data_8YYP
# 
_entry.id   8YYP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8YYP         pdb_00008yyp 10.2210/pdb8yyp/pdb 
WWPDB D_1300046649 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YYP 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-04 
_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 ADENINE                                                      135.127   2   ? ? ? ? 
3 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                            616.487   2   ? ? ? ? 
4 non-polymer nat '(3S,6S)-3,6-bis[(1H-indol-3-yl)methyl]piperazine-2,5-dione' 372.420   1   ? ? ? ? 
5 water       nat water                                                        18.015    201 ? ? ? ? 
# 
_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 ADENINE                                                      ADE 
3 'PROTOPORPHYRIN IX CONTAINING FE'                            HEM 
4 '(3S,6S)-3,6-bis[(1H-indol-3-yl)methyl]piperazine-2,5-dione' UYM 
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 
ADE non-polymer         . ADENINE                                                      ?    'C5 H5 N5'         135.127 
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  
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  ?   ?   ?   A . n 
A 1 99  ASN 99  99  ?   ?   ?   A . n 
A 1 100 MET 100 100 ?   ?   ?   A . n 
A 1 101 GLY 101 101 ?   ?   ?   A . n 
A 1 102 ASN 102 102 ?   ?   ?   A . n 
A 1 103 ILE 103 103 ?   ?   ?   A . n 
A 1 104 ASN 104 104 ?   ?   ?   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 229 229 229 PRO PRO 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 ADE 1   501 501 ADE ADF A . 
D 3 HEM 1   502 502 HEM DRG A . 
E 2 ADE 1   501 501 ADE ADF B . 
F 3 HEM 1   502 502 HEM DRG B . 
G 4 UYM 1   503 504 UYM CWW B . 
H 5 HOH 1   601 178 HOH HOH A . 
H 5 HOH 2   602 173 HOH HOH A . 
H 5 HOH 3   603 132 HOH HOH A . 
H 5 HOH 4   604 133 HOH HOH A . 
H 5 HOH 5   605 45  HOH HOH A . 
H 5 HOH 6   606 39  HOH HOH A . 
H 5 HOH 7   607 146 HOH HOH A . 
H 5 HOH 8   608 105 HOH HOH A . 
H 5 HOH 9   609 193 HOH HOH A . 
H 5 HOH 10  610 151 HOH HOH A . 
H 5 HOH 11  611 166 HOH HOH A . 
H 5 HOH 12  612 21  HOH HOH A . 
H 5 HOH 13  613 65  HOH HOH A . 
H 5 HOH 14  614 55  HOH HOH A . 
H 5 HOH 15  615 16  HOH HOH A . 
H 5 HOH 16  616 74  HOH HOH A . 
H 5 HOH 17  617 56  HOH HOH A . 
H 5 HOH 18  618 128 HOH HOH A . 
H 5 HOH 19  619 60  HOH HOH A . 
H 5 HOH 20  620 112 HOH HOH A . 
H 5 HOH 21  621 54  HOH HOH A . 
H 5 HOH 22  622 85  HOH HOH A . 
H 5 HOH 23  623 196 HOH HOH A . 
H 5 HOH 24  624 47  HOH HOH A . 
H 5 HOH 25  625 184 HOH HOH A . 
H 5 HOH 26  626 191 HOH HOH A . 
H 5 HOH 27  627 198 HOH HOH A . 
H 5 HOH 28  628 19  HOH HOH A . 
H 5 HOH 29  629 136 HOH HOH A . 
H 5 HOH 30  630 165 HOH HOH A . 
H 5 HOH 31  631 125 HOH HOH A . 
H 5 HOH 32  632 64  HOH HOH A . 
H 5 HOH 33  633 189 HOH HOH A . 
H 5 HOH 34  634 26  HOH HOH A . 
H 5 HOH 35  635 49  HOH HOH A . 
H 5 HOH 36  636 11  HOH HOH A . 
H 5 HOH 37  637 37  HOH HOH A . 
H 5 HOH 38  638 180 HOH HOH A . 
H 5 HOH 39  639 86  HOH HOH A . 
H 5 HOH 40  640 154 HOH HOH A . 
H 5 HOH 41  641 9   HOH HOH A . 
H 5 HOH 42  642 8   HOH HOH A . 
H 5 HOH 43  643 13  HOH HOH A . 
H 5 HOH 44  644 28  HOH HOH A . 
H 5 HOH 45  645 3   HOH HOH A . 
H 5 HOH 46  646 195 HOH HOH A . 
H 5 HOH 47  647 163 HOH HOH A . 
H 5 HOH 48  648 91  HOH HOH A . 
H 5 HOH 49  649 89  HOH HOH A . 
H 5 HOH 50  650 135 HOH HOH A . 
H 5 HOH 51  651 187 HOH HOH A . 
H 5 HOH 52  652 186 HOH HOH A . 
H 5 HOH 53  653 94  HOH HOH A . 
H 5 HOH 54  654 36  HOH HOH A . 
H 5 HOH 55  655 70  HOH HOH A . 
H 5 HOH 56  656 68  HOH HOH A . 
H 5 HOH 57  657 90  HOH HOH A . 
H 5 HOH 58  658 161 HOH HOH A . 
H 5 HOH 59  659 134 HOH HOH A . 
H 5 HOH 60  660 62  HOH HOH A . 
H 5 HOH 61  661 121 HOH HOH A . 
H 5 HOH 62  662 41  HOH HOH A . 
H 5 HOH 63  663 115 HOH HOH A . 
H 5 HOH 64  664 174 HOH HOH A . 
H 5 HOH 65  665 59  HOH HOH A . 
H 5 HOH 66  666 131 HOH HOH A . 
H 5 HOH 67  667 48  HOH HOH A . 
H 5 HOH 68  668 43  HOH HOH A . 
H 5 HOH 69  669 102 HOH HOH A . 
H 5 HOH 70  670 172 HOH HOH A . 
H 5 HOH 71  671 14  HOH HOH A . 
H 5 HOH 72  672 181 HOH HOH A . 
H 5 HOH 73  673 162 HOH HOH A . 
H 5 HOH 74  674 30  HOH HOH A . 
H 5 HOH 75  675 156 HOH HOH A . 
H 5 HOH 76  676 153 HOH HOH A . 
H 5 HOH 77  677 188 HOH HOH A . 
H 5 HOH 78  678 99  HOH HOH A . 
H 5 HOH 79  679 177 HOH HOH A . 
H 5 HOH 80  680 144 HOH HOH A . 
H 5 HOH 81  681 168 HOH HOH A . 
H 5 HOH 82  682 110 HOH HOH A . 
H 5 HOH 83  683 182 HOH HOH A . 
H 5 HOH 84  684 97  HOH HOH A . 
H 5 HOH 85  685 87  HOH HOH A . 
H 5 HOH 86  686 175 HOH HOH A . 
H 5 HOH 87  687 185 HOH HOH A . 
H 5 HOH 88  688 117 HOH HOH A . 
I 5 HOH 1   601 29  HOH HOH B . 
I 5 HOH 2   602 5   HOH HOH B . 
I 5 HOH 3   603 199 HOH HOH B . 
I 5 HOH 4   604 22  HOH HOH B . 
I 5 HOH 5   605 152 HOH HOH B . 
I 5 HOH 6   606 4   HOH HOH B . 
I 5 HOH 7   607 203 HOH HOH B . 
I 5 HOH 8   608 126 HOH HOH B . 
I 5 HOH 9   609 17  HOH HOH B . 
I 5 HOH 10  610 52  HOH HOH B . 
I 5 HOH 11  611 108 HOH HOH B . 
I 5 HOH 12  612 92  HOH HOH B . 
I 5 HOH 13  613 33  HOH HOH B . 
I 5 HOH 14  614 61  HOH HOH B . 
I 5 HOH 15  615 130 HOH HOH B . 
I 5 HOH 16  616 109 HOH HOH B . 
I 5 HOH 17  617 83  HOH HOH B . 
I 5 HOH 18  618 111 HOH HOH B . 
I 5 HOH 19  619 76  HOH HOH B . 
I 5 HOH 20  620 32  HOH HOH B . 
I 5 HOH 21  621 129 HOH HOH B . 
I 5 HOH 22  622 53  HOH HOH B . 
I 5 HOH 23  623 7   HOH HOH B . 
I 5 HOH 24  624 24  HOH HOH B . 
I 5 HOH 25  625 25  HOH HOH B . 
I 5 HOH 26  626 150 HOH HOH B . 
I 5 HOH 27  627 98  HOH HOH B . 
I 5 HOH 28  628 44  HOH HOH B . 
I 5 HOH 29  629 114 HOH HOH B . 
I 5 HOH 30  630 82  HOH HOH B . 
I 5 HOH 31  631 127 HOH HOH B . 
I 5 HOH 32  632 194 HOH HOH B . 
I 5 HOH 33  633 167 HOH HOH B . 
I 5 HOH 34  634 158 HOH HOH B . 
I 5 HOH 35  635 202 HOH HOH B . 
I 5 HOH 36  636 164 HOH HOH B . 
I 5 HOH 37  637 73  HOH HOH B . 
I 5 HOH 38  638 104 HOH HOH B . 
I 5 HOH 39  639 171 HOH HOH B . 
I 5 HOH 40  640 79  HOH HOH B . 
I 5 HOH 41  641 23  HOH HOH B . 
I 5 HOH 42  642 100 HOH HOH B . 
I 5 HOH 43  643 18  HOH HOH B . 
I 5 HOH 44  644 2   HOH HOH B . 
I 5 HOH 45  645 20  HOH HOH B . 
I 5 HOH 46  646 160 HOH HOH B . 
I 5 HOH 47  647 42  HOH HOH B . 
I 5 HOH 48  648 31  HOH HOH B . 
I 5 HOH 49  649 95  HOH HOH B . 
I 5 HOH 50  650 57  HOH HOH B . 
I 5 HOH 51  651 183 HOH HOH B . 
I 5 HOH 52  652 1   HOH HOH B . 
I 5 HOH 53  653 80  HOH HOH B . 
I 5 HOH 54  654 103 HOH HOH B . 
I 5 HOH 55  655 142 HOH HOH B . 
I 5 HOH 56  656 15  HOH HOH B . 
I 5 HOH 57  657 141 HOH HOH B . 
I 5 HOH 58  658 190 HOH HOH B . 
I 5 HOH 59  659 35  HOH HOH B . 
I 5 HOH 60  660 170 HOH HOH B . 
I 5 HOH 61  661 116 HOH HOH B . 
I 5 HOH 62  662 124 HOH HOH B . 
I 5 HOH 63  663 139 HOH HOH B . 
I 5 HOH 64  664 147 HOH HOH B . 
I 5 HOH 65  665 10  HOH HOH B . 
I 5 HOH 66  666 93  HOH HOH B . 
I 5 HOH 67  667 78  HOH HOH B . 
I 5 HOH 68  668 119 HOH HOH B . 
I 5 HOH 69  669 72  HOH HOH B . 
I 5 HOH 70  670 12  HOH HOH B . 
I 5 HOH 71  671 84  HOH HOH B . 
I 5 HOH 72  672 40  HOH HOH B . 
I 5 HOH 73  673 123 HOH HOH B . 
I 5 HOH 74  674 69  HOH HOH B . 
I 5 HOH 75  675 81  HOH HOH B . 
I 5 HOH 76  676 46  HOH HOH B . 
I 5 HOH 77  677 137 HOH HOH B . 
I 5 HOH 78  678 145 HOH HOH B . 
I 5 HOH 79  679 71  HOH HOH B . 
I 5 HOH 80  680 50  HOH HOH B . 
I 5 HOH 81  681 179 HOH HOH B . 
I 5 HOH 82  682 58  HOH HOH B . 
I 5 HOH 83  683 51  HOH HOH B . 
I 5 HOH 84  684 27  HOH HOH B . 
I 5 HOH 85  685 140 HOH HOH B . 
I 5 HOH 86  686 63  HOH HOH B . 
I 5 HOH 87  687 67  HOH HOH B . 
I 5 HOH 88  688 149 HOH HOH B . 
I 5 HOH 89  689 66  HOH HOH B . 
I 5 HOH 90  690 155 HOH HOH B . 
I 5 HOH 91  691 148 HOH HOH B . 
I 5 HOH 92  692 34  HOH HOH B . 
I 5 HOH 93  693 77  HOH HOH B . 
I 5 HOH 94  694 96  HOH HOH B . 
I 5 HOH 95  695 159 HOH HOH B . 
I 5 HOH 96  696 169 HOH HOH B . 
I 5 HOH 97  697 201 HOH HOH B . 
I 5 HOH 98  698 101 HOH HOH B . 
I 5 HOH 99  699 113 HOH HOH B . 
I 5 HOH 100 700 38  HOH HOH B . 
I 5 HOH 101 701 157 HOH HOH B . 
I 5 HOH 102 702 192 HOH HOH B . 
I 5 HOH 103 703 120 HOH HOH B . 
I 5 HOH 104 704 122 HOH HOH B . 
I 5 HOH 105 705 88  HOH HOH B . 
I 5 HOH 106 706 200 HOH HOH B . 
I 5 HOH 107 707 197 HOH HOH B . 
I 5 HOH 108 708 143 HOH HOH B . 
I 5 HOH 109 709 176 HOH HOH B . 
I 5 HOH 110 710 106 HOH HOH B . 
I 5 HOH 111 711 138 HOH HOH B . 
I 5 HOH 112 712 75  HOH HOH B . 
I 5 HOH 113 713 107 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 ARG 27  ? CG  ? A ARG 27  CG  
2  1 Y 1 A ARG 27  ? CD  ? A ARG 27  CD  
3  1 Y 1 A ARG 27  ? NE  ? A ARG 27  NE  
4  1 Y 1 A ARG 27  ? CZ  ? A ARG 27  CZ  
5  1 Y 1 A ARG 27  ? NH1 ? A ARG 27  NH1 
6  1 Y 1 A ARG 27  ? NH2 ? A ARG 27  NH2 
7  1 Y 1 A ARG 40  ? CG  ? A ARG 40  CG  
8  1 Y 1 A ARG 40  ? CD  ? A ARG 40  CD  
9  1 Y 1 A ARG 40  ? NE  ? A ARG 40  NE  
10 1 Y 1 A ARG 40  ? CZ  ? A ARG 40  CZ  
11 1 Y 1 A ARG 40  ? NH1 ? A ARG 40  NH1 
12 1 Y 1 A ARG 40  ? NH2 ? A ARG 40  NH2 
13 1 Y 1 A ARG 122 ? CG  ? A ARG 122 CG  
14 1 Y 1 A ARG 122 ? CD  ? A ARG 122 CD  
15 1 Y 1 A ARG 122 ? NE  ? A ARG 122 NE  
16 1 Y 1 A ARG 122 ? CZ  ? A ARG 122 CZ  
17 1 Y 1 A ARG 122 ? NH1 ? A ARG 122 NH1 
18 1 Y 1 A ARG 122 ? NH2 ? A ARG 122 NH2 
19 1 Y 1 A ARG 174 ? CG  ? A ARG 174 CG  
20 1 Y 1 A ARG 174 ? CD  ? A ARG 174 CD  
21 1 Y 1 A ARG 174 ? NE  ? A ARG 174 NE  
22 1 Y 1 A ARG 174 ? CZ  ? A ARG 174 CZ  
23 1 Y 1 A ARG 174 ? NH1 ? A ARG 174 NH1 
24 1 Y 1 A ARG 174 ? NH2 ? A ARG 174 NH2 
25 1 Y 1 A ARG 207 ? CG  ? A ARG 207 CG  
26 1 Y 1 A ARG 207 ? CD  ? A ARG 207 CD  
27 1 Y 1 A ARG 207 ? NE  ? A ARG 207 NE  
28 1 Y 1 A ARG 207 ? CZ  ? A ARG 207 CZ  
29 1 Y 1 A ARG 207 ? NH1 ? A ARG 207 NH1 
30 1 Y 1 A ARG 207 ? NH2 ? A ARG 207 NH2 
31 1 Y 1 A ASP 211 ? CG  ? A ASP 211 CG  
32 1 Y 1 A ASP 211 ? OD1 ? A ASP 211 OD1 
33 1 Y 1 A ASP 211 ? OD2 ? A ASP 211 OD2 
34 1 Y 1 A GLU 213 ? CG  ? A GLU 213 CG  
35 1 Y 1 A GLU 213 ? CD  ? A GLU 213 CD  
36 1 Y 1 A GLU 213 ? OE1 ? A GLU 213 OE1 
37 1 Y 1 A GLU 213 ? OE2 ? A GLU 213 OE2 
38 1 Y 1 A ARG 277 ? CG  ? A ARG 277 CG  
39 1 Y 1 A ARG 277 ? CD  ? A ARG 277 CD  
40 1 Y 1 A ARG 277 ? NE  ? A ARG 277 NE  
41 1 Y 1 A ARG 277 ? CZ  ? A ARG 277 CZ  
42 1 Y 1 A ARG 277 ? NH1 ? A ARG 277 NH1 
43 1 Y 1 A ARG 277 ? NH2 ? A ARG 277 NH2 
44 1 Y 1 A GLU 327 ? CG  ? A GLU 327 CG  
45 1 Y 1 A GLU 327 ? CD  ? A GLU 327 CD  
46 1 Y 1 A GLU 327 ? OE1 ? A GLU 327 OE1 
47 1 Y 1 A GLU 327 ? OE2 ? A GLU 327 OE2 
48 1 Y 1 A ARG 341 ? CG  ? A ARG 341 CG  
49 1 Y 1 A ARG 341 ? CD  ? A ARG 341 CD  
50 1 Y 1 A ARG 341 ? NE  ? A ARG 341 NE  
51 1 Y 1 A ARG 341 ? CZ  ? A ARG 341 CZ  
52 1 Y 1 A ARG 341 ? NH1 ? A ARG 341 NH1 
53 1 Y 1 A ARG 341 ? NH2 ? A ARG 341 NH2 
54 1 Y 1 B LYS 77  ? CG  ? B LYS 77  CG  
55 1 Y 1 B LYS 77  ? CD  ? B LYS 77  CD  
56 1 Y 1 B LYS 77  ? CE  ? B LYS 77  CE  
57 1 Y 1 B LYS 77  ? NZ  ? B LYS 77  NZ  
58 1 Y 1 B ARG 174 ? CG  ? B ARG 174 CG  
59 1 Y 1 B ARG 174 ? CD  ? B ARG 174 CD  
60 1 Y 1 B ARG 174 ? NE  ? B ARG 174 NE  
61 1 Y 1 B ARG 174 ? CZ  ? B ARG 174 CZ  
62 1 Y 1 B ARG 174 ? NH1 ? B ARG 174 NH1 
63 1 Y 1 B ARG 174 ? NH2 ? B ARG 174 NH2 
64 1 Y 1 B PRO 229 ? CG  ? B PRO 229 CG  
65 1 Y 1 B PRO 229 ? CD  ? B PRO 229 CD  
# 
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        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0267 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                     8YYP 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.453 
_cell.length_a_esd                 ? 
_cell.length_b                     84.453 
_cell.length_b_esd                 ? 
_cell.length_c                     133.377 
_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                         8YYP 
_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                   8YYP 
_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             2.62 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.14 
_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                                       8YYP 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.6 
_reflns.d_resolution_low                               25.01 
_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                                     28724 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.87 
_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                          17.29 
_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                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1549 
_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                                    2.6 
_reflns_shell.d_res_low                                     2.693 
_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                             2865 
_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                               13.8 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.851 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.73 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.73 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.47 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               40.630 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.951 
_refine.correlation_coeff_Fo_to_Fc_free          0.922 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8YYP 
_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                            2.60 
_refine.ls_d_res_low                             25.01 
_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                     28724 
_refine.ls_number_reflns_R_free                  1439 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17102 
_refine.ls_R_factor_R_free                       0.2569 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2064 
_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                    MASK 
_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       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.931 
_refine.pdbx_overall_ESU_R_Free                  0.296 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_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                             10.111 
_refine.overall_SU_ML                            0.216 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.60 
_refine_hist.d_res_low                        25.01 
_refine_hist.number_atoms_solvent             201 
_refine_hist.number_atoms_total               6251 
_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        5916 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         134 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  0.013  6400  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.015  6104  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.637  1.646  8736  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.288  1.572  13992 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.350  5.000  786   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 30.552 19.896 386   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.057 15.000 998   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.462 15.000 68    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.073  0.200  798   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  7374  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1492  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.882  4.189  3150  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.882  4.189  3149  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.954  6.277  3934  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.953  6.276  3935  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.958  4.460  3250  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.957  4.461  3251  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.040  6.574  4803  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.636  49.376 7124  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 8.645  49.375 7090  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.600 
_refine_ls_shell.d_res_low                        2.668 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             110 
_refine_ls_shell.number_reflns_R_work             2013 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.204 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.296 
# 
_struct.entry_id                     8YYP 
_struct.title                        'Crystal structure of PtmB in complex with cyclo-(L-Trp-L-Trp) and Adenine' 
_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        8YYP 
_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 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8YYP 
_struct_ref.pdbx_db_accession          8YYP 
_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 8YYP A 1 ? 412 ? 8YYP 1 ? 412 ? 1 412 
2 1 8YYP B 1 ? 412 ? 8YYP 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)' 5690  ? 
1 MORE         -52   ? 
1 'SSA (A^2)'  30630 ? 
# 
_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 
# 
_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  ? VAL A 97  ? PRO A 93  VAL A 97  5 ? 5  
HELX_P HELX_P5  AA5 LEU A 108 ? LEU A 116 ? LEU A 108 LEU A 116 1 ? 9  
HELX_P HELX_P6  AA6 SER A 117 ? ARG A 122 ? SER A 117 ARG A 122 5 ? 6  
HELX_P HELX_P7  AA7 GLU A 123 ? GLY A 143 ? GLU A 123 GLY A 143 1 ? 21 
HELX_P HELX_P8  AA8 LEU A 148 ? PHE A 152 ? LEU A 148 PHE A 152 1 ? 5  
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 GLY A 192 ? ASN A 209 ? GLY A 192 ASN A 209 1 ? 18 
HELX_P HELX_P12 AB3 GLU A 216 ? LEU A 225 ? GLU A 216 LEU A 225 1 ? 10 
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  ? ASP B 71  ? SER B 61  ASP B 71  1 ? 11 
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  ? VAL B 97  ? PRO B 93  VAL B 97  5 ? 5  
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 ? SER B 117 ? LEU B 108 SER B 117 1 ? 10 
HELX_P HELX_P26 AC8 GLU B 123 ? GLY B 143 ? GLU B 123 GLY B 143 1 ? 21 
HELX_P HELX_P27 AC9 LEU B 148 ? PHE B 152 ? LEU B 148 PHE B 152 1 ? 5  
HELX_P HELX_P28 AD1 PHE B 152 ? GLY B 166 ? PHE B 152 GLY B 166 1 ? 15 
HELX_P HELX_P29 AD2 ASP B 171 ? PHE B 183 ? ASP B 171 PHE B 183 1 ? 13 
HELX_P HELX_P30 AD3 GLY B 192 ? ASN B 209 ? GLY B 192 ASN B 209 1 ? 18 
HELX_P HELX_P31 AD4 GLU B 216 ? ARG B 226 ? GLU B 216 ARG B 226 1 ? 11 
HELX_P HELX_P32 AD5 SER B 236 ? GLN B 269 ? SER B 236 GLN B 269 1 ? 34 
HELX_P HELX_P33 AD6 GLN B 269 ? GLU B 279 ? GLN B 269 GLU B 279 1 ? 11 
HELX_P HELX_P34 AD7 VAL B 282 ? ASN B 294 ? VAL B 282 ASN B 294 1 ? 13 
HELX_P HELX_P35 AD8 LEU B 325 ? TYR B 331 ? LEU B 325 TYR B 331 1 ? 7  
HELX_P HELX_P36 AD9 GLY B 356 ? PHE B 360 ? GLY B 356 PHE B 360 5 ? 5  
HELX_P HELX_P37 AE1 ALA B 363 ? LEU B 382 ? ALA B 363 LEU B 382 1 ? 20 
HELX_P HELX_P38 AE2 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   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 361 SG ? ? ? 1_555 D HEM . FE ? ? A CYS 361 A HEM 502 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc2 metalc ? ? B CYS 361 SG ? ? ? 1_555 F HEM . FE ? ? B CYS 361 B HEM 502 1_555 ? ? ? ? ? ? ? 2.430 ? ? 
# 
_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  SG ? A CYS 361 ? A CYS 361 ? 1_555 FE ? D HEM . ? A HEM 502 ? 1_555 NA ? D HEM . ? A HEM 502 ? 1_555 107.0 ? 
2  SG ? A CYS 361 ? A CYS 361 ? 1_555 FE ? D HEM . ? A HEM 502 ? 1_555 NB ? D HEM . ? A HEM 502 ? 1_555 101.2 ? 
3  NA ? D HEM .   ? A HEM 502 ? 1_555 FE ? D HEM . ? A HEM 502 ? 1_555 NB ? D HEM . ? A HEM 502 ? 1_555 83.4  ? 
4  SG ? A CYS 361 ? A CYS 361 ? 1_555 FE ? D HEM . ? A HEM 502 ? 1_555 NC ? D HEM . ? A HEM 502 ? 1_555 100.6 ? 
5  NA ? D HEM .   ? A HEM 502 ? 1_555 FE ? D HEM . ? A HEM 502 ? 1_555 NC ? D HEM . ? A HEM 502 ? 1_555 152.4 ? 
6  NB ? D HEM .   ? A HEM 502 ? 1_555 FE ? D HEM . ? A HEM 502 ? 1_555 NC ? D HEM . ? A HEM 502 ? 1_555 91.2  ? 
7  SG ? A CYS 361 ? A CYS 361 ? 1_555 FE ? D HEM . ? A HEM 502 ? 1_555 ND ? D HEM . ? A HEM 502 ? 1_555 103.9 ? 
8  NA ? D HEM .   ? A HEM 502 ? 1_555 FE ? D HEM . ? A HEM 502 ? 1_555 ND ? D HEM . ? A HEM 502 ? 1_555 87.3  ? 
9  NB ? D HEM .   ? A HEM 502 ? 1_555 FE ? D HEM . ? A HEM 502 ? 1_555 ND ? D HEM . ? A HEM 502 ? 1_555 154.8 ? 
10 NC ? D HEM .   ? A HEM 502 ? 1_555 FE ? D HEM . ? A HEM 502 ? 1_555 ND ? D HEM . ? A HEM 502 ? 1_555 86.3  ? 
11 SG ? B CYS 361 ? B CYS 361 ? 1_555 FE ? F HEM . ? B HEM 502 ? 1_555 NA ? F HEM . ? B HEM 502 ? 1_555 104.8 ? 
12 SG ? B CYS 361 ? B CYS 361 ? 1_555 FE ? F HEM . ? B HEM 502 ? 1_555 NB ? F HEM . ? B HEM 502 ? 1_555 95.4  ? 
13 NA ? F HEM .   ? B HEM 502 ? 1_555 FE ? F HEM . ? B HEM 502 ? 1_555 NB ? F HEM . ? B HEM 502 ? 1_555 92.2  ? 
14 SG ? B CYS 361 ? B CYS 361 ? 1_555 FE ? F HEM . ? B HEM 502 ? 1_555 NC ? F HEM . ? B HEM 502 ? 1_555 84.7  ? 
15 NA ? F HEM .   ? B HEM 502 ? 1_555 FE ? F HEM . ? B HEM 502 ? 1_555 NC ? F HEM . ? B HEM 502 ? 1_555 170.4 ? 
16 NB ? F HEM .   ? B HEM 502 ? 1_555 FE ? F HEM . ? B HEM 502 ? 1_555 NC ? F HEM . ? B HEM 502 ? 1_555 87.2  ? 
17 SG ? B CYS 361 ? B CYS 361 ? 1_555 FE ? F HEM . ? B HEM 502 ? 1_555 ND ? F HEM . ? B HEM 502 ? 1_555 98.8  ? 
18 NA ? F HEM .   ? B HEM 502 ? 1_555 FE ? F HEM . ? B HEM 502 ? 1_555 ND ? F HEM . ? B HEM 502 ? 1_555 91.7  ? 
19 NB ? F HEM .   ? B HEM 502 ? 1_555 FE ? F HEM . ? B HEM 502 ? 1_555 ND ? F HEM . ? B HEM 502 ? 1_555 163.8 ? 
20 NC ? F HEM .   ? B HEM 502 ? 1_555 FE ? F HEM . ? B HEM 502 ? 1_555 ND ? F HEM . ? B HEM 502 ? 1_555 86.3  ? 
# 
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 3.10  
2 PRO 144 A . ? PRO 144 A PRO 145 A ? PRO 145 A 1 -5.04 
3 PHE 23  B . ? PHE 23  B PRO 24  B ? PRO 24  B 1 6.57  
4 PRO 144 B . ? PRO 144 B PRO 145 B ? PRO 145 B 1 -2.57 
# 
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 TRP A 57  ? N TRP A 57  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 TRP B 57  ? N TRP B 57  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 VAL B 309 ? N VAL B 309 O ILE B 316 ? O ILE B 316 
# 
_pdbx_entry_details.entry_id                   8YYP 
_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 GLN A 43  ? ? -151.54 79.85   
2  1 GLN A 119 ? ? -97.79  35.47   
3  1 ARG A 122 ? ? 44.27   -81.45  
4  1 PHE A 152 ? ? -140.72 -62.64  
5  1 PRO A 212 ? ? -69.31  82.47   
6  1 GLU A 213 ? ? -28.00  134.94  
7  1 GLU A 216 ? ? 88.54   131.72  
8  1 ASP A 299 ? ? -117.28 -163.45 
9  1 ALA A 307 ? ? 178.45  159.96  
10 1 ASP A 345 ? ? -141.91 33.46   
11 1 ASN A 349 ? ? -160.66 72.85   
12 1 GLN B 43  ? ? -150.13 75.83   
13 1 ASN B 98  ? ? -104.90 46.91   
14 1 PHE B 152 ? ? -136.13 -68.47  
15 1 GLU B 216 ? ? 77.87   131.50  
# 
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 ASN 98  ? A ASN 98  
20 1 Y 1 A ASN 99  ? A ASN 99  
21 1 Y 1 A MET 100 ? A MET 100 
22 1 Y 1 A GLY 101 ? A GLY 101 
23 1 Y 1 A ASN 102 ? A ASN 102 
24 1 Y 1 A ILE 103 ? A ILE 103 
25 1 Y 1 A ASN 104 ? A ASN 104 
26 1 Y 1 A PRO 229 ? A PRO 229 
27 1 Y 1 A ASP 230 ? A ASP 230 
28 1 Y 1 A VAL 231 ? A VAL 231 
29 1 Y 1 A SER 232 ? A SER 232 
30 1 Y 1 A ASP 233 ? A ASP 233 
31 1 Y 1 A GLN 234 ? A GLN 234 
32 1 Y 1 B MET 1   ? B MET 1   
33 1 Y 1 B THR 2   ? B THR 2   
34 1 Y 1 B THR 3   ? B THR 3   
35 1 Y 1 B THR 4   ? B THR 4   
36 1 Y 1 B ALA 5   ? B ALA 5   
37 1 Y 1 B GLN 6   ? B GLN 6   
38 1 Y 1 B ARG 7   ? B ARG 7   
39 1 Y 1 B ASP 8   ? B ASP 8   
40 1 Y 1 B PRO 9   ? B PRO 9   
41 1 Y 1 B VAL 10  ? B VAL 10  
42 1 Y 1 B LEU 11  ? B LEU 11  
43 1 Y 1 B PRO 12  ? B PRO 12  
44 1 Y 1 B GLY 13  ? B GLY 13  
45 1 Y 1 B THR 14  ? B THR 14  
46 1 Y 1 B ALA 15  ? B ALA 15  
47 1 Y 1 B HIS 16  ? B HIS 16  
48 1 Y 1 B HIS 17  ? B HIS 17  
49 1 Y 1 B PRO 18  ? B PRO 18  
50 1 Y 1 B ASP 230 ? B ASP 230 
51 1 Y 1 B VAL 231 ? B VAL 231 
52 1 Y 1 B SER 232 ? B SER 232 
53 1 Y 1 B ASP 233 ? B ASP 233 
54 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 
ADE N9   N  Y N 1   
ADE C8   C  Y N 2   
ADE N7   N  Y N 3   
ADE C5   C  Y N 4   
ADE C6   C  Y N 5   
ADE N6   N  N N 6   
ADE N1   N  Y N 7   
ADE C2   C  Y N 8   
ADE N3   N  Y N 9   
ADE C4   C  Y N 10  
ADE HN9  H  N N 11  
ADE H8   H  N N 12  
ADE HN61 H  N N 13  
ADE HN62 H  N N 14  
ADE H2   H  N N 15  
ALA N    N  N N 16  
ALA CA   C  N S 17  
ALA C    C  N N 18  
ALA O    O  N N 19  
ALA CB   C  N N 20  
ALA OXT  O  N N 21  
ALA H    H  N N 22  
ALA H2   H  N N 23  
ALA HA   H  N N 24  
ALA HB1  H  N N 25  
ALA HB2  H  N N 26  
ALA HB3  H  N N 27  
ALA HXT  H  N N 28  
ARG N    N  N N 29  
ARG CA   C  N S 30  
ARG C    C  N N 31  
ARG O    O  N N 32  
ARG CB   C  N N 33  
ARG CG   C  N N 34  
ARG CD   C  N N 35  
ARG NE   N  N N 36  
ARG CZ   C  N N 37  
ARG NH1  N  N N 38  
ARG NH2  N  N N 39  
ARG OXT  O  N N 40  
ARG H    H  N N 41  
ARG H2   H  N N 42  
ARG HA   H  N N 43  
ARG HB2  H  N N 44  
ARG HB3  H  N N 45  
ARG HG2  H  N N 46  
ARG HG3  H  N N 47  
ARG HD2  H  N N 48  
ARG HD3  H  N N 49  
ARG HE   H  N N 50  
ARG HH11 H  N N 51  
ARG HH12 H  N N 52  
ARG HH21 H  N N 53  
ARG HH22 H  N N 54  
ARG HXT  H  N N 55  
ASN N    N  N N 56  
ASN CA   C  N S 57  
ASN C    C  N N 58  
ASN O    O  N N 59  
ASN CB   C  N N 60  
ASN CG   C  N N 61  
ASN OD1  O  N N 62  
ASN ND2  N  N N 63  
ASN OXT  O  N N 64  
ASN H    H  N N 65  
ASN H2   H  N N 66  
ASN HA   H  N N 67  
ASN HB2  H  N N 68  
ASN HB3  H  N N 69  
ASN HD21 H  N N 70  
ASN HD22 H  N N 71  
ASN HXT  H  N N 72  
ASP N    N  N N 73  
ASP CA   C  N S 74  
ASP C    C  N N 75  
ASP O    O  N N 76  
ASP CB   C  N N 77  
ASP CG   C  N N 78  
ASP OD1  O  N N 79  
ASP OD2  O  N N 80  
ASP OXT  O  N N 81  
ASP H    H  N N 82  
ASP H2   H  N N 83  
ASP HA   H  N N 84  
ASP HB2  H  N N 85  
ASP HB3  H  N N 86  
ASP HD2  H  N N 87  
ASP HXT  H  N N 88  
CYS N    N  N N 89  
CYS CA   C  N R 90  
CYS C    C  N N 91  
CYS O    O  N N 92  
CYS CB   C  N N 93  
CYS SG   S  N N 94  
CYS OXT  O  N N 95  
CYS H    H  N N 96  
CYS H2   H  N N 97  
CYS HA   H  N N 98  
CYS HB2  H  N N 99  
CYS HB3  H  N N 100 
CYS HG   H  N N 101 
CYS HXT  H  N N 102 
GLN N    N  N N 103 
GLN CA   C  N S 104 
GLN C    C  N N 105 
GLN O    O  N N 106 
GLN CB   C  N N 107 
GLN CG   C  N N 108 
GLN CD   C  N N 109 
GLN OE1  O  N N 110 
GLN NE2  N  N N 111 
GLN OXT  O  N N 112 
GLN H    H  N N 113 
GLN H2   H  N N 114 
GLN HA   H  N N 115 
GLN HB2  H  N N 116 
GLN HB3  H  N N 117 
GLN HG2  H  N N 118 
GLN HG3  H  N N 119 
GLN HE21 H  N N 120 
GLN HE22 H  N N 121 
GLN HXT  H  N N 122 
GLU N    N  N N 123 
GLU CA   C  N S 124 
GLU C    C  N N 125 
GLU O    O  N N 126 
GLU CB   C  N N 127 
GLU CG   C  N N 128 
GLU CD   C  N N 129 
GLU OE1  O  N N 130 
GLU OE2  O  N N 131 
GLU OXT  O  N N 132 
GLU H    H  N N 133 
GLU H2   H  N N 134 
GLU HA   H  N N 135 
GLU HB2  H  N N 136 
GLU HB3  H  N N 137 
GLU HG2  H  N N 138 
GLU HG3  H  N N 139 
GLU HE2  H  N N 140 
GLU HXT  H  N N 141 
GLY N    N  N N 142 
GLY CA   C  N N 143 
GLY C    C  N N 144 
GLY O    O  N N 145 
GLY OXT  O  N N 146 
GLY H    H  N N 147 
GLY H2   H  N N 148 
GLY HA2  H  N N 149 
GLY HA3  H  N N 150 
GLY HXT  H  N N 151 
HEM CHA  C  N N 152 
HEM CHB  C  N N 153 
HEM CHC  C  N N 154 
HEM CHD  C  N N 155 
HEM C1A  C  Y N 156 
HEM C2A  C  Y N 157 
HEM C3A  C  Y N 158 
HEM C4A  C  Y N 159 
HEM CMA  C  N N 160 
HEM CAA  C  N N 161 
HEM CBA  C  N N 162 
HEM CGA  C  N N 163 
HEM O1A  O  N N 164 
HEM O2A  O  N N 165 
HEM C1B  C  N N 166 
HEM C2B  C  N N 167 
HEM C3B  C  N N 168 
HEM C4B  C  N N 169 
HEM CMB  C  N N 170 
HEM CAB  C  N N 171 
HEM CBB  C  N N 172 
HEM C1C  C  Y N 173 
HEM C2C  C  Y N 174 
HEM C3C  C  Y N 175 
HEM C4C  C  Y N 176 
HEM CMC  C  N N 177 
HEM CAC  C  N N 178 
HEM CBC  C  N N 179 
HEM C1D  C  N N 180 
HEM C2D  C  N N 181 
HEM C3D  C  N N 182 
HEM C4D  C  N N 183 
HEM CMD  C  N N 184 
HEM CAD  C  N N 185 
HEM CBD  C  N N 186 
HEM CGD  C  N N 187 
HEM O1D  O  N N 188 
HEM O2D  O  N N 189 
HEM NA   N  Y N 190 
HEM NB   N  N N 191 
HEM NC   N  Y N 192 
HEM ND   N  N N 193 
HEM FE   FE N N 194 
HEM HHB  H  N N 195 
HEM HHC  H  N N 196 
HEM HHD  H  N N 197 
HEM HMA  H  N N 198 
HEM HMAA H  N N 199 
HEM HMAB H  N N 200 
HEM HAA  H  N N 201 
HEM HAAA H  N N 202 
HEM HBA  H  N N 203 
HEM HBAA H  N N 204 
HEM HMB  H  N N 205 
HEM HMBA H  N N 206 
HEM HMBB H  N N 207 
HEM HAB  H  N N 208 
HEM HBB  H  N N 209 
HEM HBBA H  N N 210 
HEM HMC  H  N N 211 
HEM HMCA H  N N 212 
HEM HMCB H  N N 213 
HEM HAC  H  N N 214 
HEM HBC  H  N N 215 
HEM HBCA H  N N 216 
HEM HMD  H  N N 217 
HEM HMDA H  N N 218 
HEM HMDB H  N N 219 
HEM HAD  H  N N 220 
HEM HADA H  N N 221 
HEM HBD  H  N N 222 
HEM HBDA H  N N 223 
HEM H2A  H  N N 224 
HEM H2D  H  N N 225 
HEM HHA  H  N N 226 
HIS N    N  N N 227 
HIS CA   C  N S 228 
HIS C    C  N N 229 
HIS O    O  N N 230 
HIS CB   C  N N 231 
HIS CG   C  Y N 232 
HIS ND1  N  Y N 233 
HIS CD2  C  Y N 234 
HIS CE1  C  Y N 235 
HIS NE2  N  Y N 236 
HIS OXT  O  N N 237 
HIS H    H  N N 238 
HIS H2   H  N N 239 
HIS HA   H  N N 240 
HIS HB2  H  N N 241 
HIS HB3  H  N N 242 
HIS HD1  H  N N 243 
HIS HD2  H  N N 244 
HIS HE1  H  N N 245 
HIS HE2  H  N N 246 
HIS HXT  H  N N 247 
HOH O    O  N N 248 
HOH H1   H  N N 249 
HOH H2   H  N N 250 
ILE N    N  N N 251 
ILE CA   C  N S 252 
ILE C    C  N N 253 
ILE O    O  N N 254 
ILE CB   C  N S 255 
ILE CG1  C  N N 256 
ILE CG2  C  N N 257 
ILE CD1  C  N N 258 
ILE OXT  O  N N 259 
ILE H    H  N N 260 
ILE H2   H  N N 261 
ILE HA   H  N N 262 
ILE HB   H  N N 263 
ILE HG12 H  N N 264 
ILE HG13 H  N N 265 
ILE HG21 H  N N 266 
ILE HG22 H  N N 267 
ILE HG23 H  N N 268 
ILE HD11 H  N N 269 
ILE HD12 H  N N 270 
ILE HD13 H  N N 271 
ILE HXT  H  N N 272 
LEU N    N  N N 273 
LEU CA   C  N S 274 
LEU C    C  N N 275 
LEU O    O  N N 276 
LEU CB   C  N N 277 
LEU CG   C  N N 278 
LEU CD1  C  N N 279 
LEU CD2  C  N N 280 
LEU OXT  O  N N 281 
LEU H    H  N N 282 
LEU H2   H  N N 283 
LEU HA   H  N N 284 
LEU HB2  H  N N 285 
LEU HB3  H  N N 286 
LEU HG   H  N N 287 
LEU HD11 H  N N 288 
LEU HD12 H  N N 289 
LEU HD13 H  N N 290 
LEU HD21 H  N N 291 
LEU HD22 H  N N 292 
LEU HD23 H  N N 293 
LEU HXT  H  N N 294 
LYS N    N  N N 295 
LYS CA   C  N S 296 
LYS C    C  N N 297 
LYS O    O  N N 298 
LYS CB   C  N N 299 
LYS CG   C  N N 300 
LYS CD   C  N N 301 
LYS CE   C  N N 302 
LYS NZ   N  N N 303 
LYS OXT  O  N N 304 
LYS H    H  N N 305 
LYS H2   H  N N 306 
LYS HA   H  N N 307 
LYS HB2  H  N N 308 
LYS HB3  H  N N 309 
LYS HG2  H  N N 310 
LYS HG3  H  N N 311 
LYS HD2  H  N N 312 
LYS HD3  H  N N 313 
LYS HE2  H  N N 314 
LYS HE3  H  N N 315 
LYS HZ1  H  N N 316 
LYS HZ2  H  N N 317 
LYS HZ3  H  N N 318 
LYS HXT  H  N N 319 
MET N    N  N N 320 
MET CA   C  N S 321 
MET C    C  N N 322 
MET O    O  N N 323 
MET CB   C  N N 324 
MET CG   C  N N 325 
MET SD   S  N N 326 
MET CE   C  N N 327 
MET OXT  O  N N 328 
MET H    H  N N 329 
MET H2   H  N N 330 
MET HA   H  N N 331 
MET HB2  H  N N 332 
MET HB3  H  N N 333 
MET HG2  H  N N 334 
MET HG3  H  N N 335 
MET HE1  H  N N 336 
MET HE2  H  N N 337 
MET HE3  H  N N 338 
MET HXT  H  N N 339 
PHE N    N  N N 340 
PHE CA   C  N S 341 
PHE C    C  N N 342 
PHE O    O  N N 343 
PHE CB   C  N N 344 
PHE CG   C  Y N 345 
PHE CD1  C  Y N 346 
PHE CD2  C  Y N 347 
PHE CE1  C  Y N 348 
PHE CE2  C  Y N 349 
PHE CZ   C  Y N 350 
PHE OXT  O  N N 351 
PHE H    H  N N 352 
PHE H2   H  N N 353 
PHE HA   H  N N 354 
PHE HB2  H  N N 355 
PHE HB3  H  N N 356 
PHE HD1  H  N N 357 
PHE HD2  H  N N 358 
PHE HE1  H  N N 359 
PHE HE2  H  N N 360 
PHE HZ   H  N N 361 
PHE HXT  H  N N 362 
PRO N    N  N N 363 
PRO CA   C  N S 364 
PRO C    C  N N 365 
PRO O    O  N N 366 
PRO CB   C  N N 367 
PRO CG   C  N N 368 
PRO CD   C  N N 369 
PRO OXT  O  N N 370 
PRO H    H  N N 371 
PRO HA   H  N N 372 
PRO HB2  H  N N 373 
PRO HB3  H  N N 374 
PRO HG2  H  N N 375 
PRO HG3  H  N N 376 
PRO HD2  H  N N 377 
PRO HD3  H  N N 378 
PRO HXT  H  N N 379 
SER N    N  N N 380 
SER CA   C  N S 381 
SER C    C  N N 382 
SER O    O  N N 383 
SER CB   C  N N 384 
SER OG   O  N N 385 
SER OXT  O  N N 386 
SER H    H  N N 387 
SER H2   H  N N 388 
SER HA   H  N N 389 
SER HB2  H  N N 390 
SER HB3  H  N N 391 
SER HG   H  N N 392 
SER HXT  H  N N 393 
THR N    N  N N 394 
THR CA   C  N S 395 
THR C    C  N N 396 
THR O    O  N N 397 
THR CB   C  N R 398 
THR OG1  O  N N 399 
THR CG2  C  N N 400 
THR OXT  O  N N 401 
THR H    H  N N 402 
THR H2   H  N N 403 
THR HA   H  N N 404 
THR HB   H  N N 405 
THR HG1  H  N N 406 
THR HG21 H  N N 407 
THR HG22 H  N N 408 
THR HG23 H  N N 409 
THR HXT  H  N N 410 
TRP N    N  N N 411 
TRP CA   C  N S 412 
TRP C    C  N N 413 
TRP O    O  N N 414 
TRP CB   C  N N 415 
TRP CG   C  Y N 416 
TRP CD1  C  Y N 417 
TRP CD2  C  Y N 418 
TRP NE1  N  Y N 419 
TRP CE2  C  Y N 420 
TRP CE3  C  Y N 421 
TRP CZ2  C  Y N 422 
TRP CZ3  C  Y N 423 
TRP CH2  C  Y N 424 
TRP OXT  O  N N 425 
TRP H    H  N N 426 
TRP H2   H  N N 427 
TRP HA   H  N N 428 
TRP HB2  H  N N 429 
TRP HB3  H  N N 430 
TRP HD1  H  N N 431 
TRP HE1  H  N N 432 
TRP HE3  H  N N 433 
TRP HZ2  H  N N 434 
TRP HZ3  H  N N 435 
TRP HH2  H  N N 436 
TRP HXT  H  N N 437 
TYR N    N  N N 438 
TYR CA   C  N S 439 
TYR C    C  N N 440 
TYR O    O  N N 441 
TYR CB   C  N N 442 
TYR CG   C  Y N 443 
TYR CD1  C  Y N 444 
TYR CD2  C  Y N 445 
TYR CE1  C  Y N 446 
TYR CE2  C  Y N 447 
TYR CZ   C  Y N 448 
TYR OH   O  N N 449 
TYR OXT  O  N N 450 
TYR H    H  N N 451 
TYR H2   H  N N 452 
TYR HA   H  N N 453 
TYR HB2  H  N N 454 
TYR HB3  H  N N 455 
TYR HD1  H  N N 456 
TYR HD2  H  N N 457 
TYR HE1  H  N N 458 
TYR HE2  H  N N 459 
TYR HH   H  N N 460 
TYR HXT  H  N N 461 
UYM N    N  Y N 462 
UYM C    C  N N 463 
UYM O    O  N N 464 
UYM C1   C  N S 465 
UYM C10  C  Y N 466 
UYM C11  C  N S 467 
UYM C12  C  N N 468 
UYM C15  C  N N 469 
UYM C2   C  N N 470 
UYM C3   C  Y N 471 
UYM C34  C  Y N 472 
UYM C35  C  Y N 473 
UYM C37  C  Y N 474 
UYM C38  C  Y N 475 
UYM C39  C  Y N 476 
UYM C4   C  Y N 477 
UYM C40  C  Y N 478 
UYM C41  C  Y N 479 
UYM C42  C  Y N 480 
UYM C5   C  Y N 481 
UYM C6   C  Y N 482 
UYM C7   C  Y N 483 
UYM C8   C  Y N 484 
UYM C9   C  Y N 485 
UYM N1   N  N N 486 
UYM N2   N  N N 487 
UYM N36  N  Y N 488 
UYM O1   O  N N 489 
UYM H1   H  N N 490 
UYM H2   H  N N 491 
UYM H3   H  N N 492 
UYM H4   H  N N 493 
UYM H5   H  N N 494 
UYM H6   H  N N 495 
UYM H7   H  N N 496 
UYM H8   H  N N 497 
UYM H9   H  N N 498 
UYM H10  H  N N 499 
UYM H11  H  N N 500 
UYM H12  H  N N 501 
UYM H13  H  N N 502 
UYM H14  H  N N 503 
UYM H15  H  N N 504 
UYM H16  H  N N 505 
UYM H17  H  N N 506 
UYM H18  H  N N 507 
UYM H19  H  N N 508 
UYM H20  H  N N 509 
VAL N    N  N N 510 
VAL CA   C  N S 511 
VAL C    C  N N 512 
VAL O    O  N N 513 
VAL CB   C  N N 514 
VAL CG1  C  N N 515 
VAL CG2  C  N N 516 
VAL OXT  O  N N 517 
VAL H    H  N N 518 
VAL H2   H  N N 519 
VAL HA   H  N N 520 
VAL HB   H  N N 521 
VAL HG11 H  N N 522 
VAL HG12 H  N N 523 
VAL HG13 H  N N 524 
VAL HG21 H  N N 525 
VAL HG22 H  N N 526 
VAL HG23 H  N N 527 
VAL HXT  H  N N 528 
# 
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 
ADE N9  C8   sing Y N 1   
ADE N9  C4   sing Y N 2   
ADE N9  HN9  sing N N 3   
ADE C8  N7   doub Y N 4   
ADE C8  H8   sing N N 5   
ADE N7  C5   sing Y N 6   
ADE C5  C6   sing Y N 7   
ADE C5  C4   doub Y N 8   
ADE C6  N6   sing N N 9   
ADE C6  N1   doub Y N 10  
ADE N6  HN61 sing N N 11  
ADE N6  HN62 sing N N 12  
ADE N1  C2   sing Y N 13  
ADE C2  N3   doub Y N 14  
ADE C2  H2   sing N N 15  
ADE N3  C4   sing Y N 16  
ALA N   CA   sing N N 17  
ALA N   H    sing N N 18  
ALA N   H2   sing N N 19  
ALA CA  C    sing N N 20  
ALA CA  CB   sing N N 21  
ALA CA  HA   sing N N 22  
ALA C   O    doub N N 23  
ALA C   OXT  sing N N 24  
ALA CB  HB1  sing N N 25  
ALA CB  HB2  sing N N 26  
ALA CB  HB3  sing N N 27  
ALA OXT HXT  sing N N 28  
ARG N   CA   sing N N 29  
ARG N   H    sing N N 30  
ARG N   H2   sing N N 31  
ARG CA  C    sing N N 32  
ARG CA  CB   sing N N 33  
ARG CA  HA   sing N N 34  
ARG C   O    doub N N 35  
ARG C   OXT  sing N N 36  
ARG CB  CG   sing N N 37  
ARG CB  HB2  sing N N 38  
ARG CB  HB3  sing N N 39  
ARG CG  CD   sing N N 40  
ARG CG  HG2  sing N N 41  
ARG CG  HG3  sing N N 42  
ARG CD  NE   sing N N 43  
ARG CD  HD2  sing N N 44  
ARG CD  HD3  sing N N 45  
ARG NE  CZ   sing N N 46  
ARG NE  HE   sing N N 47  
ARG CZ  NH1  sing N N 48  
ARG CZ  NH2  doub N N 49  
ARG NH1 HH11 sing N N 50  
ARG NH1 HH12 sing N N 51  
ARG NH2 HH21 sing N N 52  
ARG NH2 HH22 sing N N 53  
ARG OXT HXT  sing N N 54  
ASN N   CA   sing N N 55  
ASN N   H    sing N N 56  
ASN N   H2   sing N N 57  
ASN CA  C    sing N N 58  
ASN CA  CB   sing N N 59  
ASN CA  HA   sing N N 60  
ASN C   O    doub N N 61  
ASN C   OXT  sing N N 62  
ASN CB  CG   sing N N 63  
ASN CB  HB2  sing N N 64  
ASN CB  HB3  sing N N 65  
ASN CG  OD1  doub N N 66  
ASN CG  ND2  sing N N 67  
ASN ND2 HD21 sing N N 68  
ASN ND2 HD22 sing N N 69  
ASN OXT HXT  sing N N 70  
ASP N   CA   sing N N 71  
ASP N   H    sing N N 72  
ASP N   H2   sing N N 73  
ASP CA  C    sing N N 74  
ASP CA  CB   sing N N 75  
ASP CA  HA   sing N N 76  
ASP C   O    doub N N 77  
ASP C   OXT  sing N N 78  
ASP CB  CG   sing N N 79  
ASP CB  HB2  sing N N 80  
ASP CB  HB3  sing N N 81  
ASP CG  OD1  doub N N 82  
ASP CG  OD2  sing N N 83  
ASP OD2 HD2  sing N N 84  
ASP OXT HXT  sing N N 85  
CYS N   CA   sing N N 86  
CYS N   H    sing N N 87  
CYS N   H2   sing N N 88  
CYS CA  C    sing N N 89  
CYS CA  CB   sing N N 90  
CYS CA  HA   sing N N 91  
CYS C   O    doub N N 92  
CYS C   OXT  sing N N 93  
CYS CB  SG   sing N N 94  
CYS CB  HB2  sing N N 95  
CYS CB  HB3  sing N N 96  
CYS SG  HG   sing N N 97  
CYS OXT HXT  sing N N 98  
GLN N   CA   sing N N 99  
GLN N   H    sing N N 100 
GLN N   H2   sing N N 101 
GLN CA  C    sing N N 102 
GLN CA  CB   sing N N 103 
GLN CA  HA   sing N N 104 
GLN C   O    doub N N 105 
GLN C   OXT  sing N N 106 
GLN CB  CG   sing N N 107 
GLN CB  HB2  sing N N 108 
GLN CB  HB3  sing N N 109 
GLN CG  CD   sing N N 110 
GLN CG  HG2  sing N N 111 
GLN CG  HG3  sing N N 112 
GLN CD  OE1  doub N N 113 
GLN CD  NE2  sing N N 114 
GLN NE2 HE21 sing N N 115 
GLN NE2 HE22 sing N N 116 
GLN OXT HXT  sing N N 117 
GLU N   CA   sing N N 118 
GLU N   H    sing N N 119 
GLU N   H2   sing N N 120 
GLU CA  C    sing N N 121 
GLU CA  CB   sing N N 122 
GLU CA  HA   sing N N 123 
GLU C   O    doub N N 124 
GLU C   OXT  sing N N 125 
GLU CB  CG   sing N N 126 
GLU CB  HB2  sing N N 127 
GLU CB  HB3  sing N N 128 
GLU CG  CD   sing N N 129 
GLU CG  HG2  sing N N 130 
GLU CG  HG3  sing N N 131 
GLU CD  OE1  doub N N 132 
GLU CD  OE2  sing N N 133 
GLU OE2 HE2  sing N N 134 
GLU OXT HXT  sing N N 135 
GLY N   CA   sing N N 136 
GLY N   H    sing N N 137 
GLY N   H2   sing N N 138 
GLY CA  C    sing N N 139 
GLY CA  HA2  sing N N 140 
GLY CA  HA3  sing N N 141 
GLY C   O    doub N N 142 
GLY C   OXT  sing N N 143 
GLY OXT HXT  sing N N 144 
HEM CHA C1A  sing N N 145 
HEM CHA C4D  doub N N 146 
HEM CHA HHA  sing N N 147 
HEM CHB C4A  sing N N 148 
HEM CHB C1B  doub N N 149 
HEM CHB HHB  sing N N 150 
HEM CHC C4B  sing N N 151 
HEM CHC C1C  doub N N 152 
HEM CHC HHC  sing N N 153 
HEM CHD C4C  doub N N 154 
HEM CHD C1D  sing N N 155 
HEM CHD HHD  sing N N 156 
HEM C1A C2A  doub Y N 157 
HEM C1A NA   sing Y N 158 
HEM C2A C3A  sing Y N 159 
HEM C2A CAA  sing N N 160 
HEM C3A C4A  doub Y N 161 
HEM C3A CMA  sing N N 162 
HEM C4A NA   sing Y N 163 
HEM CMA HMA  sing N N 164 
HEM CMA HMAA sing N N 165 
HEM CMA HMAB sing N N 166 
HEM CAA CBA  sing N N 167 
HEM CAA HAA  sing N N 168 
HEM CAA HAAA sing N N 169 
HEM CBA CGA  sing N N 170 
HEM CBA HBA  sing N N 171 
HEM CBA HBAA sing N N 172 
HEM CGA O1A  doub N N 173 
HEM CGA O2A  sing N N 174 
HEM C1B C2B  sing N N 175 
HEM C1B NB   sing N N 176 
HEM C2B C3B  doub N N 177 
HEM C2B CMB  sing N N 178 
HEM C3B C4B  sing N N 179 
HEM C3B CAB  sing N N 180 
HEM C4B NB   doub N N 181 
HEM CMB HMB  sing N N 182 
HEM CMB HMBA sing N N 183 
HEM CMB HMBB sing N N 184 
HEM CAB CBB  doub N N 185 
HEM CAB HAB  sing N N 186 
HEM CBB HBB  sing N N 187 
HEM CBB HBBA sing N N 188 
HEM C1C C2C  sing Y N 189 
HEM C1C NC   sing Y N 190 
HEM C2C C3C  doub Y N 191 
HEM C2C CMC  sing N N 192 
HEM C3C C4C  sing Y N 193 
HEM C3C CAC  sing N N 194 
HEM C4C NC   sing Y N 195 
HEM CMC HMC  sing N N 196 
HEM CMC HMCA sing N N 197 
HEM CMC HMCB sing N N 198 
HEM CAC CBC  doub N N 199 
HEM CAC HAC  sing N N 200 
HEM CBC HBC  sing N N 201 
HEM CBC HBCA sing N N 202 
HEM C1D C2D  sing N N 203 
HEM C1D ND   doub N N 204 
HEM C2D C3D  doub N N 205 
HEM C2D CMD  sing N N 206 
HEM C3D C4D  sing N N 207 
HEM C3D CAD  sing N N 208 
HEM C4D ND   sing N N 209 
HEM CMD HMD  sing N N 210 
HEM CMD HMDA sing N N 211 
HEM CMD HMDB sing N N 212 
HEM CAD CBD  sing N N 213 
HEM CAD HAD  sing N N 214 
HEM CAD HADA sing N N 215 
HEM CBD CGD  sing N N 216 
HEM CBD HBD  sing N N 217 
HEM CBD HBDA sing N N 218 
HEM CGD O1D  doub N N 219 
HEM CGD O2D  sing N N 220 
HEM O2A H2A  sing N N 221 
HEM O2D H2D  sing N N 222 
HEM FE  NA   sing N N 223 
HEM FE  NB   sing N N 224 
HEM FE  NC   sing N N 225 
HEM FE  ND   sing N N 226 
HIS N   CA   sing N N 227 
HIS N   H    sing N N 228 
HIS N   H2   sing N N 229 
HIS CA  C    sing N N 230 
HIS CA  CB   sing N N 231 
HIS CA  HA   sing N N 232 
HIS C   O    doub N N 233 
HIS C   OXT  sing N N 234 
HIS CB  CG   sing N N 235 
HIS CB  HB2  sing N N 236 
HIS CB  HB3  sing N N 237 
HIS CG  ND1  sing Y N 238 
HIS CG  CD2  doub Y N 239 
HIS ND1 CE1  doub Y N 240 
HIS ND1 HD1  sing N N 241 
HIS CD2 NE2  sing Y N 242 
HIS CD2 HD2  sing N N 243 
HIS CE1 NE2  sing Y N 244 
HIS CE1 HE1  sing N N 245 
HIS NE2 HE2  sing N N 246 
HIS OXT HXT  sing N N 247 
HOH O   H1   sing N N 248 
HOH O   H2   sing N N 249 
ILE N   CA   sing N N 250 
ILE N   H    sing N N 251 
ILE N   H2   sing N N 252 
ILE CA  C    sing N N 253 
ILE CA  CB   sing N N 254 
ILE CA  HA   sing N N 255 
ILE C   O    doub N N 256 
ILE C   OXT  sing N N 257 
ILE CB  CG1  sing N N 258 
ILE CB  CG2  sing N N 259 
ILE CB  HB   sing N N 260 
ILE CG1 CD1  sing N N 261 
ILE CG1 HG12 sing N N 262 
ILE CG1 HG13 sing N N 263 
ILE CG2 HG21 sing N N 264 
ILE CG2 HG22 sing N N 265 
ILE CG2 HG23 sing N N 266 
ILE CD1 HD11 sing N N 267 
ILE CD1 HD12 sing N N 268 
ILE CD1 HD13 sing N N 269 
ILE OXT HXT  sing N N 270 
LEU N   CA   sing N N 271 
LEU N   H    sing N N 272 
LEU N   H2   sing N N 273 
LEU CA  C    sing N N 274 
LEU CA  CB   sing N N 275 
LEU CA  HA   sing N N 276 
LEU C   O    doub N N 277 
LEU C   OXT  sing N N 278 
LEU CB  CG   sing N N 279 
LEU CB  HB2  sing N N 280 
LEU CB  HB3  sing N N 281 
LEU CG  CD1  sing N N 282 
LEU CG  CD2  sing N N 283 
LEU CG  HG   sing N N 284 
LEU CD1 HD11 sing N N 285 
LEU CD1 HD12 sing N N 286 
LEU CD1 HD13 sing N N 287 
LEU CD2 HD21 sing N N 288 
LEU CD2 HD22 sing N N 289 
LEU CD2 HD23 sing N N 290 
LEU OXT HXT  sing N N 291 
LYS N   CA   sing N N 292 
LYS N   H    sing N N 293 
LYS N   H2   sing N N 294 
LYS CA  C    sing N N 295 
LYS CA  CB   sing N N 296 
LYS CA  HA   sing N N 297 
LYS C   O    doub N N 298 
LYS C   OXT  sing N N 299 
LYS CB  CG   sing N N 300 
LYS CB  HB2  sing N N 301 
LYS CB  HB3  sing N N 302 
LYS CG  CD   sing N N 303 
LYS CG  HG2  sing N N 304 
LYS CG  HG3  sing N N 305 
LYS CD  CE   sing N N 306 
LYS CD  HD2  sing N N 307 
LYS CD  HD3  sing N N 308 
LYS CE  NZ   sing N N 309 
LYS CE  HE2  sing N N 310 
LYS CE  HE3  sing N N 311 
LYS NZ  HZ1  sing N N 312 
LYS NZ  HZ2  sing N N 313 
LYS NZ  HZ3  sing N N 314 
LYS OXT HXT  sing N N 315 
MET N   CA   sing N N 316 
MET N   H    sing N N 317 
MET N   H2   sing N N 318 
MET CA  C    sing N N 319 
MET CA  CB   sing N N 320 
MET CA  HA   sing N N 321 
MET C   O    doub N N 322 
MET C   OXT  sing N N 323 
MET CB  CG   sing N N 324 
MET CB  HB2  sing N N 325 
MET CB  HB3  sing N N 326 
MET CG  SD   sing N N 327 
MET CG  HG2  sing N N 328 
MET CG  HG3  sing N N 329 
MET SD  CE   sing N N 330 
MET CE  HE1  sing N N 331 
MET CE  HE2  sing N N 332 
MET CE  HE3  sing N N 333 
MET OXT HXT  sing N N 334 
PHE N   CA   sing N N 335 
PHE N   H    sing N N 336 
PHE N   H2   sing N N 337 
PHE CA  C    sing N N 338 
PHE CA  CB   sing N N 339 
PHE CA  HA   sing N N 340 
PHE C   O    doub N N 341 
PHE C   OXT  sing N N 342 
PHE CB  CG   sing N N 343 
PHE CB  HB2  sing N N 344 
PHE CB  HB3  sing N N 345 
PHE CG  CD1  doub Y N 346 
PHE CG  CD2  sing Y N 347 
PHE CD1 CE1  sing Y N 348 
PHE CD1 HD1  sing N N 349 
PHE CD2 CE2  doub Y N 350 
PHE CD2 HD2  sing N N 351 
PHE CE1 CZ   doub Y N 352 
PHE CE1 HE1  sing N N 353 
PHE CE2 CZ   sing Y N 354 
PHE CE2 HE2  sing N N 355 
PHE CZ  HZ   sing N N 356 
PHE OXT HXT  sing N N 357 
PRO N   CA   sing N N 358 
PRO N   CD   sing N N 359 
PRO N   H    sing N N 360 
PRO CA  C    sing N N 361 
PRO CA  CB   sing N N 362 
PRO CA  HA   sing N N 363 
PRO C   O    doub N N 364 
PRO C   OXT  sing N N 365 
PRO CB  CG   sing N N 366 
PRO CB  HB2  sing N N 367 
PRO CB  HB3  sing N N 368 
PRO CG  CD   sing N N 369 
PRO CG  HG2  sing N N 370 
PRO CG  HG3  sing N N 371 
PRO CD  HD2  sing N N 372 
PRO CD  HD3  sing N N 373 
PRO OXT HXT  sing N N 374 
SER N   CA   sing N N 375 
SER N   H    sing N N 376 
SER N   H2   sing N N 377 
SER CA  C    sing N N 378 
SER CA  CB   sing N N 379 
SER CA  HA   sing N N 380 
SER C   O    doub N N 381 
SER C   OXT  sing N N 382 
SER CB  OG   sing N N 383 
SER CB  HB2  sing N N 384 
SER CB  HB3  sing N N 385 
SER OG  HG   sing N N 386 
SER OXT HXT  sing N N 387 
THR N   CA   sing N N 388 
THR N   H    sing N N 389 
THR N   H2   sing N N 390 
THR CA  C    sing N N 391 
THR CA  CB   sing N N 392 
THR CA  HA   sing N N 393 
THR C   O    doub N N 394 
THR C   OXT  sing N N 395 
THR CB  OG1  sing N N 396 
THR CB  CG2  sing N N 397 
THR CB  HB   sing N N 398 
THR OG1 HG1  sing N N 399 
THR CG2 HG21 sing N N 400 
THR CG2 HG22 sing N N 401 
THR CG2 HG23 sing N N 402 
THR OXT HXT  sing N N 403 
TRP N   CA   sing N N 404 
TRP N   H    sing N N 405 
TRP N   H2   sing N N 406 
TRP CA  C    sing N N 407 
TRP CA  CB   sing N N 408 
TRP CA  HA   sing N N 409 
TRP C   O    doub N N 410 
TRP C   OXT  sing N N 411 
TRP CB  CG   sing N N 412 
TRP CB  HB2  sing N N 413 
TRP CB  HB3  sing N N 414 
TRP CG  CD1  doub Y N 415 
TRP CG  CD2  sing Y N 416 
TRP CD1 NE1  sing Y N 417 
TRP CD1 HD1  sing N N 418 
TRP CD2 CE2  doub Y N 419 
TRP CD2 CE3  sing Y N 420 
TRP NE1 CE2  sing Y N 421 
TRP NE1 HE1  sing N N 422 
TRP CE2 CZ2  sing Y N 423 
TRP CE3 CZ3  doub Y N 424 
TRP CE3 HE3  sing N N 425 
TRP CZ2 CH2  doub Y N 426 
TRP CZ2 HZ2  sing N N 427 
TRP CZ3 CH2  sing Y N 428 
TRP CZ3 HZ3  sing N N 429 
TRP CH2 HH2  sing N N 430 
TRP OXT HXT  sing N N 431 
TYR N   CA   sing N N 432 
TYR N   H    sing N N 433 
TYR N   H2   sing N N 434 
TYR CA  C    sing N N 435 
TYR CA  CB   sing N N 436 
TYR CA  HA   sing N N 437 
TYR C   O    doub N N 438 
TYR C   OXT  sing N N 439 
TYR CB  CG   sing N N 440 
TYR CB  HB2  sing N N 441 
TYR CB  HB3  sing N N 442 
TYR CG  CD1  doub Y N 443 
TYR CG  CD2  sing Y N 444 
TYR CD1 CE1  sing Y N 445 
TYR CD1 HD1  sing N N 446 
TYR CD2 CE2  doub Y N 447 
TYR CD2 HD2  sing N N 448 
TYR CE1 CZ   doub Y N 449 
TYR CE1 HE1  sing N N 450 
TYR CE2 CZ   sing Y N 451 
TYR CE2 HE2  sing N N 452 
TYR CZ  OH   sing N N 453 
TYR OH  HH   sing N N 454 
TYR OXT HXT  sing N N 455 
UYM C8  C9   doub Y N 456 
UYM C8  C7   sing Y N 457 
UYM C9  C10  sing Y N 458 
UYM C7  C6   doub Y N 459 
UYM C10 C5   doub Y N 460 
UYM C6  C5   sing Y N 461 
UYM C6  C3   sing Y N 462 
UYM C5  N    sing Y N 463 
UYM O   C    doub N N 464 
UYM C3  C2   sing N N 465 
UYM C3  C4   doub Y N 466 
UYM C1  C    sing N N 467 
UYM C1  C2   sing N N 468 
UYM C1  N1   sing N N 469 
UYM N   C4   sing Y N 470 
UYM C   N2   sing N N 471 
UYM N1  C15  sing N N 472 
UYM N2  C11  sing N N 473 
UYM C15 C11  sing N N 474 
UYM C15 O1   doub N N 475 
UYM C11 C12  sing N N 476 
UYM C35 C34  doub Y N 477 
UYM C35 N36  sing Y N 478 
UYM C12 C34  sing N N 479 
UYM C34 C38  sing Y N 480 
UYM N36 C37  sing Y N 481 
UYM C38 C37  doub Y N 482 
UYM C38 C39  sing Y N 483 
UYM C37 C42  sing Y N 484 
UYM C39 C40  doub Y N 485 
UYM C42 C41  doub Y N 486 
UYM C40 C41  sing Y N 487 
UYM N   H1   sing N N 488 
UYM C1  H2   sing N N 489 
UYM C10 H3   sing N N 490 
UYM C11 H4   sing N N 491 
UYM C12 H5   sing N N 492 
UYM C12 H6   sing N N 493 
UYM C2  H7   sing N N 494 
UYM C2  H8   sing N N 495 
UYM C35 H9   sing N N 496 
UYM C39 H10  sing N N 497 
UYM C4  H11  sing N N 498 
UYM C40 H12  sing N N 499 
UYM C41 H13  sing N N 500 
UYM C42 H14  sing N N 501 
UYM C7  H15  sing N N 502 
UYM C8  H16  sing N N 503 
UYM C9  H17  sing N N 504 
UYM N1  H18  sing N N 505 
UYM N2  H19  sing N N 506 
UYM N36 H20  sing N N 507 
VAL N   CA   sing N N 508 
VAL N   H    sing N N 509 
VAL N   H2   sing N N 510 
VAL CA  C    sing N N 511 
VAL CA  CB   sing N N 512 
VAL CA  HA   sing N N 513 
VAL C   O    doub N N 514 
VAL C   OXT  sing N N 515 
VAL CB  CG1  sing N N 516 
VAL CB  CG2  sing N N 517 
VAL CB  HB   sing N N 518 
VAL CG1 HG11 sing N N 519 
VAL CG1 HG12 sing N N 520 
VAL CG1 HG13 sing N N 521 
VAL CG2 HG21 sing N N 522 
VAL CG2 HG22 sing N N 523 
VAL CG2 HG23 sing N N 524 
VAL OXT HXT  sing N N 525 
# 
_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                    8YYP 
_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]   0.011841 
_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]   0.011841 
_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]   0.007498 
_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  ? 8.586   1.617  -8.253  1.00 94.43  ?  19  PRO A N   1 
ATOM   2    C  CA  . PRO A 1 19  ? 8.016   2.893  -7.776  1.00 88.39  ?  19  PRO A CA  1 
ATOM   3    C  C   . PRO A 1 19  ? 9.068   3.959  -7.403  1.00 82.19  ?  19  PRO A C   1 
ATOM   4    O  O   . PRO A 1 19  ? 9.783   3.765  -6.444  1.00 81.90  ?  19  PRO A O   1 
ATOM   5    C  CB  . PRO A 1 19  ? 7.223   2.423  -6.547  1.00 85.97  ?  19  PRO A CB  1 
ATOM   6    C  CG  . PRO A 1 19  ? 8.064   1.295  -5.959  1.00 89.08  ?  19  PRO A CG  1 
ATOM   7    C  CD  . PRO A 1 19  ? 8.869   0.727  -7.112  1.00 90.61  ?  19  PRO A CD  1 
ATOM   8    N  N   . LEU A 1 20  ? 9.143   5.061  -8.159  1.00 71.23  ?  20  LEU A N   1 
ATOM   9    C  CA  . LEU A 1 20  ? 10.149  6.150  -7.966  1.00 63.79  ?  20  LEU A CA  1 
ATOM   10   C  C   . LEU A 1 20  ? 9.803   7.015  -6.758  1.00 65.46  ?  20  LEU A C   1 
ATOM   11   O  O   . LEU A 1 20  ? 8.637   7.365  -6.578  1.00 69.85  ?  20  LEU A O   1 
ATOM   12   C  CB  . LEU A 1 20  ? 10.175  7.054  -9.201  1.00 56.53  ?  20  LEU A CB  1 
ATOM   13   C  CG  . LEU A 1 20  ? 10.694  6.434  -10.491 1.00 54.09  ?  20  LEU A CG  1 
ATOM   14   C  CD1 . LEU A 1 20  ? 10.937  7.512  -11.534 1.00 56.93  ?  20  LEU A CD1 1 
ATOM   15   C  CD2 . LEU A 1 20  ? 11.967  5.638  -10.265 1.00 53.16  ?  20  LEU A CD2 1 
ATOM   16   N  N   . PRO A 1 21  ? 10.797  7.473  -5.951  1.00 62.14  ?  21  PRO A N   1 
ATOM   17   C  CA  . PRO A 1 21  ? 10.558  8.512  -4.945  1.00 59.13  ?  21  PRO A CA  1 
ATOM   18   C  C   . PRO A 1 21  ? 9.922   9.778  -5.545  1.00 53.74  ?  21  PRO A C   1 
ATOM   19   O  O   . PRO A 1 21  ? 10.274  10.176 -6.657  1.00 57.26  ?  21  PRO A O   1 
ATOM   20   C  CB  . PRO A 1 21  ? 11.956  8.832  -4.379  1.00 57.29  ?  21  PRO A CB  1 
ATOM   21   C  CG  . PRO A 1 21  ? 12.914  8.273  -5.388  1.00 53.22  ?  21  PRO A CG  1 
ATOM   22   C  CD  . PRO A 1 21  ? 12.205  7.061  -5.965  1.00 56.26  ?  21  PRO A CD  1 
ATOM   23   N  N   . ASP A 1 22  ? 8.993   10.385 -4.811  1.00 55.77  ?  22  ASP A N   1 
ATOM   24   C  CA  . ASP A 1 22  ? 8.221   11.560 -5.304  1.00 57.53  ?  22  ASP A CA  1 
ATOM   25   C  C   . ASP A 1 22  ? 8.991   12.855 -5.059  1.00 46.56  ?  22  ASP A C   1 
ATOM   26   O  O   . ASP A 1 22  ? 9.728   12.993 -4.079  1.00 40.57  ?  22  ASP A O   1 
ATOM   27   C  CB  . ASP A 1 22  ? 6.823   11.643 -4.693  1.00 63.18  ?  22  ASP A CB  1 
ATOM   28   C  CG  . ASP A 1 22  ? 5.868   10.681 -5.369  1.00 67.40  ?  22  ASP A CG  1 
ATOM   29   O  OD1 . ASP A 1 22  ? 5.493   10.954 -6.553  1.00 56.57  ?  22  ASP A OD1 1 
ATOM   30   O  OD2 . ASP A 1 22  ? 5.571   9.639  -4.732  1.00 63.68  ?  22  ASP A OD2 1 
ATOM   31   N  N   . PHE A 1 23  ? 8.812   13.780 -5.967  1.00 38.39  ?  23  PHE A N   1 
ATOM   32   C  CA  . PHE A 1 23  ? 9.441   15.104 -5.888  1.00 39.89  ?  23  PHE A CA  1 
ATOM   33   C  C   . PHE A 1 23  ? 8.344   16.080 -6.285  1.00 37.63  ?  23  PHE A C   1 
ATOM   34   O  O   . PHE A 1 23  ? 7.533   15.733 -7.134  1.00 49.87  ?  23  PHE A O   1 
ATOM   35   C  CB  . PHE A 1 23  ? 10.721  15.135 -6.731  1.00 36.18  ?  23  PHE A CB  1 
ATOM   36   C  CG  . PHE A 1 23  ? 11.498  16.392 -6.467  1.00 33.04  ?  23  PHE A CG  1 
ATOM   37   C  CD1 . PHE A 1 23  ? 12.346  16.464 -5.384  1.00 32.34  ?  23  PHE A CD1 1 
ATOM   38   C  CD2 . PHE A 1 23  ? 11.246  17.543 -7.197  1.00 34.94  ?  23  PHE A CD2 1 
ATOM   39   C  CE1 . PHE A 1 23  ? 13.011  17.642 -5.085  1.00 35.49  ?  23  PHE A CE1 1 
ATOM   40   C  CE2 . PHE A 1 23  ? 11.922  18.719 -6.914  1.00 38.84  ?  23  PHE A CE2 1 
ATOM   41   C  CZ  . PHE A 1 23  ? 12.799  18.769 -5.850  1.00 37.87  ?  23  PHE A CZ  1 
ATOM   42   N  N   . PRO A 1 24  ? 8.203   17.266 -5.658  1.00 37.47  ?  24  PRO A N   1 
ATOM   43   C  CA  . PRO A 1 24  ? 9.106   17.741 -4.613  1.00 37.27  ?  24  PRO A CA  1 
ATOM   44   C  C   . PRO A 1 24  ? 8.934   16.955 -3.302  1.00 40.57  ?  24  PRO A C   1 
ATOM   45   O  O   . PRO A 1 24  ? 8.153   16.015 -3.256  1.00 38.44  ?  24  PRO A O   1 
ATOM   46   C  CB  . PRO A 1 24  ? 8.735   19.229 -4.493  1.00 39.91  ?  24  PRO A CB  1 
ATOM   47   C  CG  . PRO A 1 24  ? 7.255   19.280 -4.859  1.00 38.20  ?  24  PRO A CG  1 
ATOM   48   C  CD  . PRO A 1 24  ? 7.095   18.209 -5.914  1.00 40.63  ?  24  PRO A CD  1 
ATOM   49   N  N   . LEU A 1 25  ? 9.689   17.361 -2.291  1.00 42.96  ?  25  LEU A N   1 
ATOM   50   C  CA  . LEU A 1 25  ? 9.598   16.715 -0.964  1.00 45.27  ?  25  LEU A CA  1 
ATOM   51   C  C   . LEU A 1 25  ? 8.700   17.562 -0.053  1.00 46.42  ?  25  LEU A C   1 
ATOM   52   O  O   . LEU A 1 25  ? 8.085   18.507 -0.556  1.00 61.26  ?  25  LEU A O   1 
ATOM   53   C  CB  . LEU A 1 25  ? 11.018  16.577 -0.421  1.00 41.55  ?  25  LEU A CB  1 
ATOM   54   C  CG  . LEU A 1 25  ? 12.077  16.034 -1.385  1.00 40.80  ?  25  LEU A CG  1 
ATOM   55   C  CD1 . LEU A 1 25  ? 13.443  16.112 -0.735  1.00 44.81  ?  25  LEU A CD1 1 
ATOM   56   C  CD2 . LEU A 1 25  ? 11.781  14.609 -1.795  1.00 42.64  ?  25  LEU A CD2 1 
ATOM   57   N  N   . SER A 1 26  ? 8.670   17.258 1.236   1.00 34.45  ?  26  SER A N   1 
ATOM   58   C  CA  . SER A 1 26  ? 7.784   17.959 2.197   1.00 35.48  ?  26  SER A CA  1 
ATOM   59   C  C   . SER A 1 26  ? 7.778   19.481 2.031   1.00 35.25  ?  26  SER A C   1 
ATOM   60   O  O   . SER A 1 26  ? 8.851   20.063 1.847   1.00 40.22  ?  26  SER A O   1 
ATOM   61   C  CB  . SER A 1 26  ? 8.141   17.586 3.604   1.00 32.86  ?  26  SER A CB  1 
ATOM   62   O  OG  . SER A 1 26  ? 9.452   18.023 3.925   1.00 29.89  ?  26  SER A OG  1 
ATOM   63   N  N   . ARG A 1 27  ? 6.604   20.101 2.163   1.00 35.94  ?  27  ARG A N   1 
ATOM   64   C  CA  . ARG A 1 27  ? 6.553   21.586 2.156   1.00 37.49  ?  27  ARG A CA  1 
ATOM   65   C  C   . ARG A 1 27  ? 6.928   22.049 3.572   1.00 35.20  ?  27  ARG A C   1 
ATOM   66   O  O   . ARG A 1 27  ? 7.079   23.272 3.778   1.00 31.59  ?  27  ARG A O   1 
ATOM   67   C  CB  . ARG A 1 27  ? 5.171   22.077 1.713   1.00 40.81  ?  27  ARG A CB  1 
ATOM   68   N  N   . ARG A 1 28  ? 7.076   21.098 4.503   1.00 30.24  ?  28  ARG A N   1 
ATOM   69   C  CA  . ARG A 1 28  ? 7.490   21.438 5.890   1.00 34.67  ?  28  ARG A CA  1 
ATOM   70   C  C   . ARG A 1 28  ? 8.915   21.990 5.847   1.00 32.76  ?  28  ARG A C   1 
ATOM   71   O  O   . ARG A 1 28  ? 9.817   21.267 5.406   1.00 26.77  ?  28  ARG A O   1 
ATOM   72   C  CB  . ARG A 1 28  ? 7.262   20.265 6.848   1.00 35.78  ?  28  ARG A CB  1 
ATOM   73   C  CG  . ARG A 1 28  ? 7.422   20.619 8.317   1.00 37.47  ?  28  ARG A CG  1 
ATOM   74   C  CD  . ARG A 1 28  ? 7.763   19.405 9.158   1.00 40.02  ?  28  ARG A CD  1 
ATOM   75   N  NE  . ARG A 1 28  ? 8.166   19.812 10.507  1.00 39.49  ?  28  ARG A NE  1 
ATOM   76   C  CZ  . ARG A 1 28  ? 7.952   19.124 11.615  1.00 37.56  ?  28  ARG A CZ  1 
ATOM   77   N  NH1 . ARG A 1 28  ? 7.487   17.893 11.549  1.00 38.49  ?  28  ARG A NH1 1 
ATOM   78   N  NH2 . ARG A 1 28  ? 8.219   19.667 12.786  1.00 36.44  ?  28  ARG A NH2 1 
ATOM   79   N  N   . GLY A 1 29  ? 9.097   23.189 6.375   1.00 33.02  ?  29  GLY A N   1 
ATOM   80   C  CA  . GLY A 1 29  ? 10.358  23.926 6.232   1.00 33.60  ?  29  GLY A CA  1 
ATOM   81   C  C   . GLY A 1 29  ? 11.075  24.147 7.545   1.00 33.30  ?  29  GLY A C   1 
ATOM   82   O  O   . GLY A 1 29  ? 12.063  24.868 7.541   1.00 34.32  ?  29  GLY A O   1 
ATOM   83   N  N   . ASP A 1 30  ? 10.652  23.543 8.639   1.00 34.56  ?  30  ASP A N   1 
ATOM   84   C  CA  . ASP A 1 30  ? 11.339  23.797 9.930   1.00 36.23  ?  30  ASP A CA  1 
ATOM   85   C  C   . ASP A 1 30  ? 12.413  22.729 10.167  1.00 38.47  ?  30  ASP A C   1 
ATOM   86   O  O   . ASP A 1 30  ? 13.355  23.080 10.892  1.00 41.99  ?  30  ASP A O   1 
ATOM   87   C  CB  . ASP A 1 30  ? 10.331  23.941 11.066  1.00 37.87  ?  30  ASP A CB  1 
ATOM   88   C  CG  . ASP A 1 30  ? 9.585   22.668 11.425  1.00 36.30  ?  30  ASP A CG  1 
ATOM   89   O  OD1 . ASP A 1 30  ? 8.690   22.273 10.660  1.00 31.88  ?  30  ASP A OD1 1 
ATOM   90   O  OD2 . ASP A 1 30  ? 9.918   22.083 12.478  1.00 37.32  ?  30  ASP A OD2 1 
ATOM   91   N  N   . ILE A 1 31  ? 12.293  21.513 9.582   1.00 39.19  ?  31  ILE A N   1 
ATOM   92   C  CA  . ILE A 1 31  ? 13.317  20.415 9.655   1.00 35.91  ?  31  ILE A CA  1 
ATOM   93   C  C   . ILE A 1 31  ? 13.663  19.923 8.267   1.00 33.58  ?  31  ILE A C   1 
ATOM   94   O  O   . ILE A 1 31  ? 12.776  19.900 7.398   1.00 37.03  ?  31  ILE A O   1 
ATOM   95   C  CB  . ILE A 1 31  ? 12.910  19.141 10.413  1.00 39.59  ?  31  ILE A CB  1 
ATOM   96   C  CG1 . ILE A 1 31  ? 12.706  19.403 11.904  1.00 40.35  ?  31  ILE A CG1 1 
ATOM   97   C  CG2 . ILE A 1 31  ? 13.833  17.964 10.113  1.00 40.14  ?  31  ILE A CG2 1 
ATOM   98   C  CD1 . ILE A 1 31  ? 12.056  18.245 12.622  1.00 44.93  ?  31  ILE A CD1 1 
ATOM   99   N  N   . LEU A 1 32  ? 14.874  19.390 8.142   1.00 29.54  ?  32  LEU A N   1 
ATOM   100  C  CA  . LEU A 1 32  ? 15.309  18.715 6.911   1.00 30.87  ?  32  LEU A CA  1 
ATOM   101  C  C   . LEU A 1 32  ? 14.403  17.507 6.685   1.00 30.03  ?  32  LEU A C   1 
ATOM   102  O  O   . LEU A 1 32  ? 14.219  16.709 7.592   1.00 31.71  ?  32  LEU A O   1 
ATOM   103  C  CB  . LEU A 1 32  ? 16.774  18.292 7.048   1.00 31.15  ?  32  LEU A CB  1 
ATOM   104  C  CG  . LEU A 1 32  ? 17.303  17.522 5.835   1.00 31.12  ?  32  LEU A CG  1 
ATOM   105  C  CD1 . LEU A 1 32  ? 17.426  18.442 4.628   1.00 29.41  ?  32  LEU A CD1 1 
ATOM   106  C  CD2 . LEU A 1 32  ? 18.623  16.834 6.146   1.00 30.97  ?  32  LEU A CD2 1 
ATOM   107  N  N   . PRO A 1 33  ? 13.786  17.334 5.502   1.00 29.65  ?  33  PRO A N   1 
ATOM   108  C  CA  . PRO A 1 33  ? 12.958  16.159 5.258   1.00 29.95  ?  33  PRO A CA  1 
ATOM   109  C  C   . PRO A 1 33  ? 13.807  14.894 5.338   1.00 30.13  ?  33  PRO A C   1 
ATOM   110  O  O   . PRO A 1 33  ? 14.831  14.847 4.713   1.00 36.15  ?  33  PRO A O   1 
ATOM   111  C  CB  . PRO A 1 33  ? 12.361  16.346 3.865   1.00 28.01  ?  33  PRO A CB  1 
ATOM   112  C  CG  . PRO A 1 33  ? 12.541  17.829 3.572   1.00 33.02  ?  33  PRO A CG  1 
ATOM   113  C  CD  . PRO A 1 33  ? 13.742  18.289 4.384   1.00 33.82  ?  33  PRO A CD  1 
ATOM   114  N  N   . ALA A 1 34  ? 13.371  13.943 6.153   1.00 29.90  ?  34  ALA A N   1 
ATOM   115  C  CA  . ALA A 1 34  ? 14.024  12.640 6.370   1.00 31.46  ?  34  ALA A CA  1 
ATOM   116  C  C   . ALA A 1 34  ? 14.388  12.075 5.010   1.00 33.81  ?  34  ALA A C   1 
ATOM   117  O  O   . ALA A 1 34  ? 15.497  11.572 4.889   1.00 40.35  ?  34  ALA A O   1 
ATOM   118  C  CB  . ALA A 1 34  ? 13.121  11.699 7.118   1.00 30.66  ?  34  ALA A CB  1 
ATOM   119  N  N   . GLU A 1 35  ? 13.487  12.194 4.037   1.00 38.58  ?  35  GLU A N   1 
ATOM   120  C  CA  . GLU A 1 35  ? 13.656  11.674 2.651   1.00 41.62  ?  35  GLU A CA  1 
ATOM   121  C  C   . GLU A 1 35  ? 14.962  12.238 2.048   1.00 42.26  ?  35  GLU A C   1 
ATOM   122  O  O   . GLU A 1 35  ? 15.712  11.463 1.481   1.00 44.77  ?  35  GLU A O   1 
ATOM   123  C  CB  . GLU A 1 35  ? 12.381  11.968 1.850   1.00 42.74  ?  35  GLU A CB  1 
ATOM   124  C  CG  . GLU A 1 35  ? 11.140  11.212 2.302   1.00 52.43  ?  35  GLU A CG  1 
ATOM   125  C  CD  . GLU A 1 35  ? 9.846   11.540 1.568   1.00 66.49  ?  35  GLU A CD  1 
ATOM   126  O  OE1 . GLU A 1 35  ? 9.803   12.526 0.775   1.00 63.62  ?  35  GLU A OE1 1 
ATOM   127  O  OE2 . GLU A 1 35  ? 8.870   10.798 1.784   1.00 83.18  ?  35  GLU A OE2 1 
ATOM   128  N  N   . ALA A 1 36  ? 15.260  13.530 2.206   1.00 45.79  ?  36  ALA A N   1 
ATOM   129  C  CA  . ALA A 1 36  ? 16.481  14.179 1.666   1.00 42.43  ?  36  ALA A CA  1 
ATOM   130  C  C   . ALA A 1 36  ? 17.714  13.519 2.270   1.00 42.97  ?  36  ALA A C   1 
ATOM   131  O  O   . ALA A 1 36  ? 18.722  13.421 1.571   1.00 41.22  ?  36  ALA A O   1 
ATOM   132  C  CB  . ALA A 1 36  ? 16.496  15.656 1.945   1.00 41.83  ?  36  ALA A CB  1 
ATOM   133  N  N   . GLU A 1 37  ? 17.627  13.100 3.529   1.00 45.43  ?  37  GLU A N   1 
ATOM   134  C  CA  . GLU A 1 37  ? 18.725  12.388 4.219   1.00 47.15  ?  37  GLU A CA  1 
ATOM   135  C  C   . GLU A 1 37  ? 18.876  10.987 3.611   1.00 44.98  ?  37  GLU A C   1 
ATOM   136  O  O   . GLU A 1 37  ? 20.024  10.579 3.340   1.00 44.03  ?  37  GLU A O   1 
ATOM   137  C  CB  . GLU A 1 37  ? 18.462  12.339 5.721   1.00 53.78  ?  37  GLU A CB  1 
ATOM   138  C  CG  . GLU A 1 37  ? 18.525  13.710 6.365   1.00 67.06  ?  37  GLU A CG  1 
ATOM   139  C  CD  . GLU A 1 37  ? 18.203  13.744 7.847   1.00 74.07  ?  37  GLU A CD  1 
ATOM   140  O  OE1 . GLU A 1 37  ? 17.730  12.704 8.377   1.00 82.37  ?  37  GLU A OE1 1 
ATOM   141  O  OE2 . GLU A 1 37  ? 18.438  14.803 8.466   1.00 81.89  ?  37  GLU A OE2 1 
ATOM   142  N  N   . ARG A 1 38  ? 17.773  10.266 3.403   1.00 44.78  ?  38  ARG A N   1 
ATOM   143  C  CA  . ARG A 1 38  ? 17.829  8.872  2.886   1.00 53.03  ?  38  ARG A CA  1 
ATOM   144  C  C   . ARG A 1 38  ? 18.393  8.911  1.456   1.00 52.99  ?  38  ARG A C   1 
ATOM   145  O  O   . ARG A 1 38  ? 19.283  8.098  1.146   1.00 53.14  ?  38  ARG A O   1 
ATOM   146  C  CB  . ARG A 1 38  ? 16.459  8.194  2.946   1.00 57.23  ?  38  ARG A CB  1 
ATOM   147  C  CG  . ARG A 1 38  ? 16.532  6.672  2.968   1.00 63.44  ?  38  ARG A CG  1 
ATOM   148  C  CD  . ARG A 1 38  ? 15.313  5.952  2.392   1.00 70.87  ?  38  ARG A CD  1 
ATOM   149  N  NE  . ARG A 1 38  ? 14.751  6.626  1.218   1.00 79.11  ?  38  ARG A NE  1 
ATOM   150  C  CZ  . ARG A 1 38  ? 15.305  6.676  -0.002  1.00 76.48  ?  38  ARG A CZ  1 
ATOM   151  N  NH1 . ARG A 1 38  ? 16.458  6.075  -0.257  1.00 78.28  ?  38  ARG A NH1 1 
ATOM   152  N  NH2 . ARG A 1 38  ? 14.701  7.345  -0.969  1.00 72.12  ?  38  ARG A NH2 1 
ATOM   153  N  N   . LEU A 1 39  ? 17.929  9.870  0.647   1.00 46.03  ?  39  LEU A N   1 
ATOM   154  C  CA  . LEU A 1 39  ? 18.360  10.081 -0.757  1.00 44.71  ?  39  LEU A CA  1 
ATOM   155  C  C   . LEU A 1 39  ? 19.854  10.433 -0.812  1.00 42.46  ?  39  LEU A C   1 
ATOM   156  O  O   . LEU A 1 39  ? 20.574  9.790  -1.571  1.00 47.88  ?  39  LEU A O   1 
ATOM   157  C  CB  . LEU A 1 39  ? 17.509  11.176 -1.413  1.00 45.11  ?  39  LEU A CB  1 
ATOM   158  C  CG  . LEU A 1 39  ? 16.151  10.725 -1.945  1.00 40.73  ?  39  LEU A CG  1 
ATOM   159  C  CD1 . LEU A 1 39  ? 15.268  11.930 -2.236  1.00 42.35  ?  39  LEU A CD1 1 
ATOM   160  C  CD2 . LEU A 1 39  ? 16.323  9.868  -3.177  1.00 40.48  ?  39  LEU A CD2 1 
ATOM   161  N  N   . ARG A 1 40  ? 20.304  11.408 -0.023  1.00 42.82  ?  40  ARG A N   1 
ATOM   162  C  CA  . ARG A 1 40  ? 21.748  11.758 -0.018  1.00 43.38  ?  40  ARG A CA  1 
ATOM   163  C  C   . ARG A 1 40  ? 22.584  10.541 0.409   1.00 44.27  ?  40  ARG A C   1 
ATOM   164  O  O   . ARG A 1 40  ? 23.696  10.369 -0.137  1.00 47.44  ?  40  ARG A O   1 
ATOM   165  C  CB  . ARG A 1 40  ? 22.022  12.945 0.914   1.00 40.90  ?  40  ARG A CB  1 
ATOM   166  N  N   . ALA A 1 41  ? 22.059  9.705  1.306   1.00 42.71  ?  41  ALA A N   1 
ATOM   167  C  CA  . ALA A 1 41  ? 22.847  8.588  1.858   1.00 48.28  ?  41  ALA A CA  1 
ATOM   168  C  C   . ALA A 1 41  ? 22.943  7.473  0.824   1.00 49.28  ?  41  ALA A C   1 
ATOM   169  O  O   . ALA A 1 41  ? 24.059  7.038  0.579   1.00 57.79  ?  41  ALA A O   1 
ATOM   170  C  CB  . ALA A 1 41  ? 22.235  8.085  3.140   1.00 55.11  ?  41  ALA A CB  1 
ATOM   171  N  N   . GLU A 1 42  ? 21.816  7.051  0.244   1.00 50.03  ?  42  GLU A N   1 
ATOM   172  C  CA  . GLU A 1 42  ? 21.678  5.746  -0.461  1.00 52.16  ?  42  GLU A CA  1 
ATOM   173  C  C   . GLU A 1 42  ? 21.729  5.913  -1.983  1.00 48.11  ?  42  GLU A C   1 
ATOM   174  O  O   . GLU A 1 42  ? 22.168  4.991  -2.636  1.00 58.75  ?  42  GLU A O   1 
ATOM   175  C  CB  . GLU A 1 42  ? 20.375  5.080  -0.029  1.00 60.26  ?  42  GLU A CB  1 
ATOM   176  C  CG  . GLU A 1 42  ? 20.292  4.883  1.485   1.00 65.10  ?  42  GLU A CG  1 
ATOM   177  C  CD  . GLU A 1 42  ? 19.002  4.260  1.995   1.00 69.74  ?  42  GLU A CD  1 
ATOM   178  O  OE1 . GLU A 1 42  ? 17.993  4.233  1.231   1.00 60.11  ?  42  GLU A OE1 1 
ATOM   179  O  OE2 . GLU A 1 42  ? 19.005  3.814  3.163   1.00 78.01  ?  42  GLU A OE2 1 
ATOM   180  N  N   . GLN A 1 43  ? 21.283  7.032  -2.532  1.00 42.71  ?  43  GLN A N   1 
ATOM   181  C  CA  . GLN A 1 43  ? 21.369  7.281  -3.984  1.00 44.00  ?  43  GLN A CA  1 
ATOM   182  C  C   . GLN A 1 43  ? 21.465  8.782  -4.220  1.00 41.97  ?  43  GLN A C   1 
ATOM   183  O  O   . GLN A 1 43  ? 20.494  9.412  -4.610  1.00 39.63  ?  43  GLN A O   1 
ATOM   184  C  CB  . GLN A 1 43  ? 20.188  6.638  -4.708  1.00 48.00  ?  43  GLN A CB  1 
ATOM   185  C  CG  . GLN A 1 43  ? 20.198  5.117  -4.669  1.00 54.35  ?  43  GLN A CG  1 
ATOM   186  C  CD  . GLN A 1 43  ? 18.988  4.492  -5.326  1.00 62.75  ?  43  GLN A CD  1 
ATOM   187  O  OE1 . GLN A 1 43  ? 17.924  5.108  -5.419  1.00 70.95  ?  43  GLN A OE1 1 
ATOM   188  N  NE2 . GLN A 1 43  ? 19.142  3.266  -5.811  1.00 66.16  ?  43  GLN A NE2 1 
ATOM   189  N  N   . PRO A 1 44  ? 22.666  9.380  -4.054  1.00 42.49  ?  44  PRO A N   1 
ATOM   190  C  CA  . PRO A 1 44  ? 22.824  10.836 -4.095  1.00 43.55  ?  44  PRO A CA  1 
ATOM   191  C  C   . PRO A 1 44  ? 22.622  11.432 -5.503  1.00 41.80  ?  44  PRO A C   1 
ATOM   192  O  O   . PRO A 1 44  ? 22.542  12.654 -5.656  1.00 40.77  ?  44  PRO A O   1 
ATOM   193  C  CB  . PRO A 1 44  ? 24.256  11.032 -3.547  1.00 43.87  ?  44  PRO A CB  1 
ATOM   194  C  CG  . PRO A 1 44  ? 24.985  9.776  -3.948  1.00 41.30  ?  44  PRO A CG  1 
ATOM   195  C  CD  . PRO A 1 44  ? 23.946  8.677  -3.884  1.00 42.36  ?  44  PRO A CD  1 
ATOM   196  N  N   . VAL A 1 45  ? 22.565  10.567 -6.514  1.00 42.16  ?  45  VAL A N   1 
ATOM   197  C  CA  . VAL A 1 45  ? 21.917  10.861 -7.825  1.00 45.00  ?  45  VAL A CA  1 
ATOM   198  C  C   . VAL A 1 45  ? 20.721  9.907  -7.944  1.00 41.65  ?  45  VAL A C   1 
ATOM   199  O  O   . VAL A 1 45  ? 20.976  8.716  -8.011  1.00 41.57  ?  45  VAL A O   1 
ATOM   200  C  CB  . VAL A 1 45  ? 22.935  10.741 -8.974  1.00 47.73  ?  45  VAL A CB  1 
ATOM   201  C  CG1 . VAL A 1 45  ? 22.285  10.914 -10.337 1.00 52.29  ?  45  VAL A CG1 1 
ATOM   202  C  CG2 . VAL A 1 45  ? 24.067  11.741 -8.809  1.00 46.70  ?  45  VAL A CG2 1 
ATOM   203  N  N   . ALA A 1 46  ? 19.478  10.406 -7.853  1.00 39.78  ?  46  ALA A N   1 
ATOM   204  C  CA  . ALA A 1 46  ? 18.253  9.571  -7.769  1.00 41.19  ?  46  ALA A CA  1 
ATOM   205  C  C   . ALA A 1 46  ? 17.258  9.922  -8.886  1.00 41.19  ?  46  ALA A C   1 
ATOM   206  O  O   . ALA A 1 46  ? 17.023  11.121 -9.160  1.00 45.02  ?  46  ALA A O   1 
ATOM   207  C  CB  . ALA A 1 46  ? 17.612  9.697  -6.408  1.00 37.38  ?  46  ALA A CB  1 
ATOM   208  N  N   . ARG A 1 47  ? 16.686  8.893  -9.502  1.00 42.84  ?  47  ARG A N   1 
ATOM   209  C  CA  . ARG A 1 47  ? 15.627  9.020  -10.532 1.00 50.14  ?  47  ARG A CA  1 
ATOM   210  C  C   . ARG A 1 47  ? 14.338  9.317  -9.761  1.00 44.89  ?  47  ARG A C   1 
ATOM   211  O  O   . ARG A 1 47  ? 13.976  8.484  -8.911  1.00 37.63  ?  47  ARG A O   1 
ATOM   212  C  CB  . ARG A 1 47  ? 15.564  7.729  -11.370 1.00 60.84  ?  47  ARG A CB  1 
ATOM   213  C  CG  . ARG A 1 47  ? 16.752  7.451  -12.293 1.00 69.29  ?  47  ARG A CG  1 
ATOM   214  C  CD  . ARG A 1 47  ? 16.532  6.350  -13.325 1.00 75.28  ?  47  ARG A CD  1 
ATOM   215  N  NE  . ARG A 1 47  ? 16.303  5.068  -12.662 1.00 82.15  ?  47  ARG A NE  1 
ATOM   216  C  CZ  . ARG A 1 47  ? 17.252  4.221  -12.258 1.00 82.23  ?  47  ARG A CZ  1 
ATOM   217  N  NH1 . ARG A 1 47  ? 18.528  4.510  -12.464 1.00 82.02  ?  47  ARG A NH1 1 
ATOM   218  N  NH2 . ARG A 1 47  ? 16.916  3.084  -11.658 1.00 75.81  ?  47  ARG A NH2 1 
ATOM   219  N  N   . VAL A 1 48  ? 13.692  10.454 -10.035 1.00 41.29  ?  48  VAL A N   1 
ATOM   220  C  CA  . VAL A 1 48  ? 12.431  10.873 -9.350  1.00 43.40  ?  48  VAL A CA  1 
ATOM   221  C  C   . VAL A 1 48  ? 11.361  11.180 -10.399 1.00 44.01  ?  48  VAL A C   1 
ATOM   222  O  O   . VAL A 1 48  ? 11.728  11.535 -11.527 1.00 42.49  ?  48  VAL A O   1 
ATOM   223  C  CB  . VAL A 1 48  ? 12.648  12.105 -8.458  1.00 40.57  ?  48  VAL A CB  1 
ATOM   224  C  CG1 . VAL A 1 48  ? 13.598  11.817 -7.314  1.00 43.55  ?  48  VAL A CG1 1 
ATOM   225  C  CG2 . VAL A 1 48  ? 13.131  13.284 -9.279  1.00 40.75  ?  48  VAL A CG2 1 
ATOM   226  N  N   . ARG A 1 49  ? 10.089  11.090 -10.004 1.00 46.13  ?  49  ARG A N   1 
ATOM   227  C  CA  . ARG A 1 49  ? 8.950   11.616 -10.795 1.00 48.12  ?  49  ARG A CA  1 
ATOM   228  C  C   . ARG A 1 49  ? 8.596   12.997 -10.266 1.00 44.26  ?  49  ARG A C   1 
ATOM   229  O  O   . ARG A 1 49  ? 8.178   13.068 -9.107  1.00 45.11  ?  49  ARG A O   1 
ATOM   230  C  CB  . ARG A 1 49  ? 7.712   10.731 -10.668 1.00 53.99  ?  49  ARG A CB  1 
ATOM   231  C  CG  . ARG A 1 49  ? 7.876   9.355  -11.299 1.00 58.35  ?  49  ARG A CG  1 
ATOM   232  C  CD  . ARG A 1 49  ? 6.585   8.550  -11.175 1.00 68.10  ?  49  ARG A CD  1 
ATOM   233  N  NE  . ARG A 1 49  ? 6.775   7.203  -11.722 1.00 69.26  ?  49  ARG A NE  1 
ATOM   234  C  CZ  . ARG A 1 49  ? 5.890   6.216  -11.669 1.00 66.69  ?  49  ARG A CZ  1 
ATOM   235  N  NH1 . ARG A 1 49  ? 4.724   6.400  -11.062 1.00 65.26  ?  49  ARG A NH1 1 
ATOM   236  N  NH2 . ARG A 1 49  ? 6.185   5.054  -12.239 1.00 63.15  ?  49  ARG A NH2 1 
ATOM   237  N  N   . THR A 1 50  ? 8.714   14.034 -11.096 1.00 43.48  ?  50  THR A N   1 
ATOM   238  C  CA  . THR A 1 50  ? 8.255   15.410 -10.756 1.00 43.20  ?  50  THR A CA  1 
ATOM   239  C  C   . THR A 1 50  ? 6.725   15.484 -10.794 1.00 40.20  ?  50  THR A C   1 
