00 33.54 ?  207 ARG B CB  1 
ATOM   4452 C  CG  . ARG B 1 207 ? -51.597 -4.835  20.376  1.00 32.54 ?  207 ARG B CG  1 
ATOM   4453 C  CD  . ARG B 1 207 ? -52.541 -4.039  19.483  1.00 26.16 ?  207 ARG B CD  1 
ATOM   4454 N  NE  . ARG B 1 207 ? -53.201 -2.964  20.219  1.00 41.37 ?  207 ARG B NE  1 
ATOM   4455 C  CZ  . ARG B 1 207 ? -52.596 -1.878  20.691  1.00 39.49 ?  207 ARG B CZ  1 
ATOM   4456 N  NH1 . ARG B 1 207 ? -51.302 -1.673  20.515  1.00 33.06 ?  207 ARG B NH1 1 
ATOM   4457 N  NH2 . ARG B 1 207 ? -53.315 -0.966  21.343  1.00 42.52 ?  207 ARG B NH2 1 
ATOM   4458 N  N   . LEU B 1 208 ? -52.943 -7.136  24.083  1.00 31.32 ?  208 LEU B N   1 
ATOM   4459 C  CA  . LEU B 1 208 ? -53.264 -8.316  24.877  1.00 34.04 ?  208 LEU B CA  1 
ATOM   4460 C  C   . LEU B 1 208 ? -54.360 -8.035  25.897  1.00 34.02 ?  208 LEU B C   1 
ATOM   4461 O  O   . LEU B 1 208 ? -55.213 -8.891  26.147  1.00 37.83 ?  208 LEU B O   1 
ATOM   4462 C  CB  . LEU B 1 208 ? -52.000 -8.799  25.592  1.00 29.27 ?  208 LEU B CB  1 
ATOM   4463 C  CG  . LEU B 1 208 ? -52.179 -9.778  26.753  1.00 35.30 ?  208 LEU B CG  1 
ATOM   4464 C  CD1 . LEU B 1 208 ? -52.568 -11.161 26.231  1.00 35.47 ?  208 LEU B CD1 1 
ATOM   4465 C  CD2 . LEU B 1 208 ? -50.932 -9.827  27.624  1.00 35.83 ?  208 LEU B CD2 1 
ATOM   4466 N  N   . ASN B 1 209 ? -54.397 -6.821  26.430  1.00 35.76 ?  209 ASN B N   1 
ATOM   4467 C  CA  . ASN B 1 209 ? -55.383 -6.442  27.481  1.00 37.03 ?  209 ASN B CA  1 
ATOM   4468 C  C   . ASN B 1 209 ? -56.551 -5.652  26.890  1.00 36.54 ?  209 ASN B C   1 
ATOM   4469 O  O   . ASN B 1 209 ? -57.269 -5.014  27.664  1.00 46.17 ?  209 ASN B O   1 
ATOM   4470 C  CB  . ASN B 1 209 ? -54.713 -5.621  28.571  1.00 33.25 ?  209 ASN B CB  1 
ATOM   4471 C  CG  . ASN B 1 209 ? -53.796 -6.457  29.427  1.00 41.01 ?  209 ASN B CG  1 
ATOM   4472 O  OD1 . ASN B 1 209 ? -54.006 -7.664  29.566  1.00 35.72 ?  209 ASN B OD1 1 
ATOM   4473 N  ND2 . ASN B 1 209 ? -52.780 -5.838  30.007  1.00 41.57 ?  209 ASN B ND2 1 
ATOM   4474 N  N   . ALA B 1 210 ? -56.740 -5.704  25.580  1.00 37.85 ?  210 ALA B N   1 
ATOM   4475 C  CA  . ALA B 1 210 ? -57.825 -4.947  24.915  1.00 44.62 ?  210 ALA B CA  1 
ATOM   4476 C  C   . ALA B 1 210 ? -59.216 -5.378  25.402  1.00 49.85 ?  210 ALA B C   1 
ATOM   4477 O  O   . ALA B 1 210 ? -59.319 -6.525  25.858  1.00 47.02 ?  210 ALA B O   1 
ATOM   4478 C  CB  . ALA B 1 210 ? -57.678 -5.092  23.426  1.00 42.78 ?  210 ALA B CB  1 
ATOM   4479 N  N   . ASP B 1 211 ? -60.217 -4.500  25.353  1.00 53.18 ?  211 ASP B N   1 
ATOM   4480 C  CA  . ASP B 1 211 ? -61.531 -4.876  25.959  1.00 57.04 ?  211 ASP B CA  1 
ATOM   4481 C  C   . ASP B 1 211 ? -62.076 -6.118  25.263  1.00 65.17 ?  211 ASP B C   1 
ATOM   4482 O  O   . ASP B 1 211 ? -62.175 -7.143  25.948  1.00 68.88 ?  211 ASP B O   1 
ATOM   4483 C  CB  . ASP B 1 211 ? -62.532 -3.739  26.068  1.00 62.49 ?  211 ASP B CB  1 
ATOM   4484 C  CG  . ASP B 1 211 ? -63.896 -4.177  26.582  1.00 64.07 ?  211 ASP B CG  1 
ATOM   4485 O  OD1 . ASP B 1 211 ? -63.927 -4.993  27.523  1.00 61.01 ?  211 ASP B OD1 1 
ATOM   4486 O  OD2 . ASP B 1 211 ? -64.912 -3.721  26.022  1.00 66.61 ?  211 ASP B OD2 1 
ATOM   4487 N  N   . PRO B 1 212 ? -62.495 -6.102  23.984  1.00 63.37 ?  212 PRO B N   1 
ATOM   4488 C  CA  . PRO B 1 212 ? -62.892 -7.349  23.357  1.00 59.92 ?  212 PRO B CA  1 
ATOM   4489 C  C   . PRO B 1 212 ? -61.624 -8.178  23.362  1.00 58.81 ?  212 PRO B C   1 
ATOM   4490 O  O   . PRO B 1 212 ? -60.911 -8.205  22.352  1.00 63.72 ?  212 PRO B O   1 
ATOM   4491 C  CB  . PRO B 1 212 ? -63.339 -6.961  21.965  1.00 55.69 ?  212 PRO B CB  1 
ATOM   4492 C  CG  . PRO B 1 212 ? -63.566 -5.469  22.053  1.00 61.14 ?  212 PRO B CG  1 
ATOM   4493 C  CD  . PRO B 1 212 ? -62.586 -4.958  23.095  1.00 63.67 ?  212 PRO B CD  1 
ATOM   4494 N  N   . GLU B 1 213 ? -61.307 -8.788  24.511  1.00 56.70 ?  213 GLU B N   1 
ATOM   4495 C  CA  . GLU B 1 213 ? -60.032 -9.535  24.682  1.00 53.05 ?  213 GLU B CA  1 
ATOM   4496 C  C   . GLU B 1 213 ? -59.616 -10.206 23.365  1.00 55.65 ?  213 GLU B C   1 
ATOM   4497 O  O   . GLU B 1 213 ? -60.439 -10.942 22.775  1.00 55.05 ?  213 GLU B O   1 
ATOM   4498 C  CB  . GLU B 1 213 ? -60.175 -10.565 25.803  1.00 57.00 ?  213 GLU B CB  1 
ATOM   4499 C  CG  . GLU B 1 213 ? -58.832 -11.067 26.322  1.00 57.68 ?  213 GLU B CG  1 
ATOM   4500 C  CD  . GLU B 1 213 ? -58.660 -11.045 27.829  1.00 61.92 ?  213 GLU B CD  1 
ATOM   4501 O  OE1 . GLU B 1 213 ? -59.546 -11.573 28.533  1.00 64.28 ?  213 GLU B OE1 1 
ATOM   4502 O  OE2 . GLU B 1 213 ? -57.635 -10.508 28.296  1.00 61.65 ?  213 GLU B OE2 1 
ATOM   4503 N  N   . PRO B 1 214 ? -58.344 -10.066 22.933  1.00 51.97 ?  214 PRO B N   1 
ATOM   4504 C  CA  . PRO B 1 214 ? -57.895 -10.708 21.693  1.00 52.53 ?  214 PRO B CA  1 
ATOM   4505 C  C   . PRO B 1 214 ? -58.195 -12.194 21.581  1.00 51.15 ?  214 PRO B C   1 
ATOM   4506 O  O   . PRO B 1 214 ? -57.905 -12.977 22.486  1.00 43.59 ?  214 PRO B O   1 
ATOM   4507 C  CB  . PRO B 1 214 ? -56.383 -10.440 21.685  1.00 43.34 ?  214 PRO B CB  1 
ATOM   4508 C  CG  . PRO B 1 214 ? -56.029 -10.257 23.116  1.00 46.36 ?  214 PRO B CG  1 
ATOM   4509 C  CD  . PRO B 1 214 ? -57.203 -9.522  23.689  1.00 50.26 ?  214 PRO B CD  1 
ATOM   4510 N  N   . THR B 1 215 ? -58.609 -12.645 20.384  1.00 45.44 ?  215 THR B N   1 
ATOM   4511 C  CA  . THR B 1 215 ? -59.015 -14.062 20.189  1.00 45.97 ?  215 THR B CA  1 
ATOM   4512 C  C   . THR B 1 215 ? -58.127 -14.902 19.271  1.00 54.88 ?  215 THR B C   1 
ATOM   4513 O  O   . THR B 1 215 ? -58.223 -16.141 19.385  1.00 57.21 ?  215 THR B O   1 
ATOM   4514 C  CB  . THR B 1 215 ? -60.441 -14.100 19.636  1.00 48.54 ?  215 THR B CB  1 
ATOM   4515 O  OG1 . THR B 1 215 ? -60.401 -13.381 18.408  1.00 54.55 ?  215 THR B OG1 1 
ATOM   4516 C  CG2 . THR B 1 215 ? -61.457 -13.482 20.577  1.00 50.80 ?  215 THR B CG2 1 
ATOM   4517 N  N   . GLU B 1 216 ? -57.326 -14.327 18.368  1.00 54.98 ?  216 GLU B N   1 
ATOM   4518 C  CA  . GLU B 1 216 ? -56.592 -15.166 17.377  1.00 45.01 ?  216 GLU B CA  1 
ATOM   4519 C  C   . GLU B 1 216 ? -55.085 -15.207 17.633  1.00 42.70 ?  216 GLU B C   1 
ATOM   4520 O  O   . GLU B 1 216 ? -54.621 -14.437 18.485  1.00 40.28 ?  216 GLU B O   1 
ATOM   4521 C  CB  . GLU B 1 216 ? -56.842 -14.551 16.007  1.00 44.66 ?  216 GLU B CB  1 
ATOM   4522 C  CG  . GLU B 1 216 ? -58.301 -14.617 15.569  1.00 52.44 ?  216 GLU B CG  1 
ATOM   4523 C  CD  . GLU B 1 216 ? -58.835 -16.036 15.526  1.00 59.68 ?  216 GLU B CD  1 
ATOM   4524 O  OE1 . GLU B 1 216 ? -58.085 -16.931 15.088  1.00 56.53 ?  216 GLU B OE1 1 
ATOM   4525 O  OE2 . GLU B 1 216 ? -59.992 -16.250 15.940  1.00 62.86 ?  216 GLU B OE2 1 
ATOM   4526 N  N   . GLY B 1 217 ? -54.349 -16.091 16.934  1.00 41.76 ?  217 GLY B N   1 
ATOM   4527 C  CA  . GLY B 1 217 ? -52.916 -15.991 17.110  1.00 34.70 ?  217 GLY B CA  1 
ATOM   4528 C  C   . GLY B 1 217 ? -52.276 -16.396 18.430  1.00 37.69 ?  217 GLY B C   1 
ATOM   4529 O  O   . GLY B 1 217 ? -52.783 -17.224 19.188  1.00 42.43 ?  217 GLY B O   1 
ATOM   4530 N  N   . LEU B 1 218 ? -51.135 -15.754 18.698  1.00 37.99 ?  218 LEU B N   1 
ATOM   4531 C  CA  . LEU B 1 218 ? -50.433 -15.976 19.963  1.00 34.59 ?  218 LEU B CA  1 
ATOM   4532 C  C   . LEU B 1 218 ? -51.126 -15.258 21.115  1.00 33.68 ?  218 LEU B C   1 
ATOM   4533 O  O   . LEU B 1 218 ? -51.243 -15.816 22.217  1.00 27.17 ?  218 LEU B O   1 
ATOM   4534 C  CB  . LEU B 1 218 ? -48.986 -15.511 19.859  1.00 26.13 ?  218 LEU B CB  1 
ATOM   4535 C  CG  . LEU B 1 218 ? -48.118 -15.787 21.089  1.00 31.87 ?  218 LEU B CG  1 
ATOM   4536 C  CD1 . LEU B 1 218 ? -47.716 -17.246 21.150  1.00 32.26 ?  218 LEU B CD1 1 
ATOM   4537 C  CD2 . LEU B 1 218 ? -46.864 -14.920 21.083  1.00 25.37 ?  218 LEU B CD2 1 
ATOM   4538 N  N   . LEU B 1 219 ? -51.570 -14.014 20.888  1.00 27.94 ?  219 LEU B N   1 
ATOM   4539 C  CA  . LEU B 1 219 ? -52.213 -13.250 21.956  1.00 34.79 ?  219 LEU B CA  1 
ATOM   4540 C  C   . LEU B 1 219 ? -53.485 -13.938 22.438  1.00 36.41 ?  219 LEU B C   1 
ATOM   4541 O  O   . LEU B 1 219 ? -53.730 -14.027 23.646  1.00 39.50 ?  219 LEU B O   1 
ATOM   4542 C  CB  . LEU B 1 219 ? -52.529 -11.827 21.484  1.00 31.55 ?  219 LEU B CB  1 
ATOM   4543 C  CG  . LEU B 1 219 ? -51.322 -10.918 21.233  1.00 32.42 ?  219 LEU B CG  1 
ATOM   4544 C  CD1 . LEU B 1 219 ? -51.734 -9.463  21.248  1.00 31.72 ?  219 LEU B CD1 1 
ATOM   4545 C  CD2 . LEU B 1 219 ? -50.216 -11.170 22.252  1.00 29.42 ?  219 LEU B CD2 1 
ATOM   4546 N  N   . GLY B 1 220 ? -54.308 -14.423 21.508  1.00 37.81 ?  220 GLY B N   1 
ATOM   4547 C  CA  . GLY B 1 220 ? -55.521 -15.121 21.900  1.00 41.89 ?  220 GLY B CA  1 
ATOM   4548 C  C   . GLY B 1 220 ? -55.236 -16.316 22.790  1.00 40.16 ?  220 GLY B C   1 
ATOM   4549 O  O   . GLY B 1 220 ? -55.857 -16.487 23.842  1.00 41.68 ?  220 GLY B O   1 
ATOM   4550 N  N   . ARG B 1 221 ? -54.285 -17.157 22.385  1.00 38.34 ?  221 ARG B N   1 
ATOM   4551 C  CA  . ARG B 1 221 ? -53.910 -18.270 23.243  1.00 38.70 ?  221 ARG B CA  1 
ATOM   4552 C  C   . ARG B 1 221 ? -53.434 -17.766 24.592  1.00 40.63 ?  221 ARG B C   1 
ATOM   4553 O  O   . ARG B 1 221 ? -53.756 -18.354 25.629  1.00 43.01 ?  221 ARG B O   1 
ATOM   4554 C  CB  . ARG B 1 221 ? -52.833 -19.123 22.581  1.00 38.23 ?  221 ARG B CB  1 
ATOM   4555 C  CG  . ARG B 1 221 ? -53.048 -19.358 21.113  1.00 39.69 ?  221 ARG B CG  1 
ATOM   4556 C  CD  . ARG B 1 221 ? -52.156 -20.475 20.611  1.00 40.07 ?  221 ARG B CD  1 
ATOM   4557 N  NE  . ARG B 1 221 ? -52.830 -21.229 19.563  1.00 48.22 ?  221 ARG B NE  1 
ATOM   4558 C  CZ  . ARG B 1 221 ? -52.735 -20.956 18.268  1.00 49.20 ?  221 ARG B CZ  1 
ATOM   4559 N  NH1 . ARG B 1 221 ? -51.918 -20.012 17.816  1.00 42.06 ?  221 ARG B NH1 1 
ATOM   4560 N  NH2 . ARG B 1 221 ? -53.474 -21.649 17.406  1.00 49.62 ?  221 ARG B NH2 1 
ATOM   4561 N  N   . PHE B 1 222 ? -52.672 -16.666 24.593  1.00 41.31 ?  222 PHE B N   1 
ATOM   4562 C  CA  . PHE B 1 222 ? -52.228 -16.055 25.841  1.00 36.72 ?  222 PHE B CA  1 
ATOM   4563 C  C   . PHE B 1 222 ? -53.416 -15.607 26.687  1.00 41.21 ?  222 PHE B C   1 
ATOM   4564 O  O   . PHE B 1 222 ? -53.406 -15.754 27.913  1.00 43.13 ?  222 PHE B O   1 
ATOM   4565 C  CB  . PHE B 1 222 ? -51.311 -14.868 25.541  1.00 41.10 ?  222 PHE B CB  1 
ATOM   4566 C  CG  . PHE B 1 222 ? -49.895 -15.250 25.199  1.00 41.99 ?  222 PHE B CG  1 
ATOM   4567 C  CD1 . PHE B 1 222 ? -49.484 -16.575 25.231  1.00 37.91 ?  222 PHE B CD1 1 
ATOM   4568 C  CD2 . PHE B 1 222 ? -48.973 -14.274 24.827  1.00 37.27 ?  222 PHE B CD2 1 
ATOM   4569 C  CE1 . PHE B 1 222 ? -48.175 -16.920 24.912  1.00 40.07 ?  222 PHE B CE1 1 
ATOM   4570 C  CE2 . PHE B 1 222 ? -47.660 -14.617 24.501  1.00 35.62 ?  222 PHE B CE2 1 
ATOM   4571 C  CZ  . PHE B 1 222 ? -47.263 -15.940 24.547  1.00 34.31 ?  222 PHE B CZ  1 
ATOM   4572 N  N   . ALA B 1 223 ? -54.447 -15.050 26.050  1.00 42.51 ?  223 ALA B N   1 
ATOM   4573 C  CA  . ALA B 1 223 ? -55.601 -14.572 26.803  1.00 46.96 ?  223 ALA B CA  1 
ATOM   4574 C  C   . ALA B 1 223 ? -56.310 -15.729 27.494  1.00 51.59 ?  223 ALA B C   1 
ATOM   4575 O  O   . ALA B 1 223 ? -56.627 -15.656 28.687  1.00 50.14 ?  223 ALA B O   1 
ATOM   4576 C  CB  . ALA B 1 223 ? -56.557 -13.818 25.881  1.00 46.31 ?  223 ALA B CB  1 
ATOM   4577 N  N   . GLU B 1 224 ? -56.552 -16.817 26.758  1.00 51.29 ?  224 GLU B N   1 
ATOM   4578 C  CA  . GLU B 1 224 ? -57.142 -18.004 27.365  1.00 53.45 ?  224 GLU B CA  1 
ATOM   4579 C  C   . GLU B 1 224 ? -56.230 -18.577 28.437  1.00 57.10 ?  224 GLU B C   1 
ATOM   4580 O  O   . GLU B 1 224 ? -56.696 -18.998 29.502  1.00 59.62 ?  224 GLU B O   1 
ATOM   4581 C  CB  . GLU B 1 224 ? -57.428 -19.048 26.290  1.00 53.36 ?  224 GLU B CB  1 
ATOM   4582 N  N   . LEU B 1 225 ? -54.920 -18.565 28.185  1.00 57.08 ?  225 LEU B N   1 
ATOM   4583 C  CA  . LEU B 1 225 ? -53.970 -19.199 29.092  1.00 56.87 ?  225 LEU B CA  1 
ATOM   4584 C  C   . LEU B 1 225 ? -54.054 -18.615 30.499  1.00 61.97 ?  225 LEU B C   1 
ATOM   4585 O  O   . LEU B 1 225 ? -54.076 -19.358 31.487  1.00 66.95 ?  225 LEU B O   1 
ATOM   4586 C  CB  . LEU B 1 225 ? -52.561 -19.070 28.518  1.00 55.64 ?  225 LEU B CB  1 
ATOM   4587 C  CG  . LEU B 1 225 ? -51.417 -19.820 29.200  1.00 68.62 ?  225 LEU B CG  1 
ATOM   4588 C  CD1 . LEU B 1 225 ? -50.384 -20.256 28.178  1.00 76.47 ?  225 LEU B CD1 1 
ATOM   4589 C  CD2 . LEU B 1 225 ? -50.781 -18.942 30.274  1.00 75.10 ?  225 LEU B CD2 1 
ATOM   4590 N  N   . ARG B 1 226 ? -54.115 -17.291 30.618  1.00 55.76 ?  226 ARG B N   1 
ATOM   4591 C  CA  . ARG B 1 226 ? -54.160 -16.705 31.953  1.00 65.05 ?  226 ARG B CA  1 
ATOM   4592 C  C   . ARG B 1 226 ? -55.550 -16.744 32.591  1.00 66.79 ?  226 ARG B C   1 
ATOM   4593 O  O   . ARG B 1 226 ? -55.698 -16.294 33.732  1.00 68.86 ?  226 ARG B O   1 
ATOM   4594 C  CB  . ARG B 1 226 ? -53.621 -15.269 31.927  1.00 59.50 ?  226 ARG B CB  1 
ATOM   4595 C  CG  . ARG B 1 226 ? -54.082 -14.429 30.765  1.00 52.61 ?  226 ARG B CG  1 
ATOM   4596 C  CD  . ARG B 1 226 ? -53.562 -12.999 30.877  1.00 45.50 ?  226 ARG B CD  1 
ATOM   4597 N  NE  . ARG B 1 226 ? -54.438 -12.082 30.159  1.00 41.71 ?  226 ARG B NE  1 
ATOM   4598 C  CZ  . ARG B 1 226 ? -54.243 -10.775 30.040  1.00 43.84 ?  226 ARG B CZ  1 
ATOM   4599 N  NH1 . ARG B 1 226 ? -53.198 -10.174 30.593  1.00 37.31 ?  226 ARG B NH1 1 
ATOM   4600 N  NH2 . ARG B 1 226 ? -55.122 -10.053 29.350  1.00 42.64 ?  226 ARG B NH2 1 
ATOM   4601 N  N   . ARG B 1 227 ? -56.566 -17.268 31.899  1.00 63.04 ?  227 ARG B N   1 
ATOM   4602 C  CA  . ARG B 1 227 ? -57.844 -17.552 32.544  1.00 67.14 ?  227 ARG B CA  1 
ATOM   4603 C  C   . ARG B 1 227 ? -57.849 -18.892 33.264  1.00 72.93 ?  227 ARG B C   1 
ATOM   4604 O  O   . ARG B 1 227 ? -58.746 -19.142 34.078  1.00 76.61 ?  227 ARG B O   1 
ATOM   4605 C  CB  . ARG B 1 227 ? -58.983 -17.542 31.523  1.00 65.63 ?  227 ARG B CB  1 
ATOM   4606 C  CG  . ARG B 1 227 ? -59.454 -16.170 31.095  1.00 60.13 ?  227 ARG B CG  1 
ATOM   4607 C  CD  . ARG B 1 227 ? -60.235 -16.288 29.807  1.00 56.78 ?  227 ARG B CD  1 
ATOM   4608 N  NE  . ARG B 1 227 ? -60.089 -15.105 28.971  1.00 60.94 ?  227 ARG B NE  1 
ATOM   4609 C  CZ  . ARG B 1 227 ? -60.589 -14.996 27.749  1.00 65.89 ?  227 ARG B CZ  1 
ATOM   4610 N  NH1 . ARG B 1 227 ? -61.260 -15.990 27.188  1.00 67.09 ?  227 ARG B NH1 1 
ATOM   4611 N  NH2 . ARG B 1 227 ? -60.398 -13.867 27.068  1.00 61.01 ?  227 ARG B NH2 1 
ATOM   4612 N  N   . SER B 1 228 ? -56.849 -19.724 32.963  1.00 74.05 ?  228 SER B N   1 
ATOM   4613 C  CA  . SER B 1 228 ? -56.706 -21.030 33.655  1.00 77.46 ?  228 SER B CA  1 
ATOM   4614 C  C   . SER B 1 228 ? -55.625 -20.884 34.734  1.00 87.74 ?  228 SER B C   1 
ATOM   4615 O  O   . SER B 1 228 ? -54.694 -20.077 34.522  1.00 88.93 ?  228 SER B O   1 
ATOM   4616 C  CB  . SER B 1 228 ? -56.354 -22.112 32.673  1.00 81.65 ?  228 SER B CB  1 
ATOM   4617 O  OG  . SER B 1 228 ? -55.260 -21.714 31.860  1.00 84.38 ?  228 SER B OG  1 
ATOM   4618 N  N   . VAL B 1 235 ? -47.492 -16.441 35.238  1.00 89.41 ?  235 VAL B N   1 
ATOM   4619 C  CA  . VAL B 1 235 ? -47.072 -15.740 34.032  1.00 70.72 ?  235 VAL B CA  1 
ATOM   4620 C  C   . VAL B 1 235 ? -47.654 -14.338 34.117  1.00 62.68 ?  235 VAL B C   1 
ATOM   4621 O  O   . VAL B 1 235 ? -48.829 -14.167 34.457  1.00 68.20 ?  235 VAL B O   1 
ATOM   4622 C  CB  . VAL B 1 235 ? -47.523 -16.458 32.743  1.00 66.42 ?  235 VAL B CB  1 
ATOM   4623 C  CG1 . VAL B 1 235 ? -47.020 -17.879 32.732  1.00 70.67 ?  235 VAL B CG1 1 
ATOM   4624 C  CG2 . VAL B 1 235 ? -49.039 -16.454 32.596  1.00 68.96 ?  235 VAL B CG2 1 
ATOM   4625 N  N   . SER B 1 236 ? -46.825 -13.339 33.874  1.00 51.85 ?  236 SER B N   1 
ATOM   4626 C  CA  . SER B 1 236 ? -47.251 -11.952 33.953  1.00 45.85 ?  236 SER B CA  1 
ATOM   4627 C  C   . SER B 1 236 ? -47.539 -11.414 32.560  1.00 45.19 ?  236 SER B C   1 
ATOM   4628 O  O   . SER B 1 236 ? -47.116 -11.987 31.550  1.00 39.84 ?  236 SER B O   1 
ATOM   4629 C  CB  . SER B 1 236 ? -46.177 -11.103 34.629  1.00 46.72 ?  236 SER B CB  1 
ATOM   4630 O  OG  . SER B 1 236 ? -45.006 -11.050 33.827  1.00 42.42 ?  236 SER B OG  1 
ATOM   4631 N  N   . ASP B 1 237 ? -48.283 -10.301 32.522  1.00 42.15 ?  237 ASP B N   1 
ATOM   4632 C  CA  . ASP B 1 237 ? -48.463 -9.568  31.275  1.00 41.92 ?  237 ASP B CA  1 
ATOM   4633 C  C   . ASP B 1 237 ? -47.112 -9.221  30.661  1.00 42.30 ?  237 ASP B C   1 
ATOM   4634 O  O   . ASP B 1 237 ? -46.930 -9.322  29.443  1.00 43.49 ?  237 ASP B O   1 
ATOM   4635 C  CB  . ASP B 1 237 ? -49.271 -8.289  31.513  1.00 42.15 ?  237 ASP B CB  1 
ATOM   4636 C  CG  . ASP B 1 237 ? -50.742 -8.553  31.808  1.00 45.26 ?  237 ASP B CG  1 
ATOM   4637 O  OD1 . ASP B 1 237 ? -51.103 -9.699  32.159  1.00 44.11 ?  237 ASP B OD1 1 
ATOM   4638 O  OD2 . ASP B 1 237 ? -51.538 -7.598  31.695  1.00 47.54 ?  237 ASP B OD2 1 
ATOM   4639 N  N   . GLU B 1 238 ? -46.149 -8.821  31.501  1.00 41.91 ?  238 GLU B N   1 
ATOM   4640 C  CA  . GLU B 1 238 ? -44.809 -8.491  31.028  1.00 42.83 ?  238 GLU B CA  1 
ATOM   4641 C  C   . GLU B 1 238 ? -44.183 -9.670  30.294  1.00 40.06 ?  238 GLU B C   1 
ATOM   4642 O  O   . GLU B 1 238 ? -43.653 -9.517  29.190  1.00 35.73 ?  238 GLU B O   1 
ATOM   4643 C  CB  . GLU B 1 238 ? -43.924 -8.070  32.203  1.00 49.21 ?  238 GLU B CB  1 
ATOM   4644 N  N   . LEU B 1 239 ? -44.235 -10.858 30.894  1.00 41.33 ?  239 LEU B N   1 
ATOM   4645 C  CA  . LEU B 1 239 ? -43.651 -12.019 30.235  1.00 38.99 ?  239 LEU B CA  1 
ATOM   4646 C  C   . LEU B 1 239 ? -44.394 -12.348 28.952  1.00 34.26 ?  239 LEU B C   1 
ATOM   4647 O  O   . LEU B 1 239 ? -43.770 -12.632 27.926  1.00 34.62 ?  239 LEU B O   1 
ATOM   4648 C  CB  . LEU B 1 239 ? -43.652 -13.227 31.166  1.00 46.90 ?  239 LEU B CB  1 
ATOM   4649 C  CG  . LEU B 1 239 ? -42.867 -14.398 30.564  1.00 41.20 ?  239 LEU B CG  1 
ATOM   4650 C  CD1 . LEU B 1 239 ? -42.207 -15.171 31.683  1.00 51.29 ?  239 LEU B CD1 1 
ATOM   4651 C  CD2 . LEU B 1 239 ? -43.763 -15.308 29.730  1.00 47.34 ?  239 LEU B CD2 1 
ATOM   4652 N  N   . LEU B 1 240 ? -45.725 -12.303 28.992  1.00 32.65 ?  240 LEU B N   1 
ATOM   4653 C  CA  . LEU B 1 240 ? -46.515 -12.589 27.801  1.00 37.08 ?  240 LEU B CA  1 
ATOM   4654 C  C   . LEU B 1 240 ? -46.162 -11.629 26.674  1.00 33.99 ?  240 LEU B C   1 
ATOM   4655 O  O   . LEU B 1 240 ? -45.880 -12.052 25.546  1.00 29.99 ?  240 LEU B O   1 
ATOM   4656 C  CB  . LEU B 1 240 ? -48.005 -12.500 28.132  1.00 36.72 ?  240 LEU B CB  1 
ATOM   4657 C  CG  . LEU B 1 240 ? -48.568 -13.632 28.990  1.00 40.51 ?  240 LEU B CG  1 
ATOM   4658 C  CD1 . LEU B 1 240 ? -50.054 -13.423 29.217  1.00 41.67 ?  240 LEU B CD1 1 
ATOM   4659 C  CD2 . LEU B 1 240 ? -48.294 -14.975 28.342  1.00 38.16 ?  240 LEU B CD2 1 
ATOM   4660 N  N   . ALA B 1 241 ? -46.171 -10.326 26.966  1.00 29.28 ?  241 ALA B N   1 
ATOM   4661 C  CA  . ALA B 1 241 ? -45.838 -9.335  25.950  1.00 27.77 ?  241 ALA B CA  1 
ATOM   4662 C  C   . ALA B 1 241 ? -44.393 -9.475  25.488  1.00 27.58 ?  241 ALA B C   1 
ATOM   4663 O  O   . ALA B 1 241 ? -44.094 -9.259  24.310  1.00 28.34 ?  241 ALA B O   1 
ATOM   4664 C  CB  . ALA B 1 241 ? -46.111 -7.928  26.483  1.00 28.45 ?  241 ALA B CB  1 
ATOM   4665 N  N   . THR B 1 242 ? -43.490 -9.857  26.395  1.00 30.56 ?  242 THR B N   1 
ATOM   4666 C  CA  . THR B 1 242 ? -42.090 -10.068 26.026  1.00 29.84 ?  242 THR B CA  1 
ATOM   4667 C  C   . THR B 1 242 ? -41.960 -11.171 24.991  1.00 30.03 ?  242 THR B C   1 
ATOM   4668 O  O   . THR B 1 242 ? -41.228 -11.034 24.003  1.00 27.69 ?  242 THR B O   1 
ATOM   4669 C  CB  . THR B 1 242 ? -41.265 -10.405 27.276  1.00 29.46 ?  242 THR B CB  1 
ATOM   4670 O  OG1 . THR B 1 242 ? -41.222 -9.260  28.133  1.00 28.82 ?  242 THR B OG1 1 
ATOM   4671 C  CG2 . THR B 1 242 ? -39.836 -10.791 26.913  1.00 31.67 ?  242 THR B CG2 1 
ATOM   4672 N  N   . VAL B 1 243 ? -42.675 -12.273 25.194  1.00 26.87 ?  243 VAL B N   1 
ATOM   4673 C  CA  . VAL B 1 243 ? -42.617 -13.368 24.239  1.00 25.81 ?  243 VAL B CA  1 
ATOM   4674 C  C   . VAL B 1 243 ? -43.218 -12.942 22.904  1.00 28.78 ?  243 VAL B C   1 
ATOM   4675 O  O   . VAL B 1 243 ? -42.667 -13.240 21.837  1.00 26.27 ?  243 VAL B O   1 
ATOM   4676 C  CB  . VAL B 1 243 ? -43.320 -14.608 24.822  1.00 28.61 ?  243 VAL B CB  1 
ATOM   4677 C  CG1 . VAL B 1 243 ? -43.428 -15.702 23.773  1.00 30.00 ?  243 VAL B CG1 1 
ATOM   4678 C  CG2 . VAL B 1 243 ? -42.572 -15.101 26.044  1.00 30.82 ?  243 VAL B CG2 1 
ATOM   4679 N  N   . ALA B 1 244 ? -44.348 -12.230 22.936  1.00 25.04 ?  244 ALA B N   1 
ATOM   4680 C  CA  . ALA B 1 244 ? -44.961 -11.773 21.693  1.00 27.18 ?  244 ALA B CA  1 
ATOM   4681 C  C   . ALA B 1 244 ? -44.030 -10.824 20.935  1.00 30.34 ?  244 ALA B C   1 
ATOM   4682 O  O   . ALA B 1 244 ? -43.814 -10.986 19.726  1.00 27.59 ?  244 ALA B O   1 
ATOM   4683 C  CB  . ALA B 1 244 ? -46.302 -11.099 21.988  1.00 27.48 ?  244 ALA B CB  1 
ATOM   4684 N  N   . LEU B 1 245 ? -43.453 -9.841  21.640  1.00 24.26 ?  245 LEU B N   1 
ATOM   4685 C  CA  . LEU B 1 245 ? -42.584 -8.854  20.998  1.00 27.40 ?  245 LEU B CA  1 
ATOM   4686 C  C   . LEU B 1 245 ? -41.346 -9.509  20.390  1.00 28.95 ?  245 LEU B C   1 
ATOM   4687 O  O   . LEU B 1 245 ? -40.958 -9.195  19.257  1.00 31.34 ?  245 LEU B O   1 
ATOM   4688 C  CB  . LEU B 1 245 ? -42.154 -7.777  22.005  1.00 24.14 ?  245 LEU B CB  1 
ATOM   4689 C  CG  . LEU B 1 245 ? -41.220 -6.688  21.428  1.00 24.54 ?  245 LEU B CG  1 
ATOM   4690 C  CD1 . LEU B 1 245 ? -41.805 -6.113  20.155  1.00 21.46 ?  245 LEU B CD1 1 
ATOM   4691 C  CD2 . LEU B 1 245 ? -40.968 -5.563  22.433  1.00 22.08 ?  245 LEU B CD2 1 
ATOM   4692 N  N   . SER B 1 246 ? -40.690 -10.395 21.144  1.00 24.82 ?  246 SER B N   1 
ATOM   4693 C  CA  . SER B 1 246 ? -39.434 -10.957 20.663  1.00 31.68 ?  246 SER B CA  1 
ATOM   4694 C  C   . SER B 1 246 ? -39.661 -11.934 19.520  1.00 30.38 ?  246 SER B C   1 
ATOM   4695 O  O   . SER B 1 246 ? -38.808 -12.044 18.635  1.00 28.05 ?  246 SER B O   1 
ATOM   4696 C  CB  . SER B 1 246 ? -38.661 -11.631 21.803  1.00 34.69 ?  246 SER B CB  1 
ATOM   4697 O  OG  . SER B 1 246 ? -39.353 -12.739 22.333  1.00 40.95 ?  246 SER B OG  1 
ATOM   4698 N  N   . LEU B 1 247 ? -40.790 -12.652 19.530  1.00 28.55 ?  247 LEU B N   1 
ATOM   4699 C  CA  . LEU B 1 247 ? -41.164 -13.492 18.397  1.00 24.02 ?  247 LEU B CA  1 
ATOM   4700 C  C   . LEU B 1 247 ? -41.469 -12.656 17.164  1.00 25.89 ?  247 LEU B C   1 
ATOM   4701 O  O   . LEU B 1 247 ? -41.044 -12.995 16.053  1.00 27.58 ?  247 LEU B O   1 
ATOM   4702 C  CB  . LEU B 1 247 ? -42.373 -14.357 18.746  1.00 23.86 ?  247 LEU B CB  1 
ATOM   4703 C  CG  . LEU B 1 247 ? -42.221 -15.414 19.832  1.00 33.75 ?  247 LEU B CG  1 
ATOM   4704 C  CD1 . LEU B 1 247 ? -43.559 -16.080 20.152  1.00 32.35 ?  247 LEU B CD1 1 
ATOM   4705 C  CD2 . LEU B 1 247 ? -41.156 -16.434 19.399  1.00 29.64 ?  247 LEU B CD2 1 
ATOM   4706 N  N   . PHE B 1 248 ? -42.233 -11.578 17.334  1.00 22.61 ?  248 PHE B N   1 
ATOM   4707 C  CA  . PHE B 1 248 ? -42.481 -10.680 16.216  1.00 26.44 ?  248 PHE B CA  1 
ATOM   4708 C  C   . PHE B 1 248 ? -41.171 -10.137 15.652  1.00 22.22 ?  248 PHE B C   1 
ATOM   4709 O  O   . PHE B 1 248 ? -40.940 -10.186 14.440  1.00 26.34 ?  248 PHE B O   1 
ATOM   4710 C  CB  . PHE B 1 248 ? -43.401 -9.526  16.636  1.00 23.75 ?  248 PHE B CB  1 
ATOM   4711 C  CG  . PHE B 1 248 ? -43.708 -8.572  15.510  1.00 27.31 ?  248 PHE B CG  1 
ATOM   4712 C  CD1 . PHE B 1 248 ? -42.790 -7.593  15.134  1.00 24.33 ?  248 PHE B CD1 1 
ATOM   4713 C  CD2 . PHE B 1 248 ? -44.894 -8.679  14.804  1.00 22.25 ?  248 PHE B CD2 1 
ATOM   4714 C  CE1 . PHE B 1 248 ? -43.055 -6.743  14.079  1.00 22.90 ?  248 PHE B CE1 1 
ATOM   4715 C  CE2 . PHE B 1 248 ? -45.172 -7.824  13.757  1.00 21.68 ?  248 PHE B CE2 1 
ATOM   4716 C  CZ  . PHE B 1 248 ? -44.253 -6.854  13.386  1.00 24.49 ?  248 PHE B CZ  1 
ATOM   4717 N  N   . GLY B 1 249 ? -40.304 -9.613  16.519  1.00 25.11 ?  249 GLY B N   1 
ATOM   4718 C  CA  . GLY B 1 249 ? -39.096 -8.954  16.040  1.00 21.75 ?  249 GLY B CA  1 
ATOM   4719 C  C   . GLY B 1 249 ? -38.135 -9.912  15.366  1.00 26.06 ?  249 GLY B C   1 
ATOM   4720 O  O   . GLY B 1 249 ? -37.681 -9.672  14.238  1.00 25.60 ?  249 GLY B O   1 
ATOM   4721 N  N   . ALA B 1 250 ? -37.820 -11.017 16.044  1.00 22.69 ?  250 ALA B N   1 
ATOM   4722 C  CA  . ALA B 1 250 ? -36.857 -11.976 15.520  1.00 24.00 ?  250 ALA B CA  1 
ATOM   4723 C  C   . ALA B 1 250 ? -37.357 -12.606 14.228  1.00 22.85 ?  250 ALA B C   1 
ATOM   4724 O  O   . ALA B 1 250 ? -36.583 -12.823 13.288  1.00 25.47 ?  250 ALA B O   1 
ATOM   4725 C  CB  . ALA B 1 250 ? -36.576 -13.055 16.567  1.00 25.51 ?  250 ALA B CB  1 
ATOM   4726 N  N   . GLY B 1 251 ? -38.654 -12.880 14.157  1.00 23.40 ?  251 GLY B N   1 
ATOM   4727 C  CA  . GLY B 1 251 ? -39.207 -13.519 12.976  1.00 22.09 ?  251 GLY B CA  1 
ATOM   4728 C  C   . GLY B 1 251 ? -39.362 -12.572 11.804  1.00 23.95 ?  251 GLY B C   1 
ATOM   4729 O  O   . GLY B 1 251 ? -39.053 -12.923 10.658  1.00 22.70 ?  251 GLY B O   1 
ATOM   4730 N  N   . ALA B 1 252 ? -39.885 -11.373 12.057  1.00 22.87 ?  252 ALA B N   1 
ATOM   4731 C  CA  . ALA B 1 252 ? -40.044 -10.429 10.952  1.00 23.36 ?  252 ALA B CA  1 
ATOM   4732 C  C   . ALA B 1 252 ? -38.687 -10.029 10.375  1.00 21.59 ?  252 ALA B C   1 
ATOM   4733 O  O   . ALA B 1 252 ? -38.539 -9.908  9.152   1.00 23.19 ?  252 ALA B O   1 
ATOM   4734 C  CB  . ALA B 1 252 ? -40.824 -9.189  11.388  1.00 22.14 ?  252 ALA B CB  1 
ATOM   4735 N  N   . VAL B 1 253 ? -37.671 -9.851  11.230  1.00 20.57 ?  253 VAL B N   1 
ATOM   4736 C  CA  . VAL B 1 253 ? -36.372 -9.408  10.724  1.00 18.41 ?  253 VAL B CA  1 
ATOM   4737 C  C   . VAL B 1 253 ? -35.676 -10.535 9.963   1.00 23.52 ?  253 VAL B C   1 
ATOM   4738 O  O   . VAL B 1 253 ? -35.071 -10.302 8.915   1.00 19.14 ?  253 VAL B O   1 
ATOM   4739 C  CB  . VAL B 1 253 ? -35.493 -8.841  11.859  1.00 21.29 ?  253 VAL B CB  1 
ATOM   4740 C  CG1 . VAL B 1 253 ? -35.150 -9.892  12.929  1.00 23.36 ?  253 VAL B CG1 1 
ATOM   4741 C  CG2 . VAL B 1 253 ? -34.213 -8.226  11.277  1.00 20.56 ?  253 VAL B CG2 1 
ATOM   4742 N  N   . SER B 1 254 ? -35.789 -11.777 10.451  1.00 20.78 ?  254 SER B N   1 
ATOM   4743 C  CA  . SER B 1 254 ? -35.059 -12.899 9.872   1.00 22.11 ?  254 SER B CA  1 
ATOM   4744 C  C   . SER B 1 254 ? -35.667 -13.342 8.552   1.00 18.60 ?  254 SER B C   1 
ATOM   4745 O  O   . SER B 1 254 ? -34.938 -13.655 7.610   1.00 17.80 ?  254 SER B O   1 
ATOM   4746 C  CB  . SER B 1 254 ? -35.032 -14.073 10.857  1.00 20.43 ?  254 SER B CB  1 
ATOM   4747 O  OG  . SER B 1 254 ? -34.299 -13.727 12.020  1.00 19.67 ?  254 SER B OG  1 
ATOM   4748 N  N   . THR B 1 255 ? -36.998 -13.396 8.479   1.00 17.72 ?  255 THR B N   1 
ATOM   4749 C  CA  . THR B 1 255 ? -37.651 -13.730 7.222   1.00 18.25 ?  255 THR B CA  1 
ATOM   4750 C  C   . THR B 1 255 ? -37.444 -12.622 6.200   1.00 20.82 ?  255 THR B C   1 
ATOM   4751 O  O   . THR B 1 255 ? -37.121 -12.898 5.043   1.00 19.83 ?  255 THR B O   1 
ATOM   4752 C  CB  . THR B 1 255 ? -39.147 -13.990 7.437   1.00 16.58 ?  255 THR B CB  1 
ATOM   4753 O  OG1 . THR B 1 255 ? -39.722 -12.894 8.157   1.00 20.91 ?  255 THR B OG1 1 
ATOM   4754 C  CG2 . THR B 1 255 ? -39.368 -15.282 8.222   1.00 18.19 ?  255 THR B CG2 1 
ATOM   4755 N  N   . SER B 1 256 ? -37.637 -11.354 6.602   1.00 20.38 ?  256 SER B N   1 
ATOM   4756 C  CA  . SER B 1 256 ? -37.478 -10.270 5.634   1.00 19.27 ?  256 SER B CA  1 
ATOM   4757 C  C   . SER B 1 256 ? -36.067 -10.245 5.064   1.00 20.20 ?  256 SER B C   1 
ATOM   4758 O  O   . SER B 1 256 ? -35.881 -10.080 3.853   1.00 18.96 ?  256 SER B O   1 
ATOM   4759 C  CB  . SER B 1 256 ? -37.798 -8.906  6.252   1.00 19.61 ?  256 SER B CB  1 
ATOM   4760 O  OG  . SER B 1 256 ? -37.750 -7.909  5.227   1.00 19.01 ?  256 SER B OG  1 
ATOM   4761 N  N   . ALA B 1 257 ? -35.058 -10.383 5.923   1.00 20.11 ?  257 ALA B N   1 
ATOM   4762 C  CA  . ALA B 1 257 ? -33.681 -10.372 5.436   1.00 20.35 ?  257 ALA B CA  1 
ATOM   4763 C  C   . ALA B 1 257 ? -33.380 -11.593 4.569   1.00 21.25 ?  257 ALA B C   1 
ATOM   4764 O  O   . ALA B 1 257 ? -32.750 -11.466 3.512   1.00 19.05 ?  257 ALA B O   1 
ATOM   4765 C  CB  . ALA B 1 257 ? -32.706 -10.277 6.613   1.00 20.53 ?  257 ALA B CB  1 
ATOM   4766 N  N   . PHE B 1 258 ? -33.822 -12.787 4.977   1.00 21.96 ?  258 PHE B N   1 
ATOM   4767 C  CA  . PHE B 1 258 ? -33.542 -13.950 4.129   1.00 21.17 ?  258 PHE B CA  1 
ATOM   4768 C  C   . PHE B 1 258 ? -34.185 -13.789 2.760   1.00 16.56 ?  258 PHE B C   1 
ATOM   4769 O  O   . PHE B 1 258 ? -33.563 -14.078 1.734   1.00 17.91 ?  258 PHE B O   1 
ATOM   4770 C  CB  . PHE B 1 258 ? -34.028 -15.262 4.754   1.00 16.45 ?  258 PHE B CB  1 
ATOM   4771 C  CG  . PHE B 1 258 ? -34.081 -16.400 3.754   1.00 15.78 ?  258 PHE B CG  1 
ATOM   4772 C  CD1 . PHE B 1 258 ? -32.944 -16.750 3.017   1.00 16.86 ?  258 PHE B CD1 1 
ATOM   4773 C  CD2 . PHE B 1 258 ? -35.254 -17.087 3.514   1.00 17.76 ?  258 PHE B CD2 1 
ATOM   4774 C  CE1 . PHE B 1 258 ? -32.970 -17.774 2.072   1.00 15.41 ?  258 PHE B CE1 1 
ATOM   4775 C  CE2 . PHE B 1 258 ? -35.290 -18.128 2.569   1.00 21.12 ?  258 PHE B CE2 1 
ATOM   4776 C  CZ  . PHE B 1 258 ? -34.142 -18.463 1.846   1.00 21.40 ?  258 PHE B CZ  1 
ATOM   4777 N  N   . LEU B 1 259 ? -35.428 -13.312 2.727   1.00 17.93 ?  259 LEU B N   1 
ATOM   4778 C  CA  . LEU B 1 259 ? -36.136 -13.175 1.459   1.00 17.62 ?  259 LEU B CA  1 
ATOM   4779 C  C   . LEU B 1 259 ? -35.424 -12.206 0.522   1.00 17.63 ?  259 LEU B C   1 
ATOM   4780 O  O   . LEU B 1 259 ? -35.371 -12.428 -0.697  1.00 17.77 ?  259 LEU B O   1 
ATOM   4781 C  CB  . LEU B 1 259 ? -37.568 -12.708 1.722   1.00 15.92 ?  259 LEU B CB  1 
ATOM   4782 C  CG  . LEU B 1 259 ? -38.489 -12.617 0.509   1.00 17.66 ?  259 LEU B CG  1 
ATOM   4783 C  CD1 . LEU B 1 259 ? -38.473 -13.937 -0.263  1.00 15.36 ?  259 LEU B CD1 1 
ATOM   4784 C  CD2 . LEU B 1 259 ? -39.930 -12.253 0.921   1.00 19.51 ?  259 LEU B CD2 1 
ATOM   4785 N  N   . GLN B 1 260 ? -34.896 -11.110 1.068   1.00 16.47 ?  260 GLN B N   1 
ATOM   4786 C  CA  . GLN B 1 260 ? -34.118 -10.170 0.259   1.00 18.47 ?  260 GLN B CA  1 
ATOM   4787 C  C   . GLN B 1 260 ? -32.917 -10.854 -0.387  1.00 17.22 ?  260 GLN B C   1 
ATOM   4788 O  O   . GLN B 1 260 ? -32.647 -10.661 -1.578  1.00 19.48 ?  260 GLN B O   1 
ATOM   4789 C  CB  . GLN B 1 260 ? -33.659 -9.006  1.136   1.00 17.66 ?  260 GLN B CB  1 
ATOM   4790 C  CG  . GLN B 1 260 ? -34.750 -8.015  1.481   1.00 20.54 ?  260 GLN B CG  1 
ATOM   4791 C  CD  . GLN B 1 260 ? -34.215 -6.835  2.288   1.00 25.67 ?  260 GLN B CD  1 
ATOM   4792 O  OE1 . GLN B 1 260 ? -33.774 -5.838  1.747   1.00 27.26 ?  260 GLN B OE1 1 
ATOM   4793 N  NE2 . GLN B 1 260 ? -34.331 -6.936  3.600   1.00 34.92 ?  260 GLN B NE2 1 
ATOM   4794 N  N   . HIS B 1 261 ? -32.169 -11.644 0.388   1.00 16.59 ?  261 HIS B N   1 
ATOM   4795 C  CA  . HIS B 1 261 ? -31.039 -12.371 -0.198  1.00 20.61 ?  261 HIS B CA  1 
ATOM   4796 C  C   . HIS B 1 261 ? -31.509 -13.371 -1.258  1.00 17.03 ?  261 HIS B C   1 
ATOM   4797 O  O   . HIS B 1 261 ? -30.857 -13.543 -2.295  1.00 19.49 ?  261 HIS B O   1 
ATOM   4798 C  CB  . HIS B 1 261 ? -30.248 -13.086 0.902   1.00 18.17 ?  261 HIS B CB  1 
ATOM   4799 C  CG  . HIS B 1 261 ? -29.419 -12.167 1.751   1.00 17.72 ?  261 HIS B CG  1 
ATOM   4800 N  ND1 . HIS B 1 261 ? -28.049 -12.077 1.633   1.00 18.48 ?  261 HIS B ND1 1 
ATOM   4801 C  CD2 . HIS B 1 261 ? -29.769 -11.295 2.727   1.00 17.53 ?  261 HIS B CD2 1 
ATOM   4802 C  CE1 . HIS B 1 261 ? -27.585 -11.203 2.508   1.00 18.12 ?  261 HIS B CE1 1 
ATOM   4803 N  NE2 . HIS B 1 261 ? -28.611 -10.704 3.177   1.00 21.12 ?  261 HIS B NE2 1 
ATOM   4804 N  N   . ALA B 1 262 ? -32.645 -14.031 -1.029  1.00 15.87 ?  262 ALA B N   1 
ATOM   4805 C  CA  . ALA B 1 262 ? -33.136 -14.973 -2.035  1.00 20.54 ?  262 ALA B CA  1 
ATOM   4806 C  C   . ALA B 1 262 ? -33.502 -14.252 -3.325  1.00 19.71 ?  262 ALA B C   1 
ATOM   4807 O  O   . ALA B 1 262 ? -33.217 -14.739 -4.434  1.00 19.12 ?  262 ALA B O   1 
ATOM   4808 C  CB  . ALA B 1 262 ? -34.342 -15.744 -1.497  1.00 17.93 ?  262 ALA B CB  1 
ATOM   4809 N  N   . ILE B 1 263 ? -34.154 -13.097 -3.194  1.00 17.36 ?  263 ILE B N   1 
ATOM   4810 C  CA  . ILE B 1 263 ? -34.531 -12.303 -4.360  1.00 20.24 ?  263 ILE B CA  1 
ATOM   4811 C  C   . ILE B 1 263 ? -33.288 -11.896 -5.145  1.00 17.63 ?  263 ILE B C   1 
ATOM   4812 O  O   . ILE B 1 263 ? -33.244 -12.025 -6.374  1.00 19.89 ?  263 ILE B O   1 
ATOM   4813 C  CB  . ILE B 1 263 ? -35.365 -11.082 -3.927  1.00 17.77 ?  263 ILE B CB  1 
ATOM   4814 C  CG1 . ILE B 1 263 ? -36.750 -11.551 -3.452  1.00 21.54 ?  263 ILE B CG1 1 
ATOM   4815 C  CG2 . ILE B 1 263 ? -35.492 -10.064 -5.092  1.00 16.78 ?  263 ILE B CG2 1 
ATOM   4816 C  CD1 . ILE B 1 263 ? -37.536 -10.492 -2.703  1.00 18.42 ?  263 ILE B CD1 1 
ATOM   4817 N  N   . ILE B 1 264 ? -32.248 -11.428 -4.443  1.00 19.68 ?  264 ILE B N   1 
ATOM   4818 C  CA  . ILE B 1 264 ? -30.999 -11.059 -5.120  1.00 17.88 ?  264 ILE B CA  1 
ATOM   4819 C  C   . ILE B 1 264 ? -30.459 -12.237 -5.931  1.00 19.06 ?  264 ILE B C   1 
ATOM   4820 O  O   . ILE B 1 264 ? -30.045 -12.074 -7.084  1.00 19.71 ?  264 ILE B O   1 
ATOM   4821 C  CB  . ILE B 1 264 ? -29.963 -10.546 -4.102  1.00 18.37 ?  264 ILE B CB  1 
ATOM   4822 C  CG1 . ILE B 1 264 ? -30.302 -9.106  -3.690  1.00 17.76 ?  264 ILE B CG1 1 
ATOM   4823 C  CG2 . ILE B 1 264 ? -28.539 -10.591 -4.713  1.00 19.29 ?  264 ILE B CG2 1 
ATOM   4824 C  CD1 . ILE B 1 264 ? -29.535 -8.620  -2.485  1.00 18.56 ?  264 ILE B CD1 1 
ATOM   4825 N  N   . ALA B 1 265 ? -30.473 -13.443 -5.351  1.00 18.14 ?  265 ALA B N   1 
ATOM   4826 C  CA  . ALA B 1 265 ? -30.031 -14.627 -6.091  1.00 20.15 ?  265 ALA B CA  1 
ATOM   4827 C  C   . ALA B 1 265 ? -30.858 -14.844 -7.356  1.00 18.59 ?  265 ALA B C   1 
ATOM   4828 O  O   . ALA B 1 265 ? -30.304 -15.109 -8.427  1.00 22.96 ?  265 ALA B O   1 
ATOM   4829 C  CB  . ALA B 1 265 ? -30.096 -15.869 -5.201  1.00 17.79 ?  265 ALA B CB  1 
ATOM   4830 N  N   . LEU B 1 266 ? -32.188 -14.734 -7.254  1.00 17.53 ?  266 LEU B N   1 
ATOM   4831 C  CA  . LEU B 1 266 ? -33.051 -14.950 -8.418  1.00 17.40 ?  266 LEU B CA  1 
ATOM   4832 C  C   . LEU B 1 266 ? -32.858 -13.866 -9.471  1.00 21.42 ?  266 LEU B C   1 
ATOM   4833 O  O   . LEU B 1 266 ? -32.933 -14.141 -10.678 1.00 23.09 ?  266 LEU B O   1 
ATOM   4834 C  CB  . LEU B 1 266 ? -34.514 -14.995 -7.990  1.00 20.04 ?  266 LEU B CB  1 
ATOM   4835 C  CG  . LEU B 1 266 ? -34.957 -16.191 -7.141  1.00 24.70 ?  266 LEU B CG  1 
ATOM   4836 C  CD1 . LEU B 1 266 ? -36.474 -16.178 -6.966  1.00 19.02 ?  266 LEU B CD1 1 
ATOM   4837 C  CD2 . LEU B 1 266 ? -34.504 -17.491 -7.795  1.00 17.53 ?  266 LEU B CD2 1 
ATOM   4838 N  N   . ALA B 1 267 ? -32.656 -12.624 -9.034  1.00 17.74 ?  267 ALA B N   1 
ATOM   4839 C  CA  . ALA B 1 267 ? -32.434 -11.534 -9.977  1.00 17.23 ?  267 ALA B CA  1 
ATOM   4840 C  C   . ALA B 1 267 ? -31.093 -11.682 -10.677 1.00 20.83 ?  267 ALA B C   1 
ATOM   4841 O  O   . ALA B 1 267 ? -30.980 -11.396 -11.872 1.00 21.17 ?  267 ALA B O   1 
ATOM   4842 C  CB  . ALA B 1 267 ? -32.491 -10.197 -9.253  1.00 20.07 ?  267 ALA B CB  1 
ATOM   4843 N  N   . GLN B 1 268 ? -30.065 -12.108 -9.935  1.00 17.98 ?  268 GLN B N   1 
ATOM   4844 C  CA  . GLN B 1 268 ? -28.725 -12.224 -10.478 1.00 20.85 ?  268 GLN B CA  1 
ATOM   4845 C  C   . GLN B 1 268 ? -28.557 -13.469 -11.335 1.00 25.07 ?  268 GLN B C   1 
ATOM   4846 O  O   . GLN B 1 268 ? -27.669 -13.505 -12.194 1.00 22.08 ?  268 GLN B O   1 
ATOM   4847 C  CB  . GLN B 1 268 ? -27.705 -12.242 -9.335  1.00 17.61 ?  268 GLN B CB  1 
ATOM   4848 C  CG  . GLN B 1 268 ? -27.449 -10.865 -8.755  1.00 22.30 ?  268 GLN B CG  1 
ATOM   4849 C  CD  . GLN B 1 268 ? -26.727 -9.967  -9.738  1.00 30.83 ?  268 GLN B CD  1 
ATOM   4850 O  OE1 . GLN B 1 268 ? -27.355 -9.285  -10.556 1.00 31.29 ?  268 GLN B OE1 1 
ATOM   4851 N  NE2 . GLN B 1 268 ? -25.400 -9.966  -9.671  1.00 28.56 ?  268 GLN B NE2 1 
ATOM   4852 N  N   . GLN B 1 269 ? -29.359 -14.503 -11.086 1.00 16.77 ?  269 GLN B N   1 
ATOM   4853 C  CA  . GLN B 1 269 ? -29.226 -15.788 -11.770 1.00 19.54 ?  269 GLN B CA  1 
ATOM   4854 C  C   . GLN B 1 269 ? -30.590 -16.149 -12.341 1.00 19.61 ?  269 GLN B C   1 
ATOM   4855 O  O   . GLN B 1 269 ? -31.292 -17.009 -11.807 1.00 21.41 ?  269 GLN B O   1 
ATOM   4856 C  CB  . GLN B 1 269 ? -28.698 -16.861 -10.815 1.00 21.88 ?  269 GLN B CB  1 
ATOM   4857 C  CG  . GLN B 1 269 ? -27.302 -16.542 -10.243 1.00 20.56 ?  269 GLN B CG  1 
ATOM   4858 C  CD  . GLN B 1 269 ? -26.647 -17.747 -9.573  1.00 22.88 ?  269 GLN B CD  1 
ATOM   4859 O  OE1 . GLN B 1 269 ? -26.683 -18.872 -10.090 1.00 26.28 ?  269 GLN B OE1 1 
ATOM   4860 N  NE2 . GLN B 1 269 ? -26.053 -17.518 -8.417  1.00 22.94 ?  269 GLN B NE2 1 
ATOM   4861 N  N   . PRO B 1 270 ? -31.004 -15.495 -13.428 1.00 21.21 ?  270 PRO B N   1 
ATOM   4862 C  CA  . PRO B 1 270 ? -32.369 -15.706 -13.924 1.00 22.10 ?  270 PRO B CA  1 
ATOM   4863 C  C   . PRO B 1 270 ? -32.650 -17.144 -14.348 1.00 23.78 ?  270 PRO B C   1 
ATOM   4864 O  O   . PRO B 1 270 ? -33.825 -17.516 -14.427 1.00 21.42 ?  270 PRO B O   1 
ATOM   4865 C  CB  . PRO B 1 270 ? -32.474 -14.723 -15.100 1.00 20.55 ?  270 PRO B CB  1 
ATOM   4866 C  CG  . PRO B 1 270 ? -31.062 -14.480 -15.525 1.00 22.50 ?  270 PRO B CG  1 
ATOM   4867 C  CD  . PRO B 1 270 ? -30.250 -14.532 -14.252 1.00 22.14 ?  270 PRO B CD  1 
ATOM   4868 N  N   . GLU B 1 271 ? -31.621 -17.981 -14.565 1.00 19.36 ?  271 GLU B N   1 
ATOM   4869 C  CA  . GLU B 1 271 ? -31.880 -19.390 -14.857 1.00 21.01 ?  271 GLU B CA  1 
ATOM   4870 C  C   . GLU B 1 271 ? -32.542 -20.093 -13.674 1.00 20.41 ?  271 GLU B C   1 
ATOM   4871 O  O   . GLU B 1 271 ? -33.296 -21.047 -13.874 1.00 21.57 ?  271 GLU B O   1 
ATOM   4872 C  CB  . GLU B 1 271 ? -30.581 -20.118 -15.261 1.00 17.99 ?  271 GLU B CB  1 
ATOM   4873 C  CG  . GLU B 1 271 ? -29.629 -20.407 -14.101 1.00 19.62 ?  271 GLU B CG  1 
ATOM   4874 C  CD  . GLU B 1 271 ? -28.758 -19.200 -13.752 1.00 24.86 ?  271 GLU B CD  1 
ATOM   4875 O  OE1 . GLU B 1 271 ? -29.066 -18.087 -14.225 1.00 24.97 ?  271 GLU B OE1 1 
ATOM   4876 O  OE2 . GLU B 1 271 ? -27.768 -19.361 -13.005 1.00 26.39 ?  271 GLU B OE2 1 
ATOM   4877 N  N   . LEU B 1 272 ? -32.290 -19.629 -12.440 1.00 21.28 ?  272 LEU B N   1 
ATOM   4878 C  CA  . LEU B 1 272 ? -32.988 -20.184 -11.281 1.00 21.15 ?  272 LEU B CA  1 
ATOM   4879 C  C   . LEU B 1 272 ? -34.478 -19.864 -11.326 1.00 22.61 ?  272 LEU B C   1 
ATOM   4880 O  O   . LEU B 1 272 ? -35.315 -20.681 -10.916 1.00 20.57 ?  272 LEU B O   1 
ATOM   4881 C  CB  . LEU B 1 272 ? -32.366 -19.648 -9.982  1.00 18.62 ?  272 LEU B CB  1 
ATOM   4882 C  CG  . LEU B 1 272 ? -30.873 -19.905 -9.753  1.00 18.36 ?  272 LEU B CG  1 
ATOM   4883 C  CD1 . LEU B 1 272 ? -30.455 -19.300 -8.401  1.00 20.98 ?  272 LEU B CD1 1 
ATOM   4884 C  CD2 . LEU B 1 272 ? -30.565 -21.402 -9.783  1.00 17.62 ?  272 LEU B CD2 1 
ATOM   4885 N  N   . ALA B 1 273 ? -34.834 -18.672 -11.805 1.00 19.61 ?  273 ALA B N   1 
ATOM   4886 C  CA  . ALA B 1 273 ? -36.248 -18.339 -11.903 1.00 21.39 ?  273 ALA B CA  1 
ATOM   4887 C  C   . ALA B 1 273 ? -36.915 -19.153 -13.003 1.00 19.90 ?  273 ALA B C   1 
ATOM   4888 O  O   . ALA B 1 273 ? -38.062 -19.583 -12.849 1.00 21.82 ?  273 ALA B O   1 
ATOM   4889 C  CB  . ALA B 1 273 ? -36.429 -16.839 -12.146 1.00 16.88 ?  273 ALA B CB  1 
ATOM   4890 N  N   . ASP B 1 274 ? -36.208 -19.375 -14.120 1.00 18.55 ?  274 ASP B N   1 
ATOM   4891 C  CA  . ASP B 1 274 ? -36.744 -20.226 -15.177 1.00 20.86 ?  274 ASP B CA  1 
ATOM   4892 C  C   . ASP B 1 274 ? -37.017 -21.628 -14.648 1.00 19.57 ?  274 ASP B C   1 
ATOM   4893 O  O   . ASP B 1 274 ? -38.038 -22.231 -14.984 1.00 20.95 ?  274 ASP B O   1 
ATOM   4894 C  CB  . ASP B 1 274 ? -35.779 -20.291 -16.369 1.00 22.03 ?  274 ASP B CB  1 
ATOM   4895 C  CG  . ASP B 1 274 ? -35.978 -19.149 -17.357 1.00 25.89 ?  274 ASP B CG  1 
ATOM   4896 O  OD1 . ASP B 1 274 ? -36.957 -18.379 -17.216 1.00 22.25 ?  274 ASP B OD1 1 
ATOM   4897 O  OD2 . ASP B 1 274 ? -35.145 -19.017 -18.280 1.00 20.53 ?  274 ASP B OD2 1 
ATOM   4898 N  N   . ARG B 1 275 ? -36.119 -22.157 -13.804 1.00 20.07 ?  275 ARG B N   1 
ATOM   4899 C  CA  . ARG B 1 275 ? -36.337 -23.482 -13.224 1.00 20.01 ?  275 ARG B CA  1 
ATOM   4900 C  C   . ARG B 1 275 ? -37.593 -23.506 -12.367 1.00 22.74 ?  275 ARG B C   1 
ATOM   4901 O  O   . ARG B 1 275 ? -38.360 -24.475 -12.407 1.00 19.84 ?  275 ARG B O   1 
ATOM   4902 C  CB  . ARG B 1 275 ? -35.130 -23.903 -12.388 1.00 22.00 ?  275 ARG B CB  1 
ATOM   4903 C  CG  . ARG B 1 275 ? -35.360 -25.163 -11.550 1.00 21.17 ?  275 ARG B CG  1 
ATOM   4904 C  CD  . ARG B 1 275 ? -35.378 -26.423 -12.425 1.00 25.92 ?  275 ARG B CD  1 
ATOM   4905 N  NE  . ARG B 1 275 ? -35.442 -27.665 -11.656 1.00 23.02 ?  275 ARG B NE  1 
ATOM   4906 C  CZ  . ARG B 1 275 ? -34.411 -28.220 -11.032 1.00 22.49 ?  275 ARG B CZ  1 
ATOM   4907 N  NH1 . ARG B 1 275 ? -33.227 -27.623 -10.972 1.00 19.55 ?  275 ARG B NH1 1 
ATOM   4908 N  NH2 . ARG B 1 275 ? -34.567 -29.402 -10.449 1.00 25.09 ?  275 ARG B NH2 1 
ATOM   4909 N  N   . LEU B 1 276 ? -37.823 -22.442 -11.587 1.00 20.19 ?  276 LEU B N   1 
ATOM   4910 C  CA  . LEU B 1 276 ? -38.967 -22.424 -10.677 1.00 20.57 ?  276 LEU B CA  1 
ATOM   4911 C  C   . LEU B 1 276 ? -40.279 -22.274 -11.425 1.00 21.94 ?  276 LEU B C   1 
ATOM   4912 O  O   . LEU B 1 276 ? -41.297 -22.837 -11.005 1.00 23.68 ?  276 LEU B O   1 
ATOM   4913 C  CB  . LEU B 1 276 ? -38.811 -21.298 -9.649  1.00 19.15 ?  276 LEU B CB  1 
ATOM   4914 C  CG  . LEU B 1 276 ? -37.727 -21.597 -8.620  1.00 19.64 ?  276 LEU B CG  1 
ATOM   4915 C  CD1 . LEU B 1 276 ? -37.440 -20.377 -7.755  1.00 24.73 ?  276 LEU B CD1 1 
ATOM   4916 C  CD2 . LEU B 1 276 ? -38.146 -22.787 -7.752  1.00 19.40 ?  276 LEU B CD2 1 
ATOM   4917 N  N   . ARG B 1 277 ? -40.273 -21.534 -12.534 1.00 18.52 ?  277 ARG B N   1 
ATOM   4918 C  CA  . ARG B 1 277 ? -41.467 -21.455 -13.357 1.00 23.44 ?  277 ARG B CA  1 
ATOM   4919 C  C   . ARG B 1 277 ? -41.737 -22.779 -14.063 1.00 27.69 ?  277 ARG B C   1 
ATOM   4920 O  O   . ARG B 1 277 ? -42.895 -23.181 -14.190 1.00 24.60 ?  277 ARG B O   1 
ATOM   4921 C  CB  . ARG B 1 277 ? -41.343 -20.326 -14.380 1.00 20.44 ?  277 ARG B CB  1 
ATOM   4922 C  CG  . ARG B 1 277 ? -41.488 -18.924 -13.800 1.00 22.28 ?  277 ARG B CG  1 
ATOM   4923 C  CD  . ARG B 1 277 ? -41.601 -17.895 -14.918 1.00 24.62 ?  277 ARG B CD  1 
ATOM   4924 N  NE  . ARG B 1 277 ? -40.296 -17.586 -15.483 1.00 26.37 ?  277 ARG B NE  1 
ATOM   4925 C  CZ  . ARG B 1 277 ? -39.382 -16.821 -14.897 1.00 28.64 ?  277 ARG B CZ  1 
ATOM   4926 N  NH1 . ARG B 1 277 ? -39.634 -16.191 -13.757 1.00 23.79 ?  277 ARG B NH1 1 
ATOM   4927 N  NH2 . ARG B 1 277 ? -38.180 -16.694 -15.463 1.00 21.14 ?  277 ARG B NH2 1 
ATOM   4928 N  N   . ALA B 1 278 ? -40.686 -23.473 -14.531 1.00 22.68 ?  278 ALA B N   1 
ATOM   4929 C  CA  . ALA B 1 278 ? -40.915 -24.715 -15.264 1.00 24.53 ?  278 ALA B CA  1 
ATOM   4930 C  C   . ALA B 1 278 ? -41.297 -25.857 -14.335 1.00 21.84 ?  278 ALA B C   1 
ATOM   4931 O  O   . ALA B 1 278 ? -42.012 -26.772 -14.746 1.00 28.11 ?  278 ALA B O   1 
ATOM   4932 C  CB  . ALA B 1 278 ? -39.678 -25.107 -16.082 1.00 22.53 ?  278 ALA B CB  1 
ATOM   4933 N  N   . GLU B 1 279 ? -40.846 -25.819 -13.091 1.00 22.04 ?  279 GLU B N   1 
ATOM   4934 C  CA  . GLU B 1 279 ? -40.977 -26.941 -12.159 1.00 24.22 ?  279 GLU B CA  1 
ATOM   4935 C  C   . GLU B 1 279 ? -41.331 -26.396 -10.782 1.00 22.96 ?  279 GLU B C   1 
ATOM   4936 O  O   . GLU B 1 279 ? -40.506 -26.393 -9.864  1.00 24.47 ?  279 GLU B O   1 
ATOM   4937 C  CB  . GLU B 1 279 ? -39.676 -27.752 -12.125 1.00 24.21 ?  279 GLU B CB  1 
ATOM   4938 C  CG  . GLU B 1 279 ? -39.779 -29.120 -11.480 1.00 33.34 ?  279 GLU B CG  1 
ATOM   4939 C  CD  . GLU B 1 279 ? -38.427 -29.804 -11.347 1.00 35.81 ?  279 GLU B CD  1 
ATOM   4940 O  OE1 . GLU B 1 279 ? -37.458 -29.361 -12.007 1.00 34.36 ?  279 GLU B OE1 1 
ATOM   4941 O  OE2 . GLU B 1 279 ? -38.341 -30.795 -10.590 1.00 43.00 ?  279 GLU B OE2 1 
ATOM   4942 N  N   . PRO B 1 280 ? -42.565 -25.913 -10.605 1.00 24.89 ?  280 PRO B N   1 
ATOM   4943 C  CA  . PRO B 1 280 ? -42.923 -25.294 -9.314  1.00 24.43 ?  280 PRO B CA  1 
ATOM   4944 C  C   . PRO B 1 280 ? -42.714 -26.192 -8.106  1.00 27.61 ?  280 PRO B C   1 
ATOM   4945 O  O   . PRO B 1 280 ? -42.398 -25.676 -7.026  1.00 25.61 ?  280 PRO B O   1 
ATOM   4946 C  CB  . PRO B 1 280 ? -44.401 -24.919 -9.489  1.00 23.98 ?  280 PRO B CB  1 
ATOM   4947 C  CG  . PRO B 1 280 ? -44.661 -24.921 -10.939 1.00 24.32 ?  280 PRO B CG  1 
ATOM   4948 C  CD  . PRO B 1 280 ? -43.586 -25.696 -11.645 1.00 22.29 ?  280 PRO B CD  1 
ATOM   4949 N  N   . ALA B 1 281 ? -42.849 -27.517 -8.249  1.00 27.43 ?  281 ALA B N   1 
ATOM   4950 C  CA  . ALA B 1 281 ? -42.685 -28.402 -7.097  1.00 29.14 ?  281 ALA B CA  1 
ATOM   4951 C  C   . ALA B 1 281 ? -41.274 -28.391 -6.528  1.00 27.14 ?  281 ALA B C   1 
ATOM   4952 O  O   . ALA B 1 281 ? -41.054 -28.954 -5.447  1.00 26.08 ?  281 ALA B O   1 
ATOM   4953 C  CB  . ALA B 1 281 ? -43.058 -29.841 -7.461  1.00 24.66 ?  281 ALA B CB  1 
ATOM   4954 N  N   . VAL B 1 282 ? -40.310 -27.781 -7.225  1.00 24.82 ?  282 VAL B N   1 
ATOM   4955 C  CA  . VAL B 1 282 ? -38.943 -27.729 -6.724  1.00 22.01 ?  282 VAL B CA  1 
ATOM   4956 C  C   . VAL B 1 282 ? -38.739 -26.582 -5.739  1.00 25.89 ?  282 VAL B C   1 
ATOM   4957 O  O   . VAL B 1 282 ? -37.629 -26.429 -5.199  1.00 20.99 ?  282 VAL B O   1 
ATOM   4958 C  CB  . VAL B 1 282 ? -37.951 -27.640 -7.909  1.00 26.60 ?  282 VAL B CB  1 
ATOM   4959 C  CG1 . VAL B 1 282 ? -38.151 -26.362 -8.703  1.00 31.50 ?  282 VAL B CG1 1 
ATOM   4960 C  CG2 . VAL B 1 282 ? -36.516 -27.782 -7.436  1.00 35.29 ?  282 VAL B CG2 1 
ATOM   4961 N  N   . ILE B 1 283 ? -39.787 -25.793 -5.464  1.00 22.85 ?  283 ILE B N   1 
ATOM   4962 C  CA  . ILE B 1 283 ? -39.647 -24.616 -4.605  1.00 22.96 ?  283 ILE B CA  1 
ATOM   4963 C  C   . ILE B 1 283 ? -39.099 -25.005 -3.234  1.00 22.31 ?  283 ILE B C   1 
ATOM   4964 O  O   . ILE B 1 283 ? -38.303 -24.268 -2.641  1.00 22.53 ?  283 ILE B O   1 
ATOM   4965 C  CB  . ILE B 1 283 ? -40.988 -23.858 -4.495  1.00 25.44 ?  283 ILE B CB  1 
ATOM   4966 C  CG1 . ILE B 1 283 ? -40.806 -22.509 -3.787  1.00 22.20 ?  283 ILE B CG1 1 
ATOM   4967 C  CG2 . ILE B 1 283 ? -42.025 -24.659 -3.720  1.00 26.86 ?  283 ILE B CG2 1 
ATOM   4968 C  CD1 . ILE B 1 283 ? -39.835 -21.580 -4.453  1.00 23.23 ?  283 ILE B CD1 1 
ATOM   4969 N  N   . GLY B 1 284 ? -39.485 -26.171 -2.721  1.00 22.14 ?  284 GLY B N   1 
ATOM   4970 C  CA  . GLY B 1 284 ? -39.000 -26.575 -1.409  1.00 21.18 ?  284 GLY B CA  1 
ATOM   4971 C  C   . GLY B 1 284 ? -37.494 -26.798 -1.388  1.00 22.63 ?  284 GLY B C   1 
ATOM   4972 O  O   . GLY B 1 284 ? -36.787 -26.274 -0.518  1.00 21.45 ?  284 GLY B O   1 
ATOM   4973 N  N   . ARG B 1 285 ? -36.992 -27.592 -2.342  1.00 21.07 ?  285 ARG B N   1 
ATOM   4974 C  CA  . ARG B 1 285 ? -35.552 -27.792 -2.508  1.00 23.22 ?  285 ARG B CA  1 
ATOM   4975 C  C   . ARG B 1 285 ? -34.835 -26.482 -2.780  1.00 21.67 ?  285 ARG B C   1 
ATOM   4976 O  O   . ARG B 1 285 ? -33.731 -26.253 -2.275  1.00 21.82 ?  285 ARG B O   1 
ATOM   4977 C  CB  . ARG B 1 285 ? -35.273 -28.734 -3.685  1.00 27.10 ?  285 ARG B CB  1 
ATOM   4978 C  CG  . ARG B 1 285 ? -35.815 -30.147 -3.583  1.00 34.36 ?  285 ARG B CG  1 
ATOM   4979 C  CD  . ARG B 1 285 ? -35.137 -30.877 -2.406  1.00 30.42 ?  285 ARG B CD  1 
ATOM   4980 N  NE  . ARG B 1 285 ? -33.697 -30.956 -2.623  1.00 42.60 ?  285 ARG B NE  1 
ATOM   4981 C  CZ  . ARG B 1 285 ? -33.087 -31.864 -3.378  1.00 42.73 ?  285 ARG B CZ  1 
ATOM   4982 N  NH1 . ARG B 1 285 ? -33.759 -32.842 -3.967  1.00 34.19 ?  285 ARG B NH1 1 
ATOM   4983 N  NH2 . ARG B 1 285 ? -31.768 -31.782 -3.554  1.00 46.78 ?  285 ARG B NH2 1 
ATOM   4984 N  N   . ALA B 1 286 ? -35.411 -25.647 -3.644  1.00 21.06 ?  286 ALA B N   1 
ATOM   4985 C  CA  . ALA B 1 286 ? -34.758 -24.397 -4.017  1.00 21.88 ?  286 ALA B CA  1 
ATOM   4986 C  C   . ALA B 1 286 ? -34.535 -23.524 -2.791  1.00 19.15 ?  286 ALA B C   1 
ATOM   4987 O  O   . ALA B 1 286 ? -33.405 -23.121 -2.498  1.00 20.34 ?  286 ALA B O   1 
ATOM   4988 C  CB  . ALA B 1 286 ? -35.597 -23.672 -5.070  1.00 21.61 ?  286 ALA B CB  1 
ATOM   4989 N  N   . VAL B 1 287 ? -35.600 -23.277 -2.028  1.00 20.30 ?  287 VAL B N   1 
ATOM   4990 C  CA  . VAL B 1 287 ? -35.499 -22.468 -0.812  1.00 19.97 ?  287 VAL B CA  1 
ATOM   4991 C  C   . VAL B 1 287 ? -34.519 -23.092 0.173   1.00 18.56 ?  287 VAL B C   1 
ATOM   4992 O  O   . VAL B 1 287 ? -33.763 -22.383 0.848   1.00 19.39 ?  287 VAL B O   1 
ATOM   4993 C  CB  . VAL B 1 287 ? -36.893 -22.275 -0.184  1.00 19.47 ?  287 VAL B CB  1 
ATOM   4994 C  CG1 . VAL B 1 287 ? -36.782 -21.719 1.247   1.00 21.08 ?  287 VAL B CG1 1 
ATOM   4995 C  CG2 . VAL B 1 287 ? -37.754 -21.360 -1.059  1.00 17.66 ?  287 VAL B CG2 1 
ATOM   4996 N  N   . ASP B 1 288 ? -34.499 -24.426 0.258   1.00 19.66 ?  288 ASP B N   1 
ATOM   4997 C  CA  . ASP B 1 288 ? -33.533 -25.089 1.132   1.00 20.47 ?  288 ASP B CA  1 
ATOM   4998 C  C   . ASP B 1 288 ? -32.101 -24.768 0.714   1.00 19.77 ?  288 ASP B C   1 
ATOM   4999 O  O   . ASP B 1 288 ? -31.236 -24.552 1.568   1.00 19.78 ?  288 ASP B O   1 
ATOM   5000 C  CB  . ASP B 1 288 ? -33.766 -26.607 1.122   1.00 21.57 ?  288 ASP B CB  1 
ATOM   5001 C  CG  . ASP B 1 288 ? -33.199 -27.297 2.351   1.00 27.82 ?  288 ASP B CG  1 
ATOM   5002 O  OD1 . ASP B 1 288 ? -33.382 -26.780 3.467   1.00 29.27 ?  288 ASP B OD1 1 
ATOM   5003 O  OD2 . ASP B 1 288 ? -32.567 -28.370 2.208   1.00 33.71 ?  288 ASP B OD2 1 
ATOM   5004 N  N   . GLU B 1 289 ? -31.833 -24.737 -0.595  1.00 18.53 ?  289 GLU B N   1 
ATOM   5005 C  CA  . GLU B 1 289 ? -30.494 -24.387 -1.075  1.00 18.78 ?  289 GLU B CA  1 
ATOM   5006 C  C   . GLU B 1 289 ? -30.214 -22.887 -0.925  1.00 19.89 ?  289 GLU B C   1 
ATOM   5007 O  O   . GLU B 1 289 ? -29.106 -22.489 -0.543  1.00 18.59 ?  289 GLU B O   1 
ATOM   5008 C  CB  . GLU B 1 289 ? -30.326 -24.841 -2.534  1.00 19.61 ?  289 GLU B CB  1 
ATOM   5009 C  CG  . GLU B 1 289 ? -29.126 -24.226 -3.277  1.00 18.01 ?  289 GLU B CG  1 
ATOM   5010 C  CD  . GLU B 1 289 ? -27.788 -24.763 -2.780  1.00 21.95 ?  289 GLU B CD  1 
ATOM   5011 O  OE1 . GLU B 1 289 ? -27.759 -25.376 -1.685  1.00 21.94 ?  289 GLU B OE1 1 
ATOM   5012 O  OE2 . GLU B 1 289 ? -26.759 -24.568 -3.481  1.00 22.45 ?  289 GLU B OE2 1 
ATOM   5013 N  N   . LEU B 1 290 ? -31.208 -22.036 -1.196  1.00 17.81 ?  290 LEU B N   1 
ATOM   5014 C  CA  . LEU B 1 290 ? -31.032 -20.606 -0.957  1.00 16.65 ?  290 LEU B CA  1 
ATOM   5015 C  C   . LEU B 1 290 ? -30.732 -20.321 0.518   1.00 19.44 ?  290 LEU B C   1 
ATOM   5016 O  O   . LEU B 1 290 ? -29.940 -19.421 0.841   1.00 20.61 ?  290 LEU B O   1 
ATOM   5017 C  CB  . LEU B 1 290 ? -32.278 -19.849 -1.436  1.00 18.17 ?  290 LEU B CB  1 
ATOM   5018 C  CG  . LEU B 1 290 ? -32.454 -19.880 -2.959  1.00 21.36 ?  290 LEU B CG  1 
ATOM   5019 C  CD1 . LEU B 1 290 ? -33.783 -19.278 -3.459  1.00 17.56 ?  290 LEU B CD1 1 
ATOM   5020 C  CD2 . LEU B 1 290 ? -31.286 -19.141 -3.590  1.00 17.04 ?  290 LEU B CD2 1 
ATOM   5021 N  N   . LEU B 1 291 ? -31.332 -21.101 1.424   1.00 17.27 ?  291 LEU B N   1 
ATOM   5022 C  CA  . LEU B 1 291 ? -31.028 -20.994 2.848   1.00 19.05 ?  291 LEU B CA  1 
ATOM   5023 C  C   . LEU B 1 291 ? -29.555 -21.306 3.127   1.00 17.27 ?  291 LEU B C   1 
ATOM   5024 O  O   . LEU B 1 291 ? -28.857 -20.528 3.791   1.00 20.72 ?  291 LEU B O   1 
ATOM   5025 C  CB  . LEU B 1 291 ? -31.964 -21.928 3.641   1.00 18.22 ?  291 LEU B CB  1 
ATOM   5026 C  CG  . LEU B 1 291 ? -33.386 -21.388 3.911   1.00 17.05 ?  291 LEU B CG  1 
ATOM   5027 C  CD1 . LEU B 1 291 ? -34.372 -22.481 4.294   1.00 20.50 ?  291 LEU B CD1 1 
ATOM   5028 C  CD2 . LEU B 1 291 ? -33.350 -20.297 5.006   1.00 17.65 ?  291 LEU B CD2 1 
ATOM   5029 N  N   . ARG B 1 292 ? -29.050 -22.429 2.606   1.00 18.38 ?  292 ARG B N   1 
ATOM   5030 C  CA  . ARG B 1 292 ? -27.613 -22.702 2.723   1.00 21.39 ?  292 ARG B CA  1 
ATOM   5031 C  C   . ARG B 1 292 ? -26.785 -21.528 2.218   1.00 20.19 ?  292 ARG B C   1 
ATOM   5032 O  O   . ARG B 1 292 ? -25.803 -21.122 2.850   1.00 20.09 ?  292 ARG B O   1 
ATOM   5033 C  CB  . ARG B 1 292 ? -27.227 -23.957 1.930   1.00 20.72 ?  292 ARG B CB  1 
ATOM   5034 C  CG  . ARG B 1 292 ? -25.715 -24.225 1.937   1.00 19.17 ?  292 ARG B CG  1 
ATOM   5035 C  CD  . ARG B 1 292 ? -25.304 -25.277 0.913   1.00 21.86 ?  292 ARG B CD  1 
ATOM   5036 N  NE  . ARG B 1 292 ? -25.307 -24.753 -0.450  1.00 20.86 ?  292 ARG B NE  1 
ATOM   5037 C  CZ  . ARG B 1 292 ? -24.309 -24.044 -0.965  1.00 19.94 ?  292 ARG B CZ  1 
ATOM   5038 N  NH1 . ARG B 1 292 ? -23.216 -23.781 -0.264  1.00 19.26 ?  292 ARG B NH1 1 
ATOM   5039 N  NH2 . ARG B 1 292 ? -24.417 -23.570 -2.207  1.00 20.43 ?  292 ARG B NH2 1 
ATOM   5040 N  N   . TYR B 1 293 ? -27.182 -20.973 1.078   1.00 17.77 ?  293 TYR B N   1 
ATOM   5041 C  CA  . TYR B 1 293 ? -26.405 -19.947 0.396   1.00 16.81 ?  293 TYR B CA  1 