ATOM   240  O  O   . THR A 1 50  ? 6.060   14.479 -11.143 1.00 33.96  ?  50  THR A O   1 
ATOM   241  C  CB  . THR A 1 50  ? 8.882   16.479 -11.654 1.00 44.12  ?  50  THR A CB  1 
ATOM   242  O  OG1 . THR A 1 50  ? 8.558   16.223 -13.024 1.00 41.39  ?  50  THR A OG1 1 
ATOM   243  C  CG2 . THR A 1 50  ? 10.380  16.571 -11.447 1.00 46.64  ?  50  THR A CG2 1 
ATOM   244  N  N   . MET A 1 51  ? 6.181   16.649 -10.448 1.00 43.99  ?  51  MET A N   1 
ATOM   245  C  CA  . MET A 1 51  ? 4.714   16.802 -10.245 1.00 40.36  ?  51  MET A CA  1 
ATOM   246  C  C   . MET A 1 51  ? 4.078   16.870 -11.640 1.00 42.76  ?  51  MET A C   1 
ATOM   247  O  O   . MET A 1 51  ? 2.827   16.739 -11.710 1.00 39.20  ?  51  MET A O   1 
ATOM   248  C  CB  . MET A 1 51  ? 4.348   18.026 -9.391  1.00 35.03  ?  51  MET A CB  1 
ATOM   249  C  CG  . MET A 1 51  ? 4.402   19.341 -10.148 1.00 36.57  ?  51  MET A CG  1 
ATOM   250  S  SD  . MET A 1 51  ? 4.117   20.834 -9.166  1.00 39.51  ?  51  MET A SD  1 
ATOM   251  C  CE  . MET A 1 51  ? 5.219   20.578 -7.779  1.00 39.26  ?  51  MET A CE  1 
ATOM   252  N  N   . THR A 1 52  ? 4.892   17.040 -12.703 1.00 37.16  ?  52  THR A N   1 
ATOM   253  C  CA  . THR A 1 52  ? 4.393   16.987 -14.101 1.00 37.29  ?  52  THR A CA  1 
ATOM   254  C  C   . THR A 1 52  ? 4.354   15.528 -14.580 1.00 41.88  ?  52  THR A C   1 
ATOM   255  O  O   . THR A 1 52  ? 3.803   15.303 -15.663 1.00 40.94  ?  52  THR A O   1 
ATOM   256  C  CB  . THR A 1 52  ? 5.211   17.833 -15.083 1.00 38.75  ?  52  THR A CB  1 
ATOM   257  O  OG1 . THR A 1 52  ? 6.438   17.150 -15.318 1.00 40.72  ?  52  THR A OG1 1 
ATOM   258  C  CG2 . THR A 1 52  ? 5.470   19.261 -14.638 1.00 39.16  ?  52  THR A CG2 1 
ATOM   259  N  N   . GLY A 1 53  ? 4.923   14.572 -13.834 1.00 40.69  ?  53  GLY A N   1 
ATOM   260  C  CA  . GLY A 1 53  ? 4.943   13.151 -14.239 1.00 43.59  ?  53  GLY A CA  1 
ATOM   261  C  C   . GLY A 1 53  ? 6.152   12.818 -15.109 1.00 43.83  ?  53  GLY A C   1 
ATOM   262  O  O   . GLY A 1 53  ? 6.430   11.610 -15.301 1.00 41.03  ?  53  GLY A O   1 
ATOM   263  N  N   . ASP A 1 54  ? 6.842   13.848 -15.610 1.00 40.93  ?  54  ASP A N   1 
ATOM   264  C  CA  . ASP A 1 54  ? 8.213   13.768 -16.179 1.00 44.60  ?  54  ASP A CA  1 
ATOM   265  C  C   . ASP A 1 54  ? 9.162   13.123 -15.172 1.00 42.47  ?  54  ASP A C   1 
ATOM   266  O  O   . ASP A 1 54  ? 8.862   13.155 -13.981 1.00 45.54  ?  54  ASP A O   1 
ATOM   267  C  CB  . ASP A 1 54  ? 8.750   15.162 -16.524 1.00 44.76  ?  54  ASP A CB  1 
ATOM   268  C  CG  . ASP A 1 54  ? 8.074   15.737 -17.744 1.00 41.77  ?  54  ASP A CG  1 
ATOM   269  O  OD1 . ASP A 1 54  ? 7.643   14.919 -18.550 1.00 46.81  ?  54  ASP A OD1 1 
ATOM   270  O  OD2 . ASP A 1 54  ? 7.993   16.986 -17.877 1.00 40.43  ?  54  ASP A OD2 1 
ATOM   271  N  N   . GLU A 1 55  ? 10.291  12.600 -15.641 1.00 46.16  ?  55  GLU A N   1 
ATOM   272  C  CA  . GLU A 1 55  ? 11.349  12.056 -14.755 1.00 46.87  ?  55  GLU A CA  1 
ATOM   273  C  C   . GLU A 1 55  ? 12.517  13.034 -14.769 1.00 44.79  ?  55  GLU A C   1 
ATOM   274  O  O   . GLU A 1 55  ? 12.608  13.871 -15.703 1.00 36.62  ?  55  GLU A O   1 
ATOM   275  C  CB  . GLU A 1 55  ? 11.776  10.653 -15.171 1.00 51.57  ?  55  GLU A CB  1 
ATOM   276  C  CG  . GLU A 1 55  ? 10.642  9.642  -15.086 1.00 56.58  ?  55  GLU A CG  1 
ATOM   277  C  CD  . GLU A 1 55  ? 10.992  8.205  -15.440 1.00 60.25  ?  55  GLU A CD  1 
ATOM   278  O  OE1 . GLU A 1 55  ? 12.201  7.882  -15.557 1.00 64.87  ?  55  GLU A OE1 1 
ATOM   279  O  OE2 . GLU A 1 55  ? 10.048  7.406  -15.589 1.00 66.26  ?  55  GLU A OE2 1 
ATOM   280  N  N   . ALA A 1 56  ? 13.343  12.954 -13.727 1.00 44.13  ?  56  ALA A N   1 
ATOM   281  C  CA  . ALA A 1 56  ? 14.555  13.780 -13.569 1.00 40.53  ?  56  ALA A CA  1 
ATOM   282  C  C   . ALA A 1 56  ? 15.511  13.052 -12.647 1.00 39.96  ?  56  ALA A C   1 
ATOM   283  O  O   . ALA A 1 56  ? 15.108  12.054 -12.010 1.00 39.59  ?  56  ALA A O   1 
ATOM   284  C  CB  . ALA A 1 56  ? 14.226  15.142 -13.024 1.00 41.37  ?  56  ALA A CB  1 
ATOM   285  N  N   . TRP A 1 57  ? 16.746  13.532 -12.648 1.00 39.70  ?  57  TRP A N   1 
ATOM   286  C  CA  . TRP A 1 57  ? 17.820  13.072 -11.749 1.00 40.78  ?  57  TRP A CA  1 
ATOM   287  C  C   . TRP A 1 57  ? 17.878  14.083 -10.603 1.00 40.28  ?  57  TRP A C   1 
ATOM   288  O  O   . TRP A 1 57  ? 18.121  15.294 -10.892 1.00 43.20  ?  57  TRP A O   1 
ATOM   289  C  CB  . TRP A 1 57  ? 19.151  12.958 -12.519 1.00 39.99  ?  57  TRP A CB  1 
ATOM   290  C  CG  . TRP A 1 57  ? 19.132  11.932 -13.607 1.00 36.71  ?  57  TRP A CG  1 
ATOM   291  C  CD1 . TRP A 1 57  ? 19.132  12.149 -14.960 1.00 37.02  ?  57  TRP A CD1 1 
ATOM   292  C  CD2 . TRP A 1 57  ? 19.064  10.508 -13.434 1.00 32.58  ?  57  TRP A CD2 1 
ATOM   293  N  NE1 . TRP A 1 57  ? 19.079  10.955 -15.635 1.00 33.35  ?  57  TRP A NE1 1 
ATOM   294  C  CE2 . TRP A 1 57  ? 19.044  9.933  -14.723 1.00 33.04  ?  57  TRP A CE2 1 
ATOM   295  C  CE3 . TRP A 1 57  ? 19.009  9.671  -12.330 1.00 32.87  ?  57  TRP A CE3 1 
ATOM   296  C  CZ2 . TRP A 1 57  ? 18.978  8.559  -14.921 1.00 33.76  ?  57  TRP A CZ2 1 
ATOM   297  C  CZ3 . TRP A 1 57  ? 18.965  8.306  -12.526 1.00 36.59  ?  57  TRP A CZ3 1 
ATOM   298  C  CH2 . TRP A 1 57  ? 18.937  7.756  -13.806 1.00 34.01  ?  57  TRP A CH2 1 
ATOM   299  N  N   . LEU A 1 58  ? 17.594  13.635 -9.377  1.00 38.10  ?  58  LEU A N   1 
ATOM   300  C  CA  . LEU A 1 58  ? 17.682  14.492 -8.170  1.00 34.88  ?  58  LEU A CA  1 
ATOM   301  C  C   . LEU A 1 58  ? 19.054  14.247 -7.557  1.00 34.58  ?  58  LEU A C   1 
ATOM   302  O  O   . LEU A 1 58  ? 19.370  13.057 -7.219  1.00 29.92  ?  58  LEU A O   1 
ATOM   303  C  CB  . LEU A 1 58  ? 16.562  14.153 -7.180  1.00 37.49  ?  58  LEU A CB  1 
ATOM   304  C  CG  . LEU A 1 58  ? 16.430  15.090 -5.972  1.00 34.89  ?  58  LEU A CG  1 
ATOM   305  C  CD1 . LEU A 1 58  ? 16.115  16.522 -6.412  1.00 35.08  ?  58  LEU A CD1 1 
ATOM   306  C  CD2 . LEU A 1 58  ? 15.379  14.576 -5.006  1.00 30.22  ?  58  LEU A CD2 1 
ATOM   307  N  N   . VAL A 1 59  ? 19.826  15.324 -7.442  1.00 32.98  ?  59  VAL A N   1 
ATOM   308  C  CA  . VAL A 1 59  ? 21.235  15.292 -6.963  1.00 34.58  ?  59  VAL A CA  1 
ATOM   309  C  C   . VAL A 1 59  ? 21.279  15.922 -5.572  1.00 32.22  ?  59  VAL A C   1 
ATOM   310  O  O   . VAL A 1 59  ? 20.973  17.141 -5.477  1.00 33.94  ?  59  VAL A O   1 
ATOM   311  C  CB  . VAL A 1 59  ? 22.130  16.028 -7.978  1.00 38.61  ?  59  VAL A CB  1 
ATOM   312  C  CG1 . VAL A 1 59  ? 23.614  15.757 -7.704  1.00 39.00  ?  59  VAL A CG1 1 
ATOM   313  C  CG2 . VAL A 1 59  ? 21.733  15.684 -9.423  1.00 34.68  ?  59  VAL A CG2 1 
ATOM   314  N  N   . SER A 1 60  ? 21.625  15.146 -4.539  1.00 31.18  ?  60  SER A N   1 
ATOM   315  C  CA  . SER A 1 60  ? 21.361  15.524 -3.122  1.00 34.84  ?  60  SER A CA  1 
ATOM   316  C  C   . SER A 1 60  ? 22.631  15.558 -2.251  1.00 36.69  ?  60  SER A C   1 
ATOM   317  O  O   . SER A 1 60  ? 22.511  15.988 -1.066  1.00 39.76  ?  60  SER A O   1 
ATOM   318  C  CB  . SER A 1 60  ? 20.286  14.652 -2.516  1.00 34.17  ?  60  SER A CB  1 
ATOM   319  O  OG  . SER A 1 60  ? 20.626  13.282 -2.616  1.00 34.42  ?  60  SER A OG  1 
ATOM   320  N  N   . SER A 1 61  ? 23.788  15.158 -2.782  1.00 34.29  ?  61  SER A N   1 
ATOM   321  C  CA  . SER A 1 61  ? 25.096  15.325 -2.108  1.00 34.71  ?  61  SER A CA  1 
ATOM   322  C  C   . SER A 1 61  ? 25.747  16.605 -2.633  1.00 36.50  ?  61  SER A C   1 
ATOM   323  O  O   . SER A 1 61  ? 25.403  17.069 -3.737  1.00 43.68  ?  61  SER A O   1 
ATOM   324  C  CB  . SER A 1 61  ? 25.980  14.147 -2.296  1.00 36.21  ?  61  SER A CB  1 
ATOM   325  O  OG  . SER A 1 61  ? 26.516  14.154 -3.605  1.00 41.19  ?  61  SER A OG  1 
ATOM   326  N  N   . TYR A 1 62  ? 26.629  17.157 -1.822  1.00 34.38  ?  62  TYR A N   1 
ATOM   327  C  CA  . TYR A 1 62  ? 27.346  18.425 -2.037  1.00 35.16  ?  62  TYR A CA  1 
ATOM   328  C  C   . TYR A 1 62  ? 28.364  18.251 -3.170  1.00 39.38  ?  62  TYR A C   1 
ATOM   329  O  O   . TYR A 1 62  ? 28.429  19.165 -4.003  1.00 37.96  ?  62  TYR A O   1 
ATOM   330  C  CB  . TYR A 1 62  ? 28.001  18.853 -0.717  1.00 32.22  ?  62  TYR A CB  1 
ATOM   331  C  CG  . TYR A 1 62  ? 28.735  20.158 -0.816  1.00 29.23  ?  62  TYR A CG  1 
ATOM   332  C  CD1 . TYR A 1 62  ? 30.031  20.213 -1.320  1.00 29.81  ?  62  TYR A CD1 1 
ATOM   333  C  CD2 . TYR A 1 62  ? 28.149  21.331 -0.414  1.00 25.08  ?  62  TYR A CD2 1 
ATOM   334  C  CE1 . TYR A 1 62  ? 30.731  21.408 -1.406  1.00 26.68  ?  62  TYR A CE1 1 
ATOM   335  C  CE2 . TYR A 1 62  ? 28.833  22.534 -0.511  1.00 28.51  ?  62  TYR A CE2 1 
ATOM   336  C  CZ  . TYR A 1 62  ? 30.130  22.577 -1.002  1.00 26.01  ?  62  TYR A CZ  1 
ATOM   337  O  OH  . TYR A 1 62  ? 30.787  23.765 -1.122  1.00 24.53  ?  62  TYR A OH  1 
ATOM   338  N  N   . GLU A 1 63  ? 29.122  17.161 -3.172  1.00 42.06  ?  63  GLU A N   1 
ATOM   339  C  CA  . GLU A 1 63  ? 30.129  16.900 -4.220  1.00 41.87  ?  63  GLU A CA  1 
ATOM   340  C  C   . GLU A 1 63  ? 29.456  16.966 -5.583  1.00 41.85  ?  63  GLU A C   1 
ATOM   341  O  O   . GLU A 1 63  ? 29.938  17.705 -6.447  1.00 42.64  ?  63  GLU A O   1 
ATOM   342  C  CB  . GLU A 1 63  ? 30.661  15.492 -3.996  1.00 46.62  ?  63  GLU A CB  1 
ATOM   343  C  CG  . GLU A 1 63  ? 32.071  15.279 -4.533  1.00 57.33  ?  63  GLU A CG  1 
ATOM   344  C  CD  . GLU A 1 63  ? 32.624  13.933 -4.106  1.00 69.77  ?  63  GLU A CD  1 
ATOM   345  O  OE1 . GLU A 1 63  ? 33.755  13.887 -3.578  1.00 58.35  ?  63  GLU A OE1 1 
ATOM   346  O  OE2 . GLU A 1 63  ? 31.911  12.928 -4.295  1.00 62.74  ?  63  GLU A OE2 1 
ATOM   347  N  N   . LEU A 1 64  ? 28.366  16.227 -5.742  1.00 37.81  ?  64  LEU A N   1 
ATOM   348  C  CA  . LEU A 1 64  ? 27.687  16.153 -7.052  1.00 37.09  ?  64  LEU A CA  1 
ATOM   349  C  C   . LEU A 1 64  ? 26.827  17.401 -7.291  1.00 38.18  ?  64  LEU A C   1 
ATOM   350  O  O   . LEU A 1 64  ? 26.745  17.826 -8.446  1.00 36.32  ?  64  LEU A O   1 
ATOM   351  C  CB  . LEU A 1 64  ? 26.918  14.838 -7.015  1.00 34.52  ?  64  LEU A CB  1 
ATOM   352  C  CG  . LEU A 1 64  ? 27.778  13.596 -6.770  1.00 37.18  ?  64  LEU A CG  1 
ATOM   353  C  CD1 . LEU A 1 64  ? 26.959  12.331 -6.666  1.00 36.50  ?  64  LEU A CD1 1 
ATOM   354  C  CD2 . LEU A 1 64  ? 28.846  13.458 -7.832  1.00 39.50  ?  64  LEU A CD2 1 
ATOM   355  N  N   . ALA A 1 65  ? 26.227  17.968 -6.246  1.00 40.15  ?  65  ALA A N   1 
ATOM   356  C  CA  . ALA A 1 65  ? 25.483  19.241 -6.414  1.00 40.88  ?  65  ALA A CA  1 
ATOM   357  C  C   . ALA A 1 65  ? 26.453  20.309 -6.930  1.00 40.84  ?  65  ALA A C   1 
ATOM   358  O  O   . ALA A 1 65  ? 26.191  20.880 -8.004  1.00 38.82  ?  65  ALA A O   1 
ATOM   359  C  CB  . ALA A 1 65  ? 24.818  19.670 -5.124  1.00 37.81  ?  65  ALA A CB  1 
ATOM   360  N  N   . LYS A 1 66  ? 27.541  20.548 -6.197  1.00 38.23  ?  66  LYS A N   1 
ATOM   361  C  CA  . LYS A 1 66  ? 28.612  21.495 -6.596  1.00 42.44  ?  66  LYS A CA  1 
ATOM   362  C  C   . LYS A 1 66  ? 29.069  21.222 -8.037  1.00 42.48  ?  66  LYS A C   1 
ATOM   363  O  O   . LYS A 1 66  ? 29.246  22.229 -8.785  1.00 43.62  ?  66  LYS A O   1 
ATOM   364  C  CB  . LYS A 1 66  ? 29.836  21.382 -5.684  1.00 46.34  ?  66  LYS A CB  1 
ATOM   365  C  CG  . LYS A 1 66  ? 30.711  22.626 -5.652  1.00 51.47  ?  66  LYS A CG  1 
ATOM   366  C  CD  . LYS A 1 66  ? 32.184  22.357 -5.809  1.00 54.02  ?  66  LYS A CD  1 
ATOM   367  C  CE  . LYS A 1 66  ? 33.011  23.558 -5.419  1.00 53.88  ?  66  LYS A CE  1 
ATOM   368  N  NZ  . LYS A 1 66  ? 34.425  23.153 -5.293  1.00 58.89  ?  66  LYS A NZ  1 
ATOM   369  N  N   . GLN A 1 67  ? 29.261  19.942 -8.405  1.00 36.39  ?  67  GLN A N   1 
ATOM   370  C  CA  . GLN A 1 67  ? 29.735  19.522 -9.755  1.00 37.42  ?  67  GLN A CA  1 
ATOM   371  C  C   . GLN A 1 67  ? 28.750  19.954 -10.846 1.00 41.63  ?  67  GLN A C   1 
ATOM   372  O  O   . GLN A 1 67  ? 29.220  20.418 -11.878 1.00 51.20  ?  67  GLN A O   1 
ATOM   373  C  CB  . GLN A 1 67  ? 29.961  18.017 -9.843  1.00 38.15  ?  67  GLN A CB  1 
ATOM   374  C  CG  . GLN A 1 67  ? 31.398  17.621 -9.552  1.00 41.62  ?  67  GLN A CG  1 
ATOM   375  C  CD  . GLN A 1 67  ? 31.591  16.136 -9.720  1.00 49.54  ?  67  GLN A CD  1 
ATOM   376  O  OE1 . GLN A 1 67  ? 30.916  15.493 -10.534 1.00 50.51  ?  67  GLN A OE1 1 
ATOM   377  N  NE2 . GLN A 1 67  ? 32.528  15.592 -8.954  1.00 49.57  ?  67  GLN A NE2 1 
ATOM   378  N  N   . VAL A 1 68  ? 27.439  19.784 -10.644 1.00 42.05  ?  68  VAL A N   1 
ATOM   379  C  CA  . VAL A 1 68  ? 26.392  20.126 -11.647 1.00 36.21  ?  68  VAL A CA  1 
ATOM   380  C  C   . VAL A 1 68  ? 26.346  21.645 -11.828 1.00 40.67  ?  68  VAL A C   1 
ATOM   381  O  O   . VAL A 1 68  ? 26.140  22.103 -12.965 1.00 45.71  ?  68  VAL A O   1 
ATOM   382  C  CB  . VAL A 1 68  ? 25.028  19.577 -11.210 1.00 37.25  ?  68  VAL A CB  1 
ATOM   383  C  CG1 . VAL A 1 68  ? 23.889  20.212 -11.999 1.00 36.91  ?  68  VAL A CG1 1 
ATOM   384  C  CG2 . VAL A 1 68  ? 25.000  18.058 -11.290 1.00 38.29  ?  68  VAL A CG2 1 
ATOM   385  N  N   . LEU A 1 69  ? 26.479  22.410 -10.747 1.00 43.25  ?  69  LEU A N   1 
ATOM   386  C  CA  . LEU A 1 69  ? 26.325  23.885 -10.785 1.00 41.87  ?  69  LEU A CA  1 
ATOM   387  C  C   . LEU A 1 69  ? 27.526  24.507 -11.497 1.00 47.42  ?  69  LEU A C   1 
ATOM   388  O  O   . LEU A 1 69  ? 27.360  25.598 -12.060 1.00 50.14  ?  69  LEU A O   1 
ATOM   389  C  CB  . LEU A 1 69  ? 26.188  24.423 -9.359  1.00 42.17  ?  69  LEU A CB  1 
ATOM   390  C  CG  . LEU A 1 69  ? 24.885  24.082 -8.636  1.00 44.33  ?  69  LEU A CG  1 
ATOM   391  C  CD1 . LEU A 1 69  ? 24.723  24.942 -7.391  1.00 44.46  ?  69  LEU A CD1 1 
ATOM   392  C  CD2 . LEU A 1 69  ? 23.688  24.262 -9.548  1.00 42.89  ?  69  LEU A CD2 1 
ATOM   393  N  N   . GLU A 1 70  ? 28.696  23.859 -11.439 1.00 56.66  ?  70  GLU A N   1 
ATOM   394  C  CA  . GLU A 1 70  ? 29.992  24.455 -11.878 1.00 60.13  ?  70  GLU A CA  1 
ATOM   395  C  C   . GLU A 1 70  ? 30.384  23.926 -13.259 1.00 56.12  ?  70  GLU A C   1 
ATOM   396  O  O   . GLU A 1 70  ? 31.377  24.426 -13.792 1.00 64.43  ?  70  GLU A O   1 
ATOM   397  C  CB  . GLU A 1 70  ? 31.101  24.164 -10.862 1.00 58.24  ?  70  GLU A CB  1 
ATOM   398  C  CG  . GLU A 1 70  ? 31.287  25.272 -9.842  1.00 59.70  ?  70  GLU A CG  1 
ATOM   399  C  CD  . GLU A 1 70  ? 32.195  24.921 -8.672  1.00 60.28  ?  70  GLU A CD  1 
ATOM   400  O  OE1 . GLU A 1 70  ? 32.608  23.747 -8.569  1.00 62.01  ?  70  GLU A OE1 1 
ATOM   401  O  OE2 . GLU A 1 70  ? 32.479  25.817 -7.860  1.00 57.26  ?  70  GLU A OE2 1 
ATOM   402  N  N   . ASP A 1 71  ? 29.641  22.947 -13.783 1.00 50.68  ?  71  ASP A N   1 
ATOM   403  C  CA  . ASP A 1 71  ? 29.856  22.304 -15.103 1.00 46.74  ?  71  ASP A CA  1 
ATOM   404  C  C   . ASP A 1 71  ? 28.838  22.871 -16.100 1.00 54.30  ?  71  ASP A C   1 
ATOM   405  O  O   . ASP A 1 71  ? 27.626  22.820 -15.798 1.00 51.76  ?  71  ASP A O   1 
ATOM   406  C  CB  . ASP A 1 71  ? 29.717  20.793 -14.962 1.00 43.55  ?  71  ASP A CB  1 
ATOM   407  C  CG  . ASP A 1 71  ? 29.967  20.027 -16.245 1.00 43.90  ?  71  ASP A CG  1 
ATOM   408  O  OD1 . ASP A 1 71  ? 29.840  20.644 -17.339 1.00 42.50  ?  71  ASP A OD1 1 
ATOM   409  O  OD2 . ASP A 1 71  ? 30.253  18.818 -16.138 1.00 37.13  ?  71  ASP A OD2 1 
ATOM   410  N  N   . ASP A 1 72  ? 29.302  23.348 -17.261 1.00 61.91  ?  72  ASP A N   1 
ATOM   411  C  CA  . ASP A 1 72  ? 28.446  24.046 -18.264 1.00 65.51  ?  72  ASP A CA  1 
ATOM   412  C  C   . ASP A 1 72  ? 27.903  23.048 -19.304 1.00 60.72  ?  72  ASP A C   1 
ATOM   413  O  O   . ASP A 1 72  ? 27.205  23.492 -20.219 1.00 60.43  ?  72  ASP A O   1 
ATOM   414  C  CB  . ASP A 1 72  ? 29.167  25.263 -18.856 1.00 69.16  ?  72  ASP A CB  1 
ATOM   415  C  CG  . ASP A 1 72  ? 29.301  26.406 -17.847 1.00 74.15  ?  72  ASP A CG  1 
ATOM   416  O  OD1 . ASP A 1 72  ? 28.602  26.376 -16.805 1.00 70.08  ?  72  ASP A OD1 1 
ATOM   417  O  OD2 . ASP A 1 72  ? 30.127  27.310 -18.086 1.00 73.62  ?  72  ASP A OD2 1 
ATOM   418  N  N   . ARG A 1 73  ? 28.102  21.742 -19.111 1.00 50.80  ?  73  ARG A N   1 
ATOM   419  C  CA  . ARG A 1 73  ? 27.299  20.700 -19.803 1.00 51.52  ?  73  ARG A CA  1 
ATOM   420  C  C   . ARG A 1 73  ? 25.910  20.512 -19.164 1.00 51.06  ?  73  ARG A C   1 
ATOM   421  O  O   . ARG A 1 73  ? 25.209  19.566 -19.583 1.00 51.60  ?  73  ARG A O   1 
ATOM   422  C  CB  . ARG A 1 73  ? 28.004  19.348 -19.734 1.00 54.30  ?  73  ARG A CB  1 
ATOM   423  C  CG  . ARG A 1 73  ? 29.426  19.377 -20.262 1.00 59.70  ?  73  ARG A CG  1 
ATOM   424  C  CD  . ARG A 1 73  ? 29.987  17.979 -20.339 1.00 53.52  ?  73  ARG A CD  1 
ATOM   425  N  NE  . ARG A 1 73  ? 30.366  17.500 -19.032 1.00 52.31  ?  73  ARG A NE  1 
ATOM   426  C  CZ  . ARG A 1 73  ? 30.863  16.294 -18.813 1.00 53.47  ?  73  ARG A CZ  1 
ATOM   427  N  NH1 . ARG A 1 73  ? 31.021  15.452 -19.822 1.00 59.15  ?  73  ARG A NH1 1 
ATOM   428  N  NH2 . ARG A 1 73  ? 31.211  15.937 -17.595 1.00 48.54  ?  73  ARG A NH2 1 
ATOM   429  N  N   . PHE A 1 74  ? 25.554  21.289 -18.135 1.00 46.71  ?  74  PHE A N   1 
ATOM   430  C  CA  . PHE A 1 74  ? 24.193  21.341 -17.535 1.00 44.18  ?  74  PHE A CA  1 
ATOM   431  C  C   . PHE A 1 74  ? 23.683  22.774 -17.700 1.00 46.88  ?  74  PHE A C   1 
ATOM   432  O  O   . PHE A 1 74  ? 24.342  23.663 -17.088 1.00 47.64  ?  74  PHE A O   1 
ATOM   433  C  CB  . PHE A 1 74  ? 24.215  20.925 -16.064 1.00 41.11  ?  74  PHE A CB  1 
ATOM   434  C  CG  . PHE A 1 74  ? 24.678  19.516 -15.807 1.00 42.08  ?  74  PHE A CG  1 
ATOM   435  C  CD1 . PHE A 1 74  ? 23.847  18.439 -16.068 1.00 38.57  ?  74  PHE A CD1 1 
ATOM   436  C  CD2 . PHE A 1 74  ? 25.947  19.260 -15.297 1.00 45.84  ?  74  PHE A CD2 1 
ATOM   437  C  CE1 . PHE A 1 74  ? 24.261  17.142 -15.813 1.00 38.61  ?  74  PHE A CE1 1 
ATOM   438  C  CE2 . PHE A 1 74  ? 26.374  17.953 -15.071 1.00 47.39  ?  74  PHE A CE2 1 
ATOM   439  C  CZ  . PHE A 1 74  ? 25.528  16.894 -15.325 1.00 42.23  ?  74  PHE A CZ  1 
ATOM   440  N  N   . SER A 1 75  ? 22.621  22.997 -18.506 1.00 42.03  ?  75  SER A N   1 
ATOM   441  C  CA  . SER A 1 75  ? 22.095  24.357 -18.799 1.00 44.45  ?  75  SER A CA  1 
ATOM   442  C  C   . SER A 1 75  ? 20.795  24.667 -18.037 1.00 45.63  ?  75  SER A C   1 
ATOM   443  O  O   . SER A 1 75  ? 19.950  23.767 -17.905 1.00 44.56  ?  75  SER A O   1 
ATOM   444  C  CB  . SER A 1 75  ? 21.879  24.612 -20.258 1.00 44.72  ?  75  SER A CB  1 
ATOM   445  O  OG  . SER A 1 75  ? 21.658  26.015 -20.449 1.00 47.15  ?  75  SER A OG  1 
ATOM   446  N  N   . LEU A 1 76  ? 20.635  25.939 -17.658 1.00 42.35  ?  76  LEU A N   1 
ATOM   447  C  CA  . LEU A 1 76  ? 19.401  26.432 -17.017 1.00 45.20  ?  76  LEU A CA  1 
ATOM   448  C  C   . LEU A 1 76  ? 18.547  27.068 -18.112 1.00 48.89  ?  76  LEU A C   1 
ATOM   449  O  O   . LEU A 1 76  ? 17.337  26.935 -18.082 1.00 56.77  ?  76  LEU A O   1 
ATOM   450  C  CB  . LEU A 1 76  ? 19.834  27.480 -16.004 1.00 45.73  ?  76  LEU A CB  1 
ATOM   451  C  CG  . LEU A 1 76  ? 18.731  28.319 -15.355 1.00 45.52  ?  76  LEU A CG  1 
ATOM   452  C  CD1 . LEU A 1 76  ? 17.766  27.445 -14.582 1.00 44.60  ?  76  LEU A CD1 1 
ATOM   453  C  CD2 . LEU A 1 76  ? 19.372  29.341 -14.442 1.00 45.46  ?  76  LEU A CD2 1 
ATOM   454  N  N   . LYS A 1 77  ? 19.180  27.739 -19.060 1.00 57.26  ?  77  LYS A N   1 
ATOM   455  C  CA  . LYS A 1 77  ? 18.430  28.417 -20.144 1.00 60.10  ?  77  LYS A CA  1 
ATOM   456  C  C   . LYS A 1 77  ? 17.589  27.389 -20.896 1.00 53.19  ?  77  LYS A C   1 
ATOM   457  O  O   . LYS A 1 77  ? 16.439  27.697 -21.254 1.00 47.40  ?  77  LYS A O   1 
ATOM   458  C  CB  . LYS A 1 77  ? 19.441  29.094 -21.070 1.00 69.34  ?  77  LYS A CB  1 
ATOM   459  C  CG  . LYS A 1 77  ? 20.246  30.257 -20.528 1.00 79.01  ?  77  LYS A CG  1 
ATOM   460  C  CD  . LYS A 1 77  ? 21.214  30.786 -21.579 1.00 76.27  ?  77  LYS A CD  1 
ATOM   461  C  CE  . LYS A 1 77  ? 22.011  31.950 -21.092 1.00 76.97  ?  77  LYS A CE  1 
ATOM   462  N  NZ  . LYS A 1 77  ? 22.952  32.430 -22.106 1.00 73.94  ?  77  LYS A NZ  1 
ATOM   463  N  N   . ASP A 1 78  ? 18.144  26.204 -21.098 1.00 51.07  ?  78  ASP A N   1 
ATOM   464  C  CA  . ASP A 1 78  ? 17.440  25.177 -21.901 1.00 52.77  ?  78  ASP A CA  1 
ATOM   465  C  C   . ASP A 1 78  ? 16.280  24.586 -21.099 1.00 52.63  ?  78  ASP A C   1 
ATOM   466  O  O   . ASP A 1 78  ? 15.466  23.868 -21.693 1.00 53.91  ?  78  ASP A O   1 
ATOM   467  C  CB  . ASP A 1 78  ? 18.433  24.162 -22.437 1.00 53.14  ?  78  ASP A CB  1 
ATOM   468  C  CG  . ASP A 1 78  ? 19.258  24.625 -23.628 1.00 56.75  ?  78  ASP A CG  1 
ATOM   469  O  OD1 . ASP A 1 78  ? 19.505  25.841 -23.730 1.00 59.91  ?  78  ASP A OD1 1 
ATOM   470  O  OD2 . ASP A 1 78  ? 19.640  23.765 -24.442 1.00 52.53  ?  78  ASP A OD2 1 
ATOM   471  N  N   . THR A 1 79  ? 16.212  24.866 -19.800 1.00 53.94  ?  79  THR A N   1 
ATOM   472  C  CA  . THR A 1 79  ? 15.137  24.234 -18.980 1.00 49.92  ?  79  THR A CA  1 
ATOM   473  C  C   . THR A 1 79  ? 13.789  24.705 -19.514 1.00 50.32  ?  79  THR A C   1 
ATOM   474  O  O   . THR A 1 79  ? 12.835  23.911 -19.408 1.00 44.95  ?  79  THR A O   1 
ATOM   475  C  CB  . THR A 1 79  ? 15.192  24.533 -17.478 1.00 48.69  ?  79  THR A CB  1 
ATOM   476  O  OG1 . THR A 1 79  ? 15.525  25.910 -17.316 1.00 45.53  ?  79  THR A OG1 1 
ATOM   477  C  CG2 . THR A 1 79  ? 16.148  23.634 -16.725 1.00 50.14  ?  79  THR A CG2 1 
ATOM   478  N  N   . ALA A 1 80  ? 13.759  25.929 -20.062 1.00 48.35  ?  80  ALA A N   1 
ATOM   479  C  CA  . ALA A 1 80  ? 12.563  26.658 -20.540 1.00 48.97  ?  80  ALA A CA  1 
ATOM   480  C  C   . ALA A 1 80  ? 12.219  26.281 -21.990 1.00 55.72  ?  80  ALA A C   1 
ATOM   481  O  O   . ALA A 1 80  ? 11.195  26.759 -22.485 1.00 56.10  ?  80  ALA A O   1 
ATOM   482  C  CB  . ALA A 1 80  ? 12.819  28.137 -20.417 1.00 50.45  ?  80  ALA A CB  1 
ATOM   483  N  N   . ASN A 1 81  ? 13.068  25.470 -22.615 1.00 62.82  ?  81  ASN A N   1 
ATOM   484  C  CA  . ASN A 1 81  ? 12.877  25.102 -24.040 1.00 65.95  ?  81  ASN A CA  1 
ATOM   485  C  C   . ASN A 1 81  ? 11.656  24.198 -24.172 1.00 69.47  ?  81  ASN A C   1 
ATOM   486  O  O   . ASN A 1 81  ? 11.324  23.483 -23.216 1.00 61.65  ?  81  ASN A O   1 
ATOM   487  C  CB  . ASN A 1 81  ? 14.130  24.455 -24.623 1.00 62.08  ?  81  ASN A CB  1 
ATOM   488  C  CG  . ASN A 1 81  ? 15.260  25.435 -24.808 1.00 54.15  ?  81  ASN A CG  1 
ATOM   489  O  OD1 . ASN A 1 81  ? 15.137  26.609 -24.446 1.00 46.92  ?  81  ASN A OD1 1 
ATOM   490  N  ND2 . ASN A 1 81  ? 16.366  24.970 -25.366 1.00 53.49  ?  81  ASN A ND2 1 
ATOM   491  N  N   . PRO A 1 82  ? 10.936  24.219 -25.323 1.00 75.74  ?  82  PRO A N   1 
ATOM   492  C  CA  . PRO A 1 82  ? 9.816   23.318 -25.509 1.00 65.44  ?  82  PRO A CA  1 
ATOM   493  C  C   . PRO A 1 82  ? 10.226  21.881 -25.698 1.00 55.39  ?  82  PRO A C   1 
ATOM   494  O  O   . PRO A 1 82  ? 11.243  21.609 -26.349 1.00 54.17  ?  82  PRO A O   1 
ATOM   495  C  CB  . PRO A 1 82  ? 9.125   23.887 -26.749 1.00 30.00  ?  82  PRO A CB  1 
ATOM   496  C  CG  . PRO A 1 82  ? 10.244  24.472 -27.558 1.00 30.00  ?  82  PRO A CG  1 
ATOM   497  C  CD  . PRO A 1 82  ? 11.084  25.125 -26.489 1.00 30.00  ?  82  PRO A CD  1 
ATOM   498  N  N   . GLY A 1 83  ? 9.465   20.978 -25.098 1.00 48.56  ?  83  GLY A N   1 
ATOM   499  C  CA  . GLY A 1 83  ? 9.697   19.541 -25.301 1.00 47.79  ?  83  GLY A CA  1 
ATOM   500  C  C   . GLY A 1 83  ? 10.508  18.918 -24.198 1.00 49.10  ?  83  GLY A C   1 
ATOM   501  O  O   . GLY A 1 83  ? 10.455  17.687 -24.057 1.00 52.71  ?  83  GLY A O   1 
ATOM   502  N  N   . VAL A 1 84  ? 11.238  19.732 -23.447 1.00 52.10  ?  84  VAL A N   1 
ATOM   503  C  CA  . VAL A 1 84  ? 12.146  19.164 -22.402 1.00 47.68  ?  84  VAL A CA  1 
ATOM   504  C  C   . VAL A 1 84  ? 11.326  18.737 -21.191 1.00 45.52  ?  84  VAL A C   1 
ATOM   505  O  O   . VAL A 1 84  ? 10.249  19.276 -20.936 1.00 39.73  ?  84  VAL A O   1 
ATOM   506  C  CB  . VAL A 1 84  ? 13.250  20.148 -21.989 1.00 53.76  ?  84  VAL A CB  1 
ATOM   507  C  CG1 . VAL A 1 84  ? 14.174  20.492 -23.155 1.00 55.36  ?  84  VAL A CG1 1 
ATOM   508  C  CG2 . VAL A 1 84  ? 12.681  21.401 -21.350 1.00 53.25  ?  84  VAL A CG2 1 
ATOM   509  N  N   . PRO A 1 85  ? 11.796  17.738 -20.409 1.00 42.38  ?  85  PRO A N   1 
ATOM   510  C  CA  . PRO A 1 85  ? 11.145  17.398 -19.149 1.00 41.93  ?  85  PRO A CA  1 
ATOM   511  C  C   . PRO A 1 85  ? 11.219  18.589 -18.185 1.00 41.86  ?  85  PRO A C   1 
ATOM   512  O  O   . PRO A 1 85  ? 12.208  19.323 -18.203 1.00 44.21  ?  85  PRO A O   1 
ATOM   513  C  CB  . PRO A 1 85  ? 11.861  16.151 -18.627 1.00 39.56  ?  85  PRO A CB  1 
ATOM   514  C  CG  . PRO A 1 85  ? 13.152  16.083 -19.424 1.00 41.67  ?  85  PRO A CG  1 
ATOM   515  C  CD  . PRO A 1 85  ? 12.947  16.882 -20.692 1.00 40.10  ?  85  PRO A CD  1 
ATOM   516  N  N   . ARG A 1 86  ? 10.159  18.738 -17.384 1.00 45.94  ?  86  ARG A N   1 
ATOM   517  C  CA  . ARG A 1 86  ? 9.877   19.896 -16.502 1.00 43.21  ?  86  ARG A CA  1 
ATOM   518  C  C   . ARG A 1 86  ? 9.636   19.389 -15.086 1.00 37.39  ?  86  ARG A C   1 
ATOM   519  O  O   . ARG A 1 86  ? 9.004   18.355 -14.964 1.00 38.23  ?  86  ARG A O   1 
ATOM   520  C  CB  . ARG A 1 86  ? 8.628   20.607 -17.020 1.00 50.24  ?  86  ARG A CB  1 
ATOM   521  C  CG  . ARG A 1 86  ? 8.753   21.100 -18.452 1.00 56.14  ?  86  ARG A CG  1 
ATOM   522  C  CD  . ARG A 1 86  ? 8.097   22.434 -18.677 1.00 63.45  ?  86  ARG A CD  1 
ATOM   523  N  NE  . ARG A 1 86  ? 8.497   23.396 -17.650 1.00 84.79  ?  86  ARG A NE  1 
ATOM   524  C  CZ  . ARG A 1 86  ? 9.559   24.207 -17.691 1.00 86.90  ?  86  ARG A CZ  1 
ATOM   525  N  NH1 . ARG A 1 86  ? 10.380  24.194 -18.728 1.00 93.24  ?  86  ARG A NH1 1 
ATOM   526  N  NH2 . ARG A 1 86  ? 9.786   25.042 -16.688 1.00 82.33  ?  86  ARG A NH2 1 
ATOM   527  N  N   . GLN A 1 87  ? 10.075  20.106 -14.054 1.00 36.74  ?  87  GLN A N   1 
ATOM   528  C  CA  . GLN A 1 87  ? 9.653   19.781 -12.663 1.00 36.67  ?  87  GLN A CA  1 
ATOM   529  C  C   . GLN A 1 87  ? 8.287   20.428 -12.394 1.00 36.51  ?  87  GLN A C   1 
ATOM   530  O  O   . GLN A 1 87  ? 7.576   19.978 -11.473 1.00 36.33  ?  87  GLN A O   1 
ATOM   531  C  CB  . GLN A 1 87  ? 10.723  20.138 -11.620 1.00 37.07  ?  87  GLN A CB  1 
ATOM   532  C  CG  . GLN A 1 87  ? 11.070  21.621 -11.491 1.00 34.74  ?  87  GLN A CG  1 
ATOM   533  C  CD  . GLN A 1 87  ? 11.981  21.888 -10.306 1.00 35.16  ?  87  GLN A CD  1 
ATOM   534  O  OE1 . GLN A 1 87  ? 12.086  21.093 -9.365  1.00 36.40  ?  87  GLN A OE1 1 
ATOM   535  N  NE2 . GLN A 1 87  ? 12.660  23.025 -10.340 1.00 32.71  ?  87  GLN A NE2 1 
ATOM   536  N  N   . TYR A 1 88  ? 7.942   21.450 -13.170 1.00 34.02  ?  88  TYR A N   1 
ATOM   537  C  CA  . TYR A 1 88  ? 6.614   22.114 -13.159 1.00 37.27  ?  88  TYR A CA  1 
ATOM   538  C  C   . TYR A 1 88  ? 6.521   23.044 -14.377 1.00 38.50  ?  88  TYR A C   1 
ATOM   539  O  O   . TYR A 1 88  ? 7.557   23.300 -15.042 1.00 35.43  ?  88  TYR A O   1 
ATOM   540  C  CB  . TYR A 1 88  ? 6.351   22.863 -11.850 1.00 33.83  ?  88  TYR A CB  1 
ATOM   541  C  CG  . TYR A 1 88  ? 7.481   23.752 -11.415 1.00 33.21  ?  88  TYR A CG  1 
ATOM   542  C  CD1 . TYR A 1 88  ? 7.718   24.980 -12.028 1.00 33.12  ?  88  TYR A CD1 1 
ATOM   543  C  CD2 . TYR A 1 88  ? 8.330   23.343 -10.397 1.00 33.02  ?  88  TYR A CD2 1 
ATOM   544  C  CE1 . TYR A 1 88  ? 8.773   25.782 -11.627 1.00 32.79  ?  88  TYR A CE1 1 
ATOM   545  C  CE2 . TYR A 1 88  ? 9.382   24.134 -9.981  1.00 32.59  ?  88  TYR A CE2 1 
ATOM   546  C  CZ  . TYR A 1 88  ? 9.604   25.353 -10.600 1.00 32.57  ?  88  TYR A CZ  1 
ATOM   547  O  OH  . TYR A 1 88  ? 10.651  26.100 -10.160 1.00 29.50  ?  88  TYR A OH  1 
ATOM   548  N  N   . ALA A 1 89  ? 5.304   23.510 -14.635 1.00 36.92  ?  89  ALA A N   1 
ATOM   549  C  CA  . ALA A 1 89  ? 4.919   24.340 -15.790 1.00 39.56  ?  89  ALA A CA  1 
ATOM   550  C  C   . ALA A 1 89  ? 5.615   25.678 -15.659 1.00 37.46  ?  89  ALA A C   1 
ATOM   551  O  O   . ALA A 1 89  ? 5.742   26.135 -14.521 1.00 45.45  ?  89  ALA A O   1 
ATOM   552  C  CB  . ALA A 1 89  ? 3.415   24.529 -15.816 1.00 41.66  ?  89  ALA A CB  1 
ATOM   553  N  N   . LEU A 1 90  ? 6.013   26.253 -16.785 1.00 42.76  ?  90  LEU A N   1 
ATOM   554  C  CA  . LEU A 1 90  ? 6.421   27.673 -16.890 1.00 53.69  ?  90  LEU A CA  1 
ATOM   555  C  C   . LEU A 1 90  ? 5.247   28.556 -16.469 1.00 54.69  ?  90  LEU A C   1 
ATOM   556  O  O   . LEU A 1 90  ? 4.079   28.150 -16.715 1.00 57.31  ?  90  LEU A O   1 
ATOM   557  C  CB  . LEU A 1 90  ? 6.836   27.992 -18.333 1.00 63.11  ?  90  LEU A CB  1 
ATOM   558  C  CG  . LEU A 1 90  ? 8.079   27.275 -18.873 1.00 65.77  ?  90  LEU A CG  1 
ATOM   559  C  CD1 . LEU A 1 90  ? 8.251   27.596 -20.352 1.00 70.07  ?  90  LEU A CD1 1 
ATOM   560  C  CD2 . LEU A 1 90  ? 9.350   27.641 -18.111 1.00 63.66  ?  90  LEU A CD2 1 
ATOM   561  N  N   . THR A 1 91  ? 5.555   29.704 -15.852 1.00 53.84  ?  91  THR A N   1 
ATOM   562  C  CA  . THR A 1 91  ? 4.579   30.757 -15.464 1.00 55.41  ?  91  THR A CA  1 
ATOM   563  C  C   . THR A 1 91  ? 4.904   32.084 -16.149 1.00 61.07  ?  91  THR A C   1 
ATOM   564  O  O   . THR A 1 91  ? 4.007   32.935 -16.229 1.00 66.01  ?  91  THR A O   1 
ATOM   565  C  CB  . THR A 1 91  ? 4.583   30.960 -13.947 1.00 56.77  ?  91  THR A CB  1 
ATOM   566  O  OG1 . THR A 1 91  ? 5.840   31.532 -13.599 1.00 50.64  ?  91  THR A OG1 1 
ATOM   567  C  CG2 . THR A 1 91  ? 4.342   29.672 -13.189 1.00 60.90  ?  91  THR A CG2 1 
ATOM   568  N  N   . ILE A 1 92  ? 6.155   32.202 -16.598 1.00 75.57  ?  92  ILE A N   1 
ATOM   569  C  CA  . ILE A 1 92  ? 6.663   33.455 -17.213 1.00 76.92  ?  92  ILE A CA  1 
ATOM   570  C  C   . ILE A 1 92  ? 7.009   33.147 -18.670 1.00 81.25  ?  92  ILE A C   1 
ATOM   571  O  O   . ILE A 1 92  ? 6.968   31.962 -19.042 1.00 76.90  ?  92  ILE A O   1 
ATOM   572  C  CB  . ILE A 1 92  ? 7.900   33.927 -16.428 1.00 77.03  ?  92  ILE A CB  1 
ATOM   573  C  CG1 . ILE A 1 92  ? 9.056   32.942 -16.546 1.00 80.78  ?  92  ILE A CG1 1 
ATOM   574  C  CG2 . ILE A 1 92  ? 7.548   34.207 -14.969 1.00 83.22  ?  92  ILE A CG2 1 
ATOM   575  C  CD1 . ILE A 1 92  ? 10.258  33.301 -15.693 1.00 70.47  ?  92  ILE A CD1 1 
ATOM   576  N  N   . PRO A 1 93  ? 7.311   34.157 -19.511 1.00 109.53 ?  93  PRO A N   1 
ATOM   577  C  CA  . PRO A 1 93  ? 7.716   33.912 -20.887 1.00 117.27 ?  93  PRO A CA  1 
ATOM   578  C  C   . PRO A 1 93  ? 9.035   33.170 -20.947 1.00 121.20 ?  93  PRO A C   1 
ATOM   579  O  O   . PRO A 1 93  ? 9.901   33.360 -20.076 1.00 112.54 ?  93  PRO A O   1 
ATOM   580  C  CB  . PRO A 1 93  ? 7.800   35.315 -21.519 1.00 118.63 ?  93  PRO A CB  1 
ATOM   581  C  CG  . PRO A 1 93  ? 7.925   36.251 -20.345 1.00 113.58 ?  93  PRO A CG  1 
ATOM   582  C  CD  . PRO A 1 93  ? 7.191   35.572 -19.206 1.00 113.74 ?  93  PRO A CD  1 
ATOM   583  N  N   . PRO A 1 94  ? 9.242   32.317 -21.969 1.00 118.30 ?  94  PRO A N   1 
ATOM   584  C  CA  . PRO A 1 94  ? 10.452  31.511 -22.038 1.00 112.75 ?  94  PRO A CA  1 
ATOM   585  C  C   . PRO A 1 94  ? 11.754  32.305 -22.105 1.00 115.93 ?  94  PRO A C   1 
ATOM   586  O  O   . PRO A 1 94  ? 12.800  31.771 -21.700 1.00 119.38 ?  94  PRO A O   1 
ATOM   587  C  CB  . PRO A 1 94  ? 10.197  30.681 -23.307 1.00 106.59 ?  94  PRO A CB  1 
ATOM   588  C  CG  . PRO A 1 94  ? 9.227   31.506 -24.110 1.00 108.20 ?  94  PRO A CG  1 
ATOM   589  C  CD  . PRO A 1 94  ? 8.317   32.099 -23.061 1.00 114.79 ?  94  PRO A CD  1 
ATOM   590  N  N   . GLU A 1 95  ? 11.702  33.551 -22.573 1.00 109.80 ?  95  GLU A N   1 
ATOM   591  C  CA  . GLU A 1 95  ? 12.945  34.342 -22.759 1.00 103.06 ?  95  GLU A CA  1 
ATOM   592  C  C   . GLU A 1 95  ? 13.381  34.975 -21.433 1.00 104.74 ?  95  GLU A C   1 
ATOM   593  O  O   . GLU A 1 95  ? 14.199  35.913 -21.474 1.00 104.26 ?  95  GLU A O   1 
ATOM   594  C  CB  . GLU A 1 95  ? 12.685  35.418 -23.808 1.00 94.68  ?  95  GLU A CB  1 
ATOM   595  C  CG  . GLU A 1 95  ? 12.446  34.847 -25.202 1.00 92.76  ?  95  GLU A CG  1 
ATOM   596  C  CD  . GLU A 1 95  ? 12.116  35.908 -26.235 1.00 85.02  ?  95  GLU A CD  1 
ATOM   597  O  OE1 . GLU A 1 95  ? 11.884  37.071 -25.840 1.00 67.86  ?  95  GLU A OE1 1 
ATOM   598  O  OE2 . GLU A 1 95  ? 12.098  35.574 -27.437 1.00 74.43  ?  95  GLU A OE2 1 
ATOM   599  N  N   . VAL A 1 96  ? 12.878  34.476 -20.306 1.00 107.15 ?  96  VAL A N   1 
ATOM   600  C  CA  . VAL A 1 96  ? 13.175  35.125 -18.983 1.00 102.84 ?  96  VAL A CA  1 
ATOM   601  C  C   . VAL A 1 96  ? 13.828  34.135 -17.997 1.00 96.58  ?  96  VAL A C   1 
ATOM   602  O  O   . VAL A 1 96  ? 14.483  34.624 -17.059 1.00 91.63  ?  96  VAL A O   1 
ATOM   603  C  CB  . VAL A 1 96  ? 11.916  35.770 -18.359 1.00 99.00  ?  96  VAL A CB  1 
ATOM   604  C  CG1 . VAL A 1 96  ? 12.192  36.374 -16.987 1.00 93.62  ?  96  VAL A CG1 1 
ATOM   605  C  CG2 . VAL A 1 96  ? 11.294  36.816 -19.275 1.00 103.45 ?  96  VAL A CG2 1 
ATOM   606  N  N   . VAL A 1 97  ? 13.670  32.811 -18.155 1.00 88.52  ?  97  VAL A N   1 
ATOM   607  C  CA  . VAL A 1 97  ? 14.448  31.808 -17.360 1.00 85.62  ?  97  VAL A CA  1 
ATOM   608  C  C   . VAL A 1 97  ? 15.938  31.931 -17.729 1.00 99.48  ?  97  VAL A C   1 
ATOM   609  O  O   . VAL A 1 97  ? 16.767  31.362 -16.995 1.00 94.50  ?  97  VAL A O   1 
ATOM   610  C  CB  . VAL A 1 97  ? 13.914  30.375 -17.545 1.00 74.95  ?  97  VAL A CB  1 
ATOM   611  C  CG1 . VAL A 1 97  ? 14.844  29.324 -16.947 1.00 64.27  ?  97  VAL A CG1 1 
ATOM   612  C  CG2 . VAL A 1 97  ? 12.510  30.240 -16.968 1.00 77.25  ?  97  VAL A CG2 1 
ATOM   613  N  N   . SER A 1 105 ? 23.519  40.251 -22.793 1.00 121.56 ?  105 SER A N   1 
ATOM   614  C  CA  . SER A 1 105 ? 23.532  40.366 -24.281 1.00 110.18 ?  105 SER A CA  1 
ATOM   615  C  C   . SER A 1 105 ? 23.217  41.799 -24.756 1.00 103.80 ?  105 SER A C   1 
ATOM   616  O  O   . SER A 1 105 ? 23.646  42.144 -25.873 1.00 106.89 ?  105 SER A O   1 
ATOM   617  C  CB  . SER A 1 105 ? 22.594  39.344 -24.915 1.00 98.29  ?  105 SER A CB  1 
ATOM   618  O  OG  . SER A 1 105 ? 21.230  39.625 -24.624 1.00 84.38  ?  105 SER A OG  1 
ATOM   619  N  N   . ALA A 1 106 ? 22.540  42.618 -23.943 1.00 96.72  ?  106 ALA A N   1 
ATOM   620  C  CA  . ALA A 1 106 ? 21.884  43.878 -24.372 1.00 88.74  ?  106 ALA A CA  1 
ATOM   621  C  C   . ALA A 1 106 ? 22.590  45.128 -23.817 1.00 75.23  ?  106 ALA A C   1 
ATOM   622  O  O   . ALA A 1 106 ? 22.001  46.212 -23.956 1.00 62.46  ?  106 ALA A O   1 
ATOM   623  C  CB  . ALA A 1 106 ? 20.432  43.829 -23.947 1.00 91.27  ?  106 ALA A CB  1 
ATOM   624  N  N   . GLY A 1 107 ? 23.777  45.001 -23.206 1.00 71.28  ?  107 GLY A N   1 
ATOM   625  C  CA  . GLY A 1 107 ? 24.482  46.115 -22.535 1.00 72.17  ?  107 GLY A CA  1 
ATOM   626  C  C   . GLY A 1 107 ? 23.625  46.788 -21.461 1.00 81.89  ?  107 GLY A C   1 
ATOM   627  O  O   . GLY A 1 107 ? 23.786  48.006 -21.232 1.00 79.97  ?  107 GLY A O   1 
ATOM   628  N  N   . LEU A 1 108 ? 22.719  46.022 -20.841 1.00 91.00  ?  108 LEU A N   1 
ATOM   629  C  CA  . LEU A 1 108 ? 21.955  46.368 -19.614 1.00 81.25  ?  108 LEU A CA  1 
ATOM   630  C  C   . LEU A 1 108 ? 22.771  45.943 -18.400 1.00 94.80  ?  108 LEU A C   1 
ATOM   631  O  O   . LEU A 1 108 ? 22.491  46.464 -17.305 1.00 101.24 ?  108 LEU A O   1 
ATOM   632  C  CB  . LEU A 1 108 ? 20.646  45.581 -19.589 1.00 78.31  ?  108 LEU A CB  1 
ATOM   633  C  CG  . LEU A 1 108 ? 19.679  45.889 -20.716 1.00 77.35  ?  108 LEU A CG  1 
ATOM   634  C  CD1 . LEU A 1 108 ? 18.567  44.856 -20.768 1.00 73.08  ?  108 LEU A CD1 1 
ATOM   635  C  CD2 . LEU A 1 108 ? 19.130  47.294 -20.540 1.00 86.86  ?  108 LEU A CD2 1 
ATOM   636  N  N   . ARG A 1 109 ? 23.692  44.989 -18.588 1.00 90.93  ?  109 ARG A N   1 
ATOM   637  C  CA  . ARG A 1 109 ? 24.413  44.310 -17.484 1.00 93.51  ?  109 ARG A CA  1 
ATOM   638  C  C   . ARG A 1 109 ? 24.940  45.360 -16.513 1.00 85.33  ?  109 ARG A C   1 
ATOM   639  O  O   . ARG A 1 109 ? 25.052  45.052 -15.320 1.00 96.87  ?  109 ARG A O   1 
ATOM   640  C  CB  . ARG A 1 109 ? 25.592  43.463 -17.975 1.00 104.67 ?  109 ARG A CB  1 
ATOM   641  C  CG  . ARG A 1 109 ? 26.092  42.484 -16.920 1.00 103.74 ?  109 ARG A CG  1 
ATOM   642  C  CD  . ARG A 1 109 ? 27.385  41.775 -17.268 1.00 101.93 ?  109 ARG A CD  1 
ATOM   643  N  NE  . ARG A 1 109 ? 28.003  41.246 -16.061 1.00 104.88 ?  109 ARG A NE  1 
ATOM   644  C  CZ  . ARG A 1 109 ? 27.547  40.219 -15.343 1.00 104.47 ?  109 ARG A CZ  1 
ATOM   645  N  NH1 . ARG A 1 109 ? 26.448  39.569 -15.698 1.00 99.74  ?  109 ARG A NH1 1 
ATOM   646  N  NH2 . ARG A 1 109 ? 28.197  39.851 -14.251 1.00 101.91 ?  109 ARG A NH2 1 
ATOM   647  N  N   . ASN A 1 110 ? 25.270  46.545 -17.013 1.00 81.11  ?  110 ASN A N   1 
ATOM   648  C  CA  . ASN A 1 110 ? 25.817  47.633 -16.168 1.00 82.56  ?  110 ASN A CA  1 
ATOM   649  C  C   . ASN A 1 110 ? 24.685  48.258 -15.319 1.00 79.22  ?  110 ASN A C   1 
ATOM   650  O  O   . ASN A 1 110 ? 24.901  48.437 -14.096 1.00 71.30  ?  110 ASN A O   1 
ATOM   651  C  CB  . ASN A 1 110 ? 26.621  48.622 -17.013 1.00 77.74  ?  110 ASN A CB  1 
ATOM   652  C  CG  . ASN A 1 110 ? 27.913  47.992 -17.468 1.00 80.95  ?  110 ASN A CG  1 
ATOM   653  O  OD1 . ASN A 1 110 ? 28.385  47.048 -16.839 1.00 87.48  ?  110 ASN A OD1 1 
ATOM   654  N  ND2 . ASN A 1 110 ? 28.531  48.567 -18.492 1.00 75.71  ?  110 ASN A ND2 1 
ATOM   655  N  N   . ALA A 1 111 ? 23.521  48.564 -15.913 1.00 70.92  ?  111 ALA A N   1 
ATOM   656  C  CA  . ALA A 1 111 ? 22.340  49.144 -15.220 1.00 69.94  ?  111 ALA A CA  1 
ATOM   657  C  C   . ALA A 1 111 ? 21.847  48.176 -14.134 1.00 65.14  ?  111 ALA A C   1 
ATOM   658  O  O   . ALA A 1 111 ? 21.570  48.642 -13.021 1.00 58.71  ?  111 ALA A O   1 
ATOM   659  C  CB  . ALA A 1 111 ? 21.240  49.449 -16.212 1.00 69.79  ?  111 ALA A CB  1 
ATOM   660  N  N   . VAL A 1 112 ? 21.744  46.881 -14.464 1.00 60.53  ?  112 VAL A N   1 
ATOM   661  C  CA  . VAL A 1 112 ? 21.225  45.811 -13.564 1.00 62.25  ?  112 VAL A CA  1 
ATOM   662  C  C   . VAL A 1 112 ? 22.257  45.567 -12.458 1.00 65.39  ?  112 VAL A C   1 
ATOM   663  O  O   . VAL A 1 112 ? 21.846  45.621 -11.277 1.00 68.30  ?  112 VAL A O   1 
ATOM   664  C  CB  . VAL A 1 112 ? 20.861  44.524 -14.331 1.00 58.25  ?  112 VAL A CB  1 
ATOM   665  C  CG1 . VAL A 1 112 ? 20.447  43.390 -13.412 1.00 61.18  ?  112 VAL A CG1 1 
ATOM   666  C  CG2 . VAL A 1 112 ? 19.771  44.782 -15.349 1.00 58.40  ?  112 VAL A CG2 1 
ATOM   667  N  N   . MET A 1 113 ? 23.532  45.339 -12.806 1.00 62.85  ?  113 MET A N   1 
ATOM   668  C  CA  . MET A 1 113 ? 24.585  44.984 -11.810 1.00 64.69  ?  113 MET A CA  1 
ATOM   669  C  C   . MET A 1 113 ? 24.852  46.179 -10.889 1.00 55.56  ?  113 MET A C   1 
ATOM   670  O  O   . MET A 1 113 ? 25.145  45.930 -9.704  1.00 51.75  ?  113 MET A O   1 
ATOM   671  C  CB  . MET A 1 113 ? 25.900  44.516 -12.452 1.00 72.52  ?  113 MET A CB  1 
ATOM   672  C  CG  . MET A 1 113 ? 25.887  43.046 -12.907 1.00 82.81  ?  113 MET A CG  1 
ATOM   673  S  SD  . MET A 1 113 ? 25.057  41.859 -11.768 1.00 93.53  ?  113 MET A SD  1 
ATOM   674  C  CE  . MET A 1 113 ? 25.914  42.164 -10.218 1.00 90.44  ?  113 MET A CE  1 
ATOM   675  N  N   . LYS A 1 114 ? 24.725  47.410 -11.396 1.00 56.63  ?  114 LYS A N   1 
ATOM   676  C  CA  . LYS A 1 114 ? 24.871  48.649 -10.585 1.00 64.04  ?  114 LYS A CA  1 
ATOM   677  C  C   . LYS A 1 114 ? 23.714  48.721 -9.579  1.00 61.01  ?  114 LYS A C   1 
ATOM   678  O  O   . LYS A 1 114 ? 23.938  49.226 -8.472  1.00 66.27  ?  114 LYS A O   1 
ATOM   679  C  CB  . LYS A 1 114 ? 24.932  49.931 -11.438 1.00 74.71  ?  114 LYS A CB  1 
ATOM   680  C  CG  . LYS A 1 114 ? 26.160  50.125 -12.339 1.00 84.11  ?  114 LYS A CG  1 
ATOM   681  C  CD  . LYS A 1 114 ? 26.198  51.394 -13.202 1.00 92.60  ?  114 LYS A CD  1 
ATOM   682  C  CE  . LYS A 1 114 ? 27.448  51.539 -14.051 1.00 96.33  ?  114 LYS A CE  1 
ATOM   683  N  NZ  . LYS A 1 114 ? 27.420  52.769 -14.880 1.00 93.57  ?  114 LYS A NZ  1 
ATOM   684  N  N   . THR A 1 115 ? 22.520  48.243 -9.935  1.00 57.10  ?  115 THR A N   1 
ATOM   685  C  CA  . THR A 1 115 ? 21.341  48.277 -9.036  1.00 55.83  ?  115 THR A CA  1 
ATOM   686  C  C   . THR A 1 115 ? 21.522  47.234 -7.922  1.00 51.73  ?  115 THR A C   1 
ATOM   687  O  O   . THR A 1 115 ? 21.279  47.609 -6.761  1.00 48.11  ?  115 THR A O   1 
ATOM   688  C  CB  . THR A 1 115 ? 20.024  48.089 -9.805  1.00 64.62  ?  115 THR A CB  1 
ATOM   689  O  OG1 . THR A 1 115 ? 19.989  48.934 -10.958 1.00 61.93  ?  115 THR A OG1 1 
ATOM   690  C  CG2 . THR A 1 115 ? 18.829  48.393 -8.925  1.00 65.50  ?  115 THR A CG2 1 
ATOM   691  N  N   . LEU A 1 116 ? 21.965  46.008 -8.257  1.00 48.11  ?  116 LEU A N   1 
ATOM   692  C  CA  . LEU A 1 116 ? 22.172  44.858 -7.318  1.00 53.77  ?  116 LEU A CA  1 
ATOM   693  C  C   . LEU A 1 116 ? 23.416  45.041 -6.425  1.00 60.16  ?  116 LEU A C   1 
ATOM   694  O  O   . LEU A 1 116 ? 23.747  44.100 -5.682  1.00 63.53  ?  116 LEU A O   1 
ATOM   695  C  CB  . LEU A 1 116 ? 22.300  43.553 -8.116  1.00 50.78  ?  116 LEU A CB  1 
ATOM   696  C  CG  . LEU A 1 116 ? 21.089  43.178 -8.971  1.00 54.89  ?  116 LEU A CG  1 
ATOM   697  C  CD1 . LEU A 1 116 ? 21.324  41.878 -9.745  1.00 52.47  ?  116 LEU A CD1 1 
ATOM   698  C  CD2 . LEU A 1 116 ? 19.830  43.087 -8.120  1.00 53.75  ?  116 LEU A CD2 1 
ATOM   699  N  N   . SER A 1 117 ? 24.058  46.205 -6.517  1.00 68.33  ?  117 SER A N   1 
ATOM   700  C  CA  . SER A 1 117 ? 25.223  46.526 -5.660  1.00 73.40  ?  117 SER A CA  1 
ATOM   701  C  C   . SER A 1 117 ? 24.749  47.415 -4.506  1.00 79.76  ?  117 SER A C   1 
ATOM   702  O  O   . SER A 1 117 ? 24.450  48.594 -4.761  1.00 85.82  ?  117 SER A O   1 
ATOM   703  C  CB  . SER A 1 117 ? 26.289  47.216 -6.445  1.00 69.46  ?  117 SER A CB  1 
ATOM   704  O  OG  . SER A 1 117 ? 25.830  48.472 -6.920  1.00 76.66  ?  117 SER A OG  1 
ATOM   705  N  N   . PRO A 1 118 ? 24.679  46.907 -3.255  1.00 83.42  ?  118 PRO A N   1 
ATOM   706  C  CA  . PRO A 1 118 ? 24.208  47.691 -2.124  1.00 73.78  ?  118 PRO A CA  1 
ATOM   707  C  C   . PRO A 1 118 ? 25.019  48.956 -1.994  1.00 86.44  ?  118 PRO A C   1 
ATOM   708  O  O   . PRO A 1 118 ? 24.592  49.880 -1.278  1.00 87.01  ?  118 PRO A O   1 
ATOM   709  C  CB  . PRO A 1 118 ? 24.449  46.746 -0.944  1.00 69.68  ?  118 PRO A CB  1 
ATOM   710  C  CG  . PRO A 1 118 ? 24.381  45.369 -1.548  1.00 71.50  ?  118 PRO A CG  1 
ATOM   711  C  CD  . PRO A 1 118 ? 25.042  45.546 -2.897  1.00 78.74  ?  118 PRO A CD  1 
ATOM   712  N  N   . GLN A 1 119 ? 26.170  49.000 -2.662  1.00 75.52  ?  119 GLN A N   1 
ATOM   713  C  CA  . GLN A 1 119 ? 27.074  50.163 -2.566  1.00 78.98  ?  119 GLN A CA  1 
ATOM   714  C  C   . GLN A 1 119 ? 26.843  51.086 -3.765  1.00 74.24  ?  119 GLN A C   1 
ATOM   715  O  O   . GLN A 1 119 ? 27.827  51.656 -4.261  1.00 71.29  ?  119 GLN A O   1 
ATOM   716  C  CB  . GLN A 1 119 ? 28.474  49.569 -2.474  1.00 93.04  ?  119 GLN A CB  1 
ATOM   717  C  CG  . GLN A 1 119 ? 28.736  48.796 -1.186  1.00 97.34  ?  119 GLN A CG  1 
ATOM   718  C  CD  . GLN A 1 119 ? 30.105  48.153 -1.144  1.00 97.87  ?  119 GLN A CD  1 
ATOM   719  O  OE1 . GLN A 1 119 ? 30.715  47.864 -2.180  1.00 95.44  ?  119 GLN A OE1 1 
ATOM   720  N  NE2 . GLN A 1 119 ? 30.602  47.923 0.063   1.00 96.10  ?  119 GLN A NE2 1 
ATOM   721  N  N   . ALA A 1 120 ? 25.598  51.197 -4.221  1.00 77.88  ?  120 ALA A N   1 
ATOM   722  C  CA  . ALA A 1 120 ? 25.238  52.141 -5.303  1.00 65.74  ?  120 ALA A CA  1 
ATOM   723  C  C   . ALA A 1 120 ? 23.924  52.793 -4.884  1.00 68.09  ?  120 ALA A C   1 
ATOM   724  O  O   . ALA A 1 120 ? 23.340  53.547 -5.683  1.00 58.11  ?  120 ALA A O   1 
ATOM   725  C  CB  . ALA A 1 120 ? 25.112  51.417 -6.607  1.00 59.47  ?  120 ALA A CB  1 
ATOM   726  N  N   . ASP A 1 121 ? 23.443  52.428 -3.690  1.00 72.57  ?  121 ASP A N   1 
ATOM   727  C  CA  . ASP A 1 121 ? 22.198  53.015 -3.127  1.00 70.86  ?  121 ASP A CA  1 
ATOM   728  C  C   . ASP A 1 121 ? 22.580  53.621 -1.777  1.00 72.75  ?  121 ASP A C   1 
ATOM   729  O  O   . ASP A 1 121 ? 21.779  54.415 -1.244  1.00 90.29  ?  121 ASP A O   1 
ATOM   730  C  CB  . ASP A 1 121 ? 21.100  51.971 -3.010  1.00 68.52  ?  121 ASP A CB  1 
ATOM   731  C  CG  . ASP A 1 121 ? 19.675  52.499 -3.088  1.00 62.08  ?  121 ASP A CG  1 
ATOM   732  O  OD1 . ASP A 1 121 ? 19.510  53.733 -3.188  1.00 61.33  ?  121 ASP A OD1 1 
ATOM   733  O  OD2 . ASP A 1 121 ? 18.743  51.671 -3.052  1.00 62.33  ?  121 ASP A OD2 1 
ATOM   734  N  N   . ARG A 1 122 ? 23.779  53.303 -1.290  1.00 73.42  ?  122 ARG A N   1 
ATOM   735  C  CA  . ARG A 1 122 ? 24.309  53.921 -0.048  1.00 79.48  ?  122 ARG A CA  1 
ATOM   736  C  C   . ARG A 1 122 ? 23.253  53.983 1.060   1.00 78.71  ?  122 ARG A C   1 
ATOM   737  O  O   . ARG A 1 122 ? 23.295  53.118 1.950   1.00 98.54  ?  122 ARG A O   1 
ATOM   738  C  CB  . ARG A 1 122 ? 24.836  55.319 -0.379  1.00 79.38  ?  122 ARG A CB  1 
ATOM   739  N  N   . GLU A 1 123 ? 22.373  54.976 1.029   1.00 65.35  ?  123 GLU A N   1 
ATOM   740  C  CA  . GLU A 1 123 ? 21.371  55.158 2.108   1.00 61.68  ?  123 GLU A CA  1 
ATOM   741  C  C   . GLU A 1 123 ? 20.536  53.884 2.320   1.00 50.99  ?  123 GLU A C   1 
ATOM   742  O  O   . GLU A 1 123 ? 19.880  53.809 3.361   1.00 42.99  ?  123 GLU A O   1 
ATOM   743  C  CB  . GLU A 1 123 ? 20.594  56.433 1.799   1.00 63.87  ?  123 GLU A CB  1 
ATOM   744  C  CG  . GLU A 1 123 ? 21.449  57.690 1.906   1.00 63.34  ?  123 GLU A CG  1 
ATOM   745  C  CD  . GLU A 1 123 ? 20.674  58.934 1.524   1.00 75.55  ?  123 GLU A CD  1 
ATOM   746  O  OE1 . GLU A 1 123 ? 19.550  58.784 1.002   1.00 79.55  ?  123 GLU A OE1 1 
ATOM   747  O  OE2 . GLU A 1 123 ? 21.197  60.047 1.737   1.00 78.39  ?  123 GLU A OE2 1 
ATOM   748  N  N   . LEU A 1 124 ? 20.587  52.924 1.393   1.00 47.40  ?  124 LEU A N   1 
ATOM   749  C  CA  . LEU A 1 124 ? 19.825  51.659 1.533   1.00 47.05  ?  124 LEU A CA  1 
ATOM   750  C  C   . LEU A 1 124 ? 19.906  51.125 2.958   1.00 42.91  ?  124 LEU A C   1 
ATOM   751  O  O   . LEU A 1 124 ? 18.849  50.942 3.570   1.00 42.33  ?  124 LEU A O   1 
ATOM   752  C  CB  . LEU A 1 124 ? 20.361  50.633 0.545   1.00 50.50  ?  124 LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 124 ? 19.446  49.439 0.269   1.00 53.54  ?  124 LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 124 ? 18.074  49.915 -0.161  1.00 53.20  ?  124 LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 124 ? 20.058  48.540 -0.781  1.00 53.74  ?  124 LEU A CD2 1 
ATOM   756  N  N   . GLY A 1 125 ? 21.120  50.893 3.447   1.00 39.82  ?  125 GLY A N   1 
ATOM   757  C  CA  . GLY A 1 125 ? 21.329  50.406 4.830   1.00 40.01  ?  125 GLY A CA  1 
ATOM   758  C  C   . GLY A 1 125 ? 20.469  51.121 5.871   1.00 39.26  ?  125 GLY A C   1 
ATOM   759  O  O   . GLY A 1 125 ? 19.636  50.452 6.511   1.00 47.72  ?  125 GLY A O   1 
ATOM   760  N  N   . GLY A 1 126 ? 20.660  52.432 6.052   1.00 36.75  ?  126 GLY A N   1 
ATOM   761  C  CA  . GLY A 1 126 ? 19.868  53.270 6.976   1.00 35.41  ?  126 GLY A CA  1 
ATOM   762  C  C   . GLY A 1 126 ? 18.389  53.356 6.601   1.00 34.86  ?  126 GLY A C   1 
ATOM   763  O  O   . GLY A 1 126 ? 17.581  53.551 7.498   1.00 37.11  ?  126 GLY A O   1 
ATOM   764  N  N   . TRP A 1 127 ? 18.031  53.199 5.327   1.00 40.63  ?  127 TRP A N   1 
ATOM   765  C  CA  . TRP A 1 127 ? 16.620  53.237 4.852   1.00 43.86  ?  127 TRP A CA  1 
ATOM   766  C  C   . TRP A 1 127 ? 15.899  51.927 5.216   1.00 42.19  ?  127 TRP A C   1 
ATOM   767  O  O   . TRP A 1 127 ? 14.860  52.004 5.891   1.00 36.99  ?  127 TRP A O   1 
ATOM   768  C  CB  . TRP A 1 127 ? 16.561  53.528 3.343   1.00 46.04  ?  127 TRP A CB  1 
ATOM   769  C  CG  . TRP A 1 127 ? 15.161  53.662 2.812   1.00 49.02  ?  127 TRP A CG  1 
ATOM   770  C  CD1 . TRP A 1 127 ? 14.350  54.761 2.884   1.00 49.83  ?  127 TRP A CD1 1 
ATOM   771  C  CD2 . TRP A 1 127 ? 14.387  52.640 2.154   1.00 48.16  ?  127 TRP A CD2 1 
ATOM   772  N  NE1 . TRP A 1 127 ? 13.133  54.495 2.311   1.00 53.87  ?  127 TRP A NE1 1 
ATOM   773  C  CE2 . TRP A 1 127 ? 13.127  53.203 1.851   1.00 52.69  ?  127 TRP A CE2 1 
ATOM   774  C  CE3 . TRP A 1 127 ? 14.621  51.305 1.823   1.00 42.92  ?  127 TRP A CE3 1 
ATOM   775  C  CZ2 . TRP A 1 127 ? 12.129  52.484 1.196   1.00 50.81  ?  127 TRP A CZ2 1 
ATOM   776  C  CZ3 . TRP A 1 127 ? 13.639  50.598 1.169   1.00 43.90  ?  127 TRP A CZ3 1 
ATOM   777  C  CH2 . TRP A 1 127 ? 12.408  51.178 0.864   1.00 46.92  ?  127 TRP A CH2 1 
ATOM   778  N  N   . LEU A 1 128 ? 16.436  50.779 4.780   1.00 38.91  ?  128 LEU A N   1 
ATOM   779  C  CA  . LEU A 1 128 ? 15.943  49.425 5.146   1.00 38.36  ?  128 LEU A CA  1 
ATOM   780  C  C   . LEU A 1 128 ? 15.836  49.313 6.661   1.00 40.73  ?  128 LEU A C   1 
ATOM   781  O  O   . LEU A 1 128 ? 14.954  48.579 7.129   1.00 42.80  ?  128 LEU A O   1 
ATOM   782  C  CB  . LEU A 1 128 ? 16.941  48.362 4.694   1.00 39.44  ?  128 LEU A CB  1 
ATOM   783  C  CG  . LEU A 1 128 ? 17.022  48.080 3.203   1.00 38.82  ?  128 LEU A CG  1 
ATOM   784  C  CD1 . LEU A 1 128 ? 18.036  46.961 2.944   1.00 35.69  ?  128 LEU A CD1 1 
ATOM   785  C  CD2 . LEU A 1 128 ? 15.645  47.744 2.650   1.00 37.10  ?  128 LEU A CD2 1 
ATOM   786  N  N   . GLU A 1 129 ? 16.758  49.945 7.391   1.00 39.22  ?  129 GLU A N   1 
ATOM   787  C  CA  . GLU A 1 129 ? 16.757  49.890 8.873   1.00 39.90  ?  129 GLU A CA  1 
ATOM   788  C  C   . GLU A 1 129 ? 15.594  50.736 9.401   1.00 43.69  ?  129 GLU A C   1 
ATOM   789  O  O   . GLU A 1 129 ? 14.976  50.325 10.395  1.00 49.73  ?  129 GLU A O   1 
ATOM   790  C  CB  . GLU A 1 129 ? 18.111  50.315 9.435   1.00 39.64  ?  129 GLU A CB  1 
ATOM   791  C  CG  . GLU A 1 129 ? 18.076  50.512 10.929  1.00 40.34  ?  129 GLU A CG  1 
ATOM   792  C  CD  . GLU A 1 129 ? 19.327  51.148 11.490  1.00 43.51  ?  129 GLU A CD  1 
ATOM   793  O  OE1 . GLU A 1 129 ? 19.932  51.949 10.773  1.00 54.77  ?  129 GLU A OE1 1 
ATOM   794  O  OE2 . GLU A 1 129 ? 19.685  50.839 12.641  1.00 47.77  ?  129 GLU A OE2 1 
ATOM   795  N  N   . ALA A 1 130 ? 15.304  51.885 8.785   1.00 45.37  ?  130 ALA A N   1 
ATOM   796  C  CA  . ALA A 1 130 ? 14.132  52.719 9.143   1.00 46.77  ?  130 ALA A CA  1 
ATOM   797  C  C   . ALA A 1 130 ? 12.855  51.919 8.844   1.00 45.44  ?  130 ALA A C   1 
ATOM   798  O  O   . ALA A 1 130 ? 11.944  52.000 9.657   1.00 44.43  ?  130 ALA A O   1 
ATOM   799  C  CB  . ALA A 1 130 ? 14.171  54.027 8.393   1.00 47.09  ?  130 ALA A CB  1 
ATOM   800  N  N   . GLN A 1 131 ? 12.823  51.167 7.731   1.00 43.22  ?  131 GLN A N   1 
ATOM   801  C  CA  . GLN A 1 131 ? 11.679  50.329 7.295   1.00 43.31  ?  131 GLN A CA  1 
ATOM   802  C  C   . GLN A 1 131 ? 11.404  49.248 8.349   1.00 43.02  ?  131 GLN A C   1 
ATOM   803  O  O   . GLN A 1 131 ? 10.249  49.149 8.836   1.00 40.23  ?  131 GLN A O   1 
ATOM   804  C  CB  . GLN A 1 131 ? 11.995  49.702 5.941   1.00 48.18  ?  131 GLN A CB  1 
ATOM   805  C  CG  . GLN A 1 131 ? 12.004  50.710 4.812   1.00 57.71  ?  131 GLN A CG  1 
ATOM   806  C  CD  . GLN A 1 131 ? 10.642  51.338 4.665   1.00 67.77  ?  131 GLN A CD  1 
ATOM   807  O  OE1 . GLN A 1 131 ? 9.619   50.652 4.610   1.00 65.59  ?  131 GLN A OE1 1 
ATOM   808  N  NE2 . GLN A 1 131 ? 10.621  52.661 4.649   1.00 76.63  ?  131 GLN A NE2 1 
ATOM   809  N  N   . ALA A 1 132 ? 12.436  48.482 8.710   1.00 36.30  ?  132 ALA A N   1 
ATOM   810  C  CA  . ALA A 1 132 ? 12.325  47.332 9.632   1.00 36.41  ?  132 ALA A CA  1 
ATOM   811  C  C   . ALA A 1 132 ? 11.748  47.839 10.956  1.00 35.54  ?  132 ALA A C   1 
ATOM   812  O  O   . ALA A 1 132 ? 10.754  47.277 11.442  1.00 38.67  ?  132 ALA A O   1 
ATOM   813  C  CB  . ALA A 1 132 ? 13.671  46.657 9.812   1.00 33.94  ?  132 ALA A CB  1 
ATOM   814  N  N   . HIS A 1 133 ? 12.352  48.896 11.478  1.00 35.83  ?  133 HIS A N   1 
ATOM   815  C  CA  . HIS A 1 133 ? 11.969  49.569 12.737  1.00 36.37  ?  133 HIS A CA  1 
ATOM   816  C  C   . HIS A 1 133 ? 10.527  50.091 12.628  1.00 36.01  ?  133 HIS A C   1 
ATOM   817  O  O   . HIS A 1 133 ? 9.739   49.792 13.549  1.00 31.91  ?  133 HIS A O   1 
ATOM   818  C  CB  . HIS A 1 133 ? 13.037  50.600 13.116  1.00 35.37  ?  133 HIS A CB  1 
ATOM   819  C  CG  . HIS A 1 133 ? 14.252  50.008 13.773  1.00 41.56  ?  133 HIS A CG  1 
ATOM   820  N  ND1 . HIS A 1 133 ? 15.369  49.568 13.056  1.00 42.56  ?  133 HIS A ND1 1 
ATOM   821  C  CD2 . HIS A 1 133 ? 14.558  49.818 15.084  1.00 42.84  ?  133 HIS A CD2 1 
ATOM   822  C  CE1 . HIS A 1 133 ? 16.306  49.151 13.896  1.00 42.95  ?  133 HIS A CE1 1 
ATOM   823  N  NE2 . HIS A 1 133 ? 15.819  49.272 15.147  1.00 44.58  ?  133 HIS A NE2 1 
ATOM   824  N  N   . GLN A 1 134 ? 10.136  50.750 11.530  1.00 40.12  ?  134 GLN A N   1 
ATOM   825  C  CA  . GLN A 1 134 ? 8.747   51.278 11.392  1.00 42.63  ?  134 GLN A CA  1 
ATOM   826  C  C   . GLN A 1 134 ? 7.758   50.105 11.397  1.00 37.52  ?  134 GLN A C   1 
ATOM   827  O  O   . GLN A 1 134 ? 6.858   50.102 12.245  1.00 33.12  ?  134 GLN A O   1 
ATOM   828  C  CB  . GLN A 1 134 ? 8.564   52.155 10.157  1.00 50.50  ?  134 GLN A CB  1 
ATOM   829  C  CG  . GLN A 1 134 ? 9.353   53.459 10.247  1.00 63.35  ?  134 GLN A CG  1 
ATOM   830  C  CD  . GLN A 1 134 ? 9.233   54.299 8.998   1.00 75.24  ?  134 GLN A CD  1 
ATOM   831  O  OE1 . GLN A 1 134 ? 8.974   53.796 7.903   1.00 74.10  ?  134 GLN A OE1 1 
ATOM   832  N  NE2 . GLN A 1 134 ? 9.459   55.595 9.153   1.00 82.24  ?  134 GLN A NE2 1 
ATOM   833  N  N   . LEU A 1 135 ? 7.966   49.099 10.557  1.00 36.00  ?  135 LEU A N   1 
ATOM   834  C  CA  . LEU A 1 135 ? 7.120   47.863 10.553  1.00 38.09  ?  135 LEU A CA  1 
ATOM   835  C  C   . LEU A 1 135 ? 7.036   47.231 11.945  1.00 34.29  ?  135 LEU A C   1 
ATOM   836  O  O   . LEU A 1 135 ? 5.905   46.944 12.380  1.00 32.34  ?  135 LEU A O   1 
ATOM   837  C  CB  . LEU A 1 135 ? 7.695   46.864 9.554   1.00 37.92  ?  135 LEU A CB  1 
ATOM   838  C  CG  . LEU A 1 135 ? 7.519   47.291 8.102   1.00 38.42  ?  135 LEU A CG  1 
ATOM   839  C  CD1 . LEU A 1 135 ? 8.432   46.466 7.209   1.00 43.47  ?  135 LEU A CD1 1 
ATOM   840  C  CD2 . LEU A 1 135 ? 6.060   47.200 7.670   1.00 35.59  ?  135 LEU A CD2 1 
ATOM   841  N  N   . LEU A 1 136 ? 8.170   47.062 12.628  1.00 33.04  ?  136 LEU A N   1 
ATOM   842  C  CA  . LEU A 1 136 ? 8.204   46.494 14.001  1.00 34.36  ?  136 LEU A CA  1 
ATOM   843  C  C   . LEU A 1 136 ? 7.496   47.427 15.005  1.00 33.59  ?  136 LEU A C   1 
ATOM   844  O  O   . LEU A 1 136 ? 6.691   46.896 15.819  1.00 31.77  ?  136 LEU A O   1 
ATOM   845  C  CB  . LEU A 1 136 ? 9.650   46.164 14.395  1.00 33.53  ?  136 LEU A CB  1 
ATOM   846  C  CG  . LEU A 1 136 ? 10.276  44.971 13.666  1.00 36.90  ?  136 LEU A CG  1 
ATOM   847  C  CD1 . LEU A 1 136 ? 11.666  44.660 14.202  1.00 39.05  ?  136 LEU A CD1 1 
ATOM   848  C  CD2 . LEU A 1 136 ? 9.406   43.730 13.744  1.00 36.79  ?  136 LEU A CD2 1 
ATOM   849  N  N   . ASP A 1 137 ? 7.755   48.744 14.968  1.00 35.35  ?  137 ASP A N   1 
ATOM   850  C  CA  . ASP A 1 137 ? 7.108   49.744 15.876  1.00 37.24  ?  137 ASP A CA  1 
ATOM   851  C  C   . ASP A 1 137 ? 5.580   49.650 15.751  1.00 35.38  ?  137 ASP A C   1 
ATOM   852  O  O   . ASP A 1 137 ? 4.890   49.754 16.772  1.00 36.83  ?  137 ASP A O   1 
ATOM   853  C  CB  . ASP A 1 137 ? 7.562   51.183 15.596  1.00 40.89  ?  137 ASP A CB  1 
ATOM   854  C  CG  . ASP A 1 137 ? 8.982   51.508 16.024  1.00 44.69  ?  137 ASP A CG  1 
ATOM   855  O  OD1 . ASP A 1 137 ? 9.409   50.948 17.060  1.00 46.28  ?  137 ASP A OD1 1 
ATOM   856  O  OD2 . ASP A 1 137 ? 9.645   52.338 15.321  1.00 43.11  ?  137 ASP A OD2 1 
ATOM   857  N  N   . ARG A 1 138 ? 5.062   49.465 14.540  1.00 36.20  ?  138 ARG A N   1 
ATOM   858  C  CA  . ARG A 1 138 ? 3.617   49.218 14.305  1.00 43.98  ?  138 ARG A CA  1 
ATOM   859  C  C   . ARG A 1 138 ? 3.163   47.986 15.123  1.00 44.21  ?  138 ARG A C   1 
ATOM   860  O  O   . ARG A 1 138 ? 2.218   48.125 15.927  1.00 47.33  ?  138 ARG A O   1 
ATOM   861  C  CB  . ARG A 1 138 ? 3.339   49.129 12.796  1.00 53.31  ?  138 ARG A CB  1 
ATOM   862  C  CG  . ARG A 1 138 ? 3.547   50.446 12.057  1.00 66.02  ?  138 ARG A CG  1 
ATOM   863  C  CD  . ARG A 1 138 ? 3.240   50.429 10.567  1.00 72.18  ?  138 ARG A CD  1 
ATOM   864  N  NE  . ARG A 1 138 ? 3.539   51.724 9.936   1.00 76.10  ?  138 ARG A NE  1 
ATOM   865  C  CZ  . ARG A 1 138 ? 3.486   51.997 8.630   1.00 73.63  ?  138 ARG A CZ  1 
ATOM   866  N  NH1 . ARG A 1 138 ? 3.129   51.074 7.753   1.00 68.07  ?  138 ARG A NH1 1 
ATOM   867  N  NH2 . ARG A 1 138 ? 3.795   53.211 8.203   1.00 67.82  ?  138 ARG A NH2 1 
ATOM   868  N  N   . LEU A 1 139 ? 3.832   46.834 15.016  1.00 36.95  ?  139 LEU A N   1 
ATOM   869  C  CA  . LEU A 1 139 ? 3.345   45.594 15.688  1.00 35.65  ?  139 LEU A CA  1 
ATOM   870  C  C   . LEU A 1 139 ? 3.468   45.736 17.213  1.00 37.16  ?  139 LEU A C   1 
ATOM   871  O  O   . LEU A 1 139 ? 2.554   45.251 17.929  1.00 37.05  ?  139 LEU A O   1 
ATOM   872  C  CB  . LEU A 1 139 ? 4.135   44.391 15.175  1.00 34.23  ?  139 LEU A CB  1 
ATOM   873  C  CG  . LEU A 1 139 ? 4.103   44.208 13.665  1.00 32.19  ?  139 LEU A CG  1 
ATOM   874  C  CD1 . LEU A 1 139 ? 5.058   43.124 13.249  1.00 30.67  ?  139 LEU A CD1 1 
ATOM   875  C  CD2 . LEU A 1 139 ? 2.696   43.916 13.190  1.00 32.77  ?  139 LEU A CD2 1 
ATOM   876  N  N   . ILE A 1 140 ? 4.534   46.390 17.697  1.00 36.64  ?  140 ILE A N   1 
ATOM   877  C  CA  . ILE A 1 140 ? 4.726   46.663 19.157  1.00 38.04  ?  140 ILE A CA  1 
ATOM   878  C  C   . ILE A 1 140 ? 3.543   47.486 19.694  1.00 36.55  ?  140 ILE A C   1 
ATOM   879  O  O   . ILE A 1 140 ? 3.129   47.213 20.785  1.00 37.14  ?  140 ILE A O   1 
ATOM   880  C  CB  . ILE A 1 140 ? 6.079   47.332 19.469  1.00 35.93  ?  140 ILE A CB  1 
ATOM   881  C  CG1 . ILE A 1 140 ? 7.262   46.407 19.163  1.00 34.84  ?  140 ILE A CG1 1 
ATOM   882  C  CG2 . ILE A 1 140 ? 6.095   47.806 20.917  1.00 33.86  ?  140 ILE A CG2 1 
ATOM   883  C  CD1 . ILE A 1 140 ? 8.616   47.101 19.168  1.00 34.24  ?  140 ILE A CD1 1 
ATOM   884  N  N   . GLU A 1 141 ? 2.983   48.409 18.917  1.00 41.20  ?  141 GLU A N   1 
ATOM   885  C  CA  . GLU A 1 141 ? 1.837   49.249 19.343  1.00 42.43  ?  141 GLU A CA  1 
ATOM   886  C  C   . GLU A 1 141 ? 0.565   48.420 19.467  1.00 38.67  ?  141 GLU A C   1 
ATOM   887  O  O   . GLU A 1 141 ? -0.198  48.645 20.407  1.00 42.39  ?  141 GLU A O   1 
ATOM   888  C  CB  . GLU A 1 141 ? 1.606   50.405 18.376  1.00 47.42  ?  141 GLU A CB  1 
ATOM   889  C  CG  . GLU A 1 141 ? 2.750   51.392 18.418  1.00 58.31  ?  141 GLU A CG  1 
ATOM   890  C  CD  . GLU A 1 141 ? 2.593   52.515 17.422  1.00 65.31  ?  141 GLU A CD  1 
ATOM   891  O  OE1 . GLU A 1 141 ? 1.681   52.407 16.571  1.00 58.29  ?  141 GLU A OE1 1 
ATOM   892  O  OE2 . GLU A 1 141 ? 3.361   53.501 17.534  1.00 71.79  ?  141 GLU A OE2 1 
ATOM   893  N  N   . GLN A 1 142 ? 0.320   47.512 18.538  1.00 39.61  ?  142 GLN A N   1 
ATOM   894  C  CA  . GLN A 1 142 ? -0.877  46.622 18.585  1.00 40.02  ?  142 GLN A CA  1 
ATOM   895  C  C   . GLN A 1 142 ? -0.715  45.643 19.752  1.00 33.95  ?  142 GLN A C   1 
ATOM   896  O  O   . GLN A 1 142 ? -1.716  45.313 20.410  1.00 29.44  ?  142 GLN A O   1 
ATOM   897  C  CB  . GLN A 1 142 ? -1.022  45.898 17.250  1.00 40.26  ?  142 GLN A CB  1 
ATOM   898  C  CG  . GLN A 1 142 ? -1.102  46.870 16.086  1.00 43.81  ?  142 GLN A CG  1 
ATOM   899  C  CD  . GLN A 1 142 ? -1.328  46.154 14.783  1.00 50.14  ?  142 GLN A CD  1 
ATOM   900  O  OE1 . GLN A 1 142 ? -1.234  44.922 14.693  1.00 46.21  ?  142 GLN A OE1 1 
ATOM   901  N  NE2 . GLN A 1 142 ? -1.638  46.950 13.771  1.00 56.03  ?  142 GLN A NE2 1 
ATOM   902  N  N   . GLY A 1 143 ? 0.533   45.263 20.019  1.00 32.32  ?  143 GLY A N   1 
ATOM   903  C  CA  . GLY A 1 143 ? 0.878   44.220 20.994  1.00 33.58  ?  143 GLY A CA  1 
ATOM   904  C  C   . GLY A 1 143 ? 0.710   42.829 20.393  1.00 30.45  ?  143 GLY A C   1 
ATOM   905  O  O   . GLY A 1 143 ? 0.015   42.628 19.393  1.00 25.26  ?  143 GLY A O   1 
ATOM   906  N  N   . PRO A 1 144 ? 1.371   41.825 20.984  1.00 30.50  ?  144 PRO A N   1 
ATOM   907  C  CA  . PRO A 1 144 ? 1.352   40.478 20.425  1.00 31.59  ?  144 PRO A CA  1 
ATOM   908  C  C   . PRO A 1 144 ? 0.003   39.801 20.639  1.00 31.32  ?  144 PRO A C   1 
ATOM   909  O  O   . PRO A 1 144 ? -0.740  40.200 21.534  1.00 32.03  ?  144 PRO A O   1 
ATOM   910  C  CB  . PRO A 1 144 ? 2.477   39.812 21.218  1.00 32.74  ?  144 PRO A CB  1 
ATOM   911  C  CG  . PRO A 1 144 ? 2.451   40.498 22.552  1.00 31.40  ?  144 PRO A CG  1 
ATOM   912  C  CD  . PRO A 1 144 ? 2.177   41.939 22.203  1.00 32.44  ?  144 PRO A CD  1 
ATOM   913  N  N   . PRO A 1 145 ? -0.323  38.737 19.867  1.00 32.45  ?  145 PRO A N   1 
ATOM   914  C  CA  . PRO A 1 145 ? 0.528   38.278 18.759  1.00 35.43  ?  145 PRO A CA  1 
ATOM   915  C  C   . PRO A 1 145 ? 0.440   39.072 17.446  1.00 34.63  ?  145 PRO A C   1 
ATOM   916  O  O   . PRO A 1 145 ? -0.501  39.789 17.232  1.00 33.62  ?  145 PRO A O   1 
ATOM   917  C  CB  . PRO A 1 145 ? 0.063   36.832 18.505  1.00 30.82  ?  145 PRO A CB  1 
ATOM   918  C  CG  . PRO A 1 145 ? -1.351  36.801 19.005  1.00 29.29  ?  145 PRO A CG  1 
ATOM   919  C  CD  . PRO A 1 145 ? -1.404  37.782 20.152  1.00 30.25  ?  145 PRO A CD  1 
ATOM   920  N  N   . ALA A 1 146 ? 1.449   38.930 16.591  1.00 34.47  ?  146 ALA A N   1 
ATOM   921  C  CA  . ALA A 1 146 ? 1.421   39.475 15.215  1.00 33.62  ?  146 ALA A CA  1 
ATOM   922  C  C   . ALA A 1 146 ? 1.897   38.394 14.250  1.00 32.44  ?  146 ALA A C   1 
ATOM   923  O  O   . ALA A 1 146 ? 2.526   37.430 14.690  1.00 36.11  ?  146 ALA A O   1 
ATOM   924  C  CB  . ALA A 1 146 ? 2.268   40.724 15.090  1.00 36.04  ?  146 ALA A CB  1 
ATOM   925  N  N   . ASP A 1 147 ? 1.541   38.528 12.977  1.00 30.36  ?  147 ASP A N   1 
ATOM   926  C  CA  . ASP A 1 147 ? 2.034   37.623 11.924  1.00 27.83  ?  147 ASP A CA  1 
ATOM   927  C  C   . ASP A 1 147 ? 3.222   38.336 11.295  1.00 29.84  ?  147 ASP A C   1 
ATOM   928  O  O   . ASP A 1 147 ? 3.004   39.376 10.619  1.00 25.90  ?  147 ASP A O   1 
ATOM   929  C  CB  . ASP A 1 147 ? 0.928   37.287 10.950  1.00 28.72  ?  147 ASP A CB  1 
ATOM   930  C  CG  . ASP A 1 147 ? 1.331   36.289 9.897   1.00 30.58  ?  147 ASP A CG  1 
ATOM   931  O  OD1 . ASP A 1 147 ? 2.487   35.839 9.940   1.00 33.49  ?  147 ASP A OD1 1 
ATOM   932  O  OD2 . ASP A 1 147 ? 0.470   35.977 9.053   1.00 36.68  ?  147 ASP A OD2 1 
ATOM   933  N  N   . LEU A 1 148 ? 4.426   37.819 11.549  1.00 28.18  ?  148 LEU A N   1 
ATOM   934  C  CA  . LEU A 1 148 ? 5.665   38.451 11.059  1.00 30.12  ?  148 LEU A CA  1 
ATOM   935  C  C   . LEU A 1 148 ? 5.794   38.239 9.539   1.00 31.12  ?  148 LEU A C   1 
ATOM   936  O  O   . LEU A 1 148 ? 6.609   38.939 8.932   1.00 33.44  ?  148 LEU A O   1 
ATOM   937  C  CB  . LEU A 1 148 ? 6.875   37.920 11.837  1.00 30.08  ?  148 LEU A CB  1 
ATOM   938  C  CG  . LEU A 1 148 ? 7.000   38.426 13.272  1.00 30.59  ?  148 LEU A CG  1 
ATOM   939  C  CD1 . LEU A 1 148 ? 8.374   38.147 13.847  1.00 31.61  ?  148 LEU A CD1 1 
ATOM   940  C  CD2 . LEU A 1 148 ? 6.701   39.905 13.370  1.00 30.86  ?  148 LEU A CD2 1 
ATOM   941  N  N   . ARG A 1 149 ? 4.953   37.439 8.896   1.00 29.18  ?  149 ARG A N   1 
ATOM   942  C  CA  . ARG A 1 149 ? 5.029   37.383 7.411   1.00 29.87  ?  149 ARG A CA  1 
ATOM   943  C  C   . ARG A 1 149 ? 4.397   38.658 6.822   1.00 33.36  ?  149 ARG A C   1 
ATOM   944  O  O   . ARG A 1 149 ? 5.133   39.430 6.199   1.00 30.38  ?  149 ARG A O   1 
ATOM   945  C  CB  . ARG A 1 149 ? 4.371   36.143 6.802   1.00 27.57  ?  149 ARG A CB  1 
ATOM   946  C  CG  . ARG A 1 149 ? 4.521   36.084 5.291   1.00 28.46  ?  149 ARG A CG  1 
ATOM   947  C  CD  . ARG A 1 149 ? 3.755   34.918 4.707   1.00 31.29  ?  149 ARG A CD  1 
ATOM   948  N  NE  . ARG A 1 149 ? 3.602   35.026 3.254   1.00 33.30  ?  149 ARG A NE  1 
ATOM   949  C  CZ  . ARG A 1 149 ? 2.682   35.764 2.658   1.00 37.39  ?  149 ARG A CZ  1 
ATOM   950  N  NH1 . ARG A 1 149 ? 1.828   36.467 3.377   1.00 37.39  ?  149 ARG A NH1 1 
ATOM   951  N  NH2 . ARG A 1 149 ? 2.621   35.801 1.342   1.00 38.97  ?  149 ARG A NH2 1 
ATOM   952  N  N   . ASP A 1 150 ? 3.104   38.888 7.048   1.00 33.95  ?  150 ASP A N   1 
ATOM   953  C  CA  . ASP A 1 150 ? 2.374   40.051 6.473   1.00 34.23  ?  150 ASP A CA  1 
ATOM   954  C  C   . ASP A 1 150 ? 2.745   41.365 7.167   1.00 32.91  ?  150 ASP A C   1 
ATOM   955  O  O   . ASP A 1 150 ? 2.559   42.420 6.551   1.00 34.32  ?  150 ASP A O   1 
ATOM   956  C  CB  . ASP A 1 150 ? 0.874   39.817 6.547   1.00 33.99  ?  150 ASP A CB  1 
ATOM   957  C  CG  . ASP A 1 150 ? -0.007  40.916 5.990   1.00 31.58  ?  150 ASP A CG  1 
ATOM   958  O  OD1 . ASP A 1 150 ? -0.093  41.009 4.756   1.00 33.74  ?  150 ASP A OD1 1 
ATOM   959  O  OD2 . ASP A 1 150 ? -0.592  41.658 6.800   1.00 29.20  ?  150 ASP A OD2 1 
ATOM   960  N  N   . GLY A 1 151 ? 3.225   41.302 8.404   1.00 33.33  ?  151 GLY A N   1 
ATOM   961  C  CA  . GLY A 1 151 ? 3.563   42.514 9.166   1.00 32.78  ?  151 GLY A CA  1 
ATOM   962  C  C   . GLY A 1 151 ? 5.028   42.884 9.079   1.00 36.36  ?  151 GLY A C   1 
ATOM   963  O  O   . GLY A 1 151 ? 5.369   43.996 9.513   1.00 32.30  ?  151 GLY A O   1 
ATOM   964  N  N   . PHE A 1 152 ? 5.866   42.000 8.543   1.00 31.07  ?  152 PHE A N   1 
ATOM   965  C  CA  . PHE A 1 152 ? 7.323   42.287 8.506   1.00 34.06  ?  152 PHE A CA  1 
ATOM   966  C  C   . PHE A 1 152 ? 8.044   41.860 7.232   1.00 32.09  ?  152 PHE A C   1 
ATOM   967  O  O   . PHE A 1 152 ? 8.563   42.740 6.566   1.00 34.72  ?  152 PHE A O   1 
ATOM   968  C  CB  . PHE A 1 152 ? 8.008   41.644 9.719   1.00 36.61  ?  152 PHE A CB  1 
ATOM   969  C  CG  . PHE A 1 152 ? 9.432   42.100 9.993   1.00 35.01  ?  152 PHE A CG  1 
ATOM   970  C  CD1 . PHE A 1 152 ? 9.784   43.439 9.893   1.00 33.72  ?  152 PHE A CD1 1 
ATOM   971  C  CD2 . PHE A 1 152 ? 10.412  41.184 10.356  1.00 34.87  ?  152 PHE A CD2 1 
ATOM   972  C  CE1 . PHE A 1 152 ? 11.080  43.845 10.145  1.00 32.23  ?  152 PHE A CE1 1 
ATOM   973  C  CE2 . PHE A 1 152 ? 11.706  41.599 10.610  1.00 33.51  ?  152 PHE A CE2 1 
ATOM   974  C  CZ  . PHE A 1 152 ? 12.035  42.927 10.506  1.00 35.24  ?  152 PHE A CZ  1 
ATOM   975  N  N   . THR A 1 153 ? 8.084   40.573 6.910   1.00 29.93  ?  153 THR A N   1 
ATOM   976  C  CA  . THR A 1 153 ? 8.896   40.066 5.778   1.00 28.77  ?  153 THR A CA  1 
ATOM   977  C  C   . THR A 1 153 ? 8.321   40.588 4.472   1.00 26.94  ?  153 THR A C   1 
ATOM   978  O  O   . THR A 1 153 ? 9.104   41.041 3.647   1.00 27.36  ?  153 THR A O   1 
ATOM   979  C  CB  . THR A 1 153 ? 8.991   38.536 5.844   1.00 27.93  ?  153 THR A CB  1 
ATOM   980  O  OG1 . THR A 1 153 ? 7.733   38.010 5.439   1.00 25.19  ?  153 THR A OG1 1 
ATOM   981  C  CG2 . THR A 1 153 ? 9.353   38.048 7.233   1.00 25.33  ?  153 THR A CG2 1 
ATOM   982  N  N   . GLU A 1 154 ? 7.012   40.522 4.286   1.00 25.33  ?  154 GLU A N   1 
ATOM   983  C  CA  . GLU A 1 154 ? 6.375   40.926 3.009   1.00 26.67  ?  154 GLU A CA  1 
ATOM   984  C  C   . GLU A 1 154 ? 6.437   42.454 2.823   1.00 28.75  ?  154 GLU A C   1 
ATOM   985  O  O   . GLU A 1 154 ? 6.935   42.873 1.775   1.00 28.87  ?  154 GLU A O   1 
ATOM   986  C  CB  . GLU A 1 154 ? 4.958   40.357 2.960   1.00 26.27  ?  154 GLU A CB  1 
ATOM   987  C  CG  . GLU A 1 154 ? 4.910   38.838 2.870   1.00 25.60  ?  154 GLU A CG  1 
ATOM   988  C  CD  . GLU A 1 154 ? 5.192   38.329 1.476   1.00 26.33  ?  154 GLU A CD  1 
ATOM   989  O  OE1 . GLU A 1 154 ? 4.411   38.622 0.555   1.00 27.33  ?  154 GLU A OE1 1 
ATOM   990  O  OE2 . GLU A 1 154 ? 6.205   37.635 1.318   1.00 26.93  ?  154 GLU A OE2 1 
ATOM   991  N  N   . PRO A 1 155 ? 5.987   43.311 3.762   1.00 27.46  ?  155 PRO A N   1 
ATOM   992  C  CA  . PRO A 1 155 ? 6.107   44.758 3.549   1.00 30.06  ?  155 PRO A CA  1 
ATOM   993  C  C   . PRO A 1 155 ? 7.582   45.124 3.362   1.00 31.50  ?  155 PRO A C   1 
ATOM   994  O  O   . PRO A 1 155 ? 7.865   45.862 2.458   1.00 33.04  ?  155 PRO A O   1 
ATOM   995  C  CB  . PRO A 1 155 ? 5.494   45.428 4.793   1.00 28.91  ?  155 PRO A CB  1 
ATOM   996  C  CG  . PRO A 1 155 ? 5.361   44.289 5.817   1.00 28.80  ?  155 PRO A CG  1 
ATOM   997  C  CD  . PRO A 1 155 ? 5.326   42.984 5.026   1.00 28.18  ?  155 PRO A CD  1 
ATOM   998  N  N   . TYR A 1 156 ? 8.477   44.519 4.155   1.00 34.88  ?  156 TYR A N   1 
ATOM   999  C  CA  . TYR A 1 156 ? 9.941   44.827 4.209   1.00 33.74  ?  156 TYR A CA  1 
ATOM   1000 C  C   . TYR A 1 156 ? 10.577  44.408 2.880   1.00 33.07  ?  156 TYR A C   1 
ATOM   1001 O  O   . TYR A 1 156 ? 11.191  45.231 2.219   1.00 37.43  ?  156 TYR A O   1 
ATOM   1002 C  CB  . TYR A 1 156 ? 10.614  44.146 5.419   1.00 30.75  ?  156 TYR A CB  1 
ATOM   1003 C  CG  . TYR A 1 156 ? 12.103  44.346 5.527   1.00 28.16  ?  156 TYR A CG  1 
ATOM   1004 C  CD1 . TYR A 1 156 ? 12.638  45.572 5.890   1.00 29.27  ?  156 TYR A CD1 1 
ATOM   1005 C  CD2 . TYR A 1 156 ? 12.973  43.329 5.211   1.00 26.06  ?  156 TYR A CD2 1 
ATOM   1006 C  CE1 . TYR A 1 156 ? 14.001  45.786 5.906   1.00 28.71  ?  156 TYR A CE1 1 
ATOM   1007 C  CE2 . TYR A 1 156 ? 14.341  43.507 5.270   1.00 30.24  ?  156 TYR A CE2 1 
ATOM   1008 C  CZ  . TYR A 1 156 ? 14.866  44.744 5.610   1.00 32.81  ?  156 TYR A CZ  1 
ATOM   1009 O  OH  . TYR A 1 156 ? 16.230  44.910 5.681   1.00 29.68  ?  156 TYR A OH  1 
ATOM   1010 N  N   . SER A 1 157 ? 10.373  43.171 2.452   1.00 30.22  ?  157 SER A N   1 
ATOM   1011 C  CA  . SER A 1 157 ? 10.990  42.663 1.204   1.00 33.14  ?  157 SER A CA  1 
ATOM   1012 C  C   . SER A 1 157 ? 10.478  43.474 -0.001  1.00 33.40  ?  157 SER A C   1 
ATOM   1013 O  O   . SER A 1 157 ? 11.257  43.731 -0.939  1.00 37.37  ?  157 SER A O   1 
ATOM   1014 C  CB  . SER A 1 157 ? 10.771  41.155 1.063   1.00 31.21  ?  157 SER A CB  1 
ATOM   1015 O  OG  . SER A 1 157 ? 11.204  40.467 2.244   1.00 27.21  ?  157 SER A OG  1 
ATOM   1016 N  N   . ALA A 1 158 ? 9.203   43.837 0.002   1.00 33.29  ?  158 ALA A N   1 
ATOM   1017 C  CA  . ALA A 1 158 ? 8.565   44.613 -1.081  1.00 34.66  ?  158 ALA A CA  1 
ATOM   1018 C  C   . ALA A 1 158 ? 9.191   46.002 -1.094  1.00 32.76  ?  158 ALA A C   1 
ATOM   1019 O  O   . ALA A 1 158 ? 9.513   46.500 -2.162  1.00 33.34  ?  158 ALA A O   1 
ATOM   1020 C  CB  . ALA A 1 158 ? 7.080   44.718 -0.856  1.00 36.02  ?  158 ALA A CB  1 
ATOM   1021 N  N   . ALA A 1 159 ? 9.291   46.611 0.073   1.00 31.90  ?  159 ALA A N   1 
ATOM   1022 C  CA  . ALA A 1 159 ? 9.929   47.924 0.244   1.00 33.66  ?  159 ALA A CA  1 
ATOM   1023 C  C   . ALA A 1 159 ? 11.307  47.876 -0.438  1.00 34.27  ?  159 ALA A C   1 
ATOM   1024 O  O   . ALA A 1 159 ? 11.526  48.663 -1.351  1.00 37.95  ?  159 ALA A O   1 
ATOM   1025 C  CB  . ALA A 1 159 ? 9.977   48.271 1.711   1.00 34.52  ?  159 ALA A CB  1 
ATOM   1026 N  N   . LEU A 1 160 ? 12.177  46.935 -0.094  1.00 31.84  ?  160 LEU A N   1 
ATOM   1027 C  CA  . LEU A 1 160 ? 13.518  46.865 -0.712  1.00 33.75  ?  160 LEU A CA  1 