ATOM   5042 C  C   . TYR B 1 293 ? -26.454 -18.602 1.108   1.00 21.87 ?  293 TYR B C   1 
ATOM   5043 O  O   . TYR B 1 293 ? -25.504 -17.814 1.008   1.00 20.81 ?  293 TYR B O   1 
ATOM   5044 C  CB  . TYR B 1 293 ? -26.952 -19.786 -1.021  1.00 18.01 ?  293 TYR B CB  1 
ATOM   5045 C  CG  . TYR B 1 293 ? -25.964 -19.209 -1.996  1.00 24.46 ?  293 TYR B CG  1 
ATOM   5046 C  CD1 . TYR B 1 293 ? -24.866 -19.945 -2.387  1.00 20.84 ?  293 TYR B CD1 1 
ATOM   5047 C  CD2 . TYR B 1 293 ? -26.131 -17.932 -2.529  1.00 21.27 ?  293 TYR B CD2 1 
ATOM   5048 C  CE1 . TYR B 1 293 ? -23.947 -19.443 -3.292  1.00 25.26 ?  293 TYR B CE1 1 
ATOM   5049 C  CE2 . TYR B 1 293 ? -25.207 -17.414 -3.440  1.00 24.81 ?  293 TYR B CE2 1 
ATOM   5050 C  CZ  . TYR B 1 293 ? -24.123 -18.193 -3.816  1.00 24.54 ?  293 TYR B CZ  1 
ATOM   5051 O  OH  . TYR B 1 293 ? -23.186 -17.744 -4.710  1.00 30.46 ?  293 TYR B OH  1 
ATOM   5052 N  N   . ASN B 1 294 ? -27.555 -18.311 1.802   1.00 17.97 ?  294 ASN B N   1 
ATOM   5053 C  CA  . ASN B 1 294 ? -27.872 -16.943 2.177   1.00 18.44 ?  294 ASN B CA  1 
ATOM   5054 C  C   . ASN B 1 294 ? -26.970 -16.417 3.293   1.00 21.01 ?  294 ASN B C   1 
ATOM   5055 O  O   . ASN B 1 294 ? -26.580 -17.144 4.221   1.00 18.66 ?  294 ASN B O   1 
ATOM   5056 C  CB  . ASN B 1 294 ? -29.342 -16.833 2.592   1.00 16.96 ?  294 ASN B CB  1 
ATOM   5057 C  CG  . ASN B 1 294 ? -29.659 -17.635 3.822   1.00 18.46 ?  294 ASN B CG  1 
ATOM   5058 O  OD1 . ASN B 1 294 ? -28.819 -17.762 4.712   1.00 19.44 ?  294 ASN B OD1 1 
ATOM   5059 N  ND2 . ASN B 1 294 ? -30.875 -18.191 3.888   1.00 20.60 ?  294 ASN B ND2 1 
ATOM   5060 N  N   . LEU B 1 295 ? -26.670 -15.116 3.199   1.00 18.81 ?  295 LEU B N   1 
ATOM   5061 C  CA  . LEU B 1 295 ? -25.738 -14.420 4.081   1.00 18.18 ?  295 LEU B CA  1 
ATOM   5062 C  C   . LEU B 1 295 ? -26.431 -13.386 4.962   1.00 19.10 ?  295 LEU B C   1 
ATOM   5063 O  O   . LEU B 1 295 ? -25.774 -12.473 5.468   1.00 17.37 ?  295 LEU B O   1 
ATOM   5064 C  CB  . LEU B 1 295 ? -24.644 -13.753 3.250   1.00 20.02 ?  295 LEU B CB  1 
ATOM   5065 C  CG  . LEU B 1 295 ? -23.835 -14.732 2.397   1.00 25.02 ?  295 LEU B CG  1 
ATOM   5066 C  CD1 . LEU B 1 295 ? -22.846 -14.026 1.462   1.00 22.36 ?  295 LEU B CD1 1 
ATOM   5067 C  CD2 . LEU B 1 295 ? -23.110 -15.714 3.311   1.00 20.80 ?  295 LEU B CD2 1 
ATOM   5068 N  N   . SER B 1 296 ? -27.743 -13.525 5.160   1.00 18.65 ?  296 SER B N   1 
ATOM   5069 C  CA  . SER B 1 296 ? -28.508 -12.574 5.962   1.00 17.74 ?  296 SER B CA  1 
ATOM   5070 C  C   . SER B 1 296 ? -28.041 -12.525 7.411   1.00 21.82 ?  296 SER B C   1 
ATOM   5071 O  O   . SER B 1 296 ? -28.210 -11.499 8.083   1.00 21.34 ?  296 SER B O   1 
ATOM   5072 C  CB  . SER B 1 296 ? -29.997 -12.934 5.925   1.00 20.95 ?  296 SER B CB  1 
ATOM   5073 O  OG  . SER B 1 296 ? -30.251 -14.109 6.692   1.00 17.26 ?  296 SER B OG  1 
ATOM   5074 N  N   . ILE B 1 297 ? -27.496 -13.621 7.930   1.00 21.06 ?  297 ILE B N   1 
ATOM   5075 C  CA  . ILE B 1 297 ? -26.979 -13.600 9.295   1.00 21.04 ?  297 ILE B CA  1 
ATOM   5076 C  C   . ILE B 1 297 ? -25.679 -12.801 9.286   1.00 18.38 ?  297 ILE B C   1 
ATOM   5077 O  O   . ILE B 1 297 ? -24.675 -13.244 8.724   1.00 21.76 ?  297 ILE B O   1 
ATOM   5078 C  CB  . ILE B 1 297 ? -26.760 -15.015 9.840   1.00 20.07 ?  297 ILE B CB  1 
ATOM   5079 C  CG1 . ILE B 1 297 ? -28.100 -15.738 9.987   1.00 25.89 ?  297 ILE B CG1 1 
ATOM   5080 C  CG2 . ILE B 1 297 ? -26.033 -14.957 11.179  1.00 17.89 ?  297 ILE B CG2 1 
ATOM   5081 C  CD1 . ILE B 1 297 ? -27.953 -17.203 10.423  1.00 25.00 ?  297 ILE B CD1 1 
ATOM   5082 N  N   . GLY B 1 298 ? -25.694 -11.622 9.901   1.00 20.72 ?  298 GLY B N   1 
ATOM   5083 C  CA  . GLY B 1 298 ? -24.585 -10.692 9.827   1.00 17.87 ?  298 GLY B CA  1 
ATOM   5084 C  C   . GLY B 1 298 ? -23.672 -10.691 11.033  1.00 24.65 ?  298 GLY B C   1 
ATOM   5085 O  O   . GLY B 1 298 ? -22.683 -9.945  11.041  1.00 22.55 ?  298 GLY B O   1 
ATOM   5086 N  N   . ASP B 1 299 ? -23.977 -11.492 12.055  1.00 17.79 ?  299 ASP B N   1 
ATOM   5087 C  CA  . ASP B 1 299 ? -23.139 -11.707 13.228  1.00 25.12 ?  299 ASP B CA  1 
ATOM   5088 C  C   . ASP B 1 299 ? -23.047 -13.237 13.313  1.00 20.50 ?  299 ASP B C   1 
ATOM   5089 O  O   . ASP B 1 299 ? -23.671 -13.951 12.504  1.00 23.26 ?  299 ASP B O   1 
ATOM   5090 C  CB  . ASP B 1 299 ? -23.903 -11.273 14.489  1.00 21.30 ?  299 ASP B CB  1 
ATOM   5091 C  CG  . ASP B 1 299 ? -25.163 -12.108 14.764  1.00 27.34 ?  299 ASP B CG  1 
ATOM   5092 O  OD1 . ASP B 1 299 ? -25.594 -12.876 13.888  1.00 25.86 ?  299 ASP B OD1 1 
ATOM   5093 O  OD2 . ASP B 1 299 ? -25.729 -12.004 15.888  1.00 25.99 ?  299 ASP B OD2 1 
ATOM   5094 N  N   . ALA B 1 300 ? -22.291 -13.739 14.279  1.00 22.47 ?  300 ALA B N   1 
ATOM   5095 C  CA  . ALA B 1 300 ? -22.287 -15.161 14.593  1.00 25.38 ?  300 ALA B CA  1 
ATOM   5096 C  C   . ALA B 1 300 ? -23.177 -15.651 15.723  1.00 24.31 ?  300 ALA B C   1 
ATOM   5097 O  O   . ALA B 1 300 ? -23.668 -14.852 16.518  1.00 23.52 ?  300 ALA B O   1 
ATOM   5098 C  CB  . ALA B 1 300 ? -20.811 -15.467 14.866  1.00 22.17 ?  300 ALA B CB  1 
ATOM   5099 N  N   . LEU B 1 301 ? -23.407 -16.966 15.782  1.00 22.02 ?  301 LEU B N   1 
ATOM   5100 C  CA  . LEU B 1 301 ? -24.233 -17.516 16.853  1.00 22.54 ?  301 LEU B CA  1 
ATOM   5101 C  C   . LEU B 1 301 ? -23.388 -17.613 18.115  1.00 25.68 ?  301 LEU B C   1 
ATOM   5102 O  O   . LEU B 1 301 ? -22.387 -18.335 18.123  1.00 25.09 ?  301 LEU B O   1 
ATOM   5103 C  CB  . LEU B 1 301 ? -24.799 -18.890 16.499  1.00 24.54 ?  301 LEU B CB  1 
ATOM   5104 C  CG  . LEU B 1 301 ? -25.588 -19.029 15.194  1.00 29.06 ?  301 LEU B CG  1 
ATOM   5105 C  CD1 . LEU B 1 301 ? -26.406 -20.319 15.183  1.00 26.91 ?  301 LEU B CD1 1 
ATOM   5106 C  CD2 . LEU B 1 301 ? -26.494 -17.812 14.962  1.00 26.85 ?  301 LEU B CD2 1 
ATOM   5107 N  N   . PRO B 1 302 ? -23.735 -16.903 19.178  1.00 25.50 ?  302 PRO B N   1 
ATOM   5108 C  CA  . PRO B 1 302 ? -22.846 -16.791 20.334  1.00 23.94 ?  302 PRO B CA  1 
ATOM   5109 C  C   . PRO B 1 302 ? -23.147 -17.801 21.434  1.00 25.43 ?  302 PRO B C   1 
ATOM   5110 O  O   . PRO B 1 302 ? -24.294 -18.166 21.697  1.00 26.50 ?  302 PRO B O   1 
ATOM   5111 C  CB  . PRO B 1 302 ? -23.134 -15.366 20.821  1.00 21.36 ?  302 PRO B CB  1 
ATOM   5112 C  CG  . PRO B 1 302 ? -24.613 -15.178 20.511  1.00 27.15 ?  302 PRO B CG  1 
ATOM   5113 C  CD  . PRO B 1 302 ? -24.928 -16.044 19.300  1.00 23.58 ?  302 PRO B CD  1 
ATOM   5114 N  N   . ARG B 1 303 ? -22.081 -18.249 22.092  1.00 26.64 ?  303 ARG B N   1 
ATOM   5115 C  CA  . ARG B 1 303 ? -22.191 -19.164 23.221  1.00 25.87 ?  303 ARG B CA  1 
ATOM   5116 C  C   . ARG B 1 303 ? -21.113 -18.813 24.235  1.00 28.67 ?  303 ARG B C   1 
ATOM   5117 O  O   . ARG B 1 303 ? -20.021 -18.376 23.862  1.00 28.61 ?  303 ARG B O   1 
ATOM   5118 C  CB  . ARG B 1 303 ? -22.024 -20.639 22.800  1.00 28.97 ?  303 ARG B CB  1 
ATOM   5119 C  CG  . ARG B 1 303 ? -22.968 -21.134 21.719  1.00 22.55 ?  303 ARG B CG  1 
ATOM   5120 C  CD  . ARG B 1 303 ? -24.337 -21.402 22.278  1.00 28.20 ?  303 ARG B CD  1 
ATOM   5121 N  NE  . ARG B 1 303 ? -25.223 -22.043 21.309  1.00 27.76 ?  303 ARG B NE  1 
ATOM   5122 C  CZ  . ARG B 1 303 ? -26.076 -21.391 20.531  1.00 32.81 ?  303 ARG B CZ  1 
ATOM   5123 N  NH1 . ARG B 1 303 ? -26.148 -20.068 20.547  1.00 25.19 ?  303 ARG B NH1 1 
ATOM   5124 N  NH2 . ARG B 1 303 ? -26.887 -22.083 19.725  1.00 23.96 ?  303 ARG B NH2 1 
ATOM   5125 N  N   . ILE B 1 304 ? -21.417 -18.999 25.529  1.00 24.61 ?  304 ILE B N   1 
ATOM   5126 C  CA  . ILE B 1 304 ? -20.368 -19.005 26.552  1.00 28.87 ?  304 ILE B CA  1 
ATOM   5127 C  C   . ILE B 1 304 ? -20.032 -20.454 26.895  1.00 29.44 ?  304 ILE B C   1 
ATOM   5128 O  O   . ILE B 1 304 ? -20.928 -21.299 27.062  1.00 27.16 ?  304 ILE B O   1 
ATOM   5129 C  CB  . ILE B 1 304 ? -20.760 -18.213 27.819  1.00 29.17 ?  304 ILE B CB  1 
ATOM   5130 C  CG1 . ILE B 1 304 ? -21.149 -16.771 27.473  1.00 25.14 ?  304 ILE B CG1 1 
ATOM   5131 C  CG2 . ILE B 1 304 ? -19.593 -18.194 28.831  1.00 26.22 ?  304 ILE B CG2 1 
ATOM   5132 C  CD1 . ILE B 1 304 ? -19.994 -15.913 27.004  1.00 28.06 ?  304 ILE B CD1 1 
ATOM   5133 N  N   . ALA B 1 305 ? -18.740 -20.744 26.989  1.00 27.74 ?  305 ALA B N   1 
ATOM   5134 C  CA  . ALA B 1 305 ? -18.292 -22.064 27.417  1.00 29.04 ?  305 ALA B CA  1 
ATOM   5135 C  C   . ALA B 1 305 ? -18.564 -22.239 28.905  1.00 35.43 ?  305 ALA B C   1 
ATOM   5136 O  O   . ALA B 1 305 ? -18.103 -21.439 29.724  1.00 31.12 ?  305 ALA B O   1 
ATOM   5137 C  CB  . ALA B 1 305 ? -16.803 -22.233 27.131  1.00 30.28 ?  305 ALA B CB  1 
ATOM   5138 N  N   . LEU B 1 306 ? -19.318 -23.279 29.260  1.00 36.14 ?  306 LEU B N   1 
ATOM   5139 C  CA  . LEU B 1 306 ? -19.503 -23.585 30.669  1.00 36.25 ?  306 LEU B CA  1 
ATOM   5140 C  C   . LEU B 1 306 ? -18.348 -24.388 31.246  1.00 42.14 ?  306 LEU B C   1 
ATOM   5141 O  O   . LEU B 1 306 ? -18.224 -24.479 32.474  1.00 39.18 ?  306 LEU B O   1 
ATOM   5142 C  CB  . LEU B 1 306 ? -20.811 -24.338 30.873  1.00 36.21 ?  306 LEU B CB  1 
ATOM   5143 C  CG  . LEU B 1 306 ? -22.020 -23.536 30.416  1.00 36.86 ?  306 LEU B CG  1 
ATOM   5144 C  CD1 . LEU B 1 306 ? -23.288 -24.364 30.553  1.00 40.73 ?  306 LEU B CD1 1 
ATOM   5145 C  CD2 . LEU B 1 306 ? -22.103 -22.249 31.223  1.00 39.57 ?  306 LEU B CD2 1 
ATOM   5146 N  N   . ALA B 1 307 ? -17.495 -24.949 30.394  1.00 38.48 ?  307 ALA B N   1 
ATOM   5147 C  CA  . ALA B 1 307 ? -16.382 -25.763 30.848  1.00 37.44 ?  307 ALA B CA  1 
ATOM   5148 C  C   . ALA B 1 307 ? -15.266 -25.642 29.829  1.00 37.76 ?  307 ALA B C   1 
ATOM   5149 O  O   . ALA B 1 307 ? -15.480 -25.185 28.703  1.00 39.24 ?  307 ALA B O   1 
ATOM   5150 C  CB  . ALA B 1 307 ? -16.804 -27.230 31.032  1.00 33.72 ?  307 ALA B CB  1 
ATOM   5151 N  N   . ASP B 1 308 ? -14.067 -26.053 30.231  1.00 37.49 ?  308 ASP B N   1 
ATOM   5152 C  CA  . ASP B 1 308 ? -12.994 -26.196 29.260  1.00 37.01 ?  308 ASP B CA  1 
ATOM   5153 C  C   . ASP B 1 308 ? -13.392 -27.245 28.227  1.00 41.33 ?  308 ASP B C   1 
ATOM   5154 O  O   . ASP B 1 308 ? -13.869 -28.328 28.578  1.00 39.34 ?  308 ASP B O   1 
ATOM   5155 C  CB  . ASP B 1 308 ? -11.688 -26.592 29.949  1.00 43.15 ?  308 ASP B CB  1 
ATOM   5156 C  CG  . ASP B 1 308 ? -11.169 -25.520 30.897  1.00 44.55 ?  308 ASP B CG  1 
ATOM   5157 O  OD1 . ASP B 1 308 ? -11.715 -24.395 30.912  1.00 42.16 ?  308 ASP B OD1 1 
ATOM   5158 O  OD2 . ASP B 1 308 ? -10.182 -25.793 31.621  1.00 49.43 ?  308 ASP B OD2 1 
ATOM   5159 N  N   . VAL B 1 309 ? -13.224 -26.912 26.949  1.00 41.78 ?  309 VAL B N   1 
ATOM   5160 C  CA  . VAL B 1 309 ? -13.588 -27.809 25.857  1.00 39.71 ?  309 VAL B CA  1 
ATOM   5161 C  C   . VAL B 1 309 ? -12.511 -27.733 24.789  1.00 40.74 ?  309 VAL B C   1 
ATOM   5162 O  O   . VAL B 1 309 ? -12.164 -26.640 24.331  1.00 39.95 ?  309 VAL B O   1 
ATOM   5163 C  CB  . VAL B 1 309 ? -14.956 -27.460 25.241  1.00 37.63 ?  309 VAL B CB  1 
ATOM   5164 C  CG1 . VAL B 1 309 ? -15.190 -28.304 23.993  1.00 39.86 ?  309 VAL B CG1 1 
ATOM   5165 C  CG2 . VAL B 1 309 ? -16.078 -27.652 26.245  1.00 37.86 ?  309 VAL B CG2 1 
ATOM   5166 N  N   . ARG B 1 310 ? -11.975 -28.887 24.396  1.00 46.70 ?  310 ARG B N   1 
ATOM   5167 C  CA  . ARG B 1 310 ? -11.054 -28.939 23.269  1.00 39.57 ?  310 ARG B CA  1 
ATOM   5168 C  C   . ARG B 1 310 ? -11.874 -28.967 21.989  1.00 39.23 ?  310 ARG B C   1 
ATOM   5169 O  O   . ARG B 1 310 ? -12.704 -29.865 21.792  1.00 37.98 ?  310 ARG B O   1 
ATOM   5170 C  CB  . ARG B 1 310 ? -10.136 -30.155 23.356  1.00 46.14 ?  310 ARG B CB  1 
ATOM   5171 C  CG  . ARG B 1 310 ? -9.064  -30.200 22.264  1.00 40.27 ?  310 ARG B CG  1 
ATOM   5172 C  CD  . ARG B 1 310 ? -8.110  -31.372 22.441  1.00 46.22 ?  310 ARG B CD  1 
ATOM   5173 N  NE  . ARG B 1 310 ? -7.114  -31.405 21.374  1.00 52.10 ?  310 ARG B NE  1 
ATOM   5174 C  CZ  . ARG B 1 310 ? -5.998  -30.687 21.366  1.00 56.26 ?  310 ARG B CZ  1 
ATOM   5175 N  NH1 . ARG B 1 310 ? -5.678  -29.888 22.377  1.00 53.69 ?  310 ARG B NH1 1 
ATOM   5176 N  NH2 . ARG B 1 310 ? -5.192  -30.754 20.308  1.00 53.98 ?  310 ARG B NH2 1 
ATOM   5177 N  N   . LEU B 1 311 ? -11.661 -27.971 21.135  1.00 35.70 ?  311 LEU B N   1 
ATOM   5178 C  CA  . LEU B 1 311 ? -12.425 -27.808 19.902  1.00 36.19 ?  311 LEU B CA  1 
ATOM   5179 C  C   . LEU B 1 311 ? -11.416 -27.666 18.778  1.00 33.07 ?  311 LEU B C   1 
ATOM   5180 O  O   . LEU B 1 311 ? -10.660 -26.691 18.745  1.00 34.11 ?  311 LEU B O   1 
ATOM   5181 C  CB  . LEU B 1 311 ? -13.351 -26.592 19.971  1.00 33.37 ?  311 LEU B CB  1 
ATOM   5182 C  CG  . LEU B 1 311 ? -14.311 -26.386 18.796  1.00 38.11 ?  311 LEU B CG  1 
ATOM   5183 C  CD1 . LEU B 1 311 ? -15.396 -27.460 18.768  1.00 36.68 ?  311 LEU B CD1 1 
ATOM   5184 C  CD2 . LEU B 1 311 ? -14.922 -24.976 18.823  1.00 33.66 ?  311 LEU B CD2 1 
ATOM   5185 N  N   . GLY B 1 312 ? -11.399 -28.633 17.870  1.00 32.68 ?  312 GLY B N   1 
ATOM   5186 C  CA  . GLY B 1 312 ? -10.344 -28.644 16.877  1.00 34.61 ?  312 GLY B CA  1 
ATOM   5187 C  C   . GLY B 1 312 ? -9.011  -28.726 17.588  1.00 44.38 ?  312 GLY B C   1 
ATOM   5188 O  O   . GLY B 1 312 ? -8.784  -29.605 18.430  1.00 40.62 ?  312 GLY B O   1 
ATOM   5189 N  N   . GLU B 1 313 ? -8.125  -27.781 17.280  1.00 41.50 ?  313 GLU B N   1 
ATOM   5190 C  CA  . GLU B 1 313 ? -6.821  -27.708 17.919  1.00 44.35 ?  313 GLU B CA  1 
ATOM   5191 C  C   . GLU B 1 313 ? -6.765  -26.668 19.028  1.00 40.39 ?  313 GLU B C   1 
ATOM   5192 O  O   . GLU B 1 313 ? -5.677  -26.363 19.523  1.00 42.44 ?  313 GLU B O   1 
ATOM   5193 C  CB  . GLU B 1 313 ? -5.747  -27.408 16.880  1.00 48.68 ?  313 GLU B CB  1 
ATOM   5194 N  N   . VAL B 1 314 ? -7.904  -26.116 19.433  1.00 38.33 ?  314 VAL B N   1 
ATOM   5195 C  CA  . VAL B 1 314 ? -7.946  -25.020 20.391  1.00 40.41 ?  314 VAL B CA  1 
ATOM   5196 C  C   . VAL B 1 314 ? -8.568  -25.516 21.687  1.00 39.84 ?  314 VAL B C   1 
ATOM   5197 O  O   . VAL B 1 314 ? -9.637  -26.143 21.679  1.00 35.05 ?  314 VAL B O   1 
ATOM   5198 C  CB  . VAL B 1 314 ? -8.722  -23.812 19.835  1.00 40.65 ?  314 VAL B CB  1 
ATOM   5199 C  CG1 . VAL B 1 314 ? -9.045  -22.827 20.956  1.00 40.94 ?  314 VAL B CG1 1 
ATOM   5200 C  CG2 . VAL B 1 314 ? -7.925  -23.133 18.732  1.00 32.14 ?  314 VAL B CG2 1 
ATOM   5201 N  N   . GLU B 1 315 ? -7.892  -25.238 22.795  1.00 43.09 ?  315 GLU B N   1 
ATOM   5202 C  CA  . GLU B 1 315 ? -8.439  -25.445 24.129  1.00 42.36 ?  315 GLU B CA  1 
ATOM   5203 C  C   . GLU B 1 315 ? -9.231  -24.200 24.505  1.00 41.73 ?  315 GLU B C   1 
ATOM   5204 O  O   . GLU B 1 315 ? -8.647  -23.146 24.784  1.00 43.71 ?  315 GLU B O   1 
ATOM   5205 C  CB  . GLU B 1 315 ? -7.319  -25.700 25.137  1.00 49.86 ?  315 GLU B CB  1 
ATOM   5206 C  CG  . GLU B 1 315 ? -7.162  -27.149 25.558  1.00 47.64 ?  315 GLU B CG  1 
ATOM   5207 C  CD  . GLU B 1 315 ? -8.404  -27.694 26.243  1.00 50.21 ?  315 GLU B CD  1 
ATOM   5208 O  OE1 . GLU B 1 315 ? -8.962  -27.009 27.124  1.00 51.55 ?  315 GLU B OE1 1 
ATOM   5209 O  OE2 . GLU B 1 315 ? -8.835  -28.806 25.886  1.00 50.11 ?  315 GLU B OE2 1 
ATOM   5210 N  N   . ILE B 1 316 ? -10.551 -24.309 24.510  1.00 37.54 ?  316 ILE B N   1 
ATOM   5211 C  CA  . ILE B 1 316 ? -11.399 -23.191 24.900  1.00 41.25 ?  316 ILE B CA  1 
ATOM   5212 C  C   . ILE B 1 316 ? -11.628 -23.257 26.403  1.00 41.10 ?  316 ILE B C   1 
ATOM   5213 O  O   . ILE B 1 316 ? -11.898 -24.332 26.954  1.00 42.07 ?  316 ILE B O   1 
ATOM   5214 C  CB  . ILE B 1 316 ? -12.725 -23.206 24.126  1.00 32.61 ?  316 ILE B CB  1 
ATOM   5215 C  CG1 . ILE B 1 316 ? -12.451 -23.103 22.629  1.00 37.11 ?  316 ILE B CG1 1 
ATOM   5216 C  CG2 . ILE B 1 316 ? -13.603 -22.047 24.542  1.00 32.10 ?  316 ILE B CG2 1 
ATOM   5217 C  CD1 . ILE B 1 316 ? -13.679 -23.312 21.798  1.00 29.44 ?  316 ILE B CD1 1 
ATOM   5218 N  N   . ARG B 1 317 ? -11.511 -22.110 27.063  1.00 39.97 ?  317 ARG B N   1 
ATOM   5219 C  CA  . ARG B 1 317 ? -11.579 -22.014 28.512  1.00 37.36 ?  317 ARG B CA  1 
ATOM   5220 C  C   . ARG B 1 317 ? -13.001 -21.699 28.958  1.00 41.46 ?  317 ARG B C   1 
ATOM   5221 O  O   . ARG B 1 317 ? -13.746 -20.998 28.271  1.00 37.99 ?  317 ARG B O   1 
ATOM   5222 C  CB  . ARG B 1 317 ? -10.632 -20.921 29.017  1.00 42.91 ?  317 ARG B CB  1 
ATOM   5223 C  CG  . ARG B 1 317 ? -9.155  -21.146 28.749  1.00 47.99 ?  317 ARG B CG  1 
ATOM   5224 C  CD  . ARG B 1 317 ? -8.629  -22.335 29.513  1.00 48.34 ?  317 ARG B CD  1 
ATOM   5225 N  NE  . ARG B 1 317 ? -7.206  -22.552 29.286  1.00 55.41 ?  317 ARG B NE  1 
ATOM   5226 C  CZ  . ARG B 1 317 ? -6.555  -23.649 29.651  1.00 53.95 ?  317 ARG B CZ  1 
ATOM   5227 N  NH1 . ARG B 1 317 ? -7.176  -24.645 30.262  1.00 54.71 ?  317 ARG B NH1 1 
ATOM   5228 N  NH2 . ARG B 1 317 ? -5.252  -23.746 29.405  1.00 53.55 ?  317 ARG B NH2 1 
ATOM   5229 N  N   . ALA B 1 318 ? -13.371 -22.221 30.127  1.00 39.60 ?  318 ALA B N   1 
ATOM   5230 C  CA  . ALA B 1 318 ? -14.658 -21.876 30.714  1.00 41.58 ?  318 ALA B CA  1 
ATOM   5231 C  C   . ALA B 1 318 ? -14.799 -20.358 30.821  1.00 37.12 ?  318 ALA B C   1 
ATOM   5232 O  O   . ALA B 1 318 ? -13.849 -19.655 31.178  1.00 32.90 ?  318 ALA B O   1 
ATOM   5233 C  CB  . ALA B 1 318 ? -14.796 -22.528 32.091  1.00 36.23 ?  318 ALA B CB  1 
ATOM   5234 N  N   . GLY B 1 319 ? -15.981 -19.849 30.463  1.00 35.76 ?  319 GLY B N   1 
ATOM   5235 C  CA  . GLY B 1 319 ? -16.255 -18.424 30.537  1.00 35.56 ?  319 GLY B CA  1 
ATOM   5236 C  C   . GLY B 1 319 ? -15.901 -17.610 29.306  1.00 36.83 ?  319 GLY B C   1 
ATOM   5237 O  O   . GLY B 1 319 ? -16.166 -16.400 29.287  1.00 35.54 ?  319 GLY B O   1 
ATOM   5238 N  N   . GLU B 1 320 ? -15.309 -18.220 28.284  1.00 34.92 ?  320 GLU B N   1 
ATOM   5239 C  CA  . GLU B 1 320 ? -14.936 -17.509 27.069  1.00 33.66 ?  320 GLU B CA  1 
ATOM   5240 C  C   . GLU B 1 320 ? -16.076 -17.524 26.054  1.00 29.39 ?  320 GLU B C   1 
ATOM   5241 O  O   . GLU B 1 320 ? -16.929 -18.416 26.056  1.00 28.65 ?  320 GLU B O   1 
ATOM   5242 C  CB  . GLU B 1 320 ? -13.677 -18.122 26.457  1.00 33.00 ?  320 GLU B CB  1 
ATOM   5243 C  CG  . GLU B 1 320 ? -12.399 -17.830 27.248  1.00 33.86 ?  320 GLU B CG  1 
ATOM   5244 C  CD  . GLU B 1 320 ? -11.180 -18.445 26.600  1.00 33.63 ?  320 GLU B CD  1 
ATOM   5245 O  OE1 . GLU B 1 320 ? -11.358 -19.381 25.792  1.00 36.42 ?  320 GLU B OE1 1 
ATOM   5246 O  OE2 . GLU B 1 320 ? -10.048 -18.025 26.916  1.00 33.76 ?  320 GLU B OE2 1 
ATOM   5247 N  N   . LEU B 1 321 ? -16.082 -16.514 25.185  1.00 32.85 ?  321 LEU B N   1 
ATOM   5248 C  CA  . LEU B 1 321 ? -17.118 -16.387 24.166  1.00 27.81 ?  321 LEU B CA  1 
ATOM   5249 C  C   . LEU B 1 321 ? -16.773 -17.221 22.936  1.00 27.05 ?  321 LEU B C   1 
ATOM   5250 O  O   . LEU B 1 321 ? -15.629 -17.227 22.469  1.00 28.40 ?  321 LEU B O   1 
ATOM   5251 C  CB  . LEU B 1 321 ? -17.284 -14.919 23.768  1.00 25.54 ?  321 LEU B CB  1 
ATOM   5252 C  CG  . LEU B 1 321 ? -18.267 -14.560 22.648  1.00 29.10 ?  321 LEU B CG  1 
ATOM   5253 C  CD1 . LEU B 1 321 ? -19.658 -15.094 22.967  1.00 25.37 ?  321 LEU B CD1 1 
ATOM   5254 C  CD2 . LEU B 1 321 ? -18.290 -13.029 22.440  1.00 29.68 ?  321 LEU B CD2 1 
ATOM   5255 N  N   . VAL B 1 322 ? -17.771 -17.920 22.404  1.00 24.90 ?  322 VAL B N   1 
ATOM   5256 C  CA  . VAL B 1 322 ? -17.618 -18.736 21.204  1.00 30.44 ?  322 VAL B CA  1 
ATOM   5257 C  C   . VAL B 1 322 ? -18.622 -18.238 20.175  1.00 25.35 ?  322 VAL B C   1 
ATOM   5258 O  O   . VAL B 1 322 ? -19.796 -18.032 20.504  1.00 24.16 ?  322 VAL B O   1 
ATOM   5259 C  CB  . VAL B 1 322 ? -17.833 -20.235 21.495  1.00 30.58 ?  322 VAL B CB  1 
ATOM   5260 C  CG1 . VAL B 1 322 ? -17.719 -21.057 20.211  1.00 28.27 ?  322 VAL B CG1 1 
ATOM   5261 C  CG2 . VAL B 1 322 ? -16.833 -20.730 22.522  1.00 25.57 ?  322 VAL B CG2 1 
ATOM   5262 N  N   . LEU B 1 323 ? -18.165 -18.060 18.933  1.00 24.20 ?  323 LEU B N   1 
ATOM   5263 C  CA  . LEU B 1 323 ? -18.986 -17.503 17.864  1.00 25.41 ?  323 LEU B CA  1 
ATOM   5264 C  C   . LEU B 1 323 ? -19.010 -18.471 16.692  1.00 21.57 ?  323 LEU B C   1 
ATOM   5265 O  O   . LEU B 1 323 ? -17.975 -18.709 16.059  1.00 22.23 ?  323 LEU B O   1 
ATOM   5266 C  CB  . LEU B 1 323 ? -18.447 -16.135 17.423  1.00 22.45 ?  323 LEU B CB  1 
ATOM   5267 C  CG  . LEU B 1 323 ? -18.439 -14.997 18.454  1.00 23.78 ?  323 LEU B CG  1 
ATOM   5268 C  CD1 . LEU B 1 323 ? -17.736 -13.764 17.877  1.00 21.50 ?  323 LEU B CD1 1 
ATOM   5269 C  CD2 . LEU B 1 323 ? -19.850 -14.657 18.897  1.00 21.68 ?  323 LEU B CD2 1 
ATOM   5270 N  N   . VAL B 1 324 ? -20.185 -19.015 16.392  1.00 22.27 ?  324 VAL B N   1 
ATOM   5271 C  CA  . VAL B 1 324 ? -20.336 -19.949 15.276  1.00 21.57 ?  324 VAL B CA  1 
ATOM   5272 C  C   . VAL B 1 324 ? -20.638 -19.159 14.007  1.00 20.87 ?  324 VAL B C   1 
ATOM   5273 O  O   . VAL B 1 324 ? -21.665 -18.478 13.916  1.00 23.91 ?  324 VAL B O   1 
ATOM   5274 C  CB  . VAL B 1 324 ? -21.434 -20.986 15.559  1.00 23.64 ?  324 VAL B CB  1 
ATOM   5275 C  CG1 . VAL B 1 324 ? -21.605 -21.929 14.361  1.00 21.85 ?  324 VAL B CG1 1 
ATOM   5276 C  CG2 . VAL B 1 324 ? -21.073 -21.779 16.808  1.00 22.24 ?  324 VAL B CG2 1 
ATOM   5277 N  N   . LEU B 1 325 ? -19.755 -19.266 13.020  1.00 21.71 ?  325 LEU B N   1 
ATOM   5278 C  CA  . LEU B 1 325 ? -19.894 -18.537 11.756  1.00 21.72 ?  325 LEU B CA  1 
ATOM   5279 C  C   . LEU B 1 325 ? -20.663 -19.404 10.770  1.00 20.66 ?  325 LEU B C   1 
ATOM   5280 O  O   . LEU B 1 325 ? -20.096 -20.300 10.139  1.00 26.12 ?  325 LEU B O   1 
ATOM   5281 C  CB  . LEU B 1 325 ? -18.530 -18.156 11.195  1.00 19.79 ?  325 LEU B CB  1 
ATOM   5282 C  CG  . LEU B 1 325 ? -18.636 -17.187 10.019  1.00 22.12 ?  325 LEU B CG  1 
ATOM   5283 C  CD1 . LEU B 1 325 ? -18.954 -15.773 10.511  1.00 21.90 ?  325 LEU B CD1 1 
ATOM   5284 C  CD2 . LEU B 1 325 ? -17.357 -17.211 9.177   1.00 18.53 ?  325 LEU B CD2 1 
ATOM   5285 N  N   . ILE B 1 326 ? -21.951 -19.098 10.600  1.00 19.70 ?  326 ILE B N   1 
ATOM   5286 C  CA  . ILE B 1 326 ? -22.844 -19.967 9.837   1.00 21.29 ?  326 ILE B CA  1 
ATOM   5287 C  C   . ILE B 1 326 ? -22.425 -20.034 8.379   1.00 21.82 ?  326 ILE B C   1 
ATOM   5288 O  O   . ILE B 1 326 ? -22.511 -21.092 7.743   1.00 21.14 ?  326 ILE B O   1 
ATOM   5289 C  CB  . ILE B 1 326 ? -24.298 -19.485 9.976   1.00 21.18 ?  326 ILE B CB  1 
ATOM   5290 C  CG1 . ILE B 1 326 ? -24.739 -19.573 11.448  1.00 20.56 ?  326 ILE B CG1 1 
ATOM   5291 C  CG2 . ILE B 1 326 ? -25.221 -20.302 9.050   1.00 19.08 ?  326 ILE B CG2 1 
ATOM   5292 C  CD1 . ILE B 1 326 ? -24.727 -21.000 12.014  1.00 19.08 ?  326 ILE B CD1 1 
ATOM   5293 N  N   . GLU B 1 327 ? -21.965 -18.912 7.821   1.00 21.09 ?  327 GLU B N   1 
ATOM   5294 C  CA  . GLU B 1 327 ? -21.575 -18.917 6.417   1.00 20.67 ?  327 GLU B CA  1 
ATOM   5295 C  C   . GLU B 1 327 ? -20.251 -19.631 6.218   1.00 21.06 ?  327 GLU B C   1 
ATOM   5296 O  O   . GLU B 1 327 ? -20.005 -20.180 5.142   1.00 20.58 ?  327 GLU B O   1 
ATOM   5297 C  CB  . GLU B 1 327 ? -21.518 -17.490 5.874   1.00 21.81 ?  327 GLU B CB  1 
ATOM   5298 C  CG  . GLU B 1 327 ? -20.397 -16.639 6.437   1.00 22.18 ?  327 GLU B CG  1 
ATOM   5299 C  CD  . GLU B 1 327 ? -20.929 -15.533 7.318   1.00 29.14 ?  327 GLU B CD  1 
ATOM   5300 O  OE1 . GLU B 1 327 ? -21.817 -15.824 8.160   1.00 33.22 ?  327 GLU B OE1 1 
ATOM   5301 O  OE2 . GLU B 1 327 ? -20.491 -14.380 7.134   1.00 33.79 ?  327 GLU B OE2 1 
ATOM   5302 N  N   . GLY B 1 328 ? -19.381 -19.631 7.227   1.00 20.68 ?  328 GLY B N   1 
ATOM   5303 C  CA  . GLY B 1 328 ? -18.248 -20.536 7.170   1.00 21.68 ?  328 GLY B CA  1 
ATOM   5304 C  C   . GLY B 1 328 ? -18.693 -21.975 6.981   1.00 23.77 ?  328 GLY B C   1 
ATOM   5305 O  O   . GLY B 1 328 ? -18.230 -22.675 6.078   1.00 22.48 ?  328 GLY B O   1 
ATOM   5306 N  N   . ALA B 1 329 ? -19.636 -22.422 7.809   1.00 21.88 ?  329 ALA B N   1 
ATOM   5307 C  CA  . ALA B 1 329 ? -20.046 -23.821 7.758   1.00 21.77 ?  329 ALA B CA  1 
ATOM   5308 C  C   . ALA B 1 329 ? -20.812 -24.125 6.477   1.00 22.77 ?  329 ALA B C   1 
ATOM   5309 O  O   . ALA B 1 329 ? -20.577 -25.157 5.827   1.00 22.70 ?  329 ALA B O   1 
ATOM   5310 C  CB  . ALA B 1 329 ? -20.883 -24.153 8.988   1.00 21.76 ?  329 ALA B CB  1 
ATOM   5311 N  N   . ASN B 1 330 ? -21.707 -23.223 6.076   1.00 20.66 ?  330 ASN B N   1 
ATOM   5312 C  CA  . ASN B 1 330 ? -22.600 -23.516 4.969   1.00 21.51 ?  330 ASN B CA  1 
ATOM   5313 C  C   . ASN B 1 330 ? -21.897 -23.462 3.615   1.00 23.07 ?  330 ASN B C   1 
ATOM   5314 O  O   . ASN B 1 330 ? -22.448 -23.978 2.632   1.00 21.38 ?  330 ASN B O   1 
ATOM   5315 C  CB  . ASN B 1 330 ? -23.798 -22.563 5.021   1.00 20.28 ?  330 ASN B CB  1 
ATOM   5316 C  CG  . ASN B 1 330 ? -24.892 -23.064 5.952   1.00 23.10 ?  330 ASN B CG  1 
ATOM   5317 O  OD1 . ASN B 1 330 ? -24.772 -24.136 6.522   1.00 20.24 ?  330 ASN B OD1 1 
ATOM   5318 N  ND2 . ASN B 1 330 ? -25.971 -22.292 6.097   1.00 22.06 ?  330 ASN B ND2 1 
ATOM   5319 N  N   . TYR B 1 331 ? -20.681 -22.912 3.554   1.00 19.35 ?  331 TYR B N   1 
ATOM   5320 C  CA  . TYR B 1 331 ? -19.875 -22.888 2.336   1.00 21.60 ?  331 TYR B CA  1 
ATOM   5321 C  C   . TYR B 1 331 ? -18.643 -23.794 2.438   1.00 25.57 ?  331 TYR B C   1 
ATOM   5322 O  O   . TYR B 1 331 ? -17.732 -23.692 1.607   1.00 23.94 ?  331 TYR B O   1 
ATOM   5323 C  CB  . TYR B 1 331 ? -19.438 -21.446 2.014   1.00 22.25 ?  331 TYR B CB  1 
ATOM   5324 C  CG  . TYR B 1 331 ? -20.507 -20.531 1.418   1.00 22.05 ?  331 TYR B CG  1 
ATOM   5325 C  CD1 . TYR B 1 331 ? -21.606 -20.125 2.164   1.00 20.35 ?  331 TYR B CD1 1 
ATOM   5326 C  CD2 . TYR B 1 331 ? -20.378 -20.037 0.127   1.00 22.59 ?  331 TYR B CD2 1 
ATOM   5327 C  CE1 . TYR B 1 331 ? -22.582 -19.281 1.622   1.00 20.97 ?  331 TYR B CE1 1 
ATOM   5328 C  CE2 . TYR B 1 331 ? -21.328 -19.182 -0.422  1.00 20.08 ?  331 TYR B CE2 1 
ATOM   5329 C  CZ  . TYR B 1 331 ? -22.431 -18.807 0.329   1.00 22.07 ?  331 TYR B CZ  1 
ATOM   5330 O  OH  . TYR B 1 331 ? -23.374 -17.962 -0.227  1.00 20.11 ?  331 TYR B OH  1 
ATOM   5331 N  N   . ASP B 1 332 ? -18.592 -24.659 3.442   1.00 23.65 ?  332 ASP B N   1 
ATOM   5332 C  CA  . ASP B 1 332 ? -17.449 -25.538 3.671   1.00 24.08 ?  332 ASP B CA  1 
ATOM   5333 C  C   . ASP B 1 332 ? -17.383 -26.622 2.597   1.00 21.96 ?  332 ASP B C   1 
ATOM   5334 O  O   . ASP B 1 332 ? -18.296 -27.454 2.517   1.00 21.77 ?  332 ASP B O   1 
ATOM   5335 C  CB  . ASP B 1 332 ? -17.576 -26.165 5.060   1.00 23.67 ?  332 ASP B CB  1 
ATOM   5336 C  CG  . ASP B 1 332 ? -16.305 -26.857 5.511   1.00 26.24 ?  332 ASP B CG  1 
ATOM   5337 O  OD1 . ASP B 1 332 ? -15.483 -27.226 4.652   1.00 25.56 ?  332 ASP B OD1 1 
ATOM   5338 O  OD2 . ASP B 1 332 ? -16.132 -27.038 6.731   1.00 25.49 ?  332 ASP B OD2 1 
ATOM   5339 N  N   . PRO B 1 333 ? -16.342 -26.652 1.758   1.00 22.72 ?  333 PRO B N   1 
ATOM   5340 C  CA  . PRO B 1 333 ? -16.294 -27.648 0.673   1.00 22.63 ?  333 PRO B CA  1 
ATOM   5341 C  C   . PRO B 1 333 ? -16.184 -29.089 1.157   1.00 30.67 ?  333 PRO B C   1 
ATOM   5342 O  O   . PRO B 1 333 ? -16.504 -30.006 0.390   1.00 29.05 ?  333 PRO B O   1 
ATOM   5343 C  CB  . PRO B 1 333 ? -15.048 -27.238 -0.132  1.00 22.82 ?  333 PRO B CB  1 
ATOM   5344 C  CG  . PRO B 1 333 ? -14.240 -26.413 0.800   1.00 24.77 ?  333 PRO B CG  1 
ATOM   5345 C  CD  . PRO B 1 333 ? -15.215 -25.706 1.697   1.00 21.35 ?  333 PRO B CD  1 
ATOM   5346 N  N   . ALA B 1 334 ? -15.745 -29.326 2.397   1.00 25.61 ?  334 ALA B N   1 
ATOM   5347 C  CA  . ALA B 1 334 ? -15.711 -30.691 2.897   1.00 26.11 ?  334 ALA B CA  1 
ATOM   5348 C  C   . ALA B 1 334 ? -17.095 -31.312 2.927   1.00 24.87 ?  334 ALA B C   1 
ATOM   5349 O  O   . ALA B 1 334 ? -17.217 -32.540 2.907   1.00 27.22 ?  334 ALA B O   1 
ATOM   5350 C  CB  . ALA B 1 334 ? -15.086 -30.730 4.297   1.00 25.67 ?  334 ALA B CB  1 
ATOM   5351 N  N   . VAL B 1 335 ? -18.138 -30.491 2.974   1.00 24.13 ?  335 VAL B N   1 
ATOM   5352 C  CA  . VAL B 1 335 ? -19.506 -30.961 3.095   1.00 22.41 ?  335 VAL B CA  1 
ATOM   5353 C  C   . VAL B 1 335 ? -20.324 -30.607 1.863   1.00 24.88 ?  335 VAL B C   1 
ATOM   5354 O  O   . VAL B 1 335 ? -21.173 -31.387 1.430   1.00 22.25 ?  335 VAL B O   1 
ATOM   5355 C  CB  . VAL B 1 335 ? -20.165 -30.380 4.367   1.00 24.25 ?  335 VAL B CB  1 
ATOM   5356 C  CG1 . VAL B 1 335 ? -21.655 -30.670 4.381   1.00 24.92 ?  335 VAL B CG1 1 
ATOM   5357 C  CG2 . VAL B 1 335 ? -19.484 -30.920 5.626   1.00 27.70 ?  335 VAL B CG2 1 
ATOM   5358 N  N   . PHE B 1 336 ? -20.095 -29.428 1.302   1.00 22.78 ?  336 PHE B N   1 
ATOM   5359 C  CA  . PHE B 1 336 ? -20.876 -28.949 0.170   1.00 22.00 ?  336 PHE B CA  1 
ATOM   5360 C  C   . PHE B 1 336 ? -19.956 -28.764 -1.029  1.00 22.60 ?  336 PHE B C   1 
ATOM   5361 O  O   . PHE B 1 336 ? -19.162 -27.805 -1.047  1.00 23.25 ?  336 PHE B O   1 
ATOM   5362 C  CB  . PHE B 1 336 ? -21.582 -27.642 0.540   1.00 22.16 ?  336 PHE B CB  1 
ATOM   5363 C  CG  . PHE B 1 336 ? -22.432 -27.737 1.786   1.00 21.85 ?  336 PHE B CG  1 
ATOM   5364 C  CD1 . PHE B 1 336 ? -23.738 -28.227 1.718   1.00 18.40 ?  336 PHE B CD1 1 
ATOM   5365 C  CD2 . PHE B 1 336 ? -21.937 -27.325 3.020   1.00 18.65 ?  336 PHE B CD2 1 
ATOM   5366 C  CE1 . PHE B 1 336 ? -24.528 -28.319 2.859   1.00 21.20 ?  336 PHE B CE1 1 
ATOM   5367 C  CE2 . PHE B 1 336 ? -22.718 -27.406 4.171   1.00 20.17 ?  336 PHE B CE2 1 
ATOM   5368 C  CZ  . PHE B 1 336 ? -24.015 -27.901 4.094   1.00 25.13 ?  336 PHE B CZ  1 
ATOM   5369 N  N   . PRO B 1 337 ? -19.978 -29.654 -2.027  1.00 23.18 ?  337 PRO B N   1 
ATOM   5370 C  CA  . PRO B 1 337 ? -19.180 -29.415 -3.238  1.00 22.45 ?  337 PRO B CA  1 
ATOM   5371 C  C   . PRO B 1 337 ? -19.649 -28.151 -3.943  1.00 21.20 ?  337 PRO B C   1 
ATOM   5372 O  O   . PRO B 1 337 ? -20.806 -27.735 -3.812  1.00 21.88 ?  337 PRO B O   1 
ATOM   5373 C  CB  . PRO B 1 337 ? -19.424 -30.665 -4.097  1.00 23.26 ?  337 PRO B CB  1 
ATOM   5374 C  CG  . PRO B 1 337 ? -20.634 -31.326 -3.503  1.00 27.63 ?  337 PRO B CG  1 
ATOM   5375 C  CD  . PRO B 1 337 ? -20.674 -30.949 -2.054  1.00 21.42 ?  337 PRO B CD  1 
ATOM   5376 N  N   . HIS B 1 338 ? -18.725 -27.549 -4.712  1.00 21.21 ?  338 HIS B N   1 
ATOM   5377 C  CA  . HIS B 1 338 ? -18.901 -26.230 -5.331  1.00 21.13 ?  338 HIS B CA  1 
ATOM   5378 C  C   . HIS B 1 338 ? -19.782 -25.351 -4.451  1.00 21.43 ?  338 HIS B C   1 
ATOM   5379 O  O   . HIS B 1 338 ? -20.879 -24.944 -4.864  1.00 18.81 ?  338 HIS B O   1 
ATOM   5380 C  CB  . HIS B 1 338 ? -19.499 -26.334 -6.740  1.00 20.05 ?  338 HIS B CB  1 
ATOM   5381 C  CG  . HIS B 1 338 ? -20.669 -27.260 -6.853  1.00 19.98 ?  338 HIS B CG  1 
ATOM   5382 N  ND1 . HIS B 1 338 ? -20.529 -28.621 -7.037  1.00 20.02 ?  338 HIS B ND1 1 
ATOM   5383 C  CD2 . HIS B 1 338 ? -22.002 -27.014 -6.858  1.00 18.28 ?  338 HIS B CD2 1 
ATOM   5384 C  CE1 . HIS B 1 338 ? -21.728 -29.174 -7.124  1.00 22.53 ?  338 HIS B CE1 1 
ATOM   5385 N  NE2 . HIS B 1 338 ? -22.638 -28.221 -7.014  1.00 23.43 ?  338 HIS B NE2 1 
ATOM   5386 N  N   . PRO B 1 339 ? -19.353 -25.068 -3.219  1.00 20.83 ?  339 PRO B N   1 
ATOM   5387 C  CA  . PRO B 1 339 ? -20.247 -24.366 -2.294  1.00 21.06 ?  339 PRO B CA  1 
ATOM   5388 C  C   . PRO B 1 339 ? -20.625 -22.986 -2.792  1.00 21.11 ?  339 PRO B C   1 
ATOM   5389 O  O   . PRO B 1 339 ? -21.697 -22.482 -2.440  1.00 18.49 ?  339 PRO B O   1 
ATOM   5390 C  CB  . PRO B 1 339 ? -19.427 -24.286 -1.002  1.00 21.79 ?  339 PRO B CB  1 
ATOM   5391 C  CG  . PRO B 1 339 ? -17.996 -24.427 -1.434  1.00 18.03 ?  339 PRO B CG  1 
ATOM   5392 C  CD  . PRO B 1 339 ? -17.962 -25.141 -2.731  1.00 21.00 ?  339 PRO B CD  1 
ATOM   5393 N  N   . GLU B 1 340 ? -19.772 -22.372 -3.617  1.00 21.41 ?  340 GLU B N   1 
ATOM   5394 C  CA  . GLU B 1 340 ? -19.974 -21.018 -4.110  1.00 24.16 ?  340 GLU B CA  1 
ATOM   5395 C  C   . GLU B 1 340 ? -20.988 -20.951 -5.241  1.00 25.67 ?  340 GLU B C   1 
ATOM   5396 O  O   . GLU B 1 340 ? -21.319 -19.844 -5.678  1.00 24.33 ?  340 GLU B O   1 
ATOM   5397 C  CB  . GLU B 1 340 ? -18.632 -20.427 -4.573  1.00 17.67 ?  340 GLU B CB  1 
ATOM   5398 C  CG  . GLU B 1 340 ? -18.220 -20.842 -5.983  1.00 22.00 ?  340 GLU B CG  1 
ATOM   5399 C  CD  . GLU B 1 340 ? -17.635 -22.256 -6.049  1.00 27.14 ?  340 GLU B CD  1 
ATOM   5400 O  OE1 . GLU B 1 340 ? -17.589 -22.950 -5.004  1.00 24.59 ?  340 GLU B OE1 1 
ATOM   5401 O  OE2 . GLU B 1 340 ? -17.225 -22.673 -7.158  1.00 30.42 ?  340 GLU B OE2 1 
ATOM   5402 N  N   . ARG B 1 341 ? -21.508 -22.089 -5.704  1.00 19.47 ?  341 ARG B N   1 
ATOM   5403 C  CA  . ARG B 1 341 ? -22.488 -22.128 -6.788  1.00 20.54 ?  341 ARG B CA  1 
ATOM   5404 C  C   . ARG B 1 341 ? -23.835 -22.619 -6.265  1.00 22.58 ?  341 ARG B C   1 
ATOM   5405 O  O   . ARG B 1 341 ? -23.918 -23.702 -5.676  1.00 19.94 ?  341 ARG B O   1 
ATOM   5406 C  CB  . ARG B 1 341 ? -21.998 -23.036 -7.920  1.00 22.75 ?  341 ARG B CB  1 
ATOM   5407 C  CG  . ARG B 1 341 ? -20.609 -22.663 -8.423  1.00 23.47 ?  341 ARG B CG  1 
ATOM   5408 C  CD  . ARG B 1 341 ? -20.176 -23.521 -9.605  1.00 19.52 ?  341 ARG B CD  1 
ATOM   5409 N  NE  . ARG B 1 341 ? -21.002 -23.280 -10.779 1.00 23.24 ?  341 ARG B NE  1 
ATOM   5410 C  CZ  . ARG B 1 341 ? -20.897 -22.209 -11.550 1.00 22.71 ?  341 ARG B CZ  1 
ATOM   5411 N  NH1 . ARG B 1 341 ? -20.009 -21.259 -11.291 1.00 22.80 ?  341 ARG B NH1 1 
ATOM   5412 N  NH2 . ARG B 1 341 ? -21.712 -22.080 -12.594 1.00 22.16 ?  341 ARG B NH2 1 
ATOM   5413 N  N   . ILE B 1 342 ? -24.890 -21.828 -6.498  1.00 26.48 ?  342 ILE B N   1 
ATOM   5414 C  CA  . ILE B 1 342 ? -26.233 -22.263 -6.141  1.00 21.67 ?  342 ILE B CA  1 
ATOM   5415 C  C   . ILE B 1 342 ? -26.595 -23.473 -6.976  1.00 22.56 ?  342 ILE B C   1 
ATOM   5416 O  O   . ILE B 1 342 ? -26.306 -23.540 -8.179  1.00 19.26 ?  342 ILE B O   1 
ATOM   5417 C  CB  . ILE B 1 342 ? -27.269 -21.145 -6.333  1.00 24.25 ?  342 ILE B CB  1 
ATOM   5418 C  CG1 . ILE B 1 342 ? -27.078 -20.055 -5.276  1.00 22.03 ?  342 ILE B CG1 1 
ATOM   5419 C  CG2 . ILE B 1 342 ? -28.702 -21.717 -6.261  1.00 21.23 ?  342 ILE B CG2 1 
ATOM   5420 C  CD1 . ILE B 1 342 ? -27.798 -18.788 -5.598  1.00 24.14 ?  342 ILE B CD1 1 
ATOM   5421 N  N   . ASP B 1 343 ? -27.218 -24.450 -6.327  1.00 19.46 ?  343 ASP B N   1 
ATOM   5422 C  CA  . ASP B 1 343 ? -27.443 -25.749 -6.940  1.00 20.63 ?  343 ASP B CA  1 
ATOM   5423 C  C   . ASP B 1 343 ? -28.697 -26.324 -6.301  1.00 21.70 ?  343 ASP B C   1 
ATOM   5424 O  O   . ASP B 1 343 ? -28.644 -26.790 -5.159  1.00 20.07 ?  343 ASP B O   1 
ATOM   5425 C  CB  . ASP B 1 343 ? -26.239 -26.649 -6.711  1.00 20.69 ?  343 ASP B CB  1 
ATOM   5426 C  CG  . ASP B 1 343 ? -26.377 -28.016 -7.367  1.00 19.74 ?  343 ASP B CG  1 
ATOM   5427 O  OD1 . ASP B 1 343 ? -27.493 -28.394 -7.810  1.00 17.24 ?  343 ASP B OD1 1 
ATOM   5428 O  OD2 . ASP B 1 343 ? -25.336 -28.717 -7.415  1.00 21.72 ?  343 ASP B OD2 1 
ATOM   5429 N  N   . PHE B 1 344 ? -29.802 -26.305 -7.042  1.00 20.67 ?  344 PHE B N   1 
ATOM   5430 C  CA  . PHE B 1 344 ? -31.097 -26.800 -6.573  1.00 21.85 ?  344 PHE B CA  1 
ATOM   5431 C  C   . PHE B 1 344 ? -31.201 -28.328 -6.566  1.00 27.52 ?  344 PHE B C   1 
ATOM   5432 O  O   . PHE B 1 344 ? -32.259 -28.859 -6.196  1.00 26.59 ?  344 PHE B O   1 
ATOM   5433 C  CB  . PHE B 1 344 ? -32.218 -26.236 -7.457  1.00 21.20 ?  344 PHE B CB  1 
ATOM   5434 C  CG  . PHE B 1 344 ? -32.474 -24.757 -7.265  1.00 22.05 ?  344 PHE B CG  1 
ATOM   5435 C  CD1 . PHE B 1 344 ? -31.855 -24.056 -6.243  1.00 19.43 ?  344 PHE B CD1 1 
ATOM   5436 C  CD2 . PHE B 1 344 ? -33.341 -24.079 -8.112  1.00 22.33 ?  344 PHE B CD2 1 
ATOM   5437 C  CE1 . PHE B 1 344 ? -32.093 -22.702 -6.064  1.00 23.54 ?  344 PHE B CE1 1 
ATOM   5438 C  CE2 . PHE B 1 344 ? -33.579 -22.715 -7.942  1.00 24.21 ?  344 PHE B CE2 1 
ATOM   5439 C  CZ  . PHE B 1 344 ? -32.959 -22.033 -6.908  1.00 19.69 ?  344 PHE B CZ  1 
ATOM   5440 N  N   . ASP B 1 345 ? -30.151 -29.054 -6.965  1.00 25.31 ?  345 ASP B N   1 
ATOM   5441 C  CA  . ASP B 1 345 ? -30.235 -30.506 -7.111  1.00 21.89 ?  345 ASP B CA  1 
ATOM   5442 C  C   . ASP B 1 345 ? -29.129 -31.234 -6.347  1.00 24.79 ?  345 ASP B C   1 
ATOM   5443 O  O   . ASP B 1 345 ? -28.646 -32.290 -6.788  1.00 25.15 ?  345 ASP B O   1 
ATOM   5444 C  CB  . ASP B 1 345 ? -30.210 -30.884 -8.591  1.00 22.31 ?  345 ASP B CB  1 
ATOM   5445 C  CG  . ASP B 1 345 ? -31.355 -30.264 -9.350  1.00 21.76 ?  345 ASP B CG  1 
ATOM   5446 O  OD1 . ASP B 1 345 ? -32.499 -30.715 -9.168  1.00 26.65 ?  345 ASP B OD1 1 
ATOM   5447 O  OD2 . ASP B 1 345 ? -31.129 -29.282 -10.082 1.00 22.76 ?  345 ASP B OD2 1 
ATOM   5448 N  N   . ARG B 1 346 ? -28.712 -30.694 -5.203  1.00 23.80 ?  346 ARG B N   1 
ATOM   5449 C  CA  . ARG B 1 346 ? -27.741 -31.389 -4.370  1.00 24.25 ?  346 ARG B CA  1 
ATOM   5450 C  C   . ARG B 1 346 ? -28.333 -32.682 -3.808  1.00 28.53 ?  346 ARG B C   1 
ATOM   5451 O  O   . ARG B 1 346 ? -29.492 -32.724 -3.389  1.00 24.83 ?  346 ARG B O   1 
ATOM   5452 C  CB  . ARG B 1 346 ? -27.270 -30.473 -3.237  1.00 26.16 ?  346 ARG B CB  1 
ATOM   5453 C  CG  . ARG B 1 346 ? -26.466 -29.254 -3.756  1.00 22.65 ?  346 ARG B CG  1 
ATOM   5454 C  CD  . ARG B 1 346 ? -26.238 -28.176 -2.705  1.00 21.46 ?  346 ARG B CD  1 
ATOM   5455 N  NE  . ARG B 1 346 ? -25.424 -27.094 -3.254  1.00 22.68 ?  346 ARG B NE  1 
ATOM   5456 C  CZ  . ARG B 1 346 ? -24.106 -27.161 -3.381  1.00 25.16 ?  346 ARG B CZ  1 
ATOM   5457 N  NH1 . ARG B 1 346 ? -23.427 -28.226 -2.968  1.00 22.86 ?  346 ARG B NH1 1 
ATOM   5458 N  NH2 . ARG B 1 346 ? -23.451 -26.136 -3.929  1.00 19.12 ?  346 ARG B NH2 1 
ATOM   5459 N  N   . GLU B 1 347 ? -27.531 -33.748 -3.832  1.00 25.76 ?  347 GLU B N   1 
ATOM   5460 C  CA  . GLU B 1 347 ? -27.933 -35.008 -3.212  1.00 31.10 ?  347 GLU B CA  1 
ATOM   5461 C  C   . GLU B 1 347 ? -28.274 -34.814 -1.737  1.00 34.38 ?  347 GLU B C   1 
ATOM   5462 O  O   . GLU B 1 347 ? -29.287 -35.323 -1.242  1.00 25.48 ?  347 GLU B O   1 
ATOM   5463 C  CB  . GLU B 1 347 ? -26.808 -36.028 -3.368  1.00 38.74 ?  347 GLU B CB  1 
ATOM   5464 C  CG  . GLU B 1 347 ? -27.121 -37.404 -2.831  1.00 46.64 ?  347 GLU B CG  1 
ATOM   5465 C  CD  . GLU B 1 347 ? -25.976 -38.367 -3.067  1.00 58.67 ?  347 GLU B CD  1 
ATOM   5466 O  OE1 . GLU B 1 347 ? -24.933 -37.932 -3.617  1.00 61.13 ?  347 GLU B OE1 1 
ATOM   5467 O  OE2 . GLU B 1 347 ? -26.118 -39.550 -2.683  1.00 57.16 ?  347 GLU B OE2 1 
ATOM   5468 N  N   . SER B 1 348 ? -27.427 -34.082 -1.024  1.00 31.55 ?  348 SER B N   1 
ATOM   5469 C  CA  . SER B 1 348 ? -27.593 -33.787 0.390   1.00 34.06 ?  348 SER B CA  1 
ATOM   5470 C  C   . SER B 1 348 ? -27.490 -32.281 0.599   1.00 33.29 ?  348 SER B C   1 
ATOM   5471 O  O   . SER B 1 348 ? -26.753 -31.592 -0.113  1.00 32.07 ?  348 SER B O   1 
ATOM   5472 C  CB  . SER B 1 348 ? -26.519 -34.503 1.212   1.00 29.71 ?  348 SER B CB  1 
ATOM   5473 O  OG  . SER B 1 348 ? -26.875 -34.554 2.579   1.00 47.61 ?  348 SER B OG  1 
ATOM   5474 N  N   . ASN B 1 349 ? -28.218 -31.759 1.586   1.00 29.11 ?  349 ASN B N   1 
ATOM   5475 C  CA  . ASN B 1 349 ? -28.071 -30.355 1.980   1.00 27.31 ?  349 ASN B CA  1 
ATOM   5476 C  C   . ASN B 1 349 ? -28.300 -30.194 3.476   1.00 25.55 ?  349 ASN B C   1 
ATOM   5477 O  O   . ASN B 1 349 ? -29.305 -29.625 3.907   1.00 25.75 ?  349 ASN B O   1 
ATOM   5478 C  CB  . ASN B 1 349 ? -29.024 -29.467 1.188   1.00 26.33 ?  349 ASN B CB  1 
ATOM   5479 C  CG  . ASN B 1 349 ? -28.477 -28.078 0.987   1.00 25.11 ?  349 ASN B CG  1 
ATOM   5480 O  OD1 . ASN B 1 349 ? -27.507 -27.678 1.644   1.00 27.28 ?  349 ASN B OD1 1 
ATOM   5481 N  ND2 . ASN B 1 349 ? -29.077 -27.333 0.065   1.00 24.80 ?  349 ASN B ND2 1 
ATOM   5482 N  N   . PRO B 1 350 ? -27.349 -30.646 4.302   1.00 27.54 ?  350 PRO B N   1 
ATOM   5483 C  CA  . PRO B 1 350 ? -27.480 -30.528 5.770   1.00 25.49 ?  350 PRO B CA  1 
ATOM   5484 C  C   . PRO B 1 350 ? -26.957 -29.208 6.343   1.00 25.46 ?  350 PRO B C   1 
ATOM   5485 O  O   . PRO B 1 350 ? -26.186 -29.176 7.314   1.00 28.72 ?  350 PRO B O   1 
ATOM   5486 C  CB  . PRO B 1 350 ? -26.682 -31.742 6.261   1.00 25.99 ?  350 PRO B CB  1 
ATOM   5487 C  CG  . PRO B 1 350 ? -25.555 -31.847 5.260   1.00 26.99 ?  350 PRO B CG  1 
ATOM   5488 C  CD  . PRO B 1 350 ? -26.138 -31.393 3.917   1.00 26.88 ?  350 PRO B CD  1 
ATOM   5489 N  N   . HIS B 1 351 ? -27.397 -28.098 5.756   1.00 22.44 ?  351 HIS B N   1 
ATOM   5490 C  CA  . HIS B 1 351 ? -26.906 -26.777 6.128   1.00 22.62 ?  351 HIS B CA  1 
ATOM   5491 C  C   . HIS B 1 351 ? -27.340 -26.353 7.535   1.00 25.35 ?  351 HIS B C   1 
ATOM   5492 O  O   . HIS B 1 351 ? -28.315 -26.867 8.096   1.00 23.37 ?  351 HIS B O   1 
ATOM   5493 C  CB  . HIS B 1 351 ? -27.417 -25.764 5.119   1.00 20.36 ?  351 HIS B CB  1 
ATOM   5494 C  CG  . HIS B 1 351 ? -28.909 -25.690 5.071   1.00 22.45 ?  351 HIS B CG  1 
ATOM   5495 N  ND1 . HIS B 1 351 ? -29.650 -25.045 6.038   1.00 23.49 ?  351 HIS B ND1 1 
ATOM   5496 C  CD2 . HIS B 1 351 ? -29.801 -26.211 4.196   1.00 23.40 ?  351 HIS B CD2 1 
ATOM   5497 C  CE1 . HIS B 1 351 ? -30.935 -25.160 5.755   1.00 21.90 ?  351 HIS B CE1 1 
ATOM   5498 N  NE2 . HIS B 1 351 ? -31.056 -25.860 4.640   1.00 26.28 ?  351 HIS B NE2 1 
ATOM   5499 N  N   . LEU B 1 352 ? -26.637 -25.347 8.069   1.00 23.64 ?  352 LEU B N   1 
ATOM   5500 C  CA  . LEU B 1 352 ? -26.858 -24.816 9.415   1.00 25.14 ?  352 LEU B CA  1 
ATOM   5501 C  C   . LEU B 1 352 ? -27.558 -23.455 9.413   1.00 26.63 ?  352 LEU B C   1 
ATOM   5502 O  O   . LEU B 1 352 ? -27.407 -22.673 10.360  1.00 21.12 ?  352 LEU B O   1 
ATOM   5503 C  CB  . LEU B 1 352 ? -25.524 -24.705 10.159  1.00 23.18 ?  352 LEU B CB  1 
ATOM   5504 C  CG  . LEU B 1 352 ? -24.670 -25.968 10.215  1.00 22.82 ?  352 LEU B CG  1 
ATOM   5505 C  CD1 . LEU B 1 352 ? -23.427 -25.741 11.062  1.00 21.46 ?  352 LEU B CD1 1 
ATOM   5506 C  CD2 . LEU B 1 352 ? -25.501 -27.080 10.779  1.00 29.24 ?  352 LEU B CD2 1 
ATOM   5507 N  N   . ALA B 1 353 ? -28.328 -23.154 8.360   1.00 23.76 ?  353 ALA B N   1 
ATOM   5508 C  CA  . ALA B 1 353 ? -28.929 -21.826 8.238   1.00 24.82 ?  353 ALA B CA  1 
ATOM   5509 C  C   . ALA B 1 353 ? -29.917 -21.539 9.364   1.00 26.56 ?  353 ALA B C   1 
ATOM   5510 O  O   . ALA B 1 353 ? -30.152 -20.373 9.705   1.00 22.60 ?  353 ALA B O   1 
ATOM   5511 C  CB  . ALA B 1 353 ? -29.627 -21.688 6.882   1.00 21.57 ?  353 ALA B CB  1 
ATOM   5512 N  N   . PHE B 1 354 ? -30.517 -22.583 9.933   1.00 25.34 ?  354 PHE B N   1 
ATOM   5513 C  CA  . PHE B 1 354 ? -31.435 -22.478 11.056  1.00 21.80 ?  354 PHE B CA  1 
ATOM   5514 C  C   . PHE B 1 354 ? -30.766 -22.827 12.381  1.00 26.86 ?  354 PHE B C   1 
ATOM   5515 O  O   . PHE B 1 354 ? -31.461 -23.009 13.384  1.00 23.74 ?  354 PHE B O   1 
ATOM   5516 C  CB  . PHE B 1 354 ? -32.643 -23.399 10.834  1.00 19.99 ?  354 PHE B CB  1 
ATOM   5517 C  CG  . PHE B 1 354 ? -33.656 -22.858 9.860   1.00 21.89 ?  354 PHE B CG  1 
ATOM   5518 C  CD1 . PHE B 1 354 ? -34.299 -21.655 10.102  1.00 26.55 ?  354 PHE B CD1 1 
ATOM   5519 C  CD2 . PHE B 1 354 ? -33.963 -23.550 8.702   1.00 21.00 ?  354 PHE B CD2 1 
ATOM   5520 C  CE1 . PHE B 1 354 ? -35.244 -21.158 9.202   1.00 23.57 ?  354 PHE B CE1 1 
ATOM   5521 C  CE2 . PHE B 1 354 ? -34.890 -23.062 7.805   1.00 22.45 ?  354 PHE B CE2 1 
ATOM   5522 C  CZ  . PHE B 1 354 ? -35.533 -21.864 8.045   1.00 23.40 ?  354 PHE B CZ  1 
ATOM   5523 N  N   . GLY B 1 355 ? -29.440 -22.952 12.397  1.00 26.75 ?  355 GLY B N   1 
ATOM   5524 C  CA  . GLY B 1 355 ? -28.729 -23.404 13.574  1.00 25.86 ?  355 GLY B CA  1 
ATOM   5525 C  C   . GLY B 1 355 ? -28.843 -24.910 13.701  1.00 30.66 ?  355 GLY B C   1 
ATOM   5526 O  O   . GLY B 1 355 ? -29.218 -25.627 12.763  1.00 25.58 ?  355 GLY B O   1 
ATOM   5527 N  N   . GLY B 1 356 ? -28.454 -25.409 14.861  1.00 23.52 ?  356 GLY B N   1 
ATOM   5528 C  CA  . GLY B 1 356 ? -28.546 -26.831 15.147  1.00 31.62 ?  356 GLY B CA  1 
ATOM   5529 C  C   . GLY B 1 356 ? -28.541 -27.095 16.639  1.00 28.85 ?  356 GLY B C   1 
ATOM   5530 O  O   . GLY B 1 356 ? -28.356 -26.188 17.454  1.00 24.82 ?  356 GLY B O   1 
ATOM   5531 N  N   . GLY B 1 357 ? -28.744 -28.366 16.991  1.00 31.17 ?  357 GLY B N   1 
ATOM   5532 C  CA  . GLY B 1 357 ? -28.714 -28.719 18.403  1.00 28.67 ?  357 GLY B CA  1 
ATOM   5533 C  C   . GLY B 1 357 ? -29.901 -28.111 19.136  1.00 28.91 ?  357 GLY B C   1 
ATOM   5534 O  O   . GLY B 1 357 ? -30.947 -27.824 18.552  1.00 26.85 ?  357 GLY B O   1 
ATOM   5535 N  N   . GLN B 1 358 ? -29.718 -27.884 20.443  1.00 30.56 ?  358 GLN B N   1 
ATOM   5536 C  CA  . GLN B 1 358 ? -30.839 -27.483 21.288  1.00 30.00 ?  358 GLN B CA  1 
ATOM   5537 C  C   . GLN B 1 358 ? -31.563 -26.220 20.816  1.00 25.05 ?  358 GLN B C   1 
ATOM   5538 O  O   . GLN B 1 358 ? -32.780 -26.103 20.989  1.00 28.97 ?  358 GLN B O   1 
ATOM   5539 C  CB  . GLN B 1 358 ? -30.344 -27.322 22.730  1.00 30.62 ?  358 GLN B CB  1 
ATOM   5540 C  CG  . GLN B 1 358 ? -31.434 -26.927 23.724  1.00 38.78 ?  358 GLN B CG  1 
ATOM   5541 C  CD  . GLN B 1 358 ? -30.866 -26.397 25.027  1.00 44.31 ?  358 GLN B CD  1 
ATOM   5542 O  OE1 . GLN B 1 358 ? -29.691 -26.614 25.336  1.00 42.76 ?  358 GLN B OE1 1 
ATOM   5543 N  NE2 . GLN B 1 358 ? -31.692 -25.691 25.794  1.00 45.26 ?  358 GLN B NE2 1 
ATOM   5544 N  N   . HIS B 1 359 ? -30.857 -25.278 20.198  1.00 31.06 ?  359 HIS B N   1 
ATOM   5545 C  CA  . HIS B 1 359 ? -31.478 -24.007 19.844  1.00 29.56 ?  359 HIS B CA  1 
ATOM   5546 C  C   . HIS B 1 359 ? -31.801 -23.885 18.356  1.00 30.07 ?  359 HIS B C   1 
ATOM   5547 O  O   . HIS B 1 359 ? -32.091 -22.774 17.887  1.00 31.61 ?  359 HIS B O   1 
ATOM   5548 C  CB  . HIS B 1 359 ? -30.588 -22.862 20.317  1.00 26.06 ?  359 HIS B CB  1 
ATOM   5549 C  CG  . HIS B 1 359 ? -30.352 -22.876 21.795  1.00 30.52 ?  359 HIS B CG  1 
ATOM   5550 N  ND1 . HIS B 1 359 ? -31.351 -22.599 22.708  1.00 31.22 ?  359 HIS B ND1 1 
ATOM   5551 C  CD2 . HIS B 1 359 ? -29.242 -23.148 22.522  1.00 26.83 ?  359 HIS B CD2 1 
ATOM   5552 C  CE1 . HIS B 1 359 ? -30.861 -22.681 23.932  1.00 30.71 ?  359 HIS B CE1 1 
ATOM   5553 N  NE2 . HIS B 1 359 ? -29.583 -23.013 23.848  1.00 30.75 ?  359 HIS B NE2 1 
ATOM   5554 N  N   . PHE B 1 360 ? -31.753 -24.996 17.606  1.00 29.29 ?  360 PHE B N   1 
ATOM   5555 C  CA  . PHE B 1 360 ? -32.277 -25.043 16.243  1.00 25.71 ?  360 PHE B CA  1 
ATOM   5556 C  C   . PHE B 1 360 ? -33.586 -24.274 16.170  1.00 30.32 ?  360 PHE B C   1 
ATOM   5557 O  O   . PHE B 1 360 ? -34.437 -24.382 17.054  1.00 29.37 ?  360 PHE B O   1 
ATOM   5558 C  CB  . PHE B 1 360 ? -32.496 -26.496 15.797  1.00 28.44 ?  360 PHE B CB  1 
ATOM   5559 C  CG  . PHE B 1 360 ? -32.959 -26.645 14.355  1.00 28.72 ?  360 PHE B CG  1 
ATOM   5560 C  CD1 . PHE B 1 360 ? -32.034 -26.704 13.314  1.00 29.09 ?  360 PHE B CD1 1 
ATOM   5561 C  CD2 . PHE B 1 360 ? -34.314 -26.741 14.046  1.00 28.77 ?  360 PHE B CD2 1 
ATOM   5562 C  CE1 . PHE B 1 360 ? -32.448 -26.860 11.990  1.00 23.72 ?  360 PHE B CE1 1 
ATOM   5563 C  CE2 . PHE B 1 360 ? -34.742 -26.900 12.736  1.00 26.14 ?  360 PHE B CE2 1 
ATOM   5564 C  CZ  . PHE B 1 360 ? -33.807 -26.952 11.699  1.00 25.15 ?  360 PHE B CZ  1 
ATOM   5565 N  N   . CYS B 1 361 ? -33.719 -23.464 15.128  1.00 29.30 ?  361 CYS B N   1 
ATOM   5566 C  CA  . CYS B 1 361 ? -34.835 -22.545 15.007  1.00 27.44 ?  361 CYS B CA  1 
ATOM   5567 C  C   . CYS B 1 361 ? -36.175 -23.269 15.163  1.00 28.24 ?  361 CYS B C   1 
ATOM   5568 O  O   . CYS B 1 361 ? -36.476 -24.185 14.384  1.00 26.52 ?  361 CYS B O   1 
ATOM   5569 C  CB  . CYS B 1 361 ? -34.788 -21.823 13.667  1.00 25.64 ?  361 CYS B CB  1 
ATOM   5570 S  SG  . CYS B 1 361 ? -36.246 -20.834 13.447  1.00 23.82 ?  361 CYS B SG  1 
ATOM   5571 N  N   . PRO B 1 362 ? -36.998 -22.882 16.140  1.00 28.61 ?  362 PRO B N   1 
ATOM   5572 C  CA  . PRO B 1 362 ? -38.325 -23.498 16.292  1.00 22.56 ?  362 PRO B CA  1 
ATOM   5573 C  C   . PRO B 1 362 ? -39.313 -23.078 15.232  1.00 25.63 ?  362 PRO B C   1 
ATOM   5574 O  O   . PRO B 1 362 ? -40.435 -23.604 15.214  1.00 25.94 ?  362 PRO B O   1 
ATOM   5575 C  CB  . PRO B 1 362 ? -38.775 -22.999 17.669  1.00 30.89 ?  362 PRO B CB  1 
ATOM   5576 C  CG  . PRO B 1 362 ? -38.162 -21.611 17.720  1.00 30.89 ?  362 PRO B CG  1 
ATOM   5577 C  CD  . PRO B 1 362 ? -36.779 -21.795 17.104  1.00 24.43 ?  362 PRO B CD  1 
ATOM   5578 N  N   . ALA B 1 363 ? -38.954 -22.128 14.369  1.00 22.39 ?  363 ALA B N   1 
ATOM   5579 C  CA  . ALA B 1 363 ? -39.861 -21.642 13.347  1.00 25.88 ?  363 ALA B CA  1 
ATOM   5580 C  C   . ALA B 1 363 ? -39.421 -22.043 11.938  1.00 25.47 ?  363 ALA B C   1 
ATOM   5581 O  O   . ALA B 1 363 ? -39.912 -21.473 10.956  1.00 25.12 ?  363 ALA B O   1 
ATOM   5582 C  CB  . ALA B 1 363 ? -39.992 -20.126 13.463  1.00 26.85 ?  363 ALA B CB  1 
ATOM   5583 N  N   . SER B 1 364 ? -38.530 -23.031 11.819  1.00 22.84 ?  364 SER B N   1 
ATOM   5584 C  CA  . SER B 1 364 ? -37.909 -23.331 10.525  1.00 27.16 ?  364 SER B CA  1 
ATOM   5585 C  C   . SER B 1 364 ? -38.958 -23.592 9.450   1.00 27.58 ?  364 SER B C   1 
ATOM   5586 O  O   . SER B 1 364 ? -38.871 -23.053 8.336   1.00 26.97 ?  364 SER B O   1 
ATOM   5587 C  CB  . SER B 1 364 ? -36.958 -24.522 10.656  1.00 27.03 ?  364 SER B CB  1 
ATOM   5588 O  OG  . SER B 1 364 ? -37.629 -25.702 11.067  1.00 29.59 ?  364 SER B OG  1 
ATOM   5589 N  N   . ALA B 1 365 ? -39.979 -24.395 9.777   1.00 26.37 ?  365 ALA B N   1 
ATOM   5590 C  CA  . ALA B 1 365 ? -41.030 -24.699 8.808   1.00 26.07 ?  365 ALA B CA  1 
ATOM   5591 C  C   . ALA B 1 365 ? -41.765 -23.444 8.370   1.00 28.69 ?  365 ALA B C   1 
ATOM   5592 O  O   . ALA B 1 365 ? -42.126 -23.303 7.191   1.00 28.31 ?  365 ALA B O   1 
ATOM   5593 C  CB  . ALA B 1 365 ? -42.016 -25.711 9.397   1.00 30.66 ?  365 ALA B CB  1 
ATOM   5594 N  N   . LEU B 1 366 ? -42.012 -22.526 9.307   1.00 23.51 ?  366 LEU B N   1 
ATOM   5595 C  CA  . LEU B 1 366 ? -42.656 -21.264 8.956   1.00 26.20 ?  366 LEU B CA  1 
ATOM   5596 C  C   . LEU B 1 366 ? -41.742 -20.404 8.086   1.00 26.29 ?  366 LEU B C   1 
ATOM   5597 O  O   . LEU B 1 366 ? -42.183 -19.830 7.083   1.00 22.58 ?  366 LEU B O   1 
ATOM   5598 C  CB  . LEU B 1 366 ? -43.052 -20.508 10.225  1.00 26.70 ?  366 LEU B CB  1 
ATOM   5599 C  CG  . LEU B 1 366 ? -44.040 -19.341 10.072  1.00 32.31 ?  366 LEU B CG  1 
ATOM   5600 C  CD1 . LEU B 1 366 ? -45.248 -19.723 9.260   1.00 35.69 ?  366 LEU B CD1 1 
ATOM   5601 C  CD2 . LEU B 1 366 ? -44.451 -18.822 11.439  1.00 41.51 ?  366 LEU B CD2 1 
ATOM   5602 N  N   . GLY B 1 367 ? -40.472 -20.274 8.476   1.00 22.19 ?  367 GLY B N   1 
ATOM   5603 C  CA  . GLY B 1 367 ? -39.518 -19.566 7.632   1.00 23.19 ?  367 GLY B CA  1 
ATOM   5604 C  C   . GLY B 1 367 ? -39.494 -20.094 6.207   1.00 23.96 ?  367 GLY B C   1 
ATOM   5605 O  O   . GLY B 1 367 ? -39.556 -19.319 5.245   1.00 22.80 ?  367 GLY B O   1 
ATOM   5606 N  N   . ARG B 1 368 ? -39.439 -21.427 6.053   1.00 22.70 ?  368 ARG B N   1 
ATOM   5607 C  CA  . ARG B 1 368 ? -39.502 -22.039 4.723   1.00 24.71 ?  368 ARG B CA  1 
ATOM   5608 C  C   . ARG B 1 368 ? -40.787 -21.658 3.998   1.00 23.38 ?  368 ARG B C   1 
ATOM   5609 O  O   . ARG B 1 368 ? -40.759 -21.216 2.842   1.00 24.56 ?  368 ARG B O   1 
ATOM   5610 C  CB  . ARG B 1 368 ? -39.405 -23.567 4.818   1.00 21.30 ?  368 ARG B CB  1 
ATOM   5611 C  CG  . ARG B 1 368 ? -38.064 -24.116 5.271   1.00 22.74 ?  368 ARG B CG  1 
ATOM   5612 C  CD  . ARG B 1 368 ? -38.140 -25.638 5.473   1.00 25.39 ?  368 ARG B CD  1 
ATOM   5613 N  NE  . ARG B 1 368 ? -36.891 -26.188 5.988   1.00 29.06 ?  368 ARG B NE  1 
ATOM   5614 C  CZ  . ARG B 1 368 ? -35.778 -26.290 5.276   1.00 29.25 ?  368 ARG B CZ  1 
ATOM   5615 N  NH1 . ARG B 1 368 ? -35.726 -25.881 4.019   1.00 30.92 ?  368 ARG B NH1 1 
ATOM   5616 N  NH2 . ARG B 1 368 ? -34.692 -26.820 5.837   1.00 24.63 ?  368 ARG B NH2 1 
ATOM   5617 N  N   . THR B 1 369 ? -41.930 -21.851 4.658   1.00 24.38 ?  369 THR B N   1 
ATOM   5618 C  CA  . THR B 1 369 ? -43.217 -21.561 4.032   1.00 22.16 ?  369 THR B CA  1 
ATOM   5619 C  C   . THR B 1 369 ? -43.310 -20.102 3.599   1.00 22.53 ?  369 THR B C   1 
ATOM   5620 O  O   . THR B 1 369 ? -43.806 -19.801 2.512   1.00 23.47 ?  369 THR B O   1 
ATOM   5621 C  CB  . THR B 1 369 ? -44.352 -21.887 5.005   1.00 26.57 ?  369 THR B CB  1 
ATOM   5622 O  OG1 . THR B 1 369 ? -44.355 -23.292 5.290   1.00 32.10 ?  369 THR B OG1 1 
ATOM   5623 C  CG2 . THR B 1 369 ? -45.701 -21.481 4.401   1.00 26.62 ?  369 THR B CG2 1 
ATOM   5624 N  N   . HIS B 1 370 ? -42.875 -19.189 4.464   1.00 21.59 ?  370 HIS B N   1 
ATOM   5625 C  CA  . HIS B 1 370 ? -42.876 -17.761 4.153   1.00 22.81 ?  370 HIS B CA  1 
ATOM   5626 C  C   . HIS B 1 370 ? -42.126 -17.478 2.852   1.00 22.42 ?  370 HIS B C   1 
ATOM   5627 O  O   . HIS B 1 370 ? -42.644 -16.795 1.959   1.00 20.88 ?  370 HIS B O   1 
ATOM   5628 C  CB  . HIS B 1 370 ? -42.268 -17.013 5.349   1.00 21.07 ?  370 HIS B CB  1 
ATOM   5629 C  CG  . HIS B 1 370 ? -42.338 -15.518 5.275   1.00 24.46 ?  370 HIS B CG  1 
ATOM   5630 N  ND1 . HIS B 1 370 ? -41.444 -14.757 4.550   1.00 25.83 ?  370 HIS B ND1 1 
ATOM   5631 C  CD2 . HIS B 1 370 ? -43.158 -14.640 5.901   1.00 23.75 ?  370 HIS B CD2 1 