ATOM   1028 C  C   . LEU A 1 160 ? 13.369  46.993 -2.228  1.00 37.69  ?  160 LEU A C   1 
ATOM   1029 O  O   . LEU A 1 160 ? 13.935  47.930 -2.809  1.00 41.60  ?  160 LEU A O   1 
ATOM   1030 C  CB  . LEU A 1 160 ? 14.205  45.541 -0.372  1.00 34.05  ?  160 LEU A CB  1 
ATOM   1031 C  CG  . LEU A 1 160 ? 15.488  45.278 -1.161  1.00 35.52  ?  160 LEU A CG  1 
ATOM   1032 C  CD1 . LEU A 1 160 ? 16.450  46.434 -1.015  1.00 36.62  ?  160 LEU A CD1 1 
ATOM   1033 C  CD2 . LEU A 1 160 ? 16.178  44.005 -0.711  1.00 39.38  ?  160 LEU A CD2 1 
ATOM   1034 N  N   . HIS A 1 161 ? 12.635  46.071 -2.836  1.00 37.21  ?  161 HIS A N   1 
ATOM   1035 C  CA  . HIS A 1 161 ? 12.543  45.901 -4.306  1.00 40.17  ?  161 HIS A CA  1 
ATOM   1036 C  C   . HIS A 1 161 ? 11.795  47.069 -4.987  1.00 39.51  ?  161 HIS A C   1 
ATOM   1037 O  O   . HIS A 1 161 ? 11.971  47.265 -6.179  1.00 39.98  ?  161 HIS A O   1 
ATOM   1038 C  CB  . HIS A 1 161 ? 11.939  44.521 -4.602  1.00 39.16  ?  161 HIS A CB  1 
ATOM   1039 C  CG  . HIS A 1 161 ? 12.890  43.448 -4.218  1.00 39.86  ?  161 HIS A CG  1 
ATOM   1040 N  ND1 . HIS A 1 161 ? 13.126  43.142 -2.899  1.00 40.06  ?  161 HIS A ND1 1 
ATOM   1041 C  CD2 . HIS A 1 161 ? 13.713  42.666 -4.955  1.00 37.56  ?  161 HIS A CD2 1 
ATOM   1042 C  CE1 . HIS A 1 161 ? 14.039  42.183 -2.839  1.00 42.63  ?  161 HIS A CE1 1 
ATOM   1043 N  NE2 . HIS A 1 161 ? 14.411  41.867 -4.087  1.00 37.46  ?  161 HIS A NE2 1 
ATOM   1044 N  N   . CYS A 1 162 ? 10.967  47.810 -4.278  1.00 37.76  ?  162 CYS A N   1 
ATOM   1045 C  CA  . CYS A 1 162 ? 10.349  49.044 -4.812  1.00 43.81  ?  162 CYS A CA  1 
ATOM   1046 C  C   . CYS A 1 162 ? 11.436  50.131 -4.879  1.00 44.20  ?  162 CYS A C   1 
ATOM   1047 O  O   . CYS A 1 162 ? 11.556  50.814 -5.912  1.00 47.20  ?  162 CYS A O   1 
ATOM   1048 C  CB  . CYS A 1 162 ? 9.120   49.425 -3.982  1.00 47.57  ?  162 CYS A CB  1 
ATOM   1049 S  SG  . CYS A 1 162 ? 7.697   48.316 -4.237  1.00 40.43  ?  162 CYS A SG  1 
ATOM   1050 N  N   . ARG A 1 163 ? 12.262  50.253 -3.847  1.00 45.24  ?  163 ARG A N   1 
ATOM   1051 C  CA  . ARG A 1 163 ? 13.403  51.198 -3.867  1.00 43.45  ?  163 ARG A CA  1 
ATOM   1052 C  C   . ARG A 1 163 ? 14.398  50.827 -4.970  1.00 41.01  ?  163 ARG A C   1 
ATOM   1053 O  O   . ARG A 1 163 ? 14.819  51.742 -5.692  1.00 47.32  ?  163 ARG A O   1 
ATOM   1054 C  CB  . ARG A 1 163 ? 14.134  51.234 -2.533  1.00 44.01  ?  163 ARG A CB  1 
ATOM   1055 C  CG  . ARG A 1 163 ? 15.373  52.112 -2.576  1.00 47.53  ?  163 ARG A CG  1 
ATOM   1056 C  CD  . ARG A 1 163 ? 15.725  52.690 -1.232  1.00 49.97  ?  163 ARG A CD  1 
ATOM   1057 N  NE  . ARG A 1 163 ? 17.017  53.349 -1.274  1.00 52.20  ?  163 ARG A NE  1 
ATOM   1058 C  CZ  . ARG A 1 163 ? 17.234  54.597 -0.888  1.00 50.53  ?  163 ARG A CZ  1 
ATOM   1059 N  NH1 . ARG A 1 163 ? 16.245  55.336 -0.421  1.00 49.73  ?  163 ARG A NH1 1 
ATOM   1060 N  NH2 . ARG A 1 163 ? 18.451  55.094 -0.940  1.00 49.44  ?  163 ARG A NH2 1 
ATOM   1061 N  N   . LEU A 1 164 ? 14.787  49.556 -5.081  1.00 40.51  ?  164 LEU A N   1 
ATOM   1062 C  CA  . LEU A 1 164 ? 15.614  49.035 -6.206  1.00 38.05  ?  164 LEU A CA  1 
ATOM   1063 C  C   . LEU A 1 164 ? 15.078  49.524 -7.558  1.00 39.64  ?  164 LEU A C   1 
ATOM   1064 O  O   . LEU A 1 164 ? 15.887  49.820 -8.414  1.00 42.76  ?  164 LEU A O   1 
ATOM   1065 C  CB  . LEU A 1 164 ? 15.584  47.507 -6.210  1.00 40.21  ?  164 LEU A CB  1 
ATOM   1066 C  CG  . LEU A 1 164 ? 16.207  46.757 -5.029  1.00 43.61  ?  164 LEU A CG  1 
ATOM   1067 C  CD1 . LEU A 1 164 ? 15.921  45.276 -5.192  1.00 42.47  ?  164 LEU A CD1 1 
ATOM   1068 C  CD2 . LEU A 1 164 ? 17.707  46.984 -4.886  1.00 44.11  ?  164 LEU A CD2 1 
ATOM   1069 N  N   . LEU A 1 165 ? 13.763  49.528 -7.780  1.00 40.13  ?  165 LEU A N   1 
ATOM   1070 C  CA  . LEU A 1 165 ? 13.194  49.829 -9.117  1.00 43.78  ?  165 LEU A CA  1 
ATOM   1071 C  C   . LEU A 1 165 ? 12.930  51.336 -9.236  1.00 45.79  ?  165 LEU A C   1 
ATOM   1072 O  O   . LEU A 1 165 ? 12.528  51.768 -10.322 1.00 48.96  ?  165 LEU A O   1 
ATOM   1073 C  CB  . LEU A 1 165 ? 11.909  49.023 -9.348  1.00 41.69  ?  165 LEU A CB  1 
ATOM   1074 C  CG  . LEU A 1 165 ? 12.055  47.502 -9.419  1.00 40.79  ?  165 LEU A CG  1 
ATOM   1075 C  CD1 . LEU A 1 165 ? 10.688  46.816 -9.504  1.00 39.82  ?  165 LEU A CD1 1 
ATOM   1076 C  CD2 . LEU A 1 165 ? 12.926  47.082 -10.581 1.00 39.91  ?  165 LEU A CD2 1 
ATOM   1077 N  N   . GLY A 1 166 ? 13.155  52.100 -8.169  1.00 43.18  ?  166 GLY A N   1 
ATOM   1078 C  CA  . GLY A 1 166 ? 12.778  53.521 -8.079  1.00 41.47  ?  166 GLY A CA  1 
ATOM   1079 C  C   . GLY A 1 166 ? 11.292  53.678 -8.298  1.00 44.52  ?  166 GLY A C   1 
ATOM   1080 O  O   . GLY A 1 166 ? 10.904  54.361 -9.232  1.00 53.21  ?  166 GLY A O   1 
ATOM   1081 N  N   . ILE A 1 167 ? 10.477  52.987 -7.509  1.00 47.69  ?  167 ILE A N   1 
ATOM   1082 C  CA  . ILE A 1 167 ? 8.996   53.098 -7.590  1.00 46.07  ?  167 ILE A CA  1 
ATOM   1083 C  C   . ILE A 1 167 ? 8.460   53.205 -6.173  1.00 46.18  ?  167 ILE A C   1 
ATOM   1084 O  O   . ILE A 1 167 ? 9.099   52.725 -5.252  1.00 43.46  ?  167 ILE A O   1 
ATOM   1085 C  CB  . ILE A 1 167 ? 8.372   51.937 -8.390  1.00 46.25  ?  167 ILE A CB  1 
ATOM   1086 C  CG1 . ILE A 1 167 ? 8.755   51.940 -9.875  1.00 44.36  ?  167 ILE A CG1 1 
ATOM   1087 C  CG2 . ILE A 1 167 ? 6.866   51.937 -8.192  1.00 45.08  ?  167 ILE A CG2 1 
ATOM   1088 C  CD1 . ILE A 1 167 ? 8.355   50.658 -10.579 1.00 41.83  ?  167 ILE A CD1 1 
ATOM   1089 N  N   . PRO A 1 168 ? 7.287   53.846 -5.969  1.00 50.25  ?  168 PRO A N   1 
ATOM   1090 C  CA  . PRO A 1 168 ? 6.734   54.011 -4.629  1.00 48.67  ?  168 PRO A CA  1 
ATOM   1091 C  C   . PRO A 1 168 ? 6.375   52.628 -4.081  1.00 42.87  ?  168 PRO A C   1 
ATOM   1092 O  O   . PRO A 1 168 ? 6.282   51.695 -4.833  1.00 36.35  ?  168 PRO A O   1 
ATOM   1093 C  CB  . PRO A 1 168 ? 5.471   54.861 -4.838  1.00 52.44  ?  168 PRO A CB  1 
ATOM   1094 C  CG  . PRO A 1 168 ? 5.607   55.421 -6.252  1.00 49.91  ?  168 PRO A CG  1 
ATOM   1095 C  CD  . PRO A 1 168 ? 6.393   54.377 -7.012  1.00 47.93  ?  168 PRO A CD  1 
ATOM   1096 N  N   . THR A 1 169 ? 6.178   52.531 -2.780  1.00 44.35  ?  169 THR A N   1 
ATOM   1097 C  CA  . THR A 1 169 ? 5.879   51.254 -2.094  1.00 48.10  ?  169 THR A CA  1 
ATOM   1098 C  C   . THR A 1 169 ? 4.367   51.090 -1.881  1.00 46.91  ?  169 THR A C   1 
ATOM   1099 O  O   . THR A 1 169 ? 3.982   50.022 -1.375  1.00 47.78  ?  169 THR A O   1 
ATOM   1100 C  CB  . THR A 1 169 ? 6.628   51.194 -0.763  1.00 47.90  ?  169 THR A CB  1 
ATOM   1101 O  OG1 . THR A 1 169 ? 6.060   52.242 0.018   1.00 49.94  ?  169 THR A OG1 1 
ATOM   1102 C  CG2 . THR A 1 169 ? 8.120   51.385 -0.902  1.00 49.97  ?  169 THR A CG2 1 
ATOM   1103 N  N   . ASP A 1 170 ? 3.543   52.068 -2.272  1.00 47.83  ?  170 ASP A N   1 
ATOM   1104 C  CA  . ASP A 1 170 ? 2.084   52.107 -1.939  1.00 54.20  ?  170 ASP A CA  1 
ATOM   1105 C  C   . ASP A 1 170 ? 1.311   50.882 -2.460  1.00 49.23  ?  170 ASP A C   1 
ATOM   1106 O  O   . ASP A 1 170 ? 0.295   50.584 -1.822  1.00 41.91  ?  170 ASP A O   1 
ATOM   1107 C  CB  . ASP A 1 170 ? 1.385   53.356 -2.470  1.00 58.81  ?  170 ASP A CB  1 
ATOM   1108 C  CG  . ASP A 1 170 ? 2.096   54.634 -2.084  1.00 62.89  ?  170 ASP A CG  1 
ATOM   1109 O  OD1 . ASP A 1 170 ? 2.497   54.765 -0.906  1.00 69.31  ?  170 ASP A OD1 1 
ATOM   1110 O  OD2 . ASP A 1 170 ? 2.275   55.458 -2.972  1.00 66.45  ?  170 ASP A OD2 1 
ATOM   1111 N  N   . ASP A 1 171 ? 1.752   50.192 -3.527  1.00 43.66  ?  171 ASP A N   1 
ATOM   1112 C  CA  . ASP A 1 171 ? 0.998   49.049 -4.116  1.00 45.14  ?  171 ASP A CA  1 
ATOM   1113 C  C   . ASP A 1 171 ? 1.676   47.727 -3.761  1.00 44.16  ?  171 ASP A C   1 
ATOM   1114 O  O   . ASP A 1 171 ? 1.621   46.788 -4.596  1.00 42.87  ?  171 ASP A O   1 
ATOM   1115 C  CB  . ASP A 1 171 ? 0.889   49.140 -5.644  1.00 48.31  ?  171 ASP A CB  1 
ATOM   1116 C  CG  . ASP A 1 171 ? 0.313   50.439 -6.173  1.00 45.85  ?  171 ASP A CG  1 
ATOM   1117 O  OD1 . ASP A 1 171 ? -0.720  50.897 -5.640  1.00 42.54  ?  171 ASP A OD1 1 
ATOM   1118 O  OD2 . ASP A 1 171 ? 0.900   50.966 -7.130  1.00 45.06  ?  171 ASP A OD2 1 
ATOM   1119 N  N   . TRP A 1 172 ? 2.305   47.644 -2.584  1.00 44.65  ?  172 TRP A N   1 
ATOM   1120 C  CA  . TRP A 1 172 ? 3.105   46.454 -2.184  1.00 41.15  ?  172 TRP A CA  1 
ATOM   1121 C  C   . TRP A 1 172 ? 2.198   45.214 -2.036  1.00 34.55  ?  172 TRP A C   1 
ATOM   1122 O  O   . TRP A 1 172 ? 2.602   44.138 -2.497  1.00 31.15  ?  172 TRP A O   1 
ATOM   1123 C  CB  . TRP A 1 172 ? 3.961   46.735 -0.939  1.00 40.82  ?  172 TRP A CB  1 
ATOM   1124 C  CG  . TRP A 1 172 ? 3.209   46.836 0.345   1.00 39.23  ?  172 TRP A CG  1 
ATOM   1125 C  CD1 . TRP A 1 172 ? 2.724   47.961 0.940   1.00 39.69  ?  172 TRP A CD1 1 
ATOM   1126 C  CD2 . TRP A 1 172 ? 2.860   45.748 1.206   1.00 40.93  ?  172 TRP A CD2 1 
ATOM   1127 N  NE1 . TRP A 1 172 ? 2.100   47.651 2.117   1.00 37.06  ?  172 TRP A NE1 1 
ATOM   1128 C  CE2 . TRP A 1 172 ? 2.138   46.300 2.293   1.00 39.75  ?  172 TRP A CE2 1 
ATOM   1129 C  CE3 . TRP A 1 172 ? 3.058   44.367 1.144   1.00 37.47  ?  172 TRP A CE3 1 
ATOM   1130 C  CZ2 . TRP A 1 172 ? 1.625   45.515 3.321   1.00 39.03  ?  172 TRP A CZ2 1 
ATOM   1131 C  CZ3 . TRP A 1 172 ? 2.562   43.591 2.167   1.00 40.67  ?  172 TRP A CZ3 1 
ATOM   1132 C  CH2 . TRP A 1 172 ? 1.865   44.159 3.243   1.00 40.53  ?  172 TRP A CH2 1 
ATOM   1133 N  N   . ARG A 1 173 ? 1.006   45.346 -1.460  1.00 33.38  ?  173 ARG A N   1 
ATOM   1134 C  CA  . ARG A 1 173 ? 0.072   44.200 -1.280  1.00 32.30  ?  173 ARG A CA  1 
ATOM   1135 C  C   . ARG A 1 173 ? -0.241  43.591 -2.643  1.00 32.12  ?  173 ARG A C   1 
ATOM   1136 O  O   . ARG A 1 173 ? -0.153  42.343 -2.759  1.00 31.03  ?  173 ARG A O   1 
ATOM   1137 C  CB  . ARG A 1 173 ? -1.214  44.612 -0.562  1.00 30.52  ?  173 ARG A CB  1 
ATOM   1138 C  CG  . ARG A 1 173 ? -0.989  44.928 0.907   1.00 33.68  ?  173 ARG A CG  1 
ATOM   1139 C  CD  . ARG A 1 173 ? -2.216  44.945 1.827   1.00 35.90  ?  173 ARG A CD  1 
ATOM   1140 N  NE  . ARG A 1 173 ? -1.757  44.983 3.221   1.00 38.11  ?  173 ARG A NE  1 
ATOM   1141 C  CZ  . ARG A 1 173 ? -1.331  43.916 3.906   1.00 38.71  ?  173 ARG A CZ  1 
ATOM   1142 N  NH1 . ARG A 1 173 ? -1.324  42.717 3.346   1.00 34.53  ?  173 ARG A NH1 1 
ATOM   1143 N  NH2 . ARG A 1 173 ? -0.869  44.059 5.136   1.00 39.03  ?  173 ARG A NH2 1 
ATOM   1144 N  N   . ARG A 1 174 ? -0.564  44.440 -3.630  1.00 32.51  ?  174 ARG A N   1 
ATOM   1145 C  CA  . ARG A 1 174 ? -0.892  44.014 -5.020  1.00 33.11  ?  174 ARG A CA  1 
ATOM   1146 C  C   . ARG A 1 174 ? 0.329   43.311 -5.624  1.00 30.11  ?  174 ARG A C   1 
ATOM   1147 O  O   . ARG A 1 174 ? 0.174   42.229 -6.250  1.00 29.40  ?  174 ARG A O   1 
ATOM   1148 C  CB  . ARG A 1 174 ? -1.376  45.199 -5.873  1.00 33.75  ?  174 ARG A CB  1 
ATOM   1149 N  N   . LEU A 1 175 ? 1.502   43.913 -5.463  1.00 30.10  ?  175 LEU A N   1 
ATOM   1150 C  CA  . LEU A 1 175 ? 2.726   43.415 -6.129  1.00 31.09  ?  175 LEU A CA  1 
ATOM   1151 C  C   . LEU A 1 175 ? 3.084   42.037 -5.573  1.00 27.40  ?  175 LEU A C   1 
ATOM   1152 O  O   . LEU A 1 175 ? 3.344   41.160 -6.377  1.00 27.59  ?  175 LEU A O   1 
ATOM   1153 C  CB  . LEU A 1 175 ? 3.849   44.439 -5.969  1.00 32.45  ?  175 LEU A CB  1 
ATOM   1154 C  CG  . LEU A 1 175 ? 3.750   45.604 -6.946  1.00 33.60  ?  175 LEU A CG  1 
ATOM   1155 C  CD1 . LEU A 1 175 ? 4.673   46.739 -6.550  1.00 33.39  ?  175 LEU A CD1 1 
ATOM   1156 C  CD2 . LEU A 1 175 ? 4.044   45.137 -8.370  1.00 34.41  ?  175 LEU A CD2 1 
ATOM   1157 N  N   . MET A 1 176 ? 3.024   41.865 -4.255  1.00 29.26  ?  176 MET A N   1 
ATOM   1158 C  CA  . MET A 1 176 ? 3.290   40.593 -3.527  1.00 30.52  ?  176 MET A CA  1 
ATOM   1159 C  C   . MET A 1 176 ? 2.193   39.545 -3.831  1.00 32.57  ?  176 MET A C   1 
ATOM   1160 O  O   . MET A 1 176 ? 2.496   38.334 -4.026  1.00 31.93  ?  176 MET A O   1 
ATOM   1161 C  CB  . MET A 1 176 ? 3.390   40.904 -2.028  1.00 33.81  ?  176 MET A CB  1 
ATOM   1162 C  CG  . MET A 1 176 ? 4.598   41.788 -1.670  1.00 35.10  ?  176 MET A CG  1 
ATOM   1163 S  SD  . MET A 1 176 ? 6.124   41.252 -2.502  1.00 34.55  ?  176 MET A SD  1 
ATOM   1164 C  CE  . MET A 1 176 ? 6.970   40.398 -1.177  1.00 41.80  ?  176 MET A CE  1 
ATOM   1165 N  N   . SER A 1 177 ? 0.953   39.976 -3.994  1.00 33.61  ?  177 SER A N   1 
ATOM   1166 C  CA  . SER A 1 177 ? -0.100  39.111 -4.564  1.00 33.42  ?  177 SER A CA  1 
ATOM   1167 C  C   . SER A 1 177 ? 0.312   38.599 -5.962  1.00 31.36  ?  177 SER A C   1 
ATOM   1168 O  O   . SER A 1 177 ? 0.102   37.409 -6.274  1.00 35.69  ?  177 SER A O   1 
ATOM   1169 C  CB  . SER A 1 177 ? -1.408  39.819 -4.560  1.00 33.11  ?  177 SER A CB  1 
ATOM   1170 O  OG  . SER A 1 177 ? -2.427  38.880 -4.868  1.00 34.95  ?  177 SER A OG  1 
ATOM   1171 N  N   . GLY A 1 178 ? 0.893   39.430 -6.810  1.00 30.21  ?  178 GLY A N   1 
ATOM   1172 C  CA  . GLY A 1 178 ? 1.347   38.964 -8.137  1.00 29.41  ?  178 GLY A CA  1 
ATOM   1173 C  C   . GLY A 1 178 ? 2.320   37.809 -7.973  1.00 32.47  ?  178 GLY A C   1 
ATOM   1174 O  O   . GLY A 1 178 ? 2.249   36.783 -8.755  1.00 30.92  ?  178 GLY A O   1 
ATOM   1175 N  N   . ILE A 1 179 ? 3.191   37.924 -6.968  1.00 31.29  ?  179 ILE A N   1 
ATOM   1176 C  CA  . ILE A 1 179 ? 4.193   36.859 -6.654  1.00 34.17  ?  179 ILE A CA  1 
ATOM   1177 C  C   . ILE A 1 179 ? 3.485   35.573 -6.180  1.00 31.55  ?  179 ILE A C   1 
ATOM   1178 O  O   . ILE A 1 179 ? 4.014   34.491 -6.488  1.00 28.72  ?  179 ILE A O   1 
ATOM   1179 C  CB  . ILE A 1 179 ? 5.245   37.382 -5.652  1.00 35.51  ?  179 ILE A CB  1 
ATOM   1180 C  CG1 . ILE A 1 179 ? 6.093   38.494 -6.287  1.00 34.85  ?  179 ILE A CG1 1 
ATOM   1181 C  CG2 . ILE A 1 179 ? 6.087   36.236 -5.103  1.00 33.95  ?  179 ILE A CG2 1 
ATOM   1182 C  CD1 . ILE A 1 179 ? 6.971   39.247 -5.309  1.00 35.26  ?  179 ILE A CD1 1 
ATOM   1183 N  N   . ASP A 1 180 ? 2.352   35.685 -5.464  1.00 28.43  ?  180 ASP A N   1 
ATOM   1184 C  CA  . ASP A 1 180 ? 1.587   34.519 -4.962  1.00 26.96  ?  180 ASP A CA  1 
ATOM   1185 C  C   . ASP A 1 180 ? 1.160   33.662 -6.171  1.00 28.18  ?  180 ASP A C   1 
ATOM   1186 O  O   . ASP A 1 180 ? 1.021   32.465 -6.000  1.00 27.52  ?  180 ASP A O   1 
ATOM   1187 C  CB  . ASP A 1 180 ? 0.380   34.943 -4.105  1.00 26.80  ?  180 ASP A CB  1 
ATOM   1188 C  CG  . ASP A 1 180 ? 0.653   35.467 -2.691  1.00 27.44  ?  180 ASP A CG  1 
ATOM   1189 O  OD1 . ASP A 1 180 ? 1.693   35.115 -2.101  1.00 24.14  ?  180 ASP A OD1 1 
ATOM   1190 O  OD2 . ASP A 1 180 ? -0.213  36.237 -2.159  1.00 27.06  ?  180 ASP A OD2 1 
ATOM   1191 N  N   . VAL A 1 181 ? 0.917   34.251 -7.353  1.00 31.58  ?  181 VAL A N   1 
ATOM   1192 C  CA  . VAL A 1 181 ? 0.488   33.519 -8.597  1.00 30.22  ?  181 VAL A CA  1 
ATOM   1193 C  C   . VAL A 1 181 ? 1.724   33.137 -9.447  1.00 30.58  ?  181 VAL A C   1 
ATOM   1194 O  O   . VAL A 1 181 ? 1.820   31.948 -9.916  1.00 28.58  ?  181 VAL A O   1 
ATOM   1195 C  CB  . VAL A 1 181 ? -0.529  34.356 -9.406  1.00 29.80  ?  181 VAL A CB  1 
ATOM   1196 C  CG1 . VAL A 1 181 ? -1.050  33.599 -10.623 1.00 30.80  ?  181 VAL A CG1 1 
ATOM   1197 C  CG2 . VAL A 1 181 ? -1.698  34.839 -8.555  1.00 28.83  ?  181 VAL A CG2 1 
ATOM   1198 N  N   . ALA A 1 182 ? 2.655   34.083 -9.631  1.00 30.63  ?  182 ALA A N   1 
ATOM   1199 C  CA  . ALA A 1 182 ? 3.861   33.934 -10.488 1.00 30.99  ?  182 ALA A CA  1 
ATOM   1200 C  C   . ALA A 1 182 ? 4.694   32.726 -10.063 1.00 30.18  ?  182 ALA A C   1 
ATOM   1201 O  O   . ALA A 1 182 ? 5.151   32.018 -10.944 1.00 33.12  ?  182 ALA A O   1 
ATOM   1202 C  CB  . ALA A 1 182 ? 4.693   35.190 -10.458 1.00 32.58  ?  182 ALA A CB  1 
ATOM   1203 N  N   . PHE A 1 183 ? 4.847   32.466 -8.772  1.00 28.18  ?  183 PHE A N   1 
ATOM   1204 C  CA  . PHE A 1 183 ? 5.777   31.416 -8.284  1.00 31.44  ?  183 PHE A CA  1 
ATOM   1205 C  C   . PHE A 1 183 ? 5.049   30.144 -7.814  1.00 30.64  ?  183 PHE A C   1 
ATOM   1206 O  O   . PHE A 1 183 ? 5.674   29.338 -7.087  1.00 28.17  ?  183 PHE A O   1 
ATOM   1207 C  CB  . PHE A 1 183 ? 6.677   32.011 -7.205  1.00 32.56  ?  183 PHE A CB  1 
ATOM   1208 C  CG  . PHE A 1 183 ? 7.627   33.030 -7.777  1.00 36.63  ?  183 PHE A CG  1 
ATOM   1209 C  CD1 . PHE A 1 183 ? 7.248   34.355 -7.899  1.00 39.17  ?  183 PHE A CD1 1 
ATOM   1210 C  CD2 . PHE A 1 183 ? 8.891   32.659 -8.211  1.00 42.01  ?  183 PHE A CD2 1 
ATOM   1211 C  CE1 . PHE A 1 183 ? 8.109   35.294 -8.442  1.00 43.66  ?  183 PHE A CE1 1 
ATOM   1212 C  CE2 . PHE A 1 183 ? 9.759   33.603 -8.741  1.00 45.29  ?  183 PHE A CE2 1 
ATOM   1213 C  CZ  . PHE A 1 183 ? 9.365   34.921 -8.858  1.00 44.39  ?  183 PHE A CZ  1 
ATOM   1214 N  N   . ILE A 1 184 ? 3.819   29.915 -8.275  1.00 28.41  ?  184 ILE A N   1 
ATOM   1215 C  CA  . ILE A 1 184 ? 3.100   28.616 -8.100  1.00 29.28  ?  184 ILE A CA  1 
ATOM   1216 C  C   . ILE A 1 184 ? 3.790   27.490 -8.900  1.00 28.57  ?  184 ILE A C   1 
ATOM   1217 O  O   . ILE A 1 184 ? 4.075   27.686 -10.101 1.00 28.25  ?  184 ILE A O   1 
ATOM   1218 C  CB  . ILE A 1 184 ? 1.630   28.767 -8.530  1.00 28.59  ?  184 ILE A CB  1 
ATOM   1219 C  CG1 . ILE A 1 184 ? 0.863   29.666 -7.554  1.00 29.82  ?  184 ILE A CG1 1 
ATOM   1220 C  CG2 . ILE A 1 184 ? 0.993   27.394 -8.705  1.00 28.63  ?  184 ILE A CG2 1 
ATOM   1221 C  CD1 . ILE A 1 184 ? -0.623  29.760 -7.818  1.00 30.04  ?  184 ILE A CD1 1 
ATOM   1222 N  N   . THR A 1 185 ? 3.966   26.312 -8.295  1.00 27.40  ?  185 THR A N   1 
ATOM   1223 C  CA  . THR A 1 185 ? 4.383   25.074 -9.003  1.00 28.67  ?  185 THR A CA  1 
ATOM   1224 C  C   . THR A 1 185 ? 3.138   24.272 -9.396  1.00 31.96  ?  185 THR A C   1 
ATOM   1225 O  O   . THR A 1 185 ? 2.526   23.701 -8.477  1.00 35.03  ?  185 THR A O   1 
ATOM   1226 C  CB  . THR A 1 185 ? 5.349   24.263 -8.140  1.00 25.82  ?  185 THR A CB  1 
ATOM   1227 O  OG1 . THR A 1 185 ? 4.685   23.840 -6.961  1.00 24.72  ?  185 THR A OG1 1 
ATOM   1228 C  CG2 . THR A 1 185 ? 6.541   25.071 -7.693  1.00 28.11  ?  185 THR A CG2 1 
ATOM   1229 N  N   . SER A 1 186 ? 2.823   24.193 -10.701 1.00 37.66  ?  186 SER A N   1 
ATOM   1230 C  CA  . SER A 1 186 ? 1.656   23.470 -11.299 1.00 36.83  ?  186 SER A CA  1 
ATOM   1231 C  C   . SER A 1 186 ? 2.089   22.334 -12.235 1.00 38.60  ?  186 SER A C   1 
ATOM   1232 O  O   . SER A 1 186 ? 2.983   22.500 -13.072 1.00 42.55  ?  186 SER A O   1 
ATOM   1233 C  CB  . SER A 1 186 ? 0.756   24.450 -12.026 1.00 36.10  ?  186 SER A CB  1 
ATOM   1234 O  OG  . SER A 1 186 ? -0.388  23.783 -12.546 1.00 34.70  ?  186 SER A OG  1 
ATOM   1235 N  N   . PRO A 1 187 ? 1.452   21.144 -12.166 1.00 39.00  ?  187 PRO A N   1 
ATOM   1236 C  CA  . PRO A 1 187 ? 1.771   20.042 -13.078 1.00 38.60  ?  187 PRO A CA  1 
ATOM   1237 C  C   . PRO A 1 187 ? 1.589   20.424 -14.550 1.00 39.11  ?  187 PRO A C   1 
ATOM   1238 O  O   . PRO A 1 187 ? 2.416   20.022 -15.350 1.00 36.36  ?  187 PRO A O   1 
ATOM   1239 C  CB  . PRO A 1 187 ? 0.747   18.960 -12.703 1.00 39.15  ?  187 PRO A CB  1 
ATOM   1240 C  CG  . PRO A 1 187 ? 0.452   19.257 -11.255 1.00 37.28  ?  187 PRO A CG  1 
ATOM   1241 C  CD  . PRO A 1 187 ? 0.411   20.768 -11.201 1.00 39.58  ?  187 PRO A CD  1 
ATOM   1242 N  N   . ARG A 1 188 ? 0.510   21.159 -14.852 1.00 41.81  ?  188 ARG A N   1 
ATOM   1243 C  CA  . ARG A 1 188 ? 0.177   21.715 -16.195 1.00 39.18  ?  188 ARG A CA  1 
ATOM   1244 C  C   . ARG A 1 188 ? 0.048   23.237 -16.087 1.00 39.63  ?  188 ARG A C   1 
ATOM   1245 O  O   . ARG A 1 188 ? -0.195  23.745 -14.969 1.00 37.21  ?  188 ARG A O   1 
ATOM   1246 C  CB  . ARG A 1 188 ? -1.108  21.098 -16.772 1.00 40.06  ?  188 ARG A CB  1 
ATOM   1247 C  CG  . ARG A 1 188 ? -0.930  19.746 -17.458 1.00 42.57  ?  188 ARG A CG  1 
ATOM   1248 C  CD  . ARG A 1 188 ? 0.055   19.738 -18.641 1.00 50.49  ?  188 ARG A CD  1 
ATOM   1249 N  NE  . ARG A 1 188 ? -0.151  20.776 -19.685 1.00 52.12  ?  188 ARG A NE  1 
ATOM   1250 C  CZ  . ARG A 1 188 ? 0.756   21.651 -20.145 1.00 42.04  ?  188 ARG A CZ  1 
ATOM   1251 N  NH1 . ARG A 1 188 ? 1.988   21.688 -19.690 1.00 50.40  ?  188 ARG A NH1 1 
ATOM   1252 N  NH2 . ARG A 1 188 ? 0.419   22.527 -21.054 1.00 39.35  ?  188 ARG A NH2 1 
ATOM   1253 N  N   . THR A 1 189 ? 0.122   23.906 -17.230 1.00 39.16  ?  189 THR A N   1 
ATOM   1254 C  CA  . THR A 1 189 ? -0.000  25.366 -17.264 1.00 35.74  ?  189 THR A CA  1 
ATOM   1255 C  C   . THR A 1 189 ? -1.406  25.745 -16.896 1.00 40.78  ?  189 THR A C   1 
ATOM   1256 O  O   . THR A 1 189 ? -2.325  24.934 -17.096 1.00 34.23  ?  189 THR A O   1 
ATOM   1257 C  CB  . THR A 1 189 ? 0.395   25.897 -18.640 1.00 39.73  ?  189 THR A CB  1 
ATOM   1258 O  OG1 . THR A 1 189 ? -0.677  25.552 -19.509 1.00 36.36  ?  189 THR A OG1 1 
ATOM   1259 C  CG2 . THR A 1 189 ? 1.695   25.295 -19.139 1.00 43.26  ?  189 THR A CG2 1 
ATOM   1260 N  N   . PHE A 1 190 ? -1.564  26.955 -16.384 1.00 39.67  ?  190 PHE A N   1 
ATOM   1261 C  CA  . PHE A 1 190 ? -2.895  27.441 -15.972 1.00 36.95  ?  190 PHE A CA  1 
ATOM   1262 C  C   . PHE A 1 190 ? -3.075  28.829 -16.534 1.00 38.69  ?  190 PHE A C   1 
ATOM   1263 O  O   . PHE A 1 190 ? -2.088  29.560 -16.690 1.00 32.68  ?  190 PHE A O   1 
ATOM   1264 C  CB  . PHE A 1 190 ? -3.008  27.403 -14.444 1.00 34.84  ?  190 PHE A CB  1 
ATOM   1265 C  CG  . PHE A 1 190 ? -1.953  28.136 -13.627 1.00 34.39  ?  190 PHE A CG  1 
ATOM   1266 C  CD1 . PHE A 1 190 ? -0.721  27.555 -13.362 1.00 36.87  ?  190 PHE A CD1 1 
ATOM   1267 C  CD2 . PHE A 1 190 ? -2.214  29.387 -13.087 1.00 33.57  ?  190 PHE A CD2 1 
ATOM   1268 C  CE1 . PHE A 1 190 ? 0.228   28.221 -12.608 1.00 33.19  ?  190 PHE A CE1 1 
ATOM   1269 C  CE2 . PHE A 1 190 ? -1.262  30.048 -12.333 1.00 34.10  ?  190 PHE A CE2 1 
ATOM   1270 C  CZ  . PHE A 1 190 ? -0.044  29.464 -12.095 1.00 34.31  ?  190 PHE A CZ  1 
ATOM   1271 N  N   . GLU A 1 191 ? -4.318  29.187 -16.842 1.00 38.30  ?  191 GLU A N   1 
ATOM   1272 C  CA  . GLU A 1 191 ? -4.611  30.566 -17.272 1.00 37.78  ?  191 GLU A CA  1 
ATOM   1273 C  C   . GLU A 1 191 ? -4.234  31.419 -16.072 1.00 40.52  ?  191 GLU A C   1 
ATOM   1274 O  O   . GLU A 1 191 ? -4.051  30.884 -14.996 1.00 48.93  ?  191 GLU A O   1 
ATOM   1275 C  CB  . GLU A 1 191 ? -6.101  30.585 -17.584 1.00 36.87  ?  191 GLU A CB  1 
ATOM   1276 C  CG  . GLU A 1 191 ? -6.557  31.692 -18.526 1.00 34.90  ?  191 GLU A CG  1 
ATOM   1277 C  CD  . GLU A 1 191 ? -8.070  31.810 -18.573 1.00 34.19  ?  191 GLU A CD  1 
ATOM   1278 O  OE1 . GLU A 1 191 ? -8.760  30.976 -17.958 1.00 38.07  ?  191 GLU A OE1 1 
ATOM   1279 O  OE2 . GLU A 1 191 ? -8.562  32.746 -19.222 1.00 34.35  ?  191 GLU A OE2 1 
ATOM   1280 N  N   . GLY A 1 192 ? -4.106  32.715 -16.216 1.00 42.37  ?  192 GLY A N   1 
ATOM   1281 C  CA  . GLY A 1 192 ? -3.737  33.427 -14.986 1.00 42.15  ?  192 GLY A CA  1 
ATOM   1282 C  C   . GLY A 1 192 ? -2.248  33.545 -14.883 1.00 36.03  ?  192 GLY A C   1 
ATOM   1283 O  O   . GLY A 1 192 ? -1.808  34.646 -14.644 1.00 39.53  ?  192 GLY A O   1 
ATOM   1284 N  N   . SER A 1 193 ? -1.496  32.476 -15.107 1.00 29.85  ?  193 SER A N   1 
ATOM   1285 C  CA  . SER A 1 193 ? -0.023  32.619 -15.157 1.00 33.91  ?  193 SER A CA  1 
ATOM   1286 C  C   . SER A 1 193 ? 0.322   33.710 -16.177 1.00 35.61  ?  193 SER A C   1 
ATOM   1287 O  O   . SER A 1 193 ? 1.111   34.601 -15.840 1.00 41.83  ?  193 SER A O   1 
ATOM   1288 C  CB  . SER A 1 193 ? 0.647   31.321 -15.481 1.00 35.90  ?  193 SER A CB  1 
ATOM   1289 O  OG  . SER A 1 193 ? 0.308   30.853 -16.778 1.00 40.04  ?  193 SER A OG  1 
ATOM   1290 N  N   . ALA A 1 194 ? -0.278  33.645 -17.364 1.00 39.82  ?  194 ALA A N   1 
ATOM   1291 C  CA  . ALA A 1 194 ? -0.032  34.656 -18.426 1.00 36.39  ?  194 ALA A CA  1 
ATOM   1292 C  C   . ALA A 1 194 ? -0.739  35.960 -18.062 1.00 35.79  ?  194 ALA A C   1 
ATOM   1293 O  O   . ALA A 1 194 ? -0.091  37.018 -18.090 1.00 39.20  ?  194 ALA A O   1 
ATOM   1294 C  CB  . ALA A 1 194 ? -0.495  34.151 -19.770 1.00 35.69  ?  194 ALA A CB  1 
ATOM   1295 N  N   . VAL A 1 195 ? -2.019  35.889 -17.692 1.00 35.54  ?  195 VAL A N   1 
ATOM   1296 C  CA  . VAL A 1 195 ? -2.801  37.096 -17.286 1.00 33.35  ?  195 VAL A CA  1 
ATOM   1297 C  C   . VAL A 1 195 ? -2.031  37.813 -16.178 1.00 31.78  ?  195 VAL A C   1 
ATOM   1298 O  O   . VAL A 1 195 ? -1.853  39.011 -16.282 1.00 31.26  ?  195 VAL A O   1 
ATOM   1299 C  CB  . VAL A 1 195 ? -4.242  36.768 -16.857 1.00 32.68  ?  195 VAL A CB  1 
ATOM   1300 C  CG1 . VAL A 1 195 ? -5.032  38.043 -16.513 1.00 32.17  ?  195 VAL A CG1 1 
ATOM   1301 C  CG2 . VAL A 1 195 ? -4.967  35.972 -17.938 1.00 31.05  ?  195 VAL A CG2 1 
ATOM   1302 N  N   . ASN A 1 196 ? -1.558  37.067 -15.180 1.00 37.68  ?  196 ASN A N   1 
ATOM   1303 C  CA  . ASN A 1 196 ? -0.812  37.603 -14.019 1.00 36.54  ?  196 ASN A CA  1 
ATOM   1304 C  C   . ASN A 1 196 ? 0.455   38.279 -14.563 1.00 37.84  ?  196 ASN A C   1 
ATOM   1305 O  O   . ASN A 1 196 ? 0.690   39.484 -14.253 1.00 35.27  ?  196 ASN A O   1 
ATOM   1306 C  CB  . ASN A 1 196 ? -0.555  36.506 -12.977 1.00 38.14  ?  196 ASN A CB  1 
ATOM   1307 C  CG  . ASN A 1 196 ? 0.101   37.039 -11.720 1.00 41.19  ?  196 ASN A CG  1 
ATOM   1308 O  OD1 . ASN A 1 196 ? -0.501  37.816 -10.985 1.00 35.06  ?  196 ASN A OD1 1 
ATOM   1309 N  ND2 . ASN A 1 196 ? 1.355   36.668 -11.495 1.00 44.30  ?  196 ASN A ND2 1 
ATOM   1310 N  N   . TRP A 1 197 ? 1.228   37.562 -15.381 1.00 37.81  ?  197 TRP A N   1 
ATOM   1311 C  CA  . TRP A 1 197 ? 2.458   38.126 -15.982 1.00 38.25  ?  197 TRP A CA  1 
ATOM   1312 C  C   . TRP A 1 197 ? 2.146   39.483 -16.628 1.00 39.74  ?  197 TRP A C   1 
ATOM   1313 O  O   . TRP A 1 197 ? 2.880   40.440 -16.333 1.00 37.98  ?  197 TRP A O   1 
ATOM   1314 C  CB  . TRP A 1 197 ? 3.097   37.173 -16.988 1.00 42.12  ?  197 TRP A CB  1 
ATOM   1315 C  CG  . TRP A 1 197 ? 4.263   37.828 -17.657 1.00 49.21  ?  197 TRP A CG  1 
ATOM   1316 C  CD1 . TRP A 1 197 ? 4.266   38.424 -18.880 1.00 50.28  ?  197 TRP A CD1 1 
ATOM   1317 C  CD2 . TRP A 1 197 ? 5.577   38.045 -17.102 1.00 56.90  ?  197 TRP A CD2 1 
ATOM   1318 N  NE1 . TRP A 1 197 ? 5.489   38.983 -19.131 1.00 54.54  ?  197 TRP A NE1 1 
ATOM   1319 C  CE2 . TRP A 1 197 ? 6.321   38.759 -18.070 1.00 53.27  ?  197 TRP A CE2 1 
ATOM   1320 C  CE3 . TRP A 1 197 ? 6.209   37.685 -15.901 1.00 57.15  ?  197 TRP A CE3 1 
ATOM   1321 C  CZ2 . TRP A 1 197 ? 7.654   39.132 -17.877 1.00 53.34  ?  197 TRP A CZ2 1 
ATOM   1322 C  CZ3 . TRP A 1 197 ? 7.527   38.057 -15.706 1.00 58.96  ?  197 TRP A CZ3 1 
ATOM   1323 C  CH2 . TRP A 1 197 ? 8.237   38.770 -16.682 1.00 59.71  ?  197 TRP A CH2 1 
ATOM   1324 N  N   . TYR A 1 198 ? 1.113   39.581 -17.480 1.00 37.11  ?  198 TYR A N   1 
ATOM   1325 C  CA  . TYR A 1 198 ? 0.866   40.802 -18.300 1.00 35.62  ?  198 TYR A CA  1 
ATOM   1326 C  C   . TYR A 1 198 ? 0.306   41.911 -17.421 1.00 32.95  ?  198 TYR A C   1 
ATOM   1327 O  O   . TYR A 1 198 ? 0.678   43.077 -17.606 1.00 34.57  ?  198 TYR A O   1 
ATOM   1328 C  CB  . TYR A 1 198 ? 0.016   40.499 -19.534 1.00 37.64  ?  198 TYR A CB  1 
ATOM   1329 C  CG  . TYR A 1 198 ? 0.800   39.806 -20.613 1.00 38.76  ?  198 TYR A CG  1 
ATOM   1330 C  CD1 . TYR A 1 198 ? 1.852   40.460 -21.245 1.00 46.23  ?  198 TYR A CD1 1 
ATOM   1331 C  CD2 . TYR A 1 198 ? 0.540   38.490 -20.973 1.00 41.93  ?  198 TYR A CD2 1 
ATOM   1332 C  CE1 . TYR A 1 198 ? 2.619   39.827 -22.217 1.00 48.63  ?  198 TYR A CE1 1 
ATOM   1333 C  CE2 . TYR A 1 198 ? 1.290   37.842 -21.948 1.00 43.13  ?  198 TYR A CE2 1 
ATOM   1334 C  CZ  . TYR A 1 198 ? 2.338   38.514 -22.560 1.00 46.30  ?  198 TYR A CZ  1 
ATOM   1335 O  OH  . TYR A 1 198 ? 3.079   37.903 -23.519 1.00 53.52  ?  198 TYR A OH  1 
ATOM   1336 N  N   . LYS A 1 199 ? -0.521  41.566 -16.450 1.00 32.43  ?  199 LYS A N   1 
ATOM   1337 C  CA  . LYS A 1 199 ? -1.018  42.568 -15.479 1.00 34.26  ?  199 LYS A CA  1 
ATOM   1338 C  C   . LYS A 1 199 ? 0.171   43.352 -14.894 1.00 35.52  ?  199 LYS A C   1 
ATOM   1339 O  O   . LYS A 1 199 ? 0.072   44.586 -14.808 1.00 34.42  ?  199 LYS A O   1 
ATOM   1340 C  CB  . LYS A 1 199 ? -1.817  41.878 -14.370 1.00 35.40  ?  199 LYS A CB  1 
ATOM   1341 C  CG  . LYS A 1 199 ? -2.012  42.705 -13.103 1.00 34.96  ?  199 LYS A CG  1 
ATOM   1342 C  CD  . LYS A 1 199 ? -2.936  42.013 -12.143 1.00 37.70  ?  199 LYS A CD  1 
ATOM   1343 C  CE  . LYS A 1 199 ? -3.167  42.735 -10.839 1.00 36.01  ?  199 LYS A CE  1 
ATOM   1344 N  NZ  . LYS A 1 199 ? -4.003  41.885 -9.962  1.00 35.36  ?  199 LYS A NZ  1 
ATOM   1345 N  N   . ASP A 1 200 ? 1.253   42.683 -14.481 1.00 35.38  ?  200 ASP A N   1 
ATOM   1346 C  CA  . ASP A 1 200 ? 2.351   43.375 -13.727 1.00 40.63  ?  200 ASP A CA  1 
ATOM   1347 C  C   . ASP A 1 200 ? 3.414   43.939 -14.701 1.00 35.91  ?  200 ASP A C   1 
ATOM   1348 O  O   . ASP A 1 200 ? 3.931   45.022 -14.422 1.00 30.71  ?  200 ASP A O   1 
ATOM   1349 C  CB  . ASP A 1 200 ? 2.922   42.510 -12.581 1.00 39.60  ?  200 ASP A CB  1 
ATOM   1350 C  CG  . ASP A 1 200 ? 2.086   42.535 -11.293 1.00 38.97  ?  200 ASP A CG  1 
ATOM   1351 O  OD1 . ASP A 1 200 ? 1.213   43.432 -11.150 1.00 35.89  ?  200 ASP A OD1 1 
ATOM   1352 O  OD2 . ASP A 1 200 ? 2.301   41.652 -10.433 1.00 39.02  ?  200 ASP A OD2 1 
ATOM   1353 N  N   . LEU A 1 201 ? 3.688   43.283 -15.829 1.00 34.94  ?  201 LEU A N   1 
ATOM   1354 C  CA  . LEU A 1 201 ? 4.474   43.887 -16.936 1.00 35.40  ?  201 LEU A CA  1 
ATOM   1355 C  C   . LEU A 1 201 ? 3.860   45.252 -17.265 1.00 36.72  ?  201 LEU A C   1 
ATOM   1356 O  O   . LEU A 1 201 ? 4.600   46.276 -17.299 1.00 31.05  ?  201 LEU A O   1 
ATOM   1357 C  CB  . LEU A 1 201 ? 4.458   42.968 -18.159 1.00 37.14  ?  201 LEU A CB  1 
ATOM   1358 C  CG  . LEU A 1 201 ? 5.440   43.349 -19.272 1.00 39.56  ?  201 LEU A CG  1 
ATOM   1359 C  CD1 . LEU A 1 201 ? 6.884   43.105 -18.850 1.00 39.57  ?  201 LEU A CD1 1 
ATOM   1360 C  CD2 . LEU A 1 201 ? 5.142   42.601 -20.565 1.00 39.95  ?  201 LEU A CD2 1 
ATOM   1361 N  N   . GLY A 1 202 ? 2.542   45.271 -17.448 1.00 35.14  ?  202 GLY A N   1 
ATOM   1362 C  CA  . GLY A 1 202 ? 1.816   46.516 -17.718 1.00 36.61  ?  202 GLY A CA  1 
ATOM   1363 C  C   . GLY A 1 202 ? 2.089   47.524 -16.632 1.00 38.83  ?  202 GLY A C   1 
ATOM   1364 O  O   . GLY A 1 202 ? 2.297   48.720 -16.933 1.00 47.58  ?  202 GLY A O   1 
ATOM   1365 N  N   . TYR A 1 203 ? 2.095   47.059 -15.391 1.00 40.69  ?  203 TYR A N   1 
ATOM   1366 C  CA  . TYR A 1 203 ? 2.409   47.909 -14.214 1.00 38.04  ?  203 TYR A CA  1 
ATOM   1367 C  C   . TYR A 1 203 ? 3.803   48.539 -14.392 1.00 34.55  ?  203 TYR A C   1 
ATOM   1368 O  O   . TYR A 1 203 ? 3.947   49.761 -14.205 1.00 31.12  ?  203 TYR A O   1 
ATOM   1369 C  CB  . TYR A 1 203 ? 2.300   47.095 -12.920 1.00 35.38  ?  203 TYR A CB  1 
ATOM   1370 C  CG  . TYR A 1 203 ? 2.484   47.946 -11.703 1.00 30.80  ?  203 TYR A CG  1 
ATOM   1371 C  CD1 . TYR A 1 203 ? 3.755   48.281 -11.249 1.00 33.40  ?  203 TYR A CD1 1 
ATOM   1372 C  CD2 . TYR A 1 203 ? 1.392   48.438 -11.036 1.00 28.49  ?  203 TYR A CD2 1 
ATOM   1373 C  CE1 . TYR A 1 203 ? 3.936   49.087 -10.136 1.00 31.96  ?  203 TYR A CE1 1 
ATOM   1374 C  CE2 . TYR A 1 203 ? 1.547   49.209 -9.898  1.00 32.50  ?  203 TYR A CE2 1 
ATOM   1375 C  CZ  . TYR A 1 203 ? 2.820   49.556 -9.466  1.00 35.34  ?  203 TYR A CZ  1 
ATOM   1376 O  OH  . TYR A 1 203 ? 2.962   50.361 -8.377  1.00 39.24  ?  203 TYR A OH  1 
ATOM   1377 N  N   . MET A 1 204 ? 4.812   47.731 -14.716 1.00 32.14  ?  204 MET A N   1 
ATOM   1378 C  CA  . MET A 1 204 ? 6.202   48.217 -14.838 1.00 36.29  ?  204 MET A CA  1 
ATOM   1379 C  C   . MET A 1 204 ? 6.327   49.142 -16.056 1.00 43.55  ?  204 MET A C   1 
ATOM   1380 O  O   . MET A 1 204 ? 7.012   50.168 -15.934 1.00 45.55  ?  204 MET A O   1 
ATOM   1381 C  CB  . MET A 1 204 ? 7.179   47.048 -14.960 1.00 39.22  ?  204 MET A CB  1 
ATOM   1382 C  CG  . MET A 1 204 ? 7.279   46.206 -13.701 1.00 43.38  ?  204 MET A CG  1 
ATOM   1383 S  SD  . MET A 1 204 ? 7.385   47.181 -12.182 1.00 42.72  ?  204 MET A SD  1 
ATOM   1384 C  CE  . MET A 1 204 ? 7.330   45.873 -10.957 1.00 45.80  ?  204 MET A CE  1 
ATOM   1385 N  N   . VAL A 1 205 ? 5.708   48.799 -17.192 1.00 48.53  ?  205 VAL A N   1 
ATOM   1386 C  CA  . VAL A 1 205 ? 5.713   49.647 -18.423 1.00 47.07  ?  205 VAL A CA  1 
ATOM   1387 C  C   . VAL A 1 205 ? 5.212   51.055 -18.088 1.00 45.78  ?  205 VAL A C   1 
ATOM   1388 O  O   . VAL A 1 205 ? 5.725   52.003 -18.674 1.00 40.70  ?  205 VAL A O   1 
ATOM   1389 C  CB  . VAL A 1 205 ? 4.856   49.058 -19.554 1.00 47.46  ?  205 VAL A CB  1 
ATOM   1390 C  CG1 . VAL A 1 205 ? 4.607   50.090 -20.636 1.00 48.92  ?  205 VAL A CG1 1 
ATOM   1391 C  CG2 . VAL A 1 205 ? 5.476   47.806 -20.148 1.00 48.24  ?  205 VAL A CG2 1 
ATOM   1392 N  N   . ASP A 1 206 ? 4.208   51.190 -17.232 1.00 45.41  ?  206 ASP A N   1 
ATOM   1393 C  CA  . ASP A 1 206 ? 3.597   52.518 -16.953 1.00 54.18  ?  206 ASP A CA  1 
ATOM   1394 C  C   . ASP A 1 206 ? 4.494   53.335 -16.015 1.00 55.52  ?  206 ASP A C   1 
ATOM   1395 O  O   . ASP A 1 206 ? 4.504   54.573 -16.148 1.00 57.86  ?  206 ASP A O   1 
ATOM   1396 C  CB  . ASP A 1 206 ? 2.168   52.374 -16.428 1.00 55.12  ?  206 ASP A CB  1 
ATOM   1397 C  CG  . ASP A 1 206 ? 1.227   51.755 -17.450 1.00 58.47  ?  206 ASP A CG  1 
ATOM   1398 O  OD1 . ASP A 1 206 ? 1.495   51.877 -18.676 1.00 58.10  ?  206 ASP A OD1 1 
ATOM   1399 O  OD2 . ASP A 1 206 ? 0.240   51.154 -17.018 1.00 60.78  ?  206 ASP A OD2 1 
ATOM   1400 N  N   . ARG A 1 207 ? 5.219   52.667 -15.127 1.00 57.25  ?  207 ARG A N   1 
ATOM   1401 C  CA  . ARG A 1 207 ? 6.148   53.365 -14.213 1.00 52.52  ?  207 ARG A CA  1 
ATOM   1402 C  C   . ARG A 1 207 ? 7.357   53.780 -15.048 1.00 52.18  ?  207 ARG A C   1 
ATOM   1403 O  O   . ARG A 1 207 ? 7.884   54.877 -14.818 1.00 57.34  ?  207 ARG A O   1 
ATOM   1404 C  CB  . ARG A 1 207 ? 6.429   52.380 -13.081 1.00 56.36  ?  207 ARG A CB  1 
ATOM   1405 N  N   . LEU A 1 208 ? 7.769   52.933 -15.977 1.00 44.90  ?  208 LEU A N   1 
ATOM   1406 C  CA  . LEU A 1 208 ? 8.846   53.286 -16.927 1.00 49.25  ?  208 LEU A CA  1 
ATOM   1407 C  C   . LEU A 1 208 ? 8.476   54.548 -17.715 1.00 55.25  ?  208 LEU A C   1 
ATOM   1408 O  O   . LEU A 1 208 ? 9.405   55.359 -17.950 1.00 54.53  ?  208 LEU A O   1 
ATOM   1409 C  CB  . LEU A 1 208 ? 9.114   52.138 -17.898 1.00 49.16  ?  208 LEU A CB  1 
ATOM   1410 C  CG  . LEU A 1 208 ? 10.352  52.345 -18.770 1.00 50.19  ?  208 LEU A CG  1 
ATOM   1411 C  CD1 . LEU A 1 208 ? 11.548  52.813 -17.950 1.00 48.01  ?  208 LEU A CD1 1 
ATOM   1412 C  CD2 . LEU A 1 208 ? 10.690  51.067 -19.509 1.00 52.32  ?  208 LEU A CD2 1 
ATOM   1413 N  N   . ASN A 1 209 ? 7.200   54.699 -18.118 1.00 54.05  ?  209 ASN A N   1 
ATOM   1414 C  CA  . ASN A 1 209 ? 6.759   55.725 -19.107 1.00 51.31  ?  209 ASN A CA  1 
ATOM   1415 C  C   . ASN A 1 209 ? 6.005   56.838 -18.392 1.00 49.09  ?  209 ASN A C   1 
ATOM   1416 O  O   . ASN A 1 209 ? 5.440   57.655 -19.102 1.00 47.34  ?  209 ASN A O   1 
ATOM   1417 C  CB  . ASN A 1 209 ? 5.897   55.176 -20.252 1.00 48.02  ?  209 ASN A CB  1 
ATOM   1418 C  CG  . ASN A 1 209 ? 6.625   54.184 -21.145 1.00 52.15  ?  209 ASN A CG  1 
ATOM   1419 O  OD1 . ASN A 1 209 ? 7.854   54.199 -21.260 1.00 51.49  ?  209 ASN A OD1 1 
ATOM   1420 N  ND2 . ASN A 1 209 ? 5.873   53.308 -21.792 1.00 47.95  ?  209 ASN A ND2 1 
ATOM   1421 N  N   . ALA A 1 210 ? 6.145   56.943 -17.081 1.00 53.56  ?  210 ALA A N   1 
ATOM   1422 C  CA  . ALA A 1 210 ? 5.488   58.025 -16.317 1.00 64.43  ?  210 ALA A CA  1 
ATOM   1423 C  C   . ALA A 1 210 ? 5.860   59.397 -16.875 1.00 71.35  ?  210 ALA A C   1 
ATOM   1424 O  O   . ALA A 1 210 ? 7.012   59.567 -17.309 1.00 67.33  ?  210 ALA A O   1 
ATOM   1425 C  CB  . ALA A 1 210 ? 5.874   57.910 -14.875 1.00 66.79  ?  210 ALA A CB  1 
ATOM   1426 N  N   . ASP A 1 211 ? 4.918   60.347 -16.836 1.00 83.72  ?  211 ASP A N   1 
ATOM   1427 C  CA  . ASP A 1 211 ? 5.164   61.708 -17.392 1.00 93.40  ?  211 ASP A CA  1 
ATOM   1428 C  C   . ASP A 1 211 ? 6.398   62.279 -16.709 1.00 87.44  ?  211 ASP A C   1 
ATOM   1429 O  O   . ASP A 1 211 ? 7.375   62.552 -17.428 1.00 102.16 ?  211 ASP A O   1 
ATOM   1430 C  CB  . ASP A 1 211 ? 3.946   62.619 -17.329 1.00 105.53 ?  211 ASP A CB  1 
ATOM   1431 N  N   . PRO A 1 212 ? 6.419   62.514 -15.382 1.00 77.84  ?  212 PRO A N   1 
ATOM   1432 C  CA  . PRO A 1 212 ? 7.660   62.910 -14.755 1.00 73.75  ?  212 PRO A CA  1 
ATOM   1433 C  C   . PRO A 1 212 ? 8.558   61.692 -14.803 1.00 75.88  ?  212 PRO A C   1 
ATOM   1434 O  O   . PRO A 1 212 ? 8.596   60.930 -13.821 1.00 76.90  ?  212 PRO A O   1 
ATOM   1435 C  CB  . PRO A 1 212 ? 7.275   63.222 -13.323 1.00 68.40  ?  212 PRO A CB  1 
ATOM   1436 C  CG  . PRO A 1 212 ? 5.781   63.437 -13.387 1.00 70.34  ?  212 PRO A CG  1 
ATOM   1437 C  CD  . PRO A 1 212 ? 5.308   62.459 -14.445 1.00 70.31  ?  212 PRO A CD  1 
ATOM   1438 N  N   . GLU A 1 213 ? 9.223   61.469 -15.936 1.00 73.06  ?  213 GLU A N   1 
ATOM   1439 C  CA  . GLU A 1 213 ? 10.150  60.317 -16.076 1.00 74.13  ?  213 GLU A CA  1 
ATOM   1440 C  C   . GLU A 1 213 ? 10.794  59.847 -14.768 1.00 70.65  ?  213 GLU A C   1 
ATOM   1441 O  O   . GLU A 1 213 ? 11.259  60.693 -13.980 1.00 57.57  ?  213 GLU A O   1 
ATOM   1442 C  CB  . GLU A 1 213 ? 11.276  60.543 -17.081 1.00 80.87  ?  213 GLU A CB  1 
ATOM   1443 N  N   . PRO A 1 214 ? 10.845  58.530 -14.500 1.00 65.59  ?  214 PRO A N   1 
ATOM   1444 C  CA  . PRO A 1 214 ? 11.526  58.027 -13.312 1.00 62.66  ?  214 PRO A CA  1 
ATOM   1445 C  C   . PRO A 1 214 ? 13.025  58.356 -13.340 1.00 65.38  ?  214 PRO A C   1 
ATOM   1446 O  O   . PRO A 1 214 ? 13.697  58.220 -14.354 1.00 66.40  ?  214 PRO A O   1 
ATOM   1447 C  CB  . PRO A 1 214 ? 11.319  56.507 -13.322 1.00 64.52  ?  214 PRO A CB  1 
ATOM   1448 C  CG  . PRO A 1 214 ? 10.875  56.179 -14.744 1.00 66.23  ?  214 PRO A CG  1 
ATOM   1449 C  CD  . PRO A 1 214 ? 10.234  57.445 -15.289 1.00 69.50  ?  214 PRO A CD  1 
ATOM   1450 N  N   . THR A 1 215 ? 13.483  58.858 -12.207 1.00 68.99  ?  215 THR A N   1 
ATOM   1451 C  CA  . THR A 1 215 ? 14.908  59.092 -12.001 1.00 73.40  ?  215 THR A CA  1 
ATOM   1452 C  C   . THR A 1 215 ? 15.103  58.358 -10.717 1.00 82.82  ?  215 THR A C   1 
ATOM   1453 O  O   . THR A 1 215 ? 14.132  58.389 -9.933  1.00 91.78  ?  215 THR A O   1 
ATOM   1454 C  CB  . THR A 1 215 ? 15.163  60.577 -11.814 1.00 72.30  ?  215 THR A CB  1 
ATOM   1455 O  OG1 . THR A 1 215 ? 14.438  60.902 -10.632 1.00 61.57  ?  215 THR A OG1 1 
ATOM   1456 C  CG2 . THR A 1 215 ? 14.678  61.406 -12.988 1.00 67.99  ?  215 THR A CG2 1 
ATOM   1457 N  N   . GLU A 1 216 ? 16.223  57.661 -10.530 1.00 78.29  ?  216 GLU A N   1 
ATOM   1458 C  CA  . GLU A 1 216 ? 16.447  56.820 -9.318  1.00 72.37  ?  216 GLU A CA  1 
ATOM   1459 C  C   . GLU A 1 216 ? 15.896  55.409 -9.573  1.00 58.18  ?  216 GLU A C   1 
ATOM   1460 O  O   . GLU A 1 216 ? 14.774  55.290 -10.087 1.00 45.15  ?  216 GLU A O   1 
ATOM   1461 C  CB  . GLU A 1 216 ? 15.898  57.374 -7.995  1.00 81.55  ?  216 GLU A CB  1 
ATOM   1462 C  CG  . GLU A 1 216 ? 16.587  58.639 -7.490  1.00 80.04  ?  216 GLU A CG  1 
ATOM   1463 C  CD  . GLU A 1 216 ? 16.030  59.259 -6.223  1.00 87.43  ?  216 GLU A CD  1 
ATOM   1464 O  OE1 . GLU A 1 216 ? 14.946  58.816 -5.791  1.00 85.23  ?  216 GLU A OE1 1 
ATOM   1465 O  OE2 . GLU A 1 216 ? 16.664  60.188 -5.678  1.00 94.12  ?  216 GLU A OE2 1 
ATOM   1466 N  N   . GLY A 1 217 ? 16.699  54.393 -9.264  1.00 49.35  ?  217 GLY A N   1 
ATOM   1467 C  CA  . GLY A 1 217 ? 16.259  53.002 -9.427  1.00 50.29  ?  217 GLY A CA  1 
ATOM   1468 C  C   . GLY A 1 217 ? 16.672  52.395 -10.741 1.00 48.53  ?  217 GLY A C   1 
ATOM   1469 O  O   . GLY A 1 217 ? 17.380  53.066 -11.503 1.00 52.81  ?  217 GLY A O   1 
ATOM   1470 N  N   . LEU A 1 218 ? 16.245  51.160 -10.987 1.00 48.01  ?  218 LEU A N   1 
ATOM   1471 C  CA  . LEU A 1 218 ? 16.556  50.477 -12.262 1.00 49.41  ?  218 LEU A CA  1 
ATOM   1472 C  C   . LEU A 1 218 ? 15.788  51.206 -13.359 1.00 53.84  ?  218 LEU A C   1 
ATOM   1473 O  O   . LEU A 1 218 ? 16.357  51.415 -14.431 1.00 57.14  ?  218 LEU A O   1 
ATOM   1474 C  CB  . LEU A 1 218 ? 16.154  49.009 -12.172 1.00 44.71  ?  218 LEU A CB  1 
ATOM   1475 C  CG  . LEU A 1 218 ? 16.598  48.109 -13.324 1.00 48.20  ?  218 LEU A CG  1 
ATOM   1476 C  CD1 . LEU A 1 218 ? 18.105  48.095 -13.432 1.00 54.28  ?  218 LEU A CD1 1 
ATOM   1477 C  CD2 . LEU A 1 218 ? 16.065  46.707 -13.121 1.00 53.92  ?  218 LEU A CD2 1 
ATOM   1478 N  N   . LEU A 1 219 ? 14.548  51.592 -13.068 1.00 55.31  ?  219 LEU A N   1 
ATOM   1479 C  CA  . LEU A 1 219 ? 13.722  52.331 -14.061 1.00 51.84  ?  219 LEU A CA  1 
ATOM   1480 C  C   . LEU A 1 219 ? 14.396  53.665 -14.383 1.00 55.55  ?  219 LEU A C   1 
ATOM   1481 O  O   . LEU A 1 219 ? 14.718  53.853 -15.555 1.00 65.28  ?  219 LEU A O   1 
ATOM   1482 C  CB  . LEU A 1 219 ? 12.310  52.520 -13.517 1.00 47.74  ?  219 LEU A CB  1 
ATOM   1483 C  CG  . LEU A 1 219 ? 11.552  51.207 -13.324 1.00 51.25  ?  219 LEU A CG  1 
ATOM   1484 C  CD1 . LEU A 1 219 ? 10.076  51.450 -13.014 1.00 44.64  ?  219 LEU A CD1 1 
ATOM   1485 C  CD2 . LEU A 1 219 ? 11.735  50.294 -14.542 1.00 50.45  ?  219 LEU A CD2 1 
ATOM   1486 N  N   . GLY A 1 220 ? 14.662  54.512 -13.384 1.00 51.40  ?  220 GLY A N   1 
ATOM   1487 C  CA  . GLY A 1 220 ? 15.499  55.720 -13.537 1.00 57.93  ?  220 GLY A CA  1 
ATOM   1488 C  C   . GLY A 1 220 ? 16.679  55.520 -14.490 1.00 61.33  ?  220 GLY A C   1 
ATOM   1489 O  O   . GLY A 1 220 ? 16.815  56.335 -15.441 1.00 62.63  ?  220 GLY A O   1 
ATOM   1490 N  N   . ARG A 1 221 ? 17.516  54.507 -14.225 1.00 57.19  ?  221 ARG A N   1 
ATOM   1491 C  CA  . ARG A 1 221 ? 18.657  54.076 -15.077 1.00 57.60  ?  221 ARG A CA  1 
ATOM   1492 C  C   . ARG A 1 221 ? 18.131  53.606 -16.435 1.00 52.84  ?  221 ARG A C   1 
ATOM   1493 O  O   . ARG A 1 221 ? 18.795  53.833 -17.432 1.00 63.16  ?  221 ARG A O   1 
ATOM   1494 C  CB  . ARG A 1 221 ? 19.468  52.941 -14.426 1.00 57.66  ?  221 ARG A CB  1 
ATOM   1495 C  CG  . ARG A 1 221 ? 20.398  53.383 -13.305 1.00 59.30  ?  221 ARG A CG  1 
ATOM   1496 C  CD  . ARG A 1 221 ? 21.313  52.290 -12.791 1.00 63.82  ?  221 ARG A CD  1 
ATOM   1497 N  NE  . ARG A 1 221 ? 21.924  52.709 -11.539 1.00 69.71  ?  221 ARG A NE  1 
ATOM   1498 C  CZ  . ARG A 1 221 ? 21.399  52.531 -10.322 1.00 72.57  ?  221 ARG A CZ  1 
ATOM   1499 N  NH1 . ARG A 1 221 ? 20.252  51.890 -10.151 1.00 76.30  ?  221 ARG A NH1 1 
ATOM   1500 N  NH2 . ARG A 1 221 ? 22.047  52.985 -9.263  1.00 72.28  ?  221 ARG A NH2 1 
ATOM   1501 N  N   . PHE A 1 222 ? 16.977  52.960 -16.498 1.00 61.29  ?  222 PHE A N   1 
ATOM   1502 C  CA  . PHE A 1 222 ? 16.517  52.418 -17.807 1.00 63.28  ?  222 PHE A CA  1 
ATOM   1503 C  C   . PHE A 1 222 ? 16.069  53.584 -18.672 1.00 68.01  ?  222 PHE A C   1 
ATOM   1504 O  O   . PHE A 1 222 ? 16.293  53.554 -19.892 1.00 68.36  ?  222 PHE A O   1 
ATOM   1505 C  CB  . PHE A 1 222 ? 15.409  51.407 -17.514 1.00 56.57  ?  222 PHE A CB  1 
ATOM   1506 C  CG  . PHE A 1 222 ? 15.854  49.973 -17.276 1.00 57.34  ?  222 PHE A CG  1 
ATOM   1507 C  CD1 . PHE A 1 222 ? 17.195  49.622 -17.334 1.00 54.13  ?  222 PHE A CD1 1 
ATOM   1508 C  CD2 . PHE A 1 222 ? 14.923  48.981 -16.997 1.00 60.52  ?  222 PHE A CD2 1 
ATOM   1509 C  CE1 . PHE A 1 222 ? 17.589  48.312 -17.122 1.00 57.76  ?  222 PHE A CE1 1 
ATOM   1510 C  CE2 . PHE A 1 222 ? 15.324  47.673 -16.790 1.00 58.19  ?  222 PHE A CE2 1 
ATOM   1511 C  CZ  . PHE A 1 222 ? 16.655  47.342 -16.855 1.00 58.00  ?  222 PHE A CZ  1 
ATOM   1512 N  N   . ALA A 1 223 ? 15.456  54.588 -18.059 1.00 64.55  ?  223 ALA A N   1 
ATOM   1513 C  CA  . ALA A 1 223 ? 14.952  55.800 -18.741 1.00 69.50  ?  223 ALA A CA  1 
ATOM   1514 C  C   . ALA A 1 223 ? 16.110  56.477 -19.476 1.00 77.09  ?  223 ALA A C   1 
ATOM   1515 O  O   . ALA A 1 223 ? 15.938  56.865 -20.662 1.00 68.10  ?  223 ALA A O   1 
ATOM   1516 C  CB  . ALA A 1 223 ? 14.337  56.734 -17.722 1.00 72.18  ?  223 ALA A CB  1 
ATOM   1517 N  N   . GLU A 1 224 ? 17.240  56.601 -18.772 1.00 85.34  ?  224 GLU A N   1 
ATOM   1518 C  CA  . GLU A 1 224 ? 18.467  57.300 -19.232 1.00 93.77  ?  224 GLU A CA  1 
ATOM   1519 C  C   . GLU A 1 224 ? 19.166  56.424 -20.284 1.00 89.46  ?  224 GLU A C   1 
ATOM   1520 O  O   . GLU A 1 224 ? 19.925  57.001 -21.076 1.00 100.69 ?  224 GLU A O   1 
ATOM   1521 C  CB  . GLU A 1 224 ? 19.344  57.672 -18.022 1.00 96.67  ?  224 GLU A CB  1 
ATOM   1522 C  CG  . GLU A 1 224 ? 18.756  58.784 -17.139 1.00 96.31  ?  224 GLU A CG  1 
ATOM   1523 C  CD  . GLU A 1 224 ? 18.996  58.735 -15.623 1.00 104.41 ?  224 GLU A CD  1 
ATOM   1524 O  OE1 . GLU A 1 224 ? 20.015  58.134 -15.174 1.00 92.48  ?  224 GLU A OE1 1 
ATOM   1525 O  OE2 . GLU A 1 224 ? 18.156  59.311 -14.873 1.00 91.96  ?  224 GLU A OE2 1 
ATOM   1526 N  N   . LEU A 1 225 ? 18.861  55.113 -20.332 1.00 86.11  ?  225 LEU A N   1 
ATOM   1527 C  CA  . LEU A 1 225 ? 19.542  54.069 -21.164 1.00 87.39  ?  225 LEU A CA  1 
ATOM   1528 C  C   . LEU A 1 225 ? 18.751  53.724 -22.439 1.00 97.25  ?  225 LEU A C   1 
ATOM   1529 O  O   . LEU A 1 225 ? 19.209  52.841 -23.196 1.00 108.00 ?  225 LEU A O   1 
ATOM   1530 C  CB  . LEU A 1 225 ? 19.741  52.801 -20.326 1.00 83.39  ?  225 LEU A CB  1 
ATOM   1531 C  CG  . LEU A 1 225 ? 20.363  51.616 -21.064 1.00 87.54  ?  225 LEU A CG  1 
ATOM   1532 C  CD1 . LEU A 1 225 ? 21.774  51.957 -21.532 1.00 96.76  ?  225 LEU A CD1 1 
ATOM   1533 C  CD2 . LEU A 1 225 ? 20.376  50.360 -20.199 1.00 84.60  ?  225 LEU A CD2 1 
ATOM   1534 N  N   . ARG A 1 226 ? 17.596  54.349 -22.674 1.00 91.53  ?  226 ARG A N   1 
ATOM   1535 C  CA  . ARG A 1 226 ? 16.921  54.305 -23.998 1.00 82.45  ?  226 ARG A CA  1 
ATOM   1536 C  C   . ARG A 1 226 ? 16.943  55.713 -24.623 1.00 82.15  ?  226 ARG A C   1 
ATOM   1537 O  O   . ARG A 1 226 ? 16.443  55.850 -25.741 1.00 80.54  ?  226 ARG A O   1 
ATOM   1538 C  CB  . ARG A 1 226 ? 15.513  53.719 -23.862 1.00 74.30  ?  226 ARG A CB  1 
ATOM   1539 C  CG  . ARG A 1 226 ? 14.693  54.346 -22.751 1.00 64.02  ?  226 ARG A CG  1 
ATOM   1540 C  CD  . ARG A 1 226 ? 13.199  54.148 -22.888 1.00 58.41  ?  226 ARG A CD  1 
ATOM   1541 N  NE  . ARG A 1 226 ? 12.539  55.011 -21.909 1.00 62.17  ?  226 ARG A NE  1 
ATOM   1542 C  CZ  . ARG A 1 226 ? 11.247  54.989 -21.598 1.00 55.52  ?  226 ARG A CZ  1 
ATOM   1543 N  NH1 . ARG A 1 226 ? 10.439  54.125 -22.188 1.00 55.46  ?  226 ARG A NH1 1 
ATOM   1544 N  NH2 . ARG A 1 226 ? 10.773  55.834 -20.696 1.00 53.16  ?  226 ARG A NH2 1 
ATOM   1545 N  N   . ARG A 1 227 ? 17.514  56.710 -23.936 1.00 80.78  ?  227 ARG A N   1 
ATOM   1546 C  CA  . ARG A 1 227 ? 17.997  57.976 -24.551 1.00 85.78  ?  227 ARG A CA  1 
ATOM   1547 C  C   . ARG A 1 227 ? 19.398  57.793 -25.164 1.00 96.42  ?  227 ARG A C   1 
ATOM   1548 O  O   . ARG A 1 227 ? 19.707  58.563 -26.074 1.00 102.92 ?  227 ARG A O   1 
ATOM   1549 C  CB  . ARG A 1 227 ? 18.080  59.112 -23.531 1.00 81.41  ?  227 ARG A CB  1 
ATOM   1550 C  CG  . ARG A 1 227 ? 16.739  59.571 -22.996 1.00 81.83  ?  227 ARG A CG  1 
ATOM   1551 C  CD  . ARG A 1 227 ? 16.980  60.721 -22.045 1.00 87.11  ?  227 ARG A CD  1 
ATOM   1552 N  NE  . ARG A 1 227 ? 15.734  61.163 -21.440 1.00 99.51  ?  227 ARG A NE  1 
ATOM   1553 C  CZ  . ARG A 1 227 ? 15.631  62.076 -20.481 1.00 101.96 ?  227 ARG A CZ  1 
ATOM   1554 N  NH1 . ARG A 1 227 ? 16.717  62.665 -20.004 1.00 99.22  ?  227 ARG A NH1 1 
ATOM   1555 N  NH2 . ARG A 1 227 ? 14.439  62.393 -20.003 1.00 101.13 ?  227 ARG A NH2 1 
ATOM   1556 N  N   . SER A 1 228 ? 20.237  56.857 -24.692 1.00 101.03 ?  228 SER A N   1 
ATOM   1557 C  CA  . SER A 1 228 ? 21.613  56.649 -25.231 1.00 104.96 ?  228 SER A CA  1 
ATOM   1558 C  C   . SER A 1 228 ? 21.526  56.396 -26.735 1.00 120.06 ?  228 SER A C   1 
ATOM   1559 O  O   . SER A 1 228 ? 20.556  55.795 -27.201 1.00 110.51 ?  228 SER A O   1 
ATOM   1560 C  CB  . SER A 1 228 ? 22.366  55.531 -24.543 1.00 103.26 ?  228 SER A CB  1 
ATOM   1561 O  OG  . SER A 1 228 ? 22.866  55.945 -23.283 1.00 99.65  ?  228 SER A OG  1 
ATOM   1562 N  N   . VAL A 1 235 ? 16.440  47.329 -27.594 1.00 96.44  ?  235 VAL A N   1 
ATOM   1563 C  CA  . VAL A 1 235 ? 15.884  47.201 -26.209 1.00 82.16  ?  235 VAL A CA  1 
ATOM   1564 C  C   . VAL A 1 235 ? 14.518  47.878 -26.124 1.00 71.41  ?  235 VAL A C   1 
ATOM   1565 O  O   . VAL A 1 235 ? 14.502  49.083 -25.842 1.00 65.84  ?  235 VAL A O   1 
ATOM   1566 C  CB  . VAL A 1 235 ? 16.821  47.780 -25.131 1.00 83.96  ?  235 VAL A CB  1 
ATOM   1567 C  CG1 . VAL A 1 235 ? 16.212  47.763 -23.743 1.00 84.76  ?  235 VAL A CG1 1 
ATOM   1568 C  CG2 . VAL A 1 235 ? 18.157  47.060 -25.117 1.00 92.42  ?  235 VAL A CG2 1 
ATOM   1569 N  N   . SER A 1 236 ? 13.434  47.102 -26.241 1.00 60.32  ?  236 SER A N   1 
ATOM   1570 C  CA  . SER A 1 236 ? 12.028  47.576 -26.130 1.00 62.56  ?  236 SER A CA  1 
ATOM   1571 C  C   . SER A 1 236 ? 11.675  47.986 -24.691 1.00 63.28  ?  236 SER A C   1 
ATOM   1572 O  O   . SER A 1 236 ? 12.445  47.700 -23.750 1.00 64.13  ?  236 SER A O   1 
ATOM   1573 C  CB  . SER A 1 236 ? 11.059  46.527 -26.636 1.00 67.79  ?  236 SER A CB  1 
ATOM   1574 O  OG  . SER A 1 236 ? 11.383  45.242 -26.128 1.00 62.06  ?  236 SER A OG  1 
ATOM   1575 N  N   . ASP A 1 237 ? 10.525  48.638 -24.540 1.00 60.72  ?  237 ASP A N   1 
ATOM   1576 C  CA  . ASP A 1 237 ? 9.827   48.855 -23.244 1.00 58.20  ?  237 ASP A CA  1 
ATOM   1577 C  C   . ASP A 1 237 ? 9.371   47.499 -22.680 1.00 61.99  ?  237 ASP A C   1 
ATOM   1578 O  O   . ASP A 1 237 ? 9.431   47.323 -21.444 1.00 62.59  ?  237 ASP A O   1 
ATOM   1579 C  CB  . ASP A 1 237 ? 8.679   49.851 -23.418 1.00 55.65  ?  237 ASP A CB  1 
ATOM   1580 C  CG  . ASP A 1 237 ? 9.182   51.278 -23.542 1.00 55.05  ?  237 ASP A CG  1 
ATOM   1581 O  OD1 . ASP A 1 237 ? 10.386  51.439 -23.864 1.00 56.18  ?  237 ASP A OD1 1 
ATOM   1582 O  OD2 . ASP A 1 237 ? 8.396   52.210 -23.259 1.00 49.30  ?  237 ASP A OD2 1 
ATOM   1583 N  N   . GLU A 1 238 ? 8.959   46.574 -23.550 1.00 61.55  ?  238 GLU A N   1 
ATOM   1584 C  CA  . GLU A 1 238 ? 8.640   45.170 -23.187 1.00 62.64  ?  238 GLU A CA  1 
ATOM   1585 C  C   . GLU A 1 238 ? 9.822   44.589 -22.409 1.00 62.32  ?  238 GLU A C   1 
ATOM   1586 O  O   . GLU A 1 238 ? 9.601   44.119 -21.270 1.00 71.12  ?  238 GLU A O   1 
ATOM   1587 C  CB  . GLU A 1 238 ? 8.342   44.351 -24.444 1.00 69.26  ?  238 GLU A CB  1 
ATOM   1588 C  CG  . GLU A 1 238 ? 7.930   42.906 -24.194 1.00 68.11  ?  238 GLU A CG  1 
ATOM   1589 C  CD  . GLU A 1 238 ? 7.594   42.129 -25.453 1.00 70.11  ?  238 GLU A CD  1 
ATOM   1590 O  OE1 . GLU A 1 238 ? 7.716   42.703 -26.538 1.00 65.16  ?  238 GLU A OE1 1 
ATOM   1591 O  OE2 . GLU A 1 238 ? 7.211   40.949 -25.341 1.00 76.48  ?  238 GLU A OE2 1 
ATOM   1592 N  N   . LEU A 1 239 ? 11.021  44.602 -22.996 1.00 58.11  ?  239 LEU A N   1 
ATOM   1593 C  CA  . LEU A 1 239 ? 12.207  43.949 -22.388 1.00 57.38  ?  239 LEU A CA  1 
ATOM   1594 C  C   . LEU A 1 239 ? 12.574  44.679 -21.090 1.00 56.70  ?  239 LEU A C   1 
ATOM   1595 O  O   . LEU A 1 239 ? 13.003  43.999 -20.158 1.00 54.27  ?  239 LEU A O   1 
ATOM   1596 C  CB  . LEU A 1 239 ? 13.386  43.949 -23.363 1.00 63.64  ?  239 LEU A CB  1 
ATOM   1597 C  CG  . LEU A 1 239 ? 14.662  43.280 -22.836 1.00 71.21  ?  239 LEU A CG  1 
ATOM   1598 C  CD1 . LEU A 1 239 ? 14.478  41.765 -22.706 1.00 67.57  ?  239 LEU A CD1 1 
ATOM   1599 C  CD2 . LEU A 1 239 ? 15.872  43.620 -23.708 1.00 70.41  ?  239 LEU A CD2 1 
ATOM   1600 N  N   . LEU A 1 240 ? 12.431  46.007 -21.027 1.00 53.61  ?  240 LEU A N   1 
ATOM   1601 C  CA  . LEU A 1 240 ? 12.859  46.790 -19.840 1.00 55.02  ?  240 LEU A CA  1 
ATOM   1602 C  C   . LEU A 1 240 ? 11.998  46.396 -18.635 1.00 58.87  ?  240 LEU A C   1 
ATOM   1603 O  O   . LEU A 1 240 ? 12.558  45.967 -17.586 1.00 57.20  ?  240 LEU A O   1 
ATOM   1604 C  CB  . LEU A 1 240 ? 12.756  48.288 -20.133 1.00 59.73  ?  240 LEU A CB  1 
ATOM   1605 C  CG  . LEU A 1 240 ? 13.870  48.872 -21.006 1.00 65.92  ?  240 LEU A CG  1 
ATOM   1606 C  CD1 . LEU A 1 240 ? 13.851  50.395 -20.947 1.00 60.72  ?  240 LEU A CD1 1 
ATOM   1607 C  CD2 . LEU A 1 240 ? 15.249  48.344 -20.603 1.00 66.00  ?  240 LEU A CD2 1 
ATOM   1608 N  N   . ALA A 1 241 ? 10.679  46.521 -18.781 1.00 55.98  ?  241 ALA A N   1 
ATOM   1609 C  CA  . ALA A 1 241 ? 9.703   46.139 -17.739 1.00 49.95  ?  241 ALA A CA  1 
ATOM   1610 C  C   . ALA A 1 241 ? 9.844   44.641 -17.417 1.00 44.28  ?  241 ALA A C   1 
ATOM   1611 O  O   . ALA A 1 241 ? 9.495   44.289 -16.312 1.00 37.82  ?  241 ALA A O   1 
ATOM   1612 C  CB  . ALA A 1 241 ? 8.309   46.496 -18.185 1.00 53.86  ?  241 ALA A CB  1 
ATOM   1613 N  N   . THR A 1 242 ? 10.318  43.806 -18.348 1.00 40.27  ?  242 THR A N   1 
ATOM   1614 C  CA  . THR A 1 242 ? 10.463  42.341 -18.174 1.00 41.07  ?  242 THR A CA  1 
ATOM   1615 C  C   . THR A 1 242 ? 11.601  42.060 -17.198 1.00 43.64  ?  242 THR A C   1 
ATOM   1616 O  O   . THR A 1 242 ? 11.422  41.198 -16.329 1.00 49.24  ?  242 THR A O   1 
ATOM   1617 C  CB  . THR A 1 242 ? 10.715  41.596 -19.490 1.00 42.17  ?  242 THR A CB  1 
ATOM   1618 O  OG1 . THR A 1 242 ? 9.582   41.830 -20.333 1.00 42.78  ?  242 THR A OG1 1 
ATOM   1619 C  CG2 . THR A 1 242 ? 10.936  40.105 -19.297 1.00 39.55  ?  242 THR A CG2 1 
ATOM   1620 N  N   . VAL A 1 243 ? 12.734  42.733 -17.351 1.00 48.04  ?  243 VAL A N   1 
ATOM   1621 C  CA  . VAL A 1 243 ? 13.884  42.610 -16.401 1.00 48.80  ?  243 VAL A CA  1 
ATOM   1622 C  C   . VAL A 1 243 ? 13.409  43.120 -15.038 1.00 47.35  ?  243 VAL A C   1 
ATOM   1623 O  O   . VAL A 1 243 ? 13.627  42.423 -14.035 1.00 48.49  ?  243 VAL A O   1 
ATOM   1624 C  CB  . VAL A 1 243 ? 15.127  43.377 -16.893 1.00 47.37  ?  243 VAL A CB  1 
ATOM   1625 C  CG1 . VAL A 1 243 ? 16.203  43.467 -15.821 1.00 49.88  ?  243 VAL A CG1 1 
ATOM   1626 C  CG2 . VAL A 1 243 ? 15.702  42.750 -18.150 1.00 44.17  ?  243 VAL A CG2 1 
ATOM   1627 N  N   . ALA A 1 244 ? 12.775  44.295 -15.027 1.00 44.14  ?  244 ALA A N   1 
ATOM   1628 C  CA  . ALA A 1 244 ? 12.307  44.989 -13.817 1.00 42.99  ?  244 ALA A CA  1 
ATOM   1629 C  C   . ALA A 1 244 ? 11.471  44.021 -12.987 1.00 47.75  ?  244 ALA A C   1 
ATOM   1630 O  O   . ALA A 1 244 ? 11.701  43.962 -11.768 1.00 45.90  ?  244 ALA A O   1 
ATOM   1631 C  CB  . ALA A 1 244 ? 11.505  46.201 -14.203 1.00 44.54  ?  244 ALA A CB  1 
ATOM   1632 N  N   . LEU A 1 245 ? 10.561  43.294 -13.651 1.00 47.13  ?  245 LEU A N   1 
ATOM   1633 C  CA  . LEU A 1 245 ? 9.485   42.481 -13.024 1.00 45.78  ?  245 LEU A CA  1 
ATOM   1634 C  C   . LEU A 1 245 ? 10.067  41.148 -12.545 1.00 46.59  ?  245 LEU A C   1 
ATOM   1635 O  O   . LEU A 1 245 ? 9.840   40.761 -11.376 1.00 44.16  ?  245 LEU A O   1 
ATOM   1636 C  CB  . LEU A 1 245 ? 8.348   42.277 -14.036 1.00 45.02  ?  245 LEU A CB  1 
ATOM   1637 C  CG  . LEU A 1 245 ? 7.133   41.478 -13.554 1.00 42.41  ?  245 LEU A CG  1 
ATOM   1638 C  CD1 . LEU A 1 245 ? 6.555   42.047 -12.276 1.00 41.48  ?  245 LEU A CD1 1 
ATOM   1639 C  CD2 . LEU A 1 245 ? 6.060   41.456 -14.617 1.00 44.75  ?  245 LEU A CD2 1 
ATOM   1640 N  N   . SER A 1 246 ? 10.803  40.459 -13.409 1.00 47.50  ?  246 SER A N   1 
ATOM   1641 C  CA  . SER A 1 246 ? 11.551  39.248 -13.001 1.00 46.86  ?  246 SER A CA  1 
ATOM   1642 C  C   . SER A 1 246 ? 12.482  39.593 -11.825 1.00 44.02  ?  246 SER A C   1 
ATOM   1643 O  O   . SER A 1 246 ? 12.539  38.811 -10.860 1.00 42.50  ?  246 SER A O   1 
ATOM   1644 C  CB  . SER A 1 246 ? 12.269  38.643 -14.162 1.00 46.65  ?  246 SER A CB  1 
ATOM   1645 O  OG  . SER A 1 246 ? 13.248  39.538 -14.641 1.00 57.01  ?  246 SER A OG  1 
ATOM   1646 N  N   . LEU A 1 247 ? 13.150  40.743 -11.853 1.00 43.39  ?  247 LEU A N   1 
ATOM   1647 C  CA  . LEU A 1 247 ? 14.072  41.138 -10.749 1.00 45.19  ?  247 LEU A CA  1 
ATOM   1648 C  C   . LEU A 1 247 ? 13.268  41.354 -9.466  1.00 39.57  ?  247 LEU A C   1 
ATOM   1649 O  O   . LEU A 1 247 ? 13.674  40.811 -8.425  1.00 40.48  ?  247 LEU A O   1 
ATOM   1650 C  CB  . LEU A 1 247 ? 14.877  42.389 -11.124 1.00 47.70  ?  247 LEU A CB  1 
ATOM   1651 C  CG  . LEU A 1 247 ? 15.845  42.208 -12.292 1.00 52.33  ?  247 LEU A CG  1 
ATOM   1652 C  CD1 . LEU A 1 247 ? 16.477  43.530 -12.674 1.00 55.49  ?  247 LEU A CD1 1 
ATOM   1653 C  CD2 . LEU A 1 247 ? 16.935  41.192 -11.965 1.00 58.39  ?  247 LEU A CD2 1 
ATOM   1654 N  N   . PHE A 1 248 ? 12.165  42.098 -9.545  1.00 37.13  ?  248 PHE A N   1 
ATOM   1655 C  CA  . PHE A 1 248 ? 11.282  42.368 -8.388  1.00 35.11  ?  248 PHE A CA  1 
ATOM   1656 C  C   . PHE A 1 248 ? 10.742  41.033 -7.884  1.00 36.15  ?  248 PHE A C   1 
ATOM   1657 O  O   . PHE A 1 248 ? 10.719  40.807 -6.663  1.00 38.58  ?  248 PHE A O   1 
ATOM   1658 C  CB  . PHE A 1 248 ? 10.127  43.291 -8.744  1.00 35.69  ?  248 PHE A CB  1 
ATOM   1659 C  CG  . PHE A 1 248 ? 9.221   43.611 -7.580  1.00 38.63  ?  248 PHE A CG  1 
ATOM   1660 C  CD1 . PHE A 1 248 ? 8.241   42.718 -7.173  1.00 36.37  ?  248 PHE A CD1 1 
ATOM   1661 C  CD2 . PHE A 1 248 ? 9.357   44.804 -6.878  1.00 40.69  ?  248 PHE A CD2 1 
ATOM   1662 C  CE1 . PHE A 1 248 ? 7.410   43.014 -6.102  1.00 35.71  ?  248 PHE A CE1 1 
ATOM   1663 C  CE2 . PHE A 1 248 ? 8.520   45.101 -5.812  1.00 41.76  ?  248 PHE A CE2 1 
ATOM   1664 C  CZ  . PHE A 1 248 ? 7.534   44.214 -5.439  1.00 38.68  ?  248 PHE A CZ  1 
ATOM   1665 N  N   . GLY A 1 249 ? 10.345  40.175 -8.812  1.00 32.03  ?  249 GLY A N   1 
ATOM   1666 C  CA  . GLY A 1 249 ? 9.716   38.897 -8.480  1.00 33.83  ?  249 GLY A CA  1 
ATOM   1667 C  C   . GLY A 1 249 ? 10.641  38.048 -7.641  1.00 34.95  ?  249 GLY A C   1 
ATOM   1668 O  O   . GLY A 1 249 ? 10.280  37.718 -6.468  1.00 40.05  ?  249 GLY A O   1 
ATOM   1669 N  N   . ALA A 1 250 ? 11.792  37.721 -8.220  1.00 32.55  ?  250 ALA A N   1 
ATOM   1670 C  CA  . ALA A 1 250 ? 12.763  36.731 -7.715  1.00 33.31  ?  250 ALA A CA  1 
ATOM   1671 C  C   . ALA A 1 250 ? 13.333  37.188 -6.362  1.00 34.50  ?  250 ALA A C   1 
ATOM   1672 O  O   . ALA A 1 250 ? 13.518  36.349 -5.447  1.00 35.91  ?  250 ALA A O   1 
ATOM   1673 C  CB  . ALA A 1 250 ? 13.833  36.565 -8.755  1.00 37.06  ?  250 ALA A CB  1 
ATOM   1674 N  N   . GLY A 1 251 ? 13.542  38.491 -6.209  1.00 31.72  ?  251 GLY A N   1 
ATOM   1675 C  CA  . GLY A 1 251 ? 14.166  39.034 -5.005  1.00 33.74  ?  251 GLY A CA  1 
ATOM   1676 C  C   . GLY A 1 251 ? 13.191  39.081 -3.849  1.00 36.17  ?  251 GLY A C   1 
ATOM   1677 O  O   . GLY A 1 251 ? 13.596  38.711 -2.730  1.00 37.77  ?  251 GLY A O   1 
ATOM   1678 N  N   . ALA A 1 252 ? 11.976  39.574 -4.081  1.00 33.82  ?  252 ALA A N   1 
ATOM   1679 C  CA  . ALA A 1 252 ? 10.972  39.747 -3.012  1.00 36.60  ?  252 ALA A CA  1 
ATOM   1680 C  C   . ALA A 1 252 ? 10.556  38.364 -2.519  1.00 33.90  ?  252 ALA A C   1 
ATOM   1681 O  O   . ALA A 1 252 ? 10.511  38.130 -1.308  1.00 34.38  ?  252 ALA A O   1 
ATOM   1682 C  CB  . ALA A 1 252 ? 9.792   40.548 -3.492  1.00 39.10  ?  252 ALA A CB  1 
ATOM   1683 N  N   . VAL A 1 253 ? 10.325  37.439 -3.424  1.00 33.35  ?  253 VAL A N   1 
ATOM   1684 C  CA  . VAL A 1 253 ? 9.858   36.097 -2.992  1.00 34.70  ?  253 VAL A CA  1 
ATOM   1685 C  C   . VAL A 1 253 ? 10.998  35.432 -2.198  1.00 37.01  ?  253 VAL A C   1 
ATOM   1686 O  O   . VAL A 1 253 ? 10.714  34.848 -1.123  1.00 37.83  ?  253 VAL A O   1 
ATOM   1687 C  CB  . VAL A 1 253 ? 9.353   35.273 -4.195  1.00 34.58  ?  253 VAL A CB  1 
ATOM   1688 C  CG1 . VAL A 1 253 ? 10.471  34.724 -5.090  1.00 34.90  ?  253 VAL A CG1 1 
ATOM   1689 C  CG2 . VAL A 1 253 ? 8.425   34.163 -3.737  1.00 35.17  ?  253 VAL A CG2 1 
ATOM   1690 N  N   . SER A 1 254 ? 12.248  35.580 -2.661  1.00 36.82  ?  254 SER A N   1 
ATOM   1691 C  CA  . SER A 1 254 ? 13.441  34.928 -2.060  1.00 36.20  ?  254 SER A CA  1 
ATOM   1692 C  C   . SER A 1 254 ? 13.829  35.597 -0.724  1.00 33.40  ?  254 SER A C   1 
ATOM   1693 O  O   . SER A 1 254 ? 14.226  34.907 0.218   1.00 33.57  ?  254 SER A O   1 
ATOM   1694 C  CB  . SER A 1 254 ? 14.598  34.914 -3.038  1.00 37.03  ?  254 SER A CB  1 
ATOM   1695 O  OG  . SER A 1 254 ? 14.313  34.053 -4.134  1.00 35.45  ?  254 SER A OG  1 
ATOM   1696 N  N   . THR A 1 255 ? 13.784  36.912 -0.619  1.00 30.48  ?  255 THR A N   1 
ATOM   1697 C  CA  . THR A 1 255 ? 14.235  37.568 0.617   1.00 32.16  ?  255 THR A CA  1 
ATOM   1698 C  C   . THR A 1 255 ? 13.162  37.333 1.674   1.00 30.24  ?  255 THR A C   1 
ATOM   1699 O  O   . THR A 1 255 ? 13.544  36.941 2.776   1.00 29.78  ?  255 THR A O   1 
ATOM   1700 C  CB  . THR A 1 255 ? 14.576  39.034 0.383   1.00 35.74  ?  255 THR A CB  1 
ATOM   1701 O  OG1 . THR A 1 255 ? 13.409  39.723 -0.075  1.00 45.42  ?  255 THR A OG1 1 
ATOM   1702 C  CG2 . THR A 1 255 ? 15.725  39.155 -0.589  1.00 36.30  ?  255 THR A CG2 1 
ATOM   1703 N  N   . SER A 1 256 ? 11.883  37.466 1.316   1.00 29.00  ?  256 SER A N   1 
ATOM   1704 C  CA  . SER A 1 256 ? 10.754  37.290 2.258   1.00 29.12  ?  256 SER A CA  1 
ATOM   1705 C  C   . SER A 1 256 ? 10.763  35.847 2.780   1.00 30.91  ?  256 SER A C   1 
ATOM   1706 O  O   . SER A 1 256 ? 10.740  35.644 4.008   1.00 32.00  ?  256 SER A O   1 
ATOM   1707 C  CB  . SER A 1 256 ? 9.430   37.656 1.645   1.00 28.39  ?  256 SER A CB  1 
ATOM   1708 O  OG  . SER A 1 256 ? 8.371   37.391 2.570   1.00 29.43  ?  256 SER A OG  1 
ATOM   1709 N  N   . ALA A 1 257 ? 10.859  34.856 1.903   1.00 29.45  ?  257 ALA A N   1 
ATOM   1710 C  CA  . ALA A 1 257 ? 10.836  33.446 2.359   1.00 29.49  ?  257 ALA A CA  1 
ATOM   1711 C  C   . ALA A 1 257 ? 12.052  33.200 3.255   1.00 27.34  ?  257 ALA A C   1 
ATOM   1712 O  O   . ALA A 1 257 ? 11.874  32.625 4.324   1.00 26.85  ?  257 ALA A O   1 
ATOM   1713 C  CB  . ALA A 1 257 ? 10.755  32.479 1.199   1.00 27.81  ?  257 ALA A CB  1 
ATOM   1714 N  N   . PHE A 1 258 ? 13.255  33.619 2.860   1.00 27.73  ?  258 PHE A N   1 
ATOM   1715 C  CA  . PHE A 1 258 ? 14.458  33.314 3.678   1.00 27.48  ?  258 PHE A CA  1 
ATOM   1716 C  C   . PHE A 1 258 ? 14.277  33.955 5.059   1.00 27.13  ?  258 PHE A C   1 
ATOM   1717 O  O   . PHE A 1 258 ? 14.542  33.284 6.048   1.00 27.51  ?  258 PHE A O   1 
ATOM   1718 C  CB  . PHE A 1 258 ? 15.761  33.757 3.021   1.00 28.00  ?  258 PHE A CB  1 
ATOM   1719 C  CG  . PHE A 1 258 ? 16.930  33.725 3.961   1.00 26.54  ?  258 PHE A CG  1 
ATOM   1720 C  CD1 . PHE A 1 258 ? 17.281  32.543 4.597   1.00 27.13  ?  258 PHE A CD1 1 
ATOM   1721 C  CD2 . PHE A 1 258 ? 17.641  34.878 4.253   1.00 26.30  ?  258 PHE A CD2 1 
ATOM   1722 C  CE1 . PHE A 1 258 ? 18.326  32.516 5.506   1.00 26.91  ?  258 PHE A CE1 1 
ATOM   1723 C  CE2 . PHE A 1 258 ? 18.699  34.852 5.152   1.00 26.42  ?  258 PHE A CE2 1 
ATOM   1724 C  CZ  . PHE A 1 258 ? 19.054  33.669 5.761   1.00 27.15  ?  258 PHE A CZ  1 
ATOM   1725 N  N   . LEU A 1 259 ? 13.772  35.187 5.124   1.00 26.70  ?  259 LEU A N   1 
ATOM   1726 C  CA  . LEU A 1 259 ? 13.685  35.961 6.387   1.00 27.23  ?  259 LEU A CA  1 
ATOM   1727 C  C   . LEU A 1 259 ? 12.702  35.270 7.340   1.00 28.12  ?  259 LEU A C   1 
ATOM   1728 O  O   . LEU A 1 259 ? 12.990  35.183 8.560   1.00 29.61  ?  259 LEU A O   1 
ATOM   1729 C  CB  . LEU A 1 259 ? 13.301  37.403 6.058   1.00 26.09  ?  259 LEU A CB  1 
ATOM   1730 C  CG  . LEU A 1 259 ? 13.103  38.321 7.253   1.00 28.05  ?  259 LEU A CG  1 
ATOM   1731 C  CD1 . LEU A 1 259 ? 14.200  38.160 8.278   1.00 29.93  ?  259 LEU A CD1 1 
ATOM   1732 C  CD2 . LEU A 1 259 ? 13.047  39.771 6.788   1.00 34.44  ?  259 LEU A CD2 1 
ATOM   1733 N  N   . GLN A 1 260 ? 11.625  34.702 6.811   1.00 29.20  ?  260 GLN A N   1 
ATOM   1734 C  CA  . GLN A 1 260 ? 10.690  33.873 7.611   1.00 29.12  ?  260 GLN A CA  1 
ATOM   1735 C  C   . GLN A 1 260 ? 11.408  32.655 8.227   1.00 29.77  ?  260 GLN A C   1 
ATOM   1736 O  O   . GLN A 1 260 ? 11.144  32.388 9.398   1.00 30.45  ?  260 GLN A O   1 
ATOM   1737 C  CB  . GLN A 1 260 ? 9.499   33.491 6.749   1.00 29.86  ?  260 GLN A CB  1 
ATOM   1738 C  CG  . GLN A 1 260 ? 8.638   34.696 6.428   1.00 31.19  ?  260 GLN A CG  1 
ATOM   1739 C  CD  . GLN A 1 260 ? 7.557   34.251 5.488   1.00 35.99  ?  260 GLN A CD  1 
ATOM   1740 O  OE1 . GLN A 1 260 ? 6.582   33.657 5.925   1.00 38.21  ?  260 GLN A OE1 1 
ATOM   1741 N  NE2 . GLN A 1 260 ? 7.756   34.479 4.195   1.00 39.46  ?  260 GLN A NE2 1 
ATOM   1742 N  N   . HIS A 1 261 ? 12.282  31.940 7.501   1.00 29.41  ?  261 HIS A N   1 
ATOM   1743 C  CA  . HIS A 1 261 ? 13.070  30.787 8.050   1.00 28.35  ?  261 HIS A CA  1 
ATOM   1744 C  C   . HIS A 1 261 ? 14.060  31.277 9.117   1.00 28.08  ?  261 HIS A C   1 
ATOM   1745 O  O   . HIS A 1 261 ? 14.071  30.728 10.241  1.00 31.15  ?  261 HIS A O   1 
ATOM   1746 C  CB  . HIS A 1 261 ? 13.748  30.000 6.927   1.00 29.00  ?  261 HIS A CB  1 
ATOM   1747 C  CG  . HIS A 1 261 ? 12.773  29.235 6.087   1.00 31.88  ?  261 HIS A CG  1 
ATOM   1748 N  ND1 . HIS A 1 261 ? 12.811  27.860 5.978   1.00 33.33  ?  261 HIS A ND1 1 
ATOM   1749 C  CD2 . HIS A 1 261 ? 11.718  29.648 5.340   1.00 31.57  ?  261 HIS A CD2 1 
ATOM   1750 C  CE1 . HIS A 1 261 ? 11.824  27.468 5.179   1.00 35.24  ?  261 HIS A CE1 1 
ATOM   1751 N  NE2 . HIS A 1 261 ? 11.146  28.553 4.763   1.00 30.22  ?  261 HIS A NE2 1 
ATOM   1752 N  N   . ALA A 1 262 ? 14.808  32.341 8.843   1.00 26.49  ?  262 ALA A N   1 
ATOM   1753 C  CA  . ALA A 1 262 ? 15.716  32.951 9.834   1.00 24.93  ?  262 ALA A CA  1 
ATOM   1754 C  C   . ALA A 1 262 ? 14.899  33.341 11.072  1.00 23.94  ?  262 ALA A C   1 
ATOM   1755 O  O   . ALA A 1 262 ? 15.373  33.125 12.207  1.00 23.53  ?  262 ALA A O   1 
ATOM   1756 C  CB  . ALA A 1 262 ? 16.463  34.107 9.228   1.00 24.91  ?  262 ALA A CB  1 
ATOM   1757 N  N   . ILE A 1 263 ? 13.689  33.853 10.898  1.00 24.67  ?  263 ILE A N   1 
ATOM   1758 C  CA  . ILE A 1 263 ? 12.876  34.293 12.073  1.00 27.58  ?  263 ILE A CA  1 
ATOM   1759 C  C   . ILE A 1 263 ? 12.491  33.061 12.897  1.00 26.84  ?  263 ILE A C   1 
ATOM   1760 O  O   . ILE A 1 263 ? 12.680  33.081 14.126  1.00 26.30  ?  263 ILE A O   1 
ATOM   1761 C  CB  . ILE A 1 263 ? 11.651  35.108 11.621  1.00 30.33  ?  263 ILE A CB  1 
ATOM   1762 C  CG1 . ILE A 1 263 ? 12.071  36.513 11.169  1.00 28.88  ?  263 ILE A CG1 1 
ATOM   1763 C  CG2 . ILE A 1 263 ? 10.592  35.143 12.720  1.00 29.54  ?  263 ILE A CG2 1 
ATOM   1764 C  CD1 . ILE A 1 263 ? 10.936  37.357 10.656  1.00 27.78  ?  263 ILE A CD1 1 
ATOM   1765 N  N   . ILE A 1 264 ? 12.031  31.999 12.235  1.00 26.36  ?  264 ILE A N   1 
ATOM   1766 C  CA  . ILE A 1 264 ? 11.720  30.715 12.917  1.00 27.11  ?  264 ILE A CA  1 
ATOM   1767 C  C   . ILE A 1 264 ? 12.970  30.245 13.695  1.00 28.45  ?  264 ILE A C   1 
ATOM   1768 O  O   . ILE A 1 264 ? 12.853  29.942 14.903  1.00 26.40  ?  264 ILE A O   1 
ATOM   1769 C  CB  . ILE A 1 264 ? 11.208  29.668 11.915  1.00 26.52  ?  264 ILE A CB  1 
ATOM   1770 C  CG1 . ILE A 1 264 ? 9.953   30.154 11.183  1.00 25.08  ?  264 ILE A CG1 1 
ATOM   1771 C  CG2 . ILE A 1 264 ? 10.962  28.350 12.638  1.00 27.12  ?  264 ILE A CG2 1 
ATOM   1772 C  CD1 . ILE A 1 264 ? 9.367   29.146 10.253  1.00 25.18  ?  264 ILE A CD1 1 
ATOM   1773 N  N   . ALA A 1 265 ? 14.136  30.210 13.045  1.00 27.98  ?  265 ALA A N   1 
ATOM   1774 C  CA  . ALA A 1 265 ? 15.413  29.803 13.673  1.00 25.74  ?  265 ALA A CA  1 
ATOM   1775 C  C   . ALA A 1 265 ? 15.642  30.612 14.959  1.00 26.54  ?  265 ALA A C   1 
ATOM   1776 O  O   . ALA A 1 265 ? 15.872  29.972 16.001  1.00 28.21  ?  265 ALA A O   1 
ATOM   1777 C  CB  . ALA A 1 265 ? 16.525  29.936 12.681  1.00 25.44  ?  265 ALA A CB  1 
ATOM   1778 N  N   . LEU A 1 266 ? 15.466  31.944 14.939  1.00 27.05  ?  266 LEU A N   1 
ATOM   1779 C  CA  . LEU A 1 266 ? 15.720  32.821 16.116  1.00 25.59  ?  266 LEU A CA  1 
ATOM   1780 C  C   . LEU A 1 266 ? 14.623  32.668 17.175  1.00 28.35  ?  266 LEU A C   1 
ATOM   1781 O  O   . LEU A 1 266 ? 14.934  32.851 18.368  1.00 32.71  ?  266 LEU A O   1 
ATOM   1782 C  CB  . LEU A 1 266 ? 15.808  34.274 15.663  1.00 26.46  ?  266 LEU A CB  1 
ATOM   1783 C  CG  . LEU A 1 266 ? 16.971  34.621 14.722  1.00 28.79  ?  266 LEU A CG  1 
ATOM   1784 C  CD1 . LEU A 1 266 ? 17.132  36.136 14.644  1.00 32.96  ?  266 LEU A CD1 1 
ATOM   1785 C  CD2 . LEU A 1 266 ? 18.291  33.999 15.141  1.00 26.17  ?  266 LEU A CD2 1 
ATOM   1786 N  N   . ALA A 1 267 ? 13.380  32.382 16.785  1.00 28.63  ?  267 ALA A N   1 
ATOM   1787 C  CA  . ALA A 1 267 ? 12.270  32.111 17.728  1.00 27.72  ?  267 ALA A CA  1 
ATOM   1788 C  C   . ALA A 1 267 ? 12.535  30.797 18.466  1.00 27.04  ?  267 ALA A C   1 
ATOM   1789 O  O   . ALA A 1 267 ? 12.554  30.788 19.703  1.00 25.35  ?  267 ALA A O   1 
ATOM   1790 C  CB  . ALA A 1 267 ? 10.962  32.056 16.979  1.00 28.81  ?  267 ALA A CB  1 
ATOM   1791 N  N   . GLN A 1 268 ? 12.740  29.718 17.718  1.00 27.32  ?  268 GLN A N   1 
ATOM   1792 C  CA  . GLN A 1 268 ? 12.882  28.341 18.257  1.00 29.71  ?  268 GLN A CA  1 
ATOM   1793 C  C   . GLN A 1 268 ? 14.196  28.218 19.037  1.00 34.08  ?  268 GLN A C   1 
ATOM   1794 O  O   . GLN A 1 268 ? 14.312  27.286 19.890  1.00 36.81  ?  268 GLN A O   1 
ATOM   1795 C  CB  . GLN A 1 268 ? 12.920  27.336 17.099  1.00 33.29  ?  268 GLN A CB  1 
ATOM   1796 C  CG  . GLN A 1 268 ? 11.602  27.153 16.379  1.00 33.12  ?  268 GLN A CG  1 
ATOM   1797 C  CD  . GLN A 1 268 ? 10.668  26.414 17.291  1.00 33.16  ?  268 GLN A CD  1 
ATOM   1798 O  OE1 . GLN A 1 268 ? 10.613  25.191 17.264  1.00 37.09  ?  268 GLN A OE1 1 
ATOM   1799 N  NE2 . GLN A 1 268 ? 10.015  27.151 18.170  1.00 32.77  ?  268 GLN A NE2 1 
ATOM   1800 N  N   . GLN A 1 269 ? 15.186  29.060 18.706  1.00 32.31  ?  269 GLN A N   1 
ATOM   1801 C  CA  . GLN A 1 269 ? 16.537  28.958 19.303  1.00 32.21  ?  269 GLN A CA  1 
ATOM   1802 C  C   . GLN A 1 269 ? 16.925  30.323 19.821  1.00 28.92  ?  269 GLN A C   1 
ATOM   1803 O  O   . GLN A 1 269 ? 17.802  30.948 19.248  1.00 31.61  ?  269 GLN A O   1 
ATOM   1804 C  CB  . GLN A 1 269 ? 17.532  28.395 18.288  1.00 32.41  ?  269 GLN A CB  1 
ATOM   1805 C  CG  . GLN A 1 269 ? 17.192  26.964 17.844  1.00 32.63  ?  269 GLN A CG  1 
ATOM   1806 C  CD  . GLN A 1 269 ? 18.350  26.329 17.113  1.00 33.14  ?  269 GLN A CD  1 
ATOM   1807 O  OE1 . GLN A 1 269 ? 18.199  25.692 16.075  1.00 30.72  ?  269 GLN A OE1 1 
ATOM   1808 N  NE2 . GLN A 1 269 ? 19.544  26.575 17.621  1.00 34.39  ?  269 GLN A NE2 1 
ATOM   1809 N  N   . PRO A 1 270 ? 16.268  30.803 20.901  1.00 27.84  ?  270 PRO A N   1 
ATOM   1810 C  CA  . PRO A 1 270 ? 16.460  32.180 21.383  1.00 27.55  ?  270 PRO A CA  1 
ATOM   1811 C  C   . PRO A 1 270 ? 17.893  32.487 21.832  1.00 26.88  ?  270 PRO A C   1 
ATOM   1812 O  O   . PRO A 1 270 ? 18.234  33.670 21.882  1.00 25.66  ?  270 PRO A O   1 
ATOM   1813 C  CB  . PRO A 1 270 ? 15.477  32.368 22.547  1.00 26.36  ?  270 PRO A CB  1 
ATOM   1814 C  CG  . PRO A 1 270 ? 15.033  30.923 22.909  1.00 27.45  ?  270 PRO A CG  1 
ATOM   1815 C  CD  . PRO A 1 270 ? 15.257  30.072 21.674  1.00 26.60  ?  270 PRO A CD  1 