ATOM   5632 C  CE1 . HIS B 1 370 ? -41.740 -13.476 4.702   1.00 25.41 ?  370 HIS B CE1 1 
ATOM   5633 N  NE2 . HIS B 1 370 ? -42.771 -13.378 5.520   1.00 24.98 ?  370 HIS B NE2 1 
ATOM   5634 N  N   . ALA B 1 371 ? -40.912 -18.025 2.721   1.00 20.25 ?  371 ALA B N   1 
ATOM   5635 C  CA  . ALA B 1 371 ? -40.077 -17.755 1.547   1.00 20.19 ?  371 ALA B CA  1 
ATOM   5636 C  C   . ALA B 1 371 ? -40.553 -18.522 0.317   1.00 21.99 ?  371 ALA B C   1 
ATOM   5637 O  O   . ALA B 1 371 ? -40.528 -17.987 -0.801  1.00 21.63 ?  371 ALA B O   1 
ATOM   5638 C  CB  . ALA B 1 371 ? -38.620 -18.117 1.842   1.00 19.06 ?  371 ALA B CB  1 
ATOM   5639 N  N   . GLU B 1 372 ? -40.941 -19.790 0.485   1.00 18.99 ?  372 GLU B N   1 
ATOM   5640 C  CA  . GLU B 1 372 ? -41.445 -20.549 -0.659  1.00 22.22 ?  372 GLU B CA  1 
ATOM   5641 C  C   . GLU B 1 372 ? -42.579 -19.807 -1.340  1.00 22.98 ?  372 GLU B C   1 
ATOM   5642 O  O   . GLU B 1 372 ? -42.586 -19.637 -2.566  1.00 19.60 ?  372 GLU B O   1 
ATOM   5643 C  CB  . GLU B 1 372 ? -41.921 -21.936 -0.216  1.00 19.05 ?  372 GLU B CB  1 
ATOM   5644 C  CG  . GLU B 1 372 ? -40.777 -22.887 0.128   1.00 18.54 ?  372 GLU B CG  1 
ATOM   5645 C  CD  . GLU B 1 372 ? -41.282 -24.120 0.820   1.00 21.65 ?  372 GLU B CD  1 
ATOM   5646 O  OE1 . GLU B 1 372 ? -42.502 -24.328 0.772   1.00 24.70 ?  372 GLU B OE1 1 
ATOM   5647 O  OE2 . GLU B 1 372 ? -40.480 -24.857 1.429   1.00 23.30 ?  372 GLU B OE2 1 
ATOM   5648 N  N   . ILE B 1 373 ? -43.541 -19.336 -0.541  1.00 20.95 ?  373 ILE B N   1 
ATOM   5649 C  CA  . ILE B 1 373 ? -44.742 -18.728 -1.094  1.00 18.78 ?  373 ILE B CA  1 
ATOM   5650 C  C   . ILE B 1 373 ? -44.407 -17.408 -1.775  1.00 20.24 ?  373 ILE B C   1 
ATOM   5651 O  O   . ILE B 1 373 ? -44.864 -17.145 -2.893  1.00 22.76 ?  373 ILE B O   1 
ATOM   5652 C  CB  . ILE B 1 373 ? -45.806 -18.582 0.013   1.00 23.21 ?  373 ILE B CB  1 
ATOM   5653 C  CG1 . ILE B 1 373 ? -46.443 -19.949 0.282   1.00 23.04 ?  373 ILE B CG1 1 
ATOM   5654 C  CG2 . ILE B 1 373 ? -46.870 -17.575 -0.373  1.00 23.59 ?  373 ILE B CG2 1 
ATOM   5655 C  CD1 . ILE B 1 373 ? -47.363 -20.001 1.520   1.00 23.76 ?  373 ILE B CD1 1 
ATOM   5656 N  N   . ALA B 1 374 ? -43.560 -16.588 -1.145  1.00 19.03 ?  374 ALA B N   1 
ATOM   5657 C  CA  . ALA B 1 374 ? -43.189 -15.293 -1.716  1.00 20.43 ?  374 ALA B CA  1 
ATOM   5658 C  C   . ALA B 1 374 ? -42.450 -15.450 -3.042  1.00 19.10 ?  374 ALA B C   1 
ATOM   5659 O  O   . ALA B 1 374 ? -42.735 -14.739 -4.011  1.00 17.12 ?  374 ALA B O   1 
ATOM   5660 C  CB  . ALA B 1 374 ? -42.327 -14.511 -0.718  1.00 17.83 ?  374 ALA B CB  1 
ATOM   5661 N  N   . LEU B 1 375 ? -41.477 -16.370 -3.098  1.00 22.38 ?  375 LEU B N   1 
ATOM   5662 C  CA  . LEU B 1 375 ? -40.683 -16.521 -4.315  1.00 20.33 ?  375 LEU B CA  1 
ATOM   5663 C  C   . LEU B 1 375 ? -41.505 -17.144 -5.439  1.00 21.61 ?  375 LEU B C   1 
ATOM   5664 O  O   . LEU B 1 375 ? -41.345 -16.768 -6.610  1.00 21.48 ?  375 LEU B O   1 
ATOM   5665 C  CB  . LEU B 1 375 ? -39.431 -17.346 -4.018  1.00 19.87 ?  375 LEU B CB  1 
ATOM   5666 C  CG  . LEU B 1 375 ? -38.522 -16.707 -2.961  1.00 20.93 ?  375 LEU B CG  1 
ATOM   5667 C  CD1 . LEU B 1 375 ? -37.538 -17.731 -2.374  1.00 22.71 ?  375 LEU B CD1 1 
ATOM   5668 C  CD2 . LEU B 1 375 ? -37.781 -15.490 -3.510  1.00 19.79 ?  375 LEU B CD2 1 
ATOM   5669 N  N   . THR B 1 376 ? -42.402 -18.085 -5.104  1.00 21.67 ?  376 THR B N   1 
ATOM   5670 C  CA  . THR B 1 376 ? -43.311 -18.640 -6.113  1.00 24.62 ?  376 THR B CA  1 
ATOM   5671 C  C   . THR B 1 376 ? -44.136 -17.538 -6.765  1.00 24.01 ?  376 THR B C   1 
ATOM   5672 O  O   . THR B 1 376 ? -44.248 -17.472 -7.994  1.00 24.17 ?  376 THR B O   1 
ATOM   5673 C  CB  . THR B 1 376 ? -44.243 -19.692 -5.494  1.00 21.14 ?  376 THR B CB  1 
ATOM   5674 O  OG1 . THR B 1 376 ? -43.473 -20.826 -5.069  1.00 21.49 ?  376 THR B OG1 1 
ATOM   5675 C  CG2 . THR B 1 376 ? -45.290 -20.141 -6.515  1.00 20.71 ?  376 THR B CG2 1 
ATOM   5676 N  N   . ALA B 1 377 ? -44.715 -16.654 -5.950  1.00 22.17 ?  377 ALA B N   1 
ATOM   5677 C  CA  . ALA B 1 377 ? -45.467 -15.533 -6.504  1.00 26.81 ?  377 ALA B CA  1 
ATOM   5678 C  C   . ALA B 1 377 ? -44.553 -14.570 -7.245  1.00 23.66 ?  377 ALA B C   1 
ATOM   5679 O  O   . ALA B 1 377 ? -44.955 -13.980 -8.256  1.00 23.47 ?  377 ALA B O   1 
ATOM   5680 C  CB  . ALA B 1 377 ? -46.222 -14.798 -5.391  1.00 24.51 ?  377 ALA B CB  1 
ATOM   5681 N  N   . LEU B 1 378 ? -43.312 -14.422 -6.779  1.00 22.30 ?  378 LEU B N   1 
ATOM   5682 C  CA  . LEU B 1 378 ? -42.400 -13.481 -7.417  1.00 21.41 ?  378 LEU B CA  1 
ATOM   5683 C  C   . LEU B 1 378 ? -42.043 -13.920 -8.837  1.00 21.04 ?  378 LEU B C   1 
ATOM   5684 O  O   . LEU B 1 378 ? -42.105 -13.118 -9.777  1.00 20.77 ?  378 LEU B O   1 
ATOM   5685 C  CB  . LEU B 1 378 ? -41.146 -13.321 -6.556  1.00 21.84 ?  378 LEU B CB  1 
ATOM   5686 C  CG  . LEU B 1 378 ? -40.127 -12.316 -7.079  1.00 23.44 ?  378 LEU B CG  1 
ATOM   5687 C  CD1 . LEU B 1 378 ? -40.682 -10.900 -6.982  1.00 26.48 ?  378 LEU B CD1 1 
ATOM   5688 C  CD2 . LEU B 1 378 ? -38.835 -12.422 -6.296  1.00 20.58 ?  378 LEU B CD2 1 
ATOM   5689 N  N   . VAL B 1 379 ? -41.654 -15.188 -9.018  1.00 19.73 ?  379 VAL B N   1 
ATOM   5690 C  CA  . VAL B 1 379 ? -41.220 -15.604 -10.351 1.00 20.36 ?  379 VAL B CA  1 
ATOM   5691 C  C   . VAL B 1 379 ? -42.402 -15.661 -11.310 1.00 23.10 ?  379 VAL B C   1 
ATOM   5692 O  O   . VAL B 1 379 ? -42.225 -15.507 -12.531 1.00 26.17 ?  379 VAL B O   1 
ATOM   5693 C  CB  . VAL B 1 379 ? -40.469 -16.952 -10.309 1.00 19.15 ?  379 VAL B CB  1 
ATOM   5694 C  CG1 . VAL B 1 379 ? -39.275 -16.876 -9.381  1.00 19.23 ?  379 VAL B CG1 1 
ATOM   5695 C  CG2 . VAL B 1 379 ? -41.405 -18.079 -9.896  1.00 19.00 ?  379 VAL B CG2 1 
ATOM   5696 N  N   . GLU B 1 380 ? -43.619 -15.870 -10.793 1.00 20.49 ?  380 GLU B N   1 
ATOM   5697 C  CA  . GLU B 1 380 ? -44.798 -15.840 -11.652 1.00 23.72 ?  380 GLU B CA  1 
ATOM   5698 C  C   . GLU B 1 380 ? -45.129 -14.418 -12.076 1.00 22.46 ?  380 GLU B C   1 
ATOM   5699 O  O   . GLU B 1 380 ? -45.420 -14.168 -13.252 1.00 24.87 ?  380 GLU B O   1 
ATOM   5700 C  CB  . GLU B 1 380 ? -46.009 -16.465 -10.943 1.00 28.32 ?  380 GLU B CB  1 
ATOM   5701 C  CG  . GLU B 1 380 ? -45.871 -17.954 -10.581 1.00 33.44 ?  380 GLU B CG  1 
ATOM   5702 C  CD  . GLU B 1 380 ? -46.941 -18.440 -9.587  1.00 39.93 ?  380 GLU B CD  1 
ATOM   5703 O  OE1 . GLU B 1 380 ? -47.242 -17.721 -8.607  1.00 36.74 ?  380 GLU B OE1 1 
ATOM   5704 O  OE2 . GLU B 1 380 ? -47.463 -19.569 -9.768  1.00 42.88 ?  380 GLU B OE2 1 
ATOM   5705 N  N   . LYS B 1 381 ? -45.131 -13.476 -11.124 1.00 26.54 ?  381 LYS B N   1 
ATOM   5706 C  CA  . LYS B 1 381 ? -45.591 -12.089 -11.425 1.00 26.70 ?  381 LYS B CA  1 
ATOM   5707 C  C   . LYS B 1 381 ? -44.524 -11.241 -12.129 1.00 26.19 ?  381 LYS B C   1 
ATOM   5708 O  O   . LYS B 1 381 ? -44.915 -10.401 -12.968 1.00 27.70 ?  381 LYS B O   1 
ATOM   5709 C  CB  . LYS B 1 381 ? -45.959 -11.362 -10.127 1.00 24.05 ?  381 LYS B CB  1 
ATOM   5710 C  CG  . LYS B 1 381 ? -47.085 -11.991 -9.322  1.00 31.09 ?  381 LYS B CG  1 
ATOM   5711 C  CD  . LYS B 1 381 ? -48.420 -11.986 -10.054 1.00 31.56 ?  381 LYS B CD  1 
ATOM   5712 C  CE  . LYS B 1 381 ? -49.514 -12.545 -9.207  1.00 37.89 ?  381 LYS B CE  1 
ATOM   5713 N  NZ  . LYS B 1 381 ? -50.801 -12.567 -9.909  1.00 30.31 ?  381 LYS B NZ  1 
ATOM   5714 N  N   . LEU B 1 382 ? -43.247 -11.419 -11.786 1.00 23.25 ?  382 LEU B N   1 
ATOM   5715 C  CA  . LEU B 1 382 ? -42.164 -10.608 -12.344 1.00 20.45 ?  382 LEU B CA  1 
ATOM   5716 C  C   . LEU B 1 382 ? -41.184 -11.527 -13.075 1.00 25.13 ?  382 LEU B C   1 
ATOM   5717 O  O   . LEU B 1 382 ? -40.038 -11.715 -12.634 1.00 22.15 ?  382 LEU B O   1 
ATOM   5718 C  CB  . LEU B 1 382 ? -41.451 -9.817  -11.245 1.00 23.21 ?  382 LEU B CB  1 
ATOM   5719 C  CG  . LEU B 1 382 ? -42.294 -8.946  -10.297 1.00 25.25 ?  382 LEU B CG  1 
ATOM   5720 C  CD1 . LEU B 1 382 ? -41.392 -8.132  -9.357  1.00 22.23 ?  382 LEU B CD1 1 
ATOM   5721 C  CD2 . LEU B 1 382 ? -43.226 -8.033  -11.076 1.00 19.97 ?  382 LEU B CD2 1 
ATOM   5722 N  N   . PRO B 1 383 ? -41.598 -12.112 -14.207 1.00 21.84 ?  383 PRO B N   1 
ATOM   5723 C  CA  . PRO B 1 383 ? -40.722 -13.092 -14.876 1.00 23.54 ?  383 PRO B CA  1 
ATOM   5724 C  C   . PRO B 1 383 ? -39.424 -12.513 -15.422 1.00 22.91 ?  383 PRO B C   1 
ATOM   5725 O  O   . PRO B 1 383 ? -38.491 -13.284 -15.650 1.00 27.19 ?  383 PRO B O   1 
ATOM   5726 C  CB  . PRO B 1 383 ? -41.600 -13.649 -16.010 1.00 25.60 ?  383 PRO B CB  1 
ATOM   5727 C  CG  . PRO B 1 383 ? -42.638 -12.603 -16.250 1.00 25.95 ?  383 PRO B CG  1 
ATOM   5728 C  CD  . PRO B 1 383 ? -42.905 -11.998 -14.876 1.00 24.33 ?  383 PRO B CD  1 
ATOM   5729 N  N   . ALA B 1 384 ? -39.314 -11.204 -15.644 1.00 23.43 ?  384 ALA B N   1 
ATOM   5730 C  CA  . ALA B 1 384 ? -38.072 -10.635 -16.143 1.00 20.74 ?  384 ALA B CA  1 
ATOM   5731 C  C   . ALA B 1 384 ? -37.285 -9.918  -15.042 1.00 23.83 ?  384 ALA B C   1 
ATOM   5732 O  O   . ALA B 1 384 ? -36.432 -9.070  -15.341 1.00 20.48 ?  384 ALA B O   1 
ATOM   5733 C  CB  . ALA B 1 384 ? -38.355 -9.700  -17.324 1.00 22.43 ?  384 ALA B CB  1 
ATOM   5734 N  N   . LEU B 1 385 ? -37.571 -10.252 -13.781 1.00 21.84 ?  385 LEU B N   1 
ATOM   5735 C  CA  . LEU B 1 385 ? -36.920 -9.674  -12.609 1.00 21.75 ?  385 LEU B CA  1 
ATOM   5736 C  C   . LEU B 1 385 ? -35.404 -9.613  -12.763 1.00 22.29 ?  385 LEU B C   1 
ATOM   5737 O  O   . LEU B 1 385 ? -34.753 -10.616 -13.063 1.00 20.07 ?  385 LEU B O   1 
ATOM   5738 C  CB  . LEU B 1 385 ? -37.265 -10.512 -11.374 1.00 19.05 ?  385 LEU B CB  1 
ATOM   5739 C  CG  . LEU B 1 385 ? -36.615 -10.110 -10.050 1.00 21.58 ?  385 LEU B CG  1 
ATOM   5740 C  CD1 . LEU B 1 385 ? -37.282 -8.849  -9.489  1.00 18.10 ?  385 LEU B CD1 1 
ATOM   5741 C  CD2 . LEU B 1 385 ? -36.719 -11.243 -9.046  1.00 18.79 ?  385 LEU B CD2 1 
ATOM   5742 N  N   . ARG B 1 386 ? -34.850 -8.428  -12.519 1.00 21.47 ?  386 ARG B N   1 
ATOM   5743 C  CA  . ARG B 1 386 ? -33.413 -8.212  -12.525 1.00 20.01 ?  386 ARG B CA  1 
ATOM   5744 C  C   . ARG B 1 386 ? -33.161 -6.973  -11.686 1.00 20.39 ?  386 ARG B C   1 
ATOM   5745 O  O   . ARG B 1 386 ? -34.067 -6.168  -11.469 1.00 18.84 ?  386 ARG B O   1 
ATOM   5746 C  CB  . ARG B 1 386 ? -32.880 -8.026  -13.951 1.00 19.22 ?  386 ARG B CB  1 
ATOM   5747 C  CG  . ARG B 1 386 ? -33.537 -6.844  -14.679 1.00 20.37 ?  386 ARG B CG  1 
ATOM   5748 C  CD  . ARG B 1 386 ? -33.335 -6.940  -16.177 1.00 24.64 ?  386 ARG B CD  1 
ATOM   5749 N  NE  . ARG B 1 386 ? -33.842 -5.775  -16.893 1.00 23.27 ?  386 ARG B NE  1 
ATOM   5750 C  CZ  . ARG B 1 386 ? -35.098 -5.634  -17.289 1.00 24.55 ?  386 ARG B CZ  1 
ATOM   5751 N  NH1 . ARG B 1 386 ? -36.028 -6.524  -16.971 1.00 26.45 ?  386 ARG B NH1 1 
ATOM   5752 N  NH2 . ARG B 1 386 ? -35.431 -4.583  -18.032 1.00 19.09 ?  386 ARG B NH2 1 
ATOM   5753 N  N   . LEU B 1 387 ? -31.919 -6.819  -11.231 1.00 19.10 ?  387 LEU B N   1 
ATOM   5754 C  CA  . LEU B 1 387 ? -31.550 -5.644  -10.461 1.00 20.25 ?  387 LEU B CA  1 
ATOM   5755 C  C   . LEU B 1 387 ? -31.513 -4.418  -11.374 1.00 22.82 ?  387 LEU B C   1 
ATOM   5756 O  O   . LEU B 1 387 ? -31.238 -4.512  -12.572 1.00 21.38 ?  387 LEU B O   1 
ATOM   5757 C  CB  . LEU B 1 387 ? -30.188 -5.849  -9.798  1.00 17.61 ?  387 LEU B CB  1 
ATOM   5758 C  CG  . LEU B 1 387 ? -29.996 -7.006  -8.821  1.00 19.20 ?  387 LEU B CG  1 
ATOM   5759 C  CD1 . LEU B 1 387 ? -28.572 -6.964  -8.252  1.00 20.38 ?  387 LEU B CD1 1 
ATOM   5760 C  CD2 . LEU B 1 387 ? -31.020 -6.971  -7.703  1.00 19.61 ?  387 LEU B CD2 1 
ATOM   5761 N  N   . ALA B 1 388 ? -31.811 -3.259  -10.798 1.00 23.42 ?  388 ALA B N   1 
ATOM   5762 C  CA  . ALA B 1 388 ? -31.905 -2.031  -11.574 1.00 23.16 ?  388 ALA B CA  1 
ATOM   5763 C  C   . ALA B 1 388 ? -30.550 -1.401  -11.836 1.00 20.90 ?  388 ALA B C   1 
ATOM   5764 O  O   . ALA B 1 388 ? -30.461 -0.464  -12.634 1.00 23.39 ?  388 ALA B O   1 
ATOM   5765 C  CB  . ALA B 1 388 ? -32.810 -1.021  -10.856 1.00 18.81 ?  388 ALA B CB  1 
ATOM   5766 N  N   . LEU B 1 389 ? -29.513 -1.896  -11.176 1.00 20.25 ?  389 LEU B N   1 
ATOM   5767 C  CA  . LEU B 1 389 ? -28.158 -1.371  -11.249 1.00 22.39 ?  389 LEU B CA  1 
ATOM   5768 C  C   . LEU B 1 389 ? -27.218 -2.505  -10.858 1.00 19.47 ?  389 LEU B C   1 
ATOM   5769 O  O   . LEU B 1 389 ? -27.675 -3.565  -10.418 1.00 20.59 ?  389 LEU B O   1 
ATOM   5770 C  CB  . LEU B 1 389 ? -27.989 -0.145  -10.330 1.00 21.85 ?  389 LEU B CB  1 
ATOM   5771 C  CG  . LEU B 1 389 ? -28.187 -0.326  -8.823  1.00 23.47 ?  389 LEU B CG  1 
ATOM   5772 C  CD1 . LEU B 1 389 ? -26.930 -0.928  -8.202  1.00 25.59 ?  389 LEU B CD1 1 
ATOM   5773 C  CD2 . LEU B 1 389 ? -28.565 0.987   -8.121  1.00 23.48 ?  389 LEU B CD2 1 
ATOM   5774 N  N   . PRO B 1 390 ? -25.907 -2.340  -11.042 1.00 24.65 ?  390 PRO B N   1 
ATOM   5775 C  CA  . PRO B 1 390 ? -24.991 -3.443  -10.707 1.00 21.53 ?  390 PRO B CA  1 
ATOM   5776 C  C   . PRO B 1 390 ? -25.057 -3.827  -9.225  1.00 22.92 ?  390 PRO B C   1 
ATOM   5777 O  O   . PRO B 1 390 ? -25.153 -2.968  -8.345  1.00 20.15 ?  390 PRO B O   1 
ATOM   5778 C  CB  . PRO B 1 390 ? -23.613 -2.886  -11.084 1.00 24.25 ?  390 PRO B CB  1 
ATOM   5779 C  CG  . PRO B 1 390 ? -23.908 -1.855  -12.136 1.00 26.76 ?  390 PRO B CG  1 
ATOM   5780 C  CD  . PRO B 1 390 ? -25.206 -1.234  -11.731 1.00 22.81 ?  390 PRO B CD  1 
ATOM   5781 N  N   . VAL B 1 391 ? -24.977 -5.137  -8.957  1.00 19.53 ?  391 VAL B N   1 
ATOM   5782 C  CA  . VAL B 1 391 ? -25.159 -5.659  -7.597  1.00 21.12 ?  391 VAL B CA  1 
ATOM   5783 C  C   . VAL B 1 391 ? -24.154 -5.038  -6.626  1.00 20.68 ?  391 VAL B C   1 
ATOM   5784 O  O   . VAL B 1 391 ? -24.473 -4.831  -5.446  1.00 18.07 ?  391 VAL B O   1 
ATOM   5785 C  CB  . VAL B 1 391 ? -25.068 -7.212  -7.604  1.00 26.74 ?  391 VAL B CB  1 
ATOM   5786 C  CG1 . VAL B 1 391 ? -23.673 -7.696  -8.076  1.00 25.80 ?  391 VAL B CG1 1 
ATOM   5787 C  CG2 . VAL B 1 391 ? -25.421 -7.827  -6.223  1.00 20.81 ?  391 VAL B CG2 1 
ATOM   5788 N  N   . GLU B 1 392 ? -22.936 -4.724  -7.104  1.00 18.28 ?  392 GLU B N   1 
ATOM   5789 C  CA  . GLU B 1 392 ? -21.881 -4.118  -6.286  1.00 21.38 ?  392 GLU B CA  1 
ATOM   5790 C  C   . GLU B 1 392 ? -22.230 -2.723  -5.810  1.00 21.45 ?  392 GLU B C   1 
ATOM   5791 O  O   . GLU B 1 392 ? -21.474 -2.172  -5.003  1.00 17.78 ?  392 GLU B O   1 
ATOM   5792 C  CB  . GLU B 1 392 ? -20.554 -3.957  -7.041  1.00 21.45 ?  392 GLU B CB  1 
ATOM   5793 C  CG  . GLU B 1 392 ? -19.888 -5.208  -7.446  1.00 26.47 ?  392 GLU B CG  1 
ATOM   5794 C  CD  . GLU B 1 392 ? -20.427 -5.710  -8.759  1.00 31.41 ?  392 GLU B CD  1 
ATOM   5795 O  OE1 . GLU B 1 392 ? -21.371 -5.088  -9.315  1.00 38.59 ?  392 GLU B OE1 1 
ATOM   5796 O  OE2 . GLU B 1 392 ? -19.927 -6.750  -9.223  1.00 29.14 ?  392 GLU B OE2 1 
ATOM   5797 N  N   . GLN B 1 393 ? -23.298 -2.116  -6.338  1.00 17.90 ?  393 GLN B N   1 
ATOM   5798 C  CA  . GLN B 1 393 ? -23.708 -0.768  -5.968  1.00 19.47 ?  393 GLN B CA  1 
ATOM   5799 C  C   . GLN B 1 393 ? -24.902 -0.756  -5.018  1.00 21.21 ?  393 GLN B C   1 
ATOM   5800 O  O   . GLN B 1 393 ? -25.361 0.321   -4.626  1.00 21.91 ?  393 GLN B O   1 
ATOM   5801 C  CB  . GLN B 1 393 ? -24.001 0.038   -7.241  1.00 19.35 ?  393 GLN B CB  1 
ATOM   5802 C  CG  . GLN B 1 393 ? -22.715 0.301   -8.055  1.00 18.44 ?  393 GLN B CG  1 
ATOM   5803 C  CD  . GLN B 1 393 ? -22.952 1.012   -9.382  1.00 21.80 ?  393 GLN B CD  1 
ATOM   5804 O  OE1 . GLN B 1 393 ? -22.407 0.606   -10.402 1.00 26.62 ?  393 GLN B OE1 1 
ATOM   5805 N  NE2 . GLN B 1 393 ? -23.741 2.080   -9.368  1.00 20.05 ?  393 GLN B NE2 1 
ATOM   5806 N  N   . LEU B 1 394 ? -25.401 -1.927  -4.627  1.00 22.56 ?  394 LEU B N   1 
ATOM   5807 C  CA  . LEU B 1 394 ? -26.367 -2.010  -3.537  1.00 19.31 ?  394 LEU B CA  1 
ATOM   5808 C  C   . LEU B 1 394 ? -25.773 -1.424  -2.264  1.00 22.17 ?  394 LEU B C   1 
ATOM   5809 O  O   . LEU B 1 394 ? -24.582 -1.593  -1.983  1.00 17.28 ?  394 LEU B O   1 
ATOM   5810 C  CB  . LEU B 1 394 ? -26.768 -3.465  -3.290  1.00 17.75 ?  394 LEU B CB  1 
ATOM   5811 C  CG  . LEU B 1 394 ? -27.544 -4.131  -4.433  1.00 18.47 ?  394 LEU B CG  1 
ATOM   5812 C  CD1 . LEU B 1 394 ? -27.769 -5.584  -4.101  1.00 18.43 ?  394 LEU B CD1 1 
ATOM   5813 C  CD2 . LEU B 1 394 ? -28.871 -3.415  -4.678  1.00 16.57 ?  394 LEU B CD2 1 
ATOM   5814 N  N   . ALA B 1 395 ? -26.612 -0.728  -1.491  1.00 18.50 ?  395 ALA B N   1 
ATOM   5815 C  CA  . ALA B 1 395 ? -26.206 -0.196  -0.196  1.00 20.55 ?  395 ALA B CA  1 
ATOM   5816 C  C   . ALA B 1 395 ? -26.493 -1.258  0.861   1.00 18.59 ?  395 ALA B C   1 
ATOM   5817 O  O   . ALA B 1 395 ? -27.655 -1.595  1.114   1.00 20.25 ?  395 ALA B O   1 
ATOM   5818 C  CB  . ALA B 1 395 ? -26.943 1.101   0.122   1.00 17.90 ?  395 ALA B CB  1 
ATOM   5819 N  N   . TRP B 1 396 ? -25.442 -1.779  1.483   1.00 15.52 ?  396 TRP B N   1 
ATOM   5820 C  CA  . TRP B 1 396 ? -25.600 -2.799  2.511   1.00 18.64 ?  396 TRP B CA  1 
ATOM   5821 C  C   . TRP B 1 396 ? -25.627 -2.140  3.885   1.00 18.75 ?  396 TRP B C   1 
ATOM   5822 O  O   . TRP B 1 396 ? -24.772 -1.306  4.203   1.00 19.89 ?  396 TRP B O   1 
ATOM   5823 C  CB  . TRP B 1 396 ? -24.481 -3.836  2.413   1.00 17.49 ?  396 TRP B CB  1 
ATOM   5824 C  CG  . TRP B 1 396 ? -24.628 -4.702  1.182   1.00 16.62 ?  396 TRP B CG  1 
ATOM   5825 C  CD1 . TRP B 1 396 ? -24.025 -4.521  -0.035  1.00 20.81 ?  396 TRP B CD1 1 
ATOM   5826 C  CD2 . TRP B 1 396 ? -25.458 -5.868  1.050   1.00 20.53 ?  396 TRP B CD2 1 
ATOM   5827 N  NE1 . TRP B 1 396 ? -24.418 -5.517  -0.912  1.00 20.63 ?  396 TRP B NE1 1 
ATOM   5828 C  CE2 . TRP B 1 396 ? -25.301 -6.351  -0.270  1.00 21.77 ?  396 TRP B CE2 1 
ATOM   5829 C  CE3 . TRP B 1 396 ? -26.311 -6.556  1.923   1.00 20.72 ?  396 TRP B CE3 1 
ATOM   5830 C  CZ2 . TRP B 1 396 ? -25.966 -7.494  -0.736  1.00 20.60 ?  396 TRP B CZ2 1 
ATOM   5831 C  CZ3 . TRP B 1 396 ? -26.982 -7.701  1.450   1.00 20.10 ?  396 TRP B CZ3 1 
ATOM   5832 C  CH2 . TRP B 1 396 ? -26.799 -8.147  0.135   1.00 19.88 ?  396 TRP B CH2 1 
ATOM   5833 N  N   . ARG B 1 397 ? -26.626 -2.494  4.682   1.00 17.32 ?  397 ARG B N   1 
ATOM   5834 C  CA  . ARG B 1 397 ? -26.827 -1.811  5.948   1.00 18.56 ?  397 ARG B CA  1 
ATOM   5835 C  C   . ARG B 1 397 ? -25.659 -2.098  6.884   1.00 18.24 ?  397 ARG B C   1 
ATOM   5836 O  O   . ARG B 1 397 ? -25.262 -3.261  7.026   1.00 18.59 ?  397 ARG B O   1 
ATOM   5837 C  CB  . ARG B 1 397 ? -28.138 -2.239  6.602   1.00 16.68 ?  397 ARG B CB  1 
ATOM   5838 C  CG  . ARG B 1 397 ? -28.374 -1.534  7.934   1.00 17.40 ?  397 ARG B CG  1 
ATOM   5839 C  CD  . ARG B 1 397 ? -29.677 -1.944  8.600   1.00 17.95 ?  397 ARG B CD  1 
ATOM   5840 N  NE  . ARG B 1 397 ? -30.859 -1.466  7.886   1.00 19.10 ?  397 ARG B NE  1 
ATOM   5841 C  CZ  . ARG B 1 397 ? -32.094 -1.548  8.367   1.00 23.23 ?  397 ARG B CZ  1 
ATOM   5842 N  NH1 . ARG B 1 397 ? -32.335 -2.047  9.567   1.00 24.13 ?  397 ARG B NH1 1 
ATOM   5843 N  NH2 . ARG B 1 397 ? -33.114 -1.114  7.630   1.00 19.90 ?  397 ARG B NH2 1 
ATOM   5844 N  N   . PRO B 1 398 ? -25.074 -1.079  7.513   1.00 18.25 ?  398 PRO B N   1 
ATOM   5845 C  CA  . PRO B 1 398 ? -24.058 -1.304  8.548   1.00 18.17 ?  398 PRO B CA  1 
ATOM   5846 C  C   . PRO B 1 398 ? -24.659 -1.486  9.934   1.00 17.75 ?  398 PRO B C   1 
ATOM   5847 O  O   . PRO B 1 398 ? -25.793 -1.089  10.212  1.00 19.76 ?  398 PRO B O   1 
ATOM   5848 C  CB  . PRO B 1 398 ? -23.235 -0.004  8.512   1.00 17.22 ?  398 PRO B CB  1 
ATOM   5849 C  CG  . PRO B 1 398 ? -24.268 1.048   8.146   1.00 20.01 ?  398 PRO B CG  1 
ATOM   5850 C  CD  . PRO B 1 398 ? -25.289 0.361   7.247   1.00 18.90 ?  398 PRO B CD  1 
ATOM   5851 N  N   . GLY B 1 399 ? -23.851 -2.073  10.813  1.00 19.87 ?  399 GLY B N   1 
ATOM   5852 C  CA  . GLY B 1 399 ? -24.137 -2.081  12.243  1.00 19.58 ?  399 GLY B CA  1 
ATOM   5853 C  C   . GLY B 1 399 ? -25.466 -2.702  12.617  1.00 22.20 ?  399 GLY B C   1 
ATOM   5854 O  O   . GLY B 1 399 ? -26.176 -2.179  13.487  1.00 22.17 ?  399 GLY B O   1 
ATOM   5855 N  N   . PHE B 1 400 ? -25.800 -3.830  12.004  1.00 18.24 ?  400 PHE B N   1 
ATOM   5856 C  CA  . PHE B 1 400 ? -27.080 -4.491  12.201  1.00 21.14 ?  400 PHE B CA  1 
ATOM   5857 C  C   . PHE B 1 400 ? -26.833 -5.988  12.309  1.00 21.12 ?  400 PHE B C   1 
ATOM   5858 O  O   . PHE B 1 400 ? -25.907 -6.523  11.693  1.00 18.03 ?  400 PHE B O   1 
ATOM   5859 C  CB  . PHE B 1 400 ? -28.030 -4.177  11.035  1.00 18.33 ?  400 PHE B CB  1 
ATOM   5860 C  CG  . PHE B 1 400 ? -29.489 -4.334  11.361  1.00 20.67 ?  400 PHE B CG  1 
ATOM   5861 C  CD1 . PHE B 1 400 ? -30.081 -3.576  12.368  1.00 22.87 ?  400 PHE B CD1 1 
ATOM   5862 C  CD2 . PHE B 1 400 ? -30.273 -5.224  10.644  1.00 16.62 ?  400 PHE B CD2 1 
ATOM   5863 C  CE1 . PHE B 1 400 ? -31.429 -3.713  12.650  1.00 19.09 ?  400 PHE B CE1 1 
ATOM   5864 C  CE2 . PHE B 1 400 ? -31.619 -5.377  10.928  1.00 19.23 ?  400 PHE B CE2 1 
ATOM   5865 C  CZ  . PHE B 1 400 ? -32.199 -4.615  11.917  1.00 20.68 ?  400 PHE B CZ  1 
ATOM   5866 N  N   . ILE B 1 401 ? -27.677 -6.669  13.080  1.00 19.37 ?  401 ILE B N   1 
ATOM   5867 C  CA  . ILE B 1 401 ? -27.505 -8.110  13.252  1.00 19.45 ?  401 ILE B CA  1 
ATOM   5868 C  C   . ILE B 1 401 ? -27.622 -8.837  11.910  1.00 20.36 ?  401 ILE B C   1 
ATOM   5869 O  O   . ILE B 1 401 ? -26.919 -9.825  11.657  1.00 21.88 ?  401 ILE B O   1 
ATOM   5870 C  CB  . ILE B 1 401 ? -28.513 -8.647  14.291  1.00 20.28 ?  401 ILE B CB  1 
ATOM   5871 C  CG1 . ILE B 1 401 ? -27.992 -8.373  15.710  1.00 23.54 ?  401 ILE B CG1 1 
ATOM   5872 C  CG2 . ILE B 1 401 ? -28.745 -10.144 14.076  1.00 22.96 ?  401 ILE B CG2 1 
ATOM   5873 C  CD1 . ILE B 1 401 ? -29.024 -8.462  16.832  1.00 21.71 ?  401 ILE B CD1 1 
ATOM   5874 N  N   . LYS B 1 402 ? -28.502 -8.370  11.032  1.00 16.81 ?  402 LYS B N   1 
ATOM   5875 C  CA  . LYS B 1 402 ? -28.647 -8.956  9.705   1.00 20.77 ?  402 LYS B CA  1 
ATOM   5876 C  C   . LYS B 1 402 ? -27.856 -8.160  8.672   1.00 20.79 ?  402 LYS B C   1 
ATOM   5877 O  O   . LYS B 1 402 ? -27.766 -6.932  8.767   1.00 19.34 ?  402 LYS B O   1 
ATOM   5878 C  CB  . LYS B 1 402 ? -30.119 -9.016  9.263   1.00 16.32 ?  402 LYS B CB  1 
ATOM   5879 C  CG  . LYS B 1 402 ? -31.053 -9.694  10.263  1.00 18.92 ?  402 LYS B CG  1 
ATOM   5880 C  CD  . LYS B 1 402 ? -30.837 -11.184 10.279  1.00 23.23 ?  402 LYS B CD  1 
ATOM   5881 C  CE  . LYS B 1 402 ? -31.720 -11.870 11.296  1.00 26.84 ?  402 LYS B CE  1 
ATOM   5882 N  NZ  . LYS B 1 402 ? -31.296 -13.288 11.407  1.00 30.38 ?  402 LYS B NZ  1 
ATOM   5883 N  N   . ARG B 1 403 ? -27.279 -8.876  7.691   1.00 16.02 ?  403 ARG B N   1 
ATOM   5884 C  CA  . ARG B 1 403 ? -26.921 -8.299  6.396   1.00 16.62 ?  403 ARG B CA  1 
ATOM   5885 C  C   . ARG B 1 403 ? -28.167 -8.112  5.540   1.00 20.62 ?  403 ARG B C   1 
ATOM   5886 O  O   . ARG B 1 403 ? -28.915 -9.075  5.303   1.00 20.22 ?  403 ARG B O   1 
ATOM   5887 C  CB  . ARG B 1 403 ? -25.972 -9.215  5.628   1.00 20.39 ?  403 ARG B CB  1 
ATOM   5888 C  CG  . ARG B 1 403 ? -24.556 -9.234  6.107   1.00 20.08 ?  403 ARG B CG  1 
ATOM   5889 C  CD  . ARG B 1 403 ? -23.662 -9.858  5.049   1.00 19.68 ?  403 ARG B CD  1 
ATOM   5890 N  NE  . ARG B 1 403 ? -22.377 -10.221 5.631   1.00 22.97 ?  403 ARG B NE  1 
ATOM   5891 C  CZ  . ARG B 1 403 ? -22.130 -11.381 6.224   1.00 26.18 ?  403 ARG B CZ  1 
ATOM   5892 N  NH1 . ARG B 1 403 ? -23.056 -12.328 6.306   1.00 22.56 ?  403 ARG B NH1 1 
ATOM   5893 N  NH2 . ARG B 1 403 ? -20.924 -11.596 6.747   1.00 25.18 ?  403 ARG B NH2 1 
ATOM   5894 N  N   . LEU B 1 404 ? -28.352 -6.906  5.007   1.00 16.60 ?  404 LEU B N   1 
ATOM   5895 C  CA  . LEU B 1 404 ? -29.474 -6.650  4.115   1.00 17.75 ?  404 LEU B CA  1 
ATOM   5896 C  C   . LEU B 1 404 ? -29.161 -5.445  3.245   1.00 18.43 ?  404 LEU B C   1 
ATOM   5897 O  O   . LEU B 1 404 ? -28.405 -4.561  3.663   1.00 17.44 ?  404 LEU B O   1 
ATOM   5898 C  CB  . LEU B 1 404 ? -30.773 -6.416  4.898   1.00 22.44 ?  404 LEU B CB  1 
ATOM   5899 C  CG  . LEU B 1 404 ? -30.857 -5.227  5.855   1.00 24.26 ?  404 LEU B CG  1 
ATOM   5900 C  CD1 . LEU B 1 404 ? -31.139 -3.919  5.109   1.00 27.97 ?  404 LEU B CD1 1 
ATOM   5901 C  CD2 . LEU B 1 404 ? -31.921 -5.494  6.882   1.00 21.19 ?  404 LEU B CD2 1 
ATOM   5902 N  N   . PRO B 1 405 ? -29.720 -5.381  2.040   1.00 20.56 ?  405 PRO B N   1 
ATOM   5903 C  CA  . PRO B 1 405 ? -29.659 -4.141  1.260   1.00 17.32 ?  405 PRO B CA  1 
ATOM   5904 C  C   . PRO B 1 405 ? -30.655 -3.132  1.815   1.00 21.43 ?  405 PRO B C   1 
ATOM   5905 O  O   . PRO B 1 405 ? -31.806 -3.473  2.112   1.00 18.97 ?  405 PRO B O   1 
ATOM   5906 C  CB  . PRO B 1 405 ? -30.047 -4.590  -0.157  1.00 19.55 ?  405 PRO B CB  1 
ATOM   5907 C  CG  . PRO B 1 405 ? -30.948 -5.832  0.070   1.00 22.55 ?  405 PRO B CG  1 
ATOM   5908 C  CD  . PRO B 1 405 ? -30.497 -6.451  1.376   1.00 20.29 ?  405 PRO B CD  1 
ATOM   5909 N  N   . GLU B 1 406 ? -30.195 -1.882  1.977   1.00 16.85 ?  406 GLU B N   1 
ATOM   5910 C  CA  . GLU B 1 406 ? -31.084 -0.819  2.459   1.00 18.08 ?  406 GLU B CA  1 
ATOM   5911 C  C   . GLU B 1 406 ? -32.279 -0.651  1.537   1.00 18.52 ?  406 GLU B C   1 
ATOM   5912 O  O   . GLU B 1 406 ? -33.409 -0.422  1.991   1.00 17.37 ?  406 GLU B O   1 
ATOM   5913 C  CB  . GLU B 1 406 ? -30.327 0.513   2.563   1.00 16.90 ?  406 GLU B CB  1 
ATOM   5914 C  CG  . GLU B 1 406 ? -29.092 0.470   3.439   1.00 20.54 ?  406 GLU B CG  1 
ATOM   5915 C  CD  . GLU B 1 406 ? -29.431 0.649   4.906   1.00 19.88 ?  406 GLU B CD  1 
ATOM   5916 O  OE1 . GLU B 1 406 ? -30.549 0.265   5.306   1.00 21.15 ?  406 GLU B OE1 1 
ATOM   5917 O  OE2 . GLU B 1 406 ? -28.576 1.153   5.659   1.00 18.44 ?  406 GLU B OE2 1 
ATOM   5918 N  N   . ARG B 1 407 ? -32.026 -0.707  0.238   1.00 18.49 ?  407 ARG B N   1 
ATOM   5919 C  CA  . ARG B 1 407 ? -33.033 -0.737  -0.803  1.00 20.61 ?  407 ARG B CA  1 
ATOM   5920 C  C   . ARG B 1 407 ? -32.671 -1.871  -1.744  1.00 19.58 ?  407 ARG B C   1 
ATOM   5921 O  O   . ARG B 1 407 ? -31.494 -2.216  -1.877  1.00 20.70 ?  407 ARG B O   1 
ATOM   5922 C  CB  . ARG B 1 407 ? -33.105 0.596   -1.579  1.00 17.91 ?  407 ARG B CB  1 
ATOM   5923 C  CG  . ARG B 1 407 ? -33.565 1.786   -0.727  1.00 20.36 ?  407 ARG B CG  1 
ATOM   5924 C  CD  . ARG B 1 407 ? -32.972 3.102   -1.231  1.00 19.75 ?  407 ARG B CD  1 
ATOM   5925 N  NE  . ARG B 1 407 ? -31.521 3.155   -1.062  1.00 20.19 ?  407 ARG B NE  1 
ATOM   5926 C  CZ  . ARG B 1 407 ? -30.914 3.444   0.081   1.00 19.78 ?  407 ARG B CZ  1 