ATOM   1816 N  N   . GLU A 1 271 ? 18.719  31.453 22.050  1.00 25.25  ?  271 GLU A N   1 
ATOM   1817 C  CA  . GLU A 1 271 ? 20.159  31.664 22.338  1.00 26.85  ?  271 GLU A CA  1 
ATOM   1818 C  C   . GLU A 1 271 ? 20.832  32.408 21.172  1.00 27.06  ?  271 GLU A C   1 
ATOM   1819 O  O   . GLU A 1 271 ? 21.866  33.082 21.392  1.00 30.12  ?  271 GLU A O   1 
ATOM   1820 C  CB  . GLU A 1 271 ? 20.840  30.335 22.689  1.00 26.95  ?  271 GLU A CB  1 
ATOM   1821 C  CG  . GLU A 1 271 ? 20.891  29.326 21.572  1.00 28.04  ?  271 GLU A CG  1 
ATOM   1822 C  CD  . GLU A 1 271 ? 19.736  28.337 21.535  1.00 30.39  ?  271 GLU A CD  1 
ATOM   1823 O  OE1 . GLU A 1 271 ? 18.585  28.691 21.946  1.00 31.99  ?  271 GLU A OE1 1 
ATOM   1824 O  OE2 . GLU A 1 271 ? 19.984  27.221 21.082  1.00 29.00  ?  271 GLU A OE2 1 
ATOM   1825 N  N   . LEU A 1 272 ? 20.356  32.200 19.951  1.00 27.75  ?  272 LEU A N   1 
ATOM   1826 C  CA  . LEU A 1 272 ? 20.924  32.826 18.728  1.00 28.89  ?  272 LEU A CA  1 
ATOM   1827 C  C   . LEU A 1 272 ? 20.631  34.320 18.788  1.00 29.64  ?  272 LEU A C   1 
ATOM   1828 O  O   . LEU A 1 272 ? 21.539  35.115 18.485  1.00 35.48  ?  272 LEU A O   1 
ATOM   1829 C  CB  . LEU A 1 272 ? 20.290  32.181 17.491  1.00 29.36  ?  272 LEU A CB  1 
ATOM   1830 C  CG  . LEU A 1 272 ? 20.533  30.673 17.355  1.00 28.13  ?  272 LEU A CG  1 
ATOM   1831 C  CD1 . LEU A 1 272 ? 19.982  30.184 16.033  1.00 28.39  ?  272 LEU A CD1 1 
ATOM   1832 C  CD2 . LEU A 1 272 ? 22.028  30.322 17.459  1.00 25.75  ?  272 LEU A CD2 1 
ATOM   1833 N  N   . ALA A 1 273 ? 19.431  34.679 19.240  1.00 28.71  ?  273 ALA A N   1 
ATOM   1834 C  CA  . ALA A 1 273 ? 19.012  36.086 19.406  1.00 29.08  ?  273 ALA A CA  1 
ATOM   1835 C  C   . ALA A 1 273 ? 19.805  36.712 20.550  1.00 29.27  ?  273 ALA A C   1 
ATOM   1836 O  O   . ALA A 1 273 ? 20.134  37.888 20.430  1.00 29.94  ?  273 ALA A O   1 
ATOM   1837 C  CB  . ALA A 1 273 ? 17.524  36.191 19.646  1.00 30.23  ?  273 ALA A CB  1 
ATOM   1838 N  N   . ASP A 1 274 ? 20.067  35.982 21.636  1.00 31.21  ?  274 ASP A N   1 
ATOM   1839 C  CA  . ASP A 1 274 ? 20.919  36.490 22.756  1.00 33.36  ?  274 ASP A CA  1 
ATOM   1840 C  C   . ASP A 1 274 ? 22.334  36.763 22.219  1.00 33.11  ?  274 ASP A C   1 
ATOM   1841 O  O   . ASP A 1 274 ? 22.858  37.859 22.519  1.00 36.71  ?  274 ASP A O   1 
ATOM   1842 C  CB  . ASP A 1 274 ? 20.940  35.546 23.972  1.00 33.80  ?  274 ASP A CB  1 
ATOM   1843 C  CG  . ASP A 1 274 ? 19.823  35.745 24.984  1.00 31.78  ?  274 ASP A CG  1 
ATOM   1844 O  OD1 . ASP A 1 274 ? 19.193  36.818 24.975  1.00 31.43  ?  274 ASP A OD1 1 
ATOM   1845 O  OD2 . ASP A 1 274 ? 19.628  34.836 25.810  1.00 33.79  ?  274 ASP A OD2 1 
ATOM   1846 N  N   . ARG A 1 275 ? 22.894  35.847 21.411  1.00 32.49  ?  275 ARG A N   1 
ATOM   1847 C  CA  . ARG A 1 275 ? 24.212  36.011 20.738  1.00 32.94  ?  275 ARG A CA  1 
ATOM   1848 C  C   . ARG A 1 275 ? 24.225  37.313 19.928  1.00 35.71  ?  275 ARG A C   1 
ATOM   1849 O  O   . ARG A 1 275 ? 25.256  38.030 19.982  1.00 37.15  ?  275 ARG A O   1 
ATOM   1850 C  CB  . ARG A 1 275 ? 24.546  34.847 19.808  1.00 32.47  ?  275 ARG A CB  1 
ATOM   1851 C  CG  . ARG A 1 275 ? 25.839  35.045 19.019  1.00 35.48  ?  275 ARG A CG  1 
ATOM   1852 C  CD  . ARG A 1 275 ? 27.085  34.967 19.892  1.00 35.73  ?  275 ARG A CD  1 
ATOM   1853 N  NE  . ARG A 1 275 ? 28.370  35.049 19.181  1.00 34.00  ?  275 ARG A NE  1 
ATOM   1854 C  CZ  . ARG A 1 275 ? 29.012  34.035 18.581  1.00 35.07  ?  275 ARG A CZ  1 
ATOM   1855 N  NH1 . ARG A 1 275 ? 28.477  32.833 18.518  1.00 35.07  ?  275 ARG A NH1 1 
ATOM   1856 N  NH2 . ARG A 1 275 ? 30.190  34.223 18.010  1.00 36.28  ?  275 ARG A NH2 1 
ATOM   1857 N  N   . LEU A 1 276 ? 23.167  37.598 19.168  1.00 31.63  ?  276 LEU A N   1 
ATOM   1858 C  CA  . LEU A 1 276 ? 23.197  38.734 18.224  1.00 30.78  ?  276 LEU A CA  1 
ATOM   1859 C  C   . LEU A 1 276 ? 23.084  40.034 19.007  1.00 31.47  ?  276 LEU A C   1 
ATOM   1860 O  O   . LEU A 1 276 ? 23.677  41.031 18.572  1.00 33.86  ?  276 LEU A O   1 
ATOM   1861 C  CB  . LEU A 1 276 ? 22.084  38.585 17.188  1.00 30.36  ?  276 LEU A CB  1 
ATOM   1862 C  CG  . LEU A 1 276 ? 22.277  37.415 16.240  1.00 31.20  ?  276 LEU A CG  1 
ATOM   1863 C  CD1 . LEU A 1 276 ? 21.149  37.356 15.233  1.00 31.29  ?  276 LEU A CD1 1 
ATOM   1864 C  CD2 . LEU A 1 276 ? 23.626  37.504 15.551  1.00 30.56  ?  276 LEU A CD2 1 
ATOM   1865 N  N   . ARG A 1 277 ? 22.332  40.045 20.107  1.00 31.74  ?  277 ARG A N   1 
ATOM   1866 C  CA  . ARG A 1 277 ? 22.257  41.275 20.937  1.00 32.51  ?  277 ARG A CA  1 
ATOM   1867 C  C   . ARG A 1 277 ? 23.624  41.529 21.587  1.00 32.44  ?  277 ARG A C   1 
ATOM   1868 O  O   . ARG A 1 277 ? 24.070  42.696 21.596  1.00 32.42  ?  277 ARG A O   1 
ATOM   1869 C  CB  . ARG A 1 277 ? 21.159  41.123 21.993  1.00 31.11  ?  277 ARG A CB  1 
ATOM   1870 N  N   . ALA A 1 278 ? 24.264  40.475 22.092  1.00 31.71  ?  278 ALA A N   1 
ATOM   1871 C  CA  . ALA A 1 278 ? 25.569  40.592 22.790  1.00 33.72  ?  278 ALA A CA  1 
ATOM   1872 C  C   . ALA A 1 278 ? 26.691  40.984 21.822  1.00 36.50  ?  278 ALA A C   1 
ATOM   1873 O  O   . ALA A 1 278 ? 27.680  41.523 22.257  1.00 41.90  ?  278 ALA A O   1 
ATOM   1874 C  CB  . ALA A 1 278 ? 25.928  39.299 23.476  1.00 31.70  ?  278 ALA A CB  1 
ATOM   1875 N  N   . GLU A 1 279 ? 26.579  40.656 20.545  1.00 43.80  ?  279 GLU A N   1 
ATOM   1876 C  CA  . GLU A 1 279 ? 27.717  40.714 19.598  1.00 39.66  ?  279 GLU A CA  1 
ATOM   1877 C  C   . GLU A 1 279 ? 27.127  41.035 18.240  1.00 34.11  ?  279 GLU A C   1 
ATOM   1878 O  O   . GLU A 1 279 ? 27.052  40.198 17.356  1.00 34.55  ?  279 GLU A O   1 
ATOM   1879 C  CB  . GLU A 1 279 ? 28.484  39.402 19.675  1.00 43.37  ?  279 GLU A CB  1 
ATOM   1880 C  CG  . GLU A 1 279 ? 29.875  39.468 19.093  1.00 53.60  ?  279 GLU A CG  1 
ATOM   1881 C  CD  . GLU A 1 279 ? 30.567  38.110 19.041  1.00 65.77  ?  279 GLU A CD  1 
ATOM   1882 O  OE1 . GLU A 1 279 ? 30.174  37.200 19.848  1.00 58.87  ?  279 GLU A OE1 1 
ATOM   1883 O  OE2 . GLU A 1 279 ? 31.503  37.957 18.201  1.00 72.17  ?  279 GLU A OE2 1 
ATOM   1884 N  N   . PRO A 1 280 ? 26.654  42.277 18.042  1.00 36.13  ?  280 PRO A N   1 
ATOM   1885 C  CA  . PRO A 1 280 ? 25.925  42.608 16.815  1.00 36.22  ?  280 PRO A CA  1 
ATOM   1886 C  C   . PRO A 1 280 ? 26.778  42.422 15.558  1.00 34.14  ?  280 PRO A C   1 
ATOM   1887 O  O   . PRO A 1 280 ? 26.174  42.272 14.541  1.00 37.33  ?  280 PRO A O   1 
ATOM   1888 C  CB  . PRO A 1 280 ? 25.484  44.068 16.985  1.00 32.79  ?  280 PRO A CB  1 
ATOM   1889 C  CG  . PRO A 1 280 ? 25.596  44.300 18.492  1.00 35.08  ?  280 PRO A CG  1 
ATOM   1890 C  CD  . PRO A 1 280 ? 26.747  43.420 18.973  1.00 33.25  ?  280 PRO A CD  1 
ATOM   1891 N  N   . ALA A 1 281 ? 28.112  42.377 15.674  1.00 35.07  ?  281 ALA A N   1 
ATOM   1892 C  CA  . ALA A 1 281 ? 29.049  42.311 14.526  1.00 34.34  ?  281 ALA A CA  1 
ATOM   1893 C  C   . ALA A 1 281 ? 29.083  40.897 13.953  1.00 35.23  ?  281 ALA A C   1 
ATOM   1894 O  O   . ALA A 1 281 ? 29.695  40.717 12.904  1.00 36.95  ?  281 ALA A O   1 
ATOM   1895 C  CB  . ALA A 1 281 ? 30.439  42.750 14.913  1.00 30.68  ?  281 ALA A CB  1 
ATOM   1896 N  N   . VAL A 1 282 ? 28.478  39.913 14.616  1.00 39.52  ?  282 VAL A N   1 
ATOM   1897 C  CA  . VAL A 1 282 ? 28.552  38.496 14.141  1.00 38.05  ?  282 VAL A CA  1 
ATOM   1898 C  C   . VAL A 1 282 ? 27.377  38.194 13.196  1.00 32.05  ?  282 VAL A C   1 
ATOM   1899 O  O   . VAL A 1 282 ? 27.307  37.060 12.642  1.00 31.03  ?  282 VAL A O   1 
ATOM   1900 C  CB  . VAL A 1 282 ? 28.632  37.525 15.328  1.00 39.36  ?  282 VAL A CB  1 
ATOM   1901 C  CG1 . VAL A 1 282 ? 28.586  36.069 14.894  1.00 42.98  ?  282 VAL A CG1 1 
ATOM   1902 C  CG2 . VAL A 1 282 ? 29.871  37.796 16.142  1.00 39.14  ?  282 VAL A CG2 1 
ATOM   1903 N  N   . ILE A 1 283 ? 26.537  39.195 12.953  1.00 28.94  ?  283 ILE A N   1 
ATOM   1904 C  CA  . ILE A 1 283 ? 25.296  39.098 12.125  1.00 33.76  ?  283 ILE A CA  1 
ATOM   1905 C  C   . ILE A 1 283 ? 25.616  38.593 10.704  1.00 33.75  ?  283 ILE A C   1 
ATOM   1906 O  O   . ILE A 1 283 ? 24.759  37.926 10.109  1.00 35.44  ?  283 ILE A O   1 
ATOM   1907 C  CB  . ILE A 1 283 ? 24.581  40.465 12.116  1.00 34.59  ?  283 ILE A CB  1 
ATOM   1908 C  CG1 . ILE A 1 283 ? 23.190  40.363 11.491  1.00 35.20  ?  283 ILE A CG1 1 
ATOM   1909 C  CG2 . ILE A 1 283 ? 25.442  41.528 11.434  1.00 32.60  ?  283 ILE A CG2 1 
ATOM   1910 C  CD1 . ILE A 1 283 ? 22.250  39.469 12.230  1.00 37.51  ?  283 ILE A CD1 1 
ATOM   1911 N  N   . GLY A 1 284 ? 26.786  38.935 10.164  1.00 33.22  ?  284 GLY A N   1 
ATOM   1912 C  CA  . GLY A 1 284 ? 27.252  38.493 8.838   1.00 31.51  ?  284 GLY A CA  1 
ATOM   1913 C  C   . GLY A 1 284 ? 27.544  37.010 8.811   1.00 30.41  ?  284 GLY A C   1 
ATOM   1914 O  O   . GLY A 1 284 ? 27.089  36.336 7.878   1.00 29.63  ?  284 GLY A O   1 
ATOM   1915 N  N   . ARG A 1 285 ? 28.328  36.529 9.770   1.00 33.33  ?  285 ARG A N   1 
ATOM   1916 C  CA  . ARG A 1 285 ? 28.578  35.088 9.935   1.00 34.75  ?  285 ARG A CA  1 
ATOM   1917 C  C   . ARG A 1 285 ? 27.243  34.422 10.255  1.00 35.99  ?  285 ARG A C   1 
ATOM   1918 O  O   . ARG A 1 285 ? 26.964  33.346 9.694   1.00 36.25  ?  285 ARG A O   1 
ATOM   1919 C  CB  . ARG A 1 285 ? 29.583  34.816 11.048  1.00 40.94  ?  285 ARG A CB  1 
ATOM   1920 C  CG  . ARG A 1 285 ? 30.975  35.320 10.711  1.00 51.68  ?  285 ARG A CG  1 
ATOM   1921 C  CD  . ARG A 1 285 ? 32.076  35.056 11.742  1.00 52.93  ?  285 ARG A CD  1 
ATOM   1922 N  NE  . ARG A 1 285 ? 33.421  35.590 11.479  1.00 54.83  ?  285 ARG A NE  1 
ATOM   1923 C  CZ  . ARG A 1 285 ? 34.476  35.564 12.296  1.00 50.34  ?  285 ARG A CZ  1 
ATOM   1924 N  NH1 . ARG A 1 285 ? 34.440  34.943 13.463  1.00 50.36  ?  285 ARG A NH1 1 
ATOM   1925 N  NH2 . ARG A 1 285 ? 35.598  36.143 11.911  1.00 50.75  ?  285 ARG A NH2 1 
ATOM   1926 N  N   . ALA A 1 286 ? 26.435  35.028 11.121  1.00 32.53  ?  286 ALA A N   1 
ATOM   1927 C  CA  . ALA A 1 286 ? 25.175  34.389 11.579  1.00 33.59  ?  286 ALA A CA  1 
ATOM   1928 C  C   . ALA A 1 286 ? 24.230  34.197 10.383  1.00 32.12  ?  286 ALA A C   1 
ATOM   1929 O  O   . ALA A 1 286 ? 23.693  33.060 10.232  1.00 28.40  ?  286 ALA A O   1 
ATOM   1930 C  CB  . ALA A 1 286 ? 24.526  35.169 12.709  1.00 32.28  ?  286 ALA A CB  1 
ATOM   1931 N  N   . VAL A 1 287 ? 24.049  35.250 9.563   1.00 32.13  ?  287 VAL A N   1 
ATOM   1932 C  CA  . VAL A 1 287 ? 23.070  35.257 8.440   1.00 31.66  ?  287 VAL A CA  1 
ATOM   1933 C  C   . VAL A 1 287 ? 23.572  34.238 7.424   1.00 31.76  ?  287 VAL A C   1 
ATOM   1934 O  O   . VAL A 1 287 ? 22.717  33.597 6.790   1.00 34.41  ?  287 VAL A O   1 
ATOM   1935 C  CB  . VAL A 1 287 ? 22.850  36.663 7.845   1.00 33.17  ?  287 VAL A CB  1 
ATOM   1936 C  CG1 . VAL A 1 287 ? 21.944  36.668 6.618   1.00 33.47  ?  287 VAL A CG1 1 
ATOM   1937 C  CG2 . VAL A 1 287 ? 22.304  37.618 8.897   1.00 32.97  ?  287 VAL A CG2 1 
ATOM   1938 N  N   . ASP A 1 288 ? 24.897  34.054 7.355   1.00 30.99  ?  288 ASP A N   1 
ATOM   1939 C  CA  . ASP A 1 288 ? 25.587  33.127 6.418   1.00 30.16  ?  288 ASP A CA  1 
ATOM   1940 C  C   . ASP A 1 288 ? 25.273  31.680 6.808   1.00 29.62  ?  288 ASP A C   1 
ATOM   1941 O  O   . ASP A 1 288 ? 25.051  30.838 5.914   1.00 32.81  ?  288 ASP A O   1 
ATOM   1942 C  CB  . ASP A 1 288 ? 27.081  33.444 6.382   1.00 34.51  ?  288 ASP A CB  1 
ATOM   1943 C  CG  . ASP A 1 288 ? 27.838  32.700 5.296   1.00 36.86  ?  288 ASP A CG  1 
ATOM   1944 O  OD1 . ASP A 1 288 ? 27.338  32.647 4.186   1.00 36.73  ?  288 ASP A OD1 1 
ATOM   1945 O  OD2 . ASP A 1 288 ? 28.904  32.165 5.589   1.00 39.39  ?  288 ASP A OD2 1 
ATOM   1946 N  N   . GLU A 1 289 ? 25.246  31.376 8.098   1.00 30.11  ?  289 GLU A N   1 
ATOM   1947 C  CA  . GLU A 1 289 ? 24.865  30.032 8.590   1.00 30.49  ?  289 GLU A CA  1 
ATOM   1948 C  C   . GLU A 1 289 ? 23.354  29.854 8.466   1.00 30.03  ?  289 GLU A C   1 
ATOM   1949 O  O   . GLU A 1 289 ? 22.941  28.720 8.196   1.00 29.20  ?  289 GLU A O   1 
ATOM   1950 C  CB  . GLU A 1 289 ? 25.259  29.813 10.047  1.00 32.01  ?  289 GLU A CB  1 
ATOM   1951 C  CG  . GLU A 1 289 ? 24.685  28.543 10.660  1.00 32.34  ?  289 GLU A CG  1 
ATOM   1952 C  CD  . GLU A 1 289 ? 25.333  27.269 10.157  1.00 32.65  ?  289 GLU A CD  1 
ATOM   1953 O  OE1 . GLU A 1 289 ? 25.998  27.325 9.106   1.00 31.16  ?  289 GLU A OE1 1 
ATOM   1954 O  OE2 . GLU A 1 289 ? 25.192  26.221 10.841  1.00 33.51  ?  289 GLU A OE2 1 
ATOM   1955 N  N   . LEU A 1 290 ? 22.557  30.891 8.725   1.00 29.46  ?  290 LEU A N   1 
ATOM   1956 C  CA  . LEU A 1 290 ? 21.082  30.754 8.569   1.00 31.61  ?  290 LEU A CA  1 
ATOM   1957 C  C   . LEU A 1 290 ? 20.763  30.459 7.103   1.00 32.59  ?  290 LEU A C   1 
ATOM   1958 O  O   . LEU A 1 290 ? 19.775  29.697 6.863   1.00 33.15  ?  290 LEU A O   1 
ATOM   1959 C  CB  . LEU A 1 290 ? 20.364  32.005 9.062   1.00 31.44  ?  290 LEU A CB  1 
ATOM   1960 C  CG  . LEU A 1 290 ? 20.461  32.185 10.568  1.00 33.21  ?  290 LEU A CG  1 
ATOM   1961 C  CD1 . LEU A 1 290 ? 19.774  33.459 11.019  1.00 32.12  ?  290 LEU A CD1 1 
ATOM   1962 C  CD2 . LEU A 1 290 ? 19.904  30.962 11.270  1.00 34.50  ?  290 LEU A CD2 1 
ATOM   1963 N  N   . LEU A 1 291 ? 21.581  30.998 6.183   1.00 31.20  ?  291 LEU A N   1 
ATOM   1964 C  CA  . LEU A 1 291 ? 21.488  30.708 4.725   1.00 31.90  ?  291 LEU A CA  1 
ATOM   1965 C  C   . LEU A 1 291 ? 21.721  29.204 4.474   1.00 30.26  ?  291 LEU A C   1 
ATOM   1966 O  O   . LEU A 1 291 ? 20.845  28.566 3.897   1.00 33.52  ?  291 LEU A O   1 
ATOM   1967 C  CB  . LEU A 1 291 ? 22.469  31.593 3.944   1.00 30.40  ?  291 LEU A CB  1 
ATOM   1968 C  CG  . LEU A 1 291 ? 22.017  33.043 3.754   1.00 33.29  ?  291 LEU A CG  1 
ATOM   1969 C  CD1 . LEU A 1 291 ? 23.187  33.935 3.347   1.00 33.31  ?  291 LEU A CD1 1 
ATOM   1970 C  CD2 . LEU A 1 291 ? 20.863  33.165 2.755   1.00 31.51  ?  291 LEU A CD2 1 
ATOM   1971 N  N   . ARG A 1 292 ? 22.840  28.638 4.916   1.00 32.37  ?  292 ARG A N   1 
ATOM   1972 C  CA  . ARG A 1 292 ? 23.142  27.179 4.792   1.00 30.65  ?  292 ARG A CA  1 
ATOM   1973 C  C   . ARG A 1 292 ? 21.953  26.344 5.281   1.00 30.45  ?  292 ARG A C   1 
ATOM   1974 O  O   . ARG A 1 292 ? 21.636  25.305 4.637   1.00 32.84  ?  292 ARG A O   1 
ATOM   1975 C  CB  . ARG A 1 292 ? 24.376  26.805 5.613   1.00 28.24  ?  292 ARG A CB  1 
ATOM   1976 C  CG  . ARG A 1 292 ? 24.730  25.326 5.544   1.00 28.63  ?  292 ARG A CG  1 
ATOM   1977 C  CD  . ARG A 1 292 ? 25.808  24.947 6.557   1.00 29.20  ?  292 ARG A CD  1 
ATOM   1978 N  NE  . ARG A 1 292 ? 25.322  24.894 7.943   1.00 29.01  ?  292 ARG A NE  1 
ATOM   1979 C  CZ  . ARG A 1 292 ? 24.638  23.866 8.471   1.00 29.32  ?  292 ARG A CZ  1 
ATOM   1980 N  NH1 . ARG A 1 292 ? 24.347  22.780 7.752   1.00 26.25  ?  292 ARG A NH1 1 
ATOM   1981 N  NH2 . ARG A 1 292 ? 24.264  23.919 9.736   1.00 28.68  ?  292 ARG A NH2 1 
ATOM   1982 N  N   . TYR A 1 293 ? 21.303  26.785 6.358   1.00 28.68  ?  293 TYR A N   1 
ATOM   1983 C  CA  . TYR A 1 293 ? 20.337  25.973 7.139   1.00 31.42  ?  293 TYR A CA  1 
ATOM   1984 C  C   . TYR A 1 293 ? 18.921  26.084 6.569   1.00 28.61  ?  293 TYR A C   1 
ATOM   1985 O  O   . TYR A 1 293 ? 18.116  25.175 6.769   1.00 29.46  ?  293 TYR A O   1 
ATOM   1986 C  CB  . TYR A 1 293 ? 20.311  26.456 8.587   1.00 33.64  ?  293 TYR A CB  1 
ATOM   1987 C  CG  . TYR A 1 293 ? 19.785  25.462 9.584   1.00 32.86  ?  293 TYR A CG  1 
ATOM   1988 C  CD1 . TYR A 1 293 ? 20.533  24.343 9.893   1.00 34.54  ?  293 TYR A CD1 1 
ATOM   1989 C  CD2 . TYR A 1 293 ? 18.580  25.649 10.249  1.00 31.52  ?  293 TYR A CD2 1 
ATOM   1990 C  CE1 . TYR A 1 293 ? 20.098  23.428 10.839  1.00 33.77  ?  293 TYR A CE1 1 
ATOM   1991 C  CE2 . TYR A 1 293 ? 18.126  24.736 11.194  1.00 30.24  ?  293 TYR A CE2 1 
ATOM   1992 C  CZ  . TYR A 1 293 ? 18.894  23.621 11.496  1.00 31.45  ?  293 TYR A CZ  1 
ATOM   1993 O  OH  . TYR A 1 293 ? 18.547  22.711 12.461  1.00 29.01  ?  293 TYR A OH  1 
ATOM   1994 N  N   . ASN A 1 294 ? 18.623  27.169 5.882   1.00 26.49  ?  294 ASN A N   1 
ATOM   1995 C  CA  . ASN A 1 294 ? 17.222  27.534 5.586   1.00 29.88  ?  294 ASN A CA  1 
ATOM   1996 C  C   . ASN A 1 294 ? 16.662  26.644 4.482   1.00 29.87  ?  294 ASN A C   1 
ATOM   1997 O  O   . ASN A 1 294 ? 17.413  26.300 3.584   1.00 29.19  ?  294 ASN A O   1 
ATOM   1998 C  CB  . ASN A 1 294 ? 17.088  29.000 5.191   1.00 30.12  ?  294 ASN A CB  1 
ATOM   1999 C  CG  . ASN A 1 294 ? 15.651  29.418 5.028   1.00 28.09  ?  294 ASN A CG  1 
ATOM   2000 O  OD1 . ASN A 1 294 ? 14.789  28.568 4.847   1.00 27.25  ?  294 ASN A OD1 1 
ATOM   2001 N  ND2 . ASN A 1 294 ? 15.397  30.713 5.120   1.00 28.95  ?  294 ASN A ND2 1 
ATOM   2002 N  N   . LEU A 1 295 ? 15.357  26.370 4.535   1.00 32.33  ?  295 LEU A N   1 
ATOM   2003 C  CA  . LEU A 1 295 ? 14.653  25.432 3.621   1.00 31.94  ?  295 LEU A CA  1 
ATOM   2004 C  C   . LEU A 1 295 ? 13.598  26.178 2.808   1.00 28.95  ?  295 LEU A C   1 
ATOM   2005 O  O   . LEU A 1 295 ? 12.629  25.521 2.363   1.00 25.46  ?  295 LEU A O   1 
ATOM   2006 C  CB  . LEU A 1 295 ? 14.068  24.290 4.451   1.00 32.97  ?  295 LEU A CB  1 
ATOM   2007 C  CG  . LEU A 1 295 ? 15.114  23.561 5.297   1.00 33.21  ?  295 LEU A CG  1 
ATOM   2008 C  CD1 . LEU A 1 295 ? 14.449  22.533 6.205   1.00 33.87  ?  295 LEU A CD1 1 
ATOM   2009 C  CD2 . LEU A 1 295 ? 16.188  22.913 4.418   1.00 32.02  ?  295 LEU A CD2 1 
ATOM   2010 N  N   . SER A 1 296 ? 13.873  27.463 2.562   1.00 27.40  ?  296 SER A N   1 
ATOM   2011 C  CA  . SER A 1 296 ? 13.068  28.375 1.712   1.00 29.53  ?  296 SER A CA  1 
ATOM   2012 C  C   . SER A 1 296 ? 12.956  27.802 0.298   1.00 29.25  ?  296 SER A C   1 
ATOM   2013 O  O   . SER A 1 296 ? 11.861  27.784 -0.233  1.00 35.80  ?  296 SER A O   1 
ATOM   2014 C  CB  . SER A 1 296 ? 13.616  29.787 1.689   1.00 28.34  ?  296 SER A CB  1 
ATOM   2015 O  OG  . SER A 1 296 ? 14.829  29.851 0.942   1.00 28.37  ?  296 SER A OG  1 
ATOM   2016 N  N   . ILE A 1 297 ? 14.041  27.336 -0.298  1.00 31.29  ?  297 ILE A N   1 
ATOM   2017 C  CA  . ILE A 1 297 ? 13.989  26.724 -1.661  1.00 32.16  ?  297 ILE A CA  1 
ATOM   2018 C  C   . ILE A 1 297 ? 13.159  25.430 -1.613  1.00 31.97  ?  297 ILE A C   1 
ATOM   2019 O  O   . ILE A 1 297 ? 13.653  24.454 -1.049  1.00 34.68  ?  297 ILE A O   1 
ATOM   2020 C  CB  . ILE A 1 297 ? 15.403  26.494 -2.198  1.00 32.64  ?  297 ILE A CB  1 
ATOM   2021 C  CG1 . ILE A 1 297 ? 16.109  27.843 -2.396  1.00 39.62  ?  297 ILE A CG1 1 
ATOM   2022 C  CG2 . ILE A 1 297 ? 15.327  25.674 -3.471  1.00 32.24  ?  297 ILE A CG2 1 
ATOM   2023 C  CD1 . ILE A 1 297 ? 17.612  27.772 -2.659  1.00 39.55  ?  297 ILE A CD1 1 
ATOM   2024 N  N   . GLY A 1 298 ? 11.958  25.447 -2.212  1.00 30.87  ?  298 GLY A N   1 
ATOM   2025 C  CA  . GLY A 1 298 ? 10.933  24.386 -2.171  1.00 31.38  ?  298 GLY A CA  1 
ATOM   2026 C  C   . GLY A 1 298 ? 10.950  23.476 -3.390  1.00 31.09  ?  298 GLY A C   1 
ATOM   2027 O  O   . GLY A 1 298 ? 10.193  22.443 -3.390  1.00 27.22  ?  298 GLY A O   1 
ATOM   2028 N  N   . ASP A 1 299 ? 11.775  23.814 -4.391  1.00 30.19  ?  299 ASP A N   1 
ATOM   2029 C  CA  . ASP A 1 299 ? 12.065  22.947 -5.566  1.00 29.20  ?  299 ASP A CA  1 
ATOM   2030 C  C   . ASP A 1 299 ? 13.553  22.593 -5.568  1.00 30.45  ?  299 ASP A C   1 
ATOM   2031 O  O   . ASP A 1 299 ? 14.163  22.702 -4.487  1.00 31.55  ?  299 ASP A O   1 
ATOM   2032 C  CB  . ASP A 1 299 ? 11.607  23.614 -6.853  1.00 29.89  ?  299 ASP A CB  1 
ATOM   2033 C  CG  . ASP A 1 299 ? 12.223  24.975 -7.099  1.00 31.96  ?  299 ASP A CG  1 
ATOM   2034 O  OD1 . ASP A 1 299 ? 12.754  25.547 -6.129  1.00 30.76  ?  299 ASP A OD1 1 
ATOM   2035 O  OD2 . ASP A 1 299 ? 12.162  25.452 -8.278  1.00 34.34  ?  299 ASP A OD2 1 
ATOM   2036 N  N   . ALA A 1 300 ? 14.088  22.112 -6.700  1.00 31.79  ?  300 ALA A N   1 
ATOM   2037 C  CA  . ALA A 1 300 ? 15.542  21.913 -6.943  1.00 30.74  ?  300 ALA A CA  1 
ATOM   2038 C  C   . ALA A 1 300 ? 15.987  22.934 -7.990  1.00 30.18  ?  300 ALA A C   1 
ATOM   2039 O  O   . ALA A 1 300 ? 15.095  23.492 -8.608  1.00 32.68  ?  300 ALA A O   1 
ATOM   2040 C  CB  . ALA A 1 300 ? 15.811  20.502 -7.381  1.00 28.22  ?  300 ALA A CB  1 
ATOM   2041 N  N   . LEU A 1 301 ? 17.288  23.237 -8.132  1.00 33.03  ?  301 LEU A N   1 
ATOM   2042 C  CA  . LEU A 1 301 ? 17.791  24.139 -9.221  1.00 31.12  ?  301 LEU A CA  1 
ATOM   2043 C  C   . LEU A 1 301 ? 17.893  23.282 -10.470 1.00 29.36  ?  301 LEU A C   1 
ATOM   2044 O  O   . LEU A 1 301 ? 18.490  22.206 -10.420 1.00 27.39  ?  301 LEU A O   1 
ATOM   2045 C  CB  . LEU A 1 301 ? 19.140  24.758 -8.861  1.00 32.98  ?  301 LEU A CB  1 
ATOM   2046 C  CG  . LEU A 1 301 ? 19.162  25.539 -7.547  1.00 36.02  ?  301 LEU A CG  1 
ATOM   2047 C  CD1 . LEU A 1 301 ? 20.500  26.246 -7.357  1.00 33.45  ?  301 LEU A CD1 1 
ATOM   2048 C  CD2 . LEU A 1 301 ? 17.989  26.519 -7.471  1.00 34.82  ?  301 LEU A CD2 1 
ATOM   2049 N  N   . PRO A 1 302 ? 17.171  23.642 -11.555 1.00 31.72  ?  302 PRO A N   1 
ATOM   2050 C  CA  . PRO A 1 302 ? 17.020  22.748 -12.698 1.00 30.95  ?  302 PRO A CA  1 
ATOM   2051 C  C   . PRO A 1 302 ? 18.066  22.971 -13.800 1.00 31.94  ?  302 PRO A C   1 
ATOM   2052 O  O   . PRO A 1 302 ? 18.361  24.112 -14.147 1.00 29.95  ?  302 PRO A O   1 
ATOM   2053 C  CB  . PRO A 1 302 ? 15.625  23.126 -13.199 1.00 29.34  ?  302 PRO A CB  1 
ATOM   2054 C  CG  . PRO A 1 302 ? 15.585  24.628 -12.996 1.00 29.87  ?  302 PRO A CG  1 
ATOM   2055 C  CD  . PRO A 1 302 ? 16.365  24.871 -11.716 1.00 31.78  ?  302 PRO A CD  1 
ATOM   2056 N  N   . ARG A 1 303 ? 18.534  21.857 -14.360 1.00 33.33  ?  303 ARG A N   1 
ATOM   2057 C  CA  . ARG A 1 303 ? 19.447  21.823 -15.517 1.00 34.72  ?  303 ARG A CA  1 
ATOM   2058 C  C   . ARG A 1 303 ? 18.976  20.776 -16.538 1.00 34.42  ?  303 ARG A C   1 
ATOM   2059 O  O   . ARG A 1 303 ? 18.505  19.672 -16.120 1.00 34.78  ?  303 ARG A O   1 
ATOM   2060 C  CB  . ARG A 1 303 ? 20.857  21.511 -15.002 1.00 37.16  ?  303 ARG A CB  1 
ATOM   2061 C  CG  . ARG A 1 303 ? 21.432  22.546 -14.043 1.00 35.67  ?  303 ARG A CG  1 
ATOM   2062 C  CD  . ARG A 1 303 ? 21.503  23.930 -14.630 1.00 32.99  ?  303 ARG A CD  1 
ATOM   2063 N  NE  . ARG A 1 303 ? 22.167  24.892 -13.768 1.00 35.29  ?  303 ARG A NE  1 
ATOM   2064 C  CZ  . ARG A 1 303 ? 21.603  25.724 -12.893 1.00 40.27  ?  303 ARG A CZ  1 
ATOM   2065 N  NH1 . ARG A 1 303 ? 20.297  25.728 -12.681 1.00 42.91  ?  303 ARG A NH1 1 
ATOM   2066 N  NH2 . ARG A 1 303 ? 22.374  26.569 -12.220 1.00 43.51  ?  303 ARG A NH2 1 
ATOM   2067 N  N   . ILE A 1 304 ? 19.125  21.092 -17.830 1.00 36.18  ?  304 ILE A N   1 
ATOM   2068 C  CA  . ILE A 1 304 ? 19.091  20.080 -18.936 1.00 41.53  ?  304 ILE A CA  1 
ATOM   2069 C  C   . ILE A 1 304 ? 20.546  19.679 -19.240 1.00 38.20  ?  304 ILE A C   1 
ATOM   2070 O  O   . ILE A 1 304 ? 21.411  20.588 -19.456 1.00 36.25  ?  304 ILE A O   1 
ATOM   2071 C  CB  . ILE A 1 304 ? 18.318  20.589 -20.191 1.00 46.40  ?  304 ILE A CB  1 
ATOM   2072 C  CG1 . ILE A 1 304 ? 16.923  21.153 -19.856 1.00 46.33  ?  304 ILE A CG1 1 
ATOM   2073 C  CG2 . ILE A 1 304 ? 18.221  19.490 -21.248 1.00 43.68  ?  304 ILE A CG2 1 
ATOM   2074 C  CD1 . ILE A 1 304 ? 15.954  20.115 -19.325 1.00 43.71  ?  304 ILE A CD1 1 
ATOM   2075 N  N   . ALA A 1 305 ? 20.823  18.373 -19.202 1.00 38.12  ?  305 ALA A N   1 
ATOM   2076 C  CA  . ALA A 1 305 ? 22.097  17.787 -19.677 1.00 39.56  ?  305 ALA A CA  1 
ATOM   2077 C  C   . ALA A 1 305 ? 22.186  18.080 -21.182 1.00 45.08  ?  305 ALA A C   1 
ATOM   2078 O  O   . ALA A 1 305 ? 21.276  17.640 -21.929 1.00 42.03  ?  305 ALA A O   1 
ATOM   2079 C  CB  . ALA A 1 305 ? 22.163  16.311 -19.358 1.00 36.64  ?  305 ALA A CB  1 
ATOM   2080 N  N   . LEU A 1 306 ? 23.179  18.890 -21.568 1.00 46.33  ?  306 LEU A N   1 
ATOM   2081 C  CA  . LEU A 1 306 ? 23.553  19.185 -22.972 1.00 45.24  ?  306 LEU A CA  1 
ATOM   2082 C  C   . LEU A 1 306 ? 24.402  18.050 -23.553 1.00 44.77  ?  306 LEU A C   1 
ATOM   2083 O  O   . LEU A 1 306 ? 24.957  18.257 -24.619 1.00 48.14  ?  306 LEU A O   1 
ATOM   2084 C  CB  . LEU A 1 306 ? 24.351  20.486 -23.006 1.00 43.46  ?  306 LEU A CB  1 
ATOM   2085 C  CG  . LEU A 1 306 ? 23.542  21.743 -22.738 1.00 51.17  ?  306 LEU A CG  1 
ATOM   2086 C  CD1 . LEU A 1 306 ? 24.423  22.993 -22.752 1.00 49.47  ?  306 LEU A CD1 1 
ATOM   2087 C  CD2 . LEU A 1 306 ? 22.420  21.866 -23.756 1.00 53.89  ?  306 LEU A CD2 1 
ATOM   2088 N  N   . ALA A 1 307 ? 24.498  16.890 -22.906 1.00 47.92  ?  307 ALA A N   1 
ATOM   2089 C  CA  . ALA A 1 307 ? 25.420  15.805 -23.317 1.00 49.36  ?  307 ALA A CA  1 
ATOM   2090 C  C   . ALA A 1 307 ? 25.313  14.636 -22.350 1.00 48.37  ?  307 ALA A C   1 
ATOM   2091 O  O   . ALA A 1 307 ? 24.892  14.842 -21.218 1.00 55.67  ?  307 ALA A O   1 
ATOM   2092 C  CB  . ALA A 1 307 ? 26.844  16.309 -23.356 1.00 50.38  ?  307 ALA A CB  1 
ATOM   2093 N  N   . ASP A 1 308 ? 25.741  13.458 -22.779 1.00 55.45  ?  308 ASP A N   1 
ATOM   2094 C  CA  . ASP A 1 308 ? 25.994  12.330 -21.851 1.00 65.10  ?  308 ASP A CA  1 
ATOM   2095 C  C   . ASP A 1 308 ? 27.058  12.799 -20.844 1.00 63.55  ?  308 ASP A C   1 
ATOM   2096 O  O   . ASP A 1 308 ? 28.138  13.281 -21.275 1.00 63.18  ?  308 ASP A O   1 
ATOM   2097 C  CB  . ASP A 1 308 ? 26.344  11.049 -22.614 1.00 73.12  ?  308 ASP A CB  1 
ATOM   2098 C  CG  . ASP A 1 308 ? 25.422  10.777 -23.791 1.00 72.01  ?  308 ASP A CG  1 
ATOM   2099 O  OD1 . ASP A 1 308 ? 24.235  10.488 -23.545 1.00 69.86  ?  308 ASP A OD1 1 
ATOM   2100 O  OD2 . ASP A 1 308 ? 25.898  10.878 -24.945 1.00 76.54  ?  308 ASP A OD2 1 
ATOM   2101 N  N   . VAL A 1 309 ? 26.710  12.752 -19.554 1.00 61.93  ?  309 VAL A N   1 
ATOM   2102 C  CA  . VAL A 1 309 ? 27.604  13.063 -18.404 1.00 58.56  ?  309 VAL A CA  1 
ATOM   2103 C  C   . VAL A 1 309 ? 27.410  11.984 -17.348 1.00 55.33  ?  309 VAL A C   1 
ATOM   2104 O  O   . VAL A 1 309 ? 26.257  11.693 -17.043 1.00 62.28  ?  309 VAL A O   1 
ATOM   2105 C  CB  . VAL A 1 309 ? 27.297  14.442 -17.806 1.00 61.06  ?  309 VAL A CB  1 
ATOM   2106 C  CG1 . VAL A 1 309 ? 28.109  14.679 -16.539 1.00 61.60  ?  309 VAL A CG1 1 
ATOM   2107 C  CG2 . VAL A 1 309 ? 27.512  15.544 -18.831 1.00 60.64  ?  309 VAL A CG2 1 
ATOM   2108 N  N   . ARG A 1 310 ? 28.500  11.404 -16.847 1.00 58.25  ?  310 ARG A N   1 
ATOM   2109 C  CA  . ARG A 1 310 ? 28.504  10.518 -15.655 1.00 54.34  ?  310 ARG A CA  1 
ATOM   2110 C  C   . ARG A 1 310 ? 28.561  11.424 -14.426 1.00 49.86  ?  310 ARG A C   1 
ATOM   2111 O  O   . ARG A 1 310 ? 29.261  12.443 -14.476 1.00 43.99  ?  310 ARG A O   1 
ATOM   2112 C  CB  . ARG A 1 310 ? 29.667  9.525  -15.682 1.00 54.06  ?  310 ARG A CB  1 
ATOM   2113 C  CG  . ARG A 1 310 ? 29.395  8.264  -14.878 1.00 57.79  ?  310 ARG A CG  1 
ATOM   2114 C  CD  . ARG A 1 310 ? 30.342  7.138  -15.240 1.00 66.55  ?  310 ARG A CD  1 
ATOM   2115 N  NE  . ARG A 1 310 ? 30.705  6.325  -14.082 1.00 72.71  ?  310 ARG A NE  1 
ATOM   2116 C  CZ  . ARG A 1 310 ? 30.005  5.295  -13.597 1.00 73.59  ?  310 ARG A CZ  1 
ATOM   2117 N  NH1 . ARG A 1 310 ? 28.864  4.925  -14.159 1.00 72.06  ?  310 ARG A NH1 1 
ATOM   2118 N  NH2 . ARG A 1 310 ? 30.456  4.640  -12.539 1.00 74.59  ?  310 ARG A NH2 1 
ATOM   2119 N  N   . LEU A 1 311 ? 27.748  11.110 -13.416 1.00 52.68  ?  311 LEU A N   1 
ATOM   2120 C  CA  . LEU A 1 311 ? 27.643  11.868 -12.138 1.00 50.75  ?  311 LEU A CA  1 
ATOM   2121 C  C   . LEU A 1 311 ? 27.509  10.834 -11.036 1.00 43.80  ?  311 LEU A C   1 
ATOM   2122 O  O   . LEU A 1 311 ? 26.527  10.069 -11.083 1.00 44.67  ?  311 LEU A O   1 
ATOM   2123 C  CB  . LEU A 1 311 ? 26.434  12.813 -12.142 1.00 48.84  ?  311 LEU A CB  1 
ATOM   2124 C  CG  . LEU A 1 311 ? 26.554  14.013 -11.206 1.00 52.20  ?  311 LEU A CG  1 
ATOM   2125 C  CD1 . LEU A 1 311 ? 27.722  14.900 -11.613 1.00 56.76  ?  311 LEU A CD1 1 
ATOM   2126 C  CD2 . LEU A 1 311 ? 25.274  14.837 -11.180 1.00 53.64  ?  311 LEU A CD2 1 
ATOM   2127 N  N   . GLY A 1 312 ? 28.472  10.811 -10.114 1.00 42.63  ?  312 GLY A N   1 
ATOM   2128 C  CA  . GLY A 1 312 ? 28.674  9.659  -9.228  1.00 43.54  ?  312 GLY A CA  1 
ATOM   2129 C  C   . GLY A 1 312 ? 28.593  8.397  -10.068 1.00 48.59  ?  312 GLY A C   1 
ATOM   2130 O  O   . GLY A 1 312 ? 29.398  8.281  -11.004 1.00 54.51  ?  312 GLY A O   1 
ATOM   2131 N  N   . GLU A 1 313 ? 27.595  7.551  -9.814  1.00 50.08  ?  313 GLU A N   1 
ATOM   2132 C  CA  . GLU A 1 313 ? 27.462  6.179  -10.371 1.00 54.55  ?  313 GLU A CA  1 
ATOM   2133 C  C   . GLU A 1 313 ? 26.353  6.150  -11.441 1.00 50.82  ?  313 GLU A C   1 
ATOM   2134 O  O   . GLU A 1 313 ? 25.940  5.055  -11.832 1.00 42.97  ?  313 GLU A O   1 
ATOM   2135 C  CB  . GLU A 1 313 ? 27.193  5.204  -9.221  1.00 60.15  ?  313 GLU A CB  1 
ATOM   2136 C  CG  . GLU A 1 313 ? 28.442  4.900  -8.403  1.00 74.35  ?  313 GLU A CG  1 
ATOM   2137 C  CD  . GLU A 1 313 ? 28.190  4.364  -6.996  1.00 86.77  ?  313 GLU A CD  1 
ATOM   2138 O  OE1 . GLU A 1 313 ? 27.415  3.395  -6.856  1.00 89.98  ?  313 GLU A OE1 1 
ATOM   2139 O  OE2 . GLU A 1 313 ? 28.766  4.918  -6.034  1.00 88.65  ?  313 GLU A OE2 1 
ATOM   2140 N  N   . VAL A 1 314 ? 25.903  7.310  -11.925 1.00 49.50  ?  314 VAL A N   1 
ATOM   2141 C  CA  . VAL A 1 314 ? 24.706  7.408  -12.815 1.00 53.77  ?  314 VAL A CA  1 
ATOM   2142 C  C   . VAL A 1 314 ? 25.131  7.950  -14.180 1.00 52.98  ?  314 VAL A C   1 
ATOM   2143 O  O   . VAL A 1 314 ? 25.833  8.972  -14.233 1.00 56.40  ?  314 VAL A O   1 
ATOM   2144 C  CB  . VAL A 1 314 ? 23.585  8.257  -12.175 1.00 48.84  ?  314 VAL A CB  1 
ATOM   2145 C  CG1 . VAL A 1 314 ? 22.482  8.579  -13.168 1.00 42.28  ?  314 VAL A CG1 1 
ATOM   2146 C  CG2 . VAL A 1 314 ? 23.025  7.561  -10.940 1.00 48.54  ?  314 VAL A CG2 1 
ATOM   2147 N  N   . GLU A 1 315 ? 24.707  7.274  -15.242 1.00 56.17  ?  315 GLU A N   1 
ATOM   2148 C  CA  . GLU A 1 315 ? 24.884  7.770  -16.624 1.00 58.67  ?  315 GLU A CA  1 
ATOM   2149 C  C   . GLU A 1 315 ? 23.679  8.660  -16.959 1.00 49.28  ?  315 GLU A C   1 
ATOM   2150 O  O   . GLU A 1 315 ? 22.608  8.132  -17.221 1.00 48.63  ?  315 GLU A O   1 
ATOM   2151 C  CB  . GLU A 1 315 ? 25.083  6.567  -17.552 1.00 66.89  ?  315 GLU A CB  1 
ATOM   2152 C  CG  . GLU A 1 315 ? 25.800  6.913  -18.850 1.00 75.85  ?  315 GLU A CG  1 
ATOM   2153 C  CD  . GLU A 1 315 ? 27.201  7.477  -18.681 1.00 78.68  ?  315 GLU A CD  1 
ATOM   2154 O  OE1 . GLU A 1 315 ? 27.983  6.895  -17.898 1.00 82.76  ?  315 GLU A OE1 1 
ATOM   2155 O  OE2 . GLU A 1 315 ? 27.498  8.501  -19.328 1.00 83.07  ?  315 GLU A OE2 1 
ATOM   2156 N  N   . ILE A 1 316 ? 23.827  9.977  -16.878 1.00 51.03  ?  316 ILE A N   1 
ATOM   2157 C  CA  . ILE A 1 316 ? 22.780  10.953 -17.317 1.00 51.46  ?  316 ILE A CA  1 
ATOM   2158 C  C   . ILE A 1 316 ? 22.947  11.149 -18.819 1.00 55.39  ?  316 ILE A C   1 
ATOM   2159 O  O   . ILE A 1 316 ? 24.055  11.556 -19.217 1.00 61.56  ?  316 ILE A O   1 
ATOM   2160 C  CB  . ILE A 1 316 ? 22.911  12.297 -16.571 1.00 47.37  ?  316 ILE A CB  1 
ATOM   2161 C  CG1 . ILE A 1 316 ? 22.725  12.131 -15.060 1.00 46.62  ?  316 ILE A CG1 1 
ATOM   2162 C  CG2 . ILE A 1 316 ? 21.983  13.349 -17.151 1.00 44.20  ?  316 ILE A CG2 1 
ATOM   2163 C  CD1 . ILE A 1 316 ? 23.102  13.373 -14.283 1.00 49.25  ?  316 ILE A CD1 1 
ATOM   2164 N  N   . ARG A 1 317 ? 21.897  10.866 -19.597 1.00 59.89  ?  317 ARG A N   1 
ATOM   2165 C  CA  . ARG A 1 317 ? 21.842  11.071 -21.072 1.00 55.34  ?  317 ARG A CA  1 
ATOM   2166 C  C   . ARG A 1 317 ? 21.548  12.543 -21.364 1.00 50.72  ?  317 ARG A C   1 
ATOM   2167 O  O   . ARG A 1 317 ? 20.880  13.195 -20.565 1.00 51.33  ?  317 ARG A O   1 
ATOM   2168 C  CB  . ARG A 1 317 ? 20.757  10.197 -21.716 1.00 67.25  ?  317 ARG A CB  1 
ATOM   2169 C  CG  . ARG A 1 317 ? 21.012  8.695  -21.668 1.00 74.38  ?  317 ARG A CG  1 
ATOM   2170 C  CD  . ARG A 1 317 ? 19.929  7.884  -22.363 1.00 86.05  ?  317 ARG A CD  1 
ATOM   2171 N  NE  . ARG A 1 317 ? 20.180  6.450  -22.230 1.00 99.97  ?  317 ARG A NE  1 
ATOM   2172 C  CZ  . ARG A 1 317 ? 19.361  5.471  -22.628 1.00 100.86 ?  317 ARG A CZ  1 
ATOM   2173 N  NH1 . ARG A 1 317 ? 18.196  5.748  -23.191 1.00 104.40 ?  317 ARG A NH1 1 
ATOM   2174 N  NH2 . ARG A 1 317 ? 19.721  4.207  -22.470 1.00 89.42  ?  317 ARG A NH2 1 
ATOM   2175 N  N   . ALA A 1 318 ? 22.006  13.031 -22.510 1.00 54.82  ?  318 ALA A N   1 
ATOM   2176 C  CA  . ALA A 1 318 ? 21.711  14.380 -23.042 1.00 53.91  ?  318 ALA A CA  1 
ATOM   2177 C  C   . ALA A 1 318 ? 20.194  14.645 -23.073 1.00 54.03  ?  318 ALA A C   1 
ATOM   2178 O  O   . ALA A 1 318 ? 19.406  13.746 -23.461 1.00 47.95  ?  318 ALA A O   1 
ATOM   2179 C  CB  . ALA A 1 318 ? 22.333  14.483 -24.408 1.00 53.71  ?  318 ALA A CB  1 
ATOM   2180 N  N   . GLY A 1 319 ? 19.782  15.831 -22.630 1.00 56.64  ?  319 GLY A N   1 
ATOM   2181 C  CA  . GLY A 1 319 ? 18.378  16.294 -22.721 1.00 60.39  ?  319 GLY A CA  1 
ATOM   2182 C  C   . GLY A 1 319 ? 17.494  15.853 -21.554 1.00 56.45  ?  319 GLY A C   1 
ATOM   2183 O  O   . GLY A 1 319 ? 16.317  16.306 -21.501 1.00 52.36  ?  319 GLY A O   1 
ATOM   2184 N  N   . GLU A 1 320 ? 18.019  15.004 -20.660 1.00 50.04  ?  320 GLU A N   1 
ATOM   2185 C  CA  . GLU A 1 320 ? 17.377  14.640 -19.367 1.00 47.16  ?  320 GLU A CA  1 
ATOM   2186 C  C   . GLU A 1 320 ? 17.472  15.820 -18.389 1.00 43.15  ?  320 GLU A C   1 
ATOM   2187 O  O   . GLU A 1 320 ? 18.389  16.692 -18.535 1.00 34.62  ?  320 GLU A O   1 
ATOM   2188 C  CB  . GLU A 1 320 ? 18.018  13.388 -18.768 1.00 46.87  ?  320 GLU A CB  1 
ATOM   2189 C  CG  . GLU A 1 320 ? 17.869  12.177 -19.657 1.00 46.41  ?  320 GLU A CG  1 
ATOM   2190 C  CD  . GLU A 1 320 ? 18.385  10.900 -19.037 1.00 48.39  ?  320 GLU A CD  1 
ATOM   2191 O  OE1 . GLU A 1 320 ? 19.478  10.926 -18.458 1.00 54.22  ?  320 GLU A OE1 1 
ATOM   2192 O  OE2 . GLU A 1 320 ? 17.690  9.883  -19.128 1.00 60.01  ?  320 GLU A OE2 1 
ATOM   2193 N  N   . LEU A 1 321 ? 16.516  15.874 -17.455 1.00 42.42  ?  321 LEU A N   1 
ATOM   2194 C  CA  . LEU A 1 321 ? 16.388  16.961 -16.448 1.00 39.97  ?  321 LEU A CA  1 
ATOM   2195 C  C   . LEU A 1 321 ? 17.209  16.562 -15.229 1.00 37.59  ?  321 LEU A C   1 
ATOM   2196 O  O   . LEU A 1 321 ? 17.067  15.413 -14.717 1.00 31.09  ?  321 LEU A O   1 
ATOM   2197 C  CB  . LEU A 1 321 ? 14.924  17.151 -16.064 1.00 41.42  ?  321 LEU A CB  1 
ATOM   2198 C  CG  . LEU A 1 321 ? 14.635  18.278 -15.084 1.00 42.33  ?  321 LEU A CG  1 
ATOM   2199 C  CD1 . LEU A 1 321 ? 15.240  19.583 -15.587 1.00 41.99  ?  321 LEU A CD1 1 
ATOM   2200 C  CD2 . LEU A 1 321 ? 13.122  18.424 -14.880 1.00 42.64  ?  321 LEU A CD2 1 
ATOM   2201 N  N   . VAL A 1 322 ? 18.068  17.473 -14.806 1.00 37.72  ?  322 VAL A N   1 
ATOM   2202 C  CA  . VAL A 1 322 ? 18.842  17.309 -13.554 1.00 38.14  ?  322 VAL A CA  1 
ATOM   2203 C  C   . VAL A 1 322 ? 18.398  18.385 -12.569 1.00 38.09  ?  322 VAL A C   1 
ATOM   2204 O  O   . VAL A 1 322 ? 18.231  19.569 -13.001 1.00 36.36  ?  322 VAL A O   1 
ATOM   2205 C  CB  . VAL A 1 322 ? 20.337  17.359 -13.858 1.00 39.10  ?  322 VAL A CB  1 
ATOM   2206 C  CG1 . VAL A 1 322 ? 21.167  17.161 -12.591 1.00 38.86  ?  322 VAL A CG1 1 
ATOM   2207 C  CG2 . VAL A 1 322 ? 20.644  16.320 -14.925 1.00 40.85  ?  322 VAL A CG2 1 
ATOM   2208 N  N   . LEU A 1 323 ? 18.171  17.957 -11.327 1.00 34.84  ?  323 LEU A N   1 
ATOM   2209 C  CA  . LEU A 1 323 ? 17.559  18.768 -10.244 1.00 36.50  ?  323 LEU A CA  1 
ATOM   2210 C  C   . LEU A 1 323 ? 18.500  18.783 -9.042  1.00 35.81  ?  323 LEU A C   1 
ATOM   2211 O  O   . LEU A 1 323 ? 18.756  17.708 -8.444  1.00 36.42  ?  323 LEU A O   1 
ATOM   2212 C  CB  . LEU A 1 323 ? 16.218  18.128 -9.881  1.00 33.47  ?  323 LEU A CB  1 
ATOM   2213 C  CG  . LEU A 1 323 ? 15.194  18.187 -11.005 1.00 33.46  ?  323 LEU A CG  1 
ATOM   2214 C  CD1 . LEU A 1 323 ? 13.897  17.507 -10.590 1.00 33.90  ?  323 LEU A CD1 1 
ATOM   2215 C  CD2 . LEU A 1 323 ? 14.958  19.641 -11.414 1.00 33.80  ?  323 LEU A CD2 1 
ATOM   2216 N  N   . VAL A 1 324 ? 18.982  19.963 -8.693  1.00 35.12  ?  324 VAL A N   1 
ATOM   2217 C  CA  . VAL A 1 324 ? 19.915  20.100 -7.545  1.00 38.77  ?  324 VAL A CA  1 
ATOM   2218 C  C   . VAL A 1 324 ? 19.139  20.422 -6.255  1.00 34.06  ?  324 VAL A C   1 
ATOM   2219 O  O   . VAL A 1 324 ? 18.590  21.526 -6.139  1.00 36.18  ?  324 VAL A O   1 
ATOM   2220 C  CB  . VAL A 1 324 ? 21.016  21.129 -7.843  1.00 40.91  ?  324 VAL A CB  1 
ATOM   2221 C  CG1 . VAL A 1 324 ? 21.999  21.199 -6.690  1.00 44.29  ?  324 VAL A CG1 1 
ATOM   2222 C  CG2 . VAL A 1 324 ? 21.741  20.795 -9.143  1.00 41.67  ?  324 VAL A CG2 1 
ATOM   2223 N  N   . LEU A 1 325 ? 19.166  19.472 -5.327  1.00 27.71  ?  325 LEU A N   1 
ATOM   2224 C  CA  . LEU A 1 325 ? 18.613  19.581 -3.975  1.00 28.12  ?  325 LEU A CA  1 
ATOM   2225 C  C   . LEU A 1 325 ? 19.623  20.248 -3.051  1.00 29.05  ?  325 LEU A C   1 
ATOM   2226 O  O   . LEU A 1 325 ? 20.391  19.519 -2.386  1.00 29.69  ?  325 LEU A O   1 
ATOM   2227 C  CB  . LEU A 1 325 ? 18.285  18.185 -3.445  1.00 28.98  ?  325 LEU A CB  1 
ATOM   2228 C  CG  . LEU A 1 325 ? 17.290  18.196 -2.287  1.00 29.28  ?  325 LEU A CG  1 
ATOM   2229 C  CD1 . LEU A 1 325 ? 15.933  18.666 -2.764  1.00 30.97  ?  325 LEU A CD1 1 
ATOM   2230 C  CD2 . LEU A 1 325 ? 17.178  16.842 -1.627  1.00 30.49  ?  325 LEU A CD2 1 
ATOM   2231 N  N   . ILE A 1 326 ? 19.488  21.560 -2.915  1.00 27.42  ?  326 ILE A N   1 
ATOM   2232 C  CA  . ILE A 1 326 ? 20.371  22.452 -2.127  1.00 30.57  ?  326 ILE A CA  1 
ATOM   2233 C  C   . ILE A 1 326 ? 20.380  22.021 -0.664  1.00 32.95  ?  326 ILE A C   1 
ATOM   2234 O  O   . ILE A 1 326 ? 21.471  22.039 -0.039  1.00 37.09  ?  326 ILE A O   1 
ATOM   2235 C  CB  . ILE A 1 326 ? 19.891  23.906 -2.284  1.00 34.22  ?  326 ILE A CB  1 
ATOM   2236 C  CG1 . ILE A 1 326 ? 20.033  24.385 -3.728  1.00 37.16  ?  326 ILE A CG1 1 
ATOM   2237 C  CG2 . ILE A 1 326 ? 20.603  24.823 -1.307  1.00 34.20  ?  326 ILE A CG2 1 
ATOM   2238 C  CD1 . ILE A 1 326 ? 21.462  24.331 -4.237  1.00 42.65  ?  326 ILE A CD1 1 
ATOM   2239 N  N   . GLU A 1 327 ? 19.215  21.722 -0.095  1.00 33.22  ?  327 GLU A N   1 
ATOM   2240 C  CA  . GLU A 1 327 ? 19.152  21.341 1.342   1.00 32.32  ?  327 GLU A CA  1 
ATOM   2241 C  C   . GLU A 1 327 ? 19.879  20.000 1.499   1.00 31.71  ?  327 GLU A C   1 
ATOM   2242 O  O   . GLU A 1 327 ? 20.339  19.716 2.602   1.00 32.09  ?  327 GLU A O   1 
ATOM   2243 C  CB  . GLU A 1 327 ? 17.715  21.321 1.868   1.00 31.56  ?  327 GLU A CB  1 
ATOM   2244 N  N   . GLY A 1 328 ? 19.950  19.203 0.431   1.00 30.03  ?  328 GLY A N   1 
ATOM   2245 C  CA  . GLY A 1 328 ? 20.772  17.981 0.377   1.00 33.06  ?  328 GLY A CA  1 
ATOM   2246 C  C   . GLY A 1 328 ? 22.245  18.315 0.581   1.00 32.53  ?  328 GLY A C   1 
ATOM   2247 O  O   . GLY A 1 328 ? 22.827  17.799 1.522   1.00 33.04  ?  328 GLY A O   1 
ATOM   2248 N  N   . ALA A 1 329 ? 22.809  19.189 -0.252  1.00 32.52  ?  329 ALA A N   1 
ATOM   2249 C  CA  . ALA A 1 329 ? 24.224  19.618 -0.191  1.00 34.10  ?  329 ALA A CA  1 
ATOM   2250 C  C   . ALA A 1 329 ? 24.523  20.391 1.109   1.00 35.96  ?  329 ALA A C   1 
ATOM   2251 O  O   . ALA A 1 329 ? 25.567  20.119 1.719   1.00 38.50  ?  329 ALA A O   1 
ATOM   2252 C  CB  . ALA A 1 329 ? 24.541  20.467 -1.387  1.00 34.74  ?  329 ALA A CB  1 
ATOM   2253 N  N   . ASN A 1 330 ? 23.645  21.300 1.549   1.00 34.15  ?  330 ASN A N   1 
ATOM   2254 C  CA  . ASN A 1 330 ? 23.903  22.186 2.724   1.00 29.65  ?  330 ASN A CA  1 
ATOM   2255 C  C   . ASN A 1 330 ? 23.819  21.452 4.081   1.00 28.63  ?  330 ASN A C   1 
ATOM   2256 O  O   . ASN A 1 330 ? 24.314  22.011 5.096   1.00 27.96  ?  330 ASN A O   1 
ATOM   2257 C  CB  . ASN A 1 330 ? 22.991  23.401 2.672   1.00 29.31  ?  330 ASN A CB  1 
ATOM   2258 C  CG  . ASN A 1 330 ? 23.415  24.369 1.593   1.00 29.16  ?  330 ASN A CG  1 
ATOM   2259 O  OD1 . ASN A 1 330 ? 24.435  24.160 0.935   1.00 34.88  ?  330 ASN A OD1 1 
ATOM   2260 N  ND2 . ASN A 1 330 ? 22.664  25.442 1.431   1.00 28.16  ?  330 ASN A ND2 1 
ATOM   2261 N  N   . TYR A 1 331 ? 23.319  20.216 4.105   1.00 27.96  ?  331 TYR A N   1 
ATOM   2262 C  CA  . TYR A 1 331 ? 23.208  19.382 5.320   1.00 27.83  ?  331 TYR A CA  1 
ATOM   2263 C  C   . TYR A 1 331 ? 24.112  18.150 5.169   1.00 30.30  ?  331 TYR A C   1 
ATOM   2264 O  O   . TYR A 1 331 ? 23.986  17.198 6.020   1.00 28.45  ?  331 TYR A O   1 
ATOM   2265 C  CB  . TYR A 1 331 ? 21.733  19.046 5.567   1.00 28.64  ?  331 TYR A CB  1 
ATOM   2266 C  CG  . TYR A 1 331 ? 20.887  20.172 6.134   1.00 30.69  ?  331 TYR A CG  1 
ATOM   2267 C  CD1 . TYR A 1 331 ? 20.471  21.250 5.363   1.00 30.44  ?  331 TYR A CD1 1 
ATOM   2268 C  CD2 . TYR A 1 331 ? 20.453  20.134 7.452   1.00 30.80  ?  331 TYR A CD2 1 
ATOM   2269 C  CE1 . TYR A 1 331 ? 19.679  22.260 5.894   1.00 32.77  ?  331 TYR A CE1 1 
ATOM   2270 C  CE2 . TYR A 1 331 ? 19.676  21.140 8.006   1.00 30.47  ?  331 TYR A CE2 1 
ATOM   2271 C  CZ  . TYR A 1 331 ? 19.279  22.206 7.221   1.00 34.23  ?  331 TYR A CZ  1 
ATOM   2272 O  OH  . TYR A 1 331 ? 18.520  23.192 7.791   1.00 32.24  ?  331 TYR A OH  1 
ATOM   2273 N  N   . ASP A 1 332 ? 24.975  18.138 4.134   1.00 30.98  ?  332 ASP A N   1 
ATOM   2274 C  CA  . ASP A 1 332 ? 25.917  17.017 3.847   1.00 31.84  ?  332 ASP A CA  1 
ATOM   2275 C  C   . ASP A 1 332 ? 27.010  16.979 4.928   1.00 30.97  ?  332 ASP A C   1 
ATOM   2276 O  O   . ASP A 1 332 ? 27.866  17.853 5.021   1.00 31.10  ?  332 ASP A O   1 
ATOM   2277 C  CB  . ASP A 1 332 ? 26.493  17.114 2.427   1.00 33.92  ?  332 ASP A CB  1 
ATOM   2278 C  CG  . ASP A 1 332 ? 27.147  15.816 1.957   1.00 37.82  ?  332 ASP A CG  1 
ATOM   2279 O  OD1 . ASP A 1 332 ? 27.467  14.954 2.837   1.00 39.81  ?  332 ASP A OD1 1 
ATOM   2280 O  OD2 . ASP A 1 332 ? 27.322  15.647 0.711   1.00 41.46  ?  332 ASP A OD2 1 
ATOM   2281 N  N   . PRO A 1 333 ? 27.037  15.965 5.805   1.00 30.41  ?  333 PRO A N   1 
ATOM   2282 C  CA  . PRO A 1 333 ? 28.065  15.907 6.837   1.00 35.62  ?  333 PRO A CA  1 
ATOM   2283 C  C   . PRO A 1 333 ? 29.516  15.714 6.338   1.00 38.57  ?  333 PRO A C   1 
ATOM   2284 O  O   . PRO A 1 333 ? 30.425  16.061 7.080   1.00 41.43  ?  333 PRO A O   1 
ATOM   2285 C  CB  . PRO A 1 333 ? 27.574  14.760 7.738   1.00 34.74  ?  333 PRO A CB  1 
ATOM   2286 C  CG  . PRO A 1 333 ? 26.742  13.886 6.830   1.00 32.23  ?  333 PRO A CG  1 
ATOM   2287 C  CD  . PRO A 1 333 ? 26.082  14.846 5.873   1.00 33.69  ?  333 PRO A CD  1 
ATOM   2288 N  N   . ALA A 1 334 ? 29.735  15.236 5.109   1.00 39.96  ?  334 ALA A N   1 
ATOM   2289 C  CA  . ALA A 1 334 ? 31.091  15.090 4.516   1.00 38.87  ?  334 ALA A CA  1 
ATOM   2290 C  C   . ALA A 1 334 ? 31.744  16.465 4.383   1.00 40.88  ?  334 ALA A C   1 
ATOM   2291 O  O   . ALA A 1 334 ? 32.977  16.490 4.262   1.00 45.27  ?  334 ALA A O   1 
ATOM   2292 C  CB  . ALA A 1 334 ? 31.054  14.411 3.174   1.00 36.78  ?  334 ALA A CB  1 
ATOM   2293 N  N   . VAL A 1 335 ? 30.956  17.547 4.378   1.00 36.58  ?  335 VAL A N   1 
ATOM   2294 C  CA  . VAL A 1 335 ? 31.464  18.938 4.201   1.00 35.60  ?  335 VAL A CA  1 
ATOM   2295 C  C   . VAL A 1 335 ? 31.174  19.762 5.454   1.00 37.38  ?  335 VAL A C   1 
ATOM   2296 O  O   . VAL A 1 335 ? 32.038  20.573 5.830   1.00 39.27  ?  335 VAL A O   1 
ATOM   2297 C  CB  . VAL A 1 335 ? 30.849  19.588 2.954   1.00 37.45  ?  335 VAL A CB  1 
ATOM   2298 C  CG1 . VAL A 1 335 ? 31.109  21.089 2.905   1.00 38.51  ?  335 VAL A CG1 1 
ATOM   2299 C  CG2 . VAL A 1 335 ? 31.302  18.902 1.659   1.00 35.81  ?  335 VAL A CG2 1 
ATOM   2300 N  N   . PHE A 1 336 ? 30.013  19.580 6.081   1.00 39.70  ?  336 PHE A N   1 
ATOM   2301 C  CA  . PHE A 1 336 ? 29.587  20.381 7.266   1.00 39.27  ?  336 PHE A CA  1 
ATOM   2302 C  C   . PHE A 1 336 ? 29.409  19.508 8.511   1.00 39.43  ?  336 PHE A C   1 
ATOM   2303 O  O   . PHE A 1 336 ? 28.440  18.767 8.636   1.00 36.99  ?  336 PHE A O   1 
ATOM   2304 C  CB  . PHE A 1 336 ? 28.281  21.119 6.985   1.00 35.80  ?  336 PHE A CB  1 
ATOM   2305 C  CG  . PHE A 1 336 ? 28.309  21.963 5.747   1.00 31.68  ?  336 PHE A CG  1 
ATOM   2306 C  CD1 . PHE A 1 336 ? 28.779  23.254 5.800   1.00 32.10  ?  336 PHE A CD1 1 
ATOM   2307 C  CD2 . PHE A 1 336 ? 27.843  21.462 4.547   1.00 32.57  ?  336 PHE A CD2 1 
ATOM   2308 C  CE1 . PHE A 1 336 ? 28.799  24.043 4.669   1.00 34.06  ?  336 PHE A CE1 1 
ATOM   2309 C  CE2 . PHE A 1 336 ? 27.843  22.247 3.415   1.00 32.42  ?  336 PHE A CE2 1 
ATOM   2310 C  CZ  . PHE A 1 336 ? 28.338  23.535 3.475   1.00 36.03  ?  336 PHE A CZ  1 
ATOM   2311 N  N   . PRO A 1 337 ? 30.316  19.593 9.503   1.00 37.28  ?  337 PRO A N   1 
ATOM   2312 C  CA  . PRO A 1 337 ? 30.112  18.860 10.737  1.00 34.27  ?  337 PRO A CA  1 
ATOM   2313 C  C   . PRO A 1 337 ? 28.815  19.325 11.417  1.00 34.62  ?  337 PRO A C   1 
ATOM   2314 O  O   . PRO A 1 337 ? 28.468  20.491 11.344  1.00 33.54  ?  337 PRO A O   1 
ATOM   2315 C  CB  . PRO A 1 337 ? 31.374  19.118 11.570  1.00 36.53  ?  337 PRO A CB  1 
ATOM   2316 C  CG  . PRO A 1 337 ? 32.133  20.235 10.863  1.00 37.07  ?  337 PRO A CG  1 
ATOM   2317 C  CD  . PRO A 1 337 ? 31.592  20.326 9.455   1.00 38.00  ?  337 PRO A CD  1 
ATOM   2318 N  N   . HIS A 1 338 ? 28.110  18.365 12.020  1.00 32.38  ?  338 HIS A N   1 
ATOM   2319 C  CA  . HIS A 1 338 ? 26.825  18.543 12.730  1.00 30.97  ?  338 HIS A CA  1 
ATOM   2320 C  C   . HIS A 1 338 ? 25.888  19.415 11.896  1.00 32.23  ?  338 HIS A C   1 
ATOM   2321 O  O   . HIS A 1 338 ? 25.278  20.358 12.389  1.00 32.85  ?  338 HIS A O   1 
ATOM   2322 C  CB  . HIS A 1 338 ? 27.085  19.047 14.153  1.00 31.48  ?  338 HIS A CB  1 
ATOM   2323 C  CG  . HIS A 1 338 ? 27.894  20.293 14.271  1.00 30.98  ?  338 HIS A CG  1 
ATOM   2324 N  ND1 . HIS A 1 338 ? 29.240  20.262 14.533  1.00 29.19  ?  338 HIS A ND1 1 
ATOM   2325 C  CD2 . HIS A 1 338 ? 27.549  21.600 14.207  1.00 31.59  ?  338 HIS A CD2 1 
ATOM   2326 C  CE1 . HIS A 1 338 ? 29.693  21.497 14.635  1.00 28.52  ?  338 HIS A CE1 1 
ATOM   2327 N  NE2 . HIS A 1 338 ? 28.681  22.343 14.428  1.00 27.45  ?  338 HIS A NE2 1 
ATOM   2328 N  N   . PRO A 1 339 ? 25.607  19.029 10.636  1.00 32.51  ?  339 PRO A N   1 
ATOM   2329 C  CA  . PRO A 1 339 ? 24.889  19.919 9.722   1.00 31.04  ?  339 PRO A CA  1 
ATOM   2330 C  C   . PRO A 1 339 ? 23.498  20.311 10.262  1.00 27.07  ?  339 PRO A C   1 
ATOM   2331 O  O   . PRO A 1 339 ? 23.006  21.349 9.907   1.00 22.15  ?  339 PRO A O   1 
ATOM   2332 C  CB  . PRO A 1 339 ? 24.845  19.064 8.438   1.00 29.92  ?  339 PRO A CB  1 
ATOM   2333 C  CG  . PRO A 1 339 ? 24.864  17.636 8.921   1.00 27.62  ?  339 PRO A CG  1 
ATOM   2334 C  CD  . PRO A 1 339 ? 25.820  17.677 10.083  1.00 29.66  ?  339 PRO A CD  1 
ATOM   2335 N  N   . GLU A 1 340 ? 22.911  19.472 11.118  1.00 28.63  ?  340 GLU A N   1 
ATOM   2336 C  CA  . GLU A 1 340 ? 21.493  19.593 11.590  1.00 31.14  ?  340 GLU A CA  1 
ATOM   2337 C  C   . GLU A 1 340 ? 21.403  20.674 12.663  1.00 33.04  ?  340 GLU A C   1 
ATOM   2338 O  O   . GLU A 1 340 ? 20.257  21.044 13.022  1.00 36.22  ?  340 GLU A O   1 
ATOM   2339 C  CB  . GLU A 1 340 ? 20.926  18.283 12.167  1.00 30.09  ?  340 GLU A CB  1 
ATOM   2340 C  CG  . GLU A 1 340 ? 21.491  17.840 13.506  1.00 27.61  ?  340 GLU A CG  1 
ATOM   2341 C  CD  . GLU A 1 340 ? 22.929  17.297 13.478  1.00 32.51  ?  340 GLU A CD  1 
ATOM   2342 O  OE1 . GLU A 1 340 ? 23.497  17.086 12.362  1.00 31.34  ?  340 GLU A OE1 1 
ATOM   2343 O  OE2 . GLU A 1 340 ? 23.525  17.124 14.588  1.00 39.66  ?  340 GLU A OE2 1 
ATOM   2344 N  N   . ARG A 1 341 ? 22.563  21.148 13.104  1.00 31.17  ?  341 ARG A N   1 
ATOM   2345 C  CA  . ARG A 1 341 ? 22.630  22.153 14.178  1.00 31.40  ?  341 ARG A CA  1 
ATOM   2346 C  C   . ARG A 1 341 ? 23.148  23.479 13.623  1.00 31.72  ?  341 ARG A C   1 
ATOM   2347 O  O   . ARG A 1 341 ? 24.074  23.450 12.810  1.00 34.88  ?  341 ARG A O   1 
ATOM   2348 C  CB  . ARG A 1 341 ? 23.564  21.592 15.251  1.00 30.89  ?  341 ARG A CB  1 
ATOM   2349 N  N   . ILE A 1 342 ? 22.568  24.590 14.077  1.00 32.40  ?  342 ILE A N   1 
ATOM   2350 C  CA  . ILE A 1 342 ? 23.012  25.945 13.631  1.00 32.98  ?  342 ILE A CA  1 
ATOM   2351 C  C   . ILE A 1 342 ? 24.274  26.328 14.420  1.00 32.81  ?  342 ILE A C   1 
ATOM   2352 O  O   . ILE A 1 342 ? 24.212  26.321 15.668  1.00 37.17  ?  342 ILE A O   1 
ATOM   2353 C  CB  . ILE A 1 342 ? 21.887  26.973 13.848  1.00 32.12  ?  342 ILE A CB  1 
ATOM   2354 C  CG1 . ILE A 1 342 ? 20.685  26.691 12.952  1.00 31.48  ?  342 ILE A CG1 1 
ATOM   2355 C  CG2 . ILE A 1 342 ? 22.400  28.401 13.666  1.00 35.04  ?  342 ILE A CG2 1 
ATOM   2356 C  CD1 . ILE A 1 342 ? 19.453  27.503 13.306  1.00 34.41  ?  342 ILE A CD1 1 
ATOM   2357 N  N   . ASP A 1 343 ? 25.365  26.650 13.720  1.00 32.21  ?  343 ASP A N   1 
ATOM   2358 C  CA  . ASP A 1 343 ? 26.619  27.074 14.403  1.00 34.75  ?  343 ASP A CA  1 
ATOM   2359 C  C   . ASP A 1 343 ? 27.075  28.420 13.830  1.00 33.60  ?  343 ASP A C   1 
ATOM   2360 O  O   . ASP A 1 343 ? 27.518  28.449 12.662  1.00 34.71  ?  343 ASP A O   1 
ATOM   2361 C  CB  . ASP A 1 343 ? 27.700  26.012 14.295  1.00 35.69  ?  343 ASP A CB  1 
ATOM   2362 C  CG  . ASP A 1 343 ? 29.023  26.361 14.962  1.00 38.15  ?  343 ASP A CG  1 
ATOM   2363 O  OD1 . ASP A 1 343 ? 29.001  27.139 15.939  1.00 37.45  ?  343 ASP A OD1 1 
ATOM   2364 O  OD2 . ASP A 1 343 ? 30.065  25.850 14.502  1.00 41.33  ?  343 ASP A OD2 1 
ATOM   2365 N  N   . PHE A 1 344 ? 26.982  29.486 14.632  1.00 32.69  ?  344 PHE A N   1 
ATOM   2366 C  CA  . PHE A 1 344 ? 27.416  30.824 14.157  1.00 33.50  ?  344 PHE A CA  1 
ATOM   2367 C  C   . PHE A 1 344 ? 28.920  30.950 14.285  1.00 35.84  ?  344 PHE A C   1 
ATOM   2368 O  O   . PHE A 1 344 ? 29.415  32.079 14.164  1.00 33.26  ?  344 PHE A O   1 
ATOM   2369 C  CB  . PHE A 1 344 ? 26.693  31.834 15.047  1.00 30.27  ?  344 PHE A CB  1 
ATOM   2370 C  CG  . PHE A 1 344 ? 25.220  32.088 14.760  1.00 28.97  ?  344 PHE A CG  1 
ATOM   2371 C  CD1 . PHE A 1 344 ? 24.577  31.472 13.695  1.00 29.91  ?  344 PHE A CD1 1 
ATOM   2372 C  CD2 . PHE A 1 344 ? 24.483  32.949 15.564  1.00 28.39  ?  344 PHE A CD2 1 
ATOM   2373 C  CE1 . PHE A 1 344 ? 23.237  31.713 13.445  1.00 32.92  ?  344 PHE A CE1 1 
ATOM   2374 C  CE2 . PHE A 1 344 ? 23.145  33.188 15.307  1.00 30.96  ?  344 PHE A CE2 1 
ATOM   2375 C  CZ  . PHE A 1 344 ? 22.525  32.569 14.250  1.00 34.61  ?  344 PHE A CZ  1 
ATOM   2376 N  N   . ASP A 1 345 ? 29.631  29.835 14.438  1.00 33.87  ?  345 ASP A N   1 
ATOM   2377 C  CA  . ASP A 1 345 ? 31.090  29.838 14.724  1.00 36.52  ?  345 ASP A CA  1 
ATOM   2378 C  C   . ASP A 1 345 ? 31.831  28.716 13.994  1.00 34.23  ?  345 ASP A C   1 
ATOM   2379 O  O   . ASP A 1 345 ? 32.828  28.252 14.547  1.00 33.05  ?  345 ASP A O   1 
ATOM   2380 C  CB  . ASP A 1 345 ? 31.346  29.743 16.218  1.00 33.87  ?  345 ASP A CB  1 
ATOM   2381 C  CG  . ASP A 1 345 ? 30.952  31.003 16.919  1.00 30.87  ?  345 ASP A CG  1 
ATOM   2382 O  OD1 . ASP A 1 345 ? 31.505  32.038 16.590  1.00 36.75  ?  345 ASP A OD1 1 
ATOM   2383 O  OD2 . ASP A 1 345 ? 30.092  30.929 17.749  1.00 31.67  ?  345 ASP A OD2 1 
ATOM   2384 N  N   . ARG A 1 346 ? 31.386  28.353 12.793  1.00 34.30  ?  346 ARG A N   1 
ATOM   2385 C  CA  . ARG A 1 346 ? 32.068  27.374 11.907  1.00 33.77  ?  346 ARG A CA  1 
ATOM   2386 C  C   . ARG A 1 346 ? 33.289  28.073 11.325  1.00 33.19  ?  346 ARG A C   1 
ATOM   2387 O  O   . ARG A 1 346 ? 33.169  29.243 10.957  1.00 33.30  ?  346 ARG A O   1 
ATOM   2388 C  CB  . ARG A 1 346 ? 31.165  26.904 10.756  1.00 32.40  ?  346 ARG A CB  1 
ATOM   2389 C  CG  . ARG A 1 346 ? 29.928  26.136 11.190  1.00 31.99  ?  346 ARG A CG  1 
ATOM   2390 C  CD  . ARG A 1 346 ? 28.905  25.905 10.087  1.00 31.98  ?  346 ARG A CD  1 
ATOM   2391 N  NE  . ARG A 1 346 ? 27.807  25.067 10.556  1.00 32.18  ?  346 ARG A NE  1 
ATOM   2392 C  CZ  . ARG A 1 346 ? 27.862  23.752 10.744  1.00 31.50  ?  346 ARG A CZ  1 
ATOM   2393 N  NH1 . ARG A 1 346 ? 28.961  23.089 10.474  1.00 32.64  ?  346 ARG A NH1 1 
ATOM   2394 N  NH2 . ARG A 1 346 ? 26.823  23.087 11.214  1.00 35.90  ?  346 ARG A NH2 1 
ATOM   2395 N  N   . GLU A 1 347 ? 34.409  27.368 11.248  1.00 39.60  ?  347 GLU A N   1 
ATOM   2396 C  CA  . GLU A 1 347 ? 35.661  27.872 10.630  1.00 49.04  ?  347 GLU A CA  1 
ATOM   2397 C  C   . GLU A 1 347 ? 35.380  28.299 9.189   1.00 46.63  ?  347 GLU A C   1 
ATOM   2398 O  O   . GLU A 1 347 ? 35.855  29.367 8.757   1.00 43.97  ?  347 GLU A O   1 
ATOM   2399 C  CB  . GLU A 1 347 ? 36.709  26.771 10.676  1.00 56.06  ?  347 GLU A CB  1 
ATOM   2400 C  CG  . GLU A 1 347 ? 37.137  26.455 12.089  1.00 65.66  ?  347 GLU A CG  1 
ATOM   2401 C  CD  . GLU A 1 347 ? 38.125  25.310 12.134  1.00 75.23  ?  347 GLU A CD  1 
ATOM   2402 O  OE1 . GLU A 1 347 ? 38.302  24.667 11.069  1.00 67.45  ?  347 GLU A OE1 1 
ATOM   2403 O  OE2 . GLU A 1 347 ? 38.741  25.106 13.217  1.00 81.31  ?  347 GLU A OE2 1 
ATOM   2404 N  N   . SER A 1 348 ? 34.559  27.501 8.519   1.00 47.18  ?  348 SER A N   1 
ATOM   2405 C  CA  . SER A 1 348 ? 34.340  27.503 7.059   1.00 45.69  ?  348 SER A CA  1 
ATOM   2406 C  C   . SER A 1 348 ? 32.850  27.246 6.795   1.00 45.15  ?  348 SER A C   1 
ATOM   2407 O  O   . SER A 1 348 ? 32.205  26.626 7.657   1.00 47.41  ?  348 SER A O   1 
ATOM   2408 C  CB  . SER A 1 348 ? 35.242  26.446 6.481   1.00 45.57  ?  348 SER A CB  1 
ATOM   2409 O  OG  . SER A 1 348 ? 35.038  26.318 5.104   1.00 49.93  ?  348 SER A OG  1 
ATOM   2410 N  N   . ASN A 1 349 ? 32.310  27.735 5.674   1.00 42.03  ?  349 ASN A N   1 
ATOM   2411 C  CA  . ASN A 1 349 ? 30.864  27.620 5.344   1.00 37.78  ?  349 ASN A CA  1 
ATOM   2412 C  C   . ASN A 1 349 ? 30.680  27.833 3.840   1.00 32.02  ?  349 ASN A C   1 
ATOM   2413 O  O   . ASN A 1 349 ? 30.200  28.878 3.403   1.00 27.96  ?  349 ASN A O   1 
ATOM   2414 C  CB  . ASN A 1 349 ? 30.026  28.602 6.164   1.00 38.22  ?  349 ASN A CB  1 
ATOM   2415 C  CG  . ASN A 1 349 ? 28.619  28.085 6.340   1.00 41.45  ?  349 ASN A CG  1 
ATOM   2416 O  OD1 . ASN A 1 349 ? 28.264  27.038 5.795   1.00 39.77  ?  349 ASN A OD1 1 
ATOM   2417 N  ND2 . ASN A 1 349 ? 27.835  28.776 7.143   1.00 44.17  ?  349 ASN A ND2 1 
ATOM   2418 N  N   . PRO A 1 350 ? 31.081  26.845 3.013   1.00 28.19  ?  350 PRO A N   1 
ATOM   2419 C  CA  . PRO A 1 350 ? 30.983  26.949 1.556   1.00 29.19  ?  350 PRO A CA  1 
ATOM   2420 C  C   . PRO A 1 350 ? 29.614  26.456 1.060   1.00 32.03  ?  350 PRO A C   1 
ATOM   2421 O  O   . PRO A 1 350 ? 29.566  25.499 0.250   1.00 33.01  ?  350 PRO A O   1 
ATOM   2422 C  CB  . PRO A 1 350 ? 32.117  26.022 1.073   1.00 25.86  ?  350 PRO A CB  1 
ATOM   2423 C  CG  . PRO A 1 350 ? 32.138  24.930 2.149   1.00 26.97  ?  350 PRO A CG  1 
ATOM   2424 C  CD  . PRO A 1 350 ? 31.957  25.720 3.428   1.00 27.78  ?  350 PRO A CD  1 
ATOM   2425 N  N   . HIS A 1 351 ? 28.539  27.118 1.497   1.00 30.89  ?  351 HIS A N   1 
ATOM   2426 C  CA  . HIS A 1 351 ? 27.151  26.614 1.311   1.00 31.60  ?  351 HIS A CA  1 
ATOM   2427 C  C   . HIS A 1 351 ? 26.651  26.975 -0.086  1.00 33.50  ?  351 HIS A C   1 
ATOM   2428 O  O   . HIS A 1 351 ? 27.219  27.900 -0.689  1.00 33.65  ?  351 HIS A O   1 
ATOM   2429 C  CB  . HIS A 1 351 ? 26.235  27.096 2.436   1.00 31.42  ?  351 HIS A CB  1 
ATOM   2430 C  CG  . HIS A 1 351 ? 26.036  28.561 2.430   1.00 30.72  ?  351 HIS A CG  1 
ATOM   2431 N  ND1 . HIS A 1 351 ? 25.403  29.210 1.386   1.00 33.25  ?  351 HIS A ND1 1 
ATOM   2432 C  CD2 . HIS A 1 351 ? 26.401  29.500 3.314   1.00 30.35  ?  351 HIS A CD2 1 
ATOM   2433 C  CE1 . HIS A 1 351 ? 25.411  30.506 1.628   1.00 32.55  ?  351 HIS A CE1 1 
ATOM   2434 N  NE2 . HIS A 1 351 ? 26.007  30.699 2.809   1.00 31.85  ?  351 HIS A NE2 1 
ATOM   2435 N  N   . LEU A 1 352 ? 25.645  26.240 -0.576  1.00 35.79  ?  352 LEU A N   1 
ATOM   2436 C  CA  . LEU A 1 352 ? 25.093  26.389 -1.948  1.00 35.20  ?  352 LEU A CA  1 
ATOM   2437 C  C   . LEU A 1 352 ? 23.725  27.074 -1.909  1.00 34.79  ?  352 LEU A C   1 
ATOM   2438 O  O   . LEU A 1 352 ? 22.950  26.856 -2.855  1.00 33.60  ?  352 LEU A O   1 
ATOM   2439 C  CB  . LEU A 1 352 ? 24.983  25.010 -2.592  1.00 33.76  ?  352 LEU A CB  1 
ATOM   2440 C  CG  . LEU A 1 352 ? 26.262  24.174 -2.561  1.00 35.78  ?  352 LEU A CG  1 
ATOM   2441 C  CD1 . LEU A 1 352 ? 26.095  22.895 -3.374  1.00 33.25  ?  352 LEU A CD1 1 
ATOM   2442 C  CD2 . LEU A 1 352 ? 27.460  24.962 -3.069  1.00 35.23  ?  352 LEU A CD2 1 
ATOM   2443 N  N   . ALA A 1 353 ? 23.459  27.895 -0.886  1.00 33.79  ?  353 ALA A N   1 
ATOM   2444 C  CA  . ALA A 1 353 ? 22.142  28.542 -0.661  1.00 34.82  ?  353 ALA A CA  1 
ATOM   2445 C  C   . ALA A 1 353 ? 21.864  29.538 -1.783  1.00 35.22  ?  353 ALA A C   1 
ATOM   2446 O  O   . ALA A 1 353 ? 20.687  29.744 -2.103  1.00 38.25  ?  353 ALA A O   1 
ATOM   2447 C  CB  . ALA A 1 353 ? 22.081  29.212 0.689   1.00 34.35  ?  353 ALA A CB  1 
ATOM   2448 N  N   . PHE A 1 354 ? 22.920  30.118 -2.351  1.00 34.99  ?  354 PHE A N   1 
ATOM   2449 C  CA  . PHE A 1 354 ? 22.875  31.068 -3.489  1.00 33.18  ?  354 PHE A CA  1 
ATOM   2450 C  C   . PHE A 1 354 ? 23.246  30.360 -4.802  1.00 35.88  ?  354 PHE A C   1 
ATOM   2451 O  O   . PHE A 1 354 ? 23.424  31.023 -5.863  1.00 34.35  ?  354 PHE A O   1 
ATOM   2452 C  CB  . PHE A 1 354 ? 23.848  32.189 -3.177  1.00 31.00  ?  354 PHE A CB  1 
ATOM   2453 C  CG  . PHE A 1 354 ? 23.374  33.166 -2.137  1.00 30.99  ?  354 PHE A CG  1 
ATOM   2454 C  CD1 . PHE A 1 354 ? 22.177  33.839 -2.297  1.00 30.62  ?  354 PHE A CD1 1 
ATOM   2455 C  CD2 . PHE A 1 354 ? 24.163  33.487 -1.052  1.00 28.98  ?  354 PHE A CD2 1 
ATOM   2456 C  CE1 . PHE A 1 354 ? 21.779  34.798 -1.383  1.00 27.70  ?  354 PHE A CE1 1 
ATOM   2457 C  CE2 . PHE A 1 354 ? 23.744  34.423 -0.123  1.00 27.84  ?  354 PHE A CE2 1 
ATOM   2458 C  CZ  . PHE A 1 354 ? 22.561  35.078 -0.295  1.00 26.96  ?  354 PHE A CZ  1 
ATOM   2459 N  N   . GLY A 1 355 ? 23.362  29.035 -4.744  1.00 36.02  ?  355 GLY A N   1 
ATOM   2460 C  CA  . GLY A 1 355 ? 23.806  28.217 -5.880  1.00 39.15  ?  355 GLY A CA  1 
ATOM   2461 C  C   . GLY A 1 355 ? 25.313  28.243 -6.008  1.00 40.40  ?  355 GLY A C   1 
ATOM   2462 O  O   . GLY A 1 355 ? 25.982  28.293 -4.986  1.00 39.69  ?  355 GLY A O   1 
ATOM   2463 N  N   . GLY A 1 356 ? 25.808  28.154 -7.238  1.00 49.31  ?  356 GLY A N   1 
ATOM   2464 C  CA  . GLY A 1 356 ? 27.238  28.223 -7.602  1.00 47.97  ?  356 GLY A CA  1 
ATOM   2465 C  C   . GLY A 1 356 ? 27.415  28.255 -9.118  1.00 49.98  ?  356 GLY A C   1 
ATOM   2466 O  O   . GLY A 1 356 ? 26.362  28.335 -9.863  1.00 41.81  ?  356 GLY A O   1 
ATOM   2467 N  N   . GLY A 1 357 ? 28.677  28.182 -9.567  1.00 46.49  ?  357 GLY A N   1 
ATOM   2468 C  CA  . GLY A 1 357 ? 29.084  28.320 -10.980 1.00 46.00  ?  357 GLY A CA  1 
ATOM   2469 C  C   . GLY A 1 357 ? 28.572  29.602 -11.612 1.00 43.33  ?  357 GLY A C   1 
ATOM   2470 O  O   . GLY A 1 357 ? 28.468  30.636 -10.914 1.00 45.18  ?  357 GLY A O   1 
ATOM   2471 N  N   . GLN A 1 358 ? 28.208  29.527 -12.887 1.00 44.71  ?  358 GLN A N   1 
ATOM   2472 C  CA  . GLN A 1 358 ? 27.823  30.689 -13.733 1.00 48.73  ?  358 GLN A CA  1 
ATOM   2473 C  C   . GLN A 1 358 ? 26.518  31.334 -13.201 1.00 47.78  ?  358 GLN A C   1 
ATOM   2474 O  O   . GLN A 1 358 ? 26.384  32.550 -13.334 1.00 41.53  ?  358 GLN A O   1 
ATOM   2475 C  CB  . GLN A 1 358 ? 27.766  30.200 -15.188 1.00 56.11  ?  358 GLN A CB  1 
ATOM   2476 C  CG  . GLN A 1 358 ? 27.525  31.283 -16.237 1.00 62.59  ?  358 GLN A CG  1 
ATOM   2477 C  CD  . GLN A 1 358 ? 27.660  30.708 -17.635 1.00 72.08  ?  358 GLN A CD  1 
ATOM   2478 O  OE1 . GLN A 1 358 ? 28.019  29.541 -17.829 1.00 66.64  ?  358 GLN A OE1 1 
ATOM   2479 N  NE2 . GLN A 1 358 ? 27.341  31.517 -18.638 1.00 71.45  ?  358 GLN A NE2 1 
ATOM   2480 N  N   . HIS A 1 359 ? 25.588  30.587 -12.589 1.00 44.50  ?  359 HIS A N   1 
ATOM   2481 C  CA  . HIS A 1 359 ? 24.249  31.116 -12.206 1.00 45.11  ?  359 HIS A CA  1 
ATOM   2482 C  C   . HIS A 1 359 ? 24.180  31.434 -10.706 1.00 45.44  ?  359 HIS A C   1 
ATOM   2483 O  O   . HIS A 1 359 ? 23.082  31.778 -10.218 1.00 47.47  ?  359 HIS A O   1 
ATOM   2484 C  CB  . HIS A 1 359 ? 23.141  30.165 -12.686 1.00 44.80  ?  359 HIS A CB  1 
ATOM   2485 C  CG  . HIS A 1 359 ? 23.097  30.036 -14.175 1.00 44.38  ?  359 HIS A CG  1 
ATOM   2486 N  ND1 . HIS A 1 359 ? 22.682  31.066 -14.989 1.00 40.94  ?  359 HIS A ND1 1 
ATOM   2487 C  CD2 . HIS A 1 359 ? 23.460  29.021 -14.998 1.00 41.69  ?  359 HIS A CD2 1 
ATOM   2488 C  CE1 . HIS A 1 359 ? 22.772  30.683 -16.249 1.00 41.19  ?  359 HIS A CE1 1 
ATOM   2489 N  NE2 . HIS A 1 359 ? 23.240  29.421 -16.276 1.00 38.67  ?  359 HIS A NE2 1 
ATOM   2490 N  N   . PHE A 1 360 ? 25.311  31.377 -10.001 1.00 43.05  ?  360 PHE A N   1 
ATOM   2491 C  CA  . PHE A 1 360 ? 25.409  31.854 -8.601  1.00 37.31  ?  360 PHE A CA  1 
ATOM   2492 C  C   . PHE A 1 360 ? 24.653  33.172 -8.508  1.00 37.74  ?  360 PHE A C   1 
ATOM   2493 O  O   . PHE A 1 360 ? 24.829  34.050 -9.389  1.00 35.08  ?  360 PHE A O   1 
ATOM   2494 C  CB  . PHE A 1 360 ? 26.862  32.056 -8.168  1.00 34.26  ?  360 PHE A CB  1 
ATOM   2495 C  CG  . PHE A 1 360 ? 27.052  32.558 -6.754  1.00 32.24  ?  360 PHE A CG  1 
ATOM   2496 C  CD1 . PHE A 1 360 ? 27.072  33.916 -6.481  1.00 28.15  ?  360 PHE A CD1 1 
ATOM   2497 C  CD2 . PHE A 1 360 ? 27.226  31.672 -5.698  1.00 30.15  ?  360 PHE A CD2 1 
ATOM   2498 C  CE1 . PHE A 1 360 ? 27.247  34.375 -5.182  1.00 28.59  ?  360 PHE A CE1 1 
ATOM   2499 C  CE2 . PHE A 1 360 ? 27.389  32.142 -4.405  1.00 28.90  ?  360 PHE A CE2 1 
ATOM   2500 C  CZ  . PHE A 1 360 ? 27.396  33.499 -4.150  1.00 27.13  ?  360 PHE A CZ  1 
ATOM   2501 N  N   . CYS A 1 361 ? 23.825  33.295 -7.479  1.00 37.78  ?  361 CYS A N   1 
ATOM   2502 C  CA  . CYS A 1 361 ? 22.949  34.473 -7.285  1.00 42.24  ?  361 CYS A CA  1 
ATOM   2503 C  C   . CYS A 1 361 ? 23.757  35.768 -7.460  1.00 44.65  ?  361 CYS A C   1 
ATOM   2504 O  O   . CYS A 1 361 ? 24.724  36.030 -6.741  1.00 44.41  ?  361 CYS A O   1 
ATOM   2505 C  CB  . CYS A 1 361 ? 22.261  34.427 -5.925  1.00 40.06  ?  361 CYS A CB  1 
ATOM   2506 S  SG  . CYS A 1 361 ? 21.194  35.857 -5.641  1.00 40.86  ?  361 CYS A SG  1 
ATOM   2507 N  N   . PRO A 1 362 ? 23.352  36.647 -8.398  1.00 40.36  ?  362 PRO A N   1 
ATOM   2508 C  CA  . PRO A 1 362 ? 24.006  37.939 -8.579  1.00 43.55  ?  362 PRO A CA  1 
ATOM   2509 C  C   . PRO A 1 362 ? 23.680  39.001 -7.529  1.00 40.66  ?  362 PRO A C   1 
ATOM   2510 O  O   . PRO A 1 362 ? 24.333  40.022 -7.531  1.00 47.09  ?  362 PRO A O   1 
ATOM   2511 C  CB  . PRO A 1 362 ? 23.420  38.439 -9.907  1.00 47.20  ?  362 PRO A CB  1 
ATOM   2512 C  CG  . PRO A 1 362 ? 22.029  37.848 -9.907  1.00 52.18  ?  362 PRO A CG  1 
ATOM   2513 C  CD  . PRO A 1 362 ? 22.217  36.462 -9.314  1.00 46.42  ?  362 PRO A CD  1 
ATOM   2514 N  N   . ALA A 1 363 ? 22.660  38.775 -6.707  1.00 39.57  ?  363 ALA A N   1 
ATOM   2515 C  CA  . ALA A 1 363 ? 22.193  39.743 -5.682  1.00 36.18  ?  363 ALA A CA  1 
ATOM   2516 C  C   . ALA A 1 363 ? 22.552  39.261 -4.271  1.00 33.27  ?  363 ALA A C   1 
ATOM   2517 O  O   . ALA A 1 363 ? 21.882  39.737 -3.303  1.00 34.16  ?  363 ALA A O   1 
ATOM   2518 C  CB  . ALA A 1 363 ? 20.702  39.954 -5.819  1.00 32.86  ?  363 ALA A CB  1 
ATOM   2519 N  N   . SER A 1 364 ? 23.531  38.359 -4.143  1.00 29.48  ?  364 SER A N   1 
ATOM   2520 C  CA  . SER A 1 364 ? 23.888  37.703 -2.856  1.00 32.11  ?  364 SER A CA  1 
ATOM   2521 C  C   . SER A 1 364 ? 24.041  38.774 -1.785  1.00 35.03  ?  364 SER A C   1 
ATOM   2522 O  O   . SER A 1 364 ? 23.379  38.661 -0.750  1.00 36.37  ?  364 SER A O   1 
ATOM   2523 C  CB  . SER A 1 364 ? 25.120  36.827 -2.947  1.00 34.87  ?  364 SER A CB  1 
ATOM   2524 O  OG  . SER A 1 364 ? 26.300  37.561 -3.291  1.00 33.95  ?  364 SER A OG  1 
ATOM   2525 N  N   . ALA A 1 365 ? 24.847  39.806 -2.038  1.00 36.55  ?  365 ALA A N   1 
ATOM   2526 C  CA  . ALA A 1 365 ? 25.193  40.804 -0.995  1.00 36.36  ?  365 ALA A CA  1 
ATOM   2527 C  C   . ALA A 1 365 ? 23.930  41.563 -0.571  1.00 35.44  ?  365 ALA A C   1 
ATOM   2528 O  O   . ALA A 1 365 ? 23.821  41.957 0.629   1.00 39.64  ?  365 ALA A O   1 
ATOM   2529 C  CB  . ALA A 1 365 ? 26.272  41.750 -1.490  1.00 36.55  ?  365 ALA A CB  1 
ATOM   2530 N  N   . LEU A 1 366 ? 23.032  41.815 -1.522  1.00 34.15  ?  366 LEU A N   1 
ATOM   2531 C  CA  . LEU A 1 366 ? 21.745  42.515 -1.272  1.00 34.83  ?  366 LEU A CA  1 
ATOM   2532 C  C   . LEU A 1 366 ? 20.884  41.612 -0.407  1.00 33.53  ?  366 LEU A C   1 
ATOM   2533 O  O   . LEU A 1 366 ? 20.332  42.103 0.596   1.00 34.38  ?  366 LEU A O   1 
ATOM   2534 C  CB  . LEU A 1 366 ? 21.045  42.790 -2.598  1.00 38.15  ?  366 LEU A CB  1 
ATOM   2535 C  CG  . LEU A 1 366 ? 21.750  43.751 -3.544  1.00 44.59  ?  366 LEU A CG  1 
ATOM   2536 C  CD1 . LEU A 1 366 ? 21.058  43.853 -4.896  1.00 46.94  ?  366 LEU A CD1 1 
ATOM   2537 C  CD2 . LEU A 1 366 ? 21.843  45.124 -2.898  1.00 44.02  ?  366 LEU A CD2 1 
ATOM   2538 N  N   . GLY A 1 367 ? 20.861  40.324 -0.760  1.00 33.85  ?  367 GLY A N   1 
ATOM   2539 C  CA  . GLY A 1 367 ? 20.219  39.255 0.025   1.00 34.36  ?  367 GLY A CA  1 
ATOM   2540 C  C   . GLY A 1 367 ? 20.669  39.290 1.466   1.00 33.54  ?  367 GLY A C   1 
ATOM   2541 O  O   . GLY A 1 367 ? 19.796  39.439 2.343   1.00 38.36  ?  367 GLY A O   1 
ATOM   2542 N  N   . ARG A 1 368 ? 21.978  39.193 1.687   1.00 30.12  ?  368 ARG A N   1 
ATOM   2543 C  CA  . ARG A 1 368 ? 22.613  39.245 3.028   1.00 33.07  ?  368 ARG A CA  1 
ATOM   2544 C  C   . ARG A 1 368 ? 22.258  40.568 3.721   1.00 31.14  ?  368 ARG A C   1 
ATOM   2545 O  O   . ARG A 1 368 ? 21.807  40.508 4.869   1.00 35.43  ?  368 ARG A O   1 
ATOM   2546 C  CB  . ARG A 1 368 ? 24.142  39.108 2.941   1.00 34.71  ?  368 ARG A CB  1 
ATOM   2547 C  CG  . ARG A 1 368 ? 24.667  37.834 2.297   1.00 31.78  ?  368 ARG A CG  1 
ATOM   2548 C  CD  . ARG A 1 368 ? 26.180  37.896 2.172   1.00 31.75  ?  368 ARG A CD  1 
ATOM   2549 N  NE  . ARG A 1 368 ? 26.775  36.665 1.678   1.00 31.23  ?  368 ARG A NE  1 
ATOM   2550 C  CZ  . ARG A 1 368 ? 26.827  35.516 2.361   1.00 38.08  ?  368 ARG A CZ  1 
ATOM   2551 N  NH1 . ARG A 1 368 ? 26.318  35.439 3.587   1.00 41.44  ?  368 ARG A NH1 1 
ATOM   2552 N  NH2 . ARG A 1 368 ? 27.400  34.440 1.830   1.00 35.45  ?  368 ARG A NH2 1 
ATOM   2553 N  N   . THR A 1 369 ? 22.460  41.715 3.073   1.00 30.28  ?  369 THR A N   1 
ATOM   2554 C  CA  . THR A 1 369 ? 22.127  43.045 3.650   1.00 34.39  ?  369 THR A CA  1 
ATOM   2555 C  C   . THR A 1 369 ? 20.658  43.071 4.110   1.00 33.89  ?  369 THR A C   1 
ATOM   2556 O  O   . THR A 1 369 ? 20.384  43.344 5.293   1.00 38.37  ?  369 THR A O   1 
ATOM   2557 C  CB  . THR A 1 369 ? 22.456  44.178 2.668   1.00 36.15  ?  369 THR A CB  1 
ATOM   2558 O  OG1 . THR A 1 369 ? 23.866  44.146 2.481   1.00 36.78  ?  369 THR A OG1 1 
ATOM   2559 C  CG2 . THR A 1 369 ? 22.055  45.551 3.167   1.00 34.47  ?  369 THR A CG2 1 
ATOM   2560 N  N   . HIS A 1 370 ? 19.726  42.793 3.222   1.00 32.69  ?  370 HIS A N   1 
ATOM   2561 C  CA  . HIS A 1 370 ? 18.299  42.645 3.594   1.00 36.11  ?  370 HIS A CA  1 
ATOM   2562 C  C   . HIS A 1 370 ? 18.153  41.929 4.946   1.00 33.26  ?  370 HIS A C   1 
ATOM   2563 O  O   . HIS A 1 370 ? 17.483  42.463 5.859   1.00 33.17  ?  370 HIS A O   1 
ATOM   2564 C  CB  . HIS A 1 370 ? 17.573  41.922 2.455   1.00 39.79  ?  370 HIS A CB  1 
ATOM   2565 C  CG  . HIS A 1 370 ? 16.169  41.539 2.767   1.00 39.37  ?  370 HIS A CG  1 
ATOM   2566 N  ND1 . HIS A 1 370 ? 15.865  40.414 3.527   1.00 41.87  ?  370 HIS A ND1 1 
ATOM   2567 C  CD2 . HIS A 1 370 ? 15.002  42.074 2.369   1.00 36.98  ?  370 HIS A CD2 1 
ATOM   2568 C  CE1 . HIS A 1 370 ? 14.553  40.308 3.623   1.00 43.72  ?  370 HIS A CE1 1 
ATOM   2569 N  NE2 . HIS A 1 370 ? 14.007  41.291 2.893   1.00 43.99  ?  370 HIS A NE2 1 
ATOM   2570 N  N   . ALA A 1 371 ? 18.701  40.727 5.062   1.00 32.14  ?  371 ALA A N   1 
ATOM   2571 C  CA  . ALA A 1 371 ? 18.464  39.842 6.220   1.00 31.70  ?  371 ALA A CA  1 
ATOM   2572 C  C   . ALA A 1 371 ? 19.216  40.400 7.434   1.00 33.31  ?  371 ALA A C   1 
ATOM   2573 O  O   . ALA A 1 371 ? 18.622  40.495 8.521   1.00 36.63  ?  371 ALA A O   1 
ATOM   2574 C  CB  . ALA A 1 371 ? 18.855  38.422 5.883   1.00 31.50  ?  371 ALA A CB  1 
ATOM   2575 N  N   . GLU A 1 372 ? 20.478  40.793 7.281   1.00 36.64  ?  372 GLU A N   1 
ATOM   2576 C  CA  . GLU A 1 372 ? 21.279  41.297 8.441   1.00 36.21  ?  372 GLU A CA  1 
ATOM   2577 C  C   . GLU A 1 372 ? 20.487  42.416 9.138   1.00 35.59  ?  372 GLU A C   1 
ATOM   2578 O  O   . GLU A 1 372 ? 20.357  42.380 10.390  1.00 34.44  ?  372 GLU A O   1 
ATOM   2579 C  CB  . GLU A 1 372 ? 22.671  41.742 8.000   1.00 34.05  ?  372 GLU A CB  1 
ATOM   2580 C  CG  . GLU A 1 372 ? 23.556  40.568 7.606   1.00 37.49  ?  372 GLU A CG  1 
ATOM   2581 C  CD  . GLU A 1 372 ? 24.876  40.939 6.949   1.00 40.28  ?  372 GLU A CD  1 
ATOM   2582 O  OE1 . GLU A 1 372 ? 25.315  42.101 7.129   1.00 46.64  ?  372 GLU A OE1 1 
ATOM   2583 O  OE2 . GLU A 1 372 ? 25.464  40.067 6.267   1.00 37.73  ?  372 GLU A OE2 1 
ATOM   2584 N  N   . ILE A 1 373 ? 19.891  43.324 8.358   1.00 32.93  ?  373 ILE A N   1 
ATOM   2585 C  CA  . ILE A 1 373 ? 19.317  44.580 8.921   1.00 33.29  ?  373 ILE A CA  1 
ATOM   2586 C  C   . ILE A 1 373 ? 17.935  44.309 9.542   1.00 31.02  ?  373 ILE A C   1 
ATOM   2587 O  O   . ILE A 1 373 ? 17.635  44.900 10.580  1.00 28.16  ?  373 ILE A O   1 
ATOM   2588 C  CB  . ILE A 1 373 ? 19.352  45.698 7.868   1.00 32.22  ?  373 ILE A CB  1 
ATOM   2589 C  CG1 . ILE A 1 373 ? 20.805  46.140 7.650   1.00 35.24  ?  373 ILE A CG1 1 
ATOM   2590 C  CG2 . ILE A 1 373 ? 18.460  46.862 8.289   1.00 30.62  ?  373 ILE A CG2 1 
ATOM   2591 C  CD1 . ILE A 1 373 ? 21.045  46.936 6.377   1.00 39.06  ?  373 ILE A CD1 1 
ATOM   2592 N  N   . ALA A 1 374 ? 17.149  43.408 8.966   1.00 32.36  ?  374 ALA A N   1 
ATOM   2593 C  CA  . ALA A 1 374 ? 15.854  42.976 9.532   1.00 34.16  ?  374 ALA A CA  1 
ATOM   2594 C  C   . ALA A 1 374 ? 16.103  42.202 10.826  1.00 32.93  ?  374 ALA A C   1 
ATOM   2595 O  O   . ALA A 1 374 ? 15.324  42.430 11.828  1.00 31.08  ?  374 ALA A O   1 
ATOM   2596 C  CB  . ALA A 1 374 ? 15.103  42.135 8.529   1.00 40.34  ?  374 ALA A CB  1 
ATOM   2597 N  N   . LEU A 1 375 ? 17.116  41.324 10.832  1.00 27.08  ?  375 LEU A N   1 
ATOM   2598 C  CA  . LEU A 1 375 ? 17.304  40.421 11.998  1.00 27.91  ?  375 LEU A CA  1 
ATOM   2599 C  C   . LEU A 1 375 ? 17.897  41.226 13.154  1.00 28.97  ?  375 LEU A C   1 
ATOM   2600 O  O   . LEU A 1 375 ? 17.442  41.032 14.307  1.00 24.88  ?  375 LEU A O   1 
ATOM   2601 C  CB  . LEU A 1 375 ? 18.180  39.230 11.619  1.00 27.44  ?  375 LEU A CB  1 
ATOM   2602 C  CG  . LEU A 1 375 ? 17.534  38.273 10.629  1.00 28.06  ?  375 LEU A CG  1 
ATOM   2603 C  CD1 . LEU A 1 375 ? 18.496  37.148 10.312  1.00 30.72  ?  375 LEU A CD1 1 