ATOM   5927 N  NH1 . ARG B 1 407 ? -31.601 3.657   1.192   1.00 20.09 ?  407 ARG B NH1 1 
ATOM   5928 N  NH2 . ARG B 1 407 ? -29.586 3.533   0.107   1.00 21.08 ?  407 ARG B NH2 1 
ATOM   5929 N  N   . LEU B 1 408 ? -33.685 -2.453  -2.393  1.00 18.63 ?  408 LEU B N   1 
ATOM   5930 C  CA  . LEU B 1 408 ? -33.493 -3.566  -3.329  1.00 21.89 ?  408 LEU B CA  1 
ATOM   5931 C  C   . LEU B 1 408 ? -34.171 -3.184  -4.637  1.00 19.40 ?  408 LEU B C   1 
ATOM   5932 O  O   . LEU B 1 408 ? -35.279 -3.641  -4.929  1.00 17.73 ?  408 LEU B O   1 
ATOM   5933 C  CB  . LEU B 1 408 ? -34.055 -4.876  -2.764  1.00 20.83 ?  408 LEU B CB  1 
ATOM   5934 C  CG  . LEU B 1 408 ? -34.024 -6.156  -3.605  1.00 22.23 ?  408 LEU B CG  1 
ATOM   5935 C  CD1 . LEU B 1 408 ? -32.604 -6.616  -3.941  1.00 19.07 ?  408 LEU B CD1 1 
ATOM   5936 C  CD2 . LEU B 1 408 ? -34.812 -7.262  -2.906  1.00 19.80 ?  408 LEU B CD2 1 
ATOM   5937 N  N   . PRO B 1 409 ? -33.551 -2.306  -5.430  1.00 20.31 ?  409 PRO B N   1 
ATOM   5938 C  CA  . PRO B 1 409 ? -34.221 -1.788  -6.630  1.00 19.40 ?  409 PRO B CA  1 
ATOM   5939 C  C   . PRO B 1 409 ? -34.104 -2.772  -7.783  1.00 19.10 ?  409 PRO B C   1 
ATOM   5940 O  O   . PRO B 1 409 ? -33.012 -3.256  -8.093  1.00 17.44 ?  409 PRO B O   1 
ATOM   5941 C  CB  . PRO B 1 409 ? -33.469 -0.488  -6.933  1.00 18.68 ?  409 PRO B CB  1 
ATOM   5942 C  CG  . PRO B 1 409 ? -32.163 -0.626  -6.272  1.00 20.93 ?  409 PRO B CG  1 
ATOM   5943 C  CD  . PRO B 1 409 ? -32.269 -1.638  -5.162  1.00 18.13 ?  409 PRO B CD  1 
ATOM   5944 N  N   . VAL B 1 410 ? -35.235 -3.066  -8.424  1.00 17.32 ?  410 VAL B N   1 
ATOM   5945 C  CA  . VAL B 1 410 ? -35.274 -4.084  -9.467  1.00 18.24 ?  410 VAL B CA  1 
ATOM   5946 C  C   . VAL B 1 410 ? -36.094 -3.595  -10.654 1.00 22.55 ?  410 VAL B C   1 
ATOM   5947 O  O   . VAL B 1 410 ? -36.932 -2.692  -10.546 1.00 19.11 ?  410 VAL B O   1 
ATOM   5948 C  CB  . VAL B 1 410 ? -35.832 -5.435  -8.955  1.00 19.98 ?  410 VAL B CB  1 
ATOM   5949 C  CG1 . VAL B 1 410 ? -35.022 -5.946  -7.770  1.00 18.22 ?  410 VAL B CG1 1 
ATOM   5950 C  CG2 . VAL B 1 410 ? -37.305 -5.306  -8.588  1.00 17.95 ?  410 VAL B CG2 1 
ATOM   5951 N  N   . LEU B 1 411 ? -35.831 -4.207  -11.801 1.00 19.33 ?  411 LEU B N   1 
ATOM   5952 C  CA  . LEU B 1 411 ? -36.613 -4.012  -13.008 1.00 17.07 ?  411 LEU B CA  1 
ATOM   5953 C  C   . LEU B 1 411 ? -37.302 -5.326  -13.378 1.00 20.01 ?  411 LEU B C   1 
ATOM   5954 O  O   . LEU B 1 411 ? -36.943 -6.396  -12.882 1.00 18.80 ?  411 LEU B O   1 
ATOM   5955 C  CB  . LEU B 1 411 ? -35.718 -3.524  -14.147 1.00 16.54 ?  411 LEU B CB  1 
ATOM   5956 C  CG  . LEU B 1 411 ? -35.008 -2.182  -13.934 1.00 19.62 ?  411 LEU B CG  1 
ATOM   5957 C  CD1 . LEU B 1 411 ? -33.861 -2.042  -14.920 1.00 18.38 ?  411 LEU B CD1 1 
ATOM   5958 C  CD2 . LEU B 1 411 ? -35.967 -1.019  -14.111 1.00 17.54 ?  411 LEU B CD2 1 
ATOM   5959 N  N   . TRP B 1 412 ? -38.295 -5.242  -14.263 1.00 21.58 ?  412 TRP B N   1 
ATOM   5960 C  CA  . TRP B 1 412 ? -39.003 -6.440  -14.742 1.00 22.12 ?  412 TRP B CA  1 
ATOM   5961 C  C   . TRP B 1 412 ? -39.790 -6.118  -16.018 1.00 21.71 ?  412 TRP B C   1 
ATOM   5962 O  O   . TRP B 1 412 ? -39.772 -4.966  -16.451 1.00 21.11 ?  412 TRP B O   1 
ATOM   5963 C  CB  . TRP B 1 412 ? -39.951 -6.993  -13.671 1.00 18.34 ?  412 TRP B CB  1 
ATOM   5964 C  CG  . TRP B 1 412 ? -41.110 -6.060  -13.363 1.00 22.44 ?  412 TRP B CG  1 
ATOM   5965 C  CD1 . TRP B 1 412 ? -42.295 -5.983  -14.030 1.00 21.34 ?  412 TRP B CD1 1 
ATOM   5966 C  CD2 . TRP B 1 412 ? -41.178 -5.084  -12.309 1.00 21.72 ?  412 TRP B CD2 1 
ATOM   5967 N  NE1 . TRP B 1 412 ? -43.099 -5.023  -13.459 1.00 23.05 ?  412 TRP B NE1 1 
ATOM   5968 C  CE2 . TRP B 1 412 ? -42.435 -4.451  -12.406 1.00 22.09 ?  412 TRP B CE2 1 
ATOM   5969 C  CE3 . TRP B 1 412 ? -40.297 -4.679  -11.302 1.00 22.95 ?  412 TRP B CE3 1 
ATOM   5970 C  CZ2 . TRP B 1 412 ? -42.837 -3.436  -11.530 1.00 23.60 ?  412 TRP B CZ2 1 
ATOM   5971 C  CZ3 . TRP B 1 412 ? -40.700 -3.667  -10.431 1.00 22.06 ?  412 TRP B CZ3 1 
ATOM   5972 C  CH2 . TRP B 1 412 ? -41.964 -3.063  -10.553 1.00 23.19 ?  412 TRP B CH2 1 
HETATM 5973 N  N   . UYM C 2 .   ? -30.575 20.648  -8.408  1.00 28.46 ?  501 UYM A N   1 
HETATM 5974 C  C   . UYM C 2 .   ? -29.303 19.306  -12.884 1.00 29.22 ?  501 UYM A C   1 
HETATM 5975 O  O   . UYM C 2 .   ? -28.209 18.737  -13.002 1.00 32.96 ?  501 UYM A O   1 
HETATM 5976 C  C1  . UYM C 2 .   ? -29.329 20.814  -12.746 1.00 26.93 ?  501 UYM A C1  1 
HETATM 5977 C  C10 . UYM C 2 .   ? -29.774 18.492  -7.403  1.00 27.28 ?  501 UYM A C10 1 
HETATM 5978 C  C11 . UYM C 2 .   ? -31.765 19.198  -12.558 1.00 29.45 ?  501 UYM A C11 1 
HETATM 5979 C  C12 . UYM C 2 .   ? -32.221 18.707  -11.161 1.00 26.32 ?  501 UYM A C12 1 
HETATM 5980 C  C15 . UYM C 2 .   ? -31.816 20.707  -12.631 1.00 28.88 ?  501 UYM A C15 1 
HETATM 5981 C  C2  . UYM C 2 .   ? -28.591 21.264  -11.458 1.00 29.51 ?  501 UYM A C2  1 
HETATM 5982 C  C3  . UYM C 2 .   ? -29.221 20.755  -10.193 1.00 30.96 ?  501 UYM A C3  1 
HETATM 5983 C  C34 . UYM C 2 .   ? -32.466 17.228  -11.163 1.00 27.19 ?  501 UYM A C34 1 
HETATM 5984 C  C35 . UYM C 2 .   ? -33.689 16.634  -11.297 1.00 25.57 ?  501 UYM A C35 1 
HETATM 5985 C  C37 . UYM C 2 .   ? -32.225 14.948  -11.159 1.00 24.88 ?  501 UYM A C37 1 
HETATM 5986 C  C38 . UYM C 2 .   ? -31.501 16.158  -11.078 1.00 25.80 ?  501 UYM A C38 1 
HETATM 5987 C  C39 . UYM C 2 .   ? -30.110 16.104  -10.936 1.00 25.47 ?  501 UYM A C39 1 
HETATM 5988 C  C4  . UYM C 2 .   ? -30.225 21.382  -9.511  1.00 30.04 ?  501 UYM A C4  1 
HETATM 5989 C  C40 . UYM C 2 .   ? -29.496 14.872  -10.873 1.00 25.94 ?  501 UYM A C40 1 
HETATM 5990 C  C41 . UYM C 2 .   ? -30.233 13.687  -10.947 1.00 23.75 ?  501 UYM A C41 1 
HETATM 5991 C  C42 . UYM C 2 .   ? -31.602 13.701  -11.097 1.00 21.06 ?  501 UYM A C42 1 
HETATM 5992 C  C5  . UYM C 2 .   ? -29.794 19.523  -8.342  1.00 27.54 ?  501 UYM A C5  1 
HETATM 5993 C  C6  . UYM C 2 .   ? -28.925 19.549  -9.452  1.00 28.01 ?  501 UYM A C6  1 
HETATM 5994 C  C7  . UYM C 2 .   ? -28.016 18.499  -9.619  1.00 28.89 ?  501 UYM A C7  1 
HETATM 5995 C  C8  . UYM C 2 .   ? -28.002 17.478  -8.696  1.00 26.90 ?  501 UYM A C8  1 
HETATM 5996 C  C9  . UYM C 2 .   ? -28.875 17.472  -7.608  1.00 26.46 ?  501 UYM A C9  1 
HETATM 5997 N  N1  . UYM C 2 .   ? -30.675 21.374  -12.771 1.00 33.37 ?  501 UYM A N1  1 
HETATM 5998 N  N2  . UYM C 2 .   ? -30.458 18.643  -12.888 1.00 27.25 ?  501 UYM A N2  1 
HETATM 5999 N  N36 . UYM C 2 .   ? -33.550 15.272  -11.293 1.00 25.93 ?  501 UYM A N36 1 
HETATM 6000 O  O1  . UYM C 2 .   ? -32.912 21.271  -12.542 1.00 32.74 ?  501 UYM A O1  1 
HETATM 6001 N  N1  . HPA D 3 .   ? -25.170 18.629  -5.961  1.00 28.08 ?  502 HPA A N1  1 
HETATM 6002 C  C2  . HPA D 3 .   ? -24.992 19.221  -7.144  1.00 24.01 ?  502 HPA A C2  1 
HETATM 6003 N  N3  . HPA D 3 .   ? -25.763 20.159  -7.630  1.00 30.30 ?  502 HPA A N3  1 
HETATM 6004 C  C4  . HPA D 3 .   ? -26.796 20.497  -6.804  1.00 24.67 ?  502 HPA A C4  1 
HETATM 6005 C  C5  . HPA D 3 .   ? -27.048 19.933  -5.561  1.00 23.39 ?  502 HPA A C5  1 
HETATM 6006 C  C6  . HPA D 3 .   ? -26.199 18.908  -5.055  1.00 25.27 ?  502 HPA A C6  1 
HETATM 6007 O  O6  . HPA D 3 .   ? -26.283 18.310  -3.985  1.00 24.77 ?  502 HPA A O6  1 
HETATM 6008 N  N7  . HPA D 3 .   ? -28.180 20.516  -5.009  1.00 21.07 ?  502 HPA A N7  1 
HETATM 6009 C  C8  . HPA D 3 .   ? -28.574 21.386  -5.909  1.00 24.85 ?  502 HPA A C8  1 
HETATM 6010 N  N9  . HPA D 3 .   ? -27.782 21.418  -7.015  1.00 26.85 ?  502 HPA A N9  1 
HETATM 6011 C  CHA . HEM E 4 .   ? -29.562 24.872  -8.182  1.00 23.10 ?  503 HEM A CHA 1 
HETATM 6012 C  CHB . HEM E 4 .   ? -28.787 24.041  -3.470  1.00 22.16 ?  503 HEM A CHB 1 
HETATM 6013 C  CHC . HEM E 4 .   ? -33.583 23.612  -2.833  1.00 22.78 ?  503 HEM A CHC 1 
HETATM 6014 C  CHD . HEM E 4 .   ? -34.313 23.919  -7.651  1.00 21.01 ?  503 HEM A CHD 1 
HETATM 6015 C  C1A . HEM E 4 .   ? -28.900 24.747  -6.952  1.00 23.02 ?  503 HEM A C1A 1 
HETATM 6016 C  C2A . HEM E 4 .   ? -27.475 24.879  -6.732  1.00 22.77 ?  503 HEM A C2A 1 
HETATM 6017 C  C3A . HEM E 4 .   ? -27.256 24.635  -5.407  1.00 25.19 ?  503 HEM A C3A 1 
HETATM 6018 C  C4A . HEM E 4 .   ? -28.547 24.364  -4.804  1.00 24.85 ?  503 HEM A C4A 1 
HETATM 6019 C  CMA . HEM E 4 .   ? -25.932 24.634  -4.700  1.00 18.28 ?  503 HEM A CMA 1 
HETATM 6020 C  CAA . HEM E 4 .   ? -26.461 25.216  -7.790  1.00 22.67 ?  503 HEM A CAA 1 
HETATM 6021 C  CBA . HEM E 4 .   ? -25.991 24.004  -8.604  1.00 23.00 ?  503 HEM A CBA 1 
HETATM 6022 C  CGA . HEM E 4 .   ? -24.925 24.317  -9.643  1.00 23.88 ?  503 HEM A CGA 1 
HETATM 6023 O  O1A . HEM E 4 .   ? -24.508 23.383  -10.369 1.00 23.75 ?  503 HEM A O1A 1 
HETATM 6024 O  O2A . HEM E 4 .   ? -24.505 25.489  -9.720  1.00 23.23 -1 503 HEM A O2A 1 
HETATM 6025 C  C1B . HEM E 4 .   ? -30.007 23.777  -2.841  1.00 23.29 ?  503 HEM A C1B 1 
HETATM 6026 C  C2B . HEM E 4 .   ? -30.208 23.519  -1.423  1.00 23.18 ?  503 HEM A C2B 1 
HETATM 6027 C  C3B . HEM E 4 .   ? -31.633 23.394  -1.283  1.00 22.31 ?  503 HEM A C3B 1 
HETATM 6028 C  C4B . HEM E 4 .   ? -32.209 23.583  -2.531  1.00 22.67 ?  503 HEM A C4B 1 
HETATM 6029 C  CMB . HEM E 4 .   ? -29.150 23.406  -0.365  1.00 22.94 ?  503 HEM A CMB 1 
HETATM 6030 C  CAB . HEM E 4 .   ? -32.425 23.169  -0.151  1.00 23.82 ?  503 HEM A CAB 1 
HETATM 6031 C  CBB . HEM E 4 .   ? -32.172 23.492  1.091   1.00 27.59 ?  503 HEM A CBB 1 
HETATM 6032 C  C1C . HEM E 4 .   ? -34.248 23.675  -4.051  1.00 25.10 ?  503 HEM A C1C 1 
HETATM 6033 C  C2C . HEM E 4 .   ? -35.687 23.587  -4.236  1.00 21.69 ?  503 HEM A C2C 1 
HETATM 6034 C  C3C . HEM E 4 .   ? -35.869 23.584  -5.652  1.00 25.18 ?  503 HEM A C3C 1 
HETATM 6035 C  C4C . HEM E 4 .   ? -34.618 23.775  -6.257  1.00 27.27 ?  503 HEM A C4C 1 
HETATM 6036 C  CMC . HEM E 4 .   ? -36.727 23.514  -3.154  1.00 26.20 ?  503 HEM A CMC 1 
HETATM 6037 C  CAC . HEM E 4 .   ? -37.036 23.466  -6.404  1.00 27.35 ?  503 HEM A CAC 1 
HETATM 6038 C  CBC . HEM E 4 .   ? -38.271 23.373  -5.989  1.00 27.19 ?  503 HEM A CBC 1 
HETATM 6039 C  C1D . HEM E 4 .   ? -33.077 24.181  -8.245  1.00 22.23 ?  503 HEM A C1D 1 
HETATM 6040 C  C2D . HEM E 4 .   ? -32.831 24.369  -9.667  1.00 26.06 ?  503 HEM A C2D 1 
HETATM 6041 C  C3D . HEM E 4 .   ? -31.494 24.594  -9.821  1.00 24.79 ?  503 HEM A C3D 1 
HETATM 6042 C  C4D . HEM E 4 .   ? -30.907 24.598  -8.485  1.00 24.03 ?  503 HEM A C4D 1 
HETATM 6043 C  CMD . HEM E 4 .   ? -33.864 24.315  -10.755 1.00 21.52 ?  503 HEM A CMD 1 
HETATM 6044 C  CAD . HEM E 4 .   ? -30.737 24.853  -11.093 1.00 21.24 ?  503 HEM A CAD 1 
HETATM 6045 C  CBD . HEM E 4 .   ? -30.508 26.349  -11.362 1.00 23.70 ?  503 HEM A CBD 1 
HETATM 6046 C  CGD . HEM E 4 .   ? -29.707 26.658  -12.620 1.00 26.98 ?  503 HEM A CGD 1 
HETATM 6047 O  O1D . HEM E 4 .   ? -29.551 27.852  -12.945 1.00 31.79 ?  503 HEM A O1D 1 
HETATM 6048 O  O2D . HEM E 4 .   ? -29.225 25.712  -13.268 1.00 27.56 -1 503 HEM A O2D 1 
HETATM 6049 N  NA  . HEM E 4 .   ? -29.512 24.436  -5.765  1.00 24.37 ?  503 HEM A NA  1 
HETATM 6050 N  NB  . HEM E 4 .   ? -31.217 23.679  -3.473  1.00 23.78 ?  503 HEM A NB  1 
HETATM 6051 N  NC  . HEM E 4 .   ? -33.652 23.835  -5.276  1.00 25.99 ?  503 HEM A NC  1 
HETATM 6052 N  ND  . HEM E 4 .   ? -31.880 24.283  -7.564  1.00 26.76 ?  503 HEM A ND  1 
HETATM 6053 FE FE  . HEM E 4 .   ? -31.534 24.276  -5.398  1.00 28.76 ?  503 HEM A FE  1 
HETATM 6054 N  N   . UYM F 2 .   ? -33.720 -14.986 16.860  1.00 34.36 ?  501 UYM B N   1 
HETATM 6055 C  C   . UYM F 2 .   ? -32.101 -13.893 21.281  1.00 36.12 ?  501 UYM B C   1 
HETATM 6056 O  O   . UYM F 2 .   ? -30.930 -13.504 21.372  1.00 37.65 ?  501 UYM B O   1 
HETATM 6057 C  C1  . UYM F 2 .   ? -32.377 -15.377 21.150  1.00 38.13 ?  501 UYM B C1  1 
HETATM 6058 C  C10 . UYM F 2 .   ? -32.543 -13.051 15.780  1.00 32.01 ?  501 UYM B C10 1 
HETATM 6059 C  C11 . UYM F 2 .   ? -34.527 -13.379 21.030  1.00 36.85 ?  501 UYM B C11 1 
HETATM 6060 C  C12 . UYM F 2 .   ? -34.971 -12.785 19.671  1.00 32.41 ?  501 UYM B C12 1 
HETATM 6061 C  C15 . UYM F 2 .   ? -34.817 -14.865 21.099  1.00 37.54 ?  501 UYM B C15 1 
HETATM 6062 C  C2  . UYM F 2 .   ? -31.756 -15.936 19.843  1.00 32.32 ?  501 UYM B C2  1 
HETATM 6063 C  C3  . UYM F 2 .   ? -32.342 -15.338 18.596  1.00 33.69 ?  501 UYM B C3  1 
HETATM 6064 C  C34 . UYM F 2 .   ? -34.943 -11.284 19.663  1.00 32.16 ?  501 UYM B C34 1 
HETATM 6065 C  C35 . UYM F 2 .   ? -36.034 -10.475 19.799  1.00 32.41 ?  501 UYM B C35 1 
HETATM 6066 C  C37 . UYM F 2 .   ? -34.290 -9.084  19.643  1.00 31.21 ?  501 UYM B C37 1 
HETATM 6067 C  C38 . UYM F 2 .   ? -33.800 -10.406 19.565  1.00 32.03 ?  501 UYM B C38 1 
HETATM 6068 C  C39 . UYM F 2 .   ? -32.423 -10.609 19.424  1.00 29.65 ?  501 UYM B C39 1 
HETATM 6069 C  C4  . UYM F 2 .   ? -33.481 -15.757 17.968  1.00 33.51 ?  501 UYM B C4  1 
HETATM 6070 C  C40 . UYM F 2 .   ? -31.595 -9.511  19.355  1.00 32.27 ?  501 UYM B C40 1 
HETATM 6071 C  C41 . UYM F 2 .   ? -32.103 -8.211  19.426  1.00 29.98 ?  501 UYM B C41 1 
HETATM 6072 C  C42 . UYM F 2 .   ? -33.451 -7.972  19.572  1.00 28.85 ?  501 UYM B C42 1 
HETATM 6073 C  C5  . UYM F 2 .   ? -32.732 -14.043 16.741  1.00 33.83 ?  501 UYM B C5  1 
HETATM 6074 C  C6  . UYM F 2 .   ? -31.838 -14.231 17.816  1.00 33.30 ?  501 UYM B C6  1 
HETATM 6075 C  C7  . UYM F 2 .   ? -30.724 -13.391 17.922  1.00 35.25 ?  501 UYM B C7  1 
HETATM 6076 C  C8  . UYM F 2 .   ? -30.543 -12.406 16.976  1.00 31.13 ?  501 UYM B C8  1 
HETATM 6077 C  C9  . UYM F 2 .   ? -31.440 -12.241 15.920  1.00 27.20 ?  501 UYM B C9  1 
HETATM 6078 N  N1  . UYM F 2 .   ? -33.796 -15.710 21.209  1.00 36.41 ?  501 UYM B N1  1 
HETATM 6079 N  N2  . UYM F 2 .   ? -33.131 -13.051 21.285  1.00 36.73 ?  501 UYM B N2  1 
HETATM 6080 N  N36 . UYM F 2 .   ? -35.651 -9.160  19.780  1.00 31.79 ?  501 UYM B N36 1 
HETATM 6081 O  O1  . UYM F 2 .   ? -35.993 -15.247 21.048  1.00 40.55 ?  501 UYM B O1  1 
HETATM 6082 N  N1  . HPA G 3 .   ? -28.004 -14.127 14.423  1.00 35.48 ?  502 HPA B N1  1 
HETATM 6083 C  C2  . HPA G 3 .   ? -27.935 -14.776 15.594  1.00 31.19 ?  502 HPA B C2  1 
HETATM 6084 N  N3  . HPA G 3 .   ? -28.877 -15.541 16.080  1.00 31.08 ?  502 HPA B N3  1 
HETATM 6085 C  C4  . HPA G 3 .   ? -29.980 -15.616 15.276  1.00 30.78 ?  502 HPA B C4  1 
HETATM 6086 C  C5  . HPA G 3 .   ? -30.132 -14.971 14.054  1.00 29.66 ?  502 HPA B C5  1 
HETATM 6087 C  C6  . HPA G 3 .   ? -29.091 -14.149 13.541  1.00 28.82 ?  502 HPA B C6  1 
HETATM 6088 O  O6  . HPA G 3 .   ? -29.070 -13.515 12.486  1.00 32.21 ?  502 HPA B O6  1 
HETATM 6089 N  N7  . HPA G 3 .   ? -31.382 -15.269 13.527  1.00 30.71 ?  502 HPA B N7  1 
HETATM 6090 C  C8  . HPA G 3 .   ? -31.927 -16.068 14.412  1.00 30.95 ?  502 HPA B C8  1 
HETATM 6091 N  N9  . HPA G 3 .   ? -31.136 -16.307 15.491  1.00 30.86 ?  502 HPA B N9  1 
HETATM 6092 C  CHA . HEM H 4 .   ? -33.311 -19.383 16.589  1.00 27.77 ?  503 HEM B CHA 1 
HETATM 6093 C  CHB . HEM H 4 .   ? -32.427 -18.624 11.869  1.00 27.06 ?  503 HEM B CHB 1 
HETATM 6094 C  CHC . HEM H 4 .   ? -37.098 -17.422 11.248  1.00 22.20 ?  503 HEM B CHC 1 
HETATM 6095 C  CHD . HEM H 4 .   ? -37.777 -17.570 16.074  1.00 27.50 ?  503 HEM B CHD 1 
HETATM 6096 C  C1A . HEM H 4 .   ? -32.649 -19.343 15.349  1.00 32.63 ?  503 HEM B C1A 1 
HETATM 6097 C  C2A . HEM H 4 .   ? -31.271 -19.705 15.117  1.00 27.88 ?  503 HEM B C2A 1 
HETATM 6098 C  C3A . HEM H 4 .   ? -30.994 -19.392 13.818  1.00 29.22 ?  503 HEM B C3A 1 
HETATM 6099 C  C4A . HEM H 4 .   ? -32.235 -18.961 13.209  1.00 30.34 ?  503 HEM B C4A 1 
HETATM 6100 C  CMA . HEM H 4 .   ? -29.661 -19.488 13.138  1.00 26.00 ?  503 HEM B CMA 1 
HETATM 6101 C  CAA . HEM H 4 .   ? -30.349 -20.290 16.145  1.00 27.35 ?  503 HEM B CAA 1 
HETATM 6102 C  CBA . HEM H 4 .   ? -29.618 -19.251 17.002  1.00 26.76 ?  503 HEM B CBA 1 
HETATM 6103 C  CGA . HEM H 4 .   ? -28.624 -19.853 17.982  1.00 29.03 ?  503 HEM B CGA 1 
HETATM 6104 O  O1A . HEM H 4 .   ? -27.950 -19.082 18.687  1.00 30.88 ?  503 HEM B O1A 1 
HETATM 6105 O  O2A . HEM H 4 .   ? -28.536 -21.095 18.051  1.00 29.93 -1 503 HEM B O2A 1 
HETATM 6106 C  C1B . HEM H 4 .   ? -33.594 -18.180 11.245  1.00 23.39 ?  503 HEM B C1B 1 
HETATM 6107 C  C2B . HEM H 4 .   ? -33.746 -17.849 9.836   1.00 23.62 ?  503 HEM B C2B 1 
HETATM 6108 C  C3B . HEM H 4 .   ? -35.141 -17.550 9.681   1.00 24.79 ?  503 HEM B C3B 1 
HETATM 6109 C  C4B . HEM H 4 .   ? -35.743 -17.631 10.935  1.00 27.12 ?  503 HEM B C4B 1 
HETATM 6110 C  CMB . HEM H 4 .   ? -32.662 -17.818 8.797   1.00 27.37 ?  503 HEM B CMB 1 
HETATM 6111 C  CAB . HEM H 4 .   ? -35.885 -17.243 8.535   1.00 27.48 ?  503 HEM B CAB 1 
HETATM 6112 C  CBB . HEM H 4 .   ? -35.575 -17.442 7.275   1.00 29.85 ?  503 HEM B CBB 1 
HETATM 6113 C  C1C . HEM H 4 .   ? -37.733 -17.338 12.484  1.00 28.51 ?  503 HEM B C1C 1 
HETATM 6114 C  C2C . HEM H 4 .   ? -39.135 -17.021 12.705  1.00 23.40 ?  503 HEM B C2C 1 
HETATM 6115 C  C3C . HEM H 4 .   ? -39.257 -16.929 14.136  1.00 29.72 ?  503 HEM B C3C 1 
HETATM 6116 C  C4C . HEM H 4 .   ? -38.057 -17.345 14.696  1.00 26.31 ?  503 HEM B C4C 1 
HETATM 6117 C  CMC . HEM H 4 .   ? -40.195 -16.831 11.659  1.00 26.74 ?  503 HEM B CMC 1 
HETATM 6118 C  CAC . HEM H 4 .   ? -40.338 -16.551 14.935  1.00 27.57 ?  503 HEM B CAC 1 
HETATM 6119 C  CBC . HEM H 4 .   ? -41.544 -16.202 14.574  1.00 34.31 ?  503 HEM B CBC 1 
HETATM 6120 C  C1D . HEM H 4 .   ? -36.615 -18.061 16.662  1.00 29.94 ?  503 HEM B C1D 1 
HETATM 6121 C  C2D . HEM H 4 .   ? -36.435 -18.343 18.069  1.00 32.75 ?  503 HEM B C2D 1 
HETATM 6122 C  C3D . HEM H 4 .   ? -35.170 -18.831 18.222  1.00 33.04 ?  503 HEM B C3D 1 
HETATM 6123 C  C4D . HEM H 4 .   ? -34.579 -18.887 16.897  1.00 30.37 ?  503 HEM B C4D 1 
HETATM 6124 C  CMD . HEM H 4 .   ? -37.454 -18.103 19.145  1.00 28.95 ?  503 HEM B CMD 1 
HETATM 6125 C  CAD . HEM H 4 .   ? -34.474 -19.233 19.491  1.00 34.45 ?  503 HEM B CAD 1 
HETATM 6126 C  CBD . HEM H 4 .   ? -34.458 -20.745 19.736  1.00 33.26 ?  503 HEM B CBD 1 
HETATM 6127 C  CGD . HEM H 4 .   ? -33.795 -21.149 21.040  1.00 37.90 ?  503 HEM B CGD 1 
HETATM 6128 O  O1D . HEM H 4 .   ? -33.894 -22.336 21.408  1.00 34.75 ?  503 HEM B O1D 1 
HETATM 6129 O  O2D . HEM H 4 .   ? -33.186 -20.279 21.685  1.00 40.14 -1 503 HEM B O2D 1 
HETATM 6130 N  NA  . HEM H 4 .   ? -33.212 -18.922 14.166  1.00 28.82 ?  503 HEM B NA  1 
HETATM 6131 N  NB  . HEM H 4 .   ? -34.782 -17.938 11.874  1.00 29.48 ?  503 HEM B NB  1 
HETATM 6132 N  NC  . HEM H 4 .   ? -37.131 -17.533 13.698  1.00 24.80 ?  503 HEM B NC  1 
HETATM 6133 N  ND  . HEM H 4 .   ? -35.447 -18.328 15.994  1.00 28.86 ?  503 HEM B ND  1 
HETATM 6134 FE FE  . HEM H 4 .   ? -35.093 -18.037 14.034  1.00 30.81 ?  503 HEM B FE  1 
HETATM 6135 O  O   . HOH I 5 .   ? -12.001 23.857  7.284   1.00 29.77 ?  601 HOH A O   1 
HETATM 6136 O  O   . HOH I 5 .   ? -23.846 13.187  -14.277 1.00 28.76 ?  602 HOH A O   1 
HETATM 6137 O  O   . HOH I 5 .   ? -10.381 18.792  9.634   1.00 41.66 ?  603 HOH A O   1 
HETATM 6138 O  O   . HOH I 5 .   ? -11.328 7.708   -7.500  1.00 32.67 ?  604 HOH A O   1 
HETATM 6139 O  O   . HOH I 5 .   ? -19.864 16.132  -26.373 1.00 39.24 ?  605 HOH A O   1 
HETATM 6140 O  O   . HOH I 5 .   ? -35.172 20.494  20.652  1.00 24.53 ?  606 HOH A O   1 
HETATM 6141 O  O   . HOH I 5 .   ? -14.615 18.036  -22.487 1.00 32.04 ?  607 HOH A O   1 
HETATM 6142 O  O   . HOH I 5 .   ? -12.967 12.497  2.875   1.00 28.63 ?  608 HOH A O   1 
HETATM 6143 O  O   . HOH I 5 .   ? -57.058 17.408  -11.942 1.00 46.33 ?  609 HOH A O   1 
HETATM 6144 O  O   . HOH I 5 .   ? -6.257  17.692  -15.649 1.00 47.36 ?  610 HOH A O   1 
HETATM 6145 O  O   . HOH I 5 .   ? -49.473 21.742  20.687  1.00 31.02 ?  611 HOH A O   1 
HETATM 6146 O  O   . HOH I 5 .   ? -23.080 27.315  -20.468 1.00 34.57 ?  612 HOH A O   1 
HETATM 6147 O  O   . HOH I 5 .   ? -43.054 5.478   15.986  1.00 27.85 ?  613 HOH A O   1 
HETATM 6148 O  O   . HOH I 5 .   ? -19.741 4.282   18.562  1.00 33.67 ?  614 HOH A O   1 
HETATM 6149 O  O   . HOH I 5 .   ? -49.197 20.648  17.417  1.00 27.66 ?  615 HOH A O   1 
HETATM 6150 O  O   . HOH I 5 .   ? -15.318 2.541   -14.391 1.00 44.48 ?  616 HOH A O   1 
HETATM 6151 O  O   . HOH I 5 .   ? -37.869 4.469   9.157   1.00 28.47 ?  617 HOH A O   1 
HETATM 6152 O  O   . HOH I 5 .   ? -26.456 34.533  3.922   1.00 37.67 ?  618 HOH A O   1 
HETATM 6153 O  O   . HOH I 5 .   ? -10.178 34.796  -7.301  1.00 36.89 ?  619 HOH A O   1 
HETATM 6154 O  O   . HOH I 5 .   ? -21.597 9.906   11.923  1.00 27.96 ?  620 HOH A O   1 
HETATM 6155 O  O   . HOH I 5 .   ? -23.683 32.572  19.118  1.00 28.33 ?  621 HOH A O   1 
HETATM 6156 O  O   . HOH I 5 .   ? -32.929 31.416  6.448   1.00 25.57 ?  622 HOH A O   1 
HETATM 6157 O  O   . HOH I 5 .   ? -52.023 9.038   14.012  1.00 35.89 ?  623 HOH A O   1 
HETATM 6158 O  O   . HOH I 5 .   ? -5.570  12.442  -0.722  1.00 42.74 ?  624 HOH A O   1 
HETATM 6159 O  O   . HOH I 5 .   ? -6.524  24.292  -24.683 1.00 36.24 ?  625 HOH A O   1 
HETATM 6160 O  O   . HOH I 5 .   ? -33.167 32.237  -5.446  1.00 30.08 ?  626 HOH A O   1 
HETATM 6161 O  O   . HOH I 5 .   ? -53.180 17.203  -9.757  1.00 39.85 ?  627 HOH A O   1 
HETATM 6162 O  O   . HOH I 5 .   ? -24.775 8.250   -11.515 1.00 24.98 ?  628 HOH A O   1 
HETATM 6163 O  O   . HOH I 5 .   ? -7.342  29.493  -2.454  1.00 29.45 ?  629 HOH A O   1 
HETATM 6164 O  O   . HOH I 5 .   ? -51.107 23.063  -5.052  1.00 32.51 ?  630 HOH A O   1 
HETATM 6165 O  O   . HOH I 5 .   ? -24.243 3.422   5.693   1.00 30.41 ?  631 HOH A O   1 
HETATM 6166 O  O   . HOH I 5 .   ? -36.756 27.054  -26.194 1.00 47.98 ?  632 HOH A O   1 
HETATM 6167 O  O   . HOH I 5 .   ? -30.708 4.085   -18.097 1.00 23.97 ?  633 HOH A O   1 
HETATM 6168 O  O   . HOH I 5 .   ? -51.164 18.371  14.422  1.00 28.63 ?  634 HOH A O   1 
HETATM 6169 O  O   . HOH I 5 .   ? -45.630 6.203   -15.740 1.00 33.50 ?  635 HOH A O   1 
HETATM 6170 O  O   . HOH I 5 .   ? -35.523 6.099   6.961   1.00 20.83 ?  636 HOH A O   1 
HETATM 6171 O  O   . HOH I 5 .   ? -26.481 34.934  -8.710  1.00 32.86 ?  637 HOH A O   1 
HETATM 6172 O  O   . HOH I 5 .   ? -35.833 6.432   0.923   1.00 35.56 ?  638 HOH A O   1 
HETATM 6173 O  O   . HOH I 5 .   ? -8.975  21.330  -3.898  1.00 23.46 ?  639 HOH A O   1 
HETATM 6174 O  O   . HOH I 5 .   ? -21.185 23.428  3.700   1.00 24.42 ?  640 HOH A O   1 
HETATM 6175 O  O   . HOH I 5 .   ? -7.985  34.129  -11.885 1.00 41.75 ?  641 HOH A O   1 
HETATM 6176 O  O   . HOH I 5 .   ? -52.425 28.421  5.767   1.00 37.86 ?  642 HOH A O   1 
HETATM 6177 O  O   . HOH I 5 .   ? -54.105 16.148  -12.244 1.00 41.42 ?  643 HOH A O   1 
HETATM 6178 O  O   . HOH I 5 .   ? -27.245 11.141  -11.271 1.00 33.43 ?  644 HOH A O   1 
HETATM 6179 O  O   . HOH I 5 .   ? -25.314 20.881  -10.374 1.00 26.66 ?  645 HOH A O   1 
HETATM 6180 O  O   . HOH I 5 .   ? -40.325 3.801   -17.536 1.00 27.35 ?  646 HOH A O   1 
HETATM 6181 O  O   . HOH I 5 .   ? -38.629 29.926  15.527  1.00 25.29 ?  647 HOH A O   1 
HETATM 6182 O  O   . HOH I 5 .   ? -53.927 20.962  -9.021  1.00 38.42 ?  648 HOH A O   1 
HETATM 6183 O  O   . HOH I 5 .   ? -10.669 31.541  0.138   1.00 29.64 ?  649 HOH A O   1 
HETATM 6184 O  O   . HOH I 5 .   ? -21.993 32.742  -13.239 1.00 24.42 ?  650 HOH A O   1 
HETATM 6185 O  O   . HOH I 5 .   ? -13.606 23.980  17.790  1.00 27.99 ?  651 HOH A O   1 
HETATM 6186 O  O   . HOH I 5 .   ? -19.587 28.628  -13.553 1.00 22.81 ?  652 HOH A O   1 
HETATM 6187 O  O   . HOH I 5 .   ? -3.780  16.299  -7.031  1.00 33.74 ?  653 HOH A O   1 
HETATM 6188 O  O   . HOH I 5 .   ? -30.641 23.817  -14.461 1.00 31.33 ?  654 HOH A O   1 
HETATM 6189 O  O   . HOH I 5 .   ? -8.939  28.592  -24.956 1.00 39.95 ?  655 HOH A O   1 
HETATM 6190 O  O   . HOH I 5 .   ? -60.284 21.933  -14.128 1.00 47.50 ?  656 HOH A O   1 
HETATM 6191 O  O   . HOH I 5 .   ? -12.649 32.566  15.622  1.00 27.52 ?  657 HOH A O   1 
HETATM 6192 O  O   . HOH I 5 .   ? -54.204 22.776  -21.318 1.00 48.22 ?  658 HOH A O   1 
HETATM 6193 O  O   . HOH I 5 .   ? -9.501  12.040  -1.468  1.00 35.22 ?  659 HOH A O   1 
HETATM 6194 O  O   . HOH I 5 .   ? -22.066 15.944  16.115  1.00 37.08 ?  660 HOH A O   1 
HETATM 6195 O  O   . HOH I 5 .   ? -17.314 9.101   -17.631 1.00 36.32 ?  661 HOH A O   1 
HETATM 6196 O  O   . HOH I 5 .   ? -33.853 11.340  2.037   1.00 33.71 ?  662 HOH A O   1 
HETATM 6197 O  O   . HOH I 5 .   ? -50.140 30.055  -16.603 1.00 44.46 ?  663 HOH A O   1 
HETATM 6198 O  O   . HOH I 5 .   ? -21.909 29.354  -18.840 1.00 31.47 ?  664 HOH A O   1 
HETATM 6199 O  O   . HOH I 5 .   ? -24.347 21.758  -24.788 1.00 45.43 ?  665 HOH A O   1 
HETATM 6200 O  O   . HOH I 5 .   ? -27.537 5.818   -15.871 1.00 29.39 ?  666 HOH A O   1 
HETATM 6201 O  O   . HOH I 5 .   ? -25.756 3.993   -5.418  1.00 26.60 ?  667 HOH A O   1 
HETATM 6202 O  O   . HOH I 5 .   ? -24.220 2.171   11.544  1.00 31.43 ?  668 HOH A O   1 
HETATM 6203 O  O   . HOH I 5 .   ? -22.115 29.528  -14.549 1.00 28.65 ?  669 HOH A O   1 
HETATM 6204 O  O   . HOH I 5 .   ? -35.837 33.714  5.727   1.00 42.41 ?  670 HOH A O   1 
HETATM 6205 O  O   . HOH I 5 .   ? -8.082  29.903  2.914   1.00 32.04 ?  671 HOH A O   1 
HETATM 6206 O  O   . HOH I 5 .   ? -21.533 19.483  1.424   1.00 28.34 ?  672 HOH A O   1 
HETATM 6207 O  O   . HOH I 5 .   ? -48.797 11.610  -4.987  1.00 38.87 ?  673 HOH A O   1 
HETATM 6208 O  O   . HOH I 5 .   ? -14.070 7.588   -6.417  1.00 31.90 ?  674 HOH A O   1 
HETATM 6209 O  O   . HOH I 5 .   ? -21.823 9.763   -4.202  1.00 26.06 ?  675 HOH A O   1 
HETATM 6210 O  O   . HOH I 5 .   ? 1.971   31.768  -5.497  1.00 41.12 ?  676 HOH A O   1 
HETATM 6211 O  O   . HOH I 5 .   ? -28.012 14.037  20.274  1.00 26.05 ?  677 HOH A O   1 
HETATM 6212 O  O   . HOH I 5 .   ? -32.402 33.372  -0.075  1.00 33.89 ?  678 HOH A O   1 
HETATM 6213 O  O   . HOH I 5 .   ? -51.134 21.331  6.661   1.00 40.96 ?  679 HOH A O   1 
HETATM 6214 O  O   . HOH I 5 .   ? -25.711 16.178  -11.097 1.00 33.61 ?  680 HOH A O   1 
HETATM 6215 O  O   . HOH I 5 .   ? -46.225 34.531  1.245   1.00 48.06 ?  681 HOH A O   1 
HETATM 6216 O  O   . HOH I 5 .   ? -29.279 26.744  -23.254 1.00 45.06 ?  682 HOH A O   1 
HETATM 6217 O  O   . HOH I 5 .   ? -11.128 17.007  -16.586 1.00 25.68 ?  683 HOH A O   1 
HETATM 6218 O  O   . HOH I 5 .   ? -44.231 10.955  22.794  1.00 27.30 ?  684 HOH A O   1 
HETATM 6219 O  O   . HOH I 5 .   ? -41.788 4.232   1.628   1.00 36.45 ?  685 HOH A O   1 
HETATM 6220 O  O   . HOH I 5 .   ? -23.254 24.205  2.464   1.00 33.50 ?  686 HOH A O   1 
HETATM 6221 O  O   . HOH I 5 .   ? -23.799 0.225   -14.646 1.00 32.05 ?  687 HOH A O   1 