ATOM   2604 C  CD2 . LEU A 1 375 ? 16.237  37.737 11.169  1.00 27.98  ?  375 LEU A CD2 1 
ATOM   2605 N  N   . THR A 1 376 ? 18.880  42.086 12.853  1.00 28.80  ?  376 THR A N   1 
ATOM   2606 C  CA  . THR A 1 376 ? 19.423  43.056 13.829  1.00 26.56  ?  376 THR A CA  1 
ATOM   2607 C  C   . THR A 1 376 ? 18.277  43.863 14.424  1.00 25.92  ?  376 THR A C   1 
ATOM   2608 O  O   . THR A 1 376 ? 18.185  43.945 15.622  1.00 29.65  ?  376 THR A O   1 
ATOM   2609 C  CB  . THR A 1 376 ? 20.452  43.977 13.189  1.00 26.64  ?  376 THR A CB  1 
ATOM   2610 O  OG1 . THR A 1 376 ? 21.575  43.163 12.819  1.00 30.84  ?  376 THR A OG1 1 
ATOM   2611 C  CG2 . THR A 1 376 ? 20.848  45.085 14.131  1.00 24.32  ?  376 THR A CG2 1 
ATOM   2612 N  N   . ALA A 1 377 ? 17.389  44.405 13.612  1.00 28.48  ?  377 ALA A N   1 
ATOM   2613 C  CA  . ALA A 1 377 ? 16.259  45.226 14.111  1.00 30.90  ?  377 ALA A CA  1 
ATOM   2614 C  C   . ALA A 1 377 ? 15.308  44.344 14.946  1.00 32.72  ?  377 ALA A C   1 
ATOM   2615 O  O   . ALA A 1 377 ? 14.850  44.794 16.015  1.00 31.18  ?  377 ALA A O   1 
ATOM   2616 C  CB  . ALA A 1 377 ? 15.576  45.902 12.941  1.00 30.27  ?  377 ALA A CB  1 
ATOM   2617 N  N   . LEU A 1 378 ? 15.098  43.090 14.521  1.00 34.42  ?  378 LEU A N   1 
ATOM   2618 C  CA  . LEU A 1 378 ? 14.162  42.126 15.166  1.00 31.80  ?  378 LEU A CA  1 
ATOM   2619 C  C   . LEU A 1 378 ? 14.637  41.754 16.567  1.00 29.06  ?  378 LEU A C   1 
ATOM   2620 O  O   . LEU A 1 378 ? 13.836  41.864 17.535  1.00 30.21  ?  378 LEU A O   1 
ATOM   2621 C  CB  . LEU A 1 378 ? 14.078  40.882 14.292  1.00 36.89  ?  378 LEU A CB  1 
ATOM   2622 C  CG  . LEU A 1 378 ? 13.150  39.794 14.807  1.00 38.43  ?  378 LEU A CG  1 
ATOM   2623 C  CD1 . LEU A 1 378 ? 11.700  40.289 14.868  1.00 38.99  ?  378 LEU A CD1 1 
ATOM   2624 C  CD2 . LEU A 1 378 ? 13.279  38.576 13.919  1.00 36.60  ?  378 LEU A CD2 1 
ATOM   2625 N  N   . VAL A 1 379 ? 15.898  41.383 16.713  1.00 25.74  ?  379 VAL A N   1 
ATOM   2626 C  CA  . VAL A 1 379 ? 16.375  40.941 18.045  1.00 29.46  ?  379 VAL A CA  1 
ATOM   2627 C  C   . VAL A 1 379 ? 16.528  42.144 18.977  1.00 33.24  ?  379 VAL A C   1 
ATOM   2628 O  O   . VAL A 1 379 ? 16.406  41.920 20.211  1.00 39.59  ?  379 VAL A O   1 
ATOM   2629 C  CB  . VAL A 1 379 ? 17.630  40.057 17.956  1.00 30.69  ?  379 VAL A CB  1 
ATOM   2630 C  CG1 . VAL A 1 379 ? 17.323  38.756 17.221  1.00 31.60  ?  379 VAL A CG1 1 
ATOM   2631 C  CG2 . VAL A 1 379 ? 18.812  40.768 17.322  1.00 31.71  ?  379 VAL A CG2 1 
ATOM   2632 N  N   . GLU A 1 380 ? 16.709  43.367 18.460  1.00 37.95  ?  380 GLU A N   1 
ATOM   2633 C  CA  . GLU A 1 380 ? 16.719  44.603 19.305  1.00 39.99  ?  380 GLU A CA  1 
ATOM   2634 C  C   . GLU A 1 380 ? 15.297  44.873 19.802  1.00 36.84  ?  380 GLU A C   1 
ATOM   2635 O  O   . GLU A 1 380 ? 15.127  45.048 20.988  1.00 34.95  ?  380 GLU A O   1 
ATOM   2636 C  CB  . GLU A 1 380 ? 17.209  45.864 18.577  1.00 48.55  ?  380 GLU A CB  1 
ATOM   2637 C  CG  . GLU A 1 380 ? 18.704  45.960 18.246  1.00 50.16  ?  380 GLU A CG  1 
ATOM   2638 C  CD  . GLU A 1 380 ? 19.046  47.243 17.482  1.00 56.26  ?  380 GLU A CD  1 
ATOM   2639 O  OE1 . GLU A 1 380 ? 18.126  48.111 17.340  1.00 55.01  ?  380 GLU A OE1 1 
ATOM   2640 O  OE2 . GLU A 1 380 ? 20.221  47.397 17.019  1.00 49.98  ?  380 GLU A OE2 1 
ATOM   2641 N  N   . LYS A 1 381 ? 14.299  44.906 18.919  1.00 40.66  ?  381 LYS A N   1 
ATOM   2642 C  CA  . LYS A 1 381 ? 12.931  45.413 19.252  1.00 39.40  ?  381 LYS A CA  1 
ATOM   2643 C  C   . LYS A 1 381 ? 12.101  44.368 20.014  1.00 37.05  ?  381 LYS A C   1 
ATOM   2644 O  O   . LYS A 1 381 ? 11.270  44.829 20.850  1.00 31.32  ?  381 LYS A O   1 
ATOM   2645 C  CB  . LYS A 1 381 ? 12.162  45.808 17.989  1.00 40.51  ?  381 LYS A CB  1 
ATOM   2646 C  CG  . LYS A 1 381 ? 12.659  47.061 17.298  1.00 45.70  ?  381 LYS A CG  1 
ATOM   2647 C  CD  . LYS A 1 381 ? 12.360  48.289 18.120  1.00 50.86  ?  381 LYS A CD  1 
ATOM   2648 C  CE  . LYS A 1 381 ? 11.800  49.399 17.272  1.00 51.79  ?  381 LYS A CE  1 
ATOM   2649 N  NZ  . LYS A 1 381 ? 12.376  50.694 17.679  1.00 58.47  ?  381 LYS A NZ  1 
ATOM   2650 N  N   . LEU A 1 382 ? 12.224  43.062 19.670  1.00 36.26  ?  382 LEU A N   1 
ATOM   2651 C  CA  . LEU A 1 382 ? 11.384  41.936 20.213  1.00 34.66  ?  382 LEU A CA  1 
ATOM   2652 C  C   . LEU A 1 382 ? 12.264  40.908 20.918  1.00 33.14  ?  382 LEU A C   1 
ATOM   2653 O  O   . LEU A 1 382 ? 12.347  39.755 20.514  1.00 32.68  ?  382 LEU A O   1 
ATOM   2654 C  CB  . LEU A 1 382 ? 10.612  41.255 19.084  1.00 33.48  ?  382 LEU A CB  1 
ATOM   2655 C  CG  . LEU A 1 382 ? 9.801   42.167 18.173  1.00 34.99  ?  382 LEU A CG  1 
ATOM   2656 C  CD1 . LEU A 1 382 ? 9.028   41.344 17.173  1.00 33.56  ?  382 LEU A CD1 1 
ATOM   2657 C  CD2 . LEU A 1 382 ? 8.843   43.029 18.975  1.00 38.59  ?  382 LEU A CD2 1 
ATOM   2658 N  N   . PRO A 1 383 ? 13.005  41.290 21.975  1.00 33.01  ?  383 PRO A N   1 
ATOM   2659 C  CA  . PRO A 1 383 ? 13.965  40.365 22.582  1.00 32.93  ?  383 PRO A CA  1 
ATOM   2660 C  C   . PRO A 1 383 ? 13.362  39.070 23.165  1.00 28.45  ?  383 PRO A C   1 
ATOM   2661 O  O   . PRO A 1 383 ? 14.097  38.164 23.300  1.00 31.27  ?  383 PRO A O   1 
ATOM   2662 C  CB  . PRO A 1 383 ? 14.675  41.223 23.663  1.00 31.19  ?  383 PRO A CB  1 
ATOM   2663 C  CG  . PRO A 1 383 ? 13.733  42.393 23.912  1.00 30.36  ?  383 PRO A CG  1 
ATOM   2664 C  CD  . PRO A 1 383 ? 13.023  42.624 22.596  1.00 30.37  ?  383 PRO A CD  1 
ATOM   2665 N  N   . ALA A 1 384 ? 12.065  39.004 23.477  1.00 27.46  ?  384 ALA A N   1 
ATOM   2666 C  CA  . ALA A 1 384 ? 11.365  37.790 23.986  1.00 26.55  ?  384 ALA A CA  1 
ATOM   2667 C  C   . ALA A 1 384 ? 10.572  37.135 22.846  1.00 28.36  ?  384 ALA A C   1 
ATOM   2668 O  O   . ALA A 1 384 ? 9.567   36.415 23.084  1.00 27.57  ?  384 ALA A O   1 
ATOM   2669 C  CB  . ALA A 1 384 ? 10.445  38.128 25.137  1.00 24.90  ?  384 ALA A CB  1 
ATOM   2670 N  N   . LEU A 1 385 ? 11.042  37.345 21.634  1.00 28.19  ?  385 LEU A N   1 
ATOM   2671 C  CA  . LEU A 1 385 ? 10.425  36.750 20.446  1.00 29.04  ?  385 LEU A CA  1 
ATOM   2672 C  C   . LEU A 1 385 ? 10.399  35.243 20.626  1.00 28.98  ?  385 LEU A C   1 
ATOM   2673 O  O   . LEU A 1 385 ? 11.484  34.657 20.863  1.00 33.61  ?  385 LEU A O   1 
ATOM   2674 C  CB  . LEU A 1 385 ? 11.262  37.155 19.237  1.00 30.19  ?  385 LEU A CB  1 
ATOM   2675 C  CG  . LEU A 1 385 ? 10.970  36.367 17.967  1.00 33.10  ?  385 LEU A CG  1 
ATOM   2676 C  CD1 . LEU A 1 385 ? 9.652   36.837 17.330  1.00 29.87  ?  385 LEU A CD1 1 
ATOM   2677 C  CD2 . LEU A 1 385 ? 12.168  36.451 17.014  1.00 31.64  ?  385 LEU A CD2 1 
ATOM   2678 N  N   . ARG A 1 386 ? 9.220   34.654 20.418  1.00 30.56  ?  386 ARG A N   1 
ATOM   2679 C  CA  . ARG A 1 386 ? 8.973   33.178 20.353  1.00 28.28  ?  386 ARG A CA  1 
ATOM   2680 C  C   . ARG A 1 386 ? 7.768   32.901 19.459  1.00 25.24  ?  386 ARG A C   1 
ATOM   2681 O  O   . ARG A 1 386 ? 6.995   33.804 19.242  1.00 24.65  ?  386 ARG A O   1 
ATOM   2682 C  CB  . ARG A 1 386 ? 8.706   32.631 21.755  1.00 28.21  ?  386 ARG A CB  1 
ATOM   2683 C  CG  . ARG A 1 386 ? 7.559   33.330 22.489  1.00 29.48  ?  386 ARG A CG  1 
ATOM   2684 C  CD  . ARG A 1 386 ? 7.705   33.177 23.989  1.00 26.85  ?  386 ARG A CD  1 
ATOM   2685 N  NE  . ARG A 1 386 ? 6.560   33.634 24.744  1.00 26.31  ?  386 ARG A NE  1 
ATOM   2686 C  CZ  . ARG A 1 386 ? 6.335   34.885 25.126  1.00 27.37  ?  386 ARG A CZ  1 
ATOM   2687 N  NH1 . ARG A 1 386 ? 7.152   35.875 24.787  1.00 25.94  ?  386 ARG A NH1 1 
ATOM   2688 N  NH2 . ARG A 1 386 ? 5.266   35.148 25.862  1.00 28.19  ?  386 ARG A NH2 1 
ATOM   2689 N  N   . LEU A 1 387 ? 7.593   31.671 18.987  1.00 29.19  ?  387 LEU A N   1 
ATOM   2690 C  CA  . LEU A 1 387 ? 6.366   31.288 18.240  1.00 26.67  ?  387 LEU A CA  1 
ATOM   2691 C  C   . LEU A 1 387 ? 5.188   31.397 19.194  1.00 26.58  ?  387 LEU A C   1 
ATOM   2692 O  O   . LEU A 1 387 ? 5.371   31.194 20.379  1.00 31.55  ?  387 LEU A O   1 
ATOM   2693 C  CB  . LEU A 1 387 ? 6.479   29.875 17.681  1.00 26.35  ?  387 LEU A CB  1 
ATOM   2694 C  CG  . LEU A 1 387 ? 7.511   29.690 16.575  1.00 30.63  ?  387 LEU A CG  1 
ATOM   2695 C  CD1 . LEU A 1 387 ? 7.467   28.274 16.018  1.00 33.20  ?  387 LEU A CD1 1 
ATOM   2696 C  CD2 . LEU A 1 387 ? 7.322   30.693 15.450  1.00 29.12  ?  387 LEU A CD2 1 
ATOM   2697 N  N   . ALA A 1 388 ? 4.029   31.774 18.686  1.00 26.99  ?  388 ALA A N   1 
ATOM   2698 C  CA  . ALA A 1 388 ? 2.771   31.802 19.454  1.00 25.58  ?  388 ALA A CA  1 
ATOM   2699 C  C   . ALA A 1 388 ? 2.224   30.393 19.636  1.00 25.15  ?  388 ALA A C   1 
ATOM   2700 O  O   . ALA A 1 388 ? 1.230   30.257 20.368  1.00 26.57  ?  388 ALA A O   1 
ATOM   2701 C  CB  . ALA A 1 388 ? 1.768   32.667 18.744  1.00 24.49  ?  388 ALA A CB  1 
ATOM   2702 N  N   . LEU A 1 389 ? 2.785   29.390 18.960  1.00 25.24  ?  389 LEU A N   1 
ATOM   2703 C  CA  . LEU A 1 389 ? 2.293   28.000 19.116  1.00 27.52  ?  389 LEU A CA  1 
ATOM   2704 C  C   . LEU A 1 389 ? 3.379   27.011 18.728  1.00 28.64  ?  389 LEU A C   1 
ATOM   2705 O  O   . LEU A 1 389 ? 4.453   27.412 18.307  1.00 29.66  ?  389 LEU A O   1 
ATOM   2706 C  CB  . LEU A 1 389 ? 1.016   27.852 18.282  1.00 28.77  ?  389 LEU A CB  1 
ATOM   2707 C  CG  . LEU A 1 389 ? 0.344   26.487 18.215  1.00 27.65  ?  389 LEU A CG  1 
ATOM   2708 C  CD1 . LEU A 1 389 ? -0.126  26.075 19.605  1.00 29.13  ?  389 LEU A CD1 1 
ATOM   2709 C  CD2 . LEU A 1 389 ? -0.837  26.509 17.262  1.00 30.25  ?  389 LEU A CD2 1 
ATOM   2710 N  N   . PRO A 1 390 ? 3.180   25.682 18.875  1.00 30.90  ?  390 PRO A N   1 
ATOM   2711 C  CA  . PRO A 1 390 ? 4.245   24.751 18.517  1.00 30.78  ?  390 PRO A CA  1 
ATOM   2712 C  C   . PRO A 1 390 ? 4.496   24.903 17.005  1.00 30.52  ?  390 PRO A C   1 
ATOM   2713 O  O   . PRO A 1 390 ? 3.525   25.055 16.236  1.00 34.72  ?  390 PRO A O   1 
ATOM   2714 C  CB  . PRO A 1 390 ? 3.717   23.383 18.983  1.00 33.14  ?  390 PRO A CB  1 
ATOM   2715 C  CG  . PRO A 1 390 ? 2.558   23.706 19.925  1.00 31.88  ?  390 PRO A CG  1 
ATOM   2716 C  CD  . PRO A 1 390 ? 1.980   25.003 19.386  1.00 32.07  ?  390 PRO A CD  1 
ATOM   2717 N  N   . VAL A 1 391 ? 5.773   24.920 16.616  1.00 27.15  ?  391 VAL A N   1 
ATOM   2718 C  CA  . VAL A 1 391 ? 6.264   25.016 15.211  1.00 27.67  ?  391 VAL A CA  1 
ATOM   2719 C  C   . VAL A 1 391 ? 5.642   23.888 14.360  1.00 29.16  ?  391 VAL A C   1 
ATOM   2720 O  O   . VAL A 1 391 ? 5.428   24.109 13.131  1.00 27.15  ?  391 VAL A O   1 
ATOM   2721 C  CB  . VAL A 1 391 ? 7.809   25.014 15.162  1.00 30.31  ?  391 VAL A CB  1 
ATOM   2722 C  CG1 . VAL A 1 391 ? 8.418   23.683 15.611  1.00 32.46  ?  391 VAL A CG1 1 
ATOM   2723 C  CG2 . VAL A 1 391 ? 8.310   25.362 13.766  1.00 32.50  ?  391 VAL A CG2 1 
ATOM   2724 N  N   . GLU A 1 392 ? 5.343   22.730 14.965  1.00 31.09  ?  392 GLU A N   1 
ATOM   2725 C  CA  . GLU A 1 392 ? 4.684   21.580 14.282  1.00 31.58  ?  392 GLU A CA  1 
ATOM   2726 C  C   . GLU A 1 392 ? 3.344   22.020 13.704  1.00 29.73  ?  392 GLU A C   1 
ATOM   2727 O  O   . GLU A 1 392 ? 2.926   21.450 12.719  1.00 30.91  ?  392 GLU A O   1 
ATOM   2728 C  CB  . GLU A 1 392 ? 4.378   20.416 15.225  1.00 36.23  ?  392 GLU A CB  1 
ATOM   2729 C  CG  . GLU A 1 392 ? 5.605   19.731 15.773  1.00 42.66  ?  392 GLU A CG  1 
ATOM   2730 C  CD  . GLU A 1 392 ? 6.382   20.533 16.804  1.00 47.40  ?  392 GLU A CD  1 
ATOM   2731 O  OE1 . GLU A 1 392 ? 5.780   21.451 17.395  1.00 41.63  ?  392 GLU A OE1 1 
ATOM   2732 O  OE2 . GLU A 1 392 ? 7.588   20.229 17.009  1.00 52.49  ?  392 GLU A OE2 1 
ATOM   2733 N  N   . GLN A 1 393 ? 2.685   23.011 14.293  1.00 31.11  ?  393 GLN A N   1 
ATOM   2734 C  CA  . GLN A 1 393 ? 1.312   23.410 13.869  1.00 29.48  ?  393 GLN A CA  1 
ATOM   2735 C  C   . GLN A 1 393 ? 1.312   24.649 12.961  1.00 29.22  ?  393 GLN A C   1 
ATOM   2736 O  O   . GLN A 1 393 ? 0.243   25.229 12.777  1.00 25.38  ?  393 GLN A O   1 
ATOM   2737 C  CB  . GLN A 1 393 ? 0.476   23.628 15.120  1.00 28.41  ?  393 GLN A CB  1 
ATOM   2738 C  CG  . GLN A 1 393 ? 0.105   22.311 15.782  1.00 27.49  ?  393 GLN A CG  1 
ATOM   2739 C  CD  . GLN A 1 393 ? -0.388  22.611 17.169  1.00 29.80  ?  393 GLN A CD  1 
ATOM   2740 O  OE1 . GLN A 1 393 ? 0.285   22.320 18.156  1.00 32.38  ?  393 GLN A OE1 1 
ATOM   2741 N  NE2 . GLN A 1 393 ? -1.530  23.286 17.241  1.00 32.95  ?  393 GLN A NE2 1 
ATOM   2742 N  N   . LEU A 1 394 ? 2.450   25.040 12.380  1.00 30.75  ?  394 LEU A N   1 
ATOM   2743 C  CA  . LEU A 1 394 ? 2.471   26.117 11.359  1.00 30.42  ?  394 LEU A CA  1 
ATOM   2744 C  C   . LEU A 1 394 ? 1.885   25.532 10.071  1.00 30.39  ?  394 LEU A C   1 
ATOM   2745 O  O   . LEU A 1 394 ? 2.118   24.324 9.841   1.00 34.82  ?  394 LEU A O   1 
ATOM   2746 C  CB  . LEU A 1 394 ? 3.894   26.623 11.111  1.00 30.46  ?  394 LEU A CB  1 
ATOM   2747 C  CG  . LEU A 1 394 ? 4.536   27.453 12.214  1.00 31.29  ?  394 LEU A CG  1 
ATOM   2748 C  CD1 . LEU A 1 394 ? 6.011   27.702 11.893  1.00 33.82  ?  394 LEU A CD1 1 
ATOM   2749 C  CD2 . LEU A 1 394 ? 3.805   28.768 12.443  1.00 29.89  ?  394 LEU A CD2 1 
ATOM   2750 N  N   . ALA A 1 395 ? 1.140   26.347 9.310   1.00 28.34  ?  395 ALA A N   1 
ATOM   2751 C  CA  . ALA A 1 395 ? 0.611   26.037 7.966   1.00 28.16  ?  395 ALA A CA  1 
ATOM   2752 C  C   . ALA A 1 395 ? 1.711   26.271 6.932   1.00 28.97  ?  395 ALA A C   1 
ATOM   2753 O  O   . ALA A 1 395 ? 2.059   27.443 6.673   1.00 29.34  ?  395 ALA A O   1 
ATOM   2754 C  CB  . ALA A 1 395 ? -0.589  26.893 7.663   1.00 28.62  ?  395 ALA A CB  1 
ATOM   2755 N  N   . TRP A 1 396 ? 2.234   25.196 6.360   1.00 28.28  ?  396 TRP A N   1 
ATOM   2756 C  CA  . TRP A 1 396 ? 3.256   25.264 5.292   1.00 30.90  ?  396 TRP A CA  1 
ATOM   2757 C  C   . TRP A 1 396 ? 2.560   25.321 3.925   1.00 31.27  ?  396 TRP A C   1 
ATOM   2758 O  O   . TRP A 1 396 ? 1.710   24.458 3.633   1.00 32.06  ?  396 TRP A O   1 
ATOM   2759 C  CB  . TRP A 1 396 ? 4.251   24.106 5.445   1.00 33.74  ?  396 TRP A CB  1 
ATOM   2760 C  CG  . TRP A 1 396 ? 5.147   24.313 6.631   1.00 31.85  ?  396 TRP A CG  1 
ATOM   2761 C  CD1 . TRP A 1 396 ? 4.983   23.823 7.888   1.00 29.74  ?  396 TRP A CD1 1 
ATOM   2762 C  CD2 . TRP A 1 396 ? 6.314   25.154 6.680   1.00 31.25  ?  396 TRP A CD2 1 
ATOM   2763 N  NE1 . TRP A 1 396 ? 5.983   24.281 8.708   1.00 29.88  ?  396 TRP A NE1 1 
ATOM   2764 C  CE2 . TRP A 1 396 ? 6.815   25.093 7.997   1.00 29.66  ?  396 TRP A CE2 1 
ATOM   2765 C  CE3 . TRP A 1 396 ? 6.964   25.959 5.743   1.00 29.90  ?  396 TRP A CE3 1 
ATOM   2766 C  CZ2 . TRP A 1 396 ? 7.959   25.774 8.395   1.00 31.85  ?  396 TRP A CZ2 1 
ATOM   2767 C  CZ3 . TRP A 1 396 ? 8.096   26.632 6.135   1.00 31.31  ?  396 TRP A CZ3 1 
ATOM   2768 C  CH2 . TRP A 1 396 ? 8.581   26.548 7.443   1.00 34.09  ?  396 TRP A CH2 1 
ATOM   2769 N  N   . ARG A 1 397 ? 2.867   26.378 3.171   1.00 31.23  ?  397 ARG A N   1 
ATOM   2770 C  CA  . ARG A 1 397 ? 2.250   26.699 1.873   1.00 30.48  ?  397 ARG A CA  1 
ATOM   2771 C  C   . ARG A 1 397 ? 2.598   25.617 0.867   1.00 30.45  ?  397 ARG A C   1 
ATOM   2772 O  O   . ARG A 1 397 ? 3.775   25.241 0.678   1.00 24.38  ?  397 ARG A O   1 
ATOM   2773 C  CB  . ARG A 1 397 ? 2.700   28.039 1.288   1.00 31.89  ?  397 ARG A CB  1 
ATOM   2774 C  CG  . ARG A 1 397 ? 2.065   28.299 -0.066  1.00 29.21  ?  397 ARG A CG  1 
ATOM   2775 C  CD  . ARG A 1 397 ? 2.511   29.613 -0.637  1.00 31.87  ?  397 ARG A CD  1 
ATOM   2776 N  NE  . ARG A 1 397 ? 1.919   30.739 0.049   1.00 32.82  ?  397 ARG A NE  1 
ATOM   2777 C  CZ  . ARG A 1 397 ? 2.096   31.995 -0.313  1.00 34.05  ?  397 ARG A CZ  1 
ATOM   2778 N  NH1 . ARG A 1 397 ? 2.862   32.284 -1.355  1.00 35.67  ?  397 ARG A NH1 1 
ATOM   2779 N  NH2 . ARG A 1 397 ? 1.556   32.958 0.409   1.00 32.64  ?  397 ARG A NH2 1 
ATOM   2780 N  N   . PRO A 1 398 ? 1.523   25.095 0.235   1.00 29.64  ?  398 PRO A N   1 
ATOM   2781 C  CA  . PRO A 1 398 ? 1.656   24.045 -0.764  1.00 28.04  ?  398 PRO A CA  1 
ATOM   2782 C  C   . PRO A 1 398 ? 1.841   24.678 -2.145  1.00 27.33  ?  398 PRO A C   1 
ATOM   2783 O  O   . PRO A 1 398 ? 1.566   25.852 -2.280  1.00 29.03  ?  398 PRO A O   1 
ATOM   2784 C  CB  . PRO A 1 398 ? 0.335   23.295 -0.581  1.00 26.15  ?  398 PRO A CB  1 
ATOM   2785 C  CG  . PRO A 1 398 ? -0.678  24.393 -0.223  1.00 27.36  ?  398 PRO A CG  1 
ATOM   2786 C  CD  . PRO A 1 398 ? 0.111   25.436 0.536   1.00 27.54  ?  398 PRO A CD  1 
ATOM   2787 N  N   . GLY A 1 399 ? 2.343   23.893 -3.099  1.00 26.83  ?  399 GLY A N   1 
ATOM   2788 C  CA  . GLY A 1 399 ? 2.362   24.215 -4.538  1.00 25.69  ?  399 GLY A CA  1 
ATOM   2789 C  C   . GLY A 1 399 ? 3.040   25.537 -4.847  1.00 29.67  ?  399 GLY A C   1 
ATOM   2790 O  O   . GLY A 1 399 ? 2.618   26.197 -5.839  1.00 32.02  ?  399 GLY A O   1 
ATOM   2791 N  N   . PHE A 1 400 ? 4.097   25.899 -4.106  1.00 28.98  ?  400 PHE A N   1 
ATOM   2792 C  CA  . PHE A 1 400 ? 4.885   27.133 -4.349  1.00 29.76  ?  400 PHE A CA  1 
ATOM   2793 C  C   . PHE A 1 400 ? 6.377   26.796 -4.509  1.00 28.70  ?  400 PHE A C   1 
ATOM   2794 O  O   . PHE A 1 400 ? 6.827   25.810 -3.951  1.00 26.86  ?  400 PHE A O   1 
ATOM   2795 C  CB  . PHE A 1 400 ? 4.594   28.086 -3.193  1.00 31.58  ?  400 PHE A CB  1 
ATOM   2796 C  CG  . PHE A 1 400 ? 4.761   29.547 -3.496  1.00 29.24  ?  400 PHE A CG  1 
ATOM   2797 C  CD1 . PHE A 1 400 ? 3.950   30.165 -4.432  1.00 28.97  ?  400 PHE A CD1 1 
ATOM   2798 C  CD2 . PHE A 1 400 ? 5.718   30.293 -2.825  1.00 28.23  ?  400 PHE A CD2 1 
ATOM   2799 C  CE1 . PHE A 1 400 ? 4.105   31.517 -4.699  1.00 28.24  ?  400 PHE A CE1 1 
ATOM   2800 C  CE2 . PHE A 1 400 ? 5.868   31.644 -3.084  1.00 28.85  ?  400 PHE A CE2 1 
ATOM   2801 C  CZ  . PHE A 1 400 ? 5.058   32.247 -4.024  1.00 31.47  ?  400 PHE A CZ  1 
ATOM   2802 N  N   . ILE A 1 401 ? 7.140   27.647 -5.201  1.00 33.80  ?  401 ILE A N   1 
ATOM   2803 C  CA  . ILE A 1 401 ? 8.614   27.480 -5.426  1.00 36.60  ?  401 ILE A CA  1 
ATOM   2804 C  C   . ILE A 1 401 ? 9.358   27.586 -4.090  1.00 36.09  ?  401 ILE A C   1 
ATOM   2805 O  O   . ILE A 1 401 ? 10.368  26.894 -3.909  1.00 34.76  ?  401 ILE A O   1 
ATOM   2806 C  CB  . ILE A 1 401 ? 9.112   28.496 -6.462  1.00 40.34  ?  401 ILE A CB  1 
ATOM   2807 C  CG1 . ILE A 1 401 ? 8.759   27.998 -7.861  1.00 48.92  ?  401 ILE A CG1 1 
ATOM   2808 C  CG2 . ILE A 1 401 ? 10.595  28.755 -6.345  1.00 43.73  ?  401 ILE A CG2 1 
ATOM   2809 C  CD1 . ILE A 1 401 ? 8.721   29.078 -8.915  1.00 57.68  ?  401 ILE A CD1 1 
ATOM   2810 N  N   . LYS A 1 402 ? 8.812   28.370 -3.165  1.00 33.00  ?  402 LYS A N   1 
ATOM   2811 C  CA  . LYS A 1 402 ? 9.347   28.540 -1.805  1.00 30.02  ?  402 LYS A CA  1 
ATOM   2812 C  C   . LYS A 1 402 ? 8.553   27.666 -0.829  1.00 31.34  ?  402 LYS A C   1 
ATOM   2813 O  O   . LYS A 1 402 ? 7.346   27.544 -1.016  1.00 33.12  ?  402 LYS A O   1 
ATOM   2814 C  CB  . LYS A 1 402 ? 9.277   30.029 -1.448  1.00 30.14  ?  402 LYS A CB  1 
ATOM   2815 C  CG  . LYS A 1 402 ? 10.047  30.975 -2.357  1.00 30.97  ?  402 LYS A CG  1 
ATOM   2816 C  CD  . LYS A 1 402 ? 11.519  30.595 -2.568  1.00 32.82  ?  402 LYS A CD  1 
ATOM   2817 C  CE  . LYS A 1 402 ? 12.170  31.454 -3.628  1.00 36.76  ?  402 LYS A CE  1 
ATOM   2818 N  NZ  . LYS A 1 402 ? 13.639  31.556 -3.436  1.00 43.32  ?  402 LYS A NZ  1 
ATOM   2819 N  N   . ARG A 1 403 ? 9.232   27.057 0.147   1.00 32.17  ?  403 ARG A N   1 
ATOM   2820 C  CA  . ARG A 1 403 ? 8.648   26.599 1.434   1.00 33.31  ?  403 ARG A CA  1 
ATOM   2821 C  C   . ARG A 1 403 ? 8.502   27.813 2.336   1.00 33.52  ?  403 ARG A C   1 
ATOM   2822 O  O   . ARG A 1 403 ? 9.528   28.512 2.574   1.00 34.45  ?  403 ARG A O   1 
ATOM   2823 C  CB  . ARG A 1 403 ? 9.574   25.648 2.201   1.00 34.65  ?  403 ARG A CB  1 
ATOM   2824 C  CG  . ARG A 1 403 ? 9.778   24.290 1.548   1.00 32.71  ?  403 ARG A CG  1 
ATOM   2825 C  CD  . ARG A 1 403 ? 10.221  23.287 2.573   1.00 32.86  ?  403 ARG A CD  1 
ATOM   2826 N  NE  . ARG A 1 403 ? 10.529  22.010 1.958   1.00 34.73  ?  403 ARG A NE  1 
ATOM   2827 C  CZ  . ARG A 1 403 ? 11.706  21.683 1.457   1.00 35.58  ?  403 ARG A CZ  1 
ATOM   2828 N  NH1 . ARG A 1 403 ? 12.713  22.541 1.527   1.00 33.65  ?  403 ARG A NH1 1 
ATOM   2829 N  NH2 . ARG A 1 403 ? 11.864  20.485 0.916   1.00 37.98  ?  403 ARG A NH2 1 
ATOM   2830 N  N   . LEU A 1 404 ? 7.303   28.064 2.834   1.00 32.47  ?  404 LEU A N   1 
ATOM   2831 C  CA  . LEU A 1 404 ? 7.103   29.191 3.777   1.00 33.99  ?  404 LEU A CA  1 
ATOM   2832 C  C   . LEU A 1 404 ? 5.839   28.977 4.594   1.00 33.42  ?  404 LEU A C   1 
ATOM   2833 O  O   . LEU A 1 404 ? 4.912   28.304 4.153   1.00 35.16  ?  404 LEU A O   1 
ATOM   2834 C  CB  . LEU A 1 404 ? 7.082   30.513 2.997   1.00 36.60  ?  404 LEU A CB  1 
ATOM   2835 C  CG  . LEU A 1 404 ? 5.909   30.749 2.054   1.00 34.97  ?  404 LEU A CG  1 
ATOM   2836 C  CD1 . LEU A 1 404 ? 4.851   31.643 2.700   1.00 33.37  ?  404 LEU A CD1 1 
ATOM   2837 C  CD2 . LEU A 1 404 ? 6.415   31.354 0.760   1.00 34.81  ?  404 LEU A CD2 1 
ATOM   2838 N  N   . PRO A 1 405 ? 5.813   29.493 5.837   1.00 33.07  ?  405 PRO A N   1 
ATOM   2839 C  CA  . PRO A 1 405 ? 4.613   29.450 6.666   1.00 32.58  ?  405 PRO A CA  1 
ATOM   2840 C  C   . PRO A 1 405 ? 3.579   30.441 6.126   1.00 31.52  ?  405 PRO A C   1 
ATOM   2841 O  O   . PRO A 1 405 ? 3.939   31.569 5.928   1.00 28.63  ?  405 PRO A O   1 
ATOM   2842 C  CB  . PRO A 1 405 ? 5.105   29.856 8.053   1.00 35.79  ?  405 PRO A CB  1 
ATOM   2843 C  CG  . PRO A 1 405 ? 6.369   30.656 7.807   1.00 37.60  ?  405 PRO A CG  1 
ATOM   2844 C  CD  . PRO A 1 405 ? 6.950   30.132 6.510   1.00 35.37  ?  405 PRO A CD  1 
ATOM   2845 N  N   . GLU A 1 406 ? 2.354   29.982 5.856   1.00 29.28  ?  406 GLU A N   1 
ATOM   2846 C  CA  . GLU A 1 406 ? 1.267   30.848 5.348   1.00 28.38  ?  406 GLU A CA  1 
ATOM   2847 C  C   . GLU A 1 406 ? 1.132   32.013 6.321   1.00 29.96  ?  406 GLU A C   1 
ATOM   2848 O  O   . GLU A 1 406 ? 0.987   33.143 5.846   1.00 30.55  ?  406 GLU A O   1 
ATOM   2849 C  CB  . GLU A 1 406 ? -0.044  30.081 5.238   1.00 29.38  ?  406 GLU A CB  1 
ATOM   2850 C  CG  . GLU A 1 406 ? 0.002   28.893 4.266   1.00 28.32  ?  406 GLU A CG  1 
ATOM   2851 C  CD  . GLU A 1 406 ? -0.152  29.269 2.802   1.00 29.64  ?  406 GLU A CD  1 
ATOM   2852 O  OE1 . GLU A 1 406 ? 0.178   30.450 2.462   1.00 29.79  ?  406 GLU A OE1 1 
ATOM   2853 O  OE2 . GLU A 1 406 ? -0.575  28.386 1.980   1.00 28.45  ?  406 GLU A OE2 1 
ATOM   2854 N  N   . ARG A 1 407 ? 1.245   31.735 7.630   1.00 30.03  ?  407 ARG A N   1 
ATOM   2855 C  CA  . ARG A 1 407 ? 1.300   32.761 8.707   1.00 29.30  ?  407 ARG A CA  1 
ATOM   2856 C  C   . ARG A 1 407 ? 2.448   32.460 9.670   1.00 29.38  ?  407 ARG A C   1 
ATOM   2857 O  O   . ARG A 1 407 ? 2.787   31.280 9.873   1.00 29.45  ?  407 ARG A O   1 
ATOM   2858 C  CB  . ARG A 1 407 ? -0.024  32.824 9.466   1.00 28.49  ?  407 ARG A CB  1 
ATOM   2859 C  CG  . ARG A 1 407 ? -1.178  33.314 8.612   1.00 29.49  ?  407 ARG A CG  1 
ATOM   2860 C  CD  . ARG A 1 407 ? -2.479  32.762 9.136   1.00 29.73  ?  407 ARG A CD  1 
ATOM   2861 N  NE  . ARG A 1 407 ? -2.548  31.313 8.944   1.00 30.23  ?  407 ARG A NE  1 
ATOM   2862 C  CZ  . ARG A 1 407 ? -2.898  30.720 7.812   1.00 30.61  ?  407 ARG A CZ  1 
ATOM   2863 N  NH1 . ARG A 1 407 ? -3.170  31.447 6.748   1.00 30.55  ?  407 ARG A NH1 1 
ATOM   2864 N  NH2 . ARG A 1 407 ? -2.941  29.403 7.730   1.00 31.82  ?  407 ARG A NH2 1 
ATOM   2865 N  N   . LEU A 1 408 ? 3.016   33.499 10.268  1.00 27.96  ?  408 LEU A N   1 
ATOM   2866 C  CA  . LEU A 1 408 ? 4.160   33.333 11.191  1.00 29.03  ?  408 LEU A CA  1 
ATOM   2867 C  C   . LEU A 1 408 ? 3.826   34.039 12.491  1.00 28.69  ?  408 LEU A C   1 
ATOM   2868 O  O   . LEU A 1 408 ? 4.327   35.127 12.755  1.00 31.85  ?  408 LEU A O   1 
ATOM   2869 C  CB  . LEU A 1 408 ? 5.399   33.904 10.510  1.00 28.73  ?  408 LEU A CB  1 
ATOM   2870 C  CG  . LEU A 1 408 ? 6.700   33.761 11.284  1.00 31.14  ?  408 LEU A CG  1 
ATOM   2871 C  CD1 . LEU A 1 408 ? 6.755   32.464 12.058  1.00 32.45  ?  408 LEU A CD1 1 
ATOM   2872 C  CD2 . LEU A 1 408 ? 7.895   33.853 10.340  1.00 33.04  ?  408 LEU A CD2 1 
ATOM   2873 N  N   . PRO A 1 409 ? 2.897   33.457 13.285  1.00 28.93  ?  409 PRO A N   1 
ATOM   2874 C  CA  . PRO A 1 409 ? 2.371   34.098 14.488  1.00 27.25  ?  409 PRO A CA  1 
ATOM   2875 C  C   . PRO A 1 409 ? 3.385   34.045 15.624  1.00 26.22  ?  409 PRO A C   1 
ATOM   2876 O  O   . PRO A 1 409 ? 3.856   32.957 15.875  1.00 26.70  ?  409 PRO A O   1 
ATOM   2877 C  CB  . PRO A 1 409 ? 1.097   33.315 14.851  1.00 27.07  ?  409 PRO A CB  1 
ATOM   2878 C  CG  . PRO A 1 409 ? 1.169   32.021 14.097  1.00 28.29  ?  409 PRO A CG  1 
ATOM   2879 C  CD  . PRO A 1 409 ? 2.243   32.163 13.024  1.00 30.03  ?  409 PRO A CD  1 
ATOM   2880 N  N   . VAL A 1 410 ? 3.707   35.195 16.226  1.00 23.90  ?  410 VAL A N   1 
ATOM   2881 C  CA  . VAL A 1 410 ? 4.765   35.280 17.267  1.00 26.75  ?  410 VAL A CA  1 
ATOM   2882 C  C   . VAL A 1 410 ? 4.260   36.076 18.468  1.00 28.18  ?  410 VAL A C   1 
ATOM   2883 O  O   . VAL A 1 410 ? 3.266   36.815 18.329  1.00 34.58  ?  410 VAL A O   1 
ATOM   2884 C  CB  . VAL A 1 410 ? 6.072   35.894 16.729  1.00 27.55  ?  410 VAL A CB  1 
ATOM   2885 C  CG1 . VAL A 1 410 ? 6.562   35.190 15.489  1.00 28.72  ?  410 VAL A CG1 1 
ATOM   2886 C  CG2 . VAL A 1 410 ? 5.949   37.382 16.489  1.00 27.96  ?  410 VAL A CG2 1 
ATOM   2887 N  N   . LEU A 1 411 ? 4.954   35.904 19.593  1.00 27.69  ?  411 LEU A N   1 
ATOM   2888 C  CA  . LEU A 1 411 ? 4.743   36.589 20.884  1.00 28.29  ?  411 LEU A CA  1 
ATOM   2889 C  C   . LEU A 1 411 ? 6.087   37.229 21.243  1.00 28.13  ?  411 LEU A C   1 
ATOM   2890 O  O   . LEU A 1 411 ? 7.068   36.771 20.654  1.00 24.01  ?  411 LEU A O   1 
ATOM   2891 C  CB  . LEU A 1 411 ? 4.316   35.560 21.940  1.00 30.48  ?  411 LEU A CB  1 
ATOM   2892 C  CG  . LEU A 1 411 ? 3.045   34.773 21.647  1.00 33.72  ?  411 LEU A CG  1 
ATOM   2893 C  CD1 . LEU A 1 411 ? 2.788   33.753 22.750  1.00 35.83  ?  411 LEU A CD1 1 
ATOM   2894 C  CD2 . LEU A 1 411 ? 1.840   35.706 21.487  1.00 36.94  ?  411 LEU A CD2 1 
ATOM   2895 N  N   . TRP A 1 412 ? 6.103   38.224 22.151  1.00 29.99  ?  412 TRP A N   1 
ATOM   2896 C  CA  . TRP A 1 412 ? 7.313   38.966 22.603  1.00 36.47  ?  412 TRP A CA  1 
ATOM   2897 C  C   . TRP A 1 412 ? 7.054   39.741 23.911  1.00 32.28  ?  412 TRP A C   1 
ATOM   2898 O  O   . TRP A 1 412 ? 5.860   39.981 24.046  1.00 31.73  ?  412 TRP A O   1 
ATOM   2899 C  CB  . TRP A 1 412 ? 7.783   39.906 21.474  1.00 39.14  ?  412 TRP A CB  1 
ATOM   2900 C  CG  . TRP A 1 412 ? 6.845   41.026 21.155  1.00 34.89  ?  412 TRP A CG  1 
ATOM   2901 C  CD1 . TRP A 1 412 ? 6.740   42.221 21.800  1.00 36.27  ?  412 TRP A CD1 1 
ATOM   2902 C  CD2 . TRP A 1 412 ? 5.875   41.054 20.089  1.00 35.35  ?  412 TRP A CD2 1 
ATOM   2903 N  NE1 . TRP A 1 412 ? 5.735   42.975 21.238  1.00 37.08  ?  412 TRP A NE1 1 
ATOM   2904 C  CE2 . TRP A 1 412 ? 5.196   42.288 20.180  1.00 34.82  ?  412 TRP A CE2 1 
ATOM   2905 C  CE3 . TRP A 1 412 ? 5.494   40.145 19.098  1.00 33.26  ?  412 TRP A CE3 1 
ATOM   2906 C  CZ2 . TRP A 1 412 ? 4.191   42.649 19.289  1.00 34.03  ?  412 TRP A CZ2 1 
ATOM   2907 C  CZ3 . TRP A 1 412 ? 4.509   40.511 18.208  1.00 36.82  ?  412 TRP A CZ3 1 
ATOM   2908 C  CH2 . TRP A 1 412 ? 3.862   41.745 18.309  1.00 34.84  ?  412 TRP A CH2 1 
ATOM   2909 N  N   . PRO B 1 19  ? -8.803  0.164  15.057  1.00 77.87  ?  19  PRO B N   1 
ATOM   2910 C  CA  . PRO B 1 19  ? -8.341  1.430  14.444  1.00 79.15  ?  19  PRO B CA  1 
ATOM   2911 C  C   . PRO B 1 19  ? -9.453  2.478  14.216  1.00 67.51  ?  19  PRO B C   1 
ATOM   2912 O  O   . PRO B 1 19  ? -10.087 2.455  13.173  1.00 63.58  ?  19  PRO B O   1 
ATOM   2913 C  CB  . PRO B 1 19  ? -7.762  0.938  13.106  1.00 78.25  ?  19  PRO B CB  1 
ATOM   2914 C  CG  . PRO B 1 19  ? -8.668  -0.236 12.714  1.00 81.80  ?  19  PRO B CG  1 
ATOM   2915 C  CD  . PRO B 1 19  ? -9.278  -0.755 14.005  1.00 79.74  ?  19  PRO B CD  1 
ATOM   2916 N  N   . LEU B 1 20  ? -9.687  3.367  15.187  1.00 57.11  ?  20  LEU B N   1 
ATOM   2917 C  CA  . LEU B 1 20  ? -10.775 4.392  15.117  1.00 55.82  ?  20  LEU B CA  1 
ATOM   2918 C  C   . LEU B 1 20  ? -10.509 5.307  13.931  1.00 48.58  ?  20  LEU B C   1 
ATOM   2919 O  O   . LEU B 1 20  ? -9.392  5.793  13.827  1.00 52.65  ?  20  LEU B O   1 
ATOM   2920 C  CB  . LEU B 1 20  ? -10.806 5.253  16.388  1.00 50.66  ?  20  LEU B CB  1 
ATOM   2921 C  CG  . LEU B 1 20  ? -11.164 4.537  17.686  1.00 47.63  ?  20  LEU B CG  1 
ATOM   2922 C  CD1 . LEU B 1 20  ? -11.375 5.549  18.806  1.00 42.86  ?  20  LEU B CD1 1 
ATOM   2923 C  CD2 . LEU B 1 20  ? -12.396 3.649  17.497  1.00 48.38  ?  20  LEU B CD2 1 
ATOM   2924 N  N   . PRO B 1 21  ? -11.505 5.627  13.067  1.00 45.60  ?  21  PRO B N   1 
ATOM   2925 C  CA  . PRO B 1 21  ? -11.367 6.708  12.091  1.00 43.14  ?  21  PRO B CA  1 
ATOM   2926 C  C   . PRO B 1 21  ? -10.913 8.011  12.765  1.00 41.06  ?  21  PRO B C   1 
ATOM   2927 O  O   . PRO B 1 21  ? -11.310 8.259  13.887  1.00 44.64  ?  21  PRO B O   1 
ATOM   2928 C  CB  . PRO B 1 21  ? -12.759 6.867  11.472  1.00 38.92  ?  21  PRO B CB  1 
ATOM   2929 C  CG  . PRO B 1 21  ? -13.686 6.069  12.344  1.00 40.99  ?  21  PRO B CG  1 
ATOM   2930 C  CD  . PRO B 1 21  ? -12.828 4.997  12.979  1.00 46.75  ?  21  PRO B CD  1 
ATOM   2931 N  N   . ASP B 1 22  ? -10.047 8.769  12.097  1.00 42.03  ?  22  ASP B N   1 
ATOM   2932 C  CA  . ASP B 1 22  ? -9.438  10.006 12.659  1.00 45.87  ?  22  ASP B CA  1 
ATOM   2933 C  C   . ASP B 1 22  ? -10.351 11.173 12.358  1.00 40.22  ?  22  ASP B C   1 
ATOM   2934 O  O   . ASP B 1 22  ? -10.843 11.251 11.251  1.00 40.52  ?  22  ASP B O   1 
ATOM   2935 C  CB  . ASP B 1 22  ? -8.035  10.319 12.124  1.00 47.73  ?  22  ASP B CB  1 
ATOM   2936 C  CG  . ASP B 1 22  ? -6.968  9.502  12.838  1.00 53.14  ?  22  ASP B CG  1 
ATOM   2937 O  OD1 . ASP B 1 22  ? -6.758  9.703  14.079  1.00 55.19  ?  22  ASP B OD1 1 
ATOM   2938 O  OD2 . ASP B 1 22  ? -6.406  8.628  12.177  1.00 55.80  ?  22  ASP B OD2 1 
ATOM   2939 N  N   . PHE B 1 23  ? -10.525 12.040 13.336  1.00 39.60  ?  23  PHE B N   1 
ATOM   2940 C  CA  . PHE B 1 23  ? -11.250 13.320 13.204  1.00 37.92  ?  23  PHE B CA  1 
ATOM   2941 C  C   . PHE B 1 23  ? -10.252 14.435 13.518  1.00 36.74  ?  23  PHE B C   1 
ATOM   2942 O  O   . PHE B 1 23  ? -9.494  14.320 14.478  1.00 39.06  ?  23  PHE B O   1 
ATOM   2943 C  CB  . PHE B 1 23  ? -12.486 13.287 14.114  1.00 35.86  ?  23  PHE B CB  1 
ATOM   2944 C  CG  . PHE B 1 23  ? -13.492 14.325 13.720  1.00 35.05  ?  23  PHE B CG  1 
ATOM   2945 C  CD1 . PHE B 1 23  ? -14.285 14.138 12.610  1.00 35.36  ?  23  PHE B CD1 1 
ATOM   2946 C  CD2 . PHE B 1 23  ? -13.555 15.536 14.388  1.00 39.39  ?  23  PHE B CD2 1 
ATOM   2947 C  CE1 . PHE B 1 23  ? -15.142 15.134 12.178  1.00 36.63  ?  23  PHE B CE1 1 
ATOM   2948 C  CE2 . PHE B 1 23  ? -14.431 16.526 13.976  1.00 39.25  ?  23  PHE B CE2 1 
ATOM   2949 C  CZ  . PHE B 1 23  ? -15.212 16.326 12.863  1.00 41.11  ?  23  PHE B CZ  1 
ATOM   2950 N  N   . PRO B 1 24  ? -10.238 15.582 12.795  1.00 36.59  ?  24  PRO B N   1 
ATOM   2951 C  CA  . PRO B 1 24  ? -11.236 15.907 11.775  1.00 34.05  ?  24  PRO B CA  1 
ATOM   2952 C  C   . PRO B 1 24  ? -11.050 15.285 10.388  1.00 36.21  ?  24  PRO B C   1 
ATOM   2953 O  O   . PRO B 1 24  ? -10.107 14.615 10.134  1.00 35.38  ?  24  PRO B O   1 
ATOM   2954 C  CB  . PRO B 1 24  ? -11.113 17.414 11.648  1.00 36.76  ?  24  PRO B CB  1 
ATOM   2955 C  CG  . PRO B 1 24  ? -9.680  17.693 11.990  1.00 35.78  ?  24  PRO B CG  1 
ATOM   2956 C  CD  . PRO B 1 24  ? -9.316  16.695 13.054  1.00 33.81  ?  24  PRO B CD  1 
ATOM   2957 N  N   . LEU B 1 25  ? -12.015 15.511 9.517   1.00 36.09  ?  25  LEU B N   1 
ATOM   2958 C  CA  . LEU B 1 25  ? -11.952 14.996 8.140   1.00 37.38  ?  25  LEU B CA  1 
ATOM   2959 C  C   . LEU B 1 25  ? -11.089 15.931 7.285   1.00 36.26  ?  25  LEU B C   1 
ATOM   2960 O  O   . LEU B 1 25  ? -10.557 16.905 7.803   1.00 38.80  ?  25  LEU B O   1 
ATOM   2961 C  CB  . LEU B 1 25  ? -13.389 14.898 7.623   1.00 36.78  ?  25  LEU B CB  1 
ATOM   2962 C  CG  . LEU B 1 25  ? -14.297 14.027 8.482   1.00 37.08  ?  25  LEU B CG  1 
ATOM   2963 C  CD1 . LEU B 1 25  ? -15.579 13.679 7.734   1.00 35.10  ?  25  LEU B CD1 1 
ATOM   2964 C  CD2 . LEU B 1 25  ? -13.558 12.775 8.937   1.00 36.70  ?  25  LEU B CD2 1 
ATOM   2965 N  N   . SER B 1 26  ? -10.970 15.625 6.001   1.00 38.01  ?  26  SER B N   1 
ATOM   2966 C  CA  . SER B 1 26  ? -10.122 16.349 5.028   1.00 38.80  ?  26  SER B CA  1 
ATOM   2967 C  C   . SER B 1 26  ? -10.331 17.867 5.166   1.00 38.40  ?  26  SER B C   1 
ATOM   2968 O  O   . SER B 1 26  ? -11.500 18.271 5.403   1.00 40.44  ?  26  SER B O   1 
ATOM   2969 C  CB  . SER B 1 26  ? -10.446 15.854 3.650   1.00 38.48  ?  26  SER B CB  1 
ATOM   2970 O  OG  . SER B 1 26  ? -9.743  16.609 2.695   1.00 37.76  ?  26  SER B OG  1 
ATOM   2971 N  N   . ARG B 1 27  ? -9.244  18.648 5.044   1.00 34.87  ?  27  ARG B N   1 
ATOM   2972 C  CA  . ARG B 1 27  ? -9.209  20.139 5.016   1.00 34.21  ?  27  ARG B CA  1 
ATOM   2973 C  C   . ARG B 1 27  ? -9.779  20.651 3.692   1.00 34.58  ?  27  ARG B C   1 
ATOM   2974 O  O   . ARG B 1 27  ? -10.177 21.829 3.620   1.00 32.13  ?  27  ARG B O   1 
ATOM   2975 C  CB  . ARG B 1 27  ? -7.770  20.648 5.160   1.00 36.94  ?  27  ARG B CB  1 
ATOM   2976 C  CG  . ARG B 1 27  ? -7.166  20.461 6.539   1.00 45.06  ?  27  ARG B CG  1 
ATOM   2977 C  CD  . ARG B 1 27  ? -8.073  20.931 7.687   1.00 52.32  ?  27  ARG B CD  1 
ATOM   2978 N  NE  . ARG B 1 27  ? -9.257  20.090 7.901   1.00 55.33  ?  27  ARG B NE  1 
ATOM   2979 C  CZ  . ARG B 1 27  ? -10.335 20.409 8.625   1.00 51.69  ?  27  ARG B CZ  1 
ATOM   2980 N  NH1 . ARG B 1 27  ? -10.420 21.578 9.248   1.00 54.31  ?  27  ARG B NH1 1 
ATOM   2981 N  NH2 . ARG B 1 27  ? -11.332 19.542 8.709   1.00 48.85  ?  27  ARG B NH2 1 
ATOM   2982 N  N   . ARG B 1 28  ? -9.765  19.806 2.664   1.00 34.11  ?  28  ARG B N   1 
ATOM   2983 C  CA  . ARG B 1 28  ? -10.200 20.173 1.303   1.00 32.78  ?  28  ARG B CA  1 
ATOM   2984 C  C   . ARG B 1 28  ? -11.715 20.431 1.355   1.00 32.76  ?  28  ARG B C   1 
ATOM   2985 O  O   . ARG B 1 28  ? -12.449 19.494 1.680   1.00 27.00  ?  28  ARG B O   1 
ATOM   2986 C  CB  . ARG B 1 28  ? -9.749  19.069 0.349   1.00 32.04  ?  28  ARG B CB  1 
ATOM   2987 C  CG  . ARG B 1 28  ? -10.231 19.242 -1.083  1.00 37.44  ?  28  ARG B CG  1 
ATOM   2988 C  CD  . ARG B 1 28  ? -10.016 18.041 -2.012  1.00 35.41  ?  28  ARG B CD  1 
ATOM   2989 N  NE  . ARG B 1 28  ? -10.449 18.427 -3.350  1.00 37.09  ?  28  ARG B NE  1 
ATOM   2990 C  CZ  . ARG B 1 28  ? -10.375 17.680 -4.445  1.00 34.53  ?  28  ARG B CZ  1 
ATOM   2991 N  NH1 . ARG B 1 28  ? -9.879  16.469 -4.406  1.00 36.78  ?  28  ARG B NH1 1 
ATOM   2992 N  NH2 . ARG B 1 28  ? -10.822 18.141 -5.588  1.00 36.35  ?  28  ARG B NH2 1 
ATOM   2993 N  N   . GLY B 1 29  ? -12.142 21.656 1.014   1.00 31.64  ?  29  GLY B N   1 
ATOM   2994 C  CA  . GLY B 1 29  ? -13.542 22.112 1.103   1.00 34.30  ?  29  GLY B CA  1 
ATOM   2995 C  C   . GLY B 1 29  ? -14.291 22.245 -0.232  1.00 34.34  ?  29  GLY B C   1 
ATOM   2996 O  O   . GLY B 1 29  ? -15.395 22.796 -0.224  1.00 30.26  ?  29  GLY B O   1 
ATOM   2997 N  N   . ASP B 1 30  ? -13.784 21.750 -1.357  1.00 36.15  ?  30  ASP B N   1 
ATOM   2998 C  CA  . ASP B 1 30  ? -14.521 21.900 -2.640  1.00 38.84  ?  30  ASP B CA  1 
ATOM   2999 C  C   . ASP B 1 30  ? -15.322 20.626 -2.962  1.00 35.91  ?  30  ASP B C   1 
ATOM   3000 O  O   . ASP B 1 30  ? -16.153 20.712 -3.832  1.00 39.08  ?  30  ASP B O   1 
ATOM   3001 C  CB  . ASP B 1 30  ? -13.573 22.274 -3.780  1.00 42.97  ?  30  ASP B CB  1 
ATOM   3002 C  CG  . ASP B 1 30  ? -12.691 21.121 -4.232  1.00 48.22  ?  30  ASP B CG  1 
ATOM   3003 O  OD1 . ASP B 1 30  ? -11.666 20.870 -3.553  1.00 41.03  ?  30  ASP B OD1 1 
ATOM   3004 O  OD2 . ASP B 1 30  ? -13.067 20.459 -5.249  1.00 51.91  ?  30  ASP B OD2 1 
ATOM   3005 N  N   . ILE B 1 31  ? -15.056 19.487 -2.325  1.00 35.25  ?  31  ILE B N   1 
ATOM   3006 C  CA  . ILE B 1 31  ? -15.886 18.244 -2.433  1.00 40.80  ?  31  ILE B CA  1 
ATOM   3007 C  C   . ILE B 1 31  ? -16.071 17.682 -1.025  1.00 38.41  ?  31  ILE B C   1 
ATOM   3008 O  O   . ILE B 1 31  ? -15.133 17.762 -0.207  1.00 42.15  ?  31  ILE B O   1 
ATOM   3009 C  CB  . ILE B 1 31  ? -15.330 17.131 -3.369  1.00 44.11  ?  31  ILE B CB  1 
ATOM   3010 C  CG1 . ILE B 1 31  ? -15.304 17.547 -4.839  1.00 49.75  ?  31  ILE B CG1 1 
ATOM   3011 C  CG2 . ILE B 1 31  ? -16.035 15.800 -3.199  1.00 45.88  ?  31  ILE B CG2 1 
ATOM   3012 C  CD1 . ILE B 1 31  ? -14.528 16.597 -5.750  1.00 58.10  ?  31  ILE B CD1 1 
ATOM   3013 N  N   . LEU B 1 32  ? -17.260 17.140 -0.771  1.00 37.85  ?  32  LEU B N   1 
ATOM   3014 C  CA  . LEU B 1 32  ? -17.565 16.339 0.430   1.00 37.20  ?  32  LEU B CA  1 
ATOM   3015 C  C   . LEU B 1 32  ? -16.514 15.245 0.521   1.00 35.41  ?  32  LEU B C   1 
ATOM   3016 O  O   . LEU B 1 32  ? -16.335 14.479 -0.427  1.00 35.55  ?  32  LEU B O   1 
ATOM   3017 C  CB  . LEU B 1 32  ? -18.976 15.745 0.306   1.00 39.76  ?  32  LEU B CB  1 
ATOM   3018 C  CG  . LEU B 1 32  ? -19.382 14.843 1.467   1.00 39.65  ?  32  LEU B CG  1 
ATOM   3019 C  CD1 . LEU B 1 32  ? -19.681 15.672 2.706   1.00 37.01  ?  32  LEU B CD1 1 
ATOM   3020 C  CD2 . LEU B 1 32  ? -20.561 13.982 1.078   1.00 42.31  ?  32  LEU B CD2 1 
ATOM   3021 N  N   . PRO B 1 33  ? -15.817 15.116 1.663   1.00 33.62  ?  33  PRO B N   1 
ATOM   3022 C  CA  . PRO B 1 33  ? -14.852 14.037 1.843   1.00 32.17  ?  33  PRO B CA  1 
ATOM   3023 C  C   . PRO B 1 33  ? -15.553 12.689 1.657   1.00 32.54  ?  33  PRO B C   1 
ATOM   3024 O  O   . PRO B 1 33  ? -16.659 12.533 2.175   1.00 34.42  ?  33  PRO B O   1 
ATOM   3025 C  CB  . PRO B 1 33  ? -14.380 14.180 3.294   1.00 32.59  ?  33  PRO B CB  1 
ATOM   3026 C  CG  . PRO B 1 33  ? -14.749 15.590 3.687   1.00 35.37  ?  33  PRO B CG  1 
ATOM   3027 C  CD  . PRO B 1 33  ? -15.994 15.917 2.883   1.00 36.65  ?  33  PRO B CD  1 
ATOM   3028 N  N   . ALA B 1 34  ? -14.948 11.777 0.897   1.00 31.85  ?  34  ALA B N   1 
ATOM   3029 C  CA  . ALA B 1 34  ? -15.454 10.401 0.685   1.00 33.72  ?  34  ALA B CA  1 
ATOM   3030 C  C   . ALA B 1 34  ? -15.729 9.748  2.051   1.00 35.50  ?  34  ALA B C   1 
ATOM   3031 O  O   . ALA B 1 34  ? -16.710 8.987  2.166   1.00 32.80  ?  34  ALA B O   1 
ATOM   3032 C  CB  . ALA B 1 34  ? -14.479 9.600  -0.138  1.00 33.17  ?  34  ALA B CB  1 
ATOM   3033 N  N   . GLU B 1 35  ? -14.945 10.104 3.069   1.00 39.82  ?  35  GLU B N   1 
ATOM   3034 C  CA  . GLU B 1 35  ? -15.059 9.543  4.448   1.00 46.56  ?  35  GLU B CA  1 
ATOM   3035 C  C   . GLU B 1 35  ? -16.423 9.936  5.071   1.00 45.37  ?  35  GLU B C   1 
ATOM   3036 O  O   . GLU B 1 35  ? -16.976 9.105  5.827   1.00 45.98  ?  35  GLU B O   1 
ATOM   3037 C  CB  . GLU B 1 35  ? -13.790 9.919  5.238   1.00 48.15  ?  35  GLU B CB  1 
ATOM   3038 C  CG  . GLU B 1 35  ? -12.500 9.273  4.761   1.00 53.91  ?  35  GLU B CG  1 
ATOM   3039 C  CD  . GLU B 1 35  ? -11.187 9.649  5.449   1.00 63.17  ?  35  GLU B CD  1 
ATOM   3040 O  OE1 . GLU B 1 35  ? -11.146 10.627 6.275   1.00 59.30  ?  35  GLU B OE1 1 
ATOM   3041 O  OE2 . GLU B 1 35  ? -10.179 8.976  5.123   1.00 63.65  ?  35  GLU B OE2 1 
ATOM   3042 N  N   . ALA B 1 36  ? -16.989 11.112 4.772   1.00 41.54  ?  36  ALA B N   1 
ATOM   3043 C  CA  . ALA B 1 36  ? -18.280 11.545 5.360   1.00 38.61  ?  36  ALA B CA  1 
ATOM   3044 C  C   . ALA B 1 36  ? -19.394 10.670 4.773   1.00 38.62  ?  36  ALA B C   1 
ATOM   3045 O  O   . ALA B 1 36  ? -20.341 10.293 5.508   1.00 34.10  ?  36  ALA B O   1 
ATOM   3046 C  CB  . ALA B 1 36  ? -18.534 13.013 5.120   1.00 33.14  ?  36  ALA B CB  1 
ATOM   3047 N  N   . GLU B 1 37  ? -19.271 10.366 3.487   1.00 41.35  ?  37  GLU B N   1 
ATOM   3048 C  CA  . GLU B 1 37  ? -20.201 9.495  2.729   1.00 45.94  ?  37  GLU B CA  1 
ATOM   3049 C  C   . GLU B 1 37  ? -20.118 8.096  3.370   1.00 40.73  ?  37  GLU B C   1 
ATOM   3050 O  O   . GLU B 1 37  ? -21.158 7.538  3.727   1.00 38.99  ?  37  GLU B O   1 
ATOM   3051 C  CB  . GLU B 1 37  ? -19.836 9.573  1.236   1.00 54.92  ?  37  GLU B CB  1 
ATOM   3052 C  CG  . GLU B 1 37  ? -20.075 10.920 0.565   1.00 61.63  ?  37  GLU B CG  1 
ATOM   3053 C  CD  . GLU B 1 37  ? -19.651 11.033 -0.900  1.00 74.08  ?  37  GLU B CD  1 
ATOM   3054 O  OE1 . GLU B 1 37  ? -18.966 10.094 -1.401  1.00 63.99  ?  37  GLU B OE1 1 
ATOM   3055 O  OE2 . GLU B 1 37  ? -19.975 12.072 -1.543  1.00 80.49  ?  37  GLU B OE2 1 
ATOM   3056 N  N   . ARG B 1 38  ? -18.921 7.575  3.606   1.00 39.27  ?  38  ARG B N   1 
ATOM   3057 C  CA  . ARG B 1 38  ? -18.753 6.188  4.108   1.00 45.42  ?  38  ARG B CA  1 
ATOM   3058 C  C   . ARG B 1 38  ? -19.319 6.108  5.537   1.00 43.23  ?  38  ARG B C   1 
ATOM   3059 O  O   . ARG B 1 38  ? -20.048 5.105  5.830   1.00 39.44  ?  38  ARG B O   1 
ATOM   3060 C  CB  . ARG B 1 38  ? -17.293 5.703  4.034   1.00 51.93  ?  38  ARG B CB  1 
ATOM   3061 C  CG  . ARG B 1 38  ? -17.113 4.247  4.473   1.00 57.66  ?  38  ARG B CG  1 
ATOM   3062 C  CD  . ARG B 1 38  ? -15.717 3.778  4.884   1.00 59.53  ?  38  ARG B CD  1 
ATOM   3063 N  NE  . ARG B 1 38  ? -15.086 4.598  5.922   1.00 63.19  ?  38  ARG B NE  1 
ATOM   3064 C  CZ  . ARG B 1 38  ? -15.354 4.563  7.230   1.00 60.06  ?  38  ARG B CZ  1 
ATOM   3065 N  NH1 . ARG B 1 38  ? -16.259 3.728  7.726   1.00 56.85  ?  38  ARG B NH1 1 
ATOM   3066 N  NH2 . ARG B 1 38  ? -14.714 5.394  8.039   1.00 54.48  ?  38  ARG B NH2 1 
ATOM   3067 N  N   . LEU B 1 39  ? -18.988 7.076  6.406   1.00 39.37  ?  39  LEU B N   1 
ATOM   3068 C  CA  . LEU B 1 39  ? -19.411 7.069  7.837   1.00 39.14  ?  39  LEU B CA  1 
ATOM   3069 C  C   . LEU B 1 39  ? -20.941 7.090  7.900   1.00 38.16  ?  39  LEU B C   1 
ATOM   3070 O  O   . LEU B 1 39  ? -21.511 6.254  8.620   1.00 41.03  ?  39  LEU B O   1 
ATOM   3071 C  CB  . LEU B 1 39  ? -18.818 8.265  8.591   1.00 40.49  ?  39  LEU B CB  1 
ATOM   3072 C  CG  . LEU B 1 39  ? -17.338 8.146  8.968   1.00 41.24  ?  39  LEU B CG  1 
ATOM   3073 C  CD1 . LEU B 1 39  ? -16.776 9.486  9.422   1.00 40.17  ?  39  LEU B CD1 1 
ATOM   3074 C  CD2 . LEU B 1 39  ? -17.129 7.103  10.044  1.00 41.92  ?  39  LEU B CD2 1 
ATOM   3075 N  N   . ARG B 1 40  ? -21.580 7.982  7.151   1.00 35.63  ?  40  ARG B N   1 
ATOM   3076 C  CA  . ARG B 1 40  ? -23.048 8.149  7.202   1.00 39.01  ?  40  ARG B CA  1 
ATOM   3077 C  C   . ARG B 1 40  ? -23.714 6.832  6.790   1.00 40.39  ?  40  ARG B C   1 
ATOM   3078 O  O   . ARG B 1 40  ? -24.797 6.519  7.314   1.00 43.48  ?  40  ARG B O   1 
ATOM   3079 C  CB  . ARG B 1 40  ? -23.494 9.295  6.294   1.00 40.01  ?  40  ARG B CB  1 
ATOM   3080 C  CG  . ARG B 1 40  ? -24.976 9.620  6.411   1.00 40.41  ?  40  ARG B CG  1 
ATOM   3081 C  CD  . ARG B 1 40  ? -25.484 10.565 5.347   1.00 40.11  ?  40  ARG B CD  1 
ATOM   3082 N  NE  . ARG B 1 40  ? -24.938 10.320 4.008   1.00 40.33  ?  40  ARG B NE  1 
ATOM   3083 C  CZ  . ARG B 1 40  ? -24.347 11.244 3.237   1.00 41.81  ?  40  ARG B CZ  1 
ATOM   3084 N  NH1 . ARG B 1 40  ? -24.182 12.493 3.651   1.00 40.14  ?  40  ARG B NH1 1 
ATOM   3085 N  NH2 . ARG B 1 40  ? -23.895 10.905 2.041   1.00 46.57  ?  40  ARG B NH2 1 
ATOM   3086 N  N   . ALA B 1 41  ? -23.085 6.076  5.895   1.00 41.43  ?  41  ALA B N   1 
ATOM   3087 C  CA  . ALA B 1 41  ? -23.678 4.863  5.286   1.00 42.99  ?  41  ALA B CA  1 
ATOM   3088 C  C   . ALA B 1 41  ? -23.431 3.636  6.165   1.00 39.80  ?  41  ALA B C   1 
ATOM   3089 O  O   . ALA B 1 41  ? -24.352 2.843  6.290   1.00 36.80  ?  41  ALA B O   1 
ATOM   3090 C  CB  . ALA B 1 41  ? -23.161 4.661  3.880   1.00 41.91  ?  41  ALA B CB  1 
ATOM   3091 N  N   . GLU B 1 42  ? -22.260 3.529  6.784   1.00 42.02  ?  42  GLU B N   1 
ATOM   3092 C  CA  . GLU B 1 42  ? -21.809 2.338  7.555   1.00 42.75  ?  42  GLU B CA  1 
ATOM   3093 C  C   . GLU B 1 42  ? -21.898 2.540  9.068   1.00 42.23  ?  42  GLU B C   1 
ATOM   3094 O  O   . GLU B 1 42  ? -22.137 1.546  9.759   1.00 51.61  ?  42  GLU B O   1 
ATOM   3095 C  CB  . GLU B 1 42  ? -20.359 2.026  7.194   1.00 46.72  ?  42  GLU B CB  1 
ATOM   3096 C  CG  . GLU B 1 42  ? -20.210 1.625  5.739   1.00 47.52  ?  42  GLU B CG  1 
ATOM   3097 C  CD  . GLU B 1 42  ? -18.800 1.298  5.320   1.00 48.62  ?  42  GLU B CD  1 
ATOM   3098 O  OE1 . GLU B 1 42  ? -17.894 1.343  6.163   1.00 51.02  ?  42  GLU B OE1 1 
ATOM   3099 O  OE2 . GLU B 1 42  ? -18.628 0.987  4.153   1.00 65.48  ?  42  GLU B OE2 1 
ATOM   3100 N  N   . GLN B 1 43  ? -21.644 3.737  9.592   1.00 40.20  ?  43  GLN B N   1 
ATOM   3101 C  CA  . GLN B 1 43  ? -21.727 3.973  11.059  1.00 40.61  ?  43  GLN B CA  1 
ATOM   3102 C  C   . GLN B 1 43  ? -22.127 5.428  11.314  1.00 35.78  ?  43  GLN B C   1 
ATOM   3103 O  O   . GLN B 1 43  ? -21.312 6.250  11.731  1.00 31.45  ?  43  GLN B O   1 
ATOM   3104 C  CB  . GLN B 1 43  ? -20.458 3.493  11.787  1.00 43.68  ?  43  GLN B CB  1 
ATOM   3105 C  CG  . GLN B 1 43  ? -20.238 1.988  11.778  1.00 48.99  ?  43  GLN B CG  1 
ATOM   3106 C  CD  . GLN B 1 43  ? -18.950 1.544  12.436  1.00 54.82  ?  43  GLN B CD  1 
ATOM   3107 O  OE1 . GLN B 1 43  ? -17.971 2.282  12.527  1.00 53.62  ?  43  GLN B OE1 1 
ATOM   3108 N  NE2 . GLN B 1 43  ? -18.936 0.302  12.896  1.00 60.41  ?  43  GLN B NE2 1 
ATOM   3109 N  N   . PRO B 1 44  ? -23.426 5.750  11.110  1.00 31.38  ?  44  PRO B N   1 
ATOM   3110 C  CA  . PRO B 1 44  ? -23.934 7.108  11.252  1.00 31.54  ?  44  PRO B CA  1 
ATOM   3111 C  C   . PRO B 1 44  ? -23.659 7.706  12.634  1.00 33.22  ?  44  PRO B C   1 
ATOM   3112 O  O   . PRO B 1 44  ? -23.736 8.915  12.805  1.00 34.24  ?  44  PRO B O   1 
ATOM   3113 C  CB  . PRO B 1 44  ? -25.453 6.972  11.025  1.00 33.25  ?  44  PRO B CB  1 
ATOM   3114 C  CG  . PRO B 1 44  ? -25.748 5.481  11.118  1.00 31.20  ?  44  PRO B CG  1 
ATOM   3115 C  CD  . PRO B 1 44  ? -24.472 4.813  10.667  1.00 31.73  ?  44  PRO B CD  1 
ATOM   3116 N  N   . VAL B 1 45  ? -23.420 6.833  13.602  1.00 34.92  ?  45  VAL B N   1 
ATOM   3117 C  CA  . VAL B 1 45  ? -22.774 7.182  14.896  1.00 34.48  ?  45  VAL B CA  1 
ATOM   3118 C  C   . VAL B 1 45  ? -21.507 6.340  15.003  1.00 31.70  ?  45  VAL B C   1 
ATOM   3119 O  O   . VAL B 1 45  ? -21.587 5.166  15.371  1.00 37.96  ?  45  VAL B O   1 
ATOM   3120 C  CB  . VAL B 1 45  ? -23.713 6.960  16.091  1.00 34.07  ?  45  VAL B CB  1 
ATOM   3121 C  CG1 . VAL B 1 45  ? -23.071 7.516  17.353  1.00 34.71  ?  45  VAL B CG1 1 
ATOM   3122 C  CG2 . VAL B 1 45  ? -25.086 7.578  15.843  1.00 35.35  ?  45  VAL B CG2 1 
ATOM   3123 N  N   . ALA B 1 46  ? -20.383 6.909  14.630  1.00 32.90  ?  46  ALA B N   1 
ATOM   3124 C  CA  . ALA B 1 46  ? -19.054 6.256  14.718  1.00 32.54  ?  46  ALA B CA  1 
ATOM   3125 C  C   . ALA B 1 46  ? -18.273 6.806  15.902  1.00 31.76  ?  46  ALA B C   1 
ATOM   3126 O  O   . ALA B 1 46  ? -18.309 8.045  16.117  1.00 34.46  ?  46  ALA B O   1 
ATOM   3127 C  CB  . ALA B 1 46  ? -18.296 6.484  13.441  1.00 31.87  ?  46  ALA B CB  1 
ATOM   3128 N  N   . ARG B 1 47  ? -17.581 5.914  16.607  1.00 33.98  ?  47  ARG B N   1 
ATOM   3129 C  CA  . ARG B 1 47  ? -16.502 6.264  17.566  1.00 38.52  ?  47  ARG B CA  1 
ATOM   3130 C  C   . ARG B 1 47  ? -15.250 6.688  16.779  1.00 34.87  ?  47  ARG B C   1 
ATOM   3131 O  O   . ARG B 1 47  ? -14.854 5.979  15.844  1.00 38.04  ?  47  ARG B O   1 
ATOM   3132 C  CB  . ARG B 1 47  ? -16.226 5.072  18.495  1.00 45.75  ?  47  ARG B CB  1 
ATOM   3133 C  CG  . ARG B 1 47  ? -15.074 5.287  19.470  1.00 52.24  ?  47  ARG B CG  1 
ATOM   3134 C  CD  . ARG B 1 47  ? -15.414 4.911  20.898  1.00 59.04  ?  47  ARG B CD  1 
ATOM   3135 N  NE  . ARG B 1 47  ? -15.812 6.072  21.700  1.00 62.79  ?  47  ARG B NE  1 
ATOM   3136 C  CZ  . ARG B 1 47  ? -16.508 6.016  22.837  1.00 65.01  ?  47  ARG B CZ  1 
ATOM   3137 N  NH1 . ARG B 1 47  ? -16.929 4.849  23.303  1.00 71.66  ?  47  ARG B NH1 1 
ATOM   3138 N  NH2 . ARG B 1 47  ? -16.801 7.129  23.491  1.00 61.82  ?  47  ARG B NH2 1 
ATOM   3139 N  N   . VAL B 1 48  ? -14.644 7.802  17.161  1.00 31.58  ?  48  VAL B N   1 
ATOM   3140 C  CA  . VAL B 1 48  ? -13.534 8.450  16.414  1.00 33.17  ?  48  VAL B CA  1 
ATOM   3141 C  C   . VAL B 1 48  ? -12.542 8.979  17.431  1.00 33.30  ?  48  VAL B C   1 
ATOM   3142 O  O   . VAL B 1 48  ? -12.932 9.135  18.590  1.00 36.46  ?  48  VAL B O   1 
ATOM   3143 C  CB  . VAL B 1 48  ? -14.042 9.598  15.519  1.00 32.28  ?  48  VAL B CB  1 
ATOM   3144 C  CG1 . VAL B 1 48  ? -15.173 9.170  14.597  1.00 31.48  ?  48  VAL B CG1 1 
ATOM   3145 C  CG2 . VAL B 1 48  ? -14.475 10.789 16.340  1.00 33.00  ?  48  VAL B CG2 1 
ATOM   3146 N  N   . ARG B 1 49  ? -11.313 9.242  17.006  1.00 32.66  ?  49  ARG B N   1 
ATOM   3147 C  CA  . ARG B 1 49  ? -10.280 9.829  17.887  1.00 34.84  ?  49  ARG B CA  1 
ATOM   3148 C  C   . ARG B 1 49  ? -10.085 11.272 17.441  1.00 33.17  ?  49  ARG B C   1 
ATOM   3149 O  O   . ARG B 1 49  ? -9.696  11.489 16.291  1.00 39.49  ?  49  ARG B O   1 
ATOM   3150 C  CB  . ARG B 1 49  ? -8.986  9.027  17.774  1.00 40.93  ?  49  ARG B CB  1 
ATOM   3151 C  CG  . ARG B 1 49  ? -7.944  9.410  18.809  1.00 49.37  ?  49  ARG B CG  1 
ATOM   3152 C  CD  . ARG B 1 49  ? -6.556  9.372  18.207  1.00 61.50  ?  49  ARG B CD  1 
ATOM   3153 N  NE  . ARG B 1 49  ? -5.510  9.671  19.188  1.00 65.10  ?  49  ARG B NE  1 
ATOM   3154 C  CZ  . ARG B 1 49  ? -4.439  10.442 18.974  1.00 66.83  ?  49  ARG B CZ  1 
ATOM   3155 N  NH1 . ARG B 1 49  ? -4.251  11.040 17.806  1.00 69.20  ?  49  ARG B NH1 1 
ATOM   3156 N  NH2 . ARG B 1 49  ? -3.576  10.642 19.957  1.00 66.72  ?  49  ARG B NH2 1 
ATOM   3157 N  N   . THR B 1 50  ? -10.360 12.249 18.281  1.00 29.18  ?  50  THR B N   1 
ATOM   3158 C  CA  . THR B 1 50  ? -10.139 13.650 17.876  1.00 29.49  ?  50  THR B CA  1 
ATOM   3159 C  C   . THR B 1 50  ? -8.648  13.995 17.851  1.00 32.36  ?  50  THR B C   1 
ATOM   3160 O  O   . THR B 1 50  ? -7.835  13.185 18.302  1.00 38.53  ?  50  THR B O   1 
ATOM   3161 C  CB  . THR B 1 50  ? -10.875 14.579 18.820  1.00 29.58  ?  50  THR B CB  1 
ATOM   3162 O  OG1 . THR B 1 50  ? -10.041 14.638 19.985  1.00 28.56  ?  50  THR B OG1 1 
ATOM   3163 C  CG2 . THR B 1 50  ? -12.286 14.082 19.046  1.00 29.78  ?  50  THR B CG2 1 
ATOM   3164 N  N   . MET B 1 51  ? -8.305  15.207 17.418  1.00 34.81  ?  51  MET B N   1 
ATOM   3165 C  CA  . MET B 1 51  ? -6.892  15.653 17.319  1.00 30.69  ?  51  MET B CA  1 
ATOM   3166 C  C   . MET B 1 51  ? -6.263  15.756 18.727  1.00 32.42  ?  51  MET B C   1 
ATOM   3167 O  O   . MET B 1 51  ? -5.005  15.727 18.823  1.00 34.76  ?  51  MET B O   1 
ATOM   3168 C  CB  . MET B 1 51  ? -6.793  16.966 16.523  1.00 29.66  ?  51  MET B CB  1 
ATOM   3169 C  CG  . MET B 1 51  ? -6.922  18.235 17.327  1.00 29.39  ?  51  MET B CG  1 
ATOM   3170 S  SD  . MET B 1 51  ? -6.799  19.755 16.330  1.00 30.15  ?  51  MET B SD  1 
ATOM   3171 C  CE  . MET B 1 51  ? -7.917  19.385 14.989  1.00 32.56  ?  51  MET B CE  1 
ATOM   3172 N  N   . THR B 1 52  ? -7.049  15.845 19.804  1.00 30.77  ?  52  THR B N   1 
ATOM   3173 C  CA  . THR B 1 52  ? -6.488  15.849 21.184  1.00 30.94  ?  52  THR B CA  1 
ATOM   3174 C  C   . THR B 1 52  ? -6.128  14.419 21.610  1.00 31.93  ?  52  THR B C   1 
ATOM   3175 O  O   . THR B 1 52  ? -5.454  14.272 22.616  1.00 30.92  ?  52  THR B O   1 
ATOM   3176 C  CB  . THR B 1 52  ? -7.445  16.438 22.229  1.00 33.66  ?  52  THR B CB  1 
ATOM   3177 O  OG1 . THR B 1 52  ? -8.619  15.626 22.339  1.00 30.92  ?  52  THR B OG1 1 
ATOM   3178 C  CG2 . THR B 1 52  ? -7.837  17.868 21.924  1.00 35.18  ?  52  THR B CG2 1 
ATOM   3179 N  N   . GLY B 1 53  ? -6.631  13.396 20.923  1.00 32.90  ?  53  GLY B N   1 
ATOM   3180 C  CA  . GLY B 1 53  ? -6.508  12.006 21.390  1.00 31.82  ?  53  GLY B CA  1 
ATOM   3181 C  C   . GLY B 1 53  ? -7.723  11.519 22.164  1.00 32.52  ?  53  GLY B C   1 
ATOM   3182 O  O   . GLY B 1 53  ? -7.888  10.276 22.239  1.00 31.76  ?  53  GLY B O   1 
ATOM   3183 N  N   . ASP B 1 54  ? -8.567  12.418 22.701  1.00 30.86  ?  54  ASP B N   1 
ATOM   3184 C  CA  . ASP B 1 54  ? -9.881  12.028 23.292  1.00 29.24  ?  54  ASP B CA  1 
ATOM   3185 C  C   . ASP B 1 54  ? -10.692 11.247 22.267  1.00 29.86  ?  54  ASP B C   1 
ATOM   3186 O  O   . ASP B 1 54  ? -10.412 11.366 21.066  1.00 34.79  ?  54  ASP B O   1 
ATOM   3187 C  CB  . ASP B 1 54  ? -10.665 13.233 23.779  1.00 29.26  ?  54  ASP B CB  1 
ATOM   3188 C  CG  . ASP B 1 54  ? -9.829  14.021 24.763  1.00 30.61  ?  54  ASP B CG  1 
ATOM   3189 O  OD1 . ASP B 1 54  ? -8.983  13.349 25.384  1.00 31.62  ?  54  ASP B OD1 1 
ATOM   3190 O  OD2 . ASP B 1 54  ? -9.990  15.296 24.871  1.00 26.48  ?  54  ASP B OD2 1 
ATOM   3191 N  N   . GLU B 1 55  ? -11.638 10.446 22.736  1.00 33.89  ?  55  GLU B N   1 
ATOM   3192 C  CA  . GLU B 1 55  ? -12.580 9.684  21.882  1.00 34.65  ?  55  GLU B CA  1 
ATOM   3193 C  C   . GLU B 1 55  ? -13.900 10.453 21.853  1.00 30.21  ?  55  GLU B C   1 
ATOM   3194 O  O   . GLU B 1 55  ? -14.165 11.167 22.815  1.00 30.72  ?  55  GLU B O   1 
ATOM   3195 C  CB  . GLU B 1 55  ? -12.744 8.270  22.433  1.00 42.94  ?  55  GLU B CB  1 
ATOM   3196 C  CG  . GLU B 1 55  ? -11.483 7.426  22.353  1.00 49.02  ?  55  GLU B CG  1 
ATOM   3197 C  CD  . GLU B 1 55  ? -11.690 5.938  22.614  1.00 55.55  ?  55  GLU B CD  1 
ATOM   3198 O  OE1 . GLU B 1 55  ? -12.737 5.564  23.205  1.00 61.87  ?  55  GLU B OE1 1 
ATOM   3199 O  OE2 . GLU B 1 55  ? -10.798 5.150  22.239  1.00 59.90  ?  55  GLU B OE2 1 
ATOM   3200 N  N   . ALA B 1 56  ? -14.674 10.323 20.773  1.00 32.67  ?  56  ALA B N   1 
ATOM   3201 C  CA  . ALA B 1 56  ? -15.934 11.064 20.509  1.00 31.42  ?  56  ALA B CA  1 
ATOM   3202 C  C   . ALA B 1 56  ? -16.914 10.210 19.703  1.00 31.53  ?  56  ALA B C   1 
ATOM   3203 O  O   . ALA B 1 56  ? -16.487 9.293  18.956  1.00 31.24  ?  56  ALA B O   1 
ATOM   3204 C  CB  . ALA B 1 56  ? -15.678 12.341 19.745  1.00 29.56  ?  56  ALA B CB  1 
ATOM   3205 N  N   . TRP B 1 57  ? -18.191 10.565 19.810  1.00 31.61  ?  57  TRP B N   1 
ATOM   3206 C  CA  . TRP B 1 57  ? -19.240 10.047 18.910  1.00 33.69  ?  57  TRP B CA  1 
ATOM   3207 C  C   . TRP B 1 57  ? -19.476 11.083 17.803  1.00 36.78  ?  57  TRP B C   1 
ATOM   3208 O  O   . TRP B 1 57  ? -19.964 12.204 18.097  1.00 39.22  ?  57  TRP B O   1 
ATOM   3209 C  CB  . TRP B 1 57  ? -20.488 9.700  19.722  1.00 33.28  ?  57  TRP B CB  1 
ATOM   3210 C  CG  . TRP B 1 57  ? -20.325 8.557  20.681  1.00 30.86  ?  57  TRP B CG  1 
ATOM   3211 C  CD1 . TRP B 1 57  ? -20.440 8.615  22.037  1.00 32.31  ?  57  TRP B CD1 1 
ATOM   3212 C  CD2 . TRP B 1 57  ? -20.050 7.180  20.369  1.00 29.74  ?  57  TRP B CD2 1 
ATOM   3213 N  NE1 . TRP B 1 57  ? -20.260 7.372  22.587  1.00 32.64  ?  57  TRP B NE1 1 
ATOM   3214 C  CE2 . TRP B 1 57  ? -20.019 6.472  21.590  1.00 31.96  ?  57  TRP B CE2 1 
ATOM   3215 C  CE3 . TRP B 1 57  ? -19.867 6.462  19.182  1.00 30.30  ?  57  TRP B CE3 1 
ATOM   3216 C  CZ2 . TRP B 1 57  ? -19.822 5.089  21.651  1.00 32.42  ?  57  TRP B CZ2 1 
ATOM   3217 C  CZ3 . TRP B 1 57  ? -19.659 5.098  19.237  1.00 30.36  ?  57  TRP B CZ3 1 
ATOM   3218 C  CH2 . TRP B 1 57  ? -19.623 4.424  20.458  1.00 30.85  ?  57  TRP B CH2 1 
ATOM   3219 N  N   . LEU B 1 58  ? -19.062 10.737 16.587  1.00 32.47  ?  58  LEU B N   1 
ATOM   3220 C  CA  . LEU B 1 58  ? -19.331 11.527 15.373  1.00 28.32  ?  58  LEU B CA  1 
ATOM   3221 C  C   . LEU B 1 58  ? -20.656 11.051 14.776  1.00 28.73  ?  58  LEU B C   1 
ATOM   3222 O  O   . LEU B 1 58  ? -20.797 9.841  14.471  1.00 23.66  ?  58  LEU B O   1 
ATOM   3223 C  CB  . LEU B 1 58  ? -18.180 11.296 14.404  1.00 26.92  ?  58  LEU B CB  1 
ATOM   3224 C  CG  . LEU B 1 58  ? -18.178 12.164 13.160  1.00 26.06  ?  58  LEU B CG  1 
ATOM   3225 C  CD1 . LEU B 1 58  ? -18.035 13.644 13.523  1.00 26.51  ?  58  LEU B CD1 1 
ATOM   3226 C  CD2 . LEU B 1 58  ? -17.053 11.725 12.242  1.00 25.61  ?  58  LEU B CD2 1 
ATOM   3227 N  N   . VAL B 1 59  ? -21.585 11.981 14.609  1.00 28.19  ?  59  VAL B N   1 
ATOM   3228 C  CA  . VAL B 1 59  ? -22.951 11.719 14.079  1.00 28.10  ?  59  VAL B CA  1 
ATOM   3229 C  C   . VAL B 1 59  ? -23.056 12.355 12.692  1.00 27.25  ?  59  VAL B C   1 
ATOM   3230 O  O   . VAL B 1 59  ? -22.863 13.577 12.586  1.00 30.68  ?  59  VAL B O   1 
ATOM   3231 C  CB  . VAL B 1 59  ? -23.975 12.312 15.060  1.00 30.61  ?  59  VAL B CB  1 
ATOM   3232 C  CG1 . VAL B 1 59  ? -25.415 11.943 14.697  1.00 29.13  ?  59  VAL B CG1 1 
ATOM   3233 C  CG2 . VAL B 1 59  ? -23.618 11.942 16.499  1.00 30.92  ?  59  VAL B CG2 1 
ATOM   3234 N  N   . SER B 1 60  ? -23.372 11.579 11.671  1.00 24.97  ?  60  SER B N   1 
ATOM   3235 C  CA  . SER B 1 60  ? -23.100 11.964 10.266  1.00 28.18  ?  60  SER B CA  1 
ATOM   3236 C  C   . SER B 1 60  ? -24.355 11.835 9.394   1.00 26.14  ?  60  SER B C   1 
ATOM   3237 O  O   . SER B 1 60  ? -24.276 12.108 8.170   1.00 28.78  ?  60  SER B O   1 
ATOM   3238 C  CB  . SER B 1 60  ? -21.906 11.159 9.715   1.00 29.57  ?  60  SER B CB  1 
ATOM   3239 O  OG  . SER B 1 60  ? -21.987 9.775  10.075  1.00 28.46  ?  60  SER B OG  1 
ATOM   3240 N  N   . SER B 1 61  ? -25.476 11.443 9.973   1.00 24.08  ?  61  SER B N   1 
ATOM   3241 C  CA  . SER B 1 61  ? -26.769 11.374 9.251   1.00 25.50  ?  61  SER B CA  1 
ATOM   3242 C  C   . SER B 1 61  ? -27.649 12.542 9.692   1.00 26.31  ?  61  SER B C   1 
ATOM   3243 O  O   . SER B 1 61  ? -27.568 13.017 10.860  1.00 23.90  ?  61  SER B O   1 
ATOM   3244 C  CB  . SER B 1 61  ? -27.471 10.045 9.452   1.00 26.11  ?  61  SER B CB  1 
ATOM   3245 O  OG  . SER B 1 61  ? -28.046 9.944  10.748  1.00 23.43  ?  61  SER B OG  1 
ATOM   3246 N  N   . TYR B 1 62  ? -28.522 12.951 8.798   1.00 28.75  ?  62  TYR B N   1 
ATOM   3247 C  CA  . TYR B 1 62  ? -29.443 14.084 9.039   1.00 31.31  ?  62  TYR B CA  1 
ATOM   3248 C  C   . TYR B 1 62  ? -30.310 13.836 10.283  1.00 32.50  ?  62  TYR B C   1 
ATOM   3249 O  O   . TYR B 1 62  ? -30.285 14.664 11.237  1.00 32.45  ?  62  TYR B O   1 
ATOM   3250 C  CB  . TYR B 1 62  ? -30.261 14.350 7.780   1.00 28.75  ?  62  TYR B CB  1 
ATOM   3251 C  CG  . TYR B 1 62  ? -31.184 15.504 7.992   1.00 29.54  ?  62  TYR B CG  1 
ATOM   3252 C  CD1 . TYR B 1 62  ? -30.738 16.793 7.797   1.00 29.42  ?  62  TYR B CD1 1 
ATOM   3253 C  CD2 . TYR B 1 62  ? -32.469 15.305 8.477   1.00 25.97  ?  62  TYR B CD2 1 
ATOM   3254 C  CE1 . TYR B 1 62  ? -31.590 17.870 8.000   1.00 31.65  ?  62  TYR B CE1 1 
ATOM   3255 C  CE2 . TYR B 1 62  ? -33.314 16.369 8.707   1.00 26.12  ?  62  TYR B CE2 1 
ATOM   3256 C  CZ  . TYR B 1 62  ? -32.880 17.654 8.458   1.00 27.89  ?  62  TYR B CZ  1 
ATOM   3257 O  OH  . TYR B 1 62  ? -33.729 18.704 8.646   1.00 26.02  ?  62  TYR B OH  1 
ATOM   3258 N  N   . GLU B 1 63  ? -31.068 12.739 10.246  1.00 38.20  ?  63  GLU B N   1 
ATOM   3259 C  CA  . GLU B 1 63  ? -32.015 12.290 11.298  1.00 37.63  ?  63  GLU B CA  1 
ATOM   3260 C  C   . GLU B 1 63  ? -31.313 12.417 12.652  1.00 31.65  ?  63  GLU B C   1 
ATOM   3261 O  O   . GLU B 1 63  ? -31.840 13.094 13.543  1.00 28.27  ?  63  GLU B O   1 
ATOM   3262 C  CB  . GLU B 1 63  ? -32.425 10.855 10.968  1.00 43.71  ?  63  GLU B CB  1 
ATOM   3263 C  CG  . GLU B 1 63  ? -33.770 10.429 11.538  1.00 54.21  ?  63  GLU B CG  1 
ATOM   3264 C  CD  . GLU B 1 63  ? -33.975 8.915  11.663  1.00 60.72  ?  63  GLU B CD  1 
ATOM   3265 O  OE1 . GLU B 1 63  ? -34.789 8.510  12.534  1.00 63.50  ?  63  GLU B OE1 1 
ATOM   3266 O  OE2 . GLU B 1 63  ? -33.315 8.129  10.904  1.00 57.39  ?  63  GLU B OE2 1 
ATOM   3267 N  N   . LEU B 1 64  ? -30.112 11.849 12.773  1.00 28.09  ?  64  LEU B N   1 
ATOM   3268 C  CA  . LEU B 1 64  ? -29.457 11.682 14.091  1.00 27.36  ?  64  LEU B CA  1 
ATOM   3269 C  C   . LEU B 1 64  ? -28.780 12.998 14.469  1.00 28.34  ?  64  LEU B C   1 
ATOM   3270 O  O   . LEU B 1 64  ? -28.747 13.343 15.684  1.00 25.99  ?  64  LEU B O   1 
ATOM   3271 C  CB  . LEU B 1 64  ? -28.508 10.488 14.045  1.00 26.09  ?  64  LEU B CB  1 
ATOM   3272 C  CG  . LEU B 1 64  ? -29.161 9.127  13.775  1.00 28.70  ?  64  LEU B CG  1 
ATOM   3273 C  CD1 . LEU B 1 64  ? -28.120 8.014  13.825  1.00 32.12  ?  64  LEU B CD1 1 
ATOM   3274 C  CD2 . LEU B 1 64  ? -30.262 8.816  14.771  1.00 27.83  ?  64  LEU B CD2 1 
ATOM   3275 N  N   . ALA B 1 65  ? -28.310 13.747 13.471  1.00 29.94  ?  65  ALA B N   1 
ATOM   3276 C  CA  . ALA B 1 65  ? -27.720 15.084 13.716  1.00 30.78  ?  65  ALA B CA  1 
ATOM   3277 C  C   . ALA B 1 65  ? -28.832 15.993 14.256  1.00 28.24  ?  65  ALA B C   1 
ATOM   3278 O  O   . ALA B 1 65  ? -28.615 16.626 15.301  1.00 26.20  ?  65  ALA B O   1 
ATOM   3279 C  CB  . ALA B 1 65  ? -27.046 15.627 12.477  1.00 29.56  ?  65  ALA B CB  1 
ATOM   3280 N  N   . LYS B 1 66  ? -29.995 16.002 13.602  1.00 29.77  ?  66  LYS B N   1 
ATOM   3281 C  CA  . LYS B 1 66  ? -31.128 16.862 14.018  1.00 33.23  ?  66  LYS B CA  1 
ATOM   3282 C  C   . LYS B 1 66  ? -31.525 16.476 15.449  1.00 32.17  ?  66  LYS B C   1 
ATOM   3283 O  O   . LYS B 1 66  ? -31.670 17.373 16.285  1.00 32.81  ?  66  LYS B O   1 
ATOM   3284 C  CB  . LYS B 1 66  ? -32.277 16.727 13.024  1.00 37.02  ?  66  LYS B CB  1 
ATOM   3285 C  CG  . LYS B 1 66  ? -33.537 17.499 13.382  1.00 43.01  ?  66  LYS B CG  1 
ATOM   3286 C  CD  . LYS B 1 66  ? -34.354 17.887 12.154  1.00 51.45  ?  66  LYS B CD  1 
ATOM   3287 C  CE  . LYS B 1 66  ? -35.795 18.242 12.477  1.00 59.41  ?  66  LYS B CE  1 
ATOM   3288 N  NZ  . LYS B 1 66  ? -36.695 17.088 12.231  1.00 65.23  ?  66  LYS B NZ  1 
ATOM   3289 N  N   . GLN B 1 67  ? -31.624 15.180 15.726  1.00 27.98  ?  67  GLN B N   1 
ATOM   3290 C  CA  . GLN B 1 67  ? -31.986 14.656 17.054  1.00 30.71  ?  67  GLN B CA  1 
ATOM   3291 C  C   . GLN B 1 67  ? -31.039 15.190 18.129  1.00 31.87  ?  67  GLN B C   1 
ATOM   3292 O  O   . GLN B 1 67  ? -31.553 15.602 19.195  1.00 30.80  ?  67  GLN B O   1 
ATOM   3293 C  CB  . GLN B 1 67  ? -31.925 13.134 17.048  1.00 32.39  ?  67  GLN B CB  1 
ATOM   3294 C  CG  . GLN B 1 67  ? -32.314 12.563 18.391  1.00 35.35  ?  67  GLN B CG  1 
ATOM   3295 C  CD  . GLN B 1 67  ? -32.738 11.121 18.290  1.00 40.15  ?  67  GLN B CD  1 
ATOM   3296 O  OE1 . GLN B 1 67  ? -32.593 10.463 17.260  1.00 36.00  ?  67  GLN B OE1 1 
ATOM   3297 N  NE2 . GLN B 1 67  ? -33.277 10.616 19.388  1.00 45.59  ?  67  GLN B NE2 1 
ATOM   3298 N  N   . VAL B 1 68  ? -29.713 15.110 17.885  1.00 34.38  ?  68  VAL B N   1 
ATOM   3299 C  CA  . VAL B 1 68  ? -28.663 15.572 18.848  1.00 32.84  ?  68  VAL B CA  1 
ATOM   3300 C  C   . VAL B 1 68  ? -28.893 17.068 19.073  1.00 30.45  ?  68  VAL B C   1 
ATOM   3301 O  O   . VAL B 1 68  ? -29.032 17.475 20.242  1.00 27.43  ?  68  VAL B O   1 
ATOM   3302 C  CB  . VAL B 1 68  ? -27.210 15.304 18.383  1.00 33.73  ?  68  VAL B CB  1 
ATOM   3303 C  CG1 . VAL B 1 68  ? -26.228 16.083 19.252  1.00 31.26  ?  68  VAL B CG1 1 
ATOM   3304 C  CG2 . VAL B 1 68  ? -26.822 13.826 18.361  1.00 31.07  ?  68  VAL B CG2 1 
ATOM   3305 N  N   . LEU B 1 69  ? -28.962 17.849 17.986  1.00 29.72  ?  69  LEU B N   1 
ATOM   3306 C  CA  . LEU B 1 69  ? -29.144 19.328 18.052  1.00 31.37  ?  69  LEU B CA  1 
ATOM   3307 C  C   . LEU B 1 69  ? -30.412 19.678 18.821  1.00 31.92  ?  69  LEU B C   1 
ATOM   3308 O  O   . LEU B 1 69  ? -30.434 20.723 19.472  1.00 32.44  ?  69  LEU B O   1 
ATOM   3309 C  CB  . LEU B 1 69  ? -29.242 19.917 16.645  1.00 30.61  ?  69  LEU B CB  1 
ATOM   3310 C  CG  . LEU B 1 69  ? -27.972 19.829 15.816  1.00 28.55  ?  69  LEU B CG  1 
ATOM   3311 C  CD1 . LEU B 1 69  ? -28.152 20.667 14.581  1.00 29.57  ?  69  LEU B CD1 1 
ATOM   3312 C  CD2 . LEU B 1 69  ? -26.755 20.268 16.619  1.00 28.91  ?  69  LEU B CD2 1 
ATOM   3313 N  N   . GLU B 1 70  ? -31.446 18.856 18.712  1.00 34.54  ?  70  GLU B N   1 
ATOM   3314 C  CA  . GLU B 1 70  ? -32.776 19.198 19.279  1.00 36.34  ?  70  GLU B CA  1 
ATOM   3315 C  C   . GLU B 1 70  ? -32.977 18.541 20.643  1.00 34.43  ?  70  GLU B C   1 
ATOM   3316 O  O   . GLU B 1 70  ? -34.036 18.777 21.229  1.00 36.69  ?  70  GLU B O   1 
ATOM   3317 C  CB  . GLU B 1 70  ? -33.869 18.803 18.294  1.00 35.03  ?  70  GLU B CB  1 
ATOM   3318 C  CG  . GLU B 1 70  ? -34.073 19.878 17.245  1.00 37.71  ?  70  GLU B CG  1 
ATOM   3319 C  CD  . GLU B 1 70  ? -35.015 19.433 16.154  1.00 38.52  ?  70  GLU B CD  1 
ATOM   3320 O  OE1 . GLU B 1 70  ? -35.415 18.264 16.166  1.00 36.63  ?  70  GLU B OE1 1 
ATOM   3321 O  OE2 . GLU B 1 70  ? -35.294 20.249 15.287  1.00 51.47  ?  70  GLU B OE2 1 
ATOM   3322 N  N   . ASP B 1 71  ? -32.032 17.729 21.104  1.00 29.89  ?  71  ASP B N   1 
ATOM   3323 C  CA  . ASP B 1 71  ? -32.130 17.053 22.414  1.00 29.41  ?  71  ASP B CA  1 
ATOM   3324 C  C   . ASP B 1 71  ? -31.235 17.814 23.402  1.00 32.91  ?  71  ASP B C   1 
ATOM   3325 O  O   . ASP B 1 71  ? -29.996 17.764 23.237  1.00 32.56  ?  71  ASP B O   1 
ATOM   3326 C  CB  . ASP B 1 71  ? -31.806 15.577 22.238  1.00 28.26  ?  71  ASP B CB  1 
ATOM   3327 C  CG  . ASP B 1 71  ? -31.872 14.746 23.505  1.00 31.39  ?  71  ASP B CG  1 
ATOM   3328 O  OD1 . ASP B 1 71  ? -31.680 15.316 24.637  1.00 31.94  ?  71  ASP B OD1 1 
ATOM   3329 O  OD2 . ASP B 1 71  ? -32.083 13.522 23.352  1.00 30.68  ?  71  ASP B OD2 1 
ATOM   3330 N  N   . ASP B 1 72  ? -31.845 18.420 24.425  1.00 35.41  ?  72  ASP B N   1 
ATOM   3331 C  CA  . ASP B 1 72  ? -31.205 19.290 25.455  1.00 39.92  ?  72  ASP B CA  1 
ATOM   3332 C  C   . ASP B 1 72  ? -30.285 18.496 26.405  1.00 42.79  ?  72  ASP B C   1 
ATOM   3333 O  O   . ASP B 1 72  ? -29.472 19.159 27.097  1.00 44.65  ?  72  ASP B O   1 
ATOM   3334 C  CB  . ASP B 1 72  ? -32.281 20.125 26.173  1.00 41.51  ?  72  ASP B CB  1 
ATOM   3335 C  CG  . ASP B 1 72  ? -33.012 21.015 25.168  1.00 47.16  ?  72  ASP B CG  1 
ATOM   3336 O  OD1 . ASP B 1 72  ? -32.319 21.911 24.570  1.00 49.19  ?  72  ASP B OD1 1 
ATOM   3337 O  OD2 . ASP B 1 72  ? -34.236 20.750 24.897  1.00 47.28  ?  72  ASP B OD2 1 
ATOM   3338 N  N   . ARG B 1 73  ? -30.341 17.155 26.426  1.00 37.64  ?  73  ARG B N   1 
ATOM   3339 C  CA  . ARG B 1 73  ? -29.409 16.342 27.242  1.00 34.66  ?  73  ARG B CA  1 
ATOM   3340 C  C   . ARG B 1 73  ? -28.016 16.275 26.579  1.00 38.26  ?  73  ARG B C   1 
ATOM   3341 O  O   . ARG B 1 73  ? -27.095 15.653 27.174  1.00 39.88  ?  73  ARG B O   1 
ATOM   3342 C  CB  . ARG B 1 73  ? -29.992 14.947 27.473  1.00 35.35  ?  73  ARG B CB  1 
ATOM   3343 C  CG  . ARG B 1 73  ? -31.320 14.950 28.205  1.00 34.64  ?  73  ARG B CG  1 
ATOM   3344 C  CD  . ARG B 1 73  ? -32.095 13.662 28.081  1.00 33.79  ?  73  ARG B CD  1 
ATOM   3345 N  NE  . ARG B 1 73  ? -32.340 13.177 26.725  1.00 32.11  ?  73  ARG B NE  1 
ATOM   3346 C  CZ  . ARG B 1 73  ? -32.552 11.897 26.416  1.00 30.89  ?  73  ARG B CZ  1 
ATOM   3347 N  NH1 . ARG B 1 73  ? -32.565 10.969 27.365  1.00 32.74  ?  73  ARG B NH1 1 
ATOM   3348 N  NH2 . ARG B 1 73  ? -32.735 11.540 25.158  1.00 29.33  ?  73  ARG B NH2 1 
ATOM   3349 N  N   . PHE B 1 74  ? -27.839 16.849 25.386  1.00 35.98  ?  74  PHE B N   1 
ATOM   3350 C  CA  . PHE B 1 74  ? -26.508 17.081 24.767  1.00 33.79  ?  74  PHE B CA  1 
ATOM   3351 C  C   . PHE B 1 74  ? -26.172 18.563 24.925  1.00 33.71  ?  74  PHE B C   1 
ATOM   3352 O  O   . PHE B 1 74  ? -26.812 19.383 24.247  1.00 29.95  ?  74  PHE B O   1 
ATOM   3353 C  CB  . PHE B 1 74  ? -26.522 16.669 23.298  1.00 31.87  ?  74  PHE B CB  1 
ATOM   3354 C  CG  . PHE B 1 74  ? -26.799 15.208 23.096  1.00 31.67  ?  74  PHE B CG  1 
ATOM   3355 C  CD1 . PHE B 1 74  ? -25.819 14.264 23.340  1.00 30.95  ?  74  PHE B CD1 1 
ATOM   3356 C  CD2 . PHE B 1 74  ? -28.047 14.776 22.677  1.00 33.96  ?  74  PHE B CD2 1 
ATOM   3357 C  CE1 . PHE B 1 74  ? -26.074 12.920 23.148  1.00 31.48  ?  74  PHE B CE1 1 
ATOM   3358 C  CE2 . PHE B 1 74  ? -28.308 13.425 22.500  1.00 33.85  ?  74  PHE B CE2 1 
ATOM   3359 C  CZ  . PHE B 1 74  ? -27.322 12.500 22.735  1.00 32.85  ?  74  PHE B CZ  1 
ATOM   3360 N  N   . SER B 1 75  ? -25.204 18.881 25.788  1.00 34.59  ?  75  SER B N   1 
ATOM   3361 C  CA  . SER B 1 75  ? -24.916 20.266 26.263  1.00 33.53  ?  75  SER B CA  1 
ATOM   3362 C  C   . SER B 1 75  ? -23.763 20.907 25.493  1.00 33.84  ?  75  SER B C   1 
ATOM   3363 O  O   . SER B 1 75  ? -22.659 20.298 25.503  1.00 36.83  ?  75  SER B O   1 
ATOM   3364 C  CB  . SER B 1 75  ? -24.580 20.290 27.719  1.00 29.64  ?  75  SER B CB  1 
ATOM   3365 O  OG  . SER B 1 75  ? -24.202 21.598 28.089  1.00 27.19  ?  75  SER B OG  1 
ATOM   3366 N  N   . LEU B 1 76  ? -23.992 22.117 24.957  1.00 30.93  ?  76  LEU B N   1 
ATOM   3367 C  CA  . LEU B 1 76  ? -22.947 22.981 24.353  1.00 32.11  ?  76  LEU B CA  1 
ATOM   3368 C  C   . LEU B 1 76  ? -22.111 23.635 25.462  1.00 34.26  ?  76  LEU B C   1 
ATOM   3369 O  O   . LEU B 1 76  ? -20.875 23.605 25.406  1.00 39.05  ?  76  LEU B O   1 
ATOM   3370 C  CB  . LEU B 1 76  ? -23.581 24.043 23.445  1.00 31.54  ?  76  LEU B CB  1 
ATOM   3371 C  CG  . LEU B 1 76  ? -22.571 25.015 22.810  1.00 34.52  ?  76  LEU B CG  1 
ATOM   3372 C  CD1 . LEU B 1 76  ? -21.426 24.271 22.115  1.00 32.30  ?  76  LEU B CD1 1 
ATOM   3373 C  CD2 . LEU B 1 76  ? -23.231 25.957 21.829  1.00 35.50  ?  76  LEU B CD2 1 
ATOM   3374 N  N   . LYS B 1 77  ? -22.774 24.285 26.400  1.00 40.57  ?  77  LYS B N   1 
ATOM   3375 C  CA  . LYS B 1 77  ? -22.149 24.954 27.565  1.00 39.68  ?  77  LYS B CA  1 
ATOM   3376 C  C   . LYS B 1 77  ? -21.069 24.009 28.121  1.00 34.79  ?  77  LYS B C   1 
ATOM   3377 O  O   . LYS B 1 77  ? -19.914 24.455 28.303  1.00 31.94  ?  77  LYS B O   1 
ATOM   3378 C  CB  . LYS B 1 77  ? -23.293 25.325 28.520  1.00 43.07  ?  77  LYS B CB  1 
ATOM   3379 N  N   . ASP B 1 78  ? -21.403 22.729 28.310  1.00 35.83  ?  78  ASP B N   1 
ATOM   3380 C  CA  . ASP B 1 78  ? -20.590 21.760 29.106  1.00 37.87  ?  78  ASP B CA  1 
ATOM   3381 C  C   . ASP B 1 78  ? -19.349 21.265 28.357  1.00 37.01  ?  78  ASP B C   1 
ATOM   3382 O  O   . ASP B 1 78  ? -18.561 20.539 29.006  1.00 35.82  ?  78  ASP B O   1 
ATOM   3383 C  CB  . ASP B 1 78  ? -21.413 20.574 29.603  1.00 36.33  ?  78  ASP B CB  1 
ATOM   3384 C  CG  . ASP B 1 78  ? -22.349 20.971 30.729  1.00 39.72  ?  78  ASP B CG  1 
ATOM   3385 O  OD1 . ASP B 1 78  ? -21.993 21.862 31.497  1.00 45.97  ?  78  ASP B OD1 1 
ATOM   3386 O  OD2 . ASP B 1 78  ? -23.437 20.420 30.794  1.00 46.48  ?  78  ASP B OD2 1 
ATOM   3387 N  N   . THR B 1 79  ? -19.171 21.646 27.083  1.00 36.32  ?  79  THR B N   1 
ATOM   3388 C  CA  . THR B 1 79  ? -17.991 21.295 26.248  1.00 35.52  ?  79  THR B CA  1 
ATOM   3389 C  C   . THR B 1 79  ? -16.753 22.066 26.697  1.00 33.80  ?  79  THR B C   1 
ATOM   3390 O  O   . THR B 1 79  ? -15.665 21.573 26.417  1.00 31.32  ?  79  THR B O   1 
ATOM   3391 C  CB  . THR B 1 79  ? -18.248 21.509 24.763  1.00 33.69  ?  79  THR B CB  1 