HETATM 6222 O  O   . HOH I 5 .   ? -36.505 3.370   -2.611  1.00 26.06 ?  688 HOH A O   1 
HETATM 6223 O  O   . HOH I 5 .   ? -21.253 25.791  18.231  1.00 27.99 ?  689 HOH A O   1 
HETATM 6224 O  O   . HOH I 5 .   ? -23.880 9.227   -0.795  1.00 22.54 ?  690 HOH A O   1 
HETATM 6225 O  O   . HOH I 5 .   ? -43.185 26.107  12.667  1.00 25.51 ?  691 HOH A O   1 
HETATM 6226 O  O   . HOH I 5 .   ? -19.562 16.221  -16.637 1.00 23.44 ?  692 HOH A O   1 
HETATM 6227 O  O   . HOH I 5 .   ? -7.790  32.862  -9.517  1.00 26.90 ?  693 HOH A O   1 
HETATM 6228 O  O   . HOH I 5 .   ? -52.893 11.638  -8.810  1.00 45.94 ?  694 HOH A O   1 
HETATM 6229 O  O   . HOH I 5 .   ? -28.801 5.705   10.763  1.00 23.10 ?  695 HOH A O   1 
HETATM 6230 O  O   . HOH I 5 .   ? -6.547  7.547   -7.328  1.00 48.38 ?  696 HOH A O   1 
HETATM 6231 O  O   . HOH I 5 .   ? -24.470 28.056  -8.744  1.00 24.84 ?  697 HOH A O   1 
HETATM 6232 O  O   . HOH I 5 .   ? -20.537 23.223  15.516  1.00 24.56 ?  698 HOH A O   1 
HETATM 6233 O  O   . HOH I 5 .   ? -23.064 26.356  20.416  1.00 29.22 ?  699 HOH A O   1 
HETATM 6234 O  O   . HOH I 5 .   ? -24.153 9.934   3.174   1.00 22.94 ?  700 HOH A O   1 
HETATM 6235 O  O   . HOH I 5 .   ? -25.557 18.958  -12.289 1.00 27.96 ?  701 HOH A O   1 
HETATM 6236 O  O   . HOH I 5 .   ? -32.899 20.602  23.501  1.00 30.38 ?  702 HOH A O   1 
HETATM 6237 O  O   . HOH I 5 .   ? -37.745 30.331  -3.598  1.00 29.22 ?  703 HOH A O   1 
HETATM 6238 O  O   . HOH I 5 .   ? -24.568 33.587  12.143  1.00 27.57 ?  704 HOH A O   1 
HETATM 6239 O  O   . HOH I 5 .   ? -24.280 16.484  -16.361 1.00 36.19 ?  705 HOH A O   1 
HETATM 6240 O  O   . HOH I 5 .   ? -27.307 20.210  -20.671 1.00 30.69 ?  706 HOH A O   1 
HETATM 6241 O  O   . HOH I 5 .   ? -19.743 12.087  -20.784 1.00 36.12 ?  707 HOH A O   1 
HETATM 6242 O  O   . HOH I 5 .   ? -19.614 20.186  -2.809  1.00 25.13 ?  708 HOH A O   1 
HETATM 6243 O  O   . HOH I 5 .   ? -54.459 11.692  -17.430 1.00 42.22 ?  709 HOH A O   1 
HETATM 6244 O  O   . HOH I 5 .   ? -4.300  27.278  -7.005  1.00 29.36 ?  710 HOH A O   1 
HETATM 6245 O  O   . HOH I 5 .   ? -16.116 36.710  -9.910  1.00 40.01 ?  711 HOH A O   1 
HETATM 6246 O  O   . HOH I 5 .   ? -11.497 24.585  11.562  1.00 34.43 ?  712 HOH A O   1 
HETATM 6247 O  O   . HOH I 5 .   ? -53.553 19.712  12.158  1.00 35.07 ?  713 HOH A O   1 
HETATM 6248 O  O   . HOH I 5 .   ? -9.379  18.914  -22.653 1.00 39.30 ?  714 HOH A O   1 
HETATM 6249 O  O   . HOH I 5 .   ? -46.640 5.612   -2.916  1.00 31.04 ?  715 HOH A O   1 
HETATM 6250 O  O   . HOH I 5 .   ? -26.930 35.408  8.363   1.00 30.55 ?  716 HOH A O   1 
HETATM 6251 O  O   . HOH I 5 .   ? -51.114 18.839  -2.637  1.00 33.88 ?  717 HOH A O   1 
HETATM 6252 O  O   . HOH I 5 .   ? -21.527 2.367   21.377  1.00 29.86 ?  718 HOH A O   1 
HETATM 6253 O  O   . HOH I 5 .   ? -48.423 5.001   -4.573  1.00 36.57 ?  719 HOH A O   1 
HETATM 6254 O  O   . HOH I 5 .   ? -18.712 19.415  -25.417 1.00 42.76 ?  720 HOH A O   1 
HETATM 6255 O  O   . HOH I 5 .   ? -38.103 9.198   -10.827 1.00 29.79 ?  721 HOH A O   1 
HETATM 6256 O  O   . HOH I 5 .   ? -44.356 29.088  -3.266  1.00 39.59 ?  722 HOH A O   1 
HETATM 6257 O  O   . HOH I 5 .   ? -39.791 11.058  -8.504  1.00 28.39 ?  723 HOH A O   1 
HETATM 6258 O  O   . HOH I 5 .   ? -30.075 38.273  18.743  1.00 43.29 ?  724 HOH A O   1 
HETATM 6259 O  O   . HOH I 5 .   ? -23.842 21.138  1.542   1.00 25.93 ?  725 HOH A O   1 
HETATM 6260 O  O   . HOH I 5 .   ? -40.595 29.529  22.065  1.00 34.70 ?  726 HOH A O   1 
HETATM 6261 O  O   . HOH I 5 .   ? -13.700 35.165  -5.326  1.00 31.66 ?  727 HOH A O   1 
HETATM 6262 O  O   . HOH I 5 .   ? -33.877 8.386   -13.148 1.00 26.80 ?  728 HOH A O   1 
HETATM 6263 O  O   . HOH I 5 .   ? -41.677 5.629   24.295  1.00 30.70 ?  729 HOH A O   1 
HETATM 6264 O  O   . HOH I 5 .   ? -16.824 11.214  -8.451  1.00 25.64 ?  730 HOH A O   1 
HETATM 6265 O  O   . HOH I 5 .   ? -44.365 31.244  -17.701 1.00 40.48 ?  731 HOH A O   1 
HETATM 6266 O  O   . HOH I 5 .   ? -24.822 26.279  -18.271 1.00 29.77 ?  732 HOH A O   1 
HETATM 6267 O  O   . HOH I 5 .   ? -34.979 23.145  3.381   1.00 22.81 ?  733 HOH A O   1 
HETATM 6268 O  O   . HOH I 5 .   ? -16.782 13.414  6.852   1.00 27.18 ?  734 HOH A O   1 
HETATM 6269 O  O   . HOH I 5 .   ? -44.932 11.268  11.500  1.00 20.83 ?  735 HOH A O   1 
HETATM 6270 O  O   . HOH I 5 .   ? -17.670 14.334  -1.799  1.00 29.88 ?  736 HOH A O   1 
HETATM 6271 O  O   . HOH I 5 .   ? -36.596 9.325   25.051  1.00 44.30 ?  737 HOH A O   1 
HETATM 6272 O  O   . HOH I 5 .   ? -32.962 1.641   -19.580 1.00 38.49 ?  738 HOH A O   1 
HETATM 6273 O  O   . HOH I 5 .   ? -41.380 6.458   -8.676  1.00 27.65 ?  739 HOH A O   1 
HETATM 6274 O  O   . HOH I 5 .   ? -29.414 19.422  -0.199  1.00 21.10 ?  740 HOH A O   1 
HETATM 6275 O  O   . HOH I 5 .   ? -13.887 8.197   -3.523  1.00 35.71 ?  741 HOH A O   1 
HETATM 6276 O  O   . HOH I 5 .   ? -23.351 11.315  19.601  1.00 32.83 ?  742 HOH A O   1 
HETATM 6277 O  O   . HOH I 5 .   ? -22.649 27.870  -16.370 1.00 26.95 ?  743 HOH A O   1 
HETATM 6278 O  O   . HOH I 5 .   ? -18.037 37.028  -0.200  1.00 39.78 ?  744 HOH A O   1 
HETATM 6279 O  O   . HOH I 5 .   ? -38.479 28.659  17.757  1.00 29.67 ?  745 HOH A O   1 
HETATM 6280 O  O   . HOH I 5 .   ? -32.875 13.550  0.524   1.00 29.91 ?  746 HOH A O   1 
HETATM 6281 O  O   . HOH I 5 .   ? -45.634 24.191  19.502  1.00 36.08 ?  747 HOH A O   1 
HETATM 6282 O  O   . HOH I 5 .   ? -22.776 34.845  -6.610  1.00 40.58 ?  748 HOH A O   1 
HETATM 6283 O  O   . HOH I 5 .   ? -51.125 20.497  12.655  1.00 32.90 ?  749 HOH A O   1 
HETATM 6284 O  O   . HOH I 5 .   ? -34.381 -0.846  -20.247 1.00 39.26 ?  750 HOH A O   1 
HETATM 6285 O  O   . HOH I 5 .   ? -19.123 12.720  -7.461  1.00 31.31 ?  751 HOH A O   1 
HETATM 6286 O  O   . HOH I 5 .   ? -26.931 30.473  20.148  1.00 28.00 ?  752 HOH A O   1 
HETATM 6287 O  O   . HOH I 5 .   ? -39.127 8.214   1.473   1.00 32.51 ?  753 HOH A O   1 
HETATM 6288 O  O   . HOH I 5 .   ? -46.520 27.317  -3.307  1.00 44.94 ?  754 HOH A O   1 
HETATM 6289 O  O   . HOH I 5 .   ? -22.133 5.013   7.487   1.00 31.22 ?  755 HOH A O   1 
HETATM 6290 O  O   . HOH I 5 .   ? -30.197 5.716   -3.101  1.00 23.86 ?  756 HOH A O   1 
HETATM 6291 O  O   . HOH I 5 .   ? -49.402 31.737  5.962   1.00 33.95 ?  757 HOH A O   1 
HETATM 6292 O  O   . HOH I 5 .   ? -15.207 3.712   -8.858  1.00 42.76 ?  758 HOH A O   1 
HETATM 6293 O  O   . HOH I 5 .   ? -4.063  19.370  -18.187 1.00 46.88 ?  759 HOH A O   1 
HETATM 6294 O  O   . HOH I 5 .   ? -39.881 31.344  9.290   1.00 36.44 ?  760 HOH A O   1 
HETATM 6295 O  O   . HOH I 5 .   ? -28.021 0.897   10.588  1.00 24.37 ?  761 HOH A O   1 
HETATM 6296 O  O   . HOH I 5 .   ? -6.615  13.537  4.454   1.00 39.43 ?  762 HOH A O   1 
HETATM 6297 O  O   . HOH I 5 .   ? -42.233 33.464  -18.978 1.00 44.68 ?  763 HOH A O   1 
HETATM 6298 O  O   . HOH I 5 .   ? -33.094 35.760  12.184  1.00 27.98 ?  764 HOH A O   1 
HETATM 6299 O  O   . HOH I 5 .   ? -42.938 8.777   -19.943 1.00 37.60 ?  765 HOH A O   1 
HETATM 6300 O  O   . HOH I 5 .   ? -23.146 29.364  -11.750 1.00 24.56 ?  766 HOH A O   1 
HETATM 6301 O  O   . HOH I 5 .   ? -29.602 17.028  22.890  1.00 27.62 ?  767 HOH A O   1 
HETATM 6302 O  O   . HOH I 5 .   ? -3.791  24.631  -6.346  1.00 28.36 ?  768 HOH A O   1 
HETATM 6303 O  O   . HOH I 5 .   ? -47.475 7.088   -0.715  1.00 29.97 ?  769 HOH A O   1 
HETATM 6304 O  O   . HOH I 5 .   ? -25.225 30.408  -1.579  1.00 26.11 ?  770 HOH A O   1 
HETATM 6305 O  O   . HOH I 5 .   ? -49.434 18.831  -0.641  1.00 30.01 ?  771 HOH A O   1 
HETATM 6306 O  O   . HOH I 5 .   ? -3.134  18.565  -8.573  1.00 32.02 ?  772 HOH A O   1 
HETATM 6307 O  O   . HOH I 5 .   ? -25.186 33.460  1.119   1.00 31.52 ?  773 HOH A O   1 
HETATM 6308 O  O   . HOH I 5 .   ? -39.188 32.920  -7.168  1.00 40.20 ?  774 HOH A O   1 
HETATM 6309 O  O   . HOH I 5 .   ? -15.028 34.881  -11.752 1.00 32.95 ?  775 HOH A O   1 
HETATM 6310 O  O   . HOH I 5 .   ? -22.968 0.438   -18.554 1.00 36.04 ?  776 HOH A O   1 
HETATM 6311 O  O   . HOH I 5 .   ? -15.208 22.844  -23.777 1.00 32.78 ?  777 HOH A O   1 
HETATM 6312 O  O   . HOH I 5 .   ? -27.735 4.058   -2.148  1.00 19.52 ?  778 HOH A O   1 
HETATM 6313 O  O   . HOH I 5 .   ? -8.014  21.667  -24.642 1.00 37.29 ?  779 HOH A O   1 
HETATM 6314 O  O   . HOH I 5 .   ? -32.059 21.310  -5.788  1.00 26.95 ?  780 HOH A O   1 
HETATM 6315 O  O   . HOH I 5 .   ? -35.362 12.662  -0.683  1.00 29.41 ?  781 HOH A O   1 
HETATM 6316 O  O   . HOH I 5 .   ? -23.585 8.939   -18.610 1.00 31.67 ?  782 HOH A O   1 
HETATM 6317 O  O   . HOH I 5 .   ? -14.261 3.602   -12.362 1.00 41.96 ?  783 HOH A O   1 
HETATM 6318 O  O   . HOH I 5 .   ? -21.537 5.166   3.081   1.00 35.40 ?  784 HOH A O   1 
HETATM 6319 O  O   . HOH I 5 .   ? -32.293 19.404  20.874  1.00 22.37 ?  785 HOH A O   1 
HETATM 6320 O  O   . HOH I 5 .   ? -23.876 18.905  8.259   1.00 27.78 ?  786 HOH A O   1 
HETATM 6321 O  O   . HOH I 5 .   ? -36.301 12.689  27.665  1.00 37.18 ?  787 HOH A O   1 
HETATM 6322 O  O   . HOH I 5 .   ? -36.259 34.872  11.235  1.00 30.80 ?  788 HOH A O   1 
HETATM 6323 O  O   . HOH I 5 .   ? -27.573 2.773   12.557  1.00 29.79 ?  789 HOH A O   1 
HETATM 6324 O  O   . HOH I 5 .   ? -12.903 18.272  10.151  1.00 42.95 ?  790 HOH A O   1 
HETATM 6325 O  O   . HOH I 5 .   ? -10.649 12.894  -17.663 1.00 33.04 ?  791 HOH A O   1 
HETATM 6326 O  O   . HOH I 5 .   ? -33.012 5.561   3.630   1.00 28.70 ?  792 HOH A O   1 
HETATM 6327 O  O   . HOH I 5 .   ? -17.403 7.187   3.327   1.00 32.46 ?  793 HOH A O   1 
HETATM 6328 O  O   . HOH I 5 .   ? -32.146 3.042   -4.883  1.00 23.02 ?  794 HOH A O   1 
HETATM 6329 O  O   . HOH I 5 .   ? -8.488  31.491  -22.949 1.00 37.77 ?  795 HOH A O   1 
HETATM 6330 O  O   . HOH I 5 .   ? -1.229  24.429  -14.148 1.00 36.53 ?  796 HOH A O   1 
HETATM 6331 O  O   . HOH I 5 .   ? -25.695 23.173  0.822   1.00 28.02 ?  797 HOH A O   1 
HETATM 6332 O  O   . HOH I 5 .   ? -26.437 8.296   -19.456 1.00 46.11 ?  798 HOH A O   1 
HETATM 6333 O  O   . HOH I 5 .   ? -19.646 7.880   -16.461 1.00 34.83 ?  799 HOH A O   1 
HETATM 6334 O  O   . HOH I 5 .   ? 1.961   20.046  4.150   1.00 50.14 ?  800 HOH A O   1 
HETATM 6335 O  O   . HOH I 5 .   ? -20.348 6.063   -1.426  1.00 36.73 ?  801 HOH A O   1 
HETATM 6336 O  O   . HOH I 5 .   ? -9.028  36.702  6.252   1.00 45.70 ?  802 HOH A O   1 
HETATM 6337 O  O   . HOH I 5 .   ? -37.812 7.112   0.068   1.00 34.52 ?  803 HOH A O   1 
HETATM 6338 O  O   . HOH I 5 .   ? -31.267 32.546  -9.115  1.00 37.16 ?  804 HOH A O   1 
HETATM 6339 O  O   . HOH I 5 .   ? -34.564 2.228   6.600   1.00 28.59 ?  805 HOH A O   1 
HETATM 6340 O  O   . HOH I 5 .   ? -19.059 19.511  10.512  1.00 28.38 ?  806 HOH A O   1 
HETATM 6341 O  O   . HOH I 5 .   ? -30.679 22.063  -23.421 1.00 42.69 ?  807 HOH A O   1 
HETATM 6342 O  O   . HOH I 5 .   ? -47.184 3.447   21.481  1.00 42.02 ?  808 HOH A O   1 
HETATM 6343 O  O   . HOH I 5 .   ? -31.112 30.092  -11.415 1.00 38.95 ?  809 HOH A O   1 
HETATM 6344 O  O   . HOH I 5 .   ? -27.292 -1.639  -15.401 1.00 33.38 ?  810 HOH A O   1 
HETATM 6345 O  O   . HOH I 5 .   ? -20.625 12.216  -5.101  1.00 23.84 ?  811 HOH A O   1 
HETATM 6346 O  O   . HOH I 5 .   ? -26.730 21.825  9.134   1.00 26.10 ?  812 HOH A O   1 
HETATM 6347 O  O   . HOH I 5 .   ? -38.054 32.944  5.288   1.00 47.34 ?  813 HOH A O   1 
HETATM 6348 O  O   . HOH I 5 .   ? -36.895 34.272  8.564   1.00 40.43 ?  814 HOH A O   1 
HETATM 6349 O  O   . HOH I 5 .   ? -32.330 -5.164  -20.691 1.00 40.65 ?  815 HOH A O   1 
HETATM 6350 O  O   . HOH I 5 .   ? -40.759 10.967  26.292  1.00 42.74 ?  816 HOH A O   1 
HETATM 6351 O  O   . HOH I 5 .   ? -46.352 13.481  2.020   1.00 36.47 ?  817 HOH A O   1 
HETATM 6352 O  O   . HOH I 5 .   ? -19.149 16.546  -1.207  1.00 28.12 ?  818 HOH A O   1 
HETATM 6353 O  O   . HOH I 5 .   ? -47.051 32.303  3.195   1.00 40.26 ?  819 HOH A O   1 
HETATM 6354 O  O   . HOH I 5 .   ? -39.570 4.482   -8.795  1.00 32.25 ?  820 HOH A O   1 
HETATM 6355 O  O   . HOH I 5 .   ? -44.581 15.502  -25.681 1.00 38.07 ?  821 HOH A O   1 
HETATM 6356 O  O   . HOH I 5 .   ? -27.339 27.444  -18.666 1.00 39.07 ?  822 HOH A O   1 
HETATM 6357 O  O   . HOH I 5 .   ? -10.073 33.030  10.803  1.00 35.23 ?  823 HOH A O   1 
HETATM 6358 O  O   . HOH I 5 .   ? -20.203 15.151  -14.235 1.00 23.68 ?  824 HOH A O   1 
HETATM 6359 O  O   . HOH I 5 .   ? -23.996 17.577  -14.212 1.00 26.63 ?  825 HOH A O   1 
HETATM 6360 O  O   . HOH I 5 .   ? -39.139 16.150  24.358  1.00 25.38 ?  826 HOH A O   1 
HETATM 6361 O  O   . HOH I 5 .   ? -26.177 33.514  10.093  1.00 25.89 ?  827 HOH A O   1 
HETATM 6362 O  O   . HOH I 5 .   ? -55.907 17.688  8.142   1.00 45.53 ?  828 HOH A O   1 
HETATM 6363 O  O   . HOH I 5 .   ? -40.487 4.864   10.410  1.00 41.88 ?  829 HOH A O   1 
HETATM 6364 O  O   . HOH I 5 .   ? -12.463 33.161  -22.996 1.00 33.80 ?  830 HOH A O   1 
HETATM 6365 O  O   . HOH I 5 .   ? -40.337 29.543  11.271  1.00 29.64 ?  831 HOH A O   1 
HETATM 6366 O  O   . HOH I 5 .   ? -21.338 4.887   -18.937 1.00 29.56 ?  832 HOH A O   1 
HETATM 6367 O  O   . HOH I 5 .   ? -29.915 34.076  -0.169  1.00 40.67 ?  833 HOH A O   1 
HETATM 6368 O  O   . HOH I 5 .   ? -29.229 33.555  -14.322 1.00 42.24 ?  834 HOH A O   1 
HETATM 6369 O  O   . HOH I 5 .   ? -51.156 4.484   10.082  1.00 48.16 ?  835 HOH A O   1 
HETATM 6370 O  O   . HOH I 5 .   ? -44.405 8.881   7.537   1.00 34.99 ?  836 HOH A O   1 
HETATM 6371 O  O   . HOH I 5 .   ? -24.856 15.936  22.658  1.00 50.36 ?  837 HOH A O   1 
HETATM 6372 O  O   . HOH I 5 .   ? -11.080 16.768  -21.367 1.00 46.19 ?  838 HOH A O   1 
HETATM 6373 O  O   . HOH I 5 .   ? -29.699 3.196   12.005  1.00 25.23 ?  839 HOH A O   1 
HETATM 6374 O  O   . HOH I 5 .   ? -35.916 25.916  26.170  1.00 24.35 ?  840 HOH A O   1 
HETATM 6375 O  O   . HOH I 5 .   ? -7.957  31.798  -0.816  1.00 37.99 ?  841 HOH A O   1 
HETATM 6376 O  O   . HOH I 5 .   ? -36.303 14.256  -10.351 1.00 26.30 ?  842 HOH A O   1 
HETATM 6377 O  O   . HOH I 5 .   ? -19.436 14.844  15.530  1.00 40.08 ?  843 HOH A O   1 
HETATM 6378 O  O   . HOH I 5 .   ? -24.743 30.330  18.397  1.00 24.22 ?  844 HOH A O   1 
HETATM 6379 O  O   . HOH I 5 .   ? -41.527 23.686  24.320  1.00 33.09 ?  845 HOH A O   1 
HETATM 6380 O  O   . HOH I 5 .   ? -18.485 37.486  13.580  1.00 45.66 ?  846 HOH A O   1 
HETATM 6381 O  O   . HOH I 5 .   ? -22.449 15.863  -12.592 1.00 30.00 ?  847 HOH A O   1 
HETATM 6382 O  O   . HOH I 5 .   ? -37.394 36.339  19.287  1.00 28.63 ?  848 HOH A O   1 
HETATM 6383 O  O   . HOH I 5 .   ? -41.965 6.837   10.610  1.00 36.15 ?  849 HOH A O   1 
HETATM 6384 O  O   . HOH I 5 .   ? -7.356  26.382  4.873   1.00 36.30 ?  850 HOH A O   1 
HETATM 6385 O  O   . HOH I 5 .   ? -21.068 10.598  20.120  1.00 34.91 ?  851 HOH A O   1 
HETATM 6386 O  O   . HOH I 5 .   ? -19.766 7.651   10.985  1.00 38.26 ?  852 HOH A O   1 
HETATM 6387 O  O   . HOH I 5 .   ? -11.554 12.633  5.150   1.00 30.56 ?  853 HOH A O   1 
HETATM 6388 O  O   . HOH I 5 .   ? -49.002 25.445  15.357  1.00 41.45 ?  854 HOH A O   1 
HETATM 6389 O  O   . HOH I 5 .   ? -26.659 12.655  -13.405 1.00 36.95 ?  855 HOH A O   1 
HETATM 6390 O  O   . HOH I 5 .   ? -53.550 15.446  -1.267  1.00 40.55 ?  856 HOH A O   1 
HETATM 6391 O  O   . HOH I 5 .   ? -10.521 30.702  12.661  1.00 33.64 ?  857 HOH A O   1 
HETATM 6392 O  O   . HOH I 5 .   ? -23.275 33.406  -3.757  1.00 30.36 ?  858 HOH A O   1 
HETATM 6393 O  O   . HOH I 5 .   ? -12.375 27.875  17.416  1.00 36.81 ?  859 HOH A O   1 
HETATM 6394 O  O   . HOH I 5 .   ? -7.468  9.977   -1.678  1.00 50.06 ?  860 HOH A O   1 
HETATM 6395 O  O   . HOH I 5 .   ? -53.145 19.474  2.167   1.00 41.55 ?  861 HOH A O   1 
HETATM 6396 O  O   . HOH I 5 .   ? -29.640 25.936  -16.500 1.00 35.47 ?  862 HOH A O   1 
HETATM 6397 O  O   . HOH I 5 .   ? -3.745  28.924  -22.970 1.00 47.53 ?  863 HOH A O   1 
HETATM 6398 O  O   . HOH I 5 .   ? -35.526 32.425  -4.160  1.00 26.79 ?  864 HOH A O   1 
HETATM 6399 O  O   . HOH I 5 .   ? -22.055 18.680  9.600   1.00 32.91 ?  865 HOH A O   1 
HETATM 6400 O  O   . HOH I 5 .   ? -2.176  21.307  -7.493  1.00 42.29 ?  866 HOH A O   1 
HETATM 6401 O  O   . HOH I 5 .   ? -15.950 43.413  16.109  1.00 41.02 ?  867 HOH A O   1 
HETATM 6402 O  O   . HOH I 5 .   ? -40.451 5.977   0.225   1.00 34.66 ?  868 HOH A O   1 
HETATM 6403 O  O   . HOH I 5 .   ? -12.971 3.244   -14.350 1.00 46.02 ?  869 HOH A O   1 
HETATM 6404 O  O   . HOH I 5 .   ? -24.019 31.180  -19.814 1.00 36.62 ?  870 HOH A O   1 
HETATM 6405 O  O   . HOH I 5 .   ? -19.521 2.988   13.362  1.00 42.47 ?  871 HOH A O   1 
HETATM 6406 O  O   . HOH I 5 .   ? -18.184 22.638  22.228  1.00 32.25 ?  872 HOH A O   1 
HETATM 6407 O  O   . HOH I 5 .   ? -44.389 4.881   23.823  1.00 35.09 ?  873 HOH A O   1 
HETATM 6408 O  O   . HOH I 5 .   ? -37.238 33.199  2.689   1.00 42.03 ?  874 HOH A O   1 
HETATM 6409 O  O   . HOH I 5 .   ? -17.544 8.062   -0.855  1.00 34.26 ?  875 HOH A O   1 
HETATM 6410 O  O   . HOH I 5 .   ? -23.039 33.863  -20.091 1.00 34.21 ?  876 HOH A O   1 
HETATM 6411 O  O   . HOH I 5 .   ? -39.712 32.386  24.600  1.00 44.95 ?  877 HOH A O   1 
HETATM 6412 O  O   . HOH I 5 .   ? -40.772 7.098   12.454  1.00 30.09 ?  878 HOH A O   1 
HETATM 6413 O  O   . HOH I 5 .   ? -40.233 32.034  6.055   1.00 50.13 ?  879 HOH A O   1 
HETATM 6414 O  O   . HOH I 5 .   ? -41.392 2.721   -5.998  1.00 31.82 ?  880 HOH A O   1 
HETATM 6415 O  O   . HOH I 5 .   ? -24.919 19.655  10.237  1.00 25.00 ?  881 HOH A O   1 
HETATM 6416 O  O   . HOH I 5 .   ? -54.851 13.806  -11.449 1.00 42.90 ?  882 HOH A O   1 
HETATM 6417 O  O   . HOH I 5 .   ? -51.826 19.733  8.026   1.00 42.17 ?  883 HOH A O   1 
HETATM 6418 O  O   . HOH I 5 .   ? -15.466 7.285   5.287   1.00 50.27 ?  884 HOH A O   1 
HETATM 6419 O  O   . HOH I 5 .   ? -42.451 28.460  -26.410 1.00 75.22 ?  885 HOH A O   1 
HETATM 6420 O  O   . HOH I 5 .   ? -36.279 5.021   15.325  1.00 30.34 ?  886 HOH A O   1 
HETATM 6421 O  O   . HOH I 5 .   ? -14.294 35.005  16.380  1.00 44.30 ?  887 HOH A O   1 
HETATM 6422 O  O   . HOH I 5 .   ? -20.167 7.628   -3.171  1.00 40.18 ?  888 HOH A O   1 
HETATM 6423 O  O   . HOH I 5 .   ? -8.872  17.830  -14.713 1.00 32.62 ?  889 HOH A O   1 
HETATM 6424 O  O   . HOH I 5 .   ? -18.918 23.771  18.118  1.00 24.20 ?  890 HOH A O   1 
HETATM 6425 O  O   . HOH I 5 .   ? -23.693 18.181  12.393  1.00 32.26 ?  891 HOH A O   1 
HETATM 6426 O  O   . HOH I 5 .   ? -27.044 15.463  -13.395 1.00 38.65 ?  892 HOH A O   1 
HETATM 6427 O  O   . HOH I 5 .   ? -25.446 10.520  21.466  1.00 37.39 ?  893 HOH A O   1 
HETATM 6428 O  O   . HOH I 5 .   ? -18.813 9.972   -20.452 1.00 50.35 ?  894 HOH A O   1 
HETATM 6429 O  O   . HOH I 5 .   ? -42.661 4.677   -19.222 1.00 44.93 ?  895 HOH A O   1 
HETATM 6430 O  O   . HOH I 5 .   ? -27.475 15.811  23.627  1.00 40.10 ?  896 HOH A O   1 
HETATM 6431 O  O   . HOH I 5 .   ? -51.608 17.825  1.893   1.00 42.81 ?  897 HOH A O   1 
HETATM 6432 O  O   . HOH I 5 .   ? -14.394 21.848  17.742  1.00 35.96 ?  898 HOH A O   1 
HETATM 6433 O  O   . HOH I 5 .   ? -39.184 13.987  27.536  1.00 43.04 ?  899 HOH A O   1 
HETATM 6434 O  O   . HOH I 5 .   ? -44.437 30.121  13.976  1.00 44.05 ?  900 HOH A O   1 
HETATM 6435 O  O   . HOH I 5 .   ? -38.741 35.077  12.545  1.00 37.14 ?  901 HOH A O   1 
HETATM 6436 O  O   . HOH I 5 .   ? -23.338 17.131  14.333  1.00 47.84 ?  902 HOH A O   1 
HETATM 6437 O  O   . HOH I 5 .   ? -36.950 3.478   7.235   1.00 38.46 ?  903 HOH A O   1 
HETATM 6438 O  O   . HOH I 5 .   ? -20.771 15.831  20.359  1.00 43.44 ?  904 HOH A O   1 
HETATM 6439 O  O   . HOH I 5 .   ? -27.169 33.150  -0.343  1.00 33.69 ?  905 HOH A O   1 
HETATM 6440 O  O   . HOH I 5 .   ? -12.407 22.843  9.418   1.00 36.68 ?  906 HOH A O   1 
HETATM 6441 O  O   . HOH I 5 .   ? -45.521 3.203   -2.164  1.00 36.69 ?  907 HOH A O   1 
HETATM 6442 O  O   . HOH I 5 .   ? -36.767 3.376   1.125   1.00 42.84 ?  908 HOH A O   1 
HETATM 6443 O  O   . HOH I 5 .   ? -14.976 11.818  7.992   1.00 30.85 ?  909 HOH A O   1 
HETATM 6444 O  O   . HOH I 5 .   ? -18.706 38.215  -11.791 1.00 33.30 ?  910 HOH A O   1 
HETATM 6445 O  O   . HOH I 5 .   ? -38.522 33.229  -4.921  1.00 50.29 ?  911 HOH A O   1 
HETATM 6446 O  O   . HOH I 5 .   ? -29.797 9.967   -21.437 1.00 45.71 ?  912 HOH A O   1 
HETATM 6447 O  O   . HOH I 5 .   ? -37.041 11.582  -9.477  1.00 29.22 ?  913 HOH A O   1 
HETATM 6448 O  O   . HOH I 5 .   ? -17.859 22.193  -24.249 1.00 44.39 ?  914 HOH A O   1 
HETATM 6449 O  O   . HOH I 5 .   ? -41.001 31.512  14.903  1.00 35.85 ?  915 HOH A O   1 
HETATM 6450 O  O   . HOH I 5 .   ? -43.256 2.625   -3.433  1.00 39.47 ?  916 HOH A O   1 
HETATM 6451 O  O   . HOH I 5 .   ? -40.371 34.030  23.190  1.00 45.77 ?  917 HOH A O   1 
HETATM 6452 O  O   . HOH I 5 .   ? -1.688  9.185   -11.009 1.00 61.45 ?  918 HOH A O   1 
HETATM 6453 O  O   . HOH I 5 .   ? -47.661 13.367  3.907   1.00 32.53 ?  919 HOH A O   1 
HETATM 6454 O  O   . HOH I 5 .   ? -55.350 17.077  -8.528  1.00 42.72 ?  920 HOH A O   1 
HETATM 6455 O  O   . HOH I 5 .   ? -54.460 18.993  4.446   1.00 52.54 ?  921 HOH A O   1 
HETATM 6456 O  O   . HOH I 5 .   ? -54.586 21.648  10.162  1.00 43.92 ?  922 HOH A O   1 
HETATM 6457 O  O   . HOH I 5 .   ? -8.828  11.496  4.999   1.00 42.11 ?  923 HOH A O   1 
HETATM 6458 O  O   . HOH I 5 .   ? -19.574 1.719   15.856  1.00 44.70 ?  924 HOH A O   1 
HETATM 6459 O  O   . HOH I 5 .   ? -33.556 37.207  9.734   1.00 38.97 ?  925 HOH A O   1 
HETATM 6460 O  O   . HOH I 5 .   ? -10.937 34.444  0.501   1.00 34.56 ?  926 HOH A O   1 
HETATM 6461 O  O   . HOH I 5 .   ? -16.320 6.755   -2.400  1.00 42.15 ?  927 HOH A O   1 
HETATM 6462 O  O   . HOH I 5 .   ? -5.676  14.778  6.329   1.00 39.26 ?  928 HOH A O   1 
HETATM 6463 O  O   . HOH I 5 .   ? -9.982  15.408  -18.826 1.00 33.99 ?  929 HOH A O   1 
HETATM 6464 O  O   . HOH I 5 .   ? -43.103 28.809  12.105  1.00 29.42 ?  930 HOH A O   1 
HETATM 6465 O  O   . HOH I 5 .   ? -34.695 2.188   -4.528  1.00 25.17 ?  931 HOH A O   1 
HETATM 6466 O  O   . HOH I 5 .   ? -12.616 35.691  -0.957  1.00 39.65 ?  932 HOH A O   1 
HETATM 6467 O  O   . HOH I 5 .   ? -25.733 35.584  -6.063  1.00 53.95 ?  933 HOH A O   1 
HETATM 6468 O  O   . HOH I 5 .   ? -38.820 26.199  -26.986 1.00 54.16 ?  934 HOH A O   1 
HETATM 6469 O  O   . HOH I 5 .   ? -18.686 3.333   21.758  1.00 43.47 ?  935 HOH A O   1 
HETATM 6470 O  O   . HOH I 5 .   ? -46.972 32.478  -18.060 1.00 53.42 ?  936 HOH A O   1 
HETATM 6471 O  O   . HOH I 5 .   ? -9.146  10.355  2.540   1.00 40.70 ?  937 HOH A O   1 
HETATM 6472 O  O   . HOH I 5 .   ? -3.190  28.811  -4.458  1.00 46.91 ?  938 HOH A O   1 
HETATM 6473 O  O   . HOH I 5 .   ? -21.164 7.750   -18.412 1.00 36.19 ?  939 HOH A O   1 
HETATM 6474 O  O   . HOH I 5 .   ? -32.067 34.617  -6.208  1.00 41.67 ?  940 HOH A O   1 
HETATM 6475 O  O   . HOH I 5 .   ? -9.958  26.459  10.218  1.00 40.96 ?  941 HOH A O   1 
HETATM 6476 O  O   . HOH I 5 .   ? -39.662 33.816  10.917  1.00 40.95 ?  942 HOH A O   1 
HETATM 6477 O  O   . HOH I 5 .   ? -13.552 20.630  10.866  1.00 38.67 ?  943 HOH A O   1 
HETATM 6478 O  O   . HOH I 5 .   ? -40.052 23.348  26.412  1.00 38.63 ?  944 HOH A O   1 
HETATM 6479 O  O   . HOH I 5 .   ? -18.832 -0.014  -13.380 1.00 42.22 ?  945 HOH A O   1 
HETATM 6480 O  O   . HOH I 5 .   ? -24.409 7.728   -21.189 1.00 44.23 ?  946 HOH A O   1 
HETATM 6481 O  O   . HOH I 5 .   ? -41.830 7.699   26.284  1.00 45.77 ?  947 HOH A O   1 
HETATM 6482 O  O   . HOH I 5 .   ? -9.591  28.396  12.008  1.00 37.90 ?  948 HOH A O   1 
HETATM 6483 O  O   . HOH I 5 .   ? -27.045 7.134   -21.327 1.00 43.27 ?  949 HOH A O   1 
HETATM 6484 O  O   . HOH I 5 .   ? -46.484 10.139  6.953   1.00 35.88 ?  950 HOH A O   1 
HETATM 6485 O  O   . HOH I 5 .   ? -16.256 19.742  -24.418 1.00 40.20 ?  951 HOH A O   1 
HETATM 6486 O  O   . HOH I 5 .   ? -14.227 36.046  -2.475  1.00 36.18 ?  952 HOH A O   1 
HETATM 6487 O  O   . HOH I 5 .   ? -39.415 35.229  5.551   1.00 55.53 ?  953 HOH A O   1 
HETATM 6488 O  O   . HOH I 5 .   ? -1.232  11.660  -12.333 1.00 57.13 ?  954 HOH A O   1 
HETATM 6489 O  O   . HOH I 5 .   ? -15.411 37.880  0.936   1.00 48.41 ?  955 HOH A O   1 
HETATM 6490 O  O   . HOH I 5 .   ? -26.849 13.232  23.646  1.00 46.97 ?  956 HOH A O   1 
HETATM 6491 O  O   . HOH I 5 .   ? -19.094 4.494   2.854   1.00 37.06 ?  957 HOH A O   1 
HETATM 6492 O  O   . HOH I 5 .   ? -8.400  11.043  7.155   1.00 50.86 ?  958 HOH A O   1 
HETATM 6493 O  O   . HOH I 5 .   ? -6.356  13.382  8.637   1.00 41.16 ?  959 HOH A O   1 
HETATM 6494 O  O   . HOH I 5 .   ? -20.066 1.517   0.418   1.00 39.18 ?  960 HOH A O   1 
HETATM 6495 O  O   . HOH I 5 .   ? -42.375 35.585  24.799  1.00 57.98 ?  961 HOH A O   1 
HETATM 6496 O  O   . HOH J 5 .   ? -25.617 -8.961  22.609  1.00 35.65 ?  601 HOH B O   1 
HETATM 6497 O  O   . HOH J 5 .   ? -10.146 -23.179 31.965  1.00 46.64 ?  602 HOH B O   1 
HETATM 6498 O  O   . HOH J 5 .   ? -15.986 -21.583 1.054   1.00 33.06 ?  603 HOH B O   1 
HETATM 6499 O  O   . HOH J 5 .   ? -38.130 -14.162 28.344  1.00 46.43 ?  604 HOH B O   1 
HETATM 6500 O  O   . HOH J 5 .   ? -48.585 -20.738 12.445  1.00 46.96 ?  605 HOH B O   1 
HETATM 6501 O  O   . HOH J 5 .   ? -29.101 -28.121 -10.420 1.00 27.56 ?  606 HOH B O   1 
HETATM 6502 O  O   . HOH J 5 .   ? -43.507 2.110   -7.565  1.00 34.27 ?  607 HOH B O   1 
HETATM 6503 O  O   . HOH J 5 .   ? -36.085 -25.624 28.032  1.00 58.06 ?  608 HOH B O   1 
HETATM 6504 O  O   . HOH J 5 .   ? -52.867 1.320   23.062  1.00 38.14 ?  609 HOH B O   1 
HETATM 6505 O  O   . HOH J 5 .   ? -23.040 -5.887  -3.257  1.00 27.28 ?  610 HOH B O   1 
HETATM 6506 O  O   . HOH J 5 .   ? -20.679 -8.461  29.586  1.00 41.65 ?  611 HOH B O   1 
HETATM 6507 O  O   . HOH J 5 .   ? -12.353 -24.323 3.527   1.00 38.44 ?  612 HOH B O   1 
HETATM 6508 O  O   . HOH J 5 .   ? -24.526 -11.507 -8.013  1.00 38.33 ?  613 HOH B O   1 
HETATM 6509 O  O   . HOH J 5 .   ? -27.274 -21.602 -12.213 1.00 32.24 ?  614 HOH B O   1 
HETATM 6510 O  O   . HOH J 5 .   ? -31.921 -29.266 4.401   1.00 33.98 ?  615 HOH B O   1 
HETATM 6511 O  O   . HOH J 5 .   ? -48.317 -17.715 -6.378  1.00 32.89 ?  616 HOH B O   1 
HETATM 6512 O  O   . HOH J 5 .   ? -20.541 -9.152  -9.200  1.00 39.30 ?  617 HOH B O   1 
HETATM 6513 O  O   . HOH J 5 .   ? -28.083 -30.358 15.029  1.00 45.77 ?  618 HOH B O   1 
HETATM 6514 O  O   . HOH J 5 .   ? -38.981 -21.801 -17.301 1.00 26.97 ?  619 HOH B O   1 
HETATM 6515 O  O   . HOH J 5 .   ? -28.942 -23.352 16.914  1.00 26.61 ?  620 HOH B O   1 
HETATM 6516 O  O   . HOH J 5 .   ? -25.657 -35.285 4.712   1.00 50.08 ?  621 HOH B O   1 
HETATM 6517 O  O   . HOH J 5 .   ? -33.930 -31.932 -7.415  1.00 36.21 ?  622 HOH B O   1 
HETATM 6518 O  O   . HOH J 5 .   ? -16.112 -30.728 29.890  1.00 46.43 ?  623 HOH B O   1 
HETATM 6519 O  O   . HOH J 5 .   ? -30.590 -15.273 29.111  1.00 41.17 ?  624 HOH B O   1 
HETATM 6520 O  O   . HOH J 5 .   ? -18.617 -7.927  17.015  1.00 30.03 ?  625 HOH B O   1 
HETATM 6521 O  O   . HOH J 5 .   ? -12.503 -5.717  16.120  1.00 37.17 ?  626 HOH B O   1 
HETATM 6522 O  O   . HOH J 5 .   ? -39.513 -0.042  4.772   1.00 32.02 ?  627 HOH B O   1 
HETATM 6523 O  O   . HOH J 5 .   ? -8.229  -6.365  15.571  1.00 43.64 ?  628 HOH B O   1 
HETATM 6524 O  O   . HOH J 5 .   ? -52.876 -3.260  30.310  1.00 44.71 ?  629 HOH B O   1 
HETATM 6525 O  O   . HOH J 5 .   ? -36.068 0.180   1.523   1.00 24.20 ?  630 HOH B O   1 
HETATM 6526 O  O   . HOH J 5 .   ? -15.635 -1.291  17.516  1.00 37.55 ?  631 HOH B O   1 
HETATM 6527 O  O   . HOH J 5 .   ? -37.942 -25.183 1.942   1.00 26.99 ?  632 HOH B O   1 
HETATM 6528 O  O   . HOH J 5 .   ? -38.014 2.502   -0.860  1.00 29.62 ?  633 HOH B O   1 
HETATM 6529 O  O   . HOH J 5 .   ? -47.026 -18.148 -3.979  1.00 32.59 ?  634 HOH B O   1 
HETATM 6530 O  O   . HOH J 5 .   ? -17.418 -15.257 31.285  1.00 43.51 ?  635 HOH B O   1 
HETATM 6531 O  O   . HOH J 5 .   ? -28.254 -34.575 -8.018  1.00 25.90 ?  636 HOH B O   1 
HETATM 6532 O  O   . HOH J 5 .   ? -55.926 -2.305  25.437  1.00 40.20 ?  637 HOH B O   1 
HETATM 6533 O  O   . HOH J 5 .   ? -6.367  -15.110 15.516  1.00 38.99 ?  638 HOH B O   1 
HETATM 6534 O  O   . HOH J 5 .   ? -62.871 -11.863 23.150  1.00 48.57 ?  639 HOH B O   1 
HETATM 6535 O  O   . HOH J 5 .   ? -27.433 -23.767 25.168  1.00 47.31 ?  640 HOH B O   1 
HETATM 6536 O  O   . HOH J 5 .   ? -34.668 -2.351  21.692  1.00 28.75 ?  641 HOH B O   1 
HETATM 6537 O  O   . HOH J 5 .   ? -37.516 -0.028  7.915   1.00 41.44 ?  642 HOH B O   1 
HETATM 6538 O  O   . HOH J 5 .   ? -42.367 -27.467 -17.269 1.00 41.39 ?  643 HOH B O   1 
HETATM 6539 O  O   . HOH J 5 .   ? -44.627 -27.698 11.523  1.00 51.36 ?  644 HOH B O   1 
HETATM 6540 O  O   . HOH J 5 .   ? -12.313 -19.311 12.401  1.00 29.32 ?  645 HOH B O   1 
HETATM 6541 O  O   . HOH J 5 .   ? -34.392 -18.316 23.005  1.00 44.43 ?  646 HOH B O   1 
HETATM 6542 O  O   . HOH J 5 .   ? -35.342 -5.271  6.490   1.00 38.64 ?  647 HOH B O   1 
HETATM 6543 O  O   . HOH J 5 .   ? -23.735 3.682   -7.240  1.00 24.82 ?  648 HOH B O   1 
HETATM 6544 O  O   . HOH J 5 .   ? -41.092 -3.739  16.928  1.00 30.49 ?  649 HOH B O   1 
HETATM 6545 O  O   . HOH J 5 .   ? -16.044 -33.113 15.847  1.00 49.56 ?  650 HOH B O   1 
HETATM 6546 O  O   . HOH J 5 .   ? -15.900 -29.386 7.989   1.00 27.68 ?  651 HOH B O   1 
HETATM 6547 O  O   . HOH J 5 .   ? -13.747 -14.934 25.083  1.00 35.60 ?  652 HOH B O   1 
HETATM 6548 O  O   . HOH J 5 .   ? -11.426 -10.290 9.922   1.00 42.84 ?  653 HOH B O   1 
HETATM 6549 O  O   . HOH J 5 .   ? -38.110 3.609   15.577  1.00 37.52 ?  654 HOH B O   1 
HETATM 6550 O  O   . HOH J 5 .   ? -9.479  -28.382 31.691  1.00 43.21 ?  655 HOH B O   1 
HETATM 6551 O  O   . HOH J 5 .   ? -39.599 5.467   13.629  1.00 29.41 ?  656 HOH B O   1 
HETATM 6552 O  O   . HOH J 5 .   ? -24.362 -15.499 7.295   1.00 26.68 ?  657 HOH B O   1 
HETATM 6553 O  O   . HOH J 5 .   ? -39.929 -19.177 -17.619 1.00 25.74 ?  658 HOH B O   1 
HETATM 6554 O  O   . HOH J 5 .   ? -26.931 -16.613 6.836   1.00 27.18 ?  659 HOH B O   1 
HETATM 6555 O  O   . HOH J 5 .   ? -56.995 -13.164 29.649  1.00 49.52 ?  660 HOH B O   1 
HETATM 6556 O  O   . HOH J 5 .   ? -22.036 -12.796 25.156  1.00 33.64 ?  661 HOH B O   1 
HETATM 6557 O  O   . HOH J 5 .   ? -8.835  -26.024 15.353  1.00 41.72 ?  662 HOH B O   1 
HETATM 6558 O  O   . HOH J 5 .   ? -12.875 -27.715 5.169   1.00 37.03 ?  663 HOH B O   1 
HETATM 6559 O  O   . HOH J 5 .   ? -43.350 -0.355  -8.930  1.00 29.48 ?  664 HOH B O   1 
HETATM 6560 O  O   . HOH J 5 .   ? -19.021 -10.132 1.446   1.00 27.08 ?  665 HOH B O   1 
HETATM 6561 O  O   . HOH J 5 .   ? -23.997 0.508   15.497  1.00 28.50 ?  666 HOH B O   1 
HETATM 6562 O  O   . HOH J 5 .   ? -24.157 0.949   2.833   1.00 29.88 ?  667 HOH B O   1 
HETATM 6563 O  O   . HOH J 5 .   ? -36.118 -14.396 -14.961 1.00 31.46 ?  668 HOH B O   1 
HETATM 6564 O  O   . HOH J 5 .   ? -38.300 -26.082 13.666  1.00 29.55 ?  669 HOH B O   1 
HETATM 6565 O  O   . HOH J 5 .   ? -45.200 -21.835 -13.711 1.00 37.02 ?  670 HOH B O   1 
HETATM 6566 O  O   . HOH J 5 .   ? -23.114 -5.757  12.602  1.00 30.44 ?  671 HOH B O   1 
HETATM 6567 O  O   . HOH J 5 .   ? -25.922 -3.904  20.017  1.00 27.31 ?  672 HOH B O   1 
HETATM 6568 O  O   . HOH J 5 .   ? -36.441 3.018   11.138  1.00 25.46 ?  673 HOH B O   1 
HETATM 6569 O  O   . HOH J 5 .   ? -43.012 -21.467 -9.400  1.00 29.40 ?  674 HOH B O   1 
HETATM 6570 O  O   . HOH J 5 .   ? -25.345 -21.555 -9.770  1.00 26.90 ?  675 HOH B O   1 
HETATM 6571 O  O   . HOH J 5 .   ? -14.392 -6.924  8.933   1.00 41.67 ?  676 HOH B O   1 
HETATM 6572 O  O   . HOH J 5 .   ? -3.155  -22.671 8.879   1.00 46.64 ?  677 HOH B O   1 
HETATM 6573 O  O   . HOH J 5 .   ? -18.131 -29.862 -7.440  1.00 28.12 ?  678 HOH B O   1 
HETATM 6574 O  O   . HOH J 5 .   ? -39.085 -29.301 -3.588  1.00 27.67 ?  679 HOH B O   1 
HETATM 6575 O  O   . HOH J 5 .   ? -27.330 -28.431 21.651  1.00 36.03 ?  680 HOH B O   1 
HETATM 6576 O  O   . HOH J 5 .   ? -43.312 -22.869 -6.875  1.00 30.86 ?  681 HOH B O   1 
HETATM 6577 O  O   . HOH J 5 .   ? -30.000 -28.705 -3.758  1.00 29.62 ?  682 HOH B O   1 
HETATM 6578 O  O   . HOH J 5 .   ? -24.011 -30.525 -1.610  1.00 39.05 ?  683 HOH B O   1 
HETATM 6579 O  O   . HOH J 5 .   ? -22.806 3.329   26.982  1.00 32.48 ?  684 HOH B O   1 
HETATM 6580 O  O   . HOH J 5 .   ? -55.257 -7.738  18.296  1.00 43.45 ?  685 HOH B O   1 
HETATM 6581 O  O   . HOH J 5 .   ? -24.166 -19.174 -7.314  1.00 24.63 ?  686 HOH B O   1 
HETATM 6582 O  O   . HOH J 5 .   ? -21.531 1.307   -12.906 1.00 27.09 ?  687 HOH B O   1 
HETATM 6583 O  O   . HOH J 5 .   ? -41.734 0.742   17.150  1.00 22.09 ?  688 HOH B O   1 
HETATM 6584 O  O   . HOH J 5 .   ? -32.552 -30.078 0.054   1.00 34.28 ?  689 HOH B O   1 
HETATM 6585 O  O   . HOH J 5 .   ? -45.439 -3.257  -14.447 1.00 29.10 ?  690 HOH B O   1 
HETATM 6586 O  O   . HOH J 5 .   ? -24.718 -19.428 4.737   1.00 24.59 ?  691 HOH B O   1 
HETATM 6587 O  O   . HOH J 5 .   ? -49.929 -3.282  13.422  1.00 34.34 ?  692 HOH B O   1 
HETATM 6588 O  O   . HOH J 5 .   ? -41.902 3.032   6.951   1.00 40.90 ?  693 HOH B O   1 
HETATM 6589 O  O   . HOH J 5 .   ? -41.971 1.754   -15.825 1.00 29.77 ?  694 HOH B O   1 
HETATM 6590 O  O   . HOH J 5 .   ? -46.310 -3.345  -2.806  1.00 24.95 ?  695 HOH B O   1 
HETATM 6591 O  O   . HOH J 5 .   ? -23.889 -33.275 8.693   1.00 35.38 ?  696 HOH B O   1 
HETATM 6592 O  O   . HOH J 5 .   ? -26.440 2.348   4.348   1.00 24.92 ?  697 HOH B O   1 
HETATM 6593 O  O   . HOH J 5 .   ? -20.694 -4.240  24.894  1.00 41.05 ?  698 HOH B O   1 
HETATM 6594 O  O   . HOH J 5 .   ? -31.981 -34.248 -5.578  1.00 42.81 ?  699 HOH B O   1 
HETATM 6595 O  O   . HOH J 5 .   ? -8.709  -20.228 25.792  1.00 44.12 ?  700 HOH B O   1 
HETATM 6596 O  O   . HOH J 5 .   ? -17.640 -20.994 -9.337  1.00 33.86 ?  701 HOH B O   1 
HETATM 6597 O  O   . HOH J 5 .   ? -25.516 -5.582  5.294   1.00 20.11 ?  702 HOH B O   1 
HETATM 6598 O  O   . HOH J 5 .   ? -36.443 -3.770  9.046   1.00 36.91 ?  703 HOH B O   1 
HETATM 6599 O  O   . HOH J 5 .   ? -43.669 -0.916  28.473  1.00 40.71 ?  704 HOH B O   1 
HETATM 6600 O  O   . HOH J 5 .   ? -28.432 -16.271 18.741  1.00 33.60 ?  705 HOH B O   1 
HETATM 6601 O  O   . HOH J 5 .   ? -15.532 -5.582  12.087  1.00 37.63 ?  706 HOH B O   1 
HETATM 6602 O  O   . HOH J 5 .   ? -29.347 -0.478  -2.306  1.00 21.10 ?  707 HOH B O   1 
HETATM 6603 O  O   . HOH J 5 .   ? -15.660 -21.836 -3.315  1.00 33.83 ?  708 HOH B O   1 
HETATM 6604 O  O   . HOH J 5 .   ? -44.554 2.984   -15.015 1.00 38.88 ?  709 HOH B O   1 
HETATM 6605 O  O   . HOH J 5 .   ? -50.165 0.909   -7.475  1.00 41.69 ?  710 HOH B O   1 
HETATM 6606 O  O   . HOH J 5 .   ? -28.345 -14.273 20.628  1.00 32.19 ?  711 HOH B O   1 
HETATM 6607 O  O   . HOH J 5 .   ? -30.828 -0.255  11.586  1.00 26.62 ?  712 HOH B O   1 
HETATM 6608 O  O   . HOH J 5 .   ? -22.403 -8.439  13.387  1.00 26.67 ?  713 HOH B O   1 
HETATM 6609 O  O   . HOH J 5 .   ? -30.013 -25.648 9.965   1.00 28.52 ?  714 HOH B O   1 
HETATM 6610 O  O   . HOH J 5 .   ? -22.729 -16.456 11.127  1.00 25.58 ?  715 HOH B O   1 
HETATM 6611 O  O   . HOH J 5 .   ? -23.465 3.728   22.893  1.00 35.77 ?  716 HOH B O   1 
HETATM 6612 O  O   . HOH J 5 .   ? -24.556 -4.844  26.853  1.00 37.49 ?  717 HOH B O   1 
HETATM 6613 O  O   . HOH J 5 .   ? -44.699 -24.018 -0.958  1.00 32.84 ?  718 HOH B O   1 
HETATM 6614 O  O   . HOH J 5 .   ? -42.227 -23.307 12.003  1.00 32.74 ?  719 HOH B O   1 
HETATM 6615 O  O   . HOH J 5 .   ? -41.809 -3.787  -17.998 1.00 32.75 ?  720 HOH B O   1 
HETATM 6616 O  O   . HOH J 5 .   ? -40.584 3.539   25.934  1.00 28.59 ?  721 HOH B O   1 
HETATM 6617 O  O   . HOH J 5 .   ? -28.100 -0.901  24.296  1.00 29.77 ?  722 HOH B O   1 
HETATM 6618 O  O   . HOH J 5 .   ? -52.567 -14.306 -11.257 1.00 43.94 ?  723 HOH B O   1 
HETATM 6619 O  O   . HOH J 5 .   ? -24.310 -24.660 21.837  1.00 32.75 ?  724 HOH B O   1 
HETATM 6620 O  O   . HOH J 5 .   ? -22.541 -11.299 -6.783  1.00 34.98 ?  725 HOH B O   1 
HETATM 6621 O  O   . HOH J 5 .   ? -20.841 -9.354  15.794  1.00 30.63 ?  726 HOH B O   1 
HETATM 6622 O  O   . HOH J 5 .   ? -31.694 -28.066 -1.533  1.00 28.49 ?  727 HOH B O   1 
HETATM 6623 O  O   . HOH J 5 .   ? -30.730 1.355   26.620  1.00 25.81 ?  728 HOH B O   1 
HETATM 6624 O  O   . HOH J 5 .   ? -26.708 -13.502 22.729  1.00 32.50 ?  729 HOH B O   1 
HETATM 6625 O  O   . HOH J 5 .   ? -51.400 -4.908  -11.326 1.00 38.65 ?  730 HOH B O   1 
HETATM 6626 O  O   . HOH J 5 .   ? -39.062 -2.576  19.392  1.00 28.64 ?  731 HOH B O   1 
HETATM 6627 O  O   . HOH J 5 .   ? -27.433 -23.209 28.451  1.00 48.33 ?  732 HOH B O   1 
HETATM 6628 O  O   . HOH J 5 .   ? -32.226 -13.941 8.726   1.00 25.36 ?  733 HOH B O   1 
HETATM 6629 O  O   . HOH J 5 .   ? -51.858 2.059   27.432  1.00 48.81 ?  734 HOH B O   1 
HETATM 6630 O  O   . HOH J 5 .   ? -48.002 1.046   9.181   1.00 32.66 ?  735 HOH B O   1 
HETATM 6631 O  O   . HOH J 5 .   ? -29.882 -25.466 -9.756  1.00 27.39 ?  736 HOH B O   1 
HETATM 6632 O  O   . HOH J 5 .   ? -56.285 -6.387  20.507  1.00 42.79 ?  737 HOH B O   1 
HETATM 6633 O  O   . HOH J 5 .   ? -18.215 -5.670  26.415  1.00 42.30 ?  738 HOH B O   1 
HETATM 6634 O  O   . HOH J 5 .   ? -25.002 -33.612 -5.137  1.00 38.06 ?  739 HOH B O   1 
HETATM 6635 O  O   . HOH J 5 .   ? -27.620 1.985   -4.125  1.00 28.17 ?  740 HOH B O   1 
HETATM 6636 O  O   . HOH J 5 .   ? -32.215 -11.602 -14.439 1.00 28.14 ?  741 HOH B O   1 
HETATM 6637 O  O   . HOH J 5 .   ? -27.785 -24.941 19.966  1.00 32.02 ?  742 HOH B O   1 
HETATM 6638 O  O   . HOH J 5 .   ? -36.853 -6.205  9.065   1.00 29.71 ?  743 HOH B O   1 
HETATM 6639 O  O   . HOH J 5 .   ? -29.854 -8.688  -11.905 1.00 25.74 ?  744 HOH B O   1 
HETATM 6640 O  O   . HOH J 5 .   ? -12.502 -17.190 30.609  1.00 44.36 ?  745 HOH B O   1 
HETATM 6641 O  O   . HOH J 5 .   ? -13.780 -14.809 29.341  1.00 42.15 ?  746 HOH B O   1 
HETATM 6642 O  O   . HOH J 5 .   ? -26.694 -25.487 22.700  1.00 44.50 ?  747 HOH B O   1 
HETATM 6643 O  O   . HOH J 5 .   ? -8.702  -12.163 3.878   1.00 44.30 ?  748 HOH B O   1 
HETATM 6644 O  O   . HOH J 5 .   ? -46.356 4.957   -13.256 1.00 32.27 ?  749 HOH B O   1 
HETATM 6645 O  O   . HOH J 5 .   ? -47.080 2.489   11.435  1.00 35.19 ?  750 HOH B O   1 
HETATM 6646 O  O   . HOH J 5 .   ? -38.387 -14.014 -12.110 1.00 22.81 ?  751 HOH B O   1 
HETATM 6647 O  O   . HOH J 5 .   ? -38.402 -16.682 5.153   1.00 21.38 ?  752 HOH B O   1 
HETATM 6648 O  O   . HOH J 5 .   ? -12.064 -27.711 10.811  1.00 39.56 ?  753 HOH B O   1 
HETATM 6649 O  O   . HOH J 5 .   ? -54.904 -6.205  9.550   1.00 45.25 ?  754 HOH B O   1 
HETATM 6650 O  O   . HOH J 5 .   ? -25.165 -5.048  9.287   1.00 23.43 ?  755 HOH B O   1 
HETATM 6651 O  O   . HOH J 5 .   ? -37.973 -6.453  -19.100 1.00 35.65 ?  756 HOH B O   1 
HETATM 6652 O  O   . HOH J 5 .   ? -45.056 -0.806  0.638   1.00 30.87 ?  757 HOH B O   1 
HETATM 6653 O  O   . HOH J 5 .   ? -27.948 -11.425 19.725  1.00 32.85 ?  758 HOH B O   1 
HETATM 6654 O  O   . HOH J 5 .   ? -39.643 2.672   17.291  1.00 27.00 ?  759 HOH B O   1 
HETATM 6655 O  O   . HOH J 5 .   ? -24.818 -31.723 24.601  1.00 45.35 ?  760 HOH B O   1 
HETATM 6656 O  O   . HOH J 5 .   ? -19.926 -11.069 10.090  1.00 34.73 ?  761 HOH B O   1 
HETATM 6657 O  O   . HOH J 5 .   ? -6.283  -17.879 17.042  1.00 44.24 ?  762 HOH B O   1 
HETATM 6658 O  O   . HOH J 5 .   ? -22.029 -1.171  5.176   1.00 32.51 ?  763 HOH B O   1 
HETATM 6659 O  O   . HOH J 5 .   ? -35.203 -13.433 -12.445 1.00 23.63 ?  764 HOH B O   1 
HETATM 6660 O  O   . HOH J 5 .   ? -35.325 -15.314 14.287  1.00 31.35 ?  765 HOH B O   1 
HETATM 6661 O  O   . HOH J 5 .   ? -23.847 2.443   -3.296  1.00 26.77 ?  766 HOH B O   1 
HETATM 6662 O  O   . HOH J 5 .   ? -27.293 -11.415 -14.209 1.00 40.12 ?  767 HOH B O   1 
HETATM 6663 O  O   . HOH J 5 .   ? -33.443 0.240   4.855   1.00 27.32 ?  768 HOH B O   1 
HETATM 6664 O  O   . HOH J 5 .   ? -41.472 -9.254  -16.029 1.00 23.61 ?  769 HOH B O   1 
HETATM 6665 O  O   . HOH J 5 .   ? -21.270 -31.911 19.855  1.00 35.16 ?  770 HOH B O   1 
HETATM 6666 O  O   . HOH J 5 .   ? -14.431 -10.322 0.538   1.00 37.53 ?  771 HOH B O   1 
HETATM 6667 O  O   . HOH J 5 .   ? -53.092 -4.952  -4.961  1.00 38.03 ?  772 HOH B O   1 
HETATM 6668 O  O   . HOH J 5 .   ? -46.709 -7.343  33.978  1.00 45.57 ?  773 HOH B O   1 
HETATM 6669 O  O   . HOH J 5 .   ? -29.864 -3.810  -15.073 1.00 37.93 ?  774 HOH B O   1 
HETATM 6670 O  O   . HOH J 5 .   ? -16.014 -28.685 -4.609  1.00 31.95 ?  775 HOH B O   1 
HETATM 6671 O  O   . HOH J 5 .   ? -22.063 -19.387 -13.735 1.00 31.71 ?  776 HOH B O   1 
HETATM 6672 O  O   . HOH J 5 .   ? -34.737 -7.477  8.143   1.00 30.44 ?  777 HOH B O   1 
HETATM 6673 O  O   . HOH J 5 .   ? -34.437 3.787   1.991   1.00 32.27 ?  778 HOH B O   1 
HETATM 6674 O  O   . HOH J 5 .   ? -33.931 7.048   28.639  1.00 35.89 ?  779 HOH B O   1 
HETATM 6675 O  O   . HOH J 5 .   ? -8.991  -26.125 8.020   1.00 40.66 ?  780 HOH B O   1 
HETATM 6676 O  O   . HOH J 5 .   ? -9.553  -9.023  10.067  1.00 40.26 ?  781 HOH B O   1 
HETATM 6677 O  O   . HOH J 5 .   ? -14.623 -4.944  14.724  1.00 34.64 ?  782 HOH B O   1 
HETATM 6678 O  O   . HOH J 5 .   ? -37.937 -7.663  18.612  1.00 30.00 ?  783 HOH B O   1 
HETATM 6679 O  O   . HOH J 5 .   ? -12.852 -31.208 17.550  1.00 45.74 ?  784 HOH B O   1 
HETATM 6680 O  O   . HOH J 5 .   ? -41.776 -28.069 -2.633  1.00 30.34 ?  785 HOH B O   1 
HETATM 6681 O  O   . HOH J 5 .   ? -54.594 -7.064  -6.237  1.00 38.11 ?  786 HOH B O   1 
HETATM 6682 O  O   . HOH J 5 .   ? -41.171 1.292   8.348   1.00 39.56 ?  787 HOH B O   1 
HETATM 6683 O  O   . HOH J 5 .   ? -39.909 -1.073  6.863   1.00 35.26 ?  788 HOH B O   1 
HETATM 6684 O  O   . HOH J 5 .   ? -22.164 -15.979 -2.106  1.00 28.92 ?  789 HOH B O   1 
HETATM 6685 O  O   . HOH J 5 .   ? -18.360 -4.059  5.166   1.00 31.92 ?  790 HOH B O   1 
HETATM 6686 O  O   . HOH J 5 .   ? -40.791 0.933   -4.378  1.00 33.01 ?  791 HOH B O   1 
HETATM 6687 O  O   . HOH J 5 .   ? -45.021 -22.046 -2.803  1.00 32.66 ?  792 HOH B O   1 
HETATM 6688 O  O   . HOH J 5 .   ? -29.964 2.019   -3.367  1.00 23.27 ?  793 HOH B O   1 
HETATM 6689 O  O   . HOH J 5 .   ? -24.939 -7.167  -11.175 1.00 32.07 ?  794 HOH B O   1 
HETATM 6690 O  O   . HOH J 5 .   ? -42.512 -25.903 5.727   1.00 38.28 ?  795 HOH B O   1 
HETATM 6691 O  O   . HOH J 5 .   ? -25.557 -14.726 -7.407  1.00 47.89 ?  796 HOH B O   1 
HETATM 6692 O  O   . HOH J 5 .   ? -54.181 -10.897 -3.745  1.00 40.20 ?  797 HOH B O   1 
HETATM 6693 O  O   . HOH J 5 .   ? -48.950 3.604   13.190  1.00 38.66 ?  798 HOH B O   1 
HETATM 6694 O  O   . HOH J 5 .   ? -25.148 -14.221 -1.274  1.00 31.94 ?  799 HOH B O   1 
HETATM 6695 O  O   . HOH J 5 .   ? -28.099 -23.868 -10.588 1.00 34.99 ?  800 HOH B O   1 
HETATM 6696 O  O   . HOH J 5 .   ? -22.024 -1.179  27.442  1.00 33.98 ?  801 HOH B O   1 
HETATM 6697 O  O   . HOH J 5 .   ? -7.835  -23.351 14.426  1.00 40.11 ?  802 HOH B O   1 
HETATM 6698 O  O   . HOH J 5 .   ? -29.224 -18.292 7.674   1.00 26.86 ?  803 HOH B O   1 
HETATM 6699 O  O   . HOH J 5 .   ? -31.963 -25.006 -11.868 1.00 27.58 ?  804 HOH B O   1 
HETATM 6700 O  O   . HOH J 5 .   ? -44.963 -15.933 -15.687 1.00 37.29 ?  805 HOH B O   1 
HETATM 6701 O  O   . HOH J 5 .   ? -32.156 2.604   13.410  1.00 28.09 ?  806 HOH B O   1 
HETATM 6702 O  O   . HOH J 5 .   ? -15.645 -30.817 -2.429  1.00 41.81 ?  807 HOH B O   1 
HETATM 6703 O  O   . HOH J 5 .   ? -22.544 -0.989  0.912   1.00 25.82 ?  808 HOH B O   1 
HETATM 6704 O  O   . HOH J 5 .   ? -26.085 0.864   13.873  1.00 27.81 ?  809 HOH B O   1 
HETATM 6705 O  O   . HOH J 5 .   ? -20.031 -1.338  -10.350 1.00 39.11 ?  810 HOH B O   1 
HETATM 6706 O  O   . HOH J 5 .   ? -3.363  -33.227 20.235  1.00 45.46 ?  811 HOH B O   1 
HETATM 6707 O  O   . HOH J 5 .   ? -43.215 -29.197 -10.802 1.00 31.41 ?  812 HOH B O   1 
HETATM 6708 O  O   . HOH J 5 .   ? -21.505 -12.855 9.610   1.00 27.42 ?  813 HOH B O   1 
HETATM 6709 O  O   . HOH J 5 .   ? -37.198 -11.030 34.674  1.00 57.83 ?  814 HOH B O   1 
HETATM 6710 O  O   . HOH J 5 .   ? -47.019 -12.572 -15.349 1.00 39.62 ?  815 HOH B O   1 
HETATM 6711 O  O   . HOH J 5 .   ? -53.599 -9.558  10.692  1.00 36.15 ?  816 HOH B O   1 
HETATM 6712 O  O   . HOH J 5 .   ? -17.870 -34.226 14.146  1.00 45.53 ?  817 HOH B O   1 
HETATM 6713 O  O   . HOH J 5 .   ? -30.175 -16.826 -0.824  1.00 23.97 ?  818 HOH B O   1 
HETATM 6714 O  O   . HOH J 5 .   ? -30.650 -28.698 7.189   1.00 34.06 ?  819 HOH B O   1 
HETATM 6715 O  O   . HOH J 5 .   ? -36.645 -27.980 8.512   1.00 40.74 ?  820 HOH B O   1 
HETATM 6716 O  O   . HOH J 5 .   ? -51.771 -23.654 5.132   1.00 44.76 ?  821 HOH B O   1 
HETATM 6717 O  O   . HOH J 5 .   ? -13.488 -30.350 9.235   1.00 38.17 ?  822 HOH B O   1 
HETATM 6718 O  O   . HOH J 5 .   ? -22.592 -11.617 22.694  1.00 32.29 ?  823 HOH B O   1 
HETATM 6719 O  O   . HOH J 5 .   ? -22.712 -31.519 26.636  1.00 48.52 ?  824 HOH B O   1 
HETATM 6720 O  O   . HOH J 5 .   ? -41.034 2.271   -1.978  1.00 34.27 ?  825 HOH B O   1 
HETATM 6721 O  O   . HOH J 5 .   ? -12.801 -8.856  7.755   1.00 42.52 ?  826 HOH B O   1 
HETATM 6722 O  O   . HOH J 5 .   ? -56.135 -4.044  19.961  1.00 41.59 ?  827 HOH B O   1 
HETATM 6723 O  O   . HOH J 5 .   ? -26.394 -21.699 33.107  1.00 51.89 ?  828 HOH B O   1 
HETATM 6724 O  O   . HOH J 5 .   ? -33.348 -20.436 24.815  1.00 48.06 ?  829 HOH B O   1 
HETATM 6725 O  O   . HOH J 5 .   ? -57.772 -15.992 7.070   1.00 44.04 ?  830 HOH B O   1 
HETATM 6726 O  O   . HOH J 5 .   ? -42.653 0.735   -1.898  1.00 40.74 ?  831 HOH B O   1 
HETATM 6727 O  O   . HOH J 5 .   ? -49.540 0.372   4.200   1.00 47.86 ?  832 HOH B O   1 
HETATM 6728 O  O   . HOH J 5 .   ? -13.529 -10.368 3.291   1.00 36.27 ?  833 HOH B O   1 
HETATM 6729 O  O   . HOH J 5 .   ? -40.375 -25.898 12.612  1.00 29.49 ?  834 HOH B O   1 
HETATM 6730 O  O   . HOH J 5 .   ? -47.600 -10.152 -14.613 1.00 42.20 ?  835 HOH B O   1 
HETATM 6731 O  O   . HOH J 5 .   ? -19.711 -16.700 -2.844  1.00 32.43 ?  836 HOH B O   1 
HETATM 6732 O  O   . HOH J 5 .   ? -5.298  -24.091 12.756  1.00 45.37 ?  837 HOH B O   1 
HETATM 6733 O  O   . HOH J 5 .   ? -27.017 -25.539 27.907  1.00 52.35 ?  838 HOH B O   1 
HETATM 6734 O  O   . HOH J 5 .   ? -13.278 -27.088 33.129  1.00 44.15 ?  839 HOH B O   1 
HETATM 6735 O  O   . HOH J 5 .   ? -26.879 -14.750 0.046   1.00 30.09 ?  840 HOH B O   1 
HETATM 6736 O  O   . HOH J 5 .   ? -27.778 -3.079  -13.600 1.00 45.61 ?  841 HOH B O   1 
HETATM 6737 O  O   . HOH J 5 .   ? -24.638 -11.930 21.203  1.00 31.52 ?  842 HOH B O   1 
HETATM 6738 O  O   . HOH J 5 .   ? -23.740 -34.779 3.320   1.00 43.21 ?  843 HOH B O   1 
HETATM 6739 O  O   . HOH J 5 .   ? -12.267 -10.443 26.498  1.00 46.01 ?  844 HOH B O   1 
HETATM 6740 O  O   . HOH J 5 .   ? -26.540 6.556   23.936  1.00 33.14 ?  845 HOH B O   1 
HETATM 6741 O  O   . HOH J 5 .   ? -25.961 -38.551 -6.677  1.00 43.23 ?  846 HOH B O   1 
HETATM 6742 O  O   . HOH J 5 .   ? -20.864 -3.982  -2.328  1.00 32.74 ?  847 HOH B O   1 
HETATM 6743 O  O   . HOH J 5 .   ? -11.327 -26.895 8.228   1.00 43.77 ?  848 HOH B O   1 
HETATM 6744 O  O   . HOH J 5 .   ? -27.299 -5.700  -12.898 1.00 33.35 ?  849 HOH B O   1 
HETATM 6745 O  O   . HOH J 5 .   ? -11.814 -16.232 23.081  1.00 39.64 ?  850 HOH B O   1 
HETATM 6746 O  O   . HOH J 5 .   ? -28.924 -22.331 27.032  1.00 38.30 ?  851 HOH B O   1 
HETATM 6747 O  O   . HOH J 5 .   ? -29.517 -10.315 -14.655 1.00 41.97 ?  852 HOH B O   1 
HETATM 6748 O  O   . HOH J 5 .   ? -47.925 5.238   -7.430  1.00 37.68 ?  853 HOH B O   1 
HETATM 6749 O  O   . HOH J 5 .   ? -24.380 -32.991 -2.062  1.00 37.80 ?  854 HOH B O   1 
HETATM 6750 O  O   . HOH J 5 .   ? -28.345 -28.866 12.235  1.00 42.22 ?  855 HOH B O   1 
HETATM 6751 O  O   . HOH J 5 .   ? -12.970 -30.504 0.827   1.00 50.81 ?  856 HOH B O   1 
HETATM 6752 O  O   . HOH J 5 .   ? -43.081 2.813   27.488  1.00 39.97 ?  857 HOH B O   1 
HETATM 6753 O  O   . HOH J 5 .   ? -36.617 1.422   -6.777  1.00 31.55 ?  858 HOH B O   1 
HETATM 6754 O  O   . HOH J 5 .   ? -32.802 -27.768 8.542   1.00 36.90 ?  859 HOH B O   1 
HETATM 6755 O  O   . HOH J 5 .   ? -56.368 -8.821  13.864  1.00 50.65 ?  860 HOH B O   1 
HETATM 6756 O  O   . HOH J 5 .   ? -19.578 -31.850 -7.826  1.00 49.19 ?  861 HOH B O   1 
HETATM 6757 O  O   . HOH J 5 .   ? -41.472 4.661   14.646  1.00 37.12 ?  862 HOH B O   1 
HETATM 6758 O  O   . HOH J 5 .   ? -19.162 -33.887 0.038   1.00 40.74 ?  863 HOH B O   1 
HETATM 6759 O  O   . HOH J 5 .   ? -47.266 -28.505 25.139  1.00 55.83 ?  864 HOH B O   1 
HETATM 6760 O  O   . HOH J 5 .   ? -54.907 -12.137 10.197  1.00 42.50 ?  865 HOH B O   1 
HETATM 6761 O  O   . HOH J 5 .   ? -41.418 -19.518 35.172  1.00 51.62 ?  866 HOH B O   1 
HETATM 6762 O  O   . HOH J 5 .   ? -26.598 -7.835  31.593  1.00 48.93 ?  867 HOH B O   1 
HETATM 6763 O  O   . HOH J 5 .   ? -16.454 -19.981 -1.357  1.00 35.70 ?  868 HOH B O   1 
HETATM 6764 O  O   . HOH J 5 .   ? -5.489  -20.283 15.274  1.00 46.94 ?  869 HOH B O   1 
HETATM 6765 O  O   . HOH J 5 .   ? -23.011 -20.082 -9.729  1.00 29.38 ?  870 HOH B O   1 
HETATM 6766 O  O   . HOH J 5 .   ? -45.812 -2.357  29.140  1.00 43.94 ?  871 HOH B O   1 
HETATM 6767 O  O   . HOH J 5 .   ? -45.609 -6.378  -15.769 1.00 38.61 ?  872 HOH B O   1 
HETATM 6768 O  O   . HOH J 5 .   ? -39.294 2.650   5.414   1.00 34.04 ?  873 HOH B O   1 
HETATM 6769 O  O   . HOH J 5 .   ? -57.320 -19.133 21.629  1.00 52.89 ?  874 HOH B O   1 
HETATM 6770 O  O   . HOH J 5 .   ? -13.402 -31.162 -1.282  1.00 43.92 ?  875 HOH B O   1 
HETATM 6771 O  O   . HOH J 5 .   ? -48.147 2.909   15.907  1.00 30.85 ?  876 HOH B O   1 
HETATM 6772 O  O   . HOH J 5 .   ? -38.633 -4.958  17.844  1.00 28.97 ?  877 HOH B O   1 
HETATM 6773 O  O   . HOH J 5 .   ? -45.591 -23.823 -6.028  1.00 39.15 ?  878 HOH B O   1 
HETATM 6774 O  O   . HOH J 5 .   ? -17.090 -25.674 -9.476  1.00 40.86 ?  879 HOH B O   1 
HETATM 6775 O  O   . HOH J 5 .   ? -48.789 2.394   6.788   1.00 39.03 ?  880 HOH B O   1 
HETATM 6776 O  O   . HOH J 5 .   ? -16.932 -9.052  0.461   1.00 31.51 ?  881 HOH B O   1 
HETATM 6777 O  O   . HOH J 5 .   ? -39.751 -25.453 35.087  1.00 64.24 ?  882 HOH B O   1 
HETATM 6778 O  O   . HOH J 5 .   ? -16.989 -33.737 -1.010  1.00 43.01 ?  883 HOH B O   1 
HETATM 6779 O  O   . HOH J 5 .   ? -42.318 4.762   11.680  1.00 35.12 ?  884 HOH B O   1 
HETATM 6780 O  O   . HOH J 5 .   ? -40.453 -27.850 7.006   1.00 37.82 ?  885 HOH B O   1 
HETATM 6781 O  O   . HOH J 5 .   ? -48.419 5.256   -12.278 1.00 50.33 ?  886 HOH B O   1 
HETATM 6782 O  O   . HOH J 5 .   ? -47.932 -5.280  32.864  1.00 52.25 ?  887 HOH B O   1 
HETATM 6783 O  O   . HOH J 5 .   ? -12.118 -13.434 27.216  1.00 47.47 ?  888 HOH B O   1 
HETATM 6784 O  O   . HOH J 5 .   ? -43.656 -6.158  -17.760 1.00 40.15 ?  889 HOH B O   1 
HETATM 6785 O  O   . HOH J 5 .   ? -21.972 1.568   5.744   1.00 36.51 ?  890 HOH B O   1 
HETATM 6786 O  O   . HOH J 5 .   ? -22.452 -3.901  26.877  1.00 38.30 ?  891 HOH B O   1 
HETATM 6787 O  O   . HOH J 5 .   ? -4.685  -17.585 19.242  1.00 48.34 ?  892 HOH B O   1 
HETATM 6788 O  O   . HOH J 5 .   ? -7.962  -13.879 2.082   1.00 49.48 ?  893 HOH B O   1 
HETATM 6789 O  O   . HOH J 5 .   ? -10.439 -9.569  3.478   1.00 44.51 ?  894 HOH B O   1 
HETATM 6790 O  O   . HOH J 5 .   ? -34.503 4.083   12.996  1.00 22.42 ?  895 HOH B O   1 
HETATM 6791 O  O   . HOH J 5 .   ? -47.713 -21.016 -3.356  1.00 34.60 ?  896 HOH B O   1 
HETATM 6792 O  O   . HOH J 5 .   ? -33.601 0.115   31.742  1.00 48.14 ?  897 HOH B O   1 
HETATM 6793 O  O   . HOH J 5 .   ? -14.576 -26.147 -3.948  1.00 41.33 ?  898 HOH B O   1 
HETATM 6794 O  O   . HOH J 5 .   ? -15.511 -21.117 -11.318 1.00 49.45 ?  899 HOH B O   1 
HETATM 6795 O  O   . HOH J 5 .   ? -10.585 -8.430  6.000   1.00 43.07 ?  900 HOH B O   1 
HETATM 6796 O  O   . HOH J 5 .   ? -17.014 -17.567 -2.935  1.00 32.75 ?  901 HOH B O   1 
HETATM 6797 O  O   . HOH J 5 .   ? -47.728 -1.883  1.819   1.00 37.99 ?  902 HOH B O   1 
HETATM 6798 O  O   . HOH J 5 .   ? -21.836 1.939   2.916   1.00 35.00 ?  903 HOH B O   1 
HETATM 6799 O  O   . HOH J 5 .   ? -23.704 6.844   24.160  1.00 54.88 ?  904 HOH B O   1 
HETATM 6800 O  O   . HOH J 5 .   ? -25.032 -6.523  29.768  1.00 46.02 ?  905 HOH B O   1 
HETATM 6801 O  O   . HOH J 5 .   ? -27.236 -2.766  30.007  1.00 51.37 ?  906 HOH B O   1 
HETATM 6802 O  O   . HOH J 5 .   ? -44.868 -2.196  -16.781 1.00 46.84 ?  907 HOH B O   1 
HETATM 6803 O  O   . HOH J 5 .   ? -25.259 -3.758  29.319  1.00 49.88 ?  908 HOH B O   1 
HETATM 6804 O  O   . HOH J 5 .   ? -20.324 -5.372  29.110  1.00 53.83 ?  909 HOH B O   1 
HETATM 6805 O  O   . HOH J 5 .   ? -49.955 5.201   -10.690 1.00 49.42 ?  910 HOH B O   1 
HETATM 6806 O  O   . HOH J 5 .   ? -19.397 -1.303  5.550   1.00 37.86 ?  911 HOH B O   1 
HETATM 6807 O  O   . HOH J 5 .   ? -12.564 -8.554  -0.436  1.00 50.50 ?  912 HOH B O   1 
HETATM 6808 O  O   . HOH J 5 .   ? -58.740 -7.702  12.793  1.00 50.67 ?  913 HOH B O   1 
HETATM 6809 O  O   . HOH J 5 .   ? -10.306 -9.345  0.687   1.00 45.85 ?  914 HOH B O   1 
HETATM 6810 O  O   . HOH J 5 .   ? -31.398 -1.070  30.641  1.00 51.51 ?  915 HOH B O   1 
HETATM 6811 O  O   . HOH J 5 .   ? -43.461 5.880   27.962  1.00 47.39 ?  916 HOH B O   1 
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