ATOM   3392 O  OG1 . THR B 1 79  ? -18.559 22.885 24.548  1.00 32.94  ?  79  THR B OG1 1 
ATOM   3393 C  CG2 . THR B 1 79  ? -19.357 20.604 24.288  1.00 37.43  ?  79  THR B CG2 1 
ATOM   3394 N  N   . ALA B 1 80  ? -16.923 23.181 27.406  1.00 37.27  ?  80  ALA B N   1 
ATOM   3395 C  CA  . ALA B 1 80  ? -15.814 23.998 27.966  1.00 42.92  ?  80  ALA B CA  1 
ATOM   3396 C  C   . ALA B 1 80  ? -15.432 23.565 29.395  1.00 41.75  ?  80  ALA B C   1 
ATOM   3397 O  O   . ALA B 1 80  ? -14.517 24.177 29.969  1.00 38.73  ?  80  ALA B O   1 
ATOM   3398 C  CB  . ALA B 1 80  ? -16.220 25.456 27.938  1.00 44.19  ?  80  ALA B CB  1 
ATOM   3399 N  N   . ASN B 1 81  ? -16.151 22.621 30.003  1.00 45.02  ?  81  ASN B N   1 
ATOM   3400 C  CA  . ASN B 1 81  ? -15.866 22.204 31.401  1.00 47.45  ?  81  ASN B CA  1 
ATOM   3401 C  C   . ASN B 1 81  ? -14.445 21.660 31.422  1.00 50.05  ?  81  ASN B C   1 
ATOM   3402 O  O   . ASN B 1 81  ? -13.976 21.098 30.433  1.00 45.39  ?  81  ASN B O   1 
ATOM   3403 C  CB  . ASN B 1 81  ? -16.834 21.156 31.968  1.00 44.40  ?  81  ASN B CB  1 
ATOM   3404 C  CG  . ASN B 1 81  ? -18.267 21.641 32.079  1.00 45.38  ?  81  ASN B CG  1 
ATOM   3405 O  OD1 . ASN B 1 81  ? -18.555 22.830 31.950  1.00 46.18  ?  81  ASN B OD1 1 
ATOM   3406 N  ND2 . ASN B 1 81  ? -19.188 20.719 32.309  1.00 45.06  ?  81  ASN B ND2 1 
ATOM   3407 N  N   . PRO B 1 82  ? -13.705 21.862 32.532  1.00 52.53  ?  82  PRO B N   1 
ATOM   3408 C  CA  . PRO B 1 82  ? -12.423 21.194 32.723  1.00 49.08  ?  82  PRO B CA  1 
ATOM   3409 C  C   . PRO B 1 82  ? -12.625 19.679 32.684  1.00 46.25  ?  82  PRO B C   1 
ATOM   3410 O  O   . PRO B 1 82  ? -13.607 19.195 33.169  1.00 55.85  ?  82  PRO B O   1 
ATOM   3411 C  CB  . PRO B 1 82  ? -12.009 21.624 34.129  1.00 48.57  ?  82  PRO B CB  1 
ATOM   3412 C  CG  . PRO B 1 82  ? -12.729 22.929 34.348  1.00 49.93  ?  82  PRO B CG  1 
ATOM   3413 C  CD  . PRO B 1 82  ? -14.051 22.759 33.642  1.00 48.71  ?  82  PRO B CD  1 
ATOM   3414 N  N   . GLY B 1 83  ? -11.698 18.968 32.077  1.00 42.86  ?  83  GLY B N   1 
ATOM   3415 C  CA  . GLY B 1 83  ? -11.609 17.516 32.258  1.00 42.40  ?  83  GLY B CA  1 
ATOM   3416 C  C   . GLY B 1 83  ? -12.570 16.749 31.384  1.00 41.51  ?  83  GLY B C   1 
ATOM   3417 O  O   . GLY B 1 83  ? -12.484 15.519 31.432  1.00 41.65  ?  83  GLY B O   1 
ATOM   3418 N  N   . VAL B 1 84  ? -13.408 17.408 30.574  1.00 38.32  ?  84  VAL B N   1 
ATOM   3419 C  CA  . VAL B 1 84  ? -14.253 16.693 29.568  1.00 37.58  ?  84  VAL B CA  1 
ATOM   3420 C  C   . VAL B 1 84  ? -13.448 16.361 28.308  1.00 36.90  ?  84  VAL B C   1 
ATOM   3421 O  O   . VAL B 1 84  ? -12.412 16.954 28.027  1.00 35.54  ?  84  VAL B O   1 
ATOM   3422 C  CB  . VAL B 1 84  ? -15.549 17.455 29.245  1.00 39.98  ?  84  VAL B CB  1 
ATOM   3423 C  CG1 . VAL B 1 84  ? -16.310 17.770 30.523  1.00 42.07  ?  84  VAL B CG1 1 
ATOM   3424 C  CG2 . VAL B 1 84  ? -15.309 18.704 28.421  1.00 38.77  ?  84  VAL B CG2 1 
ATOM   3425 N  N   . PRO B 1 85  ? -13.853 15.342 27.516  1.00 35.20  ?  85  PRO B N   1 
ATOM   3426 C  CA  . PRO B 1 85  ? -13.179 15.091 26.248  1.00 34.12  ?  85  PRO B CA  1 
ATOM   3427 C  C   . PRO B 1 85  ? -13.411 16.281 25.289  1.00 38.98  ?  85  PRO B C   1 
ATOM   3428 O  O   . PRO B 1 85  ? -14.510 16.879 25.279  1.00 35.19  ?  85  PRO B O   1 
ATOM   3429 C  CB  . PRO B 1 85  ? -13.766 13.749 25.795  1.00 29.12  ?  85  PRO B CB  1 
ATOM   3430 C  CG  . PRO B 1 85  ? -15.064 13.627 26.514  1.00 29.56  ?  85  PRO B CG  1 
ATOM   3431 C  CD  . PRO B 1 85  ? -14.926 14.387 27.801  1.00 29.51  ?  85  PRO B CD  1 
ATOM   3432 N  N   . ARG B 1 86  ? -12.358 16.634 24.541  1.00 40.01  ?  86  ARG B N   1 
ATOM   3433 C  CA  . ARG B 1 86  ? -12.255 17.871 23.722  1.00 43.61  ?  86  ARG B CA  1 
ATOM   3434 C  C   . ARG B 1 86  ? -11.954 17.446 22.282  1.00 39.72  ?  86  ARG B C   1 
ATOM   3435 O  O   . ARG B 1 86  ? -11.162 16.519 22.073  1.00 38.04  ?  86  ARG B O   1 
ATOM   3436 C  CB  . ARG B 1 86  ? -11.139 18.807 24.210  1.00 48.61  ?  86  ARG B CB  1 
ATOM   3437 C  CG  . ARG B 1 86  ? -11.329 19.445 25.585  1.00 57.54  ?  86  ARG B CG  1 
ATOM   3438 C  CD  . ARG B 1 86  ? -12.366 20.563 25.640  1.00 74.11  ?  86  ARG B CD  1 
ATOM   3439 N  NE  . ARG B 1 86  ? -12.142 21.560 24.590  1.00 88.96  ?  86  ARG B NE  1 
ATOM   3440 C  CZ  . ARG B 1 86  ? -13.025 22.467 24.152  1.00 89.24  ?  86  ARG B CZ  1 
ATOM   3441 N  NH1 . ARG B 1 86  ? -14.237 22.545 24.674  1.00 90.71  ?  86  ARG B NH1 1 
ATOM   3442 N  NH2 . ARG B 1 86  ? -12.687 23.294 23.171  1.00 92.41  ?  86  ARG B NH2 1 
ATOM   3443 N  N   . GLN B 1 87  ? -12.552 18.110 21.304  1.00 34.49  ?  87  GLN B N   1 
ATOM   3444 C  CA  . GLN B 1 87  ? -12.172 17.859 19.903  1.00 32.90  ?  87  GLN B CA  1 
ATOM   3445 C  C   . GLN B 1 87  ? -10.903 18.671 19.594  1.00 31.72  ?  87  GLN B C   1 
ATOM   3446 O  O   . GLN B 1 87  ? -10.174 18.287 18.650  1.00 31.81  ?  87  GLN B O   1 
ATOM   3447 C  CB  . GLN B 1 87  ? -13.380 18.129 19.011  1.00 33.31  ?  87  GLN B CB  1 
ATOM   3448 C  CG  . GLN B 1 87  ? -13.699 19.597 18.853  1.00 32.45  ?  87  GLN B CG  1 
ATOM   3449 C  CD  . GLN B 1 87  ? -14.625 19.809 17.689  1.00 31.27  ?  87  GLN B CD  1 
ATOM   3450 O  OE1 . GLN B 1 87  ? -14.415 19.289 16.600  1.00 33.58  ?  87  GLN B OE1 1 
ATOM   3451 N  NE2 . GLN B 1 87  ? -15.662 20.582 17.920  1.00 30.78  ?  87  GLN B NE2 1 
ATOM   3452 N  N   . TYR B 1 88  ? -10.671 19.755 20.350  1.00 32.02  ?  88  TYR B N   1 
ATOM   3453 C  CA  . TYR B 1 88  ? -9.429  20.577 20.332  1.00 31.76  ?  88  TYR B CA  1 
ATOM   3454 C  C   . TYR B 1 88  ? -9.385  21.474 21.580  1.00 33.56  ?  88  TYR B C   1 
ATOM   3455 O  O   . TYR B 1 88  ? -10.358 21.567 22.316  1.00 36.92  ?  88  TYR B O   1 
ATOM   3456 C  CB  . TYR B 1 88  ? -9.330  21.388 19.037  1.00 31.77  ?  88  TYR B CB  1 
ATOM   3457 C  CG  . TYR B 1 88  ? -10.612 22.070 18.613  1.00 33.55  ?  88  TYR B CG  1 
ATOM   3458 C  CD1 . TYR B 1 88  ? -11.047 23.229 19.238  1.00 32.46  ?  88  TYR B CD1 1 
ATOM   3459 C  CD2 . TYR B 1 88  ? -11.382 21.574 17.572  1.00 32.05  ?  88  TYR B CD2 1 
ATOM   3460 C  CE1 . TYR B 1 88  ? -12.199 23.885 18.839  1.00 31.32  ?  88  TYR B CE1 1 
ATOM   3461 C  CE2 . TYR B 1 88  ? -12.545 22.215 17.170  1.00 33.01  ?  88  TYR B CE2 1 
ATOM   3462 C  CZ  . TYR B 1 88  ? -12.963 23.360 17.820  1.00 30.38  ?  88  TYR B CZ  1 
ATOM   3463 O  OH  . TYR B 1 88  ? -14.114 23.973 17.462  1.00 28.00  ?  88  TYR B OH  1 
ATOM   3464 N  N   . ALA B 1 89  ? -8.239  22.087 21.831  1.00 33.70  ?  89  ALA B N   1 
ATOM   3465 C  CA  . ALA B 1 89  ? -8.002  23.020 22.948  1.00 30.92  ?  89  ALA B CA  1 
ATOM   3466 C  C   . ALA B 1 89  ? -8.998  24.171 22.863  1.00 28.98  ?  89  ALA B C   1 
ATOM   3467 O  O   . ALA B 1 89  ? -9.170  24.684 21.790  1.00 30.04  ?  89  ALA B O   1 
ATOM   3468 C  CB  . ALA B 1 89  ? -6.571  23.536 22.908  1.00 27.01  ?  89  ALA B CB  1 
ATOM   3469 N  N   . LEU B 1 90  ? -9.566  24.552 23.995  1.00 33.90  ?  90  LEU B N   1 
ATOM   3470 C  CA  . LEU B 1 90  ? -10.183 25.864 24.288  1.00 39.32  ?  90  LEU B CA  1 
ATOM   3471 C  C   . LEU B 1 90  ? -9.209  26.965 23.889  1.00 40.51  ?  90  LEU B C   1 
ATOM   3472 O  O   . LEU B 1 90  ? -8.083  26.964 24.449  1.00 37.35  ?  90  LEU B O   1 
ATOM   3473 C  CB  . LEU B 1 90  ? -10.466 25.955 25.795  1.00 45.77  ?  90  LEU B CB  1 
ATOM   3474 C  CG  . LEU B 1 90  ? -11.497 24.975 26.344  1.00 53.16  ?  90  LEU B CG  1 
ATOM   3475 C  CD1 . LEU B 1 90  ? -11.578 25.067 27.866  1.00 55.69  ?  90  LEU B CD1 1 
ATOM   3476 C  CD2 . LEU B 1 90  ? -12.873 25.232 25.744  1.00 54.93  ?  90  LEU B CD2 1 
ATOM   3477 N  N   . THR B 1 91  ? -9.643  27.890 23.020  1.00 40.50  ?  91  THR B N   1 
ATOM   3478 C  CA  . THR B 1 91  ? -8.842  29.073 22.605  1.00 43.93  ?  91  THR B CA  1 
ATOM   3479 C  C   . THR B 1 91  ? -9.387  30.361 23.238  1.00 50.59  ?  91  THR B C   1 
ATOM   3480 O  O   . THR B 1 91  ? -8.691  31.392 23.157  1.00 54.20  ?  91  THR B O   1 
ATOM   3481 C  CB  . THR B 1 91  ? -8.787  29.140 21.083  1.00 44.04  ?  91  THR B CB  1 
ATOM   3482 O  OG1 . THR B 1 91  ? -10.153 29.004 20.687  1.00 44.76  ?  91  THR B OG1 1 
ATOM   3483 C  CG2 . THR B 1 91  ? -7.873  28.077 20.492  1.00 42.53  ?  91  THR B CG2 1 
ATOM   3484 N  N   . ILE B 1 92  ? -10.557 30.294 23.884  1.00 60.78  ?  92  ILE B N   1 
ATOM   3485 C  CA  . ILE B 1 92  ? -11.269 31.436 24.537  1.00 59.93  ?  92  ILE B CA  1 
ATOM   3486 C  C   . ILE B 1 92  ? -11.515 31.062 25.998  1.00 57.93  ?  92  ILE B C   1 
ATOM   3487 O  O   . ILE B 1 92  ? -11.248 29.931 26.396  1.00 60.02  ?  92  ILE B O   1 
ATOM   3488 C  CB  . ILE B 1 92  ? -12.564 31.776 23.758  1.00 65.02  ?  92  ILE B CB  1 
ATOM   3489 C  CG1 . ILE B 1 92  ? -13.471 30.557 23.558  1.00 63.69  ?  92  ILE B CG1 1 
ATOM   3490 C  CG2 . ILE B 1 92  ? -12.235 32.443 22.423  1.00 65.19  ?  92  ILE B CG2 1 
ATOM   3491 C  CD1 . ILE B 1 92  ? -14.785 30.870 22.879  1.00 60.89  ?  92  ILE B CD1 1 
ATOM   3492 N  N   . PRO B 1 93  ? -11.948 31.995 26.880  1.00 65.18  ?  93  PRO B N   1 
ATOM   3493 C  CA  . PRO B 1 93  ? -12.400 31.614 28.223  1.00 64.34  ?  93  PRO B CA  1 
ATOM   3494 C  C   . PRO B 1 93  ? -13.526 30.577 28.164  1.00 64.50  ?  93  PRO B C   1 
ATOM   3495 O  O   . PRO B 1 93  ? -14.276 30.536 27.188  1.00 54.01  ?  93  PRO B O   1 
ATOM   3496 C  CB  . PRO B 1 93  ? -12.863 32.953 28.823  1.00 61.59  ?  93  PRO B CB  1 
ATOM   3497 C  CG  . PRO B 1 93  ? -12.031 33.991 28.108  1.00 55.97  ?  93  PRO B CG  1 
ATOM   3498 C  CD  . PRO B 1 93  ? -11.932 33.456 26.692  1.00 59.96  ?  93  PRO B CD  1 
ATOM   3499 N  N   . PRO B 1 94  ? -13.636 29.652 29.152  1.00 68.37  ?  94  PRO B N   1 
ATOM   3500 C  CA  . PRO B 1 94  ? -14.790 28.748 29.233  1.00 74.09  ?  94  PRO B CA  1 
ATOM   3501 C  C   . PRO B 1 94  ? -16.181 29.425 29.130  1.00 78.26  ?  94  PRO B C   1 
ATOM   3502 O  O   . PRO B 1 94  ? -17.072 28.909 28.449  1.00 70.41  ?  94  PRO B O   1 
ATOM   3503 C  CB  . PRO B 1 94  ? -14.644 28.063 30.608  1.00 69.54  ?  94  PRO B CB  1 
ATOM   3504 C  CG  . PRO B 1 94  ? -13.260 28.426 31.148  1.00 61.34  ?  94  PRO B CG  1 
ATOM   3505 C  CD  . PRO B 1 94  ? -12.612 29.374 30.170  1.00 62.27  ?  94  PRO B CD  1 
ATOM   3506 N  N   . GLU B 1 95  ? -16.330 30.589 29.770  1.00 78.39  ?  95  GLU B N   1 
ATOM   3507 C  CA  . GLU B 1 95  ? -17.608 31.334 29.935  1.00 77.16  ?  95  GLU B CA  1 
ATOM   3508 C  C   . GLU B 1 95  ? -18.181 31.719 28.559  1.00 76.64  ?  95  GLU B C   1 
ATOM   3509 O  O   . GLU B 1 95  ? -19.432 31.683 28.404  1.00 71.91  ?  95  GLU B O   1 
ATOM   3510 C  CB  . GLU B 1 95  ? -17.392 32.566 30.822  1.00 82.46  ?  95  GLU B CB  1 
ATOM   3511 C  CG  . GLU B 1 95  ? -17.053 32.233 32.270  1.00 86.58  ?  95  GLU B CG  1 
ATOM   3512 C  CD  . GLU B 1 95  ? -16.764 33.443 33.149  1.00 84.82  ?  95  GLU B CD  1 
ATOM   3513 O  OE1 . GLU B 1 95  ? -16.641 34.546 32.587  1.00 84.51  ?  95  GLU B OE1 1 
ATOM   3514 O  OE2 . GLU B 1 95  ? -16.636 33.280 34.387  1.00 77.05  ?  95  GLU B OE2 1 
ATOM   3515 N  N   . VAL B 1 96  ? -17.323 32.061 27.593  1.00 68.71  ?  96  VAL B N   1 
ATOM   3516 C  CA  . VAL B 1 96  ? -17.742 32.546 26.238  1.00 72.27  ?  96  VAL B CA  1 
ATOM   3517 C  C   . VAL B 1 96  ? -18.360 31.416 25.378  1.00 71.33  ?  96  VAL B C   1 
ATOM   3518 O  O   . VAL B 1 96  ? -19.126 31.767 24.457  1.00 75.32  ?  96  VAL B O   1 
ATOM   3519 C  CB  . VAL B 1 96  ? -16.573 33.228 25.495  1.00 68.44  ?  96  VAL B CB  1 
ATOM   3520 C  CG1 . VAL B 1 96  ? -17.017 33.783 24.148  1.00 68.00  ?  96  VAL B CG1 1 
ATOM   3521 C  CG2 . VAL B 1 96  ? -15.917 34.314 26.335  1.00 65.86  ?  96  VAL B CG2 1 
ATOM   3522 N  N   . VAL B 1 97  ? -18.056 30.124 25.611  1.00 70.76  ?  97  VAL B N   1 
ATOM   3523 C  CA  . VAL B 1 97  ? -18.573 29.003 24.752  1.00 74.79  ?  97  VAL B CA  1 
ATOM   3524 C  C   . VAL B 1 97  ? -20.082 28.873 25.003  1.00 76.11  ?  97  VAL B C   1 
ATOM   3525 O  O   . VAL B 1 97  ? -20.787 28.318 24.144  1.00 69.33  ?  97  VAL B O   1 
ATOM   3526 C  CB  . VAL B 1 97  ? -17.799 27.672 24.922  1.00 66.84  ?  97  VAL B CB  1 
ATOM   3527 C  CG1 . VAL B 1 97  ? -18.508 26.481 24.274  1.00 59.65  ?  97  VAL B CG1 1 
ATOM   3528 C  CG2 . VAL B 1 97  ? -16.377 27.793 24.370  1.00 60.28  ?  97  VAL B CG2 1 
ATOM   3529 N  N   . ASN B 1 98  ? -20.548 29.452 26.111  1.00 85.19  ?  98  ASN B N   1 
ATOM   3530 C  CA  . ASN B 1 98  ? -21.978 29.681 26.447  1.00 82.99  ?  98  ASN B CA  1 
ATOM   3531 C  C   . ASN B 1 98  ? -22.304 31.177 26.248  1.00 83.67  ?  98  ASN B C   1 
ATOM   3532 O  O   . ASN B 1 98  ? -22.924 31.779 27.151  1.00 91.53  ?  98  ASN B O   1 
ATOM   3533 C  CB  . ASN B 1 98  ? -22.235 29.170 27.869  1.00 74.52  ?  98  ASN B CB  1 
ATOM   3534 C  CG  . ASN B 1 98  ? -23.679 29.263 28.305  1.00 73.43  ?  98  ASN B CG  1 
ATOM   3535 O  OD1 . ASN B 1 98  ? -24.590 28.866 27.580  1.00 66.67  ?  98  ASN B OD1 1 
ATOM   3536 N  ND2 . ASN B 1 98  ? -23.895 29.784 29.500  1.00 78.39  ?  98  ASN B ND2 1 
ATOM   3537 N  N   . ASN B 1 99  ? -21.897 31.777 25.121  1.00 79.28  ?  99  ASN B N   1 
ATOM   3538 C  CA  . ASN B 1 99  ? -22.073 33.237 24.861  1.00 79.41  ?  99  ASN B CA  1 
ATOM   3539 C  C   . ASN B 1 99  ? -23.570 33.601 24.930  1.00 75.00  ?  99  ASN B C   1 
ATOM   3540 O  O   . ASN B 1 99  ? -23.914 34.464 25.770  1.00 59.53  ?  99  ASN B O   1 
ATOM   3541 C  CB  . ASN B 1 99  ? -21.435 33.681 23.537  1.00 76.44  ?  99  ASN B CB  1 
ATOM   3542 C  CG  . ASN B 1 99  ? -21.519 35.177 23.307  1.00 69.22  ?  99  ASN B CG  1 
ATOM   3543 O  OD1 . ASN B 1 99  ? -22.114 35.620 22.326  1.00 72.04  ?  99  ASN B OD1 1 
ATOM   3544 N  ND2 . ASN B 1 99  ? -20.955 35.960 24.214  1.00 60.23  ?  99  ASN B ND2 1 
ATOM   3545 N  N   . MET B 1 100 ? -24.424 32.974 24.103  1.00 68.86  ?  100 MET B N   1 
ATOM   3546 C  CA  . MET B 1 100 ? -25.899 33.220 24.083  1.00 73.65  ?  100 MET B CA  1 
ATOM   3547 C  C   . MET B 1 100 ? -26.518 32.984 25.474  1.00 74.75  ?  100 MET B C   1 
ATOM   3548 O  O   . MET B 1 100 ? -27.468 33.724 25.831  1.00 66.05  ?  100 MET B O   1 
ATOM   3549 C  CB  . MET B 1 100 ? -26.626 32.342 23.058  1.00 70.78  ?  100 MET B CB  1 
ATOM   3550 C  CG  . MET B 1 100 ? -26.735 32.973 21.678  1.00 73.17  ?  100 MET B CG  1 
ATOM   3551 S  SD  . MET B 1 100 ? -27.516 34.624 21.613  1.00 76.50  ?  100 MET B SD  1 
ATOM   3552 C  CE  . MET B 1 100 ? -26.085 35.655 21.310  1.00 76.00  ?  100 MET B CE  1 
ATOM   3553 N  N   . GLY B 1 101 ? -26.031 31.986 26.221  1.00 77.08  ?  101 GLY B N   1 
ATOM   3554 C  CA  . GLY B 1 101 ? -26.435 31.745 27.619  1.00 71.90  ?  101 GLY B CA  1 
ATOM   3555 C  C   . GLY B 1 101 ? -26.293 33.013 28.441  1.00 76.48  ?  101 GLY B C   1 
ATOM   3556 O  O   . GLY B 1 101 ? -27.334 33.550 28.833  1.00 77.56  ?  101 GLY B O   1 
ATOM   3557 N  N   . ASN B 1 102 ? -25.049 33.489 28.624  1.00 85.58  ?  102 ASN B N   1 
ATOM   3558 C  CA  . ASN B 1 102 ? -24.627 34.636 29.484  1.00 90.50  ?  102 ASN B CA  1 
ATOM   3559 C  C   . ASN B 1 102 ? -25.320 35.939 29.050  1.00 91.11  ?  102 ASN B C   1 
ATOM   3560 O  O   . ASN B 1 102 ? -25.832 36.662 29.953  1.00 90.43  ?  102 ASN B O   1 
ATOM   3561 C  CB  . ASN B 1 102 ? -23.107 34.846 29.437  1.00 92.77  ?  102 ASN B CB  1 
ATOM   3562 C  CG  . ASN B 1 102 ? -22.307 33.776 30.155  1.00 96.29  ?  102 ASN B CG  1 
ATOM   3563 O  OD1 . ASN B 1 102 ? -22.854 32.764 30.596  1.00 91.74  ?  102 ASN B OD1 1 
ATOM   3564 N  ND2 . ASN B 1 102 ? -21.006 33.997 30.280  1.00 94.09  ?  102 ASN B ND2 1 
ATOM   3565 N  N   . ILE B 1 103 ? -25.261 36.244 27.741  1.00 83.40  ?  103 ILE B N   1 
ATOM   3566 C  CA  . ILE B 1 103 ? -26.018 37.322 27.021  1.00 82.47  ?  103 ILE B CA  1 
ATOM   3567 C  C   . ILE B 1 103 ? -27.484 37.322 27.481  1.00 84.27  ?  103 ILE B C   1 
ATOM   3568 O  O   . ILE B 1 103 ? -27.980 38.421 27.805  1.00 89.88  ?  103 ILE B O   1 
ATOM   3569 C  CB  . ILE B 1 103 ? -25.925 37.169 25.477  1.00 78.50  ?  103 ILE B CB  1 
ATOM   3570 C  CG1 . ILE B 1 103 ? -24.574 37.655 24.929  1.00 75.54  ?  103 ILE B CG1 1 
ATOM   3571 C  CG2 . ILE B 1 103 ? -27.102 37.859 24.784  1.00 71.73  ?  103 ILE B CG2 1 
ATOM   3572 C  CD1 . ILE B 1 103 ? -24.309 37.358 23.456  1.00 65.59  ?  103 ILE B CD1 1 
ATOM   3573 N  N   . ASN B 1 104 ? -28.156 36.158 27.469  1.00 84.73  ?  104 ASN B N   1 
ATOM   3574 C  CA  . ASN B 1 104 ? -29.597 36.014 27.839  1.00 89.19  ?  104 ASN B CA  1 
ATOM   3575 C  C   . ASN B 1 104 ? -29.786 36.396 29.321  1.00 88.96  ?  104 ASN B C   1 
ATOM   3576 O  O   . ASN B 1 104 ? -30.722 37.176 29.603  1.00 91.97  ?  104 ASN B O   1 
ATOM   3577 C  CB  . ASN B 1 104 ? -30.162 34.621 27.509  1.00 81.08  ?  104 ASN B CB  1 
ATOM   3578 C  CG  . ASN B 1 104 ? -30.277 34.317 26.023  1.00 83.70  ?  104 ASN B CG  1 
ATOM   3579 O  OD1 . ASN B 1 104 ? -30.310 35.211 25.174  1.00 71.83  ?  104 ASN B OD1 1 
ATOM   3580 N  ND2 . ASN B 1 104 ? -30.342 33.039 25.686  1.00 84.09  ?  104 ASN B ND2 1 
ATOM   3581 N  N   . SER B 1 105 ? -28.880 35.945 30.203  1.00 85.67  ?  105 SER B N   1 
ATOM   3582 C  CA  . SER B 1 105 ? -29.003 35.951 31.686  1.00 78.52  ?  105 SER B CA  1 
ATOM   3583 C  C   . SER B 1 105 ? -28.727 37.339 32.294  1.00 75.17  ?  105 SER B C   1 
ATOM   3584 O  O   . SER B 1 105 ? -29.069 37.534 33.489  1.00 63.23  ?  105 SER B O   1 
ATOM   3585 C  CB  . SER B 1 105 ? -28.094 34.906 32.277  1.00 77.24  ?  105 SER B CB  1 
ATOM   3586 O  OG  . SER B 1 105 ? -26.736 35.220 32.006  1.00 75.56  ?  105 SER B OG  1 
ATOM   3587 N  N   . ALA B 1 106 ? -28.184 38.283 31.514  1.00 76.30  ?  106 ALA B N   1 
ATOM   3588 C  CA  . ALA B 1 106 ? -27.780 39.640 31.971  1.00 77.46  ?  106 ALA B CA  1 
ATOM   3589 C  C   . ALA B 1 106 ? -28.748 40.752 31.494  1.00 70.93  ?  106 ALA B C   1 
ATOM   3590 O  O   . ALA B 1 106 ? -28.416 41.951 31.699  1.00 64.27  ?  106 ALA B O   1 
ATOM   3591 C  CB  . ALA B 1 106 ? -26.363 39.892 31.504  1.00 74.07  ?  106 ALA B CB  1 
ATOM   3592 N  N   . GLY B 1 107 ? -29.892 40.403 30.887  1.00 68.91  ?  107 GLY B N   1 
ATOM   3593 C  CA  . GLY B 1 107 ? -30.844 41.362 30.285  1.00 75.39  ?  107 GLY B CA  1 
ATOM   3594 C  C   . GLY B 1 107 ? -30.232 42.110 29.106  1.00 86.10  ?  107 GLY B C   1 
ATOM   3595 O  O   . GLY B 1 107 ? -30.737 43.218 28.786  1.00 89.36  ?  107 GLY B O   1 
ATOM   3596 N  N   . LEU B 1 108 ? -29.187 41.516 28.496  1.00 84.08  ?  108 LEU B N   1 
ATOM   3597 C  CA  . LEU B 1 108 ? -28.368 42.020 27.350  1.00 66.00  ?  108 LEU B CA  1 
ATOM   3598 C  C   . LEU B 1 108 ? -28.970 41.542 26.034  1.00 59.99  ?  108 LEU B C   1 
ATOM   3599 O  O   . LEU B 1 108 ? -28.550 42.051 24.967  1.00 51.75  ?  108 LEU B O   1 
ATOM   3600 C  CB  . LEU B 1 108 ? -26.942 41.467 27.441  1.00 61.69  ?  108 LEU B CB  1 
ATOM   3601 C  CG  . LEU B 1 108 ? -26.125 41.924 28.633  1.00 57.47  ?  108 LEU B CG  1 
ATOM   3602 C  CD1 . LEU B 1 108 ? -24.801 41.174 28.654  1.00 58.97  ?  108 LEU B CD1 1 
ATOM   3603 C  CD2 . LEU B 1 108 ? -25.910 43.429 28.591  1.00 55.81  ?  108 LEU B CD2 1 
ATOM   3604 N  N   . ARG B 1 109 ? -29.868 40.563 26.124  1.00 62.61  ?  109 ARG B N   1 
ATOM   3605 C  CA  . ARG B 1 109 ? -30.486 39.892 24.960  1.00 69.10  ?  109 ARG B CA  1 
ATOM   3606 C  C   . ARG B 1 109 ? -31.056 40.968 24.029  1.00 68.64  ?  109 ARG B C   1 
ATOM   3607 O  O   . ARG B 1 109 ? -31.015 40.756 22.799  1.00 91.55  ?  109 ARG B O   1 
ATOM   3608 C  CB  . ARG B 1 109 ? -31.549 38.877 25.405  1.00 74.12  ?  109 ARG B CB  1 
ATOM   3609 C  CG  . ARG B 1 109 ? -32.110 38.044 24.258  1.00 78.09  ?  109 ARG B CG  1 
ATOM   3610 C  CD  . ARG B 1 109 ? -33.137 36.995 24.642  1.00 84.02  ?  109 ARG B CD  1 
ATOM   3611 N  NE  . ARG B 1 109 ? -33.578 36.251 23.460  1.00 89.40  ?  109 ARG B NE  1 
ATOM   3612 C  CZ  . ARG B 1 109 ? -32.898 35.263 22.869  1.00 85.72  ?  109 ARG B CZ  1 
ATOM   3613 N  NH1 . ARG B 1 109 ? -31.734 34.858 23.351  1.00 83.36  ?  109 ARG B NH1 1 
ATOM   3614 N  NH2 . ARG B 1 109 ? -33.388 34.674 21.791  1.00 78.14  ?  109 ARG B NH2 1 
ATOM   3615 N  N   . ASN B 1 110 ? -31.570 42.080 24.555  1.00 60.29  ?  110 ASN B N   1 
ATOM   3616 C  CA  . ASN B 1 110 ? -32.309 43.042 23.694  1.00 61.22  ?  110 ASN B CA  1 
ATOM   3617 C  C   . ASN B 1 110 ? -31.305 43.833 22.843  1.00 52.38  ?  110 ASN B C   1 
ATOM   3618 O  O   . ASN B 1 110 ? -31.496 43.872 21.616  1.00 46.59  ?  110 ASN B O   1 
ATOM   3619 C  CB  . ASN B 1 110 ? -33.306 43.897 24.483  1.00 67.01  ?  110 ASN B CB  1 
ATOM   3620 C  CG  . ASN B 1 110 ? -34.489 43.068 24.943  1.00 70.20  ?  110 ASN B CG  1 
ATOM   3621 O  OD1 . ASN B 1 110 ? -34.796 42.024 24.361  1.00 61.08  ?  110 ASN B OD1 1 
ATOM   3622 N  ND2 . ASN B 1 110 ? -35.192 43.560 25.952  1.00 73.11  ?  110 ASN B ND2 1 
ATOM   3623 N  N   . ALA B 1 111 ? -30.268 44.409 23.457  1.00 41.71  ?  111 ALA B N   1 
ATOM   3624 C  CA  . ALA B 1 111 ? -29.134 45.032 22.736  1.00 43.12  ?  111 ALA B CA  1 
ATOM   3625 C  C   . ALA B 1 111 ? -28.588 44.052 21.674  1.00 42.88  ?  111 ALA B C   1 
ATOM   3626 O  O   . ALA B 1 111 ? -28.396 44.452 20.502  1.00 36.21  ?  111 ALA B O   1 
ATOM   3627 C  CB  . ALA B 1 111 ? -28.058 45.445 23.718  1.00 43.05  ?  111 ALA B CB  1 
ATOM   3628 N  N   . VAL B 1 112 ? -28.331 42.797 22.049  1.00 40.26  ?  112 VAL B N   1 
ATOM   3629 C  CA  . VAL B 1 112 ? -27.723 41.829 21.107  1.00 40.16  ?  112 VAL B CA  1 
ATOM   3630 C  C   . VAL B 1 112 ? -28.746 41.580 19.993  1.00 40.84  ?  112 VAL B C   1 
ATOM   3631 O  O   . VAL B 1 112 ? -28.380 41.819 18.816  1.00 39.74  ?  112 VAL B O   1 
ATOM   3632 C  CB  . VAL B 1 112 ? -27.202 40.573 21.836  1.00 41.96  ?  112 VAL B CB  1 
ATOM   3633 C  CG1 . VAL B 1 112 ? -26.791 39.448 20.888  1.00 38.83  ?  112 VAL B CG1 1 
ATOM   3634 C  CG2 . VAL B 1 112 ? -26.039 40.941 22.755  1.00 41.90  ?  112 VAL B CG2 1 
ATOM   3635 N  N   . MET B 1 113 ? -29.994 41.238 20.321  1.00 43.93  ?  113 MET B N   1 
ATOM   3636 C  CA  . MET B 1 113 ? -31.004 40.830 19.292  1.00 51.29  ?  113 MET B CA  1 
ATOM   3637 C  C   . MET B 1 113 ? -31.304 42.003 18.340  1.00 46.49  ?  113 MET B C   1 
ATOM   3638 O  O   . MET B 1 113 ? -31.506 41.752 17.151  1.00 54.71  ?  113 MET B O   1 
ATOM   3639 C  CB  . MET B 1 113 ? -32.314 40.296 19.901  1.00 57.05  ?  113 MET B CB  1 
ATOM   3640 C  CG  . MET B 1 113 ? -32.256 38.841 20.495  1.00 63.44  ?  113 MET B CG  1 
ATOM   3641 S  SD  . MET B 1 113 ? -30.976 37.633 19.872  1.00 77.78  ?  113 MET B SD  1 
ATOM   3642 C  CE  . MET B 1 113 ? -31.599 37.152 18.256  1.00 71.39  ?  113 MET B CE  1 
ATOM   3643 N  N   . LYS B 1 114 ? -31.318 43.240 18.819  1.00 43.89  ?  114 LYS B N   1 
ATOM   3644 C  CA  . LYS B 1 114 ? -31.528 44.428 17.956  1.00 50.51  ?  114 LYS B CA  1 
ATOM   3645 C  C   . LYS B 1 114 ? -30.340 44.517 16.984  1.00 47.96  ?  114 LYS B C   1 
ATOM   3646 O  O   . LYS B 1 114 ? -30.575 44.745 15.790  1.00 42.13  ?  114 LYS B O   1 
ATOM   3647 C  CB  . LYS B 1 114 ? -31.691 45.705 18.799  1.00 58.33  ?  114 LYS B CB  1 
ATOM   3648 C  CG  . LYS B 1 114 ? -32.951 45.787 19.660  1.00 63.87  ?  114 LYS B CG  1 
ATOM   3649 C  CD  . LYS B 1 114 ? -33.039 47.070 20.490  1.00 76.25  ?  114 LYS B CD  1 
ATOM   3650 C  CE  . LYS B 1 114 ? -34.294 47.194 21.342  1.00 81.96  ?  114 LYS B CE  1 
ATOM   3651 N  NZ  . LYS B 1 114 ? -34.292 48.451 22.133  1.00 78.91  ?  114 LYS B NZ  1 
ATOM   3652 N  N   . THR B 1 115 ? -29.107 44.336 17.475  1.00 46.72  ?  115 THR B N   1 
ATOM   3653 C  CA  . THR B 1 115 ? -27.862 44.370 16.656  1.00 45.71  ?  115 THR B CA  1 
ATOM   3654 C  C   . THR B 1 115 ? -27.916 43.301 15.547  1.00 44.84  ?  115 THR B C   1 
ATOM   3655 O  O   . THR B 1 115 ? -27.666 43.661 14.376  1.00 40.43  ?  115 THR B O   1 
ATOM   3656 C  CB  . THR B 1 115 ? -26.619 44.184 17.525  1.00 45.63  ?  115 THR B CB  1 
ATOM   3657 O  OG1 . THR B 1 115 ? -26.699 45.205 18.516  1.00 41.16  ?  115 THR B OG1 1 
ATOM   3658 C  CG2 . THR B 1 115 ? -25.331 44.271 16.734  1.00 45.25  ?  115 THR B CG2 1 
ATOM   3659 N  N   . LEU B 1 116 ? -28.267 42.058 15.883  1.00 41.44  ?  116 LEU B N   1 
ATOM   3660 C  CA  . LEU B 1 116 ? -28.303 40.919 14.917  1.00 46.83  ?  116 LEU B CA  1 
ATOM   3661 C  C   . LEU B 1 116 ? -29.455 41.046 13.896  1.00 49.08  ?  116 LEU B C   1 
ATOM   3662 O  O   . LEU B 1 116 ? -29.267 40.554 12.742  1.00 50.71  ?  116 LEU B O   1 
ATOM   3663 C  CB  . LEU B 1 116 ? -28.370 39.600 15.699  1.00 45.34  ?  116 LEU B CB  1 
ATOM   3664 C  CG  . LEU B 1 116 ? -27.165 39.341 16.605  1.00 48.39  ?  116 LEU B CG  1 
ATOM   3665 C  CD1 . LEU B 1 116 ? -27.254 37.979 17.298  1.00 50.55  ?  116 LEU B CD1 1 
ATOM   3666 C  CD2 . LEU B 1 116 ? -25.855 39.496 15.833  1.00 48.59  ?  116 LEU B CD2 1 
ATOM   3667 N  N   . SER B 1 117 ? -30.578 41.691 14.251  1.00 54.20  ?  117 SER B N   1 
ATOM   3668 C  CA  . SER B 1 117 ? -31.755 41.893 13.354  1.00 56.35  ?  117 SER B CA  1 
ATOM   3669 C  C   . SER B 1 117 ? -31.414 42.808 12.180  1.00 56.68  ?  117 SER B C   1 
ATOM   3670 O  O   . SER B 1 117 ? -31.142 43.988 12.393  1.00 59.52  ?  117 SER B O   1 
ATOM   3671 C  CB  . SER B 1 117 ? -32.940 42.452 14.063  1.00 51.63  ?  117 SER B CB  1 
ATOM   3672 O  OG  . SER B 1 117 ? -33.945 42.721 13.097  1.00 52.49  ?  117 SER B OG  1 
ATOM   3673 N  N   . PRO B 1 118 ? -31.454 42.319 10.912  1.00 58.87  ?  118 PRO B N   1 
ATOM   3674 C  CA  . PRO B 1 118 ? -31.213 43.177 9.747   1.00 59.20  ?  118 PRO B CA  1 
ATOM   3675 C  C   . PRO B 1 118 ? -32.291 44.269 9.582   1.00 69.02  ?  118 PRO B C   1 
ATOM   3676 O  O   . PRO B 1 118 ? -31.951 45.347 9.108   1.00 66.28  ?  118 PRO B O   1 
ATOM   3677 C  CB  . PRO B 1 118 ? -31.200 42.206 8.553   1.00 54.77  ?  118 PRO B CB  1 
ATOM   3678 C  CG  . PRO B 1 118 ? -30.986 40.840 9.171   1.00 54.95  ?  118 PRO B CG  1 
ATOM   3679 C  CD  . PRO B 1 118 ? -31.658 40.910 10.527  1.00 57.73  ?  118 PRO B CD  1 
ATOM   3680 N  N   . GLN B 1 119 ? -33.537 43.964 9.985   1.00 72.28  ?  119 GLN B N   1 
ATOM   3681 C  CA  . GLN B 1 119 ? -34.702 44.893 10.031  1.00 69.47  ?  119 GLN B CA  1 
ATOM   3682 C  C   . GLN B 1 119 ? -34.335 46.137 10.836  1.00 65.70  ?  119 GLN B C   1 
ATOM   3683 O  O   . GLN B 1 119 ? -34.689 47.241 10.410  1.00 69.94  ?  119 GLN B O   1 
ATOM   3684 C  CB  . GLN B 1 119 ? -35.916 44.239 10.698  1.00 76.58  ?  119 GLN B CB  1 
ATOM   3685 C  CG  . GLN B 1 119 ? -36.839 43.505 9.731   1.00 83.70  ?  119 GLN B CG  1 
ATOM   3686 C  CD  . GLN B 1 119 ? -36.159 42.431 8.911   1.00 90.17  ?  119 GLN B CD  1 
ATOM   3687 O  OE1 . GLN B 1 119 ? -35.191 41.787 9.335   1.00 85.19  ?  119 GLN B OE1 1 
ATOM   3688 N  NE2 . GLN B 1 119 ? -36.685 42.215 7.715   1.00 90.63  ?  119 GLN B NE2 1 
ATOM   3689 N  N   . ALA B 1 120 ? -33.651 45.960 11.963  1.00 57.81  ?  120 ALA B N   1 
ATOM   3690 C  CA  . ALA B 1 120 ? -33.388 47.035 12.944  1.00 58.10  ?  120 ALA B CA  1 
ATOM   3691 C  C   . ALA B 1 120 ? -32.401 48.084 12.405  1.00 58.63  ?  120 ALA B C   1 
ATOM   3692 O  O   . ALA B 1 120 ? -32.090 48.984 13.170  1.00 56.77  ?  120 ALA B O   1 
ATOM   3693 C  CB  . ALA B 1 120 ? -32.869 46.419 14.219  1.00 55.73  ?  120 ALA B CB  1 
ATOM   3694 N  N   . ASP B 1 121 ? -31.869 47.949 11.181  1.00 61.76  ?  121 ASP B N   1 
ATOM   3695 C  CA  . ASP B 1 121 ? -30.858 48.874 10.582  1.00 55.25  ?  121 ASP B CA  1 
ATOM   3696 C  C   . ASP B 1 121 ? -31.277 49.066 9.125   1.00 54.31  ?  121 ASP B C   1 
ATOM   3697 O  O   . ASP B 1 121 ? -30.823 48.308 8.258   1.00 49.14  ?  121 ASP B O   1 
ATOM   3698 C  CB  . ASP B 1 121 ? -29.422 48.370 10.804  1.00 54.58  ?  121 ASP B CB  1 
ATOM   3699 C  CG  . ASP B 1 121 ? -28.297 49.179 10.153  1.00 54.35  ?  121 ASP B CG  1 
ATOM   3700 O  OD1 . ASP B 1 121 ? -28.612 50.115 9.415   1.00 54.96  ?  121 ASP B OD1 1 
ATOM   3701 O  OD2 . ASP B 1 121 ? -27.097 48.848 10.368  1.00 44.60  ?  121 ASP B OD2 1 
ATOM   3702 N  N   . ARG B 1 122 ? -32.157 50.041 8.903   1.00 64.44  ?  122 ARG B N   1 
ATOM   3703 C  CA  . ARG B 1 122 ? -32.872 50.308 7.627   1.00 67.96  ?  122 ARG B CA  1 
ATOM   3704 C  C   . ARG B 1 122 ? -31.861 50.495 6.477   1.00 62.09  ?  122 ARG B C   1 
ATOM   3705 O  O   . ARG B 1 122 ? -32.216 50.147 5.338   1.00 50.90  ?  122 ARG B O   1 
ATOM   3706 C  CB  . ARG B 1 122 ? -33.783 51.527 7.832   1.00 81.11  ?  122 ARG B CB  1 
ATOM   3707 C  CG  . ARG B 1 122 ? -34.804 51.772 6.728   1.00 94.15  ?  122 ARG B CG  1 
ATOM   3708 C  CD  . ARG B 1 122 ? -36.050 50.904 6.849   1.00 104.48 ?  122 ARG B CD  1 
ATOM   3709 N  NE  . ARG B 1 122 ? -37.203 51.497 6.171   1.00 109.26 ?  122 ARG B NE  1 
ATOM   3710 C  CZ  . ARG B 1 122 ? -37.538 51.303 4.893   1.00 104.34 ?  122 ARG B CZ  1 
ATOM   3711 N  NH1 . ARG B 1 122 ? -36.819 50.511 4.117   1.00 108.83 ?  122 ARG B NH1 1 
ATOM   3712 N  NH2 . ARG B 1 122 ? -38.603 51.902 4.389   1.00 99.31  ?  122 ARG B NH2 1 
ATOM   3713 N  N   . GLU B 1 123 ? -30.652 51.013 6.752   1.00 57.48  ?  123 GLU B N   1 
ATOM   3714 C  CA  . GLU B 1 123 ? -29.628 51.375 5.724   1.00 54.40  ?  123 GLU B CA  1 
ATOM   3715 C  C   . GLU B 1 123 ? -28.624 50.229 5.499   1.00 42.03  ?  123 GLU B C   1 
ATOM   3716 O  O   . GLU B 1 123 ? -27.810 50.348 4.598   1.00 38.20  ?  123 GLU B O   1 
ATOM   3717 C  CB  . GLU B 1 123 ? -28.881 52.656 6.126   1.00 60.84  ?  123 GLU B CB  1 
ATOM   3718 C  CG  . GLU B 1 123 ? -29.730 53.915 6.029   1.00 67.80  ?  123 GLU B CG  1 
ATOM   3719 C  CD  . GLU B 1 123 ? -30.872 54.009 7.033   1.00 77.39  ?  123 GLU B CD  1 
ATOM   3720 O  OE1 . GLU B 1 123 ? -30.794 53.349 8.096   1.00 77.95  ?  123 GLU B OE1 1 
ATOM   3721 O  OE2 . GLU B 1 123 ? -31.854 54.724 6.749   1.00 85.60  ?  123 GLU B OE2 1 
ATOM   3722 N  N   . LEU B 1 124 ? -28.663 49.155 6.279   1.00 40.08  ?  124 LEU B N   1 
ATOM   3723 C  CA  . LEU B 1 124 ? -27.661 48.050 6.202   1.00 40.29  ?  124 LEU B CA  1 
ATOM   3724 C  C   . LEU B 1 124 ? -27.501 47.554 4.756   1.00 38.10  ?  124 LEU B C   1 
ATOM   3725 O  O   . LEU B 1 124 ? -26.344 47.541 4.246   1.00 35.79  ?  124 LEU B O   1 
ATOM   3726 C  CB  . LEU B 1 124 ? -28.098 46.894 7.099   1.00 38.48  ?  124 LEU B CB  1 
ATOM   3727 C  CG  . LEU B 1 124 ? -27.064 45.785 7.215   1.00 42.53  ?  124 LEU B CG  1 
ATOM   3728 C  CD1 . LEU B 1 124 ? -25.708 46.355 7.637   1.00 37.73  ?  124 LEU B CD1 1 
ATOM   3729 C  CD2 . LEU B 1 124 ? -27.561 44.705 8.174   1.00 47.01  ?  124 LEU B CD2 1 
ATOM   3730 N  N   . GLY B 1 125 ? -28.619 47.162 4.131   1.00 32.54  ?  125 GLY B N   1 
ATOM   3731 C  CA  . GLY B 1 125 ? -28.673 46.703 2.740   1.00 29.33  ?  125 GLY B CA  1 
ATOM   3732 C  C   . GLY B 1 125 ? -27.866 47.622 1.839   1.00 28.69  ?  125 GLY B C   1 
ATOM   3733 O  O   . GLY B 1 125 ? -26.947 47.109 1.121   1.00 27.88  ?  125 GLY B O   1 
ATOM   3734 N  N   . GLY B 1 126 ? -28.202 48.919 1.821   1.00 25.53  ?  126 GLY B N   1 
ATOM   3735 C  CA  . GLY B 1 126 ? -27.607 49.866 0.867   1.00 23.37  ?  126 GLY B CA  1 
ATOM   3736 C  C   . GLY B 1 126 ? -26.138 50.000 1.175   1.00 27.49  ?  126 GLY B C   1 
ATOM   3737 O  O   . GLY B 1 126 ? -25.316 50.113 0.242   1.00 33.16  ?  126 GLY B O   1 
ATOM   3738 N  N   . TRP B 1 127 ? -25.796 49.988 2.458   1.00 28.56  ?  127 TRP B N   1 
ATOM   3739 C  CA  . TRP B 1 127 ? -24.396 50.166 2.901   1.00 31.90  ?  127 TRP B CA  1 
ATOM   3740 C  C   . TRP B 1 127 ? -23.602 48.888 2.547   1.00 32.17  ?  127 TRP B C   1 
ATOM   3741 O  O   . TRP B 1 127 ? -22.539 49.047 1.907   1.00 33.16  ?  127 TRP B O   1 
ATOM   3742 C  CB  . TRP B 1 127 ? -24.347 50.573 4.385   1.00 32.46  ?  127 TRP B CB  1 
ATOM   3743 C  CG  . TRP B 1 127 ? -22.974 50.860 4.929   1.00 34.46  ?  127 TRP B CG  1 
ATOM   3744 C  CD1 . TRP B 1 127 ? -22.378 52.080 5.072   1.00 36.87  ?  127 TRP B CD1 1 
ATOM   3745 C  CD2 . TRP B 1 127 ? -22.044 49.910 5.482   1.00 35.30  ?  127 TRP B CD2 1 
ATOM   3746 N  NE1 . TRP B 1 127 ? -21.139 51.956 5.653   1.00 36.06  ?  127 TRP B NE1 1 
ATOM   3747 C  CE2 . TRP B 1 127 ? -20.902 50.635 5.902   1.00 38.08  ?  127 TRP B CE2 1 
ATOM   3748 C  CE3 . TRP B 1 127 ? -22.051 48.522 5.638   1.00 35.62  ?  127 TRP B CE3 1 
ATOM   3749 C  CZ2 . TRP B 1 127 ? -19.787 50.015 6.464   1.00 38.42  ?  127 TRP B CZ2 1 
ATOM   3750 C  CZ3 . TRP B 1 127 ? -20.948 47.911 6.195   1.00 38.57  ?  127 TRP B CZ3 1 
ATOM   3751 C  CH2 . TRP B 1 127 ? -19.836 48.647 6.608   1.00 37.25  ?  127 TRP B CH2 1 
ATOM   3752 N  N   . LEU B 1 128 ? -24.088 47.680 2.867   1.00 27.78  ?  128 LEU B N   1 
ATOM   3753 C  CA  . LEU B 1 128 ? -23.426 46.407 2.431   1.00 32.33  ?  128 LEU B CA  1 
ATOM   3754 C  C   . LEU B 1 128 ? -23.240 46.417 0.904   1.00 33.39  ?  128 LEU B C   1 
ATOM   3755 O  O   . LEU B 1 128 ? -22.146 46.092 0.388   1.00 32.34  ?  128 LEU B O   1 
ATOM   3756 C  CB  . LEU B 1 128 ? -24.245 45.183 2.875   1.00 32.42  ?  128 LEU B CB  1 
ATOM   3757 C  CG  . LEU B 1 128 ? -24.148 44.842 4.367   1.00 34.71  ?  128 LEU B CG  1 
ATOM   3758 C  CD1 . LEU B 1 128 ? -24.987 43.631 4.715   1.00 34.37  ?  128 LEU B CD1 1 
ATOM   3759 C  CD2 . LEU B 1 128 ? -22.690 44.630 4.801   1.00 36.75  ?  128 LEU B CD2 1 
ATOM   3760 N  N   . GLU B 1 129 ? -24.265 46.850 0.190   1.00 35.85  ?  129 GLU B N   1 
ATOM   3761 C  CA  . GLU B 1 129 ? -24.252 46.850 -1.286  1.00 37.44  ?  129 GLU B CA  1 
ATOM   3762 C  C   . GLU B 1 129 ? -23.129 47.766 -1.758  1.00 34.22  ?  129 GLU B C   1 
ATOM   3763 O  O   . GLU B 1 129 ? -22.347 47.307 -2.586  1.00 36.48  ?  129 GLU B O   1 
ATOM   3764 C  CB  . GLU B 1 129 ? -25.620 47.253 -1.828  1.00 40.36  ?  129 GLU B CB  1 
ATOM   3765 C  CG  . GLU B 1 129 ? -25.679 47.177 -3.333  1.00 44.04  ?  129 GLU B CG  1 
ATOM   3766 C  CD  . GLU B 1 129 ? -27.086 47.275 -3.874  1.00 49.80  ?  129 GLU B CD  1 
ATOM   3767 O  OE1 . GLU B 1 129 ? -28.042 47.008 -3.075  1.00 51.44  ?  129 GLU B OE1 1 
ATOM   3768 O  OE2 . GLU B 1 129 ? -27.216 47.623 -5.086  1.00 47.47  ?  129 GLU B OE2 1 
ATOM   3769 N  N   . ALA B 1 130 ? -23.061 48.991 -1.231  1.00 31.32  ?  130 ALA B N   1 
ATOM   3770 C  CA  . ALA B 1 130 ? -22.010 49.995 -1.527  1.00 30.89  ?  130 ALA B CA  1 
ATOM   3771 C  C   . ALA B 1 130 ? -20.616 49.413 -1.195  1.00 29.17  ?  130 ALA B C   1 
ATOM   3772 O  O   . ALA B 1 130 ? -19.766 49.467 -2.069  1.00 28.48  ?  130 ALA B O   1 
ATOM   3773 C  CB  . ALA B 1 130 ? -22.323 51.281 -0.772  1.00 29.91  ?  130 ALA B CB  1 
ATOM   3774 N  N   . GLN B 1 131 ? -20.404 48.798 -0.016  1.00 32.20  ?  131 GLN B N   1 
ATOM   3775 C  CA  . GLN B 1 131 ? -19.119 48.132 0.366   1.00 33.54  ?  131 GLN B CA  1 
ATOM   3776 C  C   . GLN B 1 131 ? -18.729 47.084 -0.676  1.00 32.53  ?  131 GLN B C   1 
ATOM   3777 O  O   . GLN B 1 131 ? -17.570 47.108 -1.109  1.00 34.25  ?  131 GLN B O   1 
ATOM   3778 C  CB  . GLN B 1 131 ? -19.195 47.424 1.712   1.00 35.49  ?  131 GLN B CB  1 
ATOM   3779 C  CG  . GLN B 1 131 ? -19.329 48.373 2.887   1.00 40.95  ?  131 GLN B CG  1 
ATOM   3780 C  CD  . GLN B 1 131 ? -18.256 49.429 2.878   1.00 44.30  ?  131 GLN B CD  1 
ATOM   3781 O  OE1 . GLN B 1 131 ? -17.111 49.191 3.295   1.00 40.69  ?  131 GLN B OE1 1 
ATOM   3782 N  NE2 . GLN B 1 131 ? -18.644 50.605 2.402   1.00 41.67  ?  131 GLN B NE2 1 
ATOM   3783 N  N   . ALA B 1 132 ? -19.652 46.197 -1.058  1.00 31.47  ?  132 ALA B N   1 
ATOM   3784 C  CA  . ALA B 1 132 ? -19.368 45.081 -1.995  1.00 33.60  ?  132 ALA B CA  1 
ATOM   3785 C  C   . ALA B 1 132 ? -18.937 45.667 -3.333  1.00 31.06  ?  132 ALA B C   1 
ATOM   3786 O  O   . ALA B 1 132 ? -17.986 45.138 -3.932  1.00 30.29  ?  132 ALA B O   1 
ATOM   3787 C  CB  . ALA B 1 132 ? -20.570 44.170 -2.152  1.00 35.20  ?  132 ALA B CB  1 
ATOM   3788 N  N   . HIS B 1 133 ? -19.592 46.754 -3.749  1.00 30.52  ?  133 HIS B N   1 
ATOM   3789 C  CA  . HIS B 1 133 ? -19.376 47.393 -5.074  1.00 33.10  ?  133 HIS B CA  1 
ATOM   3790 C  C   . HIS B 1 133 ? -17.990 48.018 -5.076  1.00 30.25  ?  133 HIS B C   1 
ATOM   3791 O  O   . HIS B 1 133 ? -17.237 47.679 -5.978  1.00 33.13  ?  133 HIS B O   1 
ATOM   3792 C  CB  . HIS B 1 133 ? -20.503 48.368 -5.457  1.00 35.58  ?  133 HIS B CB  1 
ATOM   3793 C  CG  . HIS B 1 133 ? -21.651 47.694 -6.130  1.00 38.98  ?  133 HIS B CG  1 
ATOM   3794 N  ND1 . HIS B 1 133 ? -22.644 47.043 -5.441  1.00 40.48  ?  133 HIS B ND1 1 
ATOM   3795 C  CD2 . HIS B 1 133 ? -21.931 47.515 -7.428  1.00 44.36  ?  133 HIS B CD2 1 
ATOM   3796 C  CE1 . HIS B 1 133 ? -23.488 46.509 -6.278  1.00 41.43  ?  133 HIS B CE1 1 
ATOM   3797 N  NE2 . HIS B 1 133 ? -23.069 46.774 -7.499  1.00 43.12  ?  133 HIS B NE2 1 
ATOM   3798 N  N   . GLN B 1 134 ? -17.655 48.812 -4.066  1.00 31.74  ?  134 GLN B N   1 
ATOM   3799 C  CA  . GLN B 1 134 ? -16.345 49.521 -3.988  1.00 37.76  ?  134 GLN B CA  1 
ATOM   3800 C  C   . GLN B 1 134 ? -15.188 48.521 -3.898  1.00 32.98  ?  134 GLN B C   1 
ATOM   3801 O  O   . GLN B 1 134 ? -14.125 48.799 -4.511  1.00 31.67  ?  134 GLN B O   1 
ATOM   3802 C  CB  . GLN B 1 134 ? -16.253 50.475 -2.794  1.00 37.23  ?  134 GLN B CB  1 
ATOM   3803 C  CG  . GLN B 1 134 ? -17.217 51.637 -2.878  1.00 41.24  ?  134 GLN B CG  1 
ATOM   3804 C  CD  . GLN B 1 134 ? -16.974 52.591 -1.740  1.00 43.99  ?  134 GLN B CD  1 
ATOM   3805 O  OE1 . GLN B 1 134 ? -16.629 52.171 -0.641  1.00 50.20  ?  134 GLN B OE1 1 
ATOM   3806 N  NE2 . GLN B 1 134 ? -17.119 53.881 -1.999  1.00 44.72  ?  134 GLN B NE2 1 
ATOM   3807 N  N   . LEU B 1 135 ? -15.360 47.419 -3.163  1.00 30.26  ?  135 LEU B N   1 
ATOM   3808 C  CA  . LEU B 1 135 ? -14.266 46.412 -3.002  1.00 32.27  ?  135 LEU B CA  1 
ATOM   3809 C  C   . LEU B 1 135 ? -13.979 45.755 -4.352  1.00 31.66  ?  135 LEU B C   1 
ATOM   3810 O  O   . LEU B 1 135 ? -12.811 45.702 -4.757  1.00 33.42  ?  135 LEU B O   1 
ATOM   3811 C  CB  . LEU B 1 135 ? -14.665 45.370 -1.953  1.00 33.52  ?  135 LEU B CB  1 
ATOM   3812 C  CG  . LEU B 1 135 ? -14.650 45.866 -0.502  1.00 31.21  ?  135 LEU B CG  1 
ATOM   3813 C  CD1 . LEU B 1 135 ? -15.322 44.840 0.428   1.00 28.80  ?  135 LEU B CD1 1 
ATOM   3814 C  CD2 . LEU B 1 135 ? -13.229 46.212 -0.065  1.00 26.14  ?  135 LEU B CD2 1 
ATOM   3815 N  N   . LEU B 1 136 ? -15.023 45.298 -5.038  1.00 34.09  ?  136 LEU B N   1 
ATOM   3816 C  CA  . LEU B 1 136 ? -14.918 44.725 -6.408  1.00 33.34  ?  136 LEU B CA  1 
ATOM   3817 C  C   . LEU B 1 136 ? -14.434 45.797 -7.407  1.00 33.02  ?  136 LEU B C   1 
ATOM   3818 O  O   . LEU B 1 136 ? -13.591 45.459 -8.233  1.00 36.53  ?  136 LEU B O   1 
ATOM   3819 C  CB  . LEU B 1 136 ? -16.280 44.142 -6.797  1.00 32.98  ?  136 LEU B CB  1 
ATOM   3820 C  CG  . LEU B 1 136 ? -16.786 42.978 -5.940  1.00 33.65  ?  136 LEU B CG  1 
ATOM   3821 C  CD1 . LEU B 1 136 ? -18.285 42.805 -6.083  1.00 32.66  ?  136 LEU B CD1 1 
ATOM   3822 C  CD2 . LEU B 1 136 ? -16.096 41.676 -6.299  1.00 35.23  ?  136 LEU B CD2 1 
ATOM   3823 N  N   . ASP B 1 137 ? -14.931 47.041 -7.359  1.00 33.10  ?  137 ASP B N   1 
ATOM   3824 C  CA  . ASP B 1 137 ? -14.434 48.150 -8.229  1.00 34.31  ?  137 ASP B CA  1 
ATOM   3825 C  C   . ASP B 1 137 ? -12.904 48.282 -8.077  1.00 33.32  ?  137 ASP B C   1 
ATOM   3826 O  O   . ASP B 1 137 ? -12.222 48.541 -9.086  1.00 30.34  ?  137 ASP B O   1 
ATOM   3827 C  CB  . ASP B 1 137 ? -15.194 49.464 -7.983  1.00 35.02  ?  137 ASP B CB  1 
ATOM   3828 C  CG  . ASP B 1 137 ? -16.608 49.485 -8.573  1.00 37.00  ?  137 ASP B CG  1 
ATOM   3829 O  OD1 . ASP B 1 137 ? -16.802 48.855 -9.624  1.00 41.19  ?  137 ASP B OD1 1 
ATOM   3830 O  OD2 . ASP B 1 137 ? -17.535 50.100 -7.962  1.00 34.73  ?  137 ASP B OD2 1 
ATOM   3831 N  N   . ARG B 1 138 ? -12.362 48.059 -6.875  1.00 37.06  ?  138 ARG B N   1 
ATOM   3832 C  CA  . ARG B 1 138 ? -10.905 48.167 -6.604  1.00 38.43  ?  138 ARG B CA  1 
ATOM   3833 C  C   . ARG B 1 138 ? -10.177 47.003 -7.268  1.00 37.44  ?  138 ARG B C   1 
ATOM   3834 O  O   . ARG B 1 138 ? -9.065  47.213 -7.758  1.00 42.18  ?  138 ARG B O   1 
ATOM   3835 C  CB  . ARG B 1 138 ? -10.650 48.199 -5.096  1.00 49.97  ?  138 ARG B CB  1 
ATOM   3836 C  CG  . ARG B 1 138 ? -9.243  48.621 -4.684  1.00 53.51  ?  138 ARG B CG  1 
ATOM   3837 C  CD  . ARG B 1 138 ? -9.160  48.873 -3.187  1.00 58.78  ?  138 ARG B CD  1 
ATOM   3838 N  NE  . ARG B 1 138 ? -7.818  48.668 -2.641  1.00 69.44  ?  138 ARG B NE  1 
ATOM   3839 C  CZ  . ARG B 1 138 ? -6.814  49.551 -2.679  1.00 72.82  ?  138 ARG B CZ  1 
ATOM   3840 N  NH1 . ARG B 1 138 ? -6.959  50.737 -3.251  1.00 76.17  ?  138 ARG B NH1 1 
ATOM   3841 N  NH2 . ARG B 1 138 ? -5.653  49.239 -2.135  1.00 70.24  ?  138 ARG B NH2 1 
ATOM   3842 N  N   . LEU B 1 139 ? -10.780 45.814 -7.318  1.00 33.98  ?  139 LEU B N   1 
ATOM   3843 C  CA  . LEU B 1 139 ? -10.114 44.654 -7.962  1.00 32.83  ?  139 LEU B CA  1 
ATOM   3844 C  C   . LEU B 1 139 ? -10.132 44.824 -9.485  1.00 35.38  ?  139 LEU B C   1 
ATOM   3845 O  O   . LEU B 1 139 ? -9.127  44.457 -10.127 1.00 37.06  ?  139 LEU B O   1 
ATOM   3846 C  CB  . LEU B 1 139 ? -10.786 43.359 -7.495  1.00 33.63  ?  139 LEU B CB  1 
ATOM   3847 C  CG  . LEU B 1 139 ? -10.629 43.072 -6.002  1.00 31.87  ?  139 LEU B CG  1 
ATOM   3848 C  CD1 . LEU B 1 139 ? -11.237 41.750 -5.646  1.00 33.10  ?  139 LEU B CD1 1 
ATOM   3849 C  CD2 . LEU B 1 139 ? -9.177  43.096 -5.565  1.00 30.87  ?  139 LEU B CD2 1 
ATOM   3850 N  N   . ILE B 1 140 ? -11.230 45.357 -10.034 1.00 35.93  ?  140 ILE B N   1 
ATOM   3851 C  CA  . ILE B 1 140 ? -11.417 45.701 -11.479 1.00 33.48  ?  140 ILE B CA  1 
ATOM   3852 C  C   . ILE B 1 140 ? -10.428 46.810 -11.885 1.00 33.86  ?  140 ILE B C   1 
ATOM   3853 O  O   . ILE B 1 140 ? -9.845  46.705 -12.965 1.00 31.40  ?  140 ILE B O   1 
ATOM   3854 C  CB  . ILE B 1 140 ? -12.889 46.114 -11.738 1.00 32.30  ?  140 ILE B CB  1 
ATOM   3855 C  CG1 . ILE B 1 140 ? -13.823 44.898 -11.717 1.00 30.86  ?  140 ILE B CG1 1 
ATOM   3856 C  CG2 . ILE B 1 140 ? -13.029 46.910 -13.037 1.00 28.27  ?  140 ILE B CG2 1 
ATOM   3857 C  CD1 . ILE B 1 140 ? -15.281 45.265 -11.606 1.00 31.13  ?  140 ILE B CD1 1 
ATOM   3858 N  N   . GLU B 1 141 ? -10.254 47.853 -11.067 1.00 36.05  ?  141 GLU B N   1 
ATOM   3859 C  CA  . GLU B 1 141 ? -9.204  48.878 -11.291 1.00 34.96  ?  141 GLU B CA  1 
ATOM   3860 C  C   . GLU B 1 141 ? -7.839  48.197 -11.500 1.00 34.86  ?  141 GLU B C   1 
ATOM   3861 O  O   . GLU B 1 141 ? -7.145  48.607 -12.403 1.00 36.78  ?  141 GLU B O   1 
ATOM   3862 C  CB  . GLU B 1 141 ? -9.220  49.863 -10.132 1.00 37.64  ?  141 GLU B CB  1 
ATOM   3863 C  CG  . GLU B 1 141 ? -8.119  50.919 -10.166 1.00 37.32  ?  141 GLU B CG  1 
ATOM   3864 C  CD  . GLU B 1 141 ? -7.811  51.520 -8.794  1.00 40.01  ?  141 GLU B CD  1 
ATOM   3865 O  OE1 . GLU B 1 141 ? -8.692  51.542 -7.859  1.00 40.01  ?  141 GLU B OE1 1 
ATOM   3866 O  OE2 . GLU B 1 141 ? -6.680  51.941 -8.632  1.00 40.93  ?  141 GLU B OE2 1 
ATOM   3867 N  N   . GLN B 1 142 ? -7.443  47.188 -10.726 1.00 35.15  ?  142 GLN B N   1 
ATOM   3868 C  CA  . GLN B 1 142 ? -6.076  46.594 -10.858 1.00 37.42  ?  142 GLN B CA  1 
ATOM   3869 C  C   . GLN B 1 142 ? -6.040  45.526 -11.948 1.00 34.94  ?  142 GLN B C   1 
ATOM   3870 O  O   . GLN B 1 142 ? -4.925  45.248 -12.457 1.00 32.25  ?  142 GLN B O   1 
ATOM   3871 C  CB  . GLN B 1 142 ? -5.587  46.013 -9.538  1.00 44.29  ?  142 GLN B CB  1 
ATOM   3872 C  CG  . GLN B 1 142 ? -5.347  47.098 -8.491  1.00 56.18  ?  142 GLN B CG  1 
ATOM   3873 C  CD  . GLN B 1 142 ? -4.928  46.594 -7.131  1.00 56.61  ?  142 GLN B CD  1 
ATOM   3874 O  OE1 . GLN B 1 142 ? -5.220  45.456 -6.753  1.00 53.91  ?  142 GLN B OE1 1 
ATOM   3875 N  NE2 . GLN B 1 142 ? -4.210  47.439 -6.403  1.00 60.55  ?  142 GLN B NE2 1 
ATOM   3876 N  N   . GLY B 1 143 ? -7.205  45.001 -12.324 1.00 29.70  ?  143 GLY B N   1 
ATOM   3877 C  CA  . GLY B 1 143 ? -7.336  43.895 -13.295 1.00 32.72  ?  143 GLY B CA  1 
ATOM   3878 C  C   . GLY B 1 143 ? -7.091  42.512 -12.669 1.00 31.62  ?  143 GLY B C   1 
ATOM   3879 O  O   . GLY B 1 143 ? -6.513  42.396 -11.592 1.00 31.17  ?  143 GLY B O   1 
ATOM   3880 N  N   . PRO B 1 144 ? -7.528  41.425 -13.337 1.00 31.81  ?  144 PRO B N   1 
ATOM   3881 C  CA  . PRO B 1 144 ? -7.281  40.061 -12.866 1.00 32.02  ?  144 PRO B CA  1 
ATOM   3882 C  C   . PRO B 1 144 ? -5.834  39.613 -13.062 1.00 32.54  ?  144 PRO B C   1 
ATOM   3883 O  O   . PRO B 1 144 ? -5.083  40.218 -13.823 1.00 36.60  ?  144 PRO B O   1 
ATOM   3884 C  CB  . PRO B 1 144 ? -8.208  39.204 -13.732 1.00 31.46  ?  144 PRO B CB  1 
ATOM   3885 C  CG  . PRO B 1 144 ? -8.389  40.004 -15.016 1.00 30.25  ?  144 PRO B CG  1 
ATOM   3886 C  CD  . PRO B 1 144 ? -8.275  41.457 -14.609 1.00 32.54  ?  144 PRO B CD  1 
ATOM   3887 N  N   . PRO B 1 145 ? -5.363  38.598 -12.315 1.00 34.43  ?  145 PRO B N   1 
ATOM   3888 C  CA  . PRO B 1 145 ? -6.170  37.944 -11.283 1.00 35.72  ?  145 PRO B CA  1 
ATOM   3889 C  C   . PRO B 1 145 ? -6.184  38.746 -9.979  1.00 34.02  ?  145 PRO B C   1 
ATOM   3890 O  O   . PRO B 1 145 ? -5.350  39.563 -9.779  1.00 39.25  ?  145 PRO B O   1 
ATOM   3891 C  CB  . PRO B 1 145 ? -5.473  36.593 -11.073 1.00 35.31  ?  145 PRO B CB  1 
ATOM   3892 C  CG  . PRO B 1 145 ? -4.018  36.880 -11.421 1.00 35.34  ?  145 PRO B CG  1 
ATOM   3893 C  CD  . PRO B 1 145 ? -4.010  38.032 -12.415 1.00 34.18  ?  145 PRO B CD  1 
ATOM   3894 N  N   . ALA B 1 146 ? -7.153  38.494 -9.116  1.00 37.13  ?  146 ALA B N   1 
ATOM   3895 C  CA  . ALA B 1 146 ? -7.141  38.991 -7.724  1.00 33.19  ?  146 ALA B CA  1 
ATOM   3896 C  C   . ALA B 1 146 ? -7.489  37.826 -6.819  1.00 30.54  ?  146 ALA B C   1 
ATOM   3897 O  O   . ALA B 1 146 ? -8.048  36.842 -7.359  1.00 26.53  ?  146 ALA B O   1 
ATOM   3898 C  CB  . ALA B 1 146 ? -8.109  40.117 -7.550  1.00 35.50  ?  146 ALA B CB  1 
ATOM   3899 N  N   . ASP B 1 147 ? -7.084  37.931 -5.541  1.00 29.68  ?  147 ASP B N   1 
ATOM   3900 C  CA  . ASP B 1 147 ? -7.510  37.052 -4.420  1.00 28.77  ?  147 ASP B CA  1 
ATOM   3901 C  C   . ASP B 1 147 ? -8.858  37.558 -3.881  1.00 30.71  ?  147 ASP B C   1 
ATOM   3902 O  O   . ASP B 1 147 ? -8.898  38.662 -3.338  1.00 27.08  ?  147 ASP B O   1 
ATOM   3903 C  CB  . ASP B 1 147 ? -6.467  37.046 -3.310  1.00 29.70  ?  147 ASP B CB  1 
ATOM   3904 C  CG  . ASP B 1 147 ? -6.895  36.240 -2.095  1.00 30.68  ?  147 ASP B CG  1 
ATOM   3905 O  OD1 . ASP B 1 147 ? -7.752  35.399 -2.240  1.00 28.46  ?  147 ASP B OD1 1 
ATOM   3906 O  OD2 . ASP B 1 147 ? -6.334  36.441 -1.017  1.00 35.02  ?  147 ASP B OD2 1 
ATOM   3907 N  N   . LEU B 1 148 ? -9.938  36.785 -4.020  1.00 31.63  ?  148 LEU B N   1 
ATOM   3908 C  CA  . LEU B 1 148 ? -11.275 37.229 -3.545  1.00 30.50  ?  148 LEU B CA  1 
ATOM   3909 C  C   . LEU B 1 148 ? -11.378 37.039 -2.027  1.00 31.96  ?  148 LEU B C   1 
ATOM   3910 O  O   . LEU B 1 148 ? -12.290 37.631 -1.420  1.00 33.94  ?  148 LEU B O   1 
ATOM   3911 C  CB  . LEU B 1 148 ? -12.369 36.488 -4.325  1.00 28.48  ?  148 LEU B CB  1 
ATOM   3912 C  CG  . LEU B 1 148 ? -12.643 37.032 -5.724  1.00 28.43  ?  148 LEU B CG  1 
ATOM   3913 C  CD1 . LEU B 1 148 ? -13.839 36.353 -6.360  1.00 28.85  ?  148 LEU B CD1 1 
ATOM   3914 C  CD2 . LEU B 1 148 ? -12.871 38.541 -5.698  1.00 30.13  ?  148 LEU B CD2 1 
ATOM   3915 N  N   . ARG B 1 149 ? -10.478 36.274 -1.400  1.00 31.85  ?  149 ARG B N   1 
ATOM   3916 C  CA  . ARG B 1 149 ? -10.410 36.257 0.090   1.00 31.45  ?  149 ARG B CA  1 
ATOM   3917 C  C   . ARG B 1 149 ? -9.906  37.628 0.599   1.00 32.25  ?  149 ARG B C   1 
ATOM   3918 O  O   . ARG B 1 149 ? -10.708 38.370 1.199   1.00 30.89  ?  149 ARG B O   1 
ATOM   3919 C  CB  . ARG B 1 149 ? -9.557  35.104 0.623   1.00 29.23  ?  149 ARG B CB  1 
ATOM   3920 C  CG  . ARG B 1 149 ? -9.682  34.938 2.129   1.00 29.61  ?  149 ARG B CG  1 
ATOM   3921 C  CD  . ARG B 1 149 ? -8.832  33.790 2.690   1.00 33.68  ?  149 ARG B CD  1 
ATOM   3922 N  NE  . ARG B 1 149 ? -8.670  33.937 4.138   1.00 33.42  ?  149 ARG B NE  1 
ATOM   3923 C  CZ  . ARG B 1 149 ? -7.839  34.795 4.707   1.00 31.93  ?  149 ARG B CZ  1 
ATOM   3924 N  NH1 . ARG B 1 149 ? -7.030  35.566 3.983   1.00 31.76  ?  149 ARG B NH1 1 
ATOM   3925 N  NH2 . ARG B 1 149 ? -7.836  34.894 6.013   1.00 34.54  ?  149 ARG B NH2 1 
ATOM   3926 N  N   . ASP B 1 150 ? -8.639  37.977 0.368   1.00 30.02  ?  150 ASP B N   1 
ATOM   3927 C  CA  . ASP B 1 150 ? -8.056  39.218 0.936   1.00 31.99  ?  150 ASP B CA  1 
ATOM   3928 C  C   . ASP B 1 150 ? -8.702  40.453 0.276   1.00 33.56  ?  150 ASP B C   1 
ATOM   3929 O  O   . ASP B 1 150 ? -8.964  41.452 0.980   1.00 32.94  ?  150 ASP B O   1 
ATOM   3930 C  CB  . ASP B 1 150 ? -6.527  39.248 0.829   1.00 31.28  ?  150 ASP B CB  1 
ATOM   3931 C  CG  . ASP B 1 150 ? -6.020  40.610 1.251   1.00 33.16  ?  150 ASP B CG  1 
ATOM   3932 O  OD1 . ASP B 1 150 ? -6.042  40.882 2.438   1.00 33.21  ?  150 ASP B OD1 1 
ATOM   3933 O  OD2 . ASP B 1 150 ? -5.788  41.443 0.376   1.00 39.18  ?  150 ASP B OD2 1 
ATOM   3934 N  N   . GLY B 1 151 ? -9.071  40.361 -0.999  1.00 33.40  ?  151 GLY B N   1 
ATOM   3935 C  CA  . GLY B 1 151 ? -9.616  41.520 -1.727  1.00 30.00  ?  151 GLY B CA  1 
ATOM   3936 C  C   . GLY B 1 151 ? -11.107 41.713 -1.569  1.00 35.05  ?  151 GLY B C   1 
ATOM   3937 O  O   . GLY B 1 151 ? -11.570 42.823 -1.873  1.00 33.29  ?  151 GLY B O   1 
ATOM   3938 N  N   . PHE B 1 152 ? -11.843 40.696 -1.125  1.00 30.05  ?  152 PHE B N   1 
ATOM   3939 C  CA  . PHE B 1 152 ? -13.318 40.842 -1.052  1.00 27.84  ?  152 PHE B CA  1 
ATOM   3940 C  C   . PHE B 1 152 ? -13.912 40.294 0.253   1.00 28.85  ?  152 PHE B C   1 
ATOM   3941 O  O   . PHE B 1 152 ? -14.374 41.124 1.033   1.00 27.67  ?  152 PHE B O   1 
ATOM   3942 C  CB  . PHE B 1 152 ? -13.888 40.184 -2.314  1.00 27.73  ?  152 PHE B CB  1 
ATOM   3943 C  CG  . PHE B 1 152 ? -15.394 40.293 -2.490  1.00 28.32  ?  152 PHE B CG  1 
ATOM   3944 C  CD1 . PHE B 1 152 ? -16.030 41.526 -2.440  1.00 26.76  ?  152 PHE B CD1 1 
ATOM   3945 C  CD2 . PHE B 1 152 ? -16.166 39.161 -2.710  1.00 26.22  ?  152 PHE B CD2 1 
ATOM   3946 C  CE1 . PHE B 1 152 ? -17.401 41.618 -2.596  1.00 25.43  ?  152 PHE B CE1 1 
ATOM   3947 C  CE2 . PHE B 1 152 ? -17.536 39.262 -2.872  1.00 26.10  ?  152 PHE B CE2 1 
ATOM   3948 C  CZ  . PHE B 1 152 ? -18.148 40.489 -2.817  1.00 26.97  ?  152 PHE B CZ  1 
ATOM   3949 N  N   . THR B 1 153 ? -13.896 38.980 0.484   1.00 27.41  ?  153 THR B N   1 
ATOM   3950 C  CA  . THR B 1 153 ? -14.594 38.341 1.633   1.00 27.42  ?  153 THR B CA  1 
ATOM   3951 C  C   . THR B 1 153 ? -14.134 38.855 2.987   1.00 24.27  ?  153 THR B C   1 
ATOM   3952 O  O   . THR B 1 153 ? -14.993 39.102 3.827   1.00 23.10  ?  153 THR B O   1 
ATOM   3953 C  CB  . THR B 1 153 ? -14.478 36.816 1.509   1.00 27.47  ?  153 THR B CB  1 
ATOM   3954 O  OG1 . THR B 1 153 ? -13.156 36.476 1.909   1.00 29.64  ?  153 THR B OG1 1 
ATOM   3955 C  CG2 . THR B 1 153 ? -14.772 36.321 0.106   1.00 27.17  ?  153 THR B CG2 1 
ATOM   3956 N  N   . GLU B 1 154 ? -12.832 38.994 3.192   1.00 23.13  ?  154 GLU B N   1 
ATOM   3957 C  CA  . GLU B 1 154 ? -12.298 39.494 4.477   1.00 26.25  ?  154 GLU B CA  1 
ATOM   3958 C  C   . GLU B 1 154 ? -12.667 40.967 4.661   1.00 26.39  ?  154 GLU B C   1 
ATOM   3959 O  O   . GLU B 1 154 ? -13.330 41.303 5.631   1.00 28.05  ?  154 GLU B O   1 
ATOM   3960 C  CB  . GLU B 1 154 ? -10.803 39.196 4.556   1.00 28.78  ?  154 GLU B CB  1 
ATOM   3961 C  CG  . GLU B 1 154 ? -10.516 37.706 4.513   1.00 29.23  ?  154 GLU B CG  1 
ATOM   3962 C  CD  . GLU B 1 154 ? -10.696 37.094 5.875   1.00 28.59  ?  154 GLU B CD  1 
ATOM   3963 O  OE1 . GLU B 1 154 ? -9.864  37.450 6.732   1.00 32.21  ?  154 GLU B OE1 1 
ATOM   3964 O  OE2 . GLU B 1 154 ? -11.670 36.306 6.075   1.00 23.99  ?  154 GLU B OE2 1 
ATOM   3965 N  N   . PRO B 1 155 ? -12.281 41.930 3.800   1.00 24.66  ?  155 PRO B N   1 
ATOM   3966 C  CA  . PRO B 1 155 ? -12.628 43.328 4.078   1.00 27.59  ?  155 PRO B CA  1 
ATOM   3967 C  C   . PRO B 1 155 ? -14.157 43.513 4.225   1.00 28.85  ?  155 PRO B C   1 
ATOM   3968 O  O   . PRO B 1 155 ? -14.567 44.328 5.052   1.00 27.47  ?  155 PRO B O   1 
ATOM   3969 C  CB  . PRO B 1 155 ? -11.998 44.134 2.928   1.00 24.94  ?  155 PRO B CB  1 
ATOM   3970 C  CG  . PRO B 1 155 ? -11.700 43.089 1.876   1.00 26.49  ?  155 PRO B CG  1 
ATOM   3971 C  CD  . PRO B 1 155 ? -11.447 41.782 2.610   1.00 24.55  ?  155 PRO B CD  1 
ATOM   3972 N  N   . TYR B 1 156 ? -14.959 42.724 3.497   1.00 28.01  ?  156 TYR B N   1 
ATOM   3973 C  CA  . TYR B 1 156 ? -16.441 42.871 3.420   1.00 28.89  ?  156 TYR B CA  1 
ATOM   3974 C  C   . TYR B 1 156 ? -17.067 42.386 4.734   1.00 29.38  ?  156 TYR B C   1 
ATOM   3975 O  O   . TYR B 1 156 ? -17.940 43.104 5.303   1.00 29.46  ?  156 TYR B O   1 
ATOM   3976 C  CB  . TYR B 1 156 ? -17.008 42.135 2.199   1.00 28.64  ?  156 TYR B CB  1 
ATOM   3977 C  CG  . TYR B 1 156 ? -18.522 42.076 2.122   1.00 30.04  ?  156 TYR B CG  1 
ATOM   3978 C  CD1 . TYR B 1 156 ? -19.278 43.199 1.791   1.00 30.40  ?  156 TYR B CD1 1 
ATOM   3979 C  CD2 . TYR B 1 156 ? -19.197 40.884 2.335   1.00 27.51  ?  156 TYR B CD2 1 
ATOM   3980 C  CE1 . TYR B 1 156 ? -20.661 43.139 1.711   1.00 30.70  ?  156 TYR B CE1 1 
ATOM   3981 C  CE2 . TYR B 1 156 ? -20.573 40.807 2.283   1.00 28.61  ?  156 TYR B CE2 1 
ATOM   3982 C  CZ  . TYR B 1 156 ? -21.308 41.940 1.973   1.00 32.34  ?  156 TYR B CZ  1 
ATOM   3983 O  OH  . TYR B 1 156 ? -22.664 41.861 1.889   1.00 29.82  ?  156 TYR B OH  1 
ATOM   3984 N  N   . SER B 1 157 ? -16.620 41.226 5.221   1.00 27.09  ?  157 SER B N   1 
ATOM   3985 C  CA  . SER B 1 157 ? -17.104 40.613 6.484   1.00 27.95  ?  157 SER B CA  1 
ATOM   3986 C  C   . SER B 1 157 ? -16.640 41.454 7.679   1.00 26.41  ?  157 SER B C   1 
ATOM   3987 O  O   . SER B 1 157 ? -17.421 41.658 8.606   1.00 27.62  ?  157 SER B O   1 
ATOM   3988 C  CB  . SER B 1 157 ? -16.661 39.176 6.585   1.00 29.23  ?  157 SER B CB  1 
ATOM   3989 O  OG  . SER B 1 157 ? -17.173 38.420 5.490   1.00 33.43  ?  157 SER B OG  1 
ATOM   3990 N  N   . ALA B 1 158 ? -15.404 41.920 7.663   1.00 26.96  ?  158 ALA B N   1 
ATOM   3991 C  CA  . ALA B 1 158 ? -14.878 42.842 8.684   1.00 30.23  ?  158 ALA B CA  1 
ATOM   3992 C  C   . ALA B 1 158 ? -15.724 44.110 8.708   1.00 29.68  ?  158 ALA B C   1 
ATOM   3993 O  O   . ALA B 1 158 ? -16.063 44.549 9.790   1.00 29.47  ?  158 ALA B O   1 
ATOM   3994 C  CB  . ALA B 1 158 ? -13.437 43.184 8.415   1.00 31.75  ?  158 ALA B CB  1 
ATOM   3995 N  N   . ALA B 1 159 ? -16.001 44.701 7.553   1.00 31.63  ?  159 ALA B N   1 
ATOM   3996 C  CA  . ALA B 1 159 ? -16.759 45.969 7.475   1.00 34.03  ?  159 ALA B CA  1 
ATOM   3997 C  C   . ALA B 1 159 ? -18.169 45.748 8.048   1.00 32.39  ?  159 ALA B C   1 
ATOM   3998 O  O   . ALA B 1 159 ? -18.618 46.565 8.850   1.00 33.37  ?  159 ALA B O   1 
ATOM   3999 C  CB  . ALA B 1 159 ? -16.790 46.464 6.056   1.00 33.74  ?  159 ALA B CB  1 
ATOM   4000 N  N   . LEU B 1 160 ? -18.814 44.635 7.730   1.00 30.67  ?  160 LEU B N   1 
ATOM   4001 C  CA  . LEU B 1 160 ? -20.159 44.352 8.300   1.00 34.55  ?  160 LEU B CA  1 
ATOM   4002 C  C   . LEU B 1 160 ? -20.071 44.386 9.827   1.00 35.47  ?  160 LEU B C   1 
ATOM   4003 O  O   . LEU B 1 160 ? -20.913 45.035 10.480  1.00 38.24  ?  160 LEU B O   1 
ATOM   4004 C  CB  . LEU B 1 160 ? -20.692 43.002 7.809   1.00 32.50  ?  160 LEU B CB  1 
ATOM   4005 C  CG  . LEU B 1 160 ? -21.944 42.497 8.529   1.00 35.30  ?  160 LEU B CG  1 
ATOM   4006 C  CD1 . LEU B 1 160 ? -23.109 43.466 8.411   1.00 34.92  ?  160 LEU B CD1 1 
ATOM   4007 C  CD2 . LEU B 1 160 ? -22.366 41.124 8.017   1.00 35.08  ?  160 LEU B CD2 1 
ATOM   4008 N  N   . HIS B 1 161 ? -19.093 43.685 10.376  1.00 33.14  ?  161 HIS B N   1 
ATOM   4009 C  CA  . HIS B 1 161 ? -19.025 43.395 11.822  1.00 31.61  ?  161 HIS B CA  1 
ATOM   4010 C  C   . HIS B 1 161 ? -18.532 44.623 12.587  1.00 30.33  ?  161 HIS B C   1 
ATOM   4011 O  O   . HIS B 1 161 ? -18.971 44.790 13.743  1.00 28.90  ?  161 HIS B O   1 
ATOM   4012 C  CB  . HIS B 1 161 ? -18.239 42.104 12.049  1.00 31.40  ?  161 HIS B CB  1 
ATOM   4013 C  CG  . HIS B 1 161 ? -19.050 40.927 11.666  1.00 31.26  ?  161 HIS B CG  1 
ATOM   4014 N  ND1 . HIS B 1 161 ? -19.228 40.583 10.362  1.00 30.35  ?  161 HIS B ND1 1 
ATOM   4015 C  CD2 . HIS B 1 161 ? -19.795 40.070 12.408  1.00 34.10  ?  161 HIS B CD2 1 
ATOM   4016 C  CE1 . HIS B 1 161 ? -20.007 39.502 10.319  1.00 34.49  ?  161 HIS B CE1 1 
ATOM   4017 N  NE2 . HIS B 1 161 ? -20.406 39.188 11.558  1.00 28.27  ?  161 HIS B NE2 1 
ATOM   4018 N  N   . CYS B 1 162 ? -17.681 45.452 11.985  1.00 32.83  ?  162 CYS B N   1 
ATOM   4019 C  CA  . CYS B 1 162 ? -17.345 46.804 12.510  1.00 32.36  ?  162 CYS B CA  1 
ATOM   4020 C  C   . CYS B 1 162 ? -18.637 47.655 12.590  1.00 36.35  ?  162 CYS B C   1 
ATOM   4021 O  O   . CYS B 1 162 ? -18.918 48.312 13.625  1.00 32.39  ?  162 CYS B O   1 
ATOM   4022 C  CB  . CYS B 1 162 ? -16.285 47.450 11.640  1.00 31.72  ?  162 CYS B CB  1 
ATOM   4023 S  SG  . CYS B 1 162 ? -14.631 46.711 11.780  1.00 32.65  ?  162 CYS B SG  1 
ATOM   4024 N  N   . ARG B 1 163 ? -19.475 47.622 11.566  1.00 38.28  ?  163 ARG B N   1 
ATOM   4025 C  CA  . ARG B 1 163 ? -20.773 48.339 11.648  1.00 41.59  ?  163 ARG B CA  1 
ATOM   4026 C  C   . ARG B 1 163 ? -21.648 47.701 12.751  1.00 42.06  ?  163 ARG B C   1 
ATOM   4027 O  O   . ARG B 1 163 ? -22.251 48.475 13.527  1.00 40.14  ?  163 ARG B O   1 
ATOM   4028 C  CB  . ARG B 1 163 ? -21.437 48.388 10.269  1.00 47.01  ?  163 ARG B CB  1 
ATOM   4029 C  CG  . ARG B 1 163 ? -22.621 49.341 10.172  1.00 52.38  ?  163 ARG B CG  1 
ATOM   4030 C  CD  . ARG B 1 163 ? -23.506 49.038 8.981   1.00 52.66  ?  163 ARG B CD  1 
ATOM   4031 N  NE  . ARG B 1 163 ? -24.827 49.646 9.029   1.00 51.76  ?  163 ARG B NE  1 
ATOM   4032 C  CZ  . ARG B 1 163 ? -25.113 50.888 8.653   1.00 51.94  ?  163 ARG B CZ  1 
ATOM   4033 N  NH1 . ARG B 1 163 ? -24.164 51.706 8.240   1.00 49.76  ?  163 ARG B NH1 1 
ATOM   4034 N  NH2 . ARG B 1 163 ? -26.360 51.315 8.695   1.00 54.01  ?  163 ARG B NH2 1 
ATOM   4035 N  N   . LEU B 1 164 ? -21.719 46.367 12.881  1.00 36.57  ?  164 LEU B N   1 
ATOM   4036 C  CA  . LEU B 1 164 ? -22.597 45.763 13.912  1.00 35.32  ?  164 LEU B CA  1 
ATOM   4037 C  C   . LEU B 1 164 ? -22.215 46.251 15.312  1.00 34.87  ?  164 LEU B C   1 
ATOM   4038 O  O   . LEU B 1 164 ? -23.141 46.442 16.125  1.00 32.12  ?  164 LEU B O   1 
ATOM   4039 C  CB  . LEU B 1 164 ? -22.516 44.244 13.851  1.00 40.65  ?  164 LEU B CB  1 
ATOM   4040 C  CG  . LEU B 1 164 ? -23.165 43.617 12.621  1.00 48.19  ?  164 LEU B CG  1 
ATOM   4041 C  CD1 . LEU B 1 164 ? -22.939 42.099 12.616  1.00 51.08  ?  164 LEU B CD1 1 
ATOM   4042 C  CD2 . LEU B 1 164 ? -24.651 43.963 12.536  1.00 44.00  ?  164 LEU B CD2 1 
ATOM   4043 N  N   . LEU B 1 165 ? -20.912 46.390 15.587  1.00 36.64  ?  165 LEU B N   1 
ATOM   4044 C  CA  . LEU B 1 165 ? -20.341 46.862 16.884  1.00 38.51  ?  165 LEU B CA  1 
ATOM   4045 C  C   . LEU B 1 165 ? -20.341 48.394 16.968  1.00 41.22  ?  165 LEU B C   1 
ATOM   4046 O  O   . LEU B 1 165 ? -20.162 48.907 18.073  1.00 47.87  ?  165 LEU B O   1 
ATOM   4047 C  CB  . LEU B 1 165 ? -18.879 46.427 17.031  1.00 38.63  ?  165 LEU B CB  1 
ATOM   4048 C  CG  . LEU B 1 165 ? -18.552 44.947 17.135  1.00 35.00  ?  165 LEU B CG  1 
ATOM   4049 C  CD1 . LEU B 1 165 ? -17.215 44.756 17.823  1.00 30.46  ?  165 LEU B CD1 1 
ATOM   4050 C  CD2 . LEU B 1 165 ? -19.630 44.195 17.858  1.00 40.45  ?  165 LEU B CD2 1 
ATOM   4051 N  N   . GLY B 1 166 ? -20.374 49.098 15.840  1.00 45.27  ?  166 GLY B N   1 
ATOM   4052 C  CA  . GLY B 1 166 ? -20.321 50.576 15.805  1.00 43.79  ?  166 GLY B CA  1 
ATOM   4053 C  C   . GLY B 1 166 ? -18.908 51.088 15.972  1.00 40.58  ?  166 GLY B C   1 
ATOM   4054 O  O   . GLY B 1 166 ? -18.743 52.169 16.506  1.00 49.09  ?  166 GLY B O   1 
ATOM   4055 N  N   . ILE B 1 167 ? -17.924 50.320 15.530  1.00 39.93  ?  167 ILE B N   1 
ATOM   4056 C  CA  . ILE B 1 167 ? -16.491 50.720 15.480  1.00 40.64  ?  167 ILE B CA  1 
ATOM   4057 C  C   . ILE B 1 167 ? -16.153 51.075 14.036  1.00 42.67  ?  167 ILE B C   1 
ATOM   4058 O  O   . ILE B 1 167 ? -16.854 50.657 13.109  1.00 42.72  ?  167 ILE B O   1 
ATOM   4059 C  CB  . ILE B 1 167 ? -15.596 49.591 16.034  1.00 44.79  ?  167 ILE B CB  1 
ATOM   4060 C  CG1 . ILE B 1 167 ? -15.609 48.320 15.173  1.00 42.87  ?  167 ILE B CG1 1 
ATOM   4061 C  CG2 . ILE B 1 167 ? -15.968 49.276 17.478  1.00 44.94  ?  167 ILE B CG2 1 
ATOM   4062 C  CD1 . ILE B 1 167 ? -14.672 47.234 15.663  1.00 40.57  ?  167 ILE B CD1 1 
ATOM   4063 N  N   . PRO B 1 168 ? -15.107 51.893 13.792  1.00 44.78  ?  168 PRO B N   1 
ATOM   4064 C  CA  . PRO B 1 168 ? -14.652 52.165 12.424  1.00 48.11  ?  168 PRO B CA  1 
ATOM   4065 C  C   . PRO B 1 168 ? -13.976 50.922 11.802  1.00 44.25  ?  168 PRO B C   1 
ATOM   4066 O  O   . PRO B 1 168 ? -13.784 49.933 12.481  1.00 38.80  ?  168 PRO B O   1 
ATOM   4067 C  CB  . PRO B 1 168 ? -13.651 53.339 12.583  1.00 48.16  ?  168 PRO B CB  1 
ATOM   4068 C  CG  . PRO B 1 168 ? -13.824 53.837 14.014  1.00 44.13  ?  168 PRO B CG  1 
ATOM   4069 C  CD  . PRO B 1 168 ? -14.345 52.651 14.797  1.00 46.90  ?  168 PRO B CD  1 
ATOM   4070 N  N   . THR B 1 169 ? -13.602 51.006 10.529  1.00 43.70  ?  169 THR B N   1 
ATOM   4071 C  CA  . THR B 1 169 ? -13.076 49.872 9.725   1.00 45.52  ?  169 THR B CA  1 
ATOM   4072 C  C   . THR B 1 169 ? -11.556 49.960 9.585   1.00 45.11  ?  169 THR B C   1 
ATOM   4073 O  O   . THR B 1 169 ? -10.980 48.994 9.046   1.00 43.33  ?  169 THR B O   1 
ATOM   4074 C  CB  . THR B 1 169 ? -13.736 49.816 8.351   1.00 44.66  ?  169 THR B CB  1 
ATOM   4075 O  OG1 . THR B 1 169 ? -13.575 51.108 7.781   1.00 51.23  ?  169 THR B OG1 1 
ATOM   4076 C  CG2 . THR B 1 169 ? -15.204 49.452 8.421   1.00 46.81  ?  169 THR B CG2 1 
ATOM   4077 N  N   . ASP B 1 170 ? -10.953 51.008 10.152  1.00 42.33  ?  170 ASP B N   1 
ATOM   4078 C  CA  . ASP B 1 170 ? -9.519  51.372 9.986   1.00 47.07  ?  170 ASP B CA  1 
ATOM   4079 C  C   . ASP B 1 170 ? -8.641  50.153 10.304  1.00 42.19  ?  170 ASP B C   1 
ATOM   4080 O  O   . ASP B 1 170 ? -7.665  49.932 9.590   1.00 39.71  ?  170 ASP B O   1 
ATOM   4081 C  CB  . ASP B 1 170 ? -9.139  52.599 10.843  1.00 55.75  ?  170 ASP B CB  1 
ATOM   4082 C  CG  . ASP B 1 170 ? -10.027 53.846 10.682  1.00 61.56  ?  170 ASP B CG  1 
ATOM   4083 O  OD1 . ASP B 1 170 ? -10.843 53.899 9.734   1.00 61.61  ?  170 ASP B OD1 1 
ATOM   4084 O  OD2 . ASP B 1 170 ? -9.906  54.769 11.517  1.00 57.18  ?  170 ASP B OD2 1 
ATOM   4085 N  N   . ASP B 1 171 ? -8.990  49.371 11.324  1.00 42.01  ?  171 ASP B N   1 
ATOM   4086 C  CA  . ASP B 1 171 ? -8.117  48.306 11.890  1.00 39.17  ?  171 ASP B CA  1 
ATOM   4087 C  C   . ASP B 1 171 ? -8.599  46.909 11.490  1.00 35.59  ?  171 ASP B C   1 
ATOM   4088 O  O   . ASP B 1 171 ? -8.190  45.964 12.135  1.00 34.49  ?  171 ASP B O   1 
ATOM   4089 C  CB  . ASP B 1 171 ? -8.097  48.423 13.410  1.00 42.45  ?  171 ASP B CB  1 
ATOM   4090 C  CG  . ASP B 1 171 ? -7.626  49.788 13.849  1.00 44.55  ?  171 ASP B CG  1 
ATOM   4091 O  OD1 . ASP B 1 171 ? -6.880  50.394 13.046  1.00 41.73  ?  171 ASP B OD1 1 
ATOM   4092 O  OD2 . ASP B 1 171 ? -8.024  50.229 14.968  1.00 42.00  ?  171 ASP B OD2 1 
ATOM   4093 N  N   . TRP B 1 172 ? -9.442  46.778 10.466  1.00 37.34  ?  172 TRP B N   1 
ATOM   4094 C  CA  . TRP B 1 172 ? -10.020 45.472 10.070  1.00 32.31  ?  172 TRP B CA  1 
ATOM   4095 C  C   . TRP B 1 172 ? -8.905  44.427 9.936   1.00 31.70  ?  172 TRP B C   1 
ATOM   4096 O  O   . TRP B 1 172 ? -9.114  43.251 10.357  1.00 30.17  ?  172 TRP B O   1 
ATOM   4097 C  CB  . TRP B 1 172 ? -10.849 45.610 8.794   1.00 31.75  ?  172 TRP B CB  1 
ATOM   4098 C  CG  . TRP B 1 172 ? -10.078 45.843 7.542   1.00 32.37  ?  172 TRP B CG  1 
ATOM   4099 C  CD1 . TRP B 1 172 ? -9.690  47.036 7.014   1.00 34.81  ?  172 TRP B CD1 1 
ATOM   4100 C  CD2 . TRP B 1 172 ? -9.630  44.835 6.622   1.00 35.32  ?  172 TRP B CD2 1 
ATOM   4101 N  NE1 . TRP B 1 172 ? -9.014  46.836 5.840   1.00 35.21  ?  172 TRP B NE1 1 
ATOM   4102 C  CE2 . TRP B 1 172 ? -8.954  45.498 5.579   1.00 32.83  ?  172 TRP B CE2 1 
ATOM   4103 C  CE3 . TRP B 1 172 ? -9.688  43.439 6.611   1.00 32.97  ?  172 TRP B CE3 1 
ATOM   4104 C  CZ2 . TRP B 1 172 ? -8.356  44.815 4.530   1.00 34.09  ?  172 TRP B CZ2 1 
ATOM   4105 C  CZ3 . TRP B 1 172 ? -9.118  42.767 5.555   1.00 35.25  ?  172 TRP B CZ3 1 
ATOM   4106 C  CH2 . TRP B 1 172 ? -8.465  43.443 4.527   1.00 34.28  ?  172 TRP B CH2 1 
ATOM   4107 N  N   . ARG B 1 173 ? -7.754  44.803 9.384   1.00 29.92  ?  173 ARG B N   1 
ATOM   4108 C  CA  . ARG B 1 173 ? -6.711  43.804 9.043   1.00 32.30  ?  173 ARG B CA  1 
ATOM   4109 C  C   . ARG B 1 173 ? -6.242  43.141 10.330  1.00 34.05  ?  173 ARG B C   1 
ATOM   4110 O  O   . ARG B 1 173 ? -6.196  41.879 10.356  1.00 36.31  ?  173 ARG B O   1 
ATOM   4111 C  CB  . ARG B 1 173 ? -5.538  44.422 8.285   1.00 34.28  ?  173 ARG B CB  1 
ATOM   4112 C  CG  . ARG B 1 173 ? -5.805  44.589 6.796   1.00 36.88  ?  173 ARG B CG  1 
ATOM   4113 C  CD  . ARG B 1 173 ? -4.549  44.816 5.959   1.00 37.62  ?  173 ARG B CD  1 
ATOM   4114 N  NE  . ARG B 1 173 ? -4.910  44.899 4.547   1.00 37.34  ?  173 ARG B NE  1 
ATOM   4115 C  CZ  . ARG B 1 173 ? -5.249  43.860 3.806   1.00 36.49  ?  173 ARG B CZ  1 
ATOM   4116 N  NH1 . ARG B 1 173 ? -5.246  42.641 4.317   1.00 40.63  ?  173 ARG B NH1 1 
ATOM   4117 N  NH2 . ARG B 1 173 ? -5.560  44.026 2.544   1.00 33.76  ?  173 ARG B NH2 1 
ATOM   4118 N  N   . ARG B 1 174 ? -6.018  43.947 11.377  1.00 31.72  ?  174 ARG B N   1 
ATOM   4119 C  CA  . ARG B 1 174 ? -5.551  43.427 12.692  1.00 31.49  ?  174 ARG B CA  1 
ATOM   4120 C  C   . ARG B 1 174 ? -6.685  42.665 13.402  1.00 31.22  ?  174 ARG B C   1 
ATOM   4121 O  O   . ARG B 1 174 ? -6.383  41.714 14.154  1.00 31.79  ?  174 ARG B O   1 
ATOM   4122 C  CB  . ARG B 1 174 ? -5.025  44.572 13.568  1.00 32.44  ?  174 ARG B CB  1 
ATOM   4123 N  N   . LEU B 1 175 ? -7.938  43.065 13.187  1.00 29.13  ?  175 LEU B N   1 
ATOM   4124 C  CA  . LEU B 1 175 ? -9.067  42.310 13.792  1.00 32.08  ?  175 LEU B CA  1 
ATOM   4125 C  C   . LEU B 1 175 ? -9.176  40.929 13.136  1.00 31.60  ?  175 LEU B C   1 
ATOM   4126 O  O   . LEU B 1 175 ? -9.236  39.930 13.873  1.00 33.30  ?  175 LEU B O   1 
ATOM   4127 C  CB  . LEU B 1 175 ? -10.379 43.099 13.679  1.00 32.39  ?  175 LEU B CB  1 
ATOM   4128 C  CG  . LEU B 1 175 ? -10.390 44.417 14.453  1.00 33.88  ?  175 LEU B CG  1 
ATOM   4129 C  CD1 . LEU B 1 175 ? -11.770 45.042 14.438  1.00 36.63  ?  175 LEU B CD1 1 
ATOM   4130 C  CD2 . LEU B 1 175 ? -9.920  44.221 15.884  1.00 35.64  ?  175 LEU B CD2 1 
ATOM   4131 N  N   . MET B 1 176 ? -9.126  40.865 11.811  1.00 32.16  ?  176 MET B N   1 
ATOM   4132 C  CA  . MET B 1 176 ? -9.196  39.591 11.062  1.00 30.92  ?  176 MET B CA  1 
ATOM   4133 C  C   . MET B 1 176 ? -7.931  38.738 11.353  1.00 33.63  ?  176 MET B C   1 
ATOM   4134 O  O   . MET B 1 176 ? -8.009  37.489 11.429  1.00 38.29  ?  176 MET B O   1 
ATOM   4135 C  CB  . MET B 1 176 ? -9.364  39.874 9.565   1.00 28.85  ?  176 MET B CB  1 
ATOM   4136 C  CG  . MET B 1 176 ? -10.603 40.654 9.200   1.00 27.81  ?  176 MET B CG  1 
ATOM   4137 S  SD  . MET B 1 176 ? -12.103 39.994 9.947   1.00 26.38  ?  176 MET B SD  1 
ATOM   4138 C  CE  . MET B 1 176 ? -12.338 38.532 8.948   1.00 27.21  ?  176 MET B CE  1 
ATOM   4139 N  N   . SER B 1 177 ? -6.788  39.354 11.591  1.00 35.74  ?  177 SER B N   1 
ATOM   4140 C  CA  . SER B 1 177 ? -5.593  38.627 12.094  1.00 35.95  ?  177 SER B CA  1 
ATOM   4141 C  C   . SER B 1 177 ? -5.882  38.034 13.480  1.00 32.19  ?  177 SER B C   1 
ATOM   4142 O  O   . SER B 1 177 ? -5.367  36.958 13.787  1.00 36.57  ?  177 SER B O   1 
ATOM   4143 C  CB  . SER B 1 177 ? -4.386  39.506 12.103  1.00 35.63  ?  177 SER B CB  1 
ATOM   4144 O  OG  . SER B 1 177 ? -4.620  40.551 13.016  1.00 43.21  ?  177 SER B OG  1 
ATOM   4145 N  N   . GLY B 1 178 ? -6.686  38.693 14.302  1.00 27.88  ?  178 GLY B N   1 
ATOM   4146 C  CA  . GLY B 1 178 ? -7.081  38.113 15.596  1.00 29.47  ?  178 GLY B CA  1 
ATOM   4147 C  C   . GLY B 1 178 ? -7.784  36.783 15.379  1.00 30.43  ?  178 GLY B C   1 
ATOM   4148 O  O   . GLY B 1 178 ? -7.513  35.853 16.124  1.00 35.33  ?  178 GLY B O   1 
ATOM   4149 N  N   . ILE B 1 179 ? -8.640  36.709 14.364  1.00 27.12  ?  179 ILE B N   1 
ATOM   4150 C  CA  . ILE B 1 179 ? -9.458  35.528 14.002  1.00 26.53  ?  179 ILE B CA  1 
ATOM   4151 C  C   . ILE B 1 179 ? -8.519  34.415 13.539  1.00 28.03  ?  179 ILE B C   1 
ATOM   4152 O  O   . ILE B 1 179 ? -8.801  33.253 13.907  1.00 26.37  ?  179 ILE B O   1 
ATOM   4153 C  CB  . ILE B 1 179 ? -10.503 35.910 12.933  1.00 27.75  ?  179 ILE B CB  1 
ATOM   4154 C  CG1 . ILE B 1 179 ? -11.694 36.635 13.567  1.00 30.09  ?  179 ILE B CG1 1 
ATOM   4155 C  CG2 . ILE B 1 179 ? -10.967 34.717 12.112  1.00 25.67  ?  179 ILE B CG2 1 
ATOM   4156 C  CD1 . ILE B 1 179 ? -12.416 37.567 12.605  1.00 32.99  ?  179 ILE B CD1 1 
ATOM   4157 N  N   . ASP B 1 180 ? -7.441  34.752 12.809  1.00 27.54  ?  180 ASP B N   1 
ATOM   4158 C  CA  . ASP B 1 180 ? -6.454  33.755 12.322  1.00 28.23  ?  180 ASP B CA  1 
ATOM   4159 C  C   . ASP B 1 180 ? -5.811  33.003 13.499  1.00 29.64  ?  180 ASP B C   1 
ATOM   4160 O  O   . ASP B 1 180 ? -5.345  31.874 13.268  1.00 32.42  ?  180 ASP B O   1 
ATOM   4161 C  CB  . ASP B 1 180 ? -5.354  34.370 11.466  1.00 30.57  ?  180 ASP B CB  1 
ATOM   4162 C  CG  . ASP B 1 180 ? -5.787  34.941 10.127  1.00 31.07  ?  180 ASP B CG  1 
ATOM   4163 O  OD1 . ASP B 1 180 ? -6.728  34.375 9.490   1.00 25.73  ?  180 ASP B OD1 1 
ATOM   4164 O  OD2 . ASP B 1 180 ? -5.145  35.950 9.726   1.00 31.45  ?  180 ASP B OD2 1 
ATOM   4165 N  N   . VAL B 1 181 ? -5.803  33.577 14.704  1.00 28.49  ?  181 VAL B N   1 
ATOM   4166 C  CA  . VAL B 1 181 ? -5.249  32.934 15.931  1.00 30.37  ?  181 VAL B CA  1 
ATOM   4167 C  C   . VAL B 1 181 ? -6.388  32.375 16.792  1.00 29.78  ?  181 VAL B C   1 
ATOM   4168 O  O   . VAL B 1 181 ? -6.286  31.215 17.219  1.00 28.13  ?  181 VAL B O   1 
ATOM   4169 C  CB  . VAL B 1 181 ? -4.361  33.923 16.718  1.00 31.29  ?  181 VAL B CB  1 
ATOM   4170 C  CG1 . VAL B 1 181 ? -3.874  33.373 18.045  1.00 29.04  ?  181 VAL B CG1 1 
ATOM   4171 C  CG2 . VAL B 1 181 ? -3.191  34.398 15.882  1.00 33.70  ?  181 VAL B CG2 1 
ATOM   4172 N  N   . ALA B 1 182 ? -7.421  33.172 17.084  1.00 31.98  ?  182 ALA B N   1 
ATOM   4173 C  CA  . ALA B 1 182 ? -8.542  32.766 17.975  1.00 31.52  ?  182 ALA B CA  1 
ATOM   4174 C  C   . ALA B 1 182 ? -9.103  31.406 17.522  1.00 30.98  ?  182 ALA B C   1 
ATOM   4175 O  O   . ALA B 1 182 ? -9.390  30.557 18.374  1.00 34.36  ?  182 ALA B O   1 
ATOM   4176 C  CB  . ALA B 1 182 ? -9.627  33.825 18.001  1.00 29.64  ?  182 ALA B CB  1 
ATOM   4177 N  N   . PHE B 1 183 ? -9.247  31.193 16.214  1.00 28.07  ?  183 PHE B N   1 
ATOM   4178 C  CA  . PHE B 1 183 ? -10.032 30.064 15.668  1.00 28.24  ?  183 PHE B CA  1 
ATOM   4179 C  C   . PHE B 1 183 ? -9.136  28.886 15.272  1.00 28.19  ?  183 PHE B C   1 
ATOM   4180 O  O   . PHE B 1 183 ? -9.648  27.980 14.585  1.00 32.93  ?  183 PHE B O   1 
ATOM   4181 C  CB  . PHE B 1 183 ? -10.928 30.586 14.546  1.00 30.37  ?  183 PHE B CB  1 
ATOM   4182 C  CG  . PHE B 1 183 ? -12.104 31.353 15.094  1.00 30.05  ?  183 PHE B CG  1 
ATOM   4183 C  CD1 . PHE B 1 183 ? -13.239 30.699 15.511  1.00 32.57  ?  183 PHE B CD1 1 
ATOM   4184 C  CD2 . PHE B 1 183 ? -12.031 32.712 15.283  1.00 31.56  ?  183 PHE B CD2 1 
ATOM   4185 C  CE1 . PHE B 1 183 ? -14.315 31.410 16.015  1.00 37.27  ?  183 PHE B CE1 1 
ATOM   4186 C  CE2 . PHE B 1 183 ? -13.086 33.421 15.833  1.00 33.90  ?  183 PHE B CE2 1 
ATOM   4187 C  CZ  . PHE B 1 183 ? -14.237 32.774 16.184  1.00 35.08  ?  183 PHE B CZ  1 
ATOM   4188 N  N   . ILE B 1 184 ? -7.893  28.838 15.744  1.00 23.89  ?  184 ILE B N   1 
ATOM   4189 C  CA  . ILE B 1 184 ? -7.002  27.687 15.482  1.00 24.23  ?  184 ILE B CA  1 
ATOM   4190 C  C   . ILE B 1 184 ? -7.539  26.489 16.265  1.00 23.64  ?  184 ILE B C   1 
ATOM   4191 O  O   . ILE B 1 184 ? -7.763  26.621 17.459  1.00 22.62  ?  184 ILE B O   1 
ATOM   4192 C  CB  . ILE B 1 184 ? -5.535  28.003 15.857  1.00 24.28  ?  184 ILE B CB  1 
ATOM   4193 C  CG1 . ILE B 1 184 ? -4.835  28.821 14.775  1.00 24.19  ?  184 ILE B CG1 1 
ATOM   4194 C  CG2 . ILE B 1 184 ? -4.763  26.722 16.171  1.00 22.35  ?  184 ILE B CG2 1 
ATOM   4195 C  CD1 . ILE B 1 184 ? -3.628  29.530 15.270  1.00 25.07  ?  184 ILE B CD1 1 
ATOM   4196 N  N   . THR B 1 185 ? -7.597  25.328 15.620  1.00 26.46  ?  185 THR B N   1 
ATOM   4197 C  CA  . THR B 1 185 ? -7.806  24.021 16.293  1.00 26.80  ?  185 THR B CA  1 
ATOM   4198 C  C   . THR B 1 185 ? -6.445  23.384 16.578  1.00 27.80  ?  185 THR B C   1 
ATOM   4199 O  O   . THR B 1 185 ? -5.754  23.035 15.601  1.00 26.95  ?  185 THR B O   1 
ATOM   4200 C  CB  . THR B 1 185 ? -8.667  23.082 15.453  1.00 27.00  ?  185 THR B CB  1 
ATOM   4201 O  OG1 . THR B 1 185 ? -7.853  22.686 14.351  1.00 27.16  ?  185 THR B OG1 1 
ATOM   4202 C  CG2 . THR B 1 185 ? -9.966  23.742 15.038  1.00 28.28  ?  185 THR B CG2 1 
ATOM   4203 N  N   . SER B 1 186 ? -6.122  23.239 17.870  1.00 28.14  ?  186 SER B N   1 
ATOM   4204 C  CA  . SER B 1 186 ? -4.867  22.665 18.399  1.00 27.83  ?  186 SER B CA  1 
ATOM   4205 C  C   . SER B 1 186 ? -5.146  21.441 19.276  1.00 28.76  ?  186 SER B C   1 
ATOM   4206 O  O   . SER B 1 186 ? -6.143  21.382 19.993  1.00 28.17  ?  186 SER B O   1 
ATOM   4207 C  CB  . SER B 1 186 ? -4.154  23.715 19.152  1.00 27.13  ?  186 SER B CB  1 
ATOM   4208 O  OG  . SER B 1 186 ? -2.863  23.253 19.466  1.00 28.72  ?  186 SER B OG  1 
ATOM   4209 N  N   . PRO B 1 187 ? -4.256  20.430 19.296  1.00 29.09  ?  187 PRO B N   1 
ATOM   4210 C  CA  . PRO B 1 187 ? -4.412  19.288 20.202  1.00 31.43  ?  187 PRO B CA  1 
ATOM   4211 C  C   . PRO B 1 187 ? -4.263  19.690 21.674  1.00 29.08  ?  187 PRO B C   1 
ATOM   4212 O  O   . PRO B 1 187 ? -4.805  19.021 22.527  1.00 29.55  ?  187 PRO B O   1 
ATOM   4213 C  CB  . PRO B 1 187 ? -3.305  18.282 19.808  1.00 29.85  ?  187 PRO B CB  1 
ATOM   4214 C  CG  . PRO B 1 187 ? -2.869  18.746 18.441  1.00 31.67  ?  187 PRO B CG  1 
ATOM   4215 C  CD  . PRO B 1 187 ? -3.110  20.254 18.401  1.00 30.75  ?  187 PRO B CD  1 
ATOM   4216 N  N   . ARG B 1 188 ? -3.504  20.743 21.948  1.00 29.66  ?  188 ARG B N   1 
ATOM   4217 C  CA  . ARG B 1 188 ? -3.234  21.218 23.334  1.00 29.08  ?  188 ARG B CA  1 
ATOM   4218 C  C   . ARG B 1 188 ? -3.312  22.743 23.349  1.00 26.24  ?  188 ARG B C   1 
ATOM   4219 O  O   . ARG B 1 188 ? -3.109  23.333 22.283  1.00 24.07  ?  188 ARG B O   1 
ATOM   4220 C  CB  . ARG B 1 188 ? -1.843  20.772 23.796  1.00 33.38  ?  188 ARG B CB  1 
ATOM   4221 C  CG  . ARG B 1 188 ? -1.514  19.303 23.530  1.00 37.83  ?  188 ARG B CG  1 
ATOM   4222 C  CD  . ARG B 1 188 ? -1.543  18.372 24.736  1.00 41.81  ?  188 ARG B CD  1 
ATOM   4223 N  NE  . ARG B 1 188 ? -2.881  17.902 25.113  1.00 48.37  ?  188 ARG B NE  1 
ATOM   4224 C  CZ  . ARG B 1 188 ? -3.514  16.798 24.662  1.00 52.05  ?  188 ARG B CZ  1 
ATOM   4225 N  NH1 . ARG B 1 188 ? -2.973  15.984 23.774  1.00 43.70  ?  188 ARG B NH1 1 
ATOM   4226 N  NH2 . ARG B 1 188 ? -4.734  16.534 25.097  1.00 64.64  ?  188 ARG B NH2 1 
ATOM   4227 N  N   . THR B 1 189 ? -3.567  23.352 24.507  1.00 27.13  ?  189 THR B N   1 
ATOM   4228 C  CA  . THR B 1 189 ? -3.562  24.825 24.676  1.00 31.23  ?  189 THR B CA  1 
ATOM   4229 C  C   . THR B 1 189 ? -2.198  25.319 24.181  1.00 32.17  ?  189 THR B C   1 
ATOM   4230 O  O   . THR B 1 189 ? -1.189  24.586 24.328  1.00 32.46  ?  189 THR B O   1 
ATOM   4231 C  CB  . THR B 1 189 ? -3.949  25.267 26.102  1.00 33.81  ?  189 THR B CB  1 
ATOM   4232 O  OG1 . THR B 1 189 ? -2.882  24.940 26.982  1.00 32.69  ?  189 THR B OG1 1 
ATOM   4233 C  CG2 . THR B 1 189 ? -5.193  24.598 26.656  1.00 34.68  ?  189 THR B CG2 1 
ATOM   4234 N  N   . PHE B 1 190 ? -2.190  26.467 23.514  1.00 31.51  ?  190 PHE B N   1 
ATOM   4235 C  CA  . PHE B 1 190 ? -0.965  27.155 23.043  1.00 29.58  ?  190 PHE B CA  1 
ATOM   4236 C  C   . PHE B 1 190 ? -0.959  28.525 23.701  1.00 29.45  ?  190 PHE B C   1 
ATOM   4237 O  O   . PHE B 1 190 ? -2.007  29.148 23.935  1.00 29.26  ?  190 PHE B O   1 
ATOM   4238 C  CB  . PHE B 1 190 ? -0.866  27.208 21.514  1.00 28.47  ?  190 PHE B CB  1 
ATOM   4239 C  CG  . PHE B 1 190 ? -2.045  27.814 20.803  1.00 25.79  ?  190 PHE B CG  1 
ATOM   4240 C  CD1 . PHE B 1 190 ? -3.167  27.062 20.530  1.00 29.17  ?  190 PHE B CD1 1 
ATOM   4241 C  CD2 . PHE B 1 190 ? -2.012  29.113 20.356  1.00 27.10  ?  190 PHE B CD2 1 
ATOM   4242 C  CE1 . PHE B 1 190 ? -4.266  27.611 19.896  1.00 29.58  ?  190 PHE B CE1 1 
ATOM   4243 C  CE2 . PHE B 1 190 ? -3.101  29.669 19.701  1.00 28.99  ?  190 PHE B CE2 1 
ATOM   4244 C  CZ  . PHE B 1 190 ? -4.240  28.924 19.491  1.00 28.65  ?  190 PHE B CZ  1 
ATOM   4245 N  N   . GLU B 1 191 ? 0.217   28.941 24.117  1.00 32.54  ?  191 GLU B N   1 
ATOM   4246 C  CA  . GLU B 1 191 ? 0.383   30.288 24.686  1.00 32.26  ?  191 GLU B CA  1 
ATOM   4247 C  C   . GLU B 1 191 ? -0.160  31.193 23.589  1.00 39.70  ?  191 GLU B C   1 
ATOM   4248 O  O   . GLU B 1 191 ? -0.086  30.827 22.367  1.00 39.44  ?  191 GLU B O   1 
ATOM   4249 C  CB  . GLU B 1 191 ? 1.859   30.511 25.024  1.00 30.08  ?  191 GLU B CB  1 
ATOM   4250 C  CG  . GLU B 1 191 ? 2.122   31.804 25.753  1.00 33.87  ?  191 GLU B CG  1 
ATOM   4251 C  CD  . GLU B 1 191 ? 3.570   32.183 25.986  1.00 34.17  ?  191 GLU B CD  1 
ATOM   4252 O  OE1 . GLU B 1 191 ? 4.505   31.606 25.349  1.00 30.18  ?  191 GLU B OE1 1 
ATOM   4253 O  OE2 . GLU B 1 191 ? 3.745   33.053 26.825  1.00 37.69  ?  191 GLU B OE2 1 
ATOM   4254 N  N   . GLY B 1 192 ? -0.690  32.342 23.921  1.00 37.72  ?  192 GLY B N   1 
ATOM   4255 C  CA  . GLY B 1 192 ? -0.912  33.239 22.774  1.00 45.66  ?  192 GLY B CA  1 
ATOM   4256 C  C   . GLY B 1 192 ? -2.297  33.080 22.202  1.00 39.13  ?  192 GLY B C   1 
ATOM   4257 O  O   . GLY B 1 192 ? -2.812  34.077 21.684  1.00 36.98  ?  192 GLY B O   1 
ATOM   4258 N  N   . SER B 1 193 ? -2.941  31.939 22.416  1.00 33.74  ?  193 SER B N   1 
ATOM   4259 C  CA  . SER B 1 193 ? -4.423  31.900 22.379  1.00 35.22  ?  193 SER B CA  1 
ATOM   4260 C  C   . SER B 1 193 ? -4.989  32.907 23.413  1.00 35.74  ?  193 SER B C   1 
ATOM   4261 O  O   . SER B 1 193 ? -5.849  33.715 23.006  1.00 37.34  ?  193 SER B O   1 
ATOM   4262 C  CB  . SER B 1 193 ? -4.958  30.505 22.511  1.00 34.32  ?  193 SER B CB  1 
ATOM   4263 O  OG  . SER B 1 193 ? -4.627  29.974 23.763  1.00 41.49  ?  193 SER B OG  1 
ATOM   4264 N  N   . ALA B 1 194 ? -4.470  32.958 24.654  1.00 33.02  ?  194 ALA B N   1 
ATOM   4265 C  CA  . ALA B 1 194 ? -4.947  33.873 25.732  1.00 31.69  ?  194 ALA B CA  1 
ATOM   4266 C  C   . ALA B 1 194 ? -4.440  35.299 25.476  1.00 33.14  ?  194 ALA B C   1 
ATOM   4267 O  O   . ALA B 1 194 ? -5.241  36.240 25.631  1.00 35.88  ?  194 ALA B O   1 
ATOM   4268 C  CB  . ALA B 1 194 ? -4.529  33.392 27.113  1.00 28.23  ?  194 ALA B CB  1 
ATOM   4269 N  N   . VAL B 1 195 ? -3.157  35.461 25.124  1.00 29.28  ?  195 VAL B N   1 
ATOM   4270 C  CA  . VAL B 1 195 ? -2.557  36.784 24.794  1.00 28.92  ?  195 VAL B CA  1 
ATOM   4271 C  C   . VAL B 1 195 ? -3.411  37.422 23.698  1.00 29.18  ?  195 VAL B C   1 
ATOM   4272 O  O   . VAL B 1 195 ? -3.696  38.624 23.774  1.00 30.96  ?  195 VAL B O   1 
ATOM   4273 C  CB  . VAL B 1 195 ? -1.077  36.651 24.365  1.00 28.54  ?  195 VAL B CB  1 
ATOM   4274 C  CG1 . VAL B 1 195 ? -0.435  37.991 23.988  1.00 25.99  ?  195 VAL B CG1 1 
ATOM   4275 C  CG2 . VAL B 1 195 ? -0.250  35.934 25.431  1.00 26.43  ?  195 VAL B CG2 1 
ATOM   4276 N  N   . ASN B 1 196 ? -3.801  36.618 22.711  1.00 33.72  ?  196 ASN B N   1 
ATOM   4277 C  CA  . ASN B 1 196 ? -4.607  37.052 21.541  1.00 33.06  ?  196 ASN B CA  1 
ATOM   4278 C  C   . ASN B 1 196 ? -5.953  37.522 22.084  1.00 31.81  ?  196 ASN B C   1 
ATOM   4279 O  O   . ASN B 1 196 ? -6.265  38.704 21.885  1.00 37.23  ?  196 ASN B O   1 
ATOM   4280 C  CB  . ASN B 1 196 ? -4.693  35.954 20.486  1.00 34.71  ?  196 ASN B CB  1 
ATOM   4281 C  CG  . ASN B 1 196 ? -5.372  36.355 19.195  1.00 36.92  ?  196 ASN B CG  1 
ATOM   4282 O  OD1 . ASN B 1 196 ? -4.809  37.108 18.400  1.00 40.67  ?  196 ASN B OD1 1 
ATOM   4283 N  ND2 . ASN B 1 196 ? -6.538  35.780 18.932  1.00 39.25  ?  196 ASN B ND2 1 
ATOM   4284 N  N   . TRP B 1 197 ? -6.626  36.690 22.866  1.00 28.13  ?  197 TRP B N   1 
ATOM   4285 C  CA  . TRP B 1 197 ? -7.960  37.011 23.430  1.00 30.47  ?  197 TRP B CA  1 
ATOM   4286 C  C   . TRP B 1 197 ? -7.920  38.355 24.174  1.00 33.32  ?  197 TRP B C   1 
ATOM   4287 O  O   . TRP B 1 197 ? -8.831  39.184 23.911  1.00 30.30  ?  197 TRP B O   1 
ATOM   4288 C  CB  . TRP B 1 197 ? -8.483  35.907 24.345  1.00 33.08  ?  197 TRP B CB  1 
ATOM   4289 C  CG  . TRP B 1 197 ? -9.716  36.369 25.049  1.00 40.12  ?  197 TRP B CG  1 
ATOM   4290 C  CD1 . TRP B 1 197 ? -9.820  36.993 26.265  1.00 41.89  ?  197 TRP B CD1 1 
ATOM   4291 C  CD2 . TRP B 1 197 ? -11.037 36.350 24.489  1.00 42.98  ?  197 TRP B CD2 1 
ATOM   4292 N  NE1 . TRP B 1 197 ? -11.129 37.314 26.521  1.00 42.76  ?  197 TRP B NE1 1 
ATOM   4293 C  CE2 . TRP B 1 197 ? -11.895 36.931 25.446  1.00 40.83  ?  197 TRP B CE2 1 
ATOM   4294 C  CE3 . TRP B 1 197 ? -11.563 35.892 23.272  1.00 43.64  ?  197 TRP B CE3 1 
ATOM   4295 C  CZ2 . TRP B 1 197 ? -13.263 37.041 25.223  1.00 42.38  ?  197 TRP B CZ2 1 
ATOM   4296 C  CZ3 . TRP B 1 197 ? -12.915 36.012 23.051  1.00 43.24  ?  197 TRP B CZ3 1 
ATOM   4297 C  CH2 . TRP B 1 197 ? -13.745 36.590 24.012  1.00 45.31  ?  197 TRP B CH2 1 
ATOM   4298 N  N   . TYR B 1 198 ? -6.917  38.576 25.049  1.00 34.38  ?  198 TYR B N   1 
ATOM   4299 C  CA  . TYR B 1 198 ? -6.815  39.791 25.907  1.00 34.27  ?  198 TYR B CA  1 
ATOM   4300 C  C   . TYR B 1 198 ? -6.398  40.981 25.040  1.00 33.45  ?  198 TYR B C   1 
ATOM   4301 O  O   . TYR B 1 198 ? -6.756  42.107 25.365  1.00 32.89  ?  198 TYR B O   1 
ATOM   4302 C  CB  . TYR B 1 198 ? -5.927  39.557 27.139  1.00 36.63  ?  198 TYR B CB  1 
ATOM   4303 C  CG  . TYR B 1 198 ? -6.591  38.676 28.169  1.00 42.34  ?  198 TYR B CG  1 
ATOM   4304 C  CD1 . TYR B 1 198 ? -7.775  39.072 28.779  1.00 44.09  ?  198 TYR B CD1 1 
ATOM   4305 C  CD2 . TYR B 1 198 ? -6.098  37.409 28.462  1.00 43.96  ?  198 TYR B CD2 1 
ATOM   4306 C  CE1 . TYR B 1 198 ? -8.444  38.242 29.662  1.00 47.79  ?  198 TYR B CE1 1 
ATOM   4307 C  CE2 . TYR B 1 198 ? -6.739  36.575 29.364  1.00 45.93  ?  198 TYR B CE2 1 
ATOM   4308 C  CZ  . TYR B 1 198 ? -7.921  36.991 29.955  1.00 50.24  ?  198 TYR B CZ  1 
ATOM   4309 O  OH  . TYR B 1 198 ? -8.572  36.173 30.832  1.00 50.74  ?  198 TYR B OH  1 
ATOM   4310 N  N   . LYS B 1 199 ? -5.717  40.748 23.924  1.00 33.55  ?  199 LYS B N   1 
ATOM   4311 C  CA  . LYS B 1 199 ? -5.288  41.866 23.045  1.00 35.94  ?  199 LYS B CA  1 
ATOM   4312 C  C   . LYS B 1 199 ? -6.528  42.580 22.474  1.00 35.69  ?  199 LYS B C   1 
ATOM   4313 O  O   . LYS B 1 199 ? -6.635  43.807 22.562  1.00 37.66  ?  199 LYS B O   1 
ATOM   4314 C  CB  . LYS B 1 199 ? -4.397  41.303 21.942  1.00 35.72  ?  199 LYS B CB  1 
ATOM   4315 C  CG  . LYS B 1 199 ? -3.816  42.342 21.010  1.00 33.80  ?  199 LYS B CG  1 
ATOM   4316 C  CD  . LYS B 1 199 ? -3.714  41.796 19.628  1.00 36.14  ?  199 LYS B CD  1 
ATOM   4317 C  CE  . LYS B 1 199 ? -2.990  42.677 18.635  1.00 35.12  ?  199 LYS B CE  1 
ATOM   4318 N  NZ  . LYS B 1 199 ? -2.172  41.862 17.701  1.00 34.29  ?  199 LYS B NZ  1 
ATOM   4319 N  N   . ASP B 1 200 ? -7.435  41.818 21.891  1.00 34.82  ?  200 ASP B N   1 
ATOM   4320 C  CA  . ASP B 1 200 ? -8.626  42.347 21.190  1.00 34.87  ?  200 ASP B CA  1 
ATOM   4321 C  C   . ASP B 1 200 ? -9.726  42.620 22.218  1.00 33.62  ?  200 ASP B C   1 
ATOM   4322 O  O   . ASP B 1 200 ? -10.585 43.452 21.937  1.00 29.87  ?  200 ASP B O   1 
ATOM   4323 C  CB  . ASP B 1 200 ? -9.049  41.393 20.074  1.00 34.28  ?  200 ASP B CB  1 
ATOM   4324 C  CG  . ASP B 1 200 ? -8.095  41.420 18.904  1.00 35.61  ?  200 ASP B CG  1 
ATOM   4325 O  OD1 . ASP B 1 200 ? -7.312  42.415 18.815  1.00 34.98  ?  200 ASP B OD1 1 
ATOM   4326 O  OD2 . ASP B 1 200 ? -8.113  40.428 18.122  1.00 38.58  ?  200 ASP B OD2 1 
ATOM   4327 N  N   . LEU B 1 201 ? -9.692  41.975 23.383  1.00 37.21  ?  201 LEU B N   1 
ATOM   4328 C  CA  . LEU B 1 201 ? -10.629 42.366 24.468  1.00 37.63  ?  201 LEU B CA  1 
ATOM   4329 C  C   . LEU B 1 201 ? -10.326 43.823 24.804  1.00 35.67  ?  201 LEU B C   1 
ATOM   4330 O  O   . LEU B 1 201 ? -11.256 44.587 24.925  1.00 32.75  ?  201 LEU B O   1 
ATOM   4331 C  CB  . LEU B 1 201 ? -10.448 41.490 25.699  1.00 37.10  ?  201 LEU B CB  1 
ATOM   4332 C  CG  . LEU B 1 201 ? -11.567 41.651 26.717  1.00 40.34  ?  201 LEU B CG  1 
ATOM   4333 C  CD1 . LEU B 1 201 ? -12.875 41.173 26.119  1.00 44.75  ?  201 LEU B CD1 1 
ATOM   4334 C  CD2 . LEU B 1 201 ? -11.259 40.899 27.998  1.00 40.58  ?  201 LEU B CD2 1 
ATOM   4335 N  N   . GLY B 1 202 ? -9.037  44.145 24.873  1.00 34.39  ?  202 GLY B N   1 
ATOM   4336 C  CA  . GLY B 1 202 ? -8.499  45.481 25.154  1.00 39.83  ?  202 GLY B CA  1 
ATOM   4337 C  C   . GLY B 1 202 ? -8.950  46.498 24.136  1.00 39.38  ?  202 GLY B C   1 
ATOM   4338 O  O   . GLY B 1 202 ? -9.327  47.599 24.563  1.00 43.29  ?  202 GLY B O   1 
ATOM   4339 N  N   . TYR B 1 203 ? -8.906  46.127 22.854  1.00 39.41  ?  203 TYR B N   1 
ATOM   4340 C  CA  . TYR B 1 203 ? -9.397  46.924 21.703  1.00 36.83  ?  203 TYR B CA  1 
ATOM   4341 C  C   . TYR B 1 203 ? -10.873 47.269 21.954  1.00 37.42  ?  203 TYR B C   1 
ATOM   4342 O  O   . TYR B 1 203 ? -11.287 48.451 21.891  1.00 34.97  ?  203 TYR B O   1 
ATOM   4343 C  CB  . TYR B 1 203 ? -9.179  46.161 20.389  1.00 35.28  ?  203 TYR B CB  1 
ATOM   4344 C  CG  . TYR B 1 203 ? -9.420  46.982 19.135  1.00 35.60  ?  203 TYR B CG  1 
ATOM   4345 C  CD1 . TYR B 1 203 ? -10.716 47.216 18.664  1.00 35.02  ?  203 TYR B CD1 1 
ATOM   4346 C  CD2 . TYR B 1 203 ? -8.366  47.533 18.411  1.00 33.48  ?  203 TYR B CD2 1 
ATOM   4347 C  CE1 . TYR B 1 203 ? -10.964 47.957 17.513  1.00 33.89  ?  203 TYR B CE1 1 
ATOM   4348 C  CE2 . TYR B 1 203 ? -8.599  48.277 17.255  1.00 36.67  ?  203 TYR B CE2 1 
ATOM   4349 C  CZ  . TYR B 1 203 ? -9.903  48.513 16.825  1.00 35.92  ?  203 TYR B CZ  1 
ATOM   4350 O  OH  . TYR B 1 203 ? -10.165 49.253 15.713  1.00 36.45  ?  203 TYR B OH  1 
ATOM   4351 N  N   . MET B 1 204 ? -11.672 46.255 22.246  1.00 36.21  ?  204 MET B N   1 
ATOM   4352 C  CA  . MET B 1 204 ? -13.120 46.461 22.480  1.00 43.52  ?  204 MET B CA  1 
ATOM   4353 C  C   . MET B 1 204 ? -13.362 47.346 23.717  1.00 42.10  ?  204 MET B C   1 
ATOM   4354 O  O   . MET B 1 204 ? -14.278 48.165 23.654  1.00 37.65  ?  204 MET B O   1 
ATOM   4355 C  CB  . MET B 1 204 ? -13.835 45.113 22.614  1.00 46.47  ?  204 MET B CB  1 
ATOM   4356 C  CG  . MET B 1 204 ? -13.891 44.370 21.294  1.00 47.03  ?  204 MET B CG  1 
ATOM   4357 S  SD  . MET B 1 204 ? -14.257 45.468 19.898  1.00 44.51  ?  204 MET B SD  1 
ATOM   4358 C  CE  . MET B 1 204 ? -13.883 44.365 18.539  1.00 47.05  ?  204 MET B CE  1 
ATOM   4359 N  N   . VAL B 1 205 ? -12.574 47.205 24.792  1.00 41.06  ?  205 VAL B N   1 
ATOM   4360 C  CA  . VAL B 1 205 ? -12.733 48.024 26.029  1.00 38.80  ?  205 VAL B CA  1 
ATOM   4361 C  C   . VAL B 1 205 ? -12.385 49.475 25.700  1.00 40.42  ?  205 VAL B C   1 
ATOM   4362 O  O   . VAL B 1 205 ? -13.122 50.354 26.117  1.00 42.30  ?  205 VAL B O   1 
ATOM   4363 C  CB  . VAL B 1 205 ? -11.870 47.498 27.181  1.00 36.46  ?  205 VAL B CB  1 
ATOM   4364 C  CG1 . VAL B 1 205 ? -11.658 48.552 28.246  1.00 37.52  ?  205 VAL B CG1 1 
ATOM   4365 C  CG2 . VAL B 1 205 ? -12.487 46.259 27.794  1.00 37.18  ?  205 VAL B CG2 1 
ATOM   4366 N  N   . ASP B 1 206 ? -11.294 49.702 24.976  1.00 40.17  ?  206 ASP B N   1 
ATOM   4367 C  CA  . ASP B 1 206 ? -10.868 51.062 24.571  1.00 45.87  ?  206 ASP B CA  1 
ATOM   4368 C  C   . ASP B 1 206 ? -11.983 51.722 23.725  1.00 49.09  ?  206 ASP B C   1 
ATOM   4369 O  O   . ASP B 1 206 ? -12.314 52.893 24.014  1.00 48.23  ?  206 ASP B O   1 
ATOM   4370 C  CB  . ASP B 1 206 ? -9.475  51.021 23.927  1.00 45.83  ?  206 ASP B CB  1 
ATOM   4371 C  CG  . ASP B 1 206 ? -8.367  50.469 24.823  1.00 48.66  ?  206 ASP B CG  1 
ATOM   4372 O  OD1 . ASP B 1 206 ? -8.635  50.203 26.031  1.00 50.91  ?  206 ASP B OD1 1 
ATOM   4373 O  OD2 . ASP B 1 206 ? -7.236  50.289 24.310  1.00 48.46  ?  206 ASP B OD2 1 
ATOM   4374 N  N   . ARG B 1 207 ? -12.561 51.019 22.741  1.00 51.28  ?  207 ARG B N   1 
ATOM   4375 C  CA  . ARG B 1 207 ? -13.563 51.593 21.791  1.00 50.84  ?  207 ARG B CA  1 
ATOM   4376 C  C   . ARG B 1 207 ? -14.830 51.968 22.560  1.00 47.94  ?  207 ARG B C   1 
ATOM   4377 O  O   . ARG B 1 207 ? -15.481 52.982 22.161  1.00 45.97  ?  207 ARG B O   1 
ATOM   4378 C  CB  . ARG B 1 207 ? -13.974 50.619 20.683  1.00 49.75  ?  207 ARG B CB  1 
ATOM   4379 C  CG  . ARG B 1 207 ? -12.861 50.240 19.721  1.00 50.67  ?  207 ARG B CG  1 
ATOM   4380 C  CD  . ARG B 1 207 ? -12.268 51.406 18.956  1.00 53.28  ?  207 ARG B CD  1 
ATOM   4381 N  NE  . ARG B 1 207 ? -11.356 52.189 19.768  1.00 58.42  ?  207 ARG B NE  1 
ATOM   4382 C  CZ  . ARG B 1 207 ? -10.150 51.791 20.174  1.00 63.79  ?  207 ARG B CZ  1 
ATOM   4383 N  NH1 . ARG B 1 207 ? -9.680  50.596 19.850  1.00 55.29  ?  207 ARG B NH1 1 
ATOM   4384 N  NH2 . ARG B 1 207 ? -9.421  52.593 20.937  1.00 69.07  ?  207 ARG B NH2 1 
ATOM   4385 N  N   . LEU B 1 208 ? -15.140 51.175 23.590  1.00 42.58  ?  208 LEU B N   1 
ATOM   4386 C  CA  . LEU B 1 208 ? -16.346 51.310 24.450  1.00 49.32  ?  208 LEU B CA  1 
ATOM   4387 C  C   . LEU B 1 208 ? -16.172 52.485 25.418  1.00 51.45  ?  208 LEU B C   1 
ATOM   4388 O  O   . LEU B 1 208 ? -17.216 53.049 25.794  1.00 58.92  ?  208 LEU B O   1 
ATOM   4389 C  CB  . LEU B 1 208 ? -16.590 50.002 25.218  1.00 51.52  ?  208 LEU B CB  1 
ATOM   4390 C  CG  . LEU B 1 208 ? -17.594 50.059 26.373  1.00 50.42  ?  208 LEU B CG  1 
ATOM   4391 C  CD1 . LEU B 1 208 ? -19.015 50.167 25.836  1.00 53.84  ?  208 LEU B CD1 1 
ATOM   4392 C  CD2 . LEU B 1 208 ? -17.472 48.854 27.292  1.00 44.78  ?  208 LEU B CD2 1 
ATOM   4393 N  N   . ASN B 1 209 ? -14.944 52.749 25.854  1.00 50.57  ?  209 ASN B N   1 
ATOM   4394 C  CA  . ASN B 1 209 ? -14.696 53.791 26.880  1.00 50.12  ?  209 ASN B CA  1 
ATOM   4395 C  C   . ASN B 1 209 ? -14.013 54.984 26.218  1.00 55.25  ?  209 ASN B C   1 
ATOM   4396 O  O   . ASN B 1 209 ? -13.303 55.719 26.920  1.00 63.58  ?  209 ASN B O   1 
ATOM   4397 C  CB  . ASN B 1 209 ? -13.880 53.230 28.034  1.00 48.58  ?  209 ASN B CB  1 
ATOM   4398 C  CG  . ASN B 1 209 ? -14.583 52.110 28.757  1.00 53.12  ?  209 ASN B CG  1 
ATOM   4399 O  OD1 . ASN B 1 209 ? -15.809 52.006 28.694  1.00 56.35  ?  209 ASN B OD1 1 
ATOM   4400 N  ND2 . ASN B 1 209 ? -13.832 51.271 29.452  1.00 47.23  ?  209 ASN B ND2 1 
ATOM   4401 N  N   . ALA B 1 210 ? -14.241 55.173 24.924  1.00 59.04  ?  210 ALA B N   1 
ATOM   4402 C  CA  . ALA B 1 210 ? -13.647 56.303 24.176  1.00 63.95  ?  210 ALA B CA  1 
ATOM   4403 C  C   . ALA B 1 210 ? -14.127 57.644 24.728  1.00 72.84  ?  210 ALA B C   1 
ATOM   4404 O  O   . ALA B 1 210 ? -15.265 57.722 25.223  1.00 60.64  ?  210 ALA B O   1 
ATOM   4405 C  CB  . ALA B 1 210 ? -14.006 56.167 22.726  1.00 62.38  ?  210 ALA B CB  1 
ATOM   4406 N  N   . ASP B 1 211 ? -13.272 58.669 24.636  1.00 85.34  ?  211 ASP B N   1 
ATOM   4407 C  CA  . ASP B 1 211 ? -13.646 60.025 25.118  1.00 90.14  ?  211 ASP B CA  1 
ATOM   4408 C  C   . ASP B 1 211 ? -14.931 60.417 24.405  1.00 95.16  ?  211 ASP B C   1 
ATOM   4409 O  O   . ASP B 1 211 ? -15.921 60.705 25.110  1.00 105.00 ?  211 ASP B O   1 
ATOM   4410 C  CB  . ASP B 1 211 ? -12.522 61.038 24.982  1.00 99.73  ?  211 ASP B CB  1 
ATOM   4411 C  CG  . ASP B 1 211 ? -12.566 62.181 25.985  1.00 96.52  ?  211 ASP B CG  1 
ATOM   4412 O  OD1 . ASP B 1 211 ? -13.684 62.582 26.367  1.00 84.22  ?  211 ASP B OD1 1 
ATOM   4413 O  OD2 . ASP B 1 211 ? -11.482 62.656 26.381  1.00 92.00  ?  211 ASP B OD2 1 
ATOM   4414 N  N   . PRO B 1 212 ? -14.985 60.487 23.061  1.00 77.51  ?  212 PRO B N   1 
ATOM   4415 C  CA  . PRO B 1 212 ? -16.263 60.696 22.418  1.00 75.35  ?  212 PRO B CA  1 
ATOM   4416 C  C   . PRO B 1 212 ? -16.878 59.322 22.629  1.00 74.85  ?  212 PRO B C   1 
ATOM   4417 O  O   . PRO B 1 212 ? -16.555 58.392 21.872  1.00 71.67  ?  212 PRO B O   1 
ATOM   4418 C  CB  . PRO B 1 212 ? -15.895 61.004 20.981  1.00 73.85  ?  212 PRO B CB  1 
ATOM   4419 C  CG  . PRO B 1 212 ? -14.428 61.362 21.051  1.00 77.15  ?  212 PRO B CG  1 
ATOM   4420 C  CD  . PRO B 1 212 ? -13.881 60.441 22.120  1.00 68.17  ?  212 PRO B CD  1 
ATOM   4421 N  N   . GLU B 1 213 ? -17.712 59.174 23.661  1.00 66.56  ?  213 GLU B N   1 
ATOM   4422 C  CA  . GLU B 1 213 ? -18.306 57.852 23.984  1.00 63.70  ?  213 GLU B CA  1 
ATOM   4423 C  C   . GLU B 1 213 ? -19.033 57.324 22.753  1.00 67.74  ?  213 GLU B C   1 
ATOM   4424 O  O   . GLU B 1 213 ? -19.729 58.110 22.086  1.00 67.39  ?  213 GLU B O   1 
ATOM   4425 C  CB  . GLU B 1 213 ? -19.303 57.937 25.133  1.00 69.42  ?  213 GLU B CB  1 
ATOM   4426 C  CG  . GLU B 1 213 ? -18.702 58.285 26.490  1.00 66.99  ?  213 GLU B CG  1 
ATOM   4427 C  CD  . GLU B 1 213 ? -19.733 58.430 27.591  1.00 73.83  ?  213 GLU B CD  1 
ATOM   4428 O  OE1 . GLU B 1 213 ? -20.937 58.448 27.270  1.00 77.23  ?  213 GLU B OE1 1 
ATOM   4429 O  OE2 . GLU B 1 213 ? -19.330 58.523 28.768  1.00 70.70  ?  213 GLU B OE2 1 
ATOM   4430 N  N   . PRO B 1 214 ? -18.932 56.022 22.440  1.00 63.05  ?  214 PRO B N   1 
ATOM   4431 C  CA  . PRO B 1 214 ? -19.525 55.465 21.245  1.00 57.67  ?  214 PRO B CA  1 
ATOM   4432 C  C   . PRO B 1 214 ? -21.016 55.528 21.114  1.00 54.81  ?  214 PRO B C   1 
ATOM   4433 O  O   . PRO B 1 214 ? -21.759 55.055 21.985  1.00 53.23  ?  214 PRO B O   1 
ATOM   4434 C  CB  . PRO B 1 214 ? -19.034 54.005 21.292  1.00 56.57  ?  214 PRO B CB  1 
ATOM   4435 C  CG  . PRO B 1 214 ? -18.926 53.705 22.754  1.00 61.05  ?  214 PRO B CG  1 
ATOM   4436 C  CD  . PRO B 1 214 ? -18.213 54.959 23.190  1.00 65.76  ?  214 PRO B CD  1 
ATOM   4437 N  N   . THR B 1 215 ? -21.458 56.178 20.051  1.00 50.54  ?  215 THR B N   1 
ATOM   4438 C  CA  . THR B 1 215 ? -22.869 56.119 19.707  1.00 49.69  ?  215 THR B CA  1 
ATOM   4439 C  C   . THR B 1 215 ? -22.839 55.126 18.589  1.00 61.05  ?  215 THR B C   1 
ATOM   4440 O  O   . THR B 1 215 ? -21.712 54.830 18.135  1.00 67.28  ?  215 THR B O   1 
ATOM   4441 C  CB  . THR B 1 215 ? -23.297 57.497 19.239  1.00 51.49  ?  215 THR B CB  1 
ATOM   4442 O  OG1 . THR B 1 215 ? -22.430 57.767 18.143  1.00 51.59  ?  215 THR B OG1 1 
ATOM   4443 C  CG2 . THR B 1 215 ? -23.125 58.550 20.317  1.00 46.12  ?  215 THR B CG2 1 
ATOM   4444 N  N   . GLU B 1 216 ? -23.977 54.586 18.177  1.00 56.72  ?  216 GLU B N   1 
ATOM   4445 C  CA  . GLU B 1 216 ? -24.007 53.668 17.005  1.00 54.68  ?  216 GLU B CA  1 
ATOM   4446 C  C   . GLU B 1 216 ? -23.513 52.254 17.362  1.00 45.55  ?  216 GLU B C   1 
ATOM   4447 O  O   . GLU B 1 216 ? -22.481 52.119 18.036  1.00 37.90  ?  216 GLU B O   1 
ATOM   4448 C  CB  . GLU B 1 216 ? -23.235 54.210 15.795  1.00 56.53  ?  216 GLU B CB  1 
ATOM   4449 C  CG  . GLU B 1 216 ? -23.689 55.590 15.335  1.00 53.61  ?  216 GLU B CG  1 
ATOM   4450 C  CD  . GLU B 1 216 ? -24.892 55.503 14.423  1.00 56.89  ?  216 GLU B CD  1 
ATOM   4451 O  OE1 . GLU B 1 216 ? -24.713 55.051 13.277  1.00 74.73  ?  216 GLU B OE1 1 
ATOM   4452 O  OE2 . GLU B 1 216 ? -25.999 55.876 14.858  1.00 56.46  ?  216 GLU B OE2 1 
ATOM   4453 N  N   . GLY B 1 217 ? -24.273 51.239 16.965  1.00 41.52  ?  217 GLY B N   1 
ATOM   4454 C  CA  . GLY B 1 217 ? -23.821 49.849 17.134  1.00 44.60  ?  217 GLY B CA  1 
ATOM   4455 C  C   . GLY B 1 217 ? -24.130 49.204 18.457  1.00 44.25  ?  217 GLY B C   1 
ATOM   4456 O  O   . GLY B 1 217 ? -24.936 49.759 19.221  1.00 38.82  ?  217 GLY B O   1 
ATOM   4457 N  N   . LEU B 1 218 ? -23.525 48.043 18.688  1.00 41.03  ?  218 LEU B N   1 
ATOM   4458 C  CA  . LEU B 1 218 ? -23.691 47.319 19.962  1.00 39.37  ?  218 LEU B CA  1 
ATOM   4459 C  C   . LEU B 1 218 ? -22.902 48.063 21.041  1.00 40.45  ?  218 LEU B C   1 
ATOM   4460 O  O   . LEU B 1 218 ? -23.317 48.032 22.201  1.00 48.31  ?  218 LEU B O   1 
ATOM   4461 C  CB  . LEU B 1 218 ? -23.166 45.902 19.748  1.00 36.37  ?  218 LEU B CB  1 
ATOM   4462 C  CG  . LEU B 1 218 ? -23.312 44.924 20.914  1.00 36.75  ?  218 LEU B CG  1 
ATOM   4463 C  CD1 . LEU B 1 218 ? -24.738 44.440 21.043  1.00 37.01  ?  218 LEU B CD1 1 
ATOM   4464 C  CD2 . LEU B 1 218 ? -22.373 43.756 20.709  1.00 38.56  ?  218 LEU B CD2 1 
ATOM   4465 N  N   . LEU B 1 219 ? -21.825 48.734 20.650  1.00 38.21  ?  219 LEU B N   1 
ATOM   4466 C  CA  . LEU B 1 219 ? -21.060 49.510 21.658  1.00 43.10  ?  219 LEU B CA  1 
ATOM   4467 C  C   . LEU B 1 219 ? -21.883 50.756 22.038  1.00 51.68  ?  219 LEU B C   1 
ATOM   4468 O  O   . LEU B 1 219 ? -21.857 51.129 23.233  1.00 54.63  ?  219 LEU B O   1 
ATOM   4469 C  CB  . LEU B 1 219 ? -19.653 49.854 21.139  1.00 40.57  ?  219 LEU B CB  1 
ATOM   4470 C  CG  . LEU B 1 219 ? -18.687 48.680 20.887  1.00 44.28  ?  219 LEU B CG  1 
ATOM   4471 C  CD1 . LEU B 1 219 ? -17.394 49.167 20.239  1.00 48.65  ?  219 LEU B CD1 1 
ATOM   4472 C  CD2 . LEU B 1 219 ? -18.339 47.897 22.154  1.00 42.42  ?  219 LEU B CD2 1 
ATOM   4473 N  N   . GLY B 1 220 ? -22.606 51.364 21.084  1.00 53.04  ?  220 GLY B N   1 
ATOM   4474 C  CA  . GLY B 1 220 ? -23.599 52.431 21.358  1.00 49.43  ?  220 GLY B CA  1 
ATOM   4475 C  C   . GLY B 1 220 ? -24.648 51.960 22.353  1.00 42.86  ?  220 GLY B C   1 
ATOM   4476 O  O   . GLY B 1 220 ? -24.768 52.555 23.419  1.00 46.60  ?  220 GLY B O   1 
ATOM   4477 N  N   . ARG B 1 221 ? -25.338 50.869 22.047  1.00 41.12  ?  221 ARG B N   1 
ATOM   4478 C  CA  . ARG B 1 221 ? -26.335 50.243 22.952  1.00 40.79  ?  221 ARG B CA  1 
ATOM   4479 C  C   . ARG B 1 221 ? -25.694 49.830 24.280  1.00 39.42  ?  221 ARG B C   1 
ATOM   4480 O  O   . ARG B 1 221 ? -26.393 49.843 25.279  1.00 44.87  ?  221 ARG B O   1 
ATOM   4481 C  CB  . ARG B 1 221 ? -26.963 49.017 22.298  1.00 42.12  ?  221 ARG B CB  1 
ATOM   4482 C  CG  . ARG B 1 221 ? -27.839 49.351 21.107  1.00 46.92  ?  221 ARG B CG  1 
ATOM   4483 C  CD  . ARG B 1 221 ? -28.239 48.086 20.381  1.00 52.33  ?  221 ARG B CD  1 
ATOM   4484 N  NE  . ARG B 1 221 ? -29.103 48.407 19.264  1.00 54.96  ?  221 ARG B NE  1 
ATOM   4485 C  CZ  . ARG B 1 221 ? -28.768 48.323 17.982  1.00 59.04  ?  221 ARG B CZ  1 
ATOM   4486 N  NH1 . ARG B 1 221 ? -27.573 47.873 17.607  1.00 52.48  ?  221 ARG B NH1 1 
ATOM   4487 N  NH2 . ARG B 1 221 ? -29.671 48.672 17.077  1.00 62.48  ?  221 ARG B NH2 1 
ATOM   4488 N  N   . PHE B 1 222 ? -24.420 49.451 24.308  1.00 42.58  ?  222 PHE B N   1 
ATOM   4489 C  CA  . PHE B 1 222 ? -23.762 49.013 25.566  1.00 45.64  ?  222 PHE B CA  1 
ATOM   4490 C  C   . PHE B 1 222 ? -23.515 50.253 26.446  1.00 46.25  ?  222 PHE B C   1 
ATOM   4491 O  O   . PHE B 1 222 ? -23.768 50.151 27.652  1.00 47.78  ?  222 PHE B O   1 
ATOM   4492 C  CB  . PHE B 1 222 ? -22.543 48.123 25.275  1.00 44.32  ?  222 PHE B CB  1 
ATOM   4493 C  CG  . PHE B 1 222 ? -22.869 46.675 24.965  1.00 45.22  ?  222 PHE B CG  1 
ATOM   4494 C  CD1 . PHE B 1 222 ? -24.156 46.169 25.094  1.00 46.44  ?  222 PHE B CD1 1 
ATOM   4495 C  CD2 . PHE B 1 222 ? -21.871 45.800 24.562  1.00 45.09  ?  222 PHE B CD2 1 
ATOM   4496 C  CE1 . PHE B 1 222 ? -24.432 44.841 24.807  1.00 48.09  ?  222 PHE B CE1 1 
ATOM   4497 C  CE2 . PHE B 1 222 ? -22.144 44.473 24.289  1.00 41.74  ?  222 PHE B CE2 1 
ATOM   4498 C  CZ  . PHE B 1 222 ? -23.423 43.994 24.411  1.00 46.35  ?  222 PHE B CZ  1 
ATOM   4499 N  N   . ALA B 1 223 ? -23.099 51.386 25.871  1.00 44.75  ?  223 ALA B N   1 
ATOM   4500 C  CA  . ALA B 1 223 ? -22.791 52.628 26.615  1.00 48.65  ?  223 ALA B CA  1 
ATOM   4501 C  C   . ALA B 1 223 ? -24.091 53.207 27.177  1.00 54.86  ?  223 ALA B C   1 
ATOM   4502 O  O   . ALA B 1 223 ? -24.114 53.601 28.365  1.00 58.79  ?  223 ALA B O   1 
ATOM   4503 C  CB  . ALA B 1 223 ? -22.074 53.620 25.734  1.00 50.79  ?  223 ALA B CB  1 
ATOM   4504 N  N   . GLU B 1 224 ? -25.143 53.230 26.361  1.00 56.48  ?  224 GLU B N   1 
ATOM   4505 C  CA  . GLU B 1 224 ? -26.503 53.554 26.837  1.00 58.90  ?  224 GLU B CA  1 
ATOM   4506 C  C   . GLU B 1 224 ? -26.833 52.641 28.018  1.00 58.96  ?  224 GLU B C   1 
ATOM   4507 O  O   . GLU B 1 224 ? -27.390 53.148 28.989  1.00 62.52  ?  224 GLU B O   1 
ATOM   4508 C  CB  . GLU B 1 224 ? -27.534 53.361 25.730  1.00 69.06  ?  224 GLU B CB  1 
ATOM   4509 C  CG  . GLU B 1 224 ? -27.403 54.339 24.574  1.00 75.93  ?  224 GLU B CG  1 
ATOM   4510 C  CD  . GLU B 1 224 ? -28.401 54.071 23.457  1.00 82.44  ?  224 GLU B CD  1 
ATOM   4511 O  OE1 . GLU B 1 224 ? -29.064 53.001 23.505  1.00 85.41  ?  224 GLU B OE1 1 
ATOM   4512 O  OE2 . GLU B 1 224 ? -28.512 54.919 22.542  1.00 79.83  ?  224 GLU B OE2 1 
ATOM   4513 N  N   . LEU B 1 225 ? -26.485 51.353 27.942  1.00 61.39  ?  225 LEU B N   1 
ATOM   4514 C  CA  . LEU B 1 225 ? -27.059 50.290 28.818  1.00 67.90  ?  225 LEU B CA  1 
ATOM   4515 C  C   . LEU B 1 225 ? -26.407 50.262 30.210  1.00 62.67  ?  225 LEU B C   1 
ATOM   4516 O  O   . LEU B 1 225 ? -27.097 49.855 31.142  1.00 57.82  ?  225 LEU B O   1 
ATOM   4517 C  CB  . LEU B 1 225 ? -26.919 48.934 28.116  1.00 74.05  ?  225 LEU B CB  1 
ATOM   4518 C  CG  . LEU B 1 225 ? -27.655 47.770 28.776  1.00 78.61  ?  225 LEU B CG  1 
ATOM   4519 C  CD1 . LEU B 1 225 ? -28.217 46.820 27.727  1.00 88.26  ?  225 LEU B CD1 1 
ATOM   4520 C  CD2 . LEU B 1 225 ? -26.748 47.017 29.736  1.00 79.38  ?  225 LEU B CD2 1 
ATOM   4521 N  N   . ARG B 1 226 ? -25.130 50.625 30.354  1.00 67.80  ?  226 ARG B N   1 
ATOM   4522 C  CA  . ARG B 1 226 ? -24.384 50.516 31.648  1.00 72.74  ?  226 ARG B CA  1 
ATOM   4523 C  C   . ARG B 1 226 ? -24.569 51.803 32.476  1.00 72.88  ?  226 ARG B C   1 
ATOM   4524 O  O   . ARG B 1 226 ? -23.899 51.933 33.516  1.00 67.62  ?  226 ARG B O   1 
ATOM   4525 C  CB  . ARG B 1 226 ? -22.897 50.215 31.403  1.00 64.81  ?  226 ARG B CB  1 
ATOM   4526 C  CG  . ARG B 1 226 ? -22.122 51.353 30.751  1.00 60.54  ?  226 ARG B CG  1 
ATOM   4527 C  CD  . ARG B 1 226 ? -20.640 51.033 30.617  1.00 56.57  ?  226 ARG B CD  1 
ATOM   4528 N  NE  . ARG B 1 226 ? -19.991 52.062 29.818  1.00 48.44  ?  226 ARG B NE  1 
ATOM   4529 C  CZ  . ARG B 1 226 ? -18.711 52.082 29.511  1.00 50.37  ?  226 ARG B CZ  1 
ATOM   4530 N  NH1 . ARG B 1 226 ? -17.921 51.114 29.934  1.00 59.56  ?  226 ARG B NH1 1 
ATOM   4531 N  NH2 . ARG B 1 226 ? -18.218 53.057 28.763  1.00 55.91  ?  226 ARG B NH2 1 
ATOM   4532 N  N   . ARG B 1 227 ? -25.505 52.648 32.035  1.00 71.88  ?  227 ARG B N   1 
ATOM   4533 C  CA  . ARG B 1 227 ? -25.840 53.900 32.749  1.00 69.39  ?  227 ARG B CA  1 
ATOM   4534 C  C   . ARG B 1 227 ? -27.285 53.793 33.247  1.00 66.09  ?  227 ARG B C   1 
ATOM   4535 O  O   . ARG B 1 227 ? -27.899 54.833 33.515  1.00 69.35  ?  227 ARG B O   1 
ATOM   4536 C  CB  . ARG B 1 227 ? -25.742 55.071 31.775  1.00 72.15  ?  227 ARG B CB  1 
ATOM   4537 C  CG  . ARG B 1 227 ? -24.348 55.455 31.308  1.00 75.26  ?  227 ARG B CG  1 
ATOM   4538 C  CD  . ARG B 1 227 ? -24.428 56.766 30.550  1.00 80.43  ?  227 ARG B CD  1 
ATOM   4539 N  NE  . ARG B 1 227 ? -24.524 56.569 29.101  1.00 88.58  ?  227 ARG B NE  1 
ATOM   4540 C  CZ  . ARG B 1 227 ? -23.493 56.699 28.280  1.00 94.73  ?  227 ARG B CZ  1 
ATOM   4541 N  NH1 . ARG B 1 227 ? -22.275 56.815 28.777  1.00 87.36  ?  227 ARG B NH1 1 
ATOM   4542 N  NH2 . ARG B 1 227 ? -23.679 56.707 26.972  1.00 88.78  ?  227 ARG B NH2 1 
ATOM   4543 N  N   . SER B 1 228 ? -27.803 52.574 33.354  1.00 73.39  ?  228 SER B N   1 
ATOM   4544 C  CA  . SER B 1 228 ? -29.200 52.363 33.803  1.00 79.31  ?  228 SER B CA  1 
ATOM   4545 C  C   . SER B 1 228 ? -29.195 51.510 35.073  1.00 88.82  ?  228 SER B C   1 
ATOM   4546 O  O   . SER B 1 228 ? -28.094 51.136 35.524  1.00 82.93  ?  228 SER B O   1 
ATOM   4547 C  CB  . SER B 1 228 ? -29.982 51.626 32.755  1.00 80.61  ?  228 SER B CB  1 
ATOM   4548 O  OG  . SER B 1 228 ? -29.476 50.317 32.539  1.00 79.43  ?  228 SER B OG  1 
ATOM   4549 N  N   . PRO B 1 229 ? -30.369 51.190 35.660  1.00 104.35 ?  229 PRO B N   1 
ATOM   4550 C  CA  . PRO B 1 229 ? -30.415 50.294 36.810  1.00 108.70 ?  229 PRO B CA  1 
ATOM   4551 C  C   . PRO B 1 229 ? -31.631 49.376 36.823  1.00 106.24 ?  229 PRO B C   1 
ATOM   4552 O  O   . PRO B 1 229 ? -31.738 48.517 35.928  1.00 104.13 ?  229 PRO B O   1 
ATOM   4553 C  CB  . PRO B 1 229 ? -30.462 51.340 37.919  1.00 112.85 ?  229 PRO B CB  1 
ATOM   4554 N  N   . VAL B 1 235 ? -23.343 43.739 34.943  1.00 88.82  ?  235 VAL B N   1 
ATOM   4555 C  CA  . VAL B 1 235 ? -22.643 43.853 33.625  1.00 74.70  ?  235 VAL B CA  1 
ATOM   4556 C  C   . VAL B 1 235 ? -21.459 44.833 33.711  1.00 63.57  ?  235 VAL B C   1 
ATOM   4557 O  O   . VAL B 1 235 ? -21.650 46.053 33.510  1.00 61.77  ?  235 VAL B O   1 
ATOM   4558 C  CB  . VAL B 1 235 ? -23.603 44.246 32.482  1.00 73.77  ?  235 VAL B CB  1 
ATOM   4559 C  CG1 . VAL B 1 235 ? -24.166 45.650 32.631  1.00 72.73  ?  235 VAL B CG1 1 
ATOM   4560 C  CG2 . VAL B 1 235 ? -22.919 44.102 31.136  1.00 79.61  ?  235 VAL B CG2 1 
ATOM   4561 N  N   . SER B 1 236 ? -20.260 44.286 33.909  1.00 50.86  ?  236 SER B N   1 
ATOM   4562 C  CA  . SER B 1 236 ? -18.961 45.005 33.882  1.00 50.80  ?  236 SER B CA  1 
ATOM   4563 C  C   . SER B 1 236 ? -18.521 45.320 32.454  1.00 46.48  ?  236 SER B C   1 
ATOM   4564 O  O   . SER B 1 236 ? -19.037 44.701 31.505  1.00 44.08  ?  236 SER B O   1 
ATOM   4565 C  CB  . SER B 1 236 ? -17.899 44.168 34.504  1.00 53.47  ?  236 SER B CB  1 
ATOM   4566 O  OG  . SER B 1 236 ? -17.720 42.994 33.718  1.00 54.28  ?  236 SER B OG  1 
ATOM   4567 N  N   . ASP B 1 237 ? -17.489 46.144 32.351  1.00 41.03  ?  237 ASP B N   1 
ATOM   4568 C  CA  . ASP B 1 237 ? -16.809 46.493 31.084  1.00 49.64  ?  237 ASP B CA  1 
ATOM   4569 C  C   . ASP B 1 237 ? -16.294 45.220 30.395  1.00 56.47  ?  237 ASP B C   1 
ATOM   4570 O  O   . ASP B 1 237 ? -16.452 45.108 29.162  1.00 57.75  ?  237 ASP B O   1 
ATOM   4571 C  CB  . ASP B 1 237 ? -15.660 47.464 31.361  1.00 52.23  ?  237 ASP B CB  1 
ATOM   4572 C  CG  . ASP B 1 237 ? -16.086 48.916 31.464  1.00 49.97  ?  237 ASP B CG  1 
ATOM   4573 O  OD1 . ASP B 1 237 ? -17.291 49.160 31.710  1.00 43.00  ?  237 ASP B OD1 1 
ATOM   4574 O  OD2 . ASP B 1 237 ? -15.207 49.789 31.263  1.00 53.76  ?  237 ASP B OD2 1 
ATOM   4575 N  N   . GLU B 1 238 ? -15.705 44.297 31.161  1.00 56.60  ?  238 GLU B N   1 
ATOM   4576 C  CA  . GLU B 1 238 ? -15.091 43.049 30.632  1.00 53.38  ?  238 GLU B CA  1 
ATOM   4577 C  C   . GLU B 1 238 ? -16.179 42.199 29.944  1.00 49.11  ?  238 GLU B C   1 
ATOM   4578 O  O   . GLU B 1 238 ? -15.921 41.701 28.843  1.00 49.33  ?  238 GLU B O   1 
ATOM   4579 C  CB  . GLU B 1 238 ? -14.332 42.331 31.754  1.00 54.21  ?  238 GLU B CB  1 
ATOM   4580 C  CG  . GLU B 1 238 ? -13.098 43.069 32.270  1.00 61.94  ?  238 GLU B CG  1 
ATOM   4581 C  CD  . GLU B 1 238 ? -12.323 42.454 33.438  1.00 66.13  ?  238 GLU B CD  1 
ATOM   4582 O  OE1 . GLU B 1 238 ? -12.819 41.472 34.064  1.00 69.49  ?  238 GLU B OE1 1 
ATOM   4583 O  OE2 . GLU B 1 238 ? -11.225 42.977 33.746  1.00 62.15  ?  238 GLU B OE2 1 
ATOM   4584 N  N   . LEU B 1 239 ? -17.363 42.037 30.530  1.00 46.33  ?  239 LEU B N   1 
ATOM   4585 C  CA  . LEU B 1 239 ? -18.430 41.209 29.905  1.00 48.02  ?  239 LEU B CA  1 
ATOM   4586 C  C   . LEU B 1 239 ? -18.946 41.908 28.639  1.00 45.37  ?  239 LEU B C   1 
ATOM   4587 O  O   . LEU B 1 239 ? -19.228 41.198 27.654  1.00 43.25  ?  239 LEU B O   1 
ATOM   4588 C  CB  . LEU B 1 239 ? -19.572 40.976 30.899  1.00 54.49  ?  239 LEU B CB  1 
ATOM   4589 C  CG  . LEU B 1 239 ? -20.747 40.153 30.362  1.00 57.41  ?  239 LEU B CG  1 
ATOM   4590 C  CD1 . LEU B 1 239 ? -20.355 38.690 30.163  1.00 57.76  ?  239 LEU B CD1 1 
ATOM   4591 C  CD2 . LEU B 1 239 ? -21.957 40.260 31.278  1.00 59.62  ?  239 LEU B CD2 1 
ATOM   4592 N  N   . LEU B 1 240 ? -19.069 43.241 28.660  1.00 41.64  ?  240 LEU B N   1 
ATOM   4593 C  CA  . LEU B 1 240 ? -19.506 44.029 27.480  1.00 39.11  ?  240 LEU B CA  1 
ATOM   4594 C  C   . LEU B 1 240 ? -18.548 43.772 26.317  1.00 37.15  ?  240 LEU B C   1 
ATOM   4595 O  O   . LEU B 1 240 ? -19.007 43.292 25.258  1.00 36.53  ?  240 LEU B O   1 
ATOM   4596 C  CB  . LEU B 1 240 ? -19.568 45.514 27.837  1.00 39.98  ?  240 LEU B CB  1 
ATOM   4597 C  CG  . LEU B 1 240 ? -20.706 45.875 28.792  1.00 45.48  ?  240 LEU B CG  1 
ATOM   4598 C  CD1 . LEU B 1 240 ? -20.820 47.390 28.961  1.00 46.15  ?  240 LEU B CD1 1 
ATOM   4599 C  CD2 . LEU B 1 240 ? -22.030 45.272 28.325  1.00 44.26  ?  240 LEU B CD2 1 
ATOM   4600 N  N   . ALA B 1 241 ? -17.265 44.042 26.536  1.00 34.37  ?  241 ALA B N   1 
ATOM   4601 C  CA  . ALA B 1 241 ? -16.179 43.788 25.573  1.00 33.05  ?  241 ALA B CA  1 
ATOM   4602 C  C   . ALA B 1 241 ? -16.221 42.327 25.103  1.00 31.09  ?  241 ALA B C   1 
ATOM   4603 O  O   . ALA B 1 241 ? -16.174 42.119 23.862  1.00 29.69  ?  241 ALA B O   1 
ATOM   4604 C  CB  . ALA B 1 241 ? -14.862 44.130 26.200  1.00 36.38  ?  241 ALA B CB  1 
ATOM   4605 N  N   . THR B 1 242 ? -16.351 41.383 26.037  1.00 27.79  ?  242 THR B N   1 
ATOM   4606 C  CA  . THR B 1 242 ? -16.415 39.920 25.777  1.00 30.72  ?  242 THR B CA  1 
ATOM   4607 C  C   . THR B 1 242 ? -17.502 39.674 24.732  1.00 32.28  ?  242 THR B C   1 
ATOM   4608 O  O   . THR B 1 242 ? -17.172 39.084 23.677  1.00 33.24  ?  242 THR B O   1 
ATOM   4609 C  CB  . THR B 1 242 ? -16.586 39.111 27.077  1.00 33.38  ?  242 THR B CB  1 
ATOM   4610 O  OG1 . THR B 1 242 ? -15.376 39.228 27.835  1.00 36.48  ?  242 THR B OG1 1 
ATOM   4611 C  CG2 . THR B 1 242 ? -16.849 37.633 26.882  1.00 31.98  ?  242 THR B CG2 1 
ATOM   4612 N  N   . VAL B 1 243 ? -18.728 40.145 24.970  1.00 32.33  ?  243 VAL B N   1 
ATOM   4613 C  CA  . VAL B 1 243 ? -19.863 39.936 24.016  1.00 29.79  ?  243 VAL B CA  1 
ATOM   4614 C  C   . VAL B 1 243 ? -19.499 40.572 22.663  1.00 27.82  ?  243 VAL B C   1 
ATOM   4615 O  O   . VAL B 1 243 ? -19.678 39.922 21.613  1.00 23.81  ?  243 VAL B O   1 
ATOM   4616 C  CB  . VAL B 1 243 ? -21.184 40.494 24.588  1.00 29.16  ?  243 VAL B CB  1 
ATOM   4617 C  CG1 . VAL B 1 243 ? -22.268 40.659 23.522  1.00 28.85  ?  243 VAL B CG1 1 
ATOM   4618 C  CG2 . VAL B 1 243 ? -21.698 39.616 25.717  1.00 28.69  ?  243 VAL B CG2 1 
ATOM   4619 N  N   . ALA B 1 244 ? -19.034 41.811 22.674  1.00 26.79  ?  244 ALA B N   1 
ATOM   4620 C  CA  . ALA B 1 244 ? -18.628 42.501 21.438  1.00 32.20  ?  244 ALA B CA  1 
ATOM   4621 C  C   . ALA B 1 244 ? -17.619 41.601 20.705  1.00 34.23  ?  244 ALA B C   1 
ATOM   4622 O  O   . ALA B 1 244 ? -17.895 41.229 19.536  1.00 36.47  ?  244 ALA B O   1 
ATOM   4623 C  CB  . ALA B 1 244 ? -18.067 43.883 21.723  1.00 32.05  ?  244 ALA B CB  1 
ATOM   4624 N  N   . LEU B 1 245 ? -16.515 41.234 21.358  1.00 32.14  ?  245 LEU B N   1 
ATOM   4625 C  CA  . LEU B 1 245 ? -15.377 40.533 20.695  1.00 32.71  ?  245 LEU B CA  1 
ATOM   4626 C  C   . LEU B 1 245 ? -15.842 39.171 20.202  1.00 34.80  ?  245 LEU B C   1 
ATOM   4627 O  O   . LEU B 1 245 ? -15.448 38.791 19.100  1.00 36.73  ?  245 LEU B O   1 
ATOM   4628 C  CB  . LEU B 1 245 ? -14.196 40.363 21.653  1.00 31.76  ?  245 LEU B CB  1 
ATOM   4629 C  CG  . LEU B 1 245 ? -12.982 39.622 21.098  1.00 30.90  ?  245 LEU B CG  1 
ATOM   4630 C  CD1 . LEU B 1 245 ? -12.616 40.115 19.721  1.00 32.66  ?  245 LEU B CD1 1 
ATOM   4631 C  CD2 . LEU B 1 245 ? -11.790 39.779 22.033  1.00 31.91  ?  245 LEU B CD2 1 
ATOM   4632 N  N   . SER B 1 246 ? -16.635 38.453 20.993  1.00 38.99  ?  246 SER B N   1 
ATOM   4633 C  CA  . SER B 1 246 ? -17.074 37.080 20.643  1.00 40.22  ?  246 SER B CA  1 
ATOM   4634 C  C   . SER B 1 246 ? -18.068 37.135 19.475  1.00 38.84  ?  246 SER B C   1 
ATOM   4635 O  O   . SER B 1 246 ? -18.048 36.186 18.671  1.00 39.40  ?  246 SER B O   1 
ATOM   4636 C  CB  . SER B 1 246 ? -17.606 36.309 21.835  1.00 42.29  ?  246 SER B CB  1 
ATOM   4637 O  OG  . SER B 1 246 ? -18.542 37.062 22.587  1.00 48.04  ?  246 SER B OG  1 
ATOM   4638 N  N   . LEU B 1 247 ? -18.892 38.182 19.355  1.00 39.51  ?  247 LEU B N   1 
ATOM   4639 C  CA  . LEU B 1 247 ? -19.882 38.290 18.239  1.00 39.60  ?  247 LEU B CA  1 
ATOM   4640 C  C   . LEU B 1 247 ? -19.138 38.627 16.946  1.00 34.88  ?  247 LEU B C   1 
ATOM   4641 O  O   . LEU B 1 247 ? -19.428 38.010 15.915  1.00 37.02  ?  247 LEU B O   1 
ATOM   4642 C  CB  . LEU B 1 247 ? -20.950 39.346 18.550  1.00 43.50  ?  247 LEU B CB  1 
ATOM   4643 C  CG  . LEU B 1 247 ? -22.011 38.918 19.571  1.00 51.17  ?  247 LEU B CG  1 
ATOM   4644 C  CD1 . LEU B 1 247 ? -23.109 39.971 19.719  1.00 51.79  ?  247 LEU B CD1 1 
ATOM   4645 C  CD2 . LEU B 1 247 ? -22.623 37.570 19.208  1.00 55.00  ?  247 LEU B CD2 1 
ATOM   4646 N  N   . PHE B 1 248 ? -18.185 39.544 17.021  1.00 32.12  ?  248 PHE B N   1 
ATOM   4647 C  CA  . PHE B 1 248 ? -17.329 39.985 15.895  1.00 31.79  ?  248 PHE B CA  1 
ATOM   4648 C  C   . PHE B 1 248 ? -16.549 38.809 15.305  1.00 30.37  ?  248 PHE B C   1 
ATOM   4649 O  O   . PHE B 1 248 ? -16.599 38.626 14.111  1.00 35.00  ?  248 PHE B O   1 
ATOM   4650 C  CB  . PHE B 1 248 ? -16.335 41.051 16.334  1.00 29.67  ?  248 PHE B CB  1 
ATOM   4651 C  CG  . PHE B 1 248 ? -15.500 41.547 15.195  1.00 32.65  ?  248 PHE B CG  1 
ATOM   4652 C  CD1 . PHE B 1 248 ? -14.394 40.833 14.761  1.00 35.41  ?  248 PHE B CD1 1 
ATOM   4653 C  CD2 . PHE B 1 248 ? -15.822 42.722 14.546  1.00 38.52  ?  248 PHE B CD2 1 
ATOM   4654 C  CE1 . PHE B 1 248 ? -13.602 41.302 13.728  1.00 35.91  ?  248 PHE B CE1 1 
ATOM   4655 C  CE2 . PHE B 1 248 ? -15.051 43.172 13.478  1.00 40.85  ?  248 PHE B CE2 1 
ATOM   4656 C  CZ  . PHE B 1 248 ? -13.941 42.468 13.081  1.00 38.95  ?  248 PHE B CZ  1 
ATOM   4657 N  N   . GLY B 1 249 ? -15.828 38.047 16.110  1.00 28.99  ?  249 GLY B N   1 
ATOM   4658 C  CA  . GLY B 1 249 ? -15.000 36.942 15.607  1.00 26.94  ?  249 GLY B CA  1 
ATOM   4659 C  C   . GLY B 1 249 ? -15.857 35.806 15.088  1.00 26.85  ?  249 GLY B C   1 
ATOM   4660 O  O   . GLY B 1 249 ? -15.504 35.225 14.048  1.00 31.52  ?  249 GLY B O   1 
ATOM   4661 N  N   . ALA B 1 250 ? -16.957 35.490 15.755  1.00 24.86  ?  250 ALA B N   1 
ATOM   4662 C  CA  . ALA B 1 250 ? -17.874 34.410 15.329  1.00 28.04  ?  250 ALA B CA  1 
ATOM   4663 C  C   . ALA B 1 250 ? -18.517 34.818 14.003  1.00 30.27  ?  250 ALA B C   1 
ATOM   4664 O  O   . ALA B 1 250 ? -18.565 33.998 13.065  1.00 34.09  ?  250 ALA B O   1 
ATOM   4665 C  CB  . ALA B 1 250 ? -18.928 34.146 16.371  1.00 28.56  ?  250 ALA B CB  1 
ATOM   4666 N  N   . GLY B 1 251 ? -18.963 36.067 13.912  1.00 28.92  ?  251 GLY B N   1 
ATOM   4667 C  CA  . GLY B 1 251 ? -19.646 36.551 12.708  1.00 29.14  ?  251 GLY B CA  1 
ATOM   4668 C  C   . GLY B 1 251 ? -18.703 36.673 11.529  1.00 27.61  ?  251 GLY B C   1 
ATOM   4669 O  O   . GLY B 1 251 ? -19.013 36.112 10.456  1.00 28.50  ?  251 GLY B O   1 
ATOM   4670 N  N   . ALA B 1 252 ? -17.644 37.457 11.678  1.00 27.06  ?  252 ALA B N   1 
ATOM   4671 C  CA  . ALA B 1 252 ? -16.596 37.636 10.640  1.00 28.63  ?  252 ALA B CA  1 
ATOM   4672 C  C   . ALA B 1 252 ? -16.059 36.281 10.132  1.00 29.00  ?  252 ALA B C   1 
ATOM   4673 O  O   . ALA B 1 252 ? -15.994 36.069 8.915   1.00 27.35  ?  252 ALA B O   1 
ATOM   4674 C  CB  . ALA B 1 252 ? -15.487 38.500 11.167  1.00 26.49  ?  252 ALA B CB  1 
ATOM   4675 N  N   . VAL B 1 253 ? -15.629 35.380 11.006  1.00 32.30  ?  253 VAL B N   1 
ATOM   4676 C  CA  . VAL B 1 253 ? -14.971 34.127 10.528  1.00 31.15  ?  253 VAL B CA  1 
ATOM   4677 C  C   . VAL B 1 253 ? -15.993 33.338 9.696   1.00 29.07  ?  253 VAL B C   1 
ATOM   4678 O  O   . VAL B 1 253 ? -15.601 32.774 8.659   1.00 28.59  ?  253 VAL B O   1 
ATOM   4679 C  CB  . VAL B 1 253 ? -14.377 33.303 11.691  1.00 33.89  ?  253 VAL B CB  1 
ATOM   4680 C  CG1 . VAL B 1 253 ? -13.806 31.961 11.247  1.00 34.99  ?  253 VAL B CG1 1 
ATOM   4681 C  CG2 . VAL B 1 253 ? -13.330 34.095 12.467  1.00 35.82  ?  253 VAL B CG2 1 
ATOM   4682 N  N   . SER B 1 254 ? -17.258 33.322 10.124  1.00 28.60  ?  254 SER B N   1 
ATOM   4683 C  CA  . SER B 1 254 ? -18.332 32.441 9.590   1.00 28.43  ?  254 SER B CA  1 
ATOM   4684 C  C   . SER B 1 254 ? -18.820 32.956 8.233   1.00 27.00  ?  254 SER B C   1 
ATOM   4685 O  O   . SER B 1 254 ? -19.067 32.135 7.349   1.00 27.05  ?  254 SER B O   1 
ATOM   4686 C  CB  . SER B 1 254 ? -19.464 32.332 10.574  1.00 30.41  ?  254 SER B CB  1 
ATOM   4687 O  OG  . SER B 1 254 ? -19.106 31.467 11.642  1.00 34.28  ?  254 SER B OG  1 
ATOM   4688 N  N   . THR B 1 255 ? -18.922 34.274 8.092   1.00 25.61  ?  255 THR B N   1 
ATOM   4689 C  CA  . THR B 1 255 ? -19.422 34.967 6.887   1.00 26.92  ?  255 THR B CA  1 
ATOM   4690 C  C   . THR B 1 255 ? -18.331 34.935 5.810   1.00 25.24  ?  255 THR B C   1 
ATOM   4691 O  O   . THR B 1 255 ? -18.629 34.546 4.681   1.00 23.75  ?  255 THR B O   1 
ATOM   4692 C  CB  . THR B 1 255 ? -19.879 36.384 7.254   1.00 29.45  ?  255 THR B CB  1 
ATOM   4693 O  OG1 . THR B 1 255 ? -18.841 37.008 8.030   1.00 29.93  ?  255 THR B OG1 1 
ATOM   4694 C  CG2 . THR B 1 255 ? -21.193 36.370 8.002   1.00 27.06  ?  255 THR B CG2 1 
ATOM   4695 N  N   . SER B 1 256 ? -17.111 35.344 6.127   1.00 24.37  ?  256 SER B N   1 
ATOM   4696 C  CA  . SER B 1 256 ? -15.988 35.262 5.167   1.00 25.29  ?  256 SER B CA  1 
ATOM   4697 C  C   . SER B 1 256 ? -15.837 33.821 4.658   1.00 27.82  ?  256 SER B C   1 
ATOM   4698 O  O   . SER B 1 256 ? -15.798 33.629 3.440   1.00 28.95  ?  256 SER B O   1 
ATOM   4699 C  CB  . SER B 1 256 ? -14.714 35.746 5.746   1.00 23.85  ?  256 SER B CB  1 
ATOM   4700 O  OG  . SER B 1 256 ? -13.739 35.870 4.711   1.00 25.46  ?  256 SER B OG  1 
ATOM   4701 N  N   . ALA B 1 257 ? -15.792 32.826 5.539   1.00 29.67  ?  257 ALA B N   1 
ATOM   4702 C  CA  . ALA B 1 257 ? -15.624 31.407 5.136   1.00 28.92  ?  257 ALA B CA  1 
ATOM   4703 C  C   . ALA B 1 257 ? -16.786 30.986 4.238   1.00 26.45  ?  257 ALA B C   1 
ATOM   4704 O  O   . ALA B 1 257 ? -16.553 30.514 3.134   1.00 28.96  ?  257 ALA B O   1 
ATOM   4705 C  CB  . ALA B 1 257 ? -15.523 30.528 6.345   1.00 31.53  ?  257 ALA B CB  1 
ATOM   4706 N  N   . PHE B 1 258 ? -18.024 31.192 4.648   1.00 27.35  ?  258 PHE B N   1 
ATOM   4707 C  CA  . PHE B 1 258 ? -19.166 30.787 3.795   1.00 26.88  ?  258 PHE B CA  1 
ATOM   4708 C  C   . PHE B 1 258 ? -19.042 31.444 2.416   1.00 25.96  ?  258 PHE B C   1 
ATOM   4709 O  O   . PHE B 1 258 ? -19.189 30.715 1.382   1.00 29.15  ?  258 PHE B O   1 
ATOM   4710 C  CB  . PHE B 1 258 ? -20.517 31.126 4.421   1.00 27.12  ?  258 PHE B CB  1 
ATOM   4711 C  CG  . PHE B 1 258 ? -21.672 30.911 3.477   1.00 25.71  ?  258 PHE B CG  1 
ATOM   4712 C  CD1 . PHE B 1 258 ? -21.819 29.707 2.807   1.00 23.98  ?  258 PHE B CD1 1 
ATOM   4713 C  CD2 . PHE B 1 258 ? -22.586 31.925 3.229   1.00 26.15  ?  258 PHE B CD2 1 
ATOM   4714 C  CE1 . PHE B 1 258 ? -22.855 29.519 1.902   1.00 25.21  ?  258 PHE B CE1 1 
ATOM   4715 C  CE2 . PHE B 1 258 ? -23.647 31.726 2.358   1.00 25.70  ?  258 PHE B CE2 1 
ATOM   4716 C  CZ  . PHE B 1 258 ? -23.773 30.526 1.686   1.00 25.93  ?  258 PHE B CZ  1 
ATOM   4717 N  N   . LEU B 1 259 ? -18.784 32.751 2.371   1.00 24.57  ?  259 LEU B N   1 
ATOM   4718 C  CA  . LEU B 1 259 ? -18.772 33.522 1.101   1.00 25.56  ?  259 LEU B CA  1 
ATOM   4719 C  C   . LEU B 1 259 ? -17.700 32.979 0.155   1.00 27.78  ?  259 LEU B C   1 
ATOM   4720 O  O   . LEU B 1 259 ? -17.982 32.886 -1.064  1.00 31.94  ?  259 LEU B O   1 
ATOM   4721 C  CB  . LEU B 1 259 ? -18.566 35.011 1.362   1.00 27.68  ?  259 LEU B CB  1 
ATOM   4722 C  CG  . LEU B 1 259 ? -18.760 35.898 0.125   1.00 31.95  ?  259 LEU B CG  1 
ATOM   4723 C  CD1 . LEU B 1 259 ? -20.205 35.816 -0.387  1.00 34.11  ?  259 LEU B CD1 1 
ATOM   4724 C  CD2 . LEU B 1 259 ? -18.408 37.355 0.423   1.00 35.26  ?  259 LEU B CD2 1 
ATOM   4725 N  N   . GLN B 1 260 ? -16.522 32.638 0.680   1.00 28.19  ?  260 GLN B N   1 
ATOM   4726 C  CA  . GLN B 1 260 ? -15.419 32.016 -0.094  1.00 27.21  ?  260 GLN B CA  1 
ATOM   4727 C  C   . GLN B 1 260 ? -15.901 30.725 -0.793  1.00 26.86  ?  260 GLN B C   1 
ATOM   4728 O  O   . GLN B 1 260 ? -15.544 30.553 -1.978  1.00 23.35  ?  260 GLN B O   1 
ATOM   4729 C  CB  . GLN B 1 260 ? -14.217 31.759 0.816   1.00 26.40  ?  260 GLN B CB  1 
ATOM   4730 C  CG  . GLN B 1 260 ? -13.433 33.023 1.127   1.00 27.05  ?  260 GLN B CG  1 
ATOM   4731 C  CD  . GLN B 1 260 ? -12.356 32.787 2.157   1.00 29.13  ?  260 GLN B CD  1 
ATOM   4732 O  OE1 . GLN B 1 260 ? -11.303 32.216 1.861   1.00 27.77  ?  260 GLN B OE1 1 
ATOM   4733 N  NE2 . GLN B 1 260 ? -12.622 33.214 3.384   1.00 29.14  ?  260 GLN B NE2 1 
ATOM   4734 N  N   . HIS B 1 261 ? -16.591 29.813 -0.086  1.00 26.56  ?  261 HIS B N   1 
ATOM   4735 C  CA  . HIS B 1 261 ? -17.154 28.549 -0.668  1.00 23.97  ?  261 HIS B CA  1 
ATOM   4736 C  C   . HIS B 1 261 ? -18.277 28.897 -1.629  1.00 23.50  ?  261 HIS B C   1 
ATOM   4737 O  O   . HIS B 1 261 ? -18.357 28.246 -2.706  1.00 23.07  ?  261 HIS B O   1 
ATOM   4738 C  CB  . HIS B 1 261 ? -17.744 27.605 0.372   1.00 23.07  ?  261 HIS B CB  1 
ATOM   4739 C  CG  . HIS B 1 261 ? -16.712 26.944 1.223   1.00 25.04  ?  261 HIS B CG  1 
ATOM   4740 N  ND1 . HIS B 1 261 ? -16.407 25.606 1.093   1.00 24.54  ?  261 HIS B ND1 1 
ATOM   4741 C  CD2 . HIS B 1 261 ? -15.903 27.438 2.191   1.00 22.57  ?  261 HIS B CD2 1 
ATOM   4742 C  CE1 . HIS B 1 261 ? -15.465 25.309 1.974   1.00 25.85  ?  261 HIS B CE1 1 
ATOM   4743 N  NE2 . HIS B 1 261 ? -15.159 26.412 2.678   1.00 22.86  ?  261 HIS B NE2 1 
ATOM   4744 N  N   . ALA B 1 262 ? -19.108 29.896 -1.302  1.00 22.11  ?  262 ALA B N   1 
ATOM   4745 C  CA  . ALA B 1 262 ? -20.180 30.307 -2.244  1.00 22.40  ?  262 ALA B CA  1 
ATOM   4746 C  C   . ALA B 1 262 ? -19.495 30.782 -3.533  1.00 23.52  ?  262 ALA B C   1 
ATOM   4747 O  O   . ALA B 1 262 ? -19.936 30.378 -4.637  1.00 23.93  ?  262 ALA B O   1 
ATOM   4748 C  CB  . ALA B 1 262 ? -21.109 31.336 -1.623  1.00 22.74  ?  262 ALA B CB  1 
ATOM   4749 N  N   . ILE B 1 263 ? -18.411 31.558 -3.411  1.00 23.02  ?  263 ILE B N   1 
ATOM   4750 C  CA  . ILE B 1 263 ? -17.653 32.074 -4.588  1.00 25.37  ?  263 ILE B CA  1 
ATOM   4751 C  C   . ILE B 1 263 ? -17.065 30.888 -5.396  1.00 27.58  ?  263 ILE B C   1 
ATOM   4752 O  O   . ILE B 1 263 ? -17.205 30.855 -6.660  1.00 27.22  ?  263 ILE B O   1 
ATOM   4753 C  CB  . ILE B 1 263 ? -16.607 33.105 -4.125  1.00 25.19  ?  263 ILE B CB  1 
ATOM   4754 C  CG1 . ILE B 1 263 ? -17.263 34.412 -3.701  1.00 26.49  ?  263 ILE B CG1 1 
ATOM   4755 C  CG2 . ILE B 1 263 ? -15.577 33.367 -5.204  1.00 27.44  ?  263 ILE B CG2 1 
ATOM   4756 C  CD1 . ILE B 1 263 ? -16.284 35.382 -3.076  1.00 27.74  ?  263 ILE B CD1 1 
ATOM   4757 N  N   . ILE B 1 264 ? -16.476 29.883 -4.739  1.00 29.19  ?  264 ILE B N   1 
ATOM   4758 C  CA  . ILE B 1 264 ? -15.973 28.675 -5.469  1.00 30.17  ?  264 ILE B CA  1 
ATOM   4759 C  C   . ILE B 1 264 ? -17.120 28.002 -6.267  1.00 30.25  ?  264 ILE B C   1 
ATOM   4760 O  O   . ILE B 1 264 ? -16.911 27.635 -7.450  1.00 26.70  ?  264 ILE B O   1 
ATOM   4761 C  CB  . ILE B 1 264 ? -15.241 27.714 -4.517  1.00 27.11  ?  264 ILE B CB  1 
ATOM   4762 C  CG1 . ILE B 1 264 ? -13.996 28.387 -3.919  1.00 26.43  ?  264 ILE B CG1 1 
ATOM   4763 C  CG2 . ILE B 1 264 ? -14.900 26.417 -5.244  1.00 24.59  ?  264 ILE B CG2 1 
ATOM   4764 C  CD1 . ILE B 1 264 ? -13.434 27.684 -2.703  1.00 27.47  ?  264 ILE B CD1 1 
ATOM   4765 N  N   . ALA B 1 265 ? -18.307 27.875 -5.675  1.00 28.86  ?  265 ALA B N   1 
ATOM   4766 C  CA  . ALA B 1 265 ? -19.484 27.296 -6.359  1.00 29.70  ?  265 ALA B CA  1 
ATOM   4767 C  C   . ALA B 1 265 ? -19.791 28.081 -7.645  1.00 30.06  ?  265 ALA B C   1 
ATOM   4768 O  O   . ALA B 1 265 ? -19.915 27.445 -8.684  1.00 34.05  ?  265 ALA B O   1 
ATOM   4769 C  CB  . ALA B 1 265 ? -20.664 27.233 -5.413  1.00 30.44  ?  265 ALA B CB  1 
ATOM   4770 N  N   . LEU B 1 266 ? -19.893 29.410 -7.592  1.00 30.32  ?  266 LEU B N   1 
ATOM   4771 C  CA  . LEU B 1 266 ? -20.251 30.235 -8.775  1.00 29.06  ?  266 LEU B CA  1 
ATOM   4772 C  C   . LEU B 1 266 ? -19.119 30.192 -9.817  1.00 31.72  ?  266 LEU B C   1 
ATOM   4773 O  O   . LEU B 1 266 ? -19.429 30.322 -11.017 1.00 35.17  ?  266 LEU B O   1 
ATOM   4774 C  CB  . LEU B 1 266 ? -20.501 31.680 -8.331  1.00 29.89  ?  266 LEU B CB  1 
ATOM   4775 C  CG  . LEU B 1 266 ? -21.740 31.903 -7.466  1.00 28.91  ?  266 LEU B CG  1 
ATOM   4776 C  CD1 . LEU B 1 266 ? -22.014 33.381 -7.308  1.00 27.78  ?  266 LEU B CD1 1 
ATOM   4777 C  CD2 . LEU B 1 266 ? -22.956 31.207 -8.043  1.00 27.26  ?  266 LEU B CD2 1 
ATOM   4778 N  N   . ALA B 1 267 ? -17.852 30.069 -9.407  1.00 33.02  ?  267 ALA B N   1 
ATOM   4779 C  CA  . ALA B 1 267 ? -16.687 30.091 -10.331 1.00 31.79  ?  267 ALA B CA  1 
ATOM   4780 C  C   . ALA B 1 267 ? -16.611 28.793 -11.126 1.00 30.45  ?  267 ALA B C   1 
ATOM   4781 O  O   . ALA B 1 267 ? -16.407 28.858 -12.334 1.00 29.65  ?  267 ALA B O   1 
ATOM   4782 C  CB  . ALA B 1 267 ? -15.415 30.323 -9.574  1.00 34.76  ?  267 ALA B CB  1 
ATOM   4783 N  N   . GLN B 1 268 ? -16.807 27.665 -10.443 1.00 33.14  ?  268 GLN B N   1 
ATOM   4784 C  CA  . GLN B 1 268 ? -16.793 26.285 -10.992 1.00 30.81  ?  268 GLN B CA  1 
ATOM   4785 C  C   . GLN B 1 268 ? -18.081 25.958 -11.755 1.00 31.38  ?  268 GLN B C   1 
ATOM   4786 O  O   . GLN B 1 268 ? -18.067 25.053 -12.633 1.00 32.54  ?  268 GLN B O   1 
ATOM   4787 C  CB  . GLN B 1 268 ? -16.618 25.337 -9.815  1.00 31.17  ?  268 GLN B CB  1 
ATOM   4788 C  CG  . GLN B 1 268 ? -15.200 25.390 -9.268  1.00 34.66  ?  268 GLN B CG  1 
ATOM   4789 C  CD  . GLN B 1 268 ? -14.210 24.908 -10.298 1.00 35.71  ?  268 GLN B CD  1 
ATOM   4790 O  OE1 . GLN B 1 268 ? -13.728 25.666 -11.147 1.00 30.35  ?  268 GLN B OE1 1 
ATOM   4791 N  NE2 . GLN B 1 268 ? -13.931 23.615 -10.238 1.00 38.49  ?  268 GLN B NE2 1 
ATOM   4792 N  N   . GLN B 1 269 ? -19.174 26.628 -11.400 1.00 29.65  ?  269 GLN B N   1 
ATOM   4793 C  CA  . GLN B 1 269 ? -20.504 26.360 -11.986 1.00 29.93  ?  269 GLN B CA  1 
ATOM   4794 C  C   . GLN B 1 269 ? -21.091 27.678 -12.479 1.00 28.73  ?  269 GLN B C   1 
ATOM   4795 O  O   . GLN B 1 269 ? -22.053 28.186 -11.916 1.00 27.67  ?  269 GLN B O   1 
ATOM   4796 C  CB  . GLN B 1 269 ? -21.359 25.631 -10.953 1.00 29.23  ?  269 GLN B CB  1 
ATOM   4797 C  CG  . GLN B 1 269 ? -20.808 24.268 -10.609 1.00 28.61  ?  269 GLN B CG  1 
ATOM   4798 C  CD  . GLN B 1 269 ? -21.838 23.409 -9.937  1.00 30.40  ?  269 GLN B CD  1 
ATOM   4799 O  OE1 . GLN B 1 269 ? -22.989 23.294 -10.369 1.00 36.03  ?  269 GLN B OE1 1 
ATOM   4800 N  NE2 . GLN B 1 269 ? -21.423 22.809 -8.845  1.00 34.31  ?  269 GLN B NE2 1 
ATOM   4801 N  N   . PRO B 1 270 ? -20.517 28.269 -13.548 1.00 29.64  ?  270 PRO B N   1 
ATOM   4802 C  CA  . PRO B 1 270 ? -20.980 29.570 -14.021 1.00 28.61  ?  270 PRO B CA  1 
ATOM   4803 C  C   . PRO B 1 270 ? -22.471 29.582 -14.429 1.00 29.70  ?  270 PRO B C   1 
ATOM   4804 O  O   . PRO B 1 270 ? -23.040 30.659 -14.439 1.00 26.34  ?  270 PRO B O   1 
ATOM   4805 C  CB  . PRO B 1 270 ? -20.025 29.904 -15.180 1.00 30.18  ?  270 PRO B CB  1 
ATOM   4806 C  CG  . PRO B 1 270 ? -19.361 28.592 -15.564 1.00 30.60  ?  270 PRO B CG  1 
ATOM   4807 C  CD  . PRO B 1 270 ? -19.371 27.742 -14.314 1.00 30.25  ?  270 PRO B CD  1 
ATOM   4808 N  N   . GLU B 1 271 ? -23.108 28.420 -14.663 1.00 26.68  ?  271 GLU B N   1 
ATOM   4809 C  CA  . GLU B 1 271 ? -24.558 28.377 -14.982 1.00 26.44  ?  271 GLU B CA  1 
ATOM   4810 C  C   . GLU B 1 271 ? -25.311 29.058 -13.824 1.00 27.50  ?  271 GLU B C   1 
ATOM   4811 O  O   . GLU B 1 271 ? -26.406 29.691 -14.060 1.00 25.67  ?  271 GLU B O   1 
ATOM   4812 C  CB  . GLU B 1 271 ? -25.055 26.952 -15.292 1.00 27.54  ?  271 GLU B CB  1 
ATOM   4813 C  CG  . GLU B 1 271 ? -25.056 25.969 -14.119 1.00 28.31  ?  271 GLU B CG  1 
ATOM   4814 C  CD  . GLU B 1 271 ? -23.779 25.147 -13.945 1.00 30.53  ?  271 GLU B CD  1 
ATOM   4815 O  OE1 . GLU B 1 271 ? -22.725 25.517 -14.516 1.00 31.70  ?  271 GLU B OE1 1 
ATOM   4816 O  OE2 . GLU B 1 271 ? -23.830 24.153 -13.212 1.00 29.18  ?  271 GLU B OE2 1 
ATOM   4817 N  N   . LEU B 1 272 ? -24.751 28.964 -12.615 1.00 27.72  ?  272 LEU B N   1 
ATOM   4818 C  CA  . LEU B 1 272 ? -25.384 29.494 -11.381 1.00 27.66  ?  272 LEU B CA  1 
ATOM   4819 C  C   . LEU B 1 272 ? -25.352 31.023 -11.403 1.00 29.05  ?  272 LEU B C   1 
ATOM   4820 O  O   . LEU B 1 272 ? -26.378 31.631 -11.048 1.00 31.03  ?  272 LEU B O   1 
ATOM   4821 C  CB  . LEU B 1 272 ? -24.659 28.924 -10.168 1.00 26.83  ?  272 LEU B CB  1 
ATOM   4822 C  CG  . LEU B 1 272 ? -24.640 27.403 -10.087 1.00 25.61  ?  272 LEU B CG  1 
ATOM   4823 C  CD1 . LEU B 1 272 ? -24.042 26.995 -8.770  1.00 27.48  ?  272 LEU B CD1 1 
ATOM   4824 C  CD2 . LEU B 1 272 ? -26.044 26.832 -10.242 1.00 25.45  ?  272 LEU B CD2 1 
ATOM   4825 N  N   . ALA B 1 273 ? -24.250 31.607 -11.840 1.00 29.40  ?  273 ALA B N   1 
ATOM   4826 C  CA  . ALA B 1 273 ? -24.118 33.075 -11.896 1.00 30.18  ?  273 ALA B CA  1 
ATOM   4827 C  C   . ALA B 1 273 ? -24.972 33.605 -13.044 1.00 30.39  ?  273 ALA B C   1 
ATOM   4828 O  O   . ALA B 1 273 ? -25.410 34.758 -13.001 1.00 32.40  ?  273 ALA B O   1 
ATOM   4829 C  CB  . ALA B 1 273 ? -22.660 33.396 -12.047 1.00 28.24  ?  273 ALA B CB  1 
ATOM   4830 N  N   . ASP B 1 274 ? -25.213 32.775 -14.050 1.00 31.61  ?  274 ASP B N   1 
ATOM   4831 C  CA  . ASP B 1 274 ? -26.093 33.157 -15.182 1.00 31.05  ?  274 ASP B CA  1 
ATOM   4832 C  C   . ASP B 1 274 ? -27.524 33.239 -14.650 1.00 28.96  ?  274 ASP B C   1 
ATOM   4833 O  O   . ASP B 1 274 ? -28.181 34.256 -14.883 1.00 24.36  ?  274 ASP B O   1 
ATOM   4834 C  CB  . ASP B 1 274 ? -25.919 32.187 -16.338 1.00 31.04  ?  274 ASP B CB  1 
ATOM   4835 C  CG  . ASP B 1 274 ? -24.808 32.495 -17.327 1.00 34.28  ?  274 ASP B CG  1 
ATOM   4836 O  OD1 . ASP B 1 274 ? -24.353 33.649 -17.358 1.00 32.40  ?  274 ASP B OD1 1 
ATOM   4837 O  OD2 . ASP B 1 274 ? -24.421 31.575 -18.067 1.00 33.85  ?  274 ASP B OD2 1 
ATOM   4838 N  N   . ARG B 1 275 ? -27.965 32.230 -13.910 1.00 28.47  ?  275 ARG B N   1 
ATOM   4839 C  CA  . ARG B 1 275 ? -29.318 32.254 -13.317 1.00 27.81  ?  275 ARG B CA  1 
ATOM   4840 C  C   . ARG B 1 275 ? -29.444 33.520 -12.475 1.00 28.00  ?  275 ARG B C   1 
ATOM   4841 O  O   . ARG B 1 275 ? -30.430 34.248 -12.629 1.00 26.09  ?  275 ARG B O   1 
ATOM   4842 C  CB  . ARG B 1 275 ? -29.554 31.009 -12.464 1.00 28.92  ?  275 ARG B CB  1 
ATOM   4843 C  CG  . ARG B 1 275 ? -30.791 31.067 -11.583 1.00 30.39  ?  275 ARG B CG  1 
ATOM   4844 C  CD  . ARG B 1 275 ? -32.040 30.817 -12.403 1.00 30.51  ?  275 ARG B CD  1 
ATOM   4845 N  NE  . ARG B 1 275 ? -33.236 30.687 -11.567 1.00 33.65  ?  275 ARG B NE  1 
ATOM   4846 C  CZ  . ARG B 1 275 ? -33.661 29.559 -11.025 1.00 30.42  ?  275 ARG B CZ  1 
ATOM   4847 N  NH1 . ARG B 1 275 ? -32.873 28.504 -10.981 1.00 30.84  ?  275 ARG B NH1 1 
ATOM   4848 N  NH2 . ARG B 1 275 ? -34.877 29.490 -10.525 1.00 27.68  ?  275 ARG B NH2 1 
ATOM   4849 N  N   . LEU B 1 276 ? -28.464 33.736 -11.610 1.00 26.99  ?  276 LEU B N   1 
ATOM   4850 C  CA  . LEU B 1 276 ? -28.493 34.942 -10.744 1.00 29.53  ?  276 LEU B CA  1 
ATOM   4851 C  C   . LEU B 1 276 ? -28.734 36.184 -11.616 1.00 27.68  ?  276 LEU B C   1 
ATOM   4852 O  O   . LEU B 1 276 ? -29.732 36.892 -11.373 1.00 26.32  ?  276 LEU B O   1 
ATOM   4853 C  CB  . LEU B 1 276 ? -27.189 35.038 -9.957  1.00 28.55  ?  276 LEU B CB  1 
ATOM   4854 C  CG  . LEU B 1 276 ? -27.017 34.001 -8.843  1.00 29.48  ?  276 LEU B CG  1 
ATOM   4855 C  CD1 . LEU B 1 276 ? -25.894 34.386 -7.898  1.00 31.65  ?  276 LEU B CD1 1 
ATOM   4856 C  CD2 . LEU B 1 276 ? -28.318 33.801 -8.083  1.00 29.05  ?  276 LEU B CD2 1 
ATOM   4857 N  N   . ARG B 1 277 ? -27.867 36.448 -12.577 1.00 30.08  ?  277 ARG B N   1 
ATOM   4858 C  CA  . ARG B 1 277 ? -28.015 37.659 -13.411 1.00 32.45  ?  277 ARG B CA  1 
ATOM   4859 C  C   . ARG B 1 277 ? -29.404 37.681 -14.069 1.00 34.41  ?  277 ARG B C   1 
ATOM   4860 O  O   . ARG B 1 277 ? -30.047 38.742 -14.032 1.00 33.37  ?  277 ARG B O   1 
ATOM   4861 C  CB  . ARG B 1 277 ? -26.858 37.659 -14.407 1.00 33.73  ?  277 ARG B CB  1 
ATOM   4862 C  CG  . ARG B 1 277 ? -25.501 38.076 -13.871 1.00 34.18  ?  277 ARG B CG  1 
ATOM   4863 C  CD  . ARG B 1 277 ? -24.495 37.869 -14.978 1.00 35.19  ?  277 ARG B CD  1 
ATOM   4864 N  NE  . ARG B 1 277 ? -23.226 37.364 -14.452 1.00 40.03  ?  277 ARG B NE  1 
ATOM   4865 C  CZ  . ARG B 1 277 ? -22.750 36.153 -14.664 1.00 38.31  ?  277 ARG B CZ  1 
ATOM   4866 N  NH1 . ARG B 1 277 ? -23.310 35.361 -15.554 1.00 35.47  ?  277 ARG B NH1 1 
ATOM   4867 N  NH2 . ARG B 1 277 ? -21.704 35.739 -13.985 1.00 49.19  ?  277 ARG B NH2 1 
ATOM   4868 N  N   . ALA B 1 278 ? -29.846 36.562 -14.629 1.00 33.94  ?  278 ALA B N   1 
ATOM   4869 C  CA  . ALA B 1 278 ? -31.150 36.454 -15.330 1.00 32.23  ?  278 ALA B CA  1 
ATOM   4870 C  C   . ALA B 1 278 ? -32.323 36.678 -14.362 1.00 34.20  ?  278 ALA B C   1 
ATOM   4871 O  O   . ALA B 1 278 ? -33.327 37.192 -14.801 1.00 33.09  ?  278 ALA B O   1 
ATOM   4872 C  CB  . ALA B 1 278 ? -31.261 35.106 -16.008 1.00 29.78  ?  278 ALA B CB  1 
ATOM   4873 N  N   . GLU B 1 279 ? -32.209 36.291 -13.090 1.00 36.29  ?  279 GLU B N   1 
ATOM   4874 C  CA  . GLU B 1 279 ? -33.359 36.242 -12.163 1.00 31.86  ?  279 GLU B CA  1 
ATOM   4875 C  C   . GLU B 1 279 ? -32.890 36.613 -10.767 1.00 30.41  ?  279 GLU B C   1 
ATOM   4876 O  O   . GLU B 1 279 ? -32.877 35.779 -9.879  1.00 31.84  ?  279 GLU B O   1 
ATOM   4877 C  CB  . GLU B 1 279 ? -33.901 34.827 -12.235 1.00 37.87  ?  279 GLU B CB  1 
ATOM   4878 C  CG  . GLU B 1 279 ? -35.041 34.556 -11.273 1.00 48.74  ?  279 GLU B CG  1 
ATOM   4879 C  CD  . GLU B 1 279 ? -35.774 33.243 -11.532 1.00 52.25  ?  279 GLU B CD  1 
ATOM   4880 O  OE1 . GLU B 1 279 ? -35.297 32.444 -12.427 1.00 45.08  ?  279 GLU B OE1 1 
ATOM   4881 O  OE2 . GLU B 1 279 ? -36.842 33.045 -10.868 1.00 52.33  ?  279 GLU B OE2 1 
ATOM   4882 N  N   . PRO B 1 280 ? -32.483 37.875 -10.510 1.00 32.44  ?  280 PRO B N   1 
ATOM   4883 C  CA  . PRO B 1 280 ? -31.952 38.278 -9.199  1.00 29.71  ?  280 PRO B CA  1 
ATOM   4884 C  C   . PRO B 1 280 ? -32.754 37.964 -7.916  1.00 30.81  ?  280 PRO B C   1 
ATOM   4885 O  O   . PRO B 1 280 ? -32.143 37.862 -6.865  1.00 36.14  ?  280 PRO B O   1 
ATOM   4886 C  CB  . PRO B 1 280 ? -31.869 39.800 -9.347  1.00 29.71  ?  280 PRO B CB  1 
ATOM   4887 C  CG  . PRO B 1 280 ? -31.586 40.004 -10.809 1.00 31.87  ?  280 PRO B CG  1 
ATOM   4888 C  CD  . PRO B 1 280 ? -32.503 38.995 -11.479 1.00 33.56  ?  280 PRO B CD  1 
ATOM   4889 N  N   . ALA B 1 281 ? -34.075 37.814 -7.997  1.00 30.92  ?  281 ALA B N   1 
ATOM   4890 C  CA  . ALA B 1 281 ? -34.979 37.528 -6.857  1.00 33.12  ?  281 ALA B CA  1 
ATOM   4891 C  C   . ALA B 1 281 ? -34.765 36.104 -6.326  1.00 35.07  ?  281 ALA B C   1 
ATOM   4892 O  O   . ALA B 1 281 ? -35.057 35.867 -5.144  1.00 39.05  ?  281 ALA B O   1 
ATOM   4893 C  CB  . ALA B 1 281 ? -36.403 37.738 -7.283  1.00 34.24  ?  281 ALA B CB  1 
ATOM   4894 N  N   . VAL B 1 282 ? -34.202 35.193 -7.120  1.00 35.07  ?  282 VAL B N   1 
ATOM   4895 C  CA  . VAL B 1 282 ? -33.920 33.794 -6.676  1.00 32.09  ?  282 VAL B CA  1 
ATOM   4896 C  C   . VAL B 1 282 ? -32.667 33.752 -5.772  1.00 33.32  ?  282 VAL B C   1 
ATOM   4897 O  O   . VAL B 1 282 ? -32.331 32.643 -5.257  1.00 31.67  ?  282 VAL B O   1 
ATOM   4898 C  CB  . VAL B 1 282 ? -33.773 32.881 -7.895  1.00 32.05  ?  282 VAL B CB  1 
ATOM   4899 C  CG1 . VAL B 1 282 ? -33.367 31.482 -7.494  1.00 33.89  ?  282 VAL B CG1 1 
ATOM   4900 C  CG2 . VAL B 1 282 ? -35.044 32.825 -8.700  1.00 37.86  ?  282 VAL B CG2 1 
ATOM   4901 N  N   . ILE B 1 283 ? -31.990 34.889 -5.547  1.00 29.14  ?  283 ILE B N   1 
ATOM   4902 C  CA  . ILE B 1 283 ? -30.755 34.941 -4.698  1.00 29.78  ?  283 ILE B CA  1 
ATOM   4903 C  C   . ILE B 1 283 ? -31.039 34.354 -3.299  1.00 31.20  ?  283 ILE B C   1 
ATOM   4904 O  O   . ILE B 1 283 ? -30.174 33.637 -2.781  1.00 31.25  ?  283 ILE B O   1 
ATOM   4905 C  CB  . ILE B 1 283 ? -30.230 36.387 -4.615  1.00 28.69  ?  283 ILE B CB  1 
ATOM   4906 C  CG1 . ILE B 1 283 ? -29.741 36.887 -5.976  1.00 26.40  ?  283 ILE B CG1 1 
ATOM   4907 C  CG2 . ILE B 1 283 ? -29.141 36.517 -3.533  1.00 26.00  ?  283 ILE B CG2 1 
ATOM   4908 C  CD1 . ILE B 1 283 ? -29.458 38.348 -6.044  1.00 28.76  ?  283 ILE B CD1 1 
ATOM   4909 N  N   . GLY B 1 284 ? -32.183 34.680 -2.683  1.00 30.20  ?  284 GLY B N   1 
ATOM   4910 C  CA  . GLY B 1 284 ? -32.619 34.082 -1.407  1.00 30.80  ?  284 GLY B CA  1 
ATOM   4911 C  C   . GLY B 1 284 ? -32.501 32.564 -1.432  1.00 34.14  ?  284 GLY B C   1 
ATOM   4912 O  O   . GLY B 1 284 ? -31.643 32.014 -0.712  1.00 34.28  ?  284 GLY B O   1 
ATOM   4913 N  N   . ARG B 1 285 ? -33.330 31.897 -2.238  1.00 35.10  ?  285 ARG B N   1 
ATOM   4914 C  CA  . ARG B 1 285 ? -33.353 30.423 -2.372  1.00 34.01  ?  285 ARG B CA  1 
ATOM   4915 C  C   . ARG B 1 285 ? -31.937 29.935 -2.693  1.00 33.11  ?  285 ARG B C   1 
ATOM   4916 O  O   . ARG B 1 285 ? -31.562 28.861 -2.170  1.00 29.18  ?  285 ARG B O   1 
ATOM   4917 C  CB  . ARG B 1 285 ? -34.332 29.992 -3.468  1.00 43.39  ?  285 ARG B CB  1 
ATOM   4918 C  CG  . ARG B 1 285 ? -35.802 30.266 -3.161  1.00 51.50  ?  285 ARG B CG  1 
ATOM   4919 C  CD  . ARG B 1 285 ? -36.807 29.797 -4.228  1.00 52.24  ?  285 ARG B CD  1 
ATOM   4920 N  NE  . ARG B 1 285 ? -38.218 30.120 -3.967  1.00 55.03  ?  285 ARG B NE  1 
ATOM   4921 C  CZ  . ARG B 1 285 ? -39.244 29.915 -4.800  1.00 55.16  ?  285 ARG B CZ  1 
ATOM   4922 N  NH1 . ARG B 1 285 ? -39.059 29.354 -5.980  1.00 61.38  ?  285 ARG B NH1 1 
ATOM   4923 N  NH2 . ARG B 1 285 ? -40.463 30.292 -4.460  1.00 51.78  ?  285 ARG B NH2 1 
ATOM   4924 N  N   . ALA B 1 286 ? -31.198 30.685 -3.526  1.00 29.26  ?  286 ALA B N   1 
ATOM   4925 C  CA  . ALA B 1 286 ? -29.839 30.328 -4.008  1.00 28.23  ?  286 ALA B CA  1 
ATOM   4926 C  C   . ALA B 1 286 ? -28.869 30.226 -2.833  1.00 28.82  ?  286 ALA B C   1 
ATOM   4927 O  O   . ALA B 1 286 ? -28.114 29.255 -2.779  1.00 27.53  ?  286 ALA B O   1 
ATOM   4928 C  CB  . ALA B 1 286 ? -29.331 31.344 -5.007  1.00 27.32  ?  286 ALA B CB  1 
ATOM   4929 N  N   . VAL B 1 287 ? -28.836 31.254 -1.976  1.00 30.53  ?  287 VAL B N   1 
ATOM   4930 C  CA  . VAL B 1 287 ? -27.941 31.299 -0.787  1.00 30.82  ?  287 VAL B CA  1 
ATOM   4931 C  C   . VAL B 1 287 ? -28.312 30.136 0.145   1.00 28.96  ?  287 VAL B C   1 
ATOM   4932 O  O   . VAL B 1 287 ? -27.413 29.594 0.817   1.00 35.22  ?  287 VAL B O   1 
ATOM   4933 C  CB  . VAL B 1 287 ? -28.021 32.663 -0.077  1.00 30.17  ?  287 VAL B CB  1 
ATOM   4934 C  CG1 . VAL B 1 287 ? -27.209 32.685 1.204   1.00 29.89  ?  287 VAL B CG1 1 
ATOM   4935 C  CG2 . VAL B 1 287 ? -27.618 33.796 -1.002  1.00 31.50  ?  287 VAL B CG2 1 
ATOM   4936 N  N   . ASP B 1 288 ? -29.591 29.794 0.208   1.00 25.30  ?  288 ASP B N   1 
ATOM   4937 C  CA  . ASP B 1 288 ? -30.123 28.739 1.099   1.00 25.36  ?  288 ASP B CA  1 
ATOM   4938 C  C   . ASP B 1 288 ? -29.536 27.412 0.621   1.00 26.56  ?  288 ASP B C   1 
ATOM   4939 O  O   . ASP B 1 288 ? -29.186 26.601 1.452   1.00 28.89  ?  288 ASP B O   1 
ATOM   4940 C  CB  . ASP B 1 288 ? -31.647 28.761 1.112   1.00 25.77  ?  288 ASP B CB  1 
ATOM   4941 C  CG  . ASP B 1 288 ? -32.265 28.088 2.318   1.00 28.18  ?  288 ASP B CG  1 
ATOM   4942 O  OD1 . ASP B 1 288 ? -31.834 28.361 3.447   1.00 28.73  ?  288 ASP B OD1 1 
ATOM   4943 O  OD2 . ASP B 1 288 ? -33.197 27.323 2.120   1.00 35.65  ?  288 ASP B OD2 1 
ATOM   4944 N  N   . GLU B 1 289 ? -29.384 27.231 -0.687  1.00 28.39  ?  289 GLU B N   1 
ATOM   4945 C  CA  . GLU B 1 289 ? -28.839 25.995 -1.282  1.00 27.85  ?  289 GLU B CA  1 
ATOM   4946 C  C   . GLU B 1 289 ? -27.327 26.016 -1.081  1.00 28.10  ?  289 GLU B C   1 
ATOM   4947 O  O   . GLU B 1 289 ? -26.766 24.978 -0.707  1.00 28.94  ?  289 GLU B O   1 
ATOM   4948 C  CB  . GLU B 1 289 ? -29.218 25.873 -2.757  1.00 30.22  ?  289 GLU B CB  1 
ATOM   4949 C  CG  . GLU B 1 289 ? -28.492 24.734 -3.487  1.00 31.69  ?  289 GLU B CG  1 
ATOM   4950 C  CD  . GLU B 1 289 ? -28.860 23.340 -3.021  1.00 28.42  ?  289 GLU B CD  1 
ATOM   4951 O  OE1 . GLU B 1 289 ? -29.268 23.212 -1.875  1.00 29.02  ?  289 GLU B OE1 1 
ATOM   4952 O  OE2 . GLU B 1 289 ? -28.751 22.389 -3.816  1.00 28.19  ?  289 GLU B OE2 1 
ATOM   4953 N  N   . LEU B 1 290 ? -26.689 27.160 -1.297  1.00 27.01  ?  290 LEU B N   1 
ATOM   4954 C  CA  . LEU B 1 290 ? -25.230 27.276 -1.082  1.00 25.78  ?  290 LEU B CA  1 
ATOM   4955 C  C   . LEU B 1 290 ? -24.951 26.996 0.392   1.00 25.63  ?  290 LEU B C   1 
ATOM   4956 O  O   . LEU B 1 290 ? -23.915 26.419 0.723   1.00 23.62  ?  290 LEU B O   1 
ATOM   4957 C  CB  . LEU B 1 290 ? -24.764 28.666 -1.522  1.00 26.81  ?  290 LEU B CB  1 
ATOM   4958 C  CG  . LEU B 1 290 ? -24.797 28.918 -3.034  1.00 30.39  ?  290 LEU B CG  1 
ATOM   4959 C  CD1 . LEU B 1 290 ? -24.098 30.206 -3.403  1.00 33.95  ?  290 LEU B CD1 1 
ATOM   4960 C  CD2 . LEU B 1 290 ? -24.174 27.784 -3.816  1.00 30.20  ?  290 LEU B CD2 1 
ATOM   4961 N  N   . LEU B 1 291 ? -25.854 27.397 1.277   1.00 27.91  ?  291 LEU B N   1 
ATOM   4962 C  CA  . LEU B 1 291 ? -25.669 27.128 2.719   1.00 27.46  ?  291 LEU B CA  1 
ATOM   4963 C  C   . LEU B 1 291 ? -25.741 25.602 2.929   1.00 26.41  ?  291 LEU B C   1 
ATOM   4964 O  O   . LEU B 1 291 ? -24.776 25.020 3.444   1.00 29.23  ?  291 LEU B O   1 
ATOM   4965 C  CB  . LEU B 1 291 ? -26.724 27.920 3.483   1.00 28.44  ?  291 LEU B CB  1 
ATOM   4966 C  CG  . LEU B 1 291 ? -26.439 29.400 3.723   1.00 28.08  ?  291 LEU B CG  1 
ATOM   4967 C  CD1 . LEU B 1 291 ? -27.689 30.046 4.290   1.00 29.38  ?  291 LEU B CD1 1 
ATOM   4968 C  CD2 . LEU B 1 291 ? -25.275 29.587 4.691   1.00 25.80  ?  291 LEU B CD2 1 
ATOM   4969 N  N   . ARG B 1 292 ? -26.760 24.934 2.417   1.00 25.07  ?  292 ARG B N   1 
ATOM   4970 C  CA  . ARG B 1 292 ? -26.820 23.461 2.501   1.00 28.56  ?  292 ARG B CA  1 
ATOM   4971 C  C   . ARG B 1 292 ? -25.490 22.844 2.047   1.00 28.78  ?  292 ARG B C   1 
ATOM   4972 O  O   . ARG B 1 292 ? -24.952 21.974 2.757   1.00 33.63  ?  292 ARG B O   1 
ATOM   4973 C  CB  . ARG B 1 292 ? -27.947 22.878 1.648   1.00 30.32  ?  292 ARG B CB  1 
ATOM   4974 C  CG  . ARG B 1 292 ? -28.071 21.374 1.844   1.00 31.47  ?  292 ARG B CG  1 
ATOM   4975 C  CD  . ARG B 1 292 ? -28.973 20.702 0.842   1.00 31.78  ?  292 ARG B CD  1 
ATOM   4976 N  NE  . ARG B 1 292 ? -28.471 20.812 -0.513  1.00 32.67  ?  292 ARG B NE  1 
ATOM   4977 C  CZ  . ARG B 1 292 ? -27.597 19.983 -1.076  1.00 30.37  ?  292 ARG B CZ  1 
ATOM   4978 N  NH1 . ARG B 1 292 ? -27.076 18.955 -0.422  1.00 28.92  ?  292 ARG B NH1 1 
ATOM   4979 N  NH2 . ARG B 1 292 ? -27.271 20.175 -2.331  1.00 30.51  ?  292 ARG B NH2 1 
ATOM   4980 N  N   . TYR B 1 293 ? -24.971 23.285 0.910   1.00 27.31  ?  293 TYR B N   1 
ATOM   4981 C  CA  . TYR B 1 293 ? -23.820 22.681 0.187   1.00 27.37  ?  293 TYR B CA  1 
ATOM   4982 C  C   . TYR B 1 293 ? -22.445 23.066 0.762   1.00 27.22  ?  293 TYR B C   1 
ATOM   4983 O  O   . TYR B 1 293 ? -21.448 22.347 0.499   1.00 27.53  ?  293 TYR B O   1 
ATOM   4984 C  CB  . TYR B 1 293 ? -23.818 23.201 -1.246  1.00 29.34  ?  293 TYR B CB  1 
ATOM   4985 C  CG  . TYR B 1 293 ? -23.181 22.291 -2.258  1.00 26.22  ?  293 TYR B CG  1 
ATOM   4986 C  CD1 . TYR B 1 293 ? -23.767 21.088 -2.563  1.00 22.69  ?  293 TYR B CD1 1 
ATOM   4987 C  CD2 . TYR B 1 293 ? -22.038 22.677 -2.935  1.00 24.07  ?  293 TYR B CD2 1 
ATOM   4988 C  CE1 . TYR B 1 293 ? -23.212 20.258 -3.511  1.00 26.59  ?  293 TYR B CE1 1 
ATOM   4989 C  CE2 . TYR B 1 293 ? -21.450 21.844 -3.860  1.00 23.91  ?  293 TYR B CE2 1 
ATOM   4990 C  CZ  . TYR B 1 293 ? -22.041 20.631 -4.144  1.00 25.47  ?  293 TYR B CZ  1 
ATOM   4991 O  OH  . TYR B 1 293 ? -21.512 19.817 -5.089  1.00 27.65  ?  293 TYR B OH  1 
ATOM   4992 N  N   . ASN B 1 294 ? -22.366 24.174 1.485   1.00 26.62  ?  294 ASN B N   1 
ATOM   4993 C  CA  . ASN B 1 294 ? -21.072 24.802 1.842   1.00 29.49  ?  294 ASN B CA  1 
ATOM   4994 C  C   . ASN B 1 294 ? -20.369 23.928 2.885   1.00 31.18  ?  294 ASN B C   1 
ATOM   4995 O  O   . ASN B 1 294 ? -21.045 23.361 3.794   1.00 28.74  ?  294 ASN B O   1 
ATOM   4996 C  CB  . ASN B 1 294 ? -21.224 26.240 2.341   1.00 30.15  ?  294 ASN B CB  1 
ATOM   4997 C  CG  . ASN B 1 294 ? -19.887 26.911 2.562   1.00 29.31  ?  294 ASN B CG  1 
ATOM   4998 O  OD1 . ASN B 1 294 ? -18.878 26.229 2.702   1.00 27.66  ?  294 ASN B OD1 1 
ATOM   4999 N  ND2 . ASN B 1 294 ? -19.892 28.236 2.624   1.00 30.31  ?  294 ASN B ND2 1 
ATOM   5000 N  N   . LEU B 1 295 ? -19.049 23.873 2.756   1.00 29.54  ?  295 LEU B N   1 
ATOM   5001 C  CA  . LEU B 1 295 ? -18.171 22.997 3.544   1.00 29.75  ?  295 LEU B CA  1 
ATOM   5002 C  C   . LEU B 1 295 ? -17.271 23.844 4.435   1.00 29.29  ?  295 LEU B C   1 
ATOM   5003 O  O   . LEU B 1 295 ? -16.202 23.323 4.791   1.00 27.60  ?  295 LEU B O   1 
ATOM   5004 C  CB  . LEU B 1 295 ? -17.383 22.133 2.557   1.00 30.80  ?  295 LEU B CB  1 
ATOM   5005 C  CG  . LEU B 1 295 ? -18.253 21.082 1.866   1.00 31.29  ?  295 LEU B CG  1 
ATOM   5006 C  CD1 . LEU B 1 295 ? -17.437 20.214 0.949   1.00 29.56  ?  295 LEU B CD1 1 
ATOM   5007 C  CD2 . LEU B 1 295 ? -18.962 20.204 2.886   1.00 31.02  ?  295 LEU B CD2 1 
ATOM   5008 N  N   . SER B 1 296 ? -17.747 25.029 4.856   1.00 27.61  ?  296 SER B N   1 
ATOM   5009 C  CA  . SER B 1 296 ? -16.938 26.051 5.575   1.00 28.74  ?  296 SER B CA  1 
ATOM   5010 C  C   . SER B 1 296 ? -16.637 25.575 6.989   1.00 29.12  ?  296 SER B C   1 
ATOM   5011 O  O   . SER B 1 296 ? -15.549 25.878 7.467   1.00 30.32  ?  296 SER B O   1 
ATOM   5012 C  CB  . SER B 1 296 ? -17.590 27.412 5.595   1.00 29.03  ?  296 SER B CB  1 
ATOM   5013 O  OG  . SER B 1 296 ? -18.805 27.408 6.340   1.00 29.77  ?  296 SER B OG  1 
ATOM   5014 N  N   . ILE B 1 297 ? -17.577 24.867 7.617   1.00 31.00  ?  297 ILE B N   1 
ATOM   5015 C  CA  . ILE B 1 297 ? -17.399 24.248 8.969   1.00 32.86  ?  297 ILE B CA  1 
ATOM   5016 C  C   . ILE B 1 297 ? -16.316 23.147 8.875   1.00 33.48  ?  297 ILE B C   1 
ATOM   5017 O  O   . ILE B 1 297 ? -16.599 22.108 8.236   1.00 31.52  ?  297 ILE B O   1 
ATOM   5018 C  CB  . ILE B 1 297 ? -18.737 23.707 9.524   1.00 28.75  ?  297 ILE B CB  1 
ATOM   5019 C  CG1 . ILE B 1 297 ? -19.747 24.829 9.775   1.00 31.78  ?  297 ILE B CG1 1 
ATOM   5020 C  CG2 . ILE B 1 297 ? -18.512 22.902 10.784  1.00 27.09  ?  297 ILE B CG2 1 
ATOM   5021 C  CD1 . ILE B 1 297 ? -21.165 24.346 10.056  1.00 33.15  ?  297 ILE B CD1 1 
ATOM   5022 N  N   . GLY B 1 298 ? -15.150 23.360 9.525   1.00 33.22  ?  298 GLY B N   1 
ATOM   5023 C  CA  . GLY B 1 298 ? -13.971 22.468 9.459   1.00 35.26  ?  298 GLY B CA  1 
ATOM   5024 C  C   . GLY B 1 298 ? -13.965 21.421 10.553  1.00 35.84  ?  298 GLY B C   1 
ATOM   5025 O  O   . GLY B 1 298 ? -13.011 20.610 10.615  1.00 38.24  ?  298 GLY B O   1 
ATOM   5026 N  N   . ASP B 1 299 ? -14.988 21.458 11.404  1.00 33.12  ?  299 ASP B N   1 
ATOM   5027 C  CA  . ASP B 1 299 ? -15.076 20.550 12.569  1.00 32.29  ?  299 ASP B CA  1 
ATOM   5028 C  C   . ASP B 1 299 ? -16.543 20.159 12.728  1.00 29.75  ?  299 ASP B C   1 
ATOM   5029 O  O   . ASP B 1 299 ? -17.315 20.351 11.788  1.00 31.27  ?  299 ASP B O   1 
ATOM   5030 C  CB  . ASP B 1 299 ? -14.744 21.317 13.836  1.00 31.54  ?  299 ASP B CB  1 
ATOM   5031 C  CG  . ASP B 1 299 ? -15.505 22.617 14.025  1.00 33.37  ?  299 ASP B CG  1 
ATOM   5032 O  OD1 . ASP B 1 299 ? -16.153 23.040 13.064  1.00 32.31  ?  299 ASP B OD1 1 
ATOM   5033 O  OD2 . ASP B 1 299 ? -15.450 23.181 15.130  1.00 36.08  ?  299 ASP B OD2 1 
ATOM   5034 N  N   . ALA B 1 300 ? -16.894 19.640 13.895  1.00 29.74  ?  300 ALA B N   1 
ATOM   5035 C  CA  . ALA B 1 300 ? -18.284 19.269 14.200  1.00 29.10  ?  300 ALA B CA  1 
ATOM   5036 C  C   . ALA B 1 300 ? -18.870 20.168 15.283  1.00 27.87  ?  300 ALA B C   1 
ATOM   5037 O  O   . ALA B 1 300 ? -18.102 20.784 16.007  1.00 26.74  ?  300 ALA B O   1 
ATOM   5038 C  CB  . ALA B 1 300 ? -18.217 17.811 14.623  1.00 28.94  ?  300 ALA B CB  1 
ATOM   5039 N  N   . LEU B 1 301 ? -20.186 20.286 15.349  1.00 26.78  ?  301 LEU B N   1 
ATOM   5040 C  CA  . LEU B 1 301 ? -20.829 20.984 16.475  1.00 27.34  ?  301 LEU B CA  1 
ATOM   5041 C  C   . LEU B 1 301 ? -20.682 20.068 17.681  1.00 28.17  ?  301 LEU B C   1 
ATOM   5042 O  O   . LEU B 1 301 ? -21.045 18.891 17.556  1.00 33.31  ?  301 LEU B O   1 
ATOM   5043 C  CB  . LEU B 1 301 ? -22.292 21.227 16.109  1.00 29.57  ?  301 LEU B CB  1 
ATOM   5044 C  CG  . LEU B 1 301 ? -22.525 22.047 14.837  1.00 30.91  ?  301 LEU B CG  1 
ATOM   5045 C  CD1 . LEU B 1 301 ? -23.964 22.537 14.810  1.00 32.60  ?  301 LEU B CD1 1 
ATOM   5046 C  CD2 . LEU B 1 301 ? -21.554 23.225 14.722  1.00 29.14  ?  301 LEU B CD2 1 
ATOM   5047 N  N   . PRO B 1 302 ? -20.018 20.504 18.790  1.00 25.44  ?  302 PRO B N   1 
ATOM   5048 C  CA  . PRO B 1 302 ? -19.785 19.635 19.943  1.00 24.44  ?  302 PRO B CA  1 
ATOM   5049 C  C   . PRO B 1 302 ? -20.842 19.718 21.057  1.00 26.08  ?  302 PRO B C   1 
ATOM   5050 O  O   . PRO B 1 302 ? -21.388 20.794 21.343  1.00 24.85  ?  302 PRO B O   1 
ATOM   5051 C  CB  . PRO B 1 302 ? -18.436 20.147 20.450  1.00 24.85  ?  302 PRO B CB  1 
ATOM   5052 C  CG  . PRO B 1 302 ? -18.533 21.665 20.220  1.00 25.00  ?  302 PRO B CG  1 
ATOM   5053 C  CD  . PRO B 1 302 ? -19.310 21.796 18.923  1.00 25.92  ?  302 PRO B CD  1 
ATOM   5054 N  N   . ARG B 1 303 ? -21.078 18.583 21.716  1.00 26.75  ?  303 ARG B N   1 
ATOM   5055 C  CA  . ARG B 1 303 ? -21.992 18.501 22.886  1.00 29.29  ?  303 ARG B CA  1 
ATOM   5056 C  C   . ARG B 1 303 ? -21.435 17.457 23.853  1.00 28.85  ?  303 ARG B C   1 
ATOM   5057 O  O   . ARG B 1 303 ? -20.890 16.448 23.366  1.00 26.94  ?  303 ARG B O   1 
ATOM   5058 C  CB  . ARG B 1 303 ? -23.409 18.079 22.469  1.00 31.28  ?  303 ARG B CB  1 
ATOM   5059 C  CG  . ARG B 1 303 ? -24.102 18.943 21.414  1.00 31.69  ?  303 ARG B CG  1 
ATOM   5060 C  CD  . ARG B 1 303 ? -24.566 20.283 21.936  1.00 30.56  ?  303 ARG B CD  1 
ATOM   5061 N  NE  . ARG B 1 303 ? -25.361 21.075 21.010  1.00 29.64  ?  303 ARG B NE  1 
ATOM   5062 C  CZ  . ARG B 1 303 ? -24.892 21.932 20.102  1.00 33.03  ?  303 ARG B CZ  1 
ATOM   5063 N  NH1 . ARG B 1 303 ? -23.587 22.072 19.916  1.00 30.46  ?  303 ARG B NH1 1 
ATOM   5064 N  NH2 . ARG B 1 303 ? -25.747 22.635 19.364  1.00 33.01  ?  303 ARG B NH2 1 
ATOM   5065 N  N   . ILE B 1 304 ? -21.579 17.689 25.156  1.00 28.98  ?  304 ILE B N   1 
ATOM   5066 C  CA  . ILE B 1 304 ? -21.345 16.654 26.207  1.00 31.30  ?  304 ILE B CA  1 
ATOM   5067 C  C   . ILE B 1 304 ? -22.693 16.046 26.588  1.00 31.98  ?  304 ILE B C   1 
ATOM   5068 O  O   . ILE B 1 304 ? -23.642 16.807 26.916  1.00 28.13  ?  304 ILE B O   1 
ATOM   5069 C  CB  . ILE B 1 304 ? -20.620 17.236 27.443  1.00 34.09  ?  304 ILE B CB  1 
ATOM   5070 C  CG1 . ILE B 1 304 ? -19.323 17.963 27.067  1.00 31.48  ?  304 ILE B CG1 1 
ATOM   5071 C  CG2 . ILE B 1 304 ? -20.361 16.125 28.451  1.00 34.25  ?  304 ILE B CG2 1 
ATOM   5072 C  CD1 . ILE B 1 304 ? -18.363 17.051 26.346  1.00 33.59  ?  304 ILE B CD1 1 
ATOM   5073 N  N   . ALA B 1 305 ? -22.787 14.719 26.532  1.00 34.62  ?  305 ALA B N   1 
ATOM   5074 C  CA  . ALA B 1 305 ? -23.964 13.988 27.052  1.00 35.96  ?  305 ALA B CA  1 
ATOM   5075 C  C   . ALA B 1 305 ? -24.045 14.208 28.578  1.00 38.94  ?  305 ALA B C   1 
ATOM   5076 O  O   . ALA B 1 305 ? -23.049 13.959 29.299  1.00 39.74  ?  305 ALA B O   1 
ATOM   5077 C  CB  . ALA B 1 305 ? -23.900 12.543 26.643  1.00 36.06  ?  305 ALA B CB  1 
ATOM   5078 N  N   . LEU B 1 306 ? -25.161 14.787 29.020  1.00 40.57  ?  306 LEU B N   1 
ATOM   5079 C  CA  . LEU B 1 306 ? -25.563 14.978 30.435  1.00 39.09  ?  306 LEU B CA  1 
ATOM   5080 C  C   . LEU B 1 306 ? -26.287 13.734 30.947  1.00 39.96  ?  306 LEU B C   1 
ATOM   5081 O  O   . LEU B 1 306 ? -26.466 13.627 32.146  1.00 45.45  ?  306 LEU B O   1 
ATOM   5082 C  CB  . LEU B 1 306 ? -26.509 16.169 30.523  1.00 38.09  ?  306 LEU B CB  1 
ATOM   5083 C  CG  . LEU B 1 306 ? -25.872 17.495 30.154  1.00 39.49  ?  306 LEU B CG  1 
ATOM   5084 C  CD1 . LEU B 1 306 ? -26.896 18.631 30.197  1.00 33.44  ?  306 LEU B CD1 1 
ATOM   5085 C  CD2 . LEU B 1 306 ? -24.691 17.753 31.077  1.00 39.75  ?  306 LEU B CD2 1 
ATOM   5086 N  N   . ALA B 1 307 ? -26.699 12.833 30.071  1.00 41.31  ?  307 ALA B N   1 
ATOM   5087 C  CA  . ALA B 1 307 ? -27.327 11.558 30.477  1.00 40.74  ?  307 ALA B CA  1 
ATOM   5088 C  C   . ALA B 1 307 ? -26.949 10.489 29.460  1.00 39.73  ?  307 ALA B C   1 
ATOM   5089 O  O   . ALA B 1 307 ? -26.563 10.867 28.338  1.00 43.22  ?  307 ALA B O   1 
ATOM   5090 C  CB  . ALA B 1 307 ? -28.829 11.726 30.561  1.00 40.53  ?  307 ALA B CB  1 
ATOM   5091 N  N   . ASP B 1 308 ? -27.093 9.218  29.835  1.00 36.75  ?  308 ASP B N   1 
ATOM   5092 C  CA  . ASP B 1 308 ? -27.062 8.087  28.878  1.00 37.65  ?  308 ASP B CA  1 
ATOM   5093 C  C   . ASP B 1 308 ? -28.201 8.306  27.872  1.00 39.67  ?  308 ASP B C   1 
ATOM   5094 O  O   . ASP B 1 308 ? -29.318 8.589  28.293  1.00 46.00  ?  308 ASP B O   1 
ATOM   5095 C  CB  . ASP B 1 308 ? -27.106 6.746  29.608  1.00 36.21  ?  308 ASP B CB  1 
ATOM   5096 C  CG  . ASP B 1 308 ? -25.813 6.454  30.337  1.00 39.30  ?  308 ASP B CG  1 
ATOM   5097 O  OD1 . ASP B 1 308 ? -24.818 7.112  30.065  1.00 55.13  ?  308 ASP B OD1 1 
ATOM   5098 O  OD2 . ASP B 1 308 ? -25.793 5.547  31.125  1.00 49.83  ?  308 ASP B OD2 1 
ATOM   5099 N  N   . VAL B 1 309 ? -27.911 8.229  26.577  1.00 41.75  ?  309 VAL B N   1 
ATOM   5100 C  CA  . VAL B 1 309 ? -28.925 8.395  25.500  1.00 40.78  ?  309 VAL B CA  1 
ATOM   5101 C  C   . VAL B 1 309 ? -28.704 7.337  24.432  1.00 38.07  ?  309 VAL B C   1 
ATOM   5102 O  O   . VAL B 1 309 ? -27.559 7.129  24.018  1.00 44.61  ?  309 VAL B O   1 
ATOM   5103 C  CB  . VAL B 1 309 ? -28.857 9.792  24.860  1.00 41.40  ?  309 VAL B CB  1 
ATOM   5104 C  CG1 . VAL B 1 309 ? -29.826 9.888  23.691  1.00 40.86  ?  309 VAL B CG1 1 
ATOM   5105 C  CG2 . VAL B 1 309 ? -29.113 10.878 25.887  1.00 40.70  ?  309 VAL B CG2 1 
ATOM   5106 N  N   . ARG B 1 310 ? -29.788 6.745  23.970  1.00 38.92  ?  310 ARG B N   1 
ATOM   5107 C  CA  . ARG B 1 310 ? -29.807 5.825  22.808  1.00 39.80  ?  310 ARG B CA  1 
ATOM   5108 C  C   . ARG B 1 310 ? -29.965 6.721  21.575  1.00 39.23  ?  310 ARG B C   1 
ATOM   5109 O  O   . ARG B 1 310 ? -31.056 7.324  21.371  1.00 39.04  ?  310 ARG B O   1 
ATOM   5110 C  CB  . ARG B 1 310 ? -30.924 4.790  22.994  1.00 40.95  ?  310 ARG B CB  1 
ATOM   5111 C  CG  . ARG B 1 310 ? -31.117 3.833  21.836  1.00 45.74  ?  310 ARG B CG  1 
ATOM   5112 C  CD  . ARG B 1 310 ? -29.889 2.983  21.726  1.00 50.92  ?  310 ARG B CD  1 
ATOM   5113 N  NE  . ARG B 1 310 ? -30.153 1.749  21.009  1.00 59.01  ?  310 ARG B NE  1 
ATOM   5114 C  CZ  . ARG B 1 310 ? -29.598 0.574  21.283  1.00 62.94  ?  310 ARG B CZ  1 
ATOM   5115 N  NH1 . ARG B 1 310 ? -28.779 0.438  22.318  1.00 63.43  ?  310 ARG B NH1 1 
ATOM   5116 N  NH2 . ARG B 1 310 ? -29.878 -0.472 20.523  1.00 63.55  ?  310 ARG B NH2 1 
ATOM   5117 N  N   . LEU B 1 311 ? -28.898 6.840  20.796  1.00 37.82  ?  311 LEU B N   1 
ATOM   5118 C  CA  . LEU B 1 311 ? -28.894 7.651  19.562  1.00 36.08  ?  311 LEU B CA  1 
ATOM   5119 C  C   . LEU B 1 311 ? -28.551 6.709  18.420  1.00 35.45  ?  311 LEU B C   1 
ATOM   5120 O  O   . LEU B 1 311 ? -27.393 6.233  18.369  1.00 36.04  ?  311 LEU B O   1 
ATOM   5121 C  CB  . LEU B 1 311 ? -27.889 8.792  19.680  1.00 36.44  ?  311 LEU B CB  1 
ATOM   5122 C  CG  . LEU B 1 311 ? -27.738 9.608  18.403  1.00 38.32  ?  311 LEU B CG  1 
ATOM   5123 C  CD1 . LEU B 1 311 ? -28.890 10.591 18.292  1.00 36.56  ?  311 LEU B CD1 1 
ATOM   5124 C  CD2 . LEU B 1 311 ? -26.379 10.304 18.351  1.00 37.44  ?  311 LEU B CD2 1 
ATOM   5125 N  N   . GLY B 1 312 ? -29.539 6.451  17.564  1.00 38.11  ?  312 GLY B N   1 
ATOM   5126 C  CA  . GLY B 1 312 ? -29.488 5.385  16.546  1.00 42.68  ?  312 GLY B CA  1 
ATOM   5127 C  C   . GLY B 1 312 ? -29.280 4.044  17.214  1.00 42.82  ?  312 GLY B C   1 
ATOM   5128 O  O   . GLY B 1 312 ? -30.061 3.704  18.148  1.00 39.52  ?  312 GLY B O   1 
ATOM   5129 N  N   . GLU B 1 313 ? -28.195 3.373  16.855  1.00 44.05  ?  313 GLU B N   1 
ATOM   5130 C  CA  . GLU B 1 313 ? -27.893 2.001  17.326  1.00 49.75  ?  313 GLU B CA  1 
ATOM   5131 C  C   . GLU B 1 313 ? -26.790 2.045  18.380  1.00 47.66  ?  313 GLU B C   1 
ATOM   5132 O  O   . GLU B 1 313 ? -26.273 0.983  18.699  1.00 57.25  ?  313 GLU B O   1 
ATOM   5133 C  CB  . GLU B 1 313 ? -27.521 1.113  16.139  1.00 50.64  ?  313 GLU B CB  1 
ATOM   5134 C  CG  . GLU B 1 313 ? -28.732 0.807  15.266  1.00 58.93  ?  313 GLU B CG  1 
ATOM   5135 C  CD  . GLU B 1 313 ? -28.491 -0.208 14.155  1.00 67.93  ?  313 GLU B CD  1 
ATOM   5136 O  OE1 . GLU B 1 313 ? -27.404 -0.148 13.554  1.00 64.21  ?  313 GLU B OE1 1 
ATOM   5137 O  OE2 . GLU B 1 313 ? -29.381 -1.079 13.913  1.00 74.12  ?  313 GLU B OE2 1 
ATOM   5138 N  N   . VAL B 1 314 ? -26.466 3.221  18.915  1.00 44.65  ?  314 VAL B N   1 
ATOM   5139 C  CA  . VAL B 1 314 ? -25.333 3.411  19.875  1.00 40.33  ?  314 VAL B CA  1 
ATOM   5140 C  C   . VAL B 1 314 ? -25.866 3.922  21.217  1.00 38.47  ?  314 VAL B C   1 
ATOM   5141 O  O   . VAL B 1 314 ? -26.814 4.725  21.236  1.00 45.28  ?  314 VAL B O   1 
ATOM   5142 C  CB  . VAL B 1 314 ? -24.249 4.343  19.299  1.00 36.00  ?  314 VAL B CB  1 
ATOM   5143 C  CG1 . VAL B 1 314 ? -23.121 4.619  20.296  1.00 33.60  ?  314 VAL B CG1 1 
ATOM   5144 C  CG2 . VAL B 1 314 ? -23.689 3.746  18.014  1.00 35.10  ?  314 VAL B CG2 1 
ATOM   5145 N  N   . GLU B 1 315 ? -25.267 3.435  22.292  1.00 36.64  ?  315 GLU B N   1 
ATOM   5146 C  CA  . GLU B 1 315 ? -25.548 3.832  23.678  1.00 40.13  ?  315 GLU B CA  1 
ATOM   5147 C  C   . GLU B 1 315 ? -24.449 4.824  24.057  1.00 40.07  ?  315 GLU B C   1 
ATOM   5148 O  O   . GLU B 1 315 ? -23.274 4.431  24.130  1.00 42.96  ?  315 GLU B O   1 
ATOM   5149 C  CB  . GLU B 1 315 ? -25.616 2.587  24.564  1.00 45.16  ?  315 GLU B CB  1 
ATOM   5150 C  CG  . GLU B 1 315 ? -26.454 2.791  25.805  1.00 53.02  ?  315 GLU B CG  1 
ATOM   5151 C  CD  . GLU B 1 315 ? -27.921 3.117  25.553  1.00 62.42  ?  315 GLU B CD  1 
ATOM   5152 O  OE1 . GLU B 1 315 ? -28.433 4.065  26.199  1.00 76.04  ?  315 GLU B OE1 1 
ATOM   5153 O  OE2 . GLU B 1 315 ? -28.561 2.410  24.734  1.00 58.48  ?  315 GLU B OE2 1 
ATOM   5154 N  N   . ILE B 1 316 ? -24.825 6.084  24.210  1.00 38.29  ?  316 ILE B N   1 
ATOM   5155 C  CA  . ILE B 1 316 ? -23.897 7.197  24.525  1.00 37.01  ?  316 ILE B CA  1 
ATOM   5156 C  C   . ILE B 1 316 ? -24.042 7.437  26.020  1.00 39.91  ?  316 ILE B C   1 
ATOM   5157 O  O   . ILE B 1 316 ? -25.184 7.708  26.481  1.00 36.34  ?  316 ILE B O   1 
ATOM   5158 C  CB  . ILE B 1 316 ? -24.219 8.443  23.673  1.00 38.44  ?  316 ILE B CB  1 
ATOM   5159 C  CG1 . ILE B 1 316 ? -24.043 8.158  22.177  1.00 38.18  ?  316 ILE B CG1 1 
ATOM   5160 C  CG2 . ILE B 1 316 ? -23.408 9.650  24.139  1.00 38.33  ?  316 ILE B CG2 1 
ATOM   5161 C  CD1 . ILE B 1 316 ? -24.355 9.344  21.279  1.00 38.98  ?  316 ILE B CD1 1 
ATOM   5162 N  N   . ARG B 1 317 ? -22.920 7.335  26.728  1.00 40.63  ?  317 ARG B N   1 
ATOM   5163 C  CA  . ARG B 1 317 ? -22.843 7.429  28.199  1.00 40.26  ?  317 ARG B CA  1 
ATOM   5164 C  C   . ARG B 1 317 ? -22.721 8.910  28.549  1.00 38.45  ?  317 ARG B C   1 
ATOM   5165 O  O   . ARG B 1 317 ? -22.072 9.626  27.783  1.00 45.91  ?  317 ARG B O   1 
ATOM   5166 C  CB  . ARG B 1 317 ? -21.647 6.618  28.713  1.00 47.56  ?  317 ARG B CB  1 
ATOM   5167 C  CG  . ARG B 1 317 ? -21.676 5.136  28.363  1.00 53.02  ?  317 ARG B CG  1 
ATOM   5168 C  CD  . ARG B 1 317 ? -22.757 4.394  29.128  1.00 70.43  ?  317 ARG B CD  1 
ATOM   5169 N  NE  . ARG B 1 317 ? -23.186 3.153  28.484  1.00 83.82  ?  317 ARG B NE  1 
ATOM   5170 C  CZ  . ARG B 1 317 ? -24.393 2.589  28.619  1.00 82.06  ?  317 ARG B CZ  1 
ATOM   5171 N  NH1 . ARG B 1 317 ? -25.324 3.141  29.384  1.00 72.95  ?  317 ARG B NH1 1 
ATOM   5172 N  NH2 . ARG B 1 317 ? -24.662 1.462  27.980  1.00 84.09  ?  317 ARG B NH2 1 
ATOM   5173 N  N   . ALA B 1 318 ? -23.334 9.342  29.651  1.00 34.96  ?  318 ALA B N   1 
ATOM   5174 C  CA  . ALA B 1 318 ? -23.164 10.677 30.260  1.00 31.24  ?  318 ALA B CA  1 
ATOM   5175 C  C   . ALA B 1 318 ? -21.663 10.991 30.331  1.00 33.17  ?  318 ALA B C   1 
ATOM   5176 O  O   . ALA B 1 318 ? -20.874 10.056 30.629  1.00 35.69  ?  318 ALA B O   1 
ATOM   5177 C  CB  . ALA B 1 318 ? -23.826 10.678 31.617  1.00 27.50  ?  318 ALA B CB  1 
ATOM   5178 N  N   . GLY B 1 319 ? -21.267 12.230 30.019  1.00 34.10  ?  319 GLY B N   1 
ATOM   5179 C  CA  . GLY B 1 319 ? -19.856 12.690 30.070  1.00 32.92  ?  319 GLY B CA  1 
ATOM   5180 C  C   . GLY B 1 319 ? -19.130 12.496 28.743  1.00 31.38  ?  319 GLY B C   1 
ATOM   5181 O  O   . GLY B 1 319 ? -18.073 13.050 28.572  1.00 33.11  ?  319 GLY B O   1 
ATOM   5182 N  N   . GLU B 1 320 ? -19.680 11.722 27.812  1.00 31.22  ?  320 GLU B N   1 
ATOM   5183 C  CA  . GLU B 1 320 ? -19.056 11.506 26.485  1.00 28.88  ?  320 GLU B CA  1 
ATOM   5184 C  C   . GLU B 1 320 ? -19.264 12.728 25.563  1.00 28.91  ?  320 GLU B C   1 
ATOM   5185 O  O   . GLU B 1 320 ? -20.220 13.560 25.749  1.00 28.90  ?  320 GLU B O   1 
ATOM   5186 C  CB  . GLU B 1 320 ? -19.539 10.178 25.911  1.00 28.58  ?  320 GLU B CB  1 
ATOM   5187 C  CG  . GLU B 1 320 ? -19.048 8.984  26.727  1.00 32.97  ?  320 GLU B CG  1 
ATOM   5188 C  CD  . GLU B 1 320 ? -19.142 7.627  26.034  1.00 37.04  ?  320 GLU B CD  1 
ATOM   5189 O  OE1 . GLU B 1 320 ? -20.241 7.267  25.581  1.00 38.52  ?  320 GLU B OE1 1 
ATOM   5190 O  OE2 . GLU B 1 320 ? -18.104 6.944  25.907  1.00 42.90  ?  320 GLU B OE2 1 
ATOM   5191 N  N   . LEU B 1 321 ? -18.343 12.878 24.614  1.00 28.60  ?  321 LEU B N   1 
ATOM   5192 C  CA  . LEU B 1 321 ? -18.336 13.980 23.631  1.00 28.10  ?  321 LEU B CA  1 
ATOM   5193 C  C   . LEU B 1 321 ? -19.053 13.471 22.387  1.00 27.83  ?  321 LEU B C   1 
ATOM   5194 O  O   . LEU B 1 321 ? -18.746 12.353 21.905  1.00 25.40  ?  321 LEU B O   1 
ATOM   5195 C  CB  . LEU B 1 321 ? -16.896 14.408 23.341  1.00 31.08  ?  321 LEU B CB  1 
ATOM   5196 C  CG  . LEU B 1 321 ? -16.709 15.510 22.291  1.00 34.07  ?  321 LEU B CG  1 
ATOM   5197 C  CD1 . LEU B 1 321 ? -17.512 16.746 22.661  1.00 32.91  ?  321 LEU B CD1 1 
ATOM   5198 C  CD2 . LEU B 1 321 ? -15.222 15.855 22.099  1.00 31.39  ?  321 LEU B CD2 1 
ATOM   5199 N  N   . VAL B 1 322 ? -20.019 14.259 21.922  1.00 30.02  ?  322 VAL B N   1 
ATOM   5200 C  CA  . VAL B 1 322 ? -20.808 13.998 20.688  1.00 29.26  ?  322 VAL B CA  1 
ATOM   5201 C  C   . VAL B 1 322 ? -20.524 15.135 19.724  1.00 28.84  ?  322 VAL B C   1 
ATOM   5202 O  O   . VAL B 1 322 ? -20.561 16.307 20.165  1.00 28.73  ?  322 VAL B O   1 
ATOM   5203 C  CB  . VAL B 1 322 ? -22.305 13.903 21.005  1.00 31.06  ?  322 VAL B CB  1 
ATOM   5204 C  CG1 . VAL B 1 322 ? -23.122 13.743 19.736  1.00 30.86  ?  322 VAL B CG1 1 
ATOM   5205 C  CG2 . VAL B 1 322 ? -22.568 12.767 21.988  1.00 31.31  ?  322 VAL B CG2 1 
ATOM   5206 N  N   . LEU B 1 323 ? -20.227 14.777 18.479  1.00 29.12  ?  323 LEU B N   1 
ATOM   5207 C  CA  . LEU B 1 323 ? -19.740 15.683 17.409  1.00 26.91  ?  323 LEU B CA  1 
ATOM   5208 C  C   . LEU B 1 323 ? -20.694 15.563 16.253  1.00 26.35  ?  323 LEU B C   1 
ATOM   5209 O  O   . LEU B 1 323 ? -20.875 14.416 15.728  1.00 27.62  ?  323 LEU B O   1 
ATOM   5210 C  CB  . LEU B 1 323 ? -18.349 15.219 16.967  1.00 28.07  ?  323 LEU B CB  1 
ATOM   5211 C  CG  . LEU B 1 323 ? -17.252 15.483 17.992  1.00 28.10  ?  323 LEU B CG  1 
ATOM   5212 C  CD1 . LEU B 1 323 ? -15.887 15.129 17.411  1.00 29.93  ?  323 LEU B CD1 1 
ATOM   5213 C  CD2 . LEU B 1 323 ? -17.303 16.937 18.413  1.00 27.49  ?  323 LEU B CD2 1 
ATOM   5214 N  N   . VAL B 1 324 ? -21.273 16.685 15.857  1.00 27.79  ?  324 VAL B N   1 
ATOM   5215 C  CA  . VAL B 1 324 ? -22.281 16.696 14.750  1.00 26.44  ?  324 VAL B CA  1 
ATOM   5216 C  C   . VAL B 1 324 ? -21.586 17.150 13.469  1.00 24.33  ?  324 VAL B C   1 
ATOM   5217 O  O   . VAL B 1 324 ? -20.951 18.212 13.471  1.00 20.19  ?  324 VAL B O   1 
ATOM   5218 C  CB  . VAL B 1 324 ? -23.482 17.583 15.088  1.00 26.80  ?  324 VAL B CB  1 
ATOM   5219 C  CG1 . VAL B 1 324 ? -24.521 17.519 13.989  1.00 29.38  ?  324 VAL B CG1 1 
ATOM   5220 C  CG2 . VAL B 1 324 ? -24.063 17.213 16.449  1.00 29.12  ?  324 VAL B CG2 1 
ATOM   5221 N  N   . LEU B 1 325 ? -21.651 16.277 12.471  1.00 27.20  ?  325 LEU B N   1 
ATOM   5222 C  CA  . LEU B 1 325 ? -21.073 16.451 11.125  1.00 28.93  ?  325 LEU B CA  1 
ATOM   5223 C  C   . LEU B 1 325 ? -22.142 17.056 10.218  1.00 25.21  ?  325 LEU B C   1 
ATOM   5224 O  O   . LEU B 1 325 ? -22.764 16.301 9.459   1.00 22.09  ?  325 LEU B O   1 
ATOM   5225 C  CB  . LEU B 1 325 ? -20.589 15.105 10.576  1.00 29.77  ?  325 LEU B CB  1 
ATOM   5226 C  CG  . LEU B 1 325 ? -19.661 15.212 9.360   1.00 30.55  ?  325 LEU B CG  1 
ATOM   5227 C  CD1 . LEU B 1 325 ? -18.349 15.860 9.759   1.00 32.32  ?  325 LEU B CD1 1 
ATOM   5228 C  CD2 . LEU B 1 325 ? -19.416 13.852 8.710   1.00 30.24  ?  325 LEU B CD2 1 
ATOM   5229 N  N   . ILE B 1 326 ? -22.233 18.379 10.260  1.00 22.72  ?  326 ILE B N   1 
ATOM   5230 C  CA  . ILE B 1 326 ? -23.145 19.183 9.415   1.00 24.52  ?  326 ILE B CA  1 
ATOM   5231 C  C   . ILE B 1 326 ? -23.108 18.707 7.964   1.00 25.88  ?  326 ILE B C   1 
ATOM   5232 O  O   . ILE B 1 326 ? -24.223 18.505 7.387   1.00 29.84  ?  326 ILE B O   1 
ATOM   5233 C  CB  . ILE B 1 326 ? -22.823 20.677 9.544   1.00 26.13  ?  326 ILE B CB  1 
ATOM   5234 C  CG1 . ILE B 1 326 ? -23.091 21.158 10.968  1.00 25.24  ?  326 ILE B CG1 1 
ATOM   5235 C  CG2 . ILE B 1 326 ? -23.625 21.474 8.527   1.00 28.92  ?  326 ILE B CG2 1 
ATOM   5236 C  CD1 . ILE B 1 326 ? -24.482 20.805 11.470  1.00 27.07  ?  326 ILE B CD1 1 
ATOM   5237 N  N   . GLU B 1 327 ? -21.925 18.530 7.373   1.00 26.26  ?  327 GLU B N   1 
ATOM   5238 C  CA  . GLU B 1 327 ? -21.821 18.164 5.928   1.00 27.62  ?  327 GLU B CA  1 
ATOM   5239 C  C   . GLU B 1 327 ? -22.353 16.726 5.720   1.00 29.06  ?  327 GLU B C   1 
ATOM   5240 O  O   . GLU B 1 327 ? -22.959 16.438 4.646   1.00 30.56  ?  327 GLU B O   1 
ATOM   5241 C  CB  . GLU B 1 327 ? -20.403 18.381 5.396   1.00 26.12  ?  327 GLU B CB  1 
ATOM   5242 C  CG  . GLU B 1 327 ? -19.350 17.470 5.979   1.00 27.32  ?  327 GLU B CG  1 
ATOM   5243 C  CD  . GLU B 1 327 ? -18.539 18.148 7.058   1.00 30.50  ?  327 GLU B CD  1 
ATOM   5244 O  OE1 . GLU B 1 327 ? -19.185 18.798 7.957   1.00 32.59  ?  327 GLU B OE1 1 
ATOM   5245 O  OE2 . GLU B 1 327 ? -17.268 18.036 6.992   1.00 28.88  ?  327 GLU B OE2 1 
ATOM   5246 N  N   . GLY B 1 328 ? -22.221 15.875 6.731   1.00 26.49  ?  328 GLY B N   1 
ATOM   5247 C  CA  . GLY B 1 328 ? -22.870 14.558 6.731   1.00 29.53  ?  328 GLY B CA  1 
ATOM   5248 C  C   . GLY B 1 328 ? -24.366 14.697 6.534   1.00 27.97  ?  328 GLY B C   1 
ATOM   5249 O  O   . GLY B 1 328 ? -24.919 14.043 5.616   1.00 28.76  ?  328 GLY B O   1 
ATOM   5250 N  N   . ALA B 1 329 ? -24.992 15.549 7.338   1.00 27.93  ?  329 ALA B N   1 
ATOM   5251 C  CA  . ALA B 1 329 ? -26.465 15.699 7.418   1.00 30.40  ?  329 ALA B CA  1 
ATOM   5252 C  C   . ALA B 1 329 ? -26.983 16.449 6.189   1.00 30.83  ?  329 ALA B C   1 
ATOM   5253 O  O   . ALA B 1 329 ? -28.007 16.040 5.600   1.00 32.37  ?  329 ALA B O   1 
ATOM   5254 C  CB  . ALA B 1 329 ? -26.840 16.434 8.670   1.00 32.07  ?  329 ALA B CB  1 
ATOM   5255 N  N   . ASN B 1 330 ? -26.279 17.503 5.795   1.00 30.66  ?  330 ASN B N   1 
ATOM   5256 C  CA  . ASN B 1 330 ? -26.717 18.354 4.665   1.00 28.53  ?  330 ASN B CA  1 
ATOM   5257 C  C   . ASN B 1 330 ? -26.481 17.628 3.343   1.00 25.02  ?  330 ASN B C   1 
ATOM   5258 O  O   . ASN B 1 330 ? -27.032 18.088 2.355   1.00 25.13  ?  330 ASN B O   1 
ATOM   5259 C  CB  . ASN B 1 330 ? -26.075 19.741 4.727   1.00 29.99  ?  330 ASN B CB  1 
ATOM   5260 C  CG  . ASN B 1 330 ? -26.705 20.622 5.783   1.00 28.74  ?  330 ASN B CG  1 
ATOM   5261 O  OD1 . ASN B 1 330 ? -27.759 20.308 6.299   1.00 28.72  ?  330 ASN B OD1 1 
ATOM   5262 N  ND2 . ASN B 1 330 ? -26.090 21.744 6.089   1.00 32.56  ?  330 ASN B ND2 1 
ATOM   5263 N  N   . TYR B 1 331 ? -25.733 16.525 3.306   1.00 26.16  ?  331 TYR B N   1 
ATOM   5264 C  CA  . TYR B 1 331 ? -25.539 15.740 2.051   1.00 24.68  ?  331 TYR B CA  1 
ATOM   5265 C  C   . TYR B 1 331 ? -26.270 14.392 2.128   1.00 25.52  ?  331 TYR B C   1 
ATOM   5266 O  O   . TYR B 1 331 ? -26.039 13.525 1.266   1.00 24.78  ?  331 TYR B O   1 
ATOM   5267 C  CB  . TYR B 1 331 ? -24.050 15.554 1.760   1.00 23.60  ?  331 TYR B CB  1 
ATOM   5268 C  CG  . TYR B 1 331 ? -23.343 16.699 1.084   1.00 22.80  ?  331 TYR B CG  1 
ATOM   5269 C  CD1 . TYR B 1 331 ? -23.139 17.906 1.732   1.00 24.00  ?  331 TYR B CD1 1 
ATOM   5270 C  CD2 . TYR B 1 331 ? -22.837 16.572 -0.193  1.00 22.37  ?  331 TYR B CD2 1 
ATOM   5271 C  CE1 . TYR B 1 331 ? -22.473 18.957 1.122   1.00 23.31  ?  331 TYR B CE1 1 
ATOM   5272 C  CE2 . TYR B 1 331 ? -22.202 17.628 -0.833  1.00 22.43  ?  331 TYR B CE2 1 
ATOM   5273 C  CZ  . TYR B 1 331 ? -21.996 18.824 -0.171  1.00 22.17  ?  331 TYR B CZ  1 
ATOM   5274 O  OH  . TYR B 1 331 ? -21.282 19.841 -0.755  1.00 19.22  ?  331 TYR B OH  1 
ATOM   5275 N  N   . ASP B 1 332 ? -27.141 14.206 3.119   1.00 29.70  ?  332 ASP B N   1 
ATOM   5276 C  CA  . ASP B 1 332 ? -27.850 12.917 3.356   1.00 30.17  ?  332 ASP B CA  1 
ATOM   5277 C  C   . ASP B 1 332 ? -28.899 12.731 2.263   1.00 27.52  ?  332 ASP B C   1 
ATOM   5278 O  O   . ASP B 1 332 ? -29.893 13.454 2.206   1.00 24.97  ?  332 ASP B O   1 
ATOM   5279 C  CB  . ASP B 1 332 ? -28.447 12.842 4.770   1.00 32.56  ?  332 ASP B CB  1 
ATOM   5280 C  CG  . ASP B 1 332 ? -28.861 11.428 5.167   1.00 33.18  ?  332 ASP B CG  1 
ATOM   5281 O  OD1 . ASP B 1 332 ? -29.253 10.673 4.256   1.00 33.87  ?  332 ASP B OD1 1 
ATOM   5282 O  OD2 . ASP B 1 332 ? -28.788 11.089 6.383   1.00 32.17  ?  332 ASP B OD2 1 
ATOM   5283 N  N   . PRO B 1 333 ? -28.729 11.729 1.375   1.00 31.15  ?  333 PRO B N   1 
ATOM   5284 C  CA  . PRO B 1 333 ? -29.712 11.442 0.330   1.00 32.92  ?  333 PRO B CA  1 
ATOM   5285 C  C   . PRO B 1 333 ? -31.081 10.981 0.843   1.00 32.22  ?  333 PRO B C   1 
ATOM   5286 O  O   . PRO B 1 333 ? -31.976 10.937 0.040   1.00 34.25  ?  333 PRO B O   1 
ATOM   5287 C  CB  . PRO B 1 333 ? -29.055 10.330 -0.513  1.00 32.13  ?  333 PRO B CB  1 
ATOM   5288 C  CG  . PRO B 1 333 ? -28.118 9.665  0.452   1.00 31.67  ?  333 PRO B CG  1 
ATOM   5289 C  CD  . PRO B 1 333 ? -27.584 10.807 1.293   1.00 32.81  ?  333 PRO B CD  1 
ATOM   5290 N  N   . ALA B 1 334 ? -31.216 10.711 2.144   1.00 30.96  ?  334 ALA B N   1 
ATOM   5291 C  CA  . ALA B 1 334 ? -32.498 10.383 2.806   1.00 31.41  ?  334 ALA B CA  1 
ATOM   5292 C  C   . ALA B 1 334 ? -33.413 11.607 2.839   1.00 32.46  ?  334 ALA B C   1 
ATOM   5293 O  O   . ALA B 1 334 ? -34.635 11.462 2.927   1.00 34.44  ?  334 ALA B O   1 
ATOM   5294 C  CB  . ALA B 1 334 ? -32.214 9.883  4.189   1.00 32.54  ?  334 ALA B CB  1 
ATOM   5295 N  N   . VAL B 1 335 ? -32.833 12.789 2.847   1.00 31.74  ?  335 VAL B N   1 
ATOM   5296 C  CA  . VAL B 1 335 ? -33.597 14.047 2.980   1.00 30.55  ?  335 VAL B CA  1 
ATOM   5297 C  C   . VAL B 1 335 ? -33.395 14.883 1.723   1.00 32.18  ?  335 VAL B C   1 
ATOM   5298 O  O   . VAL B 1 335 ? -34.354 15.453 1.249   1.00 31.32  ?  335 VAL B O   1 
ATOM   5299 C  CB  . VAL B 1 335 ? -33.110 14.795 4.222   1.00 31.53  ?  335 VAL B CB  1 
ATOM   5300 C  CG1 . VAL B 1 335 ? -33.756 16.163 4.321   1.00 31.36  ?  335 VAL B CG1 1 
ATOM   5301 C  CG2 . VAL B 1 335 ? -33.292 13.970 5.497   1.00 29.85  ?  335 VAL B CG2 1 
ATOM   5302 N  N   . PHE B 1 336 ? -32.167 14.975 1.210   1.00 36.45  ?  336 PHE B N   1 
ATOM   5303 C  CA  . PHE B 1 336 ? -31.851 15.826 0.027   1.00 33.02  ?  336 PHE B CA  1 
ATOM   5304 C  C   . PHE B 1 336 ? -31.641 14.984 -1.233  1.00 32.48  ?  336 PHE B C   1 
ATOM   5305 O  O   . PHE B 1 336 ? -30.587 14.387 -1.406  1.00 32.41  ?  336 PHE B O   1 
ATOM   5306 C  CB  . PHE B 1 336 ? -30.636 16.681 0.354   1.00 29.21  ?  336 PHE B CB  1 
ATOM   5307 C  CG  . PHE B 1 336 ? -30.828 17.476 1.611   1.00 28.65  ?  336 PHE B CG  1 
ATOM   5308 C  CD1 . PHE B 1 336 ? -31.674 18.570 1.624   1.00 27.17  ?  336 PHE B CD1 1 
ATOM   5309 C  CD2 . PHE B 1 336 ? -30.211 17.086 2.785   1.00 28.90  ?  336 PHE B CD2 1 
ATOM   5310 C  CE1 . PHE B 1 336 ? -31.830 19.313 2.771   1.00 26.08  ?  336 PHE B CE1 1 
ATOM   5311 C  CE2 . PHE B 1 336 ? -30.367 17.827 3.938   1.00 27.26  ?  336 PHE B CE2 1 
ATOM   5312 C  CZ  . PHE B 1 336 ? -31.168 18.942 3.920   1.00 29.12  ?  336 PHE B CZ  1 
ATOM   5313 N  N   . PRO B 1 337 ? -32.612 14.950 -2.174  1.00 28.94  ?  337 PRO B N   1 
ATOM   5314 C  CA  . PRO B 1 337 ? -32.400 14.276 -3.455  1.00 29.09  ?  337 PRO B CA  1 
ATOM   5315 C  C   . PRO B 1 337 ? -31.169 14.881 -4.150  1.00 29.90  ?  337 PRO B C   1 
ATOM   5316 O  O   . PRO B 1 337 ? -30.938 16.081 -3.993  1.00 30.75  ?  337 PRO B O   1 
ATOM   5317 C  CB  . PRO B 1 337 ? -33.705 14.493 -4.241  1.00 27.88  ?  337 PRO B CB  1 
ATOM   5318 C  CG  . PRO B 1 337 ? -34.720 14.895 -3.180  1.00 30.01  ?  337 PRO B CG  1 
ATOM   5319 C  CD  . PRO B 1 337 ? -33.935 15.583 -2.071  1.00 27.61  ?  337 PRO B CD  1 
ATOM   5320 N  N   . HIS B 1 338 ? -30.380 14.034 -4.826  1.00 31.02  ?  338 HIS B N   1 
ATOM   5321 C  CA  . HIS B 1 338 ? -29.128 14.384 -5.559  1.00 30.67  ?  338 HIS B CA  1 
ATOM   5322 C  C   . HIS B 1 338 ? -28.306 15.354 -4.717  1.00 27.96  ?  338 HIS B C   1 
ATOM   5323 O  O   . HIS B 1 338 ? -27.958 16.454 -5.122  1.00 28.87  ?  338 HIS B O   1 
ATOM   5324 C  CB  . HIS B 1 338 ? -29.422 14.905 -6.983  1.00 33.07  ?  338 HIS B CB  1 
ATOM   5325 C  CG  . HIS B 1 338 ? -30.537 15.896 -7.087  1.00 33.82  ?  338 HIS B CG  1 
ATOM   5326 N  ND1 . HIS B 1 338 ? -31.858 15.502 -7.285  1.00 32.00  ?  338 HIS B ND1 1 
ATOM   5327 C  CD2 . HIS B 1 338 ? -30.545 17.250 -7.041  1.00 33.85  ?  338 HIS B CD2 1 
ATOM   5328 C  CE1 . HIS B 1 338 ? -32.627 16.576 -7.335  1.00 33.15  ?  338 HIS B CE1 1 
ATOM   5329 N  NE2 . HIS B 1 338 ? -31.854 17.661 -7.217  1.00 32.48  ?  338 HIS B NE2 1 
ATOM   5330 N  N   . PRO B 1 339 ? -27.956 14.982 -3.488  1.00 26.33  ?  339 PRO B N   1 
ATOM   5331 C  CA  . PRO B 1 339 ? -27.414 15.973 -2.560  1.00 27.78  ?  339 PRO B CA  1 
ATOM   5332 C  C   . PRO B 1 339 ? -26.089 16.598 -3.028  1.00 26.18  ?  339 PRO B C   1 
ATOM   5333 O  O   . PRO B 1 339 ? -25.794 17.717 -2.615  1.00 27.26  ?  339 PRO B O   1 
ATOM   5334 C  CB  . PRO B 1 339 ? -27.263 15.133 -1.287  1.00 27.89  ?  339 PRO B CB  1 
ATOM   5335 C  CG  . PRO B 1 339 ? -27.029 13.715 -1.821  1.00 26.00  ?  339 PRO B CG  1 
ATOM   5336 C  CD  . PRO B 1 339 ? -28.044 13.632 -2.936  1.00 24.91  ?  339 PRO B CD  1 
ATOM   5337 N  N   . GLU B 1 340 ? -25.324 15.881 -3.859  1.00 27.66  ?  340 GLU B N   1 
ATOM   5338 C  CA  . GLU B 1 340 ? -23.957 16.263 -4.368  1.00 28.61  ?  340 GLU B CA  1 
ATOM   5339 C  C   . GLU B 1 340 ? -24.045 17.368 -5.445  1.00 30.81  ?  340 GLU B C   1 
ATOM   5340 O  O   . GLU B 1 340 ? -23.023 17.979 -5.765  1.00 25.55  ?  340 GLU B O   1 
ATOM   5341 C  CB  . GLU B 1 340 ? -23.221 15.036 -4.922  1.00 27.90  ?  340 GLU B CB  1 
ATOM   5342 C  CG  . GLU B 1 340 ? -23.705 14.517 -6.271  1.00 24.96  ?  340 GLU B CG  1 
ATOM   5343 C  CD  . GLU B 1 340 ? -25.056 13.803 -6.300  1.00 28.58  ?  340 GLU B CD  1 
ATOM   5344 O  OE1 . GLU B 1 340 ? -25.705 13.553 -5.199  1.00 28.71  ?  340 GLU B OE1 1 
ATOM   5345 O  OE2 . GLU B 1 340 ? -25.499 13.497 -7.441  1.00 30.88  ?  340 GLU B OE2 1 
ATOM   5346 N  N   . ARG B 1 341 ? -25.250 17.653 -5.950  1.00 32.82  ?  341 ARG B N   1 
ATOM   5347 C  CA  . ARG B 1 341 ? -25.473 18.615 -7.061  1.00 30.79  ?  341 ARG B CA  1 
ATOM   5348 C  C   . ARG B 1 341 ? -26.169 19.866 -6.520  1.00 28.65  ?  341 ARG B C   1 
ATOM   5349 O  O   . ARG B 1 341 ? -27.197 19.727 -5.897  1.00 26.78  ?  341 ARG B O   1 
ATOM   5350 C  CB  . ARG B 1 341 ? -26.287 17.925 -8.158  1.00 31.03  ?  341 ARG B CB  1 
ATOM   5351 C  CG  . ARG B 1 341 ? -25.783 16.546 -8.565  1.00 29.28  ?  341 ARG B CG  1 
ATOM   5352 C  CD  . ARG B 1 341 ? -26.499 16.018 -9.790  1.00 31.74  ?  341 ARG B CD  1 
ATOM   5353 N  NE  . ARG B 1 341 ? -26.450 17.027 -10.842 1.00 33.89  ?  341 ARG B NE  1 
ATOM   5354 C  CZ  . ARG B 1 341 ? -25.467 17.176 -11.728 1.00 32.35  ?  341 ARG B CZ  1 
ATOM   5355 N  NH1 . ARG B 1 341 ? -24.451 16.338 -11.769 1.00 33.79  ?  341 ARG B NH1 1 
ATOM   5356 N  NH2 . ARG B 1 341 ? -25.494 18.177 -12.583 1.00 34.34  ?  341 ARG B NH2 1 
ATOM   5357 N  N   . ILE B 1 342 ? -25.570 21.040 -6.703  1.00 30.56  ?  342 ILE B N   1 
ATOM   5358 C  CA  . ILE B 1 342 ? -26.208 22.346 -6.395  1.00 29.65  ?  342 ILE B CA  1 
ATOM   5359 C  C   . ILE B 1 342 ? -27.479 22.486 -7.240  1.00 30.08  ?  342 ILE B C   1 
ATOM   5360 O  O   . ILE B 1 342 ? -27.390 22.308 -8.458  1.00 31.15  ?  342 ILE B O   1 
ATOM   5361 C  CB  . ILE B 1 342 ? -25.247 23.500 -6.674  1.00 30.36  ?  342 ILE B CB  1 
ATOM   5362 C  CG1 . ILE B 1 342 ? -24.011 23.433 -5.780  1.00 30.00  ?  342 ILE B CG1 1 
ATOM   5363 C  CG2 . ILE B 1 342 ? -25.954 24.842 -6.546  1.00 29.32  ?  342 ILE B CG2 1 
ATOM   5364 C  CD1 . ILE B 1 342 ? -23.015 24.546 -6.098  1.00 28.76  ?  342 ILE B CD1 1 
ATOM   5365 N  N   . ASP B 1 343 ? -28.590 22.856 -6.592  1.00 29.46  ?  343 ASP B N   1 
ATOM   5366 C  CA  . ASP B 1 343 ? -29.959 22.948 -7.167  1.00 28.64  ?  343 ASP B CA  1 
ATOM   5367 C  C   . ASP B 1 343 ? -30.725 24.102 -6.486  1.00 26.97  ?  343 ASP B C   1 
ATOM   5368 O  O   . ASP B 1 343 ? -31.060 24.052 -5.279  1.00 29.00  ?  343 ASP B O   1 
ATOM   5369 C  CB  . ASP B 1 343 ? -30.637 21.587 -7.048  1.00 29.41  ?  343 ASP B CB  1 
ATOM   5370 C  CG  . ASP B 1 343 ? -32.084 21.573 -7.464  1.00 30.90  ?  343 ASP B CG  1 
ATOM   5371 O  OD1 . ASP B 1 343 ? -32.630 22.670 -7.663  1.00 30.98  ?  343 ASP B OD1 1 
ATOM   5372 O  OD2 . ASP B 1 343 ? -32.641 20.452 -7.584  1.00 33.77  ?  343 ASP B OD2 1 
ATOM   5373 N  N   . PHE B 1 344 ? -30.984 25.149 -7.247  1.00 27.18  ?  344 PHE B N   1 
ATOM   5374 C  CA  . PHE B 1 344 ? -31.598 26.405 -6.762  1.00 27.62  ?  344 PHE B CA  1 
ATOM   5375 C  C   . PHE B 1 344 ? -33.126 26.293 -6.821  1.00 28.07  ?  344 PHE B C   1 
ATOM   5376 O  O   . PHE B 1 344 ? -33.804 27.309 -6.546  1.00 28.48  ?  344 PHE B O   1 
ATOM   5377 C  CB  . PHE B 1 344 ? -31.108 27.568 -7.626  1.00 26.37  ?  344 PHE B CB  1 
ATOM   5378 C  CG  . PHE B 1 344 ? -29.707 28.036 -7.351  1.00 27.51  ?  344 PHE B CG  1 
ATOM   5379 C  CD1 . PHE B 1 344 ? -28.882 27.368 -6.465  1.00 26.46  ?  344 PHE B CD1 1 
ATOM   5380 C  CD2 . PHE B 1 344 ? -29.192 29.131 -8.037  1.00 31.56  ?  344 PHE B CD2 1 
ATOM   5381 C  CE1 . PHE B 1 344 ? -27.592 27.807 -6.253  1.00 25.01  ?  344 PHE B CE1 1 
ATOM   5382 C  CE2 . PHE B 1 344 ? -27.891 29.562 -7.836  1.00 28.18  ?  344 PHE B CE2 1 
ATOM   5383 C  CZ  . PHE B 1 344 ? -27.100 28.894 -6.942  1.00 28.41  ?  344 PHE B CZ  1 
ATOM   5384 N  N   . ASP B 1 345 ? -33.657 25.120 -7.161  1.00 29.06  ?  345 ASP B N   1 
ATOM   5385 C  CA  . ASP B 1 345 ? -35.112 24.939 -7.400  1.00 32.71  ?  345 ASP B CA  1 
ATOM   5386 C  C   . ASP B 1 345 ? -35.622 23.771 -6.545  1.00 32.98  ?  345 ASP B C   1 
ATOM   5387 O  O   . ASP B 1 345 ? -36.622 23.142 -6.931  1.00 35.28  ?  345 ASP B O   1 
ATOM   5388 C  CB  . ASP B 1 345 ? -35.370 24.831 -8.909  1.00 33.86  ?  345 ASP B CB  1 
ATOM   5389 C  CG  . ASP B 1 345 ? -34.909 26.077 -9.665  1.00 37.50  ?  345 ASP B CG  1 
ATOM   5390 O  OD1 . ASP B 1 345 ? -35.612 27.108 -9.589  1.00 35.61  ?  345 ASP B OD1 1 
ATOM   5391 O  OD2 . ASP B 1 345 ? -33.828 26.029 -10.298 1.00 38.02  ?  345 ASP B OD2 1 
ATOM   5392 N  N   . ARG B 1 346 ? -35.000 23.514 -5.393  1.00 35.98  ?  346 ARG B N   1 
ATOM   5393 C  CA  . ARG B 1 346 ? -35.488 22.480 -4.435  1.00 34.28  ?  346 ARG B CA  1 
ATOM   5394 C  C   . ARG B 1 346 ? -36.829 22.976 -3.861  1.00 37.08  ?  346 ARG B C   1 
ATOM   5395 O  O   . ARG B 1 346 ? -36.896 24.151 -3.434  1.00 38.84  ?  346 ARG B O   1 
ATOM   5396 C  CB  . ARG B 1 346 ? -34.443 22.193 -3.348  1.00 33.42  ?  346 ARG B CB  1 
ATOM   5397 C  CG  . ARG B 1 346 ? -33.083 21.702 -3.855  1.00 34.13  ?  346 ARG B CG  1 
ATOM   5398 C  CD  . ARG B 1 346 ? -32.083 21.415 -2.720  1.00 32.83  ?  346 ARG B CD  1 
ATOM   5399 N  NE  . ARG B 1 346 ? -30.882 20.757 -3.191  1.00 31.04  ?  346 ARG B NE  1 
ATOM   5400 C  CZ  . ARG B 1 346 ? -30.810 19.475 -3.571  1.00 36.26  ?  346 ARG B CZ  1 
ATOM   5401 N  NH1 . ARG B 1 346 ? -31.866 18.676 -3.464  1.00 31.54  ?  346 ARG B NH1 1 
ATOM   5402 N  NH2 . ARG B 1 346 ? -29.669 18.990 -4.047  1.00 36.19  ?  346 ARG B NH2 1 
ATOM   5403 N  N   . GLU B 1 347 ? -37.872 22.143 -3.918  1.00 41.60  ?  347 GLU B N   1 
ATOM   5404 C  CA  . GLU B 1 347 ? -39.203 22.425 -3.327  1.00 44.39  ?  347 GLU B CA  1 
ATOM   5405 C  C   . GLU B 1 347 ? -39.014 22.724 -1.851  1.00 43.93  ?  347 GLU B C   1 
ATOM   5406 O  O   . GLU B 1 347 ? -39.630 23.676 -1.388  1.00 44.48  ?  347 GLU B O   1 
ATOM   5407 C  CB  . GLU B 1 347 ? -40.152 21.235 -3.481  1.00 51.73  ?  347 GLU B CB  1 
ATOM   5408 C  CG  . GLU B 1 347 ? -40.924 21.282 -4.786  1.00 57.86  ?  347 GLU B CG  1 
ATOM   5409 C  CD  . GLU B 1 347 ? -41.839 20.101 -5.055  1.00 69.06  ?  347 GLU B CD  1 
ATOM   5410 O  OE1 . GLU B 1 347 ? -41.964 19.223 -4.159  1.00 71.56  ?  347 GLU B OE1 1 
ATOM   5411 O  OE2 . GLU B 1 347 ? -42.416 20.060 -6.172  1.00 78.91  ?  347 GLU B OE2 1 
ATOM   5412 N  N   . SER B 1 348 ? -38.168 21.926 -1.189  1.00 45.31  ?  348 SER B N   1 
ATOM   5413 C  CA  . SER B 1 348 ? -37.858 21.961 0.265   1.00 43.50  ?  348 SER B CA  1 
ATOM   5414 C  C   . SER B 1 348 ? -36.337 21.994 0.515   1.00 40.80  ?  348 SER B C   1 
ATOM   5415 O  O   . SER B 1 348 ? -35.609 21.298 -0.224  1.00 38.46  ?  348 SER B O   1 
ATOM   5416 C  CB  . SER B 1 348 ? -38.456 20.736 0.918   1.00 44.88  ?  348 SER B CB  1 
ATOM   5417 O  OG  . SER B 1 348 ? -37.831 19.573 0.400   1.00 49.56  ?  348 SER B OG  1 
ATOM   5418 N  N   . ASN B 1 349 ? -35.879 22.662 1.585   1.00 34.67  ?  349 ASN B N   1 
ATOM   5419 C  CA  . ASN B 1 349 ? -34.439 22.685 1.961   1.00 34.88  ?  349 ASN B CA  1 
ATOM   5420 C  C   . ASN B 1 349 ? -34.203 22.828 3.478   1.00 33.52  ?  349 ASN B C   1 
ATOM   5421 O  O   . ASN B 1 349 ? -33.647 23.827 3.963   1.00 29.65  ?  349 ASN B O   1 
ATOM   5422 C  CB  . ASN B 1 349 ? -33.712 23.768 1.175   1.00 37.07  ?  349 ASN B CB  1 
ATOM   5423 C  CG  . ASN B 1 349 ? -32.245 23.447 1.073   1.00 42.34  ?  349 ASN B CG  1 
ATOM   5424 O  OD1 . ASN B 1 349 ? -31.799 22.419 1.621   1.00 37.43  ?  349 ASN B OD1 1 
ATOM   5425 N  ND2 . ASN B 1 349 ? -31.521 24.315 0.375   1.00 43.70  ?  349 ASN B ND2 1 
ATOM   5426 N  N   . PRO B 1 350 ? -34.540 21.779 4.263   1.00 28.45  ?  350 PRO B N   1 
ATOM   5427 C  CA  . PRO B 1 350 ? -34.480 21.834 5.718   1.00 27.97  ?  350 PRO B CA  1 
ATOM   5428 C  C   . PRO B 1 350 ? -33.049 21.556 6.218   1.00 28.15  ?  350 PRO B C   1 
ATOM   5429 O  O   . PRO B 1 350 ? -32.827 20.674 7.042   1.00 27.35  ?  350 PRO B O   1 
ATOM   5430 C  CB  . PRO B 1 350 ? -35.478 20.704 6.072   1.00 27.77  ?  350 PRO B CB  1 
ATOM   5431 C  CG  . PRO B 1 350 ? -35.162 19.618 5.033   1.00 26.93  ?  350 PRO B CG  1 
ATOM   5432 C  CD  . PRO B 1 350 ? -34.983 20.448 3.777   1.00 29.19  ?  350 PRO B CD  1 
ATOM   5433 N  N   . HIS B 1 351 ? -32.090 22.333 5.735   1.00 28.29  ?  351 HIS B N   1 
ATOM   5434 C  CA  . HIS B 1 351 ? -30.652 22.074 5.985   1.00 27.54  ?  351 HIS B CA  1 
ATOM   5435 C  C   . HIS B 1 351 ? -30.247 22.509 7.395   1.00 29.16  ?  351 HIS B C   1 
ATOM   5436 O  O   . HIS B 1 351 ? -30.968 23.327 8.006   1.00 33.45  ?  351 HIS B O   1 
ATOM   5437 C  CB  . HIS B 1 351 ? -29.838 22.773 4.910   1.00 29.89  ?  351 HIS B CB  1 
ATOM   5438 C  CG  . HIS B 1 351 ? -29.881 24.262 5.000   1.00 27.33  ?  351 HIS B CG  1 
ATOM   5439 N  ND1 . HIS B 1 351 ? -29.286 24.952 6.032   1.00 27.61  ?  351 HIS B ND1 1 
ATOM   5440 C  CD2 . HIS B 1 351 ? -30.384 25.177 4.158   1.00 26.85  ?  351 HIS B CD2 1 
ATOM   5441 C  CE1 . HIS B 1 351 ? -29.435 26.243 5.826   1.00 29.33  ?  351 HIS B CE1 1 
ATOM   5442 N  NE2 . HIS B 1 351 ? -30.132 26.402 4.693   1.00 28.76  ?  351 HIS B NE2 1 
ATOM   5443 N  N   . LEU B 1 352 ? -29.104 22.002 7.853   1.00 28.48  ?  352 LEU B N   1 
ATOM   5444 C  CA  . LEU B 1 352 ? -28.496 22.265 9.183   1.00 27.33  ?  352 LEU B CA  1 
ATOM   5445 C  C   . LEU B 1 352 ? -27.313 23.277 9.139   1.00 24.84  ?  352 LEU B C   1 
ATOM   5446 O  O   . LEU B 1 352 ? -26.645 23.437 10.170  1.00 21.94  ?  352 LEU B O   1 
ATOM   5447 C  CB  . LEU B 1 352 ? -28.075 20.896 9.731   1.00 27.05  ?  352 LEU B CB  1 
ATOM   5448 C  CG  . LEU B 1 352 ? -29.163 19.803 9.753   1.00 30.43  ?  352 LEU B CG  1 
ATOM   5449 C  CD1 . LEU B 1 352 ? -28.784 18.657 10.682  1.00 27.34  ?  352 LEU B CD1 1 
ATOM   5450 C  CD2 . LEU B 1 352 ? -30.542 20.329 10.171  1.00 28.87  ?  352 LEU B CD2 1 
ATOM   5451 N  N   . ALA B 1 353 ? -27.082 24.019 8.056   1.00 22.61  ?  353 ALA B N   1 
ATOM   5452 C  CA  . ALA B 1 353 ? -25.913 24.925 7.931   1.00 25.14  ?  353 ALA B CA  1 
ATOM   5453 C  C   . ALA B 1 353 ? -25.809 25.934 9.085   1.00 26.91  ?  353 ALA B C   1 
ATOM   5454 O  O   . ALA B 1 353 ? -24.708 26.449 9.320   1.00 30.13  ?  353 ALA B O   1 
ATOM   5455 C  CB  . ALA B 1 353 ? -25.987 25.678 6.649   1.00 27.67  ?  353 ALA B CB  1 
ATOM   5456 N  N   . PHE B 1 354 ? -26.925 26.244 9.730   1.00 27.55  ?  354 PHE B N   1 
ATOM   5457 C  CA  . PHE B 1 354 ? -27.066 27.197 10.856  1.00 27.87  ?  354 PHE B CA  1 
ATOM   5458 C  C   . PHE B 1 354 ? -27.281 26.411 12.152  1.00 30.70  ?  354 PHE B C   1 
ATOM   5459 O  O   . PHE B 1 354 ? -27.599 27.028 13.198  1.00 31.48  ?  354 PHE B O   1 
ATOM   5460 C  CB  . PHE B 1 354 ? -28.240 28.142 10.569  1.00 27.32  ?  354 PHE B CB  1 
ATOM   5461 C  CG  . PHE B 1 354 ? -27.931 29.260 9.603   1.00 26.35  ?  354 PHE B CG  1 
ATOM   5462 C  CD1 . PHE B 1 354 ? -26.753 29.978 9.696   1.00 27.32  ?  354 PHE B CD1 1 
ATOM   5463 C  CD2 . PHE B 1 354 ? -28.818 29.600 8.606   1.00 27.16  ?  354 PHE B CD2 1 
ATOM   5464 C  CE1 . PHE B 1 354 ? -26.480 31.028 8.831   1.00 31.05  ?  354 PHE B CE1 1 
ATOM   5465 C  CE2 . PHE B 1 354 ? -28.535 30.628 7.717   1.00 30.35  ?  354 PHE B CE2 1 
ATOM   5466 C  CZ  . PHE B 1 354 ? -27.382 31.367 7.849   1.00 30.53  ?  354 PHE B CZ  1 
ATOM   5467 N  N   . GLY B 1 355 ? -27.118 25.082 12.086  1.00 29.41  ?  355 GLY B N   1 
ATOM   5468 C  CA  . GLY B 1 355 ? -27.346 24.184 13.225  1.00 29.44  ?  355 GLY B CA  1 
ATOM   5469 C  C   . GLY B 1 355 ? -28.827 23.934 13.409  1.00 30.18  ?  355 GLY B C   1 
ATOM   5470 O  O   . GLY B 1 355 ? -29.576 23.922 12.396  1.00 29.87  ?  355 GLY B O   1 
ATOM   5471 N  N   . GLY B 1 356 ? -29.240 23.741 14.648  1.00 28.24  ?  356 GLY B N   1 
ATOM   5472 C  CA  . GLY B 1 356 ? -30.624 23.356 14.956  1.00 32.25  ?  356 GLY B CA  1 
ATOM   5473 C  C   . GLY B 1 356 ? -30.906 23.412 16.445  1.00 30.77  ?  356 GLY B C   1 
ATOM   5474 O  O   . GLY B 1 356 ? -29.940 23.704 17.219  1.00 35.61  ?  356 GLY B O   1 
ATOM   5475 N  N   . GLY B 1 357 ? -32.173 23.228 16.831  1.00 28.91  ?  357 GLY B N   1 
ATOM   5476 C  CA  . GLY B 1 357 ? -32.611 23.315 18.244  1.00 31.97  ?  357 GLY B CA  1 
ATOM   5477 C  C   . GLY B 1 357 ? -32.185 24.623 18.896  1.00 30.89  ?  357 GLY B C   1 
ATOM   5478 O  O   . GLY B 1 357 ? -32.115 25.648 18.172  1.00 32.49  ?  357 GLY B O   1 
ATOM   5479 N  N   . GLN B 1 358 ? -31.846 24.596 20.185  1.00 32.22  ?  358 GLN B N   1 
ATOM   5480 C  CA  . GLN B 1 358 ? -31.754 25.831 21.017  1.00 37.33  ?  358 GLN B CA  1 
ATOM   5481 C  C   . GLN B 1 358 ? -30.536 26.667 20.581  1.00 35.68  ?  358 GLN B C   1 
ATOM   5482 O  O   . GLN B 1 358 ? -30.599 27.869 20.767  1.00 32.73  ?  358 GLN B O   1 
ATOM   5483 C  CB  . GLN B 1 358 ? -31.780 25.513 22.525  1.00 40.88  ?  358 GLN B CB  1 
ATOM   5484 C  CG  . GLN B 1 358 ? -33.103 24.950 23.027  1.00 49.51  ?  358 GLN B CG  1 
ATOM   5485 C  CD  . GLN B 1 358 ? -33.113 24.569 24.494  1.00 55.56  ?  358 GLN B CD  1 
ATOM   5486 O  OE1 . GLN B 1 358 ? -32.077 24.273 25.093  1.00 66.06  ?  358 GLN B OE1 1 
ATOM   5487 N  NE2 . GLN B 1 358 ? -34.288 24.614 25.105  1.00 52.69  ?  358 GLN B NE2 1 
ATOM   5488 N  N   . HIS B 1 359 ? -29.481 26.093 19.993  1.00 35.56  ?  359 HIS B N   1 
ATOM   5489 C  CA  . HIS B 1 359 ? -28.269 26.874 19.605  1.00 35.47  ?  359 HIS B CA  1 
ATOM   5490 C  C   . HIS B 1 359 ? -28.285 27.223 18.111  1.00 35.80  ?  359 HIS B C   1 
ATOM   5491 O  O   . HIS B 1 359 ? -27.199 27.490 17.553  1.00 36.98  ?  359 HIS B O   1 
ATOM   5492 C  CB  . HIS B 1 359 ? -26.995 26.127 20.008  1.00 34.35  ?  359 HIS B CB  1 
ATOM   5493 C  CG  . HIS B 1 359 ? -26.887 25.962 21.482  1.00 34.48  ?  359 HIS B CG  1 
ATOM   5494 N  ND1 . HIS B 1 359 ? -26.620 27.028 22.319  1.00 31.86  ?  359 HIS B ND1 1 
ATOM   5495 C  CD2 . HIS B 1 359 ? -27.040 24.870 22.265  1.00 32.81  ?  359 HIS B CD2 1 
ATOM   5496 C  CE1 . HIS B 1 359 ? -26.603 26.596 23.556  1.00 32.61  ?  359 HIS B CE1 1 
ATOM   5497 N  NE2 . HIS B 1 359 ? -26.876 25.273 23.549  1.00 32.55  ?  359 HIS B NE2 1 
ATOM   5498 N  N   . PHE B 1 360 ? -29.451 27.177 17.470  1.00 31.98  ?  360 PHE B N   1 
ATOM   5499 C  CA  . PHE B 1 360 ? -29.632 27.605 16.062  1.00 31.03  ?  360 PHE B CA  1 
ATOM   5500 C  C   . PHE B 1 360 ? -29.060 29.018 15.944  1.00 29.20  ?  360 PHE B C   1 
ATOM   5501 O  O   . PHE B 1 360 ? -29.300 29.855 16.818  1.00 31.58  ?  360 PHE B O   1 
ATOM   5502 C  CB  . PHE B 1 360 ? -31.104 27.533 15.627  1.00 30.18  ?  360 PHE B CB  1 
ATOM   5503 C  CG  . PHE B 1 360 ? -31.370 28.024 14.221  1.00 30.99  ?  360 PHE B CG  1 
ATOM   5504 C  CD1 . PHE B 1 360 ? -31.629 29.376 13.971  1.00 29.99  ?  360 PHE B CD1 1 
ATOM   5505 C  CD2 . PHE B 1 360 ? -31.368 27.138 13.144  1.00 28.96  ?  360 PHE B CD2 1 
ATOM   5506 C  CE1 . PHE B 1 360 ? -31.892 29.825 12.679  1.00 28.50  ?  360 PHE B CE1 1 
ATOM   5507 C  CE2 . PHE B 1 360 ? -31.632 27.586 11.853  1.00 29.80  ?  360 PHE B CE2 1 
ATOM   5508 C  CZ  . PHE B 1 360 ? -31.885 28.933 11.620  1.00 28.28  ?  360 PHE B CZ  1 
ATOM   5509 N  N   . CYS B 1 361 ? -28.288 29.283 14.897  1.00 30.63  ?  361 CYS B N   1 
ATOM   5510 C  CA  . CYS B 1 361 ? -27.529 30.557 14.783  1.00 32.16  ?  361 CYS B CA  1 
ATOM   5511 C  C   . CYS B 1 361 ? -28.527 31.709 14.955  1.00 29.99  ?  361 CYS B C   1 
ATOM   5512 O  O   . CYS B 1 361 ? -29.553 31.761 14.284  1.00 28.84  ?  361 CYS B O   1 
ATOM   5513 C  CB  . CYS B 1 361 ? -26.750 30.624 13.472  1.00 31.75  ?  361 CYS B CB  1 
ATOM   5514 S  SG  . CYS B 1 361 ? -25.971 32.228 13.169  1.00 27.99  ?  361 CYS B SG  1 
ATOM   5515 N  N   . PRO B 1 362 ? -28.290 32.633 15.903  1.00 26.92  ?  362 PRO B N   1 
ATOM   5516 C  CA  . PRO B 1 362 ? -29.197 33.754 16.121  1.00 29.73  ?  362 PRO B CA  1 
ATOM   5517 C  C   . PRO B 1 362 ? -29.026 34.888 15.088  1.00 29.55  ?  362 PRO B C   1 
ATOM   5518 O  O   . PRO B 1 362 ? -29.736 35.844 15.124  1.00 33.71  ?  362 PRO B O   1 
ATOM   5519 C  CB  . PRO B 1 362 ? -28.807 34.191 17.553  1.00 29.75  ?  362 PRO B CB  1 
ATOM   5520 C  CG  . PRO B 1 362 ? -27.329 33.885 17.664  1.00 29.98  ?  362 PRO B CG  1 
ATOM   5521 C  CD  . PRO B 1 362 ? -27.141 32.640 16.820  1.00 30.48  ?  362 PRO B CD  1 
ATOM   5522 N  N   . ALA B 1 363 ? -28.066 34.741 14.189  1.00 27.77  ?  363 ALA B N   1 
ATOM   5523 C  CA  . ALA B 1 363 ? -27.661 35.736 13.189  1.00 27.44  ?  363 ALA B CA  1 
ATOM   5524 C  C   . ALA B 1 363 ? -27.960 35.211 11.790  1.00 26.91  ?  363 ALA B C   1 
ATOM   5525 O  O   . ALA B 1 363 ? -27.390 35.760 10.847  1.00 27.82  ?  363 ALA B O   1 
ATOM   5526 C  CB  . ALA B 1 363 ? -26.196 36.000 13.354  1.00 29.88  ?  363 ALA B CB  1 
ATOM   5527 N  N   . SER B 1 364 ? -28.812 34.191 11.664  1.00 27.02  ?  364 SER B N   1 
ATOM   5528 C  CA  . SER B 1 364 ? -29.103 33.508 10.378  1.00 27.83  ?  364 SER B CA  1 
ATOM   5529 C  C   . SER B 1 364 ? -29.539 34.567 9.379   1.00 29.34  ?  364 SER B C   1 
ATOM   5530 O  O   . SER B 1 364 ? -28.956 34.582 8.310   1.00 38.15  ?  364 SER B O   1 
ATOM   5531 C  CB  . SER B 1 364 ? -30.134 32.391 10.487  1.00 28.35  ?  364 SER B CB  1 
ATOM   5532 O  OG  . SER B 1 364 ? -31.450 32.882 10.776  1.00 25.47  ?  364 SER B OG  1 
ATOM   5533 N  N   . ALA B 1 365 ? -30.535 35.395 9.692   1.00 27.95  ?  365 ALA B N   1 
ATOM   5534 C  CA  . ALA B 1 365 ? -31.032 36.428 8.746   1.00 27.55  ?  365 ALA B CA  1 
ATOM   5535 C  C   . ALA B 1 365 ? -29.874 37.302 8.241   1.00 26.14  ?  365 ALA B C   1 
ATOM   5536 O  O   . ALA B 1 365 ? -29.855 37.655 7.052   1.00 28.14  ?  365 ALA B O   1 
ATOM   5537 C  CB  . ALA B 1 365 ? -32.089 37.289 9.397   1.00 27.63  ?  365 ALA B CB  1 
ATOM   5538 N  N   . LEU B 1 366 ? -28.949 37.657 9.123   1.00 26.78  ?  366 LEU B N   1 
ATOM   5539 C  CA  . LEU B 1 366 ? -27.803 38.559 8.841   1.00 28.15  ?  366 LEU B CA  1 
ATOM   5540 C  C   . LEU B 1 366 ? -26.766 37.859 7.966   1.00 28.69  ?  366 LEU B C   1 
ATOM   5541 O  O   . LEU B 1 366 ? -26.126 38.557 7.112   1.00 31.05  ?  366 LEU B O   1 
ATOM   5542 C  CB  . LEU B 1 366 ? -27.189 38.943 10.184  1.00 32.78  ?  366 LEU B CB  1 
ATOM   5543 C  CG  . LEU B 1 366 ? -26.242 40.126 10.166  1.00 37.26  ?  366 LEU B CG  1 
ATOM   5544 C  CD1 . LEU B 1 366 ? -26.934 41.348 9.596   1.00 48.43  ?  366 LEU B CD1 1 
ATOM   5545 C  CD2 . LEU B 1 366 ? -25.783 40.410 11.570  1.00 40.97  ?  366 LEU B CD2 1 
ATOM   5546 N  N   . GLY B 1 367 ? -26.569 36.559 8.217   1.00 26.10  ?  367 GLY B N   1 
ATOM   5547 C  CA  . GLY B 1 367 ? -25.697 35.674 7.421   1.00 29.73  ?  367 GLY B CA  1 
ATOM   5548 C  C   . GLY B 1 367 ? -26.160 35.659 5.987   1.00 30.91  ?  367 GLY B C   1 
ATOM   5549 O  O   . GLY B 1 367 ? -25.320 35.922 5.101   1.00 34.02  ?  367 GLY B O   1 
ATOM   5550 N  N   . ARG B 1 368 ? -27.469 35.449 5.795   1.00 30.12  ?  368 ARG B N   1 
ATOM   5551 C  CA  . ARG B 1 368 ? -28.159 35.433 4.479   1.00 32.44  ?  368 ARG B CA  1 
ATOM   5552 C  C   . ARG B 1 368 ? -27.959 36.772 3.762   1.00 35.39  ?  368 ARG B C   1 
ATOM   5553 O  O   . ARG B 1 368 ? -27.446 36.777 2.627   1.00 35.58  ?  368 ARG B O   1 
ATOM   5554 C  CB  . ARG B 1 368 ? -29.654 35.183 4.673   1.00 33.56  ?  368 ARG B CB  1 
ATOM   5555 C  CG  . ARG B 1 368 ? -29.991 33.765 5.104   1.00 34.48  ?  368 ARG B CG  1 
ATOM   5556 C  CD  . ARG B 1 368 ? -31.489 33.527 5.160   1.00 31.47  ?  368 ARG B CD  1 
ATOM   5557 N  NE  . ARG B 1 368 ? -31.714 32.264 5.834   1.00 29.93  ?  368 ARG B NE  1 
ATOM   5558 C  CZ  . ARG B 1 368 ? -31.600 31.078 5.243   1.00 28.85  ?  368 ARG B CZ  1 
ATOM   5559 N  NH1 . ARG B 1 368 ? -31.270 30.982 3.968   1.00 25.54  ?  368 ARG B NH1 1 
ATOM   5560 N  NH2 . ARG B 1 368 ? -31.820 29.986 5.941   1.00 29.74  ?  368 ARG B NH2 1 
ATOM   5561 N  N   . THR B 1 369 ? -28.382 37.860 4.407   1.00 35.85  ?  369 THR B N   1 
ATOM   5562 C  CA  . THR B 1 369 ? -28.285 39.241 3.883   1.00 35.56  ?  369 THR B CA  1 
ATOM   5563 C  C   . THR B 1 369 ? -26.837 39.494 3.442   1.00 32.58  ?  369 THR B C   1 
ATOM   5564 O  O   . THR B 1 369 ? -26.633 39.920 2.321   1.00 30.23  ?  369 THR B O   1 
ATOM   5565 C  CB  . THR B 1 369 ? -28.752 40.250 4.938   1.00 35.71  ?  369 THR B CB  1 
ATOM   5566 O  OG1 . THR B 1 369 ? -30.060 39.914 5.412   1.00 35.50  ?  369 THR B OG1 1 
ATOM   5567 C  CG2 . THR B 1 369 ? -28.754 41.650 4.380   1.00 34.54  ?  369 THR B CG2 1 
ATOM   5568 N  N   . HIS B 1 370 ? -25.869 39.211 4.302   1.00 31.88  ?  370 HIS B N   1 
ATOM   5569 C  CA  . HIS B 1 370 ? -24.426 39.347 3.988   1.00 34.08  ?  370 HIS B CA  1 
ATOM   5570 C  C   . HIS B 1 370 ? -24.154 38.675 2.636   1.00 31.68  ?  370 HIS B C   1 
ATOM   5571 O  O   . HIS B 1 370 ? -23.560 39.332 1.760   1.00 30.62  ?  370 HIS B O   1 
ATOM   5572 C  CB  . HIS B 1 370 ? -23.578 38.775 5.153   1.00 35.37  ?  370 HIS B CB  1 
ATOM   5573 C  CG  . HIS B 1 370 ? -22.112 38.641 4.880   1.00 36.38  ?  370 HIS B CG  1 
ATOM   5574 N  ND1 . HIS B 1 370 ? -21.581 37.545 4.206   1.00 37.08  ?  370 HIS B ND1 1 
ATOM   5575 C  CD2 . HIS B 1 370 ? -21.055 39.420 5.230   1.00 38.07  ?  370 HIS B CD2 1 
ATOM   5576 C  CE1 . HIS B 1 370 ? -20.262 37.674 4.137   1.00 38.49  ?  370 HIS B CE1 1 
ATOM   5577 N  NE2 . HIS B 1 370 ? -19.910 38.808 4.775   1.00 37.48  ?  370 HIS B NE2 1 
ATOM   5578 N  N   . ALA B 1 371 ? -24.530 37.399 2.492   1.00 31.04  ?  371 ALA B N   1 
ATOM   5579 C  CA  . ALA B 1 371 ? -24.124 36.528 1.359   1.00 28.90  ?  371 ALA B CA  1 
ATOM   5580 C  C   . ALA B 1 371 ? -24.905 36.938 0.119   1.00 26.97  ?  371 ALA B C   1 
ATOM   5581 O  O   . ALA B 1 371 ? -24.291 37.132 -0.952  1.00 25.45  ?  371 ALA B O   1 
ATOM   5582 C  CB  . ALA B 1 371 ? -24.356 35.067 1.680   1.00 28.58  ?  371 ALA B CB  1 
ATOM   5583 N  N   . GLU B 1 372 ? -26.221 37.061 0.266   1.00 28.61  ?  372 GLU B N   1 
ATOM   5584 C  CA  . GLU B 1 372 ? -27.106 37.527 -0.821  1.00 32.03  ?  372 GLU B CA  1 
ATOM   5585 C  C   . GLU B 1 372 ? -26.498 38.802 -1.460  1.00 32.40  ?  372 GLU B C   1 
ATOM   5586 O  O   . GLU B 1 372 ? -26.399 38.865 -2.722  1.00 29.16  ?  372 GLU B O   1 
ATOM   5587 C  CB  . GLU B 1 372 ? -28.504 37.741 -0.251  1.00 34.77  ?  372 GLU B CB  1 
ATOM   5588 C  CG  . GLU B 1 372 ? -29.198 36.446 0.127   1.00 38.55  ?  372 GLU B CG  1 
ATOM   5589 C  CD  . GLU B 1 372 ? -30.565 36.681 0.750   1.00 39.61  ?  372 GLU B CD  1 
ATOM   5590 O  OE1 . GLU B 1 372 ? -31.034 37.810 0.603   1.00 40.34  ?  372 GLU B OE1 1 
ATOM   5591 O  OE2 . GLU B 1 372 ? -31.137 35.751 1.391   1.00 34.87  ?  372 GLU B OE2 1 
ATOM   5592 N  N   . ILE B 1 373 ? -26.066 39.784 -0.662  1.00 28.81  ?  373 ILE B N   1 
ATOM   5593 C  CA  . ILE B 1 373 ? -25.666 41.101 -1.238  1.00 31.18  ?  373 ILE B CA  1 
ATOM   5594 C  C   . ILE B 1 373 ? -24.296 40.953 -1.919  1.00 31.13  ?  373 ILE B C   1 
ATOM   5595 O  O   . ILE B 1 373 ? -24.121 41.470 -3.070  1.00 29.78  ?  373 ILE B O   1 
ATOM   5596 C  CB  . ILE B 1 373 ? -25.749 42.258 -0.220  1.00 29.28  ?  373 ILE B CB  1 
ATOM   5597 C  CG1 . ILE B 1 373 ? -27.214 42.587 0.079   1.00 35.45  ?  373 ILE B CG1 1 
ATOM   5598 C  CG2 . ILE B 1 373 ? -25.051 43.478 -0.770  1.00 29.29  ?  373 ILE B CG2 1 
ATOM   5599 C  CD1 . ILE B 1 373 ? -27.445 43.391 1.353   1.00 38.94  ?  373 ILE B CD1 1 
ATOM   5600 N  N   . ALA B 1 374 ? -23.360 40.261 -1.274  1.00 29.66  ?  374 ALA B N   1 
ATOM   5601 C  CA  . ALA B 1 374 ? -21.997 40.074 -1.804  1.00 26.98  ?  374 ALA B CA  1 
ATOM   5602 C  C   . ALA B 1 374 ? -22.099 39.296 -3.112  1.00 25.92  ?  374 ALA B C   1 
ATOM   5603 O  O   . ALA B 1 374 ? -21.408 39.667 -4.065  1.00 26.29  ?  374 ALA B O   1 
ATOM   5604 C  CB  . ALA B 1 374 ? -21.146 39.369 -0.788  1.00 30.10  ?  374 ALA B CB  1 
ATOM   5605 N  N   . LEU B 1 375 ? -22.976 38.299 -3.172  1.00 25.58  ?  375 LEU B N   1 
ATOM   5606 C  CA  . LEU B 1 375 ? -23.070 37.382 -4.346  1.00 27.35  ?  375 LEU B CA  1 
ATOM   5607 C  C   . LEU B 1 375 ? -23.771 38.069 -5.500  1.00 27.70  ?  375 LEU B C   1 
ATOM   5608 O  O   . LEU B 1 375 ? -23.304 37.913 -6.646  1.00 29.36  ?  375 LEU B O   1 
ATOM   5609 C  CB  . LEU B 1 375 ? -23.782 36.091 -3.948  1.00 26.37  ?  375 LEU B CB  1 
ATOM   5610 C  CG  . LEU B 1 375 ? -22.934 35.239 -3.007  1.00 26.68  ?  375 LEU B CG  1 
ATOM   5611 C  CD1 . LEU B 1 375 ? -23.715 34.039 -2.520  1.00 29.94  ?  375 LEU B CD1 1 
ATOM   5612 C  CD2 . LEU B 1 375 ? -21.627 34.833 -3.672  1.00 26.83  ?  375 LEU B CD2 1 
ATOM   5613 N  N   . THR B 1 376 ? -24.832 38.816 -5.206  1.00 29.59  ?  376 THR B N   1 
ATOM   5614 C  CA  . THR B 1 376 ? -25.498 39.701 -6.193  1.00 28.16  ?  376 THR B CA  1 
ATOM   5615 C  C   . THR B 1 376 ? -24.481 40.666 -6.814  1.00 26.59  ?  376 THR B C   1 
ATOM   5616 O  O   . THR B 1 376 ? -24.473 40.817 -8.039  1.00 30.22  ?  376 THR B O   1 
ATOM   5617 C  CB  . THR B 1 376 ? -26.657 40.460 -5.557  1.00 28.91  ?  376 THR B CB  1 
ATOM   5618 O  OG1 . THR B 1 376 ? -27.589 39.458 -5.138  1.00 31.45  ?  376 THR B OG1 1 
ATOM   5619 C  CG2 . THR B 1 376 ? -27.295 41.435 -6.516  1.00 27.36  ?  376 THR B CG2 1 
ATOM   5620 N  N   . ALA B 1 377 ? -23.671 41.323 -6.008  1.00 26.27  ?  377 ALA B N   1 
ATOM   5621 C  CA  . ALA B 1 377 ? -22.719 42.332 -6.499  1.00 27.64  ?  377 ALA B CA  1 
ATOM   5622 C  C   . ALA B 1 377 ? -21.681 41.641 -7.369  1.00 28.65  ?  377 ALA B C   1 
ATOM   5623 O  O   . ALA B 1 377 ? -21.307 42.191 -8.427  1.00 31.62  ?  377 ALA B O   1 
ATOM   5624 C  CB  . ALA B 1 377 ? -22.078 43.043 -5.347  1.00 30.36  ?  377 ALA B CB  1 
ATOM   5625 N  N   . LEU B 1 378 ? -21.236 40.463 -6.954  1.00 30.25  ?  378 LEU B N   1 
ATOM   5626 C  CA  . LEU B 1 378 ? -20.110 39.756 -7.614  1.00 29.60  ?  378 LEU B CA  1 
ATOM   5627 C  C   . LEU B 1 378 ? -20.523 39.316 -9.017  1.00 30.06  ?  378 LEU B C   1 
ATOM   5628 O  O   . LEU B 1 378 ? -19.725 39.507 -9.922  1.00 33.86  ?  378 LEU B O   1 
ATOM   5629 C  CB  . LEU B 1 378 ? -19.711 38.556 -6.757  1.00 33.35  ?  378 LEU B CB  1 
ATOM   5630 C  CG  . LEU B 1 378 ? -18.645 37.649 -7.361  1.00 32.93  ?  378 LEU B CG  1 
ATOM   5631 C  CD1 . LEU B 1 378 ? -17.260 38.207 -7.081  1.00 33.66  ?  378 LEU B CD1 1 
ATOM   5632 C  CD2 . LEU B 1 378 ? -18.795 36.257 -6.799  1.00 31.69  ?  378 LEU B CD2 1 
ATOM   5633 N  N   . VAL B 1 379 ? -21.731 38.787 -9.216  1.00 28.49  ?  379 VAL B N   1 
ATOM   5634 C  CA  . VAL B 1 379 ? -22.130 38.252 -10.550 1.00 30.17  ?  379 VAL B CA  1 
ATOM   5635 C  C   . VAL B 1 379 ? -22.442 39.412 -11.487 1.00 30.53  ?  379 VAL B C   1 
ATOM   5636 O  O   . VAL B 1 379 ? -22.281 39.235 -12.727 1.00 32.65  ?  379 VAL B O   1 
ATOM   5637 C  CB  . VAL B 1 379 ? -23.293 37.249 -10.484 1.00 32.05  ?  379 VAL B CB  1 
ATOM   5638 C  CG1 . VAL B 1 379 ? -22.882 35.999 -9.710  1.00 29.80  ?  379 VAL B CG1 1 
ATOM   5639 C  CG2 . VAL B 1 379 ? -24.566 37.875 -9.896  1.00 32.48  ?  379 VAL B CG2 1 
ATOM   5640 N  N   . GLU B 1 380 ? -22.844 40.555 -10.943 1.00 32.70  ?  380 GLU B N   1 
ATOM   5641 C  CA  . GLU B 1 380 ? -23.018 41.788 -11.758 1.00 36.37  ?  380 GLU B CA  1 
ATOM   5642 C  C   . GLU B 1 380 ? -21.664 42.403 -12.099 1.00 33.76  ?  380 GLU B C   1 
ATOM   5643 O  O   . GLU B 1 380 ? -21.512 42.843 -13.218 1.00 32.74  ?  380 GLU B O   1 
ATOM   5644 C  CB  . GLU B 1 380 ? -23.882 42.806 -11.045 1.00 42.82  ?  380 GLU B CB  1 
ATOM   5645 C  CG  . GLU B 1 380 ? -25.302 42.319 -10.901 1.00 54.35  ?  380 GLU B CG  1 
ATOM   5646 C  CD  . GLU B 1 380 ? -26.072 43.224 -9.972  1.00 59.29  ?  380 GLU B CD  1 
ATOM   5647 O  OE1 . GLU B 1 380 ? -27.246 42.902 -9.657  1.00 67.45  ?  380 GLU B OE1 1 
ATOM   5648 O  OE2 . GLU B 1 380 ? -25.472 44.251 -9.580  1.00 50.73  ?  380 GLU B OE2 1 
ATOM   5649 N  N   . LYS B 1 381 ? -20.708 42.422 -11.184 1.00 34.14  ?  381 LYS B N   1 
ATOM   5650 C  CA  . LYS B 1 381 ? -19.417 43.111 -11.441 1.00 38.30  ?  381 LYS B CA  1 
ATOM   5651 C  C   . LYS B 1 381 ? -18.421 42.188 -12.179 1.00 34.96  ?  381 LYS B C   1 
ATOM   5652 O  O   . LYS B 1 381 ? -17.599 42.727 -12.920 1.00 34.55  ?  381 LYS B O   1 
ATOM   5653 C  CB  . LYS B 1 381 ? -18.933 43.703 -10.118 1.00 38.84  ?  381 LYS B CB  1 
ATOM   5654 C  CG  . LYS B 1 381 ? -19.902 44.728 -9.534  1.00 44.46  ?  381 LYS B CG  1 
ATOM   5655 C  CD  . LYS B 1 381 ? -20.043 45.957 -10.439 1.00 54.78  ?  381 LYS B CD  1 
ATOM   5656 C  CE  . LYS B 1 381 ? -20.931 47.056 -9.901  1.00 53.19  ?  381 LYS B CE  1 
ATOM   5657 N  NZ  . LYS B 1 381 ? -21.015 48.178 -10.862 1.00 60.44  ?  381 LYS B NZ  1 
ATOM   5658 N  N   . LEU B 1 382 ? -18.482 40.860 -12.035 1.00 32.91  ?  382 LEU B N   1 
ATOM   5659 C  CA  . LEU B 1 382 ? -17.484 39.938 -12.663 1.00 31.07  ?  382 LEU B CA  1 
ATOM   5660 C  C   . LEU B 1 382 ? -18.217 38.826 -13.385 1.00 31.13  ?  382 LEU B C   1 
ATOM   5661 O  O   . LEU B 1 382 ? -18.210 37.672 -12.961 1.00 30.25  ?  382 LEU B O   1 
ATOM   5662 C  CB  . LEU B 1 382 ? -16.568 39.310 -11.609 1.00 30.61  ?  382 LEU B CB  1 
ATOM   5663 C  CG  . LEU B 1 382 ? -15.886 40.252 -10.632 1.00 31.14  ?  382 LEU B CG  1 
ATOM   5664 C  CD1 . LEU B 1 382 ? -15.026 39.457 -9.675  1.00 32.60  ?  382 LEU B CD1 1 
ATOM   5665 C  CD2 . LEU B 1 382 ? -15.058 41.280 -11.374 1.00 33.07  ?  382 LEU B CD2 1 
ATOM   5666 N  N   . PRO B 1 383 ? -18.941 39.134 -14.473 1.00 36.18  ?  383 PRO B N   1 
ATOM   5667 C  CA  . PRO B 1 383 ? -19.752 38.111 -15.117 1.00 32.39  ?  383 PRO B CA  1 
ATOM   5668 C  C   . PRO B 1 383 ? -18.911 36.966 -15.707 1.00 30.56  ?  383 PRO B C   1 
ATOM   5669 O  O   . PRO B 1 383 ? -19.524 35.938 -15.903 1.00 31.30  ?  383 PRO B O   1 
ATOM   5670 C  CB  . PRO B 1 383 ? -20.578 38.909 -16.136 1.00 32.69  ?  383 PRO B CB  1 
ATOM   5671 C  CG  . PRO B 1 383 ? -19.793 40.168 -16.380 1.00 31.14  ?  383 PRO B CG  1 
ATOM   5672 C  CD  . PRO B 1 383 ? -19.153 40.471 -15.046 1.00 33.07  ?  383 PRO B CD  1 
ATOM   5673 N  N   . ALA B 1 384 ? -17.585 37.113 -15.918 1.00 27.38  ?  384 ALA B N   1 
ATOM   5674 C  CA  . ALA B 1 384 ? -16.716 36.017 -16.439 1.00 28.11  ?  384 ALA B CA  1 
ATOM   5675 C  C   . ALA B 1 384 ? -15.849 35.411 -15.313 1.00 31.20  ?  384 ALA B C   1 
ATOM   5676 O  O   . ALA B 1 384 ? -14.787 34.760 -15.601 1.00 29.61  ?  384 ALA B O   1 
ATOM   5677 C  CB  . ALA B 1 384 ? -15.877 36.484 -17.601 1.00 25.83  ?  384 ALA B CB  1 
ATOM   5678 N  N   . LEU B 1 385 ? -16.316 35.559 -14.071 1.00 30.03  ?  385 LEU B N   1 
ATOM   5679 C  CA  . LEU B 1 385 ? -15.687 34.979 -12.861 1.00 29.01  ?  385 LEU B CA  1 
ATOM   5680 C  C   . LEU B 1 385 ? -15.355 33.501 -13.076 1.00 28.39  ?  385 LEU B C   1 
ATOM   5681 O  O   . LEU B 1 385 ? -16.286 32.707 -13.378 1.00 27.91  ?  385 LEU B O   1 
ATOM   5682 C  CB  . LEU B 1 385 ? -16.643 35.126 -11.681 1.00 30.03  ?  385 LEU B CB  1 
ATOM   5683 C  CG  . LEU B 1 385 ? -16.173 34.412 -10.417 1.00 33.08  ?  385 LEU B CG  1 
ATOM   5684 C  CD1 . LEU B 1 385 ? -14.934 35.090 -9.819  1.00 33.62  ?  385 LEU B CD1 1 
ATOM   5685 C  CD2 . LEU B 1 385 ? -17.287 34.361 -9.405  1.00 34.70  ?  385 LEU B CD2 1 
ATOM   5686 N  N   . ARG B 1 386 ? -14.088 33.144 -12.863 1.00 27.85  ?  386 ARG B N   1 
ATOM   5687 C  CA  . ARG B 1 386 ? -13.598 31.736 -12.850 1.00 28.36  ?  386 ARG B CA  1 
ATOM   5688 C  C   . ARG B 1 386 ? -12.327 31.626 -12.002 1.00 29.81  ?  386 ARG B C   1 
ATOM   5689 O  O   . ARG B 1 386 ? -11.609 32.622 -11.840 1.00 31.40  ?  386 ARG B O   1 
ATOM   5690 C  CB  . ARG B 1 386 ? -13.273 31.264 -14.265 1.00 27.22  ?  386 ARG B CB  1 
ATOM   5691 C  CG  . ARG B 1 386 ? -12.376 32.212 -15.040 1.00 28.89  ?  386 ARG B CG  1 
ATOM   5692 C  CD  . ARG B 1 386 ? -12.376 31.898 -16.529 1.00 28.64  ?  386 ARG B CD  1 
ATOM   5693 N  NE  . ARG B 1 386 ? -11.387 32.652 -17.282 1.00 28.28  ?  386 ARG B NE  1 
ATOM   5694 C  CZ  . ARG B 1 386 ? -11.516 33.924 -17.668 1.00 29.70  ?  386 ARG B CZ  1 
ATOM   5695 N  NH1 . ARG B 1 386 ? -12.577 34.643 -17.338 1.00 32.15  ?  386 ARG B NH1 1 
ATOM   5696 N  NH2 . ARG B 1 386 ? -10.553 34.500 -18.363 1.00 28.85  ?  386 ARG B NH2 1 
ATOM   5697 N  N   . LEU B 1 387 ? -12.039 30.442 -11.483 1.00 30.95  ?  387 LEU B N   1 
ATOM   5698 C  CA  . LEU B 1 387 ? -10.752 30.186 -10.785 1.00 31.87  ?  387 LEU B CA  1 
ATOM   5699 C  C   . LEU B 1 387 ? -9.596  30.457 -11.746 1.00 29.89  ?  387 LEU B C   1 
ATOM   5700 O  O   . LEU B 1 387 ? -9.726  30.147 -12.919 1.00 31.23  ?  387 LEU B O   1 
ATOM   5701 C  CB  . LEU B 1 387 ? -10.730 28.747 -10.277 1.00 30.44  ?  387 LEU B CB  1 
ATOM   5702 C  CG  . LEU B 1 387 ? -11.712 28.457 -9.148  1.00 31.64  ?  387 LEU B CG  1 
ATOM   5703 C  CD1 . LEU B 1 387 ? -11.379 27.123 -8.479  1.00 33.17  ?  387 LEU B CD1 1 
ATOM   5704 C  CD2 . LEU B 1 387 ? -11.704 29.580 -8.120  1.00 31.35  ?  387 LEU B CD2 1 
ATOM   5705 N  N   . ALA B 1 388 ? -8.510  31.045 -11.258 1.00 29.15  ?  388 ALA B N   1 
ATOM   5706 C  CA  . ALA B 1 388 ? -7.316  31.329 -12.076 1.00 28.35  ?  388 ALA B CA  1 
ATOM   5707 C  C   . ALA B 1 388 ? -6.552  30.038 -12.370 1.00 27.44  ?  388 ALA B C   1 
ATOM   5708 O  O   . ALA B 1 388 ? -5.639  30.078 -13.220 1.00 28.81  ?  388 ALA B O   1 
ATOM   5709 C  CB  . ALA B 1 388 ? -6.441  32.342 -11.389 1.00 28.29  ?  388 ALA B CB  1 
ATOM   5710 N  N   . LEU B 1 389 ? -6.872  28.959 -11.669 1.00 25.69  ?  389 LEU B N   1 
ATOM   5711 C  CA  . LEU B 1 389 ? -6.133  27.677 -11.777 1.00 29.20  ?  389 LEU B CA  1 
ATOM   5712 C  C   . LEU B 1 389 ? -7.083  26.557 -11.377 1.00 29.86  ?  389 LEU B C   1 
ATOM   5713 O  O   . LEU B 1 389 ? -8.145  26.828 -10.812 1.00 27.83  ?  389 LEU B O   1 
ATOM   5714 C  CB  . LEU B 1 389 ? -4.872  27.733 -10.895 1.00 28.41  ?  389 LEU B CB  1 
ATOM   5715 C  CG  . LEU B 1 389 ? -4.000  26.479 -10.808 1.00 33.75  ?  389 LEU B CG  1 
ATOM   5716 C  CD1 . LEU B 1 389 ? -3.423  26.142 -12.188 1.00 35.91  ?  389 LEU B CD1 1 
ATOM   5717 C  CD2 . LEU B 1 389 ? -2.868  26.608 -9.770  1.00 34.64  ?  389 LEU B CD2 1 
ATOM   5718 N  N   . PRO B 1 390 ? -6.732  25.283 -11.635 1.00 31.37  ?  390 PRO B N   1 
ATOM   5719 C  CA  . PRO B 1 390 ? -7.613  24.169 -11.293 1.00 33.90  ?  390 PRO B CA  1 
ATOM   5720 C  C   . PRO B 1 390 ? -7.903  24.227 -9.786  1.00 33.41  ?  390 PRO B C   1 
ATOM   5721 O  O   . PRO B 1 390 ? -6.998  24.628 -9.031  1.00 32.82  ?  390 PRO B O   1 
ATOM   5722 C  CB  . PRO B 1 390 ? -6.825  22.904 -11.695 1.00 34.36  ?  390 PRO B CB  1 
ATOM   5723 C  CG  . PRO B 1 390 ? -5.796  23.407 -12.694 1.00 36.13  ?  390 PRO B CG  1 
ATOM   5724 C  CD  . PRO B 1 390 ? -5.476  24.829 -12.251 1.00 36.43  ?  390 PRO B CD  1 
ATOM   5725 N  N   . VAL B 1 391 ? -9.131  23.855 -9.410  1.00 29.50  ?  391 VAL B N   1 
ATOM   5726 C  CA  . VAL B 1 391 ? -9.672  23.856 -8.012  1.00 29.89  ?  391 VAL B CA  1 
ATOM   5727 C  C   . VAL B 1 391 ? -8.861  22.896 -7.131  1.00 28.39  ?  391 VAL B C   1 
ATOM   5728 O  O   . VAL B 1 391 ? -8.739  23.180 -5.947  1.00 30.90  ?  391 VAL B O   1 
ATOM   5729 C  CB  . VAL B 1 391 ? -11.192 23.529 -7.982  1.00 30.06  ?  391 VAL B CB  1 
ATOM   5730 C  CG1 . VAL B 1 391 ? -11.497 22.077 -8.378  1.00 31.82  ?  391 VAL B CG1 1 
ATOM   5731 C  CG2 . VAL B 1 391 ? -11.834 23.857 -6.636  1.00 26.02  ?  391 VAL B CG2 1 
ATOM   5732 N  N   . GLU B 1 392 ? -8.328  21.809 -7.690  1.00 32.51  ?  392 GLU B N   1 
ATOM   5733 C  CA  . GLU B 1 392 ? -7.481  20.789 -6.994  1.00 31.36  ?  392 GLU B CA  1 
ATOM   5734 C  C   . GLU B 1 392 ? -6.234  21.447 -6.380  1.00 30.39  ?  392 GLU B C   1 
ATOM   5735 O  O   . GLU B 1 392 ? -5.717  20.906 -5.378  1.00 29.66  ?  392 GLU B O   1 
ATOM   5736 C  CB  . GLU B 1 392 ? -7.053  19.676 -7.958  1.00 31.25  ?  392 GLU B CB  1 
ATOM   5737 C  CG  . GLU B 1 392 ? -8.222  18.864 -8.504  1.00 36.90  ?  392 GLU B CG  1 
ATOM   5738 C  CD  . GLU B 1 392 ? -9.008  19.408 -9.703  1.00 41.51  ?  392 GLU B CD  1 
ATOM   5739 O  OE1 . GLU B 1 392 ? -8.509  20.316 -10.418 1.00 35.03  ?  392 GLU B OE1 1 
ATOM   5740 O  OE2 . GLU B 1 392 ? -10.140 18.898 -9.924  1.00 45.23  ?  392 GLU B OE2 1 
ATOM   5741 N  N   . GLN B 1 393 ? -5.790  22.589 -6.909  1.00 28.82  ?  393 GLN B N   1 
ATOM   5742 C  CA  . GLN B 1 393 ? -4.496  23.226 -6.539  1.00 28.74  ?  393 GLN B CA  1 
ATOM   5743 C  C   . GLN B 1 393 ? -4.677  24.388 -5.561  1.00 28.59  ?  393 GLN B C   1 
ATOM   5744 O  O   . GLN B 1 393 ? -3.674  24.887 -5.080  1.00 31.66  ?  393 GLN B O   1 
ATOM   5745 C  CB  . GLN B 1 393 ? -3.773  23.632 -7.817  1.00 30.59  ?  393 GLN B CB  1 
ATOM   5746 C  CG  . GLN B 1 393 ? -3.338  22.385 -8.590  1.00 37.35  ?  393 GLN B CG  1 
ATOM   5747 C  CD  . GLN B 1 393 ? -2.839  22.670 -9.985  1.00 41.31  ?  393 GLN B CD  1 
ATOM   5748 O  OE1 . GLN B 1 393 ? -3.417  22.198 -10.971 1.00 41.51  ?  393 GLN B OE1 1 
ATOM   5749 N  NE2 . GLN B 1 393 ? -1.772  23.461 -10.062 1.00 40.15  ?  393 GLN B NE2 1 
ATOM   5750 N  N   . LEU B 1 394 ? -5.899  24.774 -5.211  1.00 30.95  ?  394 LEU B N   1 
ATOM   5751 C  CA  . LEU B 1 394 ? -6.146  25.672 -4.053  1.00 29.03  ?  394 LEU B CA  1 
ATOM   5752 C  C   . LEU B 1 394 ? -5.432  25.104 -2.812  1.00 30.06  ?  394 LEU B C   1 
ATOM   5753 O  O   . LEU B 1 394 ? -5.431  23.853 -2.602  1.00 31.28  ?  394 LEU B O   1 
ATOM   5754 C  CB  . LEU B 1 394 ? -7.647  25.808 -3.798  1.00 28.23  ?  394 LEU B CB  1 
ATOM   5755 C  CG  . LEU B 1 394 ? -8.458  26.511 -4.882  1.00 28.77  ?  394 LEU B CG  1 
ATOM   5756 C  CD1 . LEU B 1 394 ? -9.930  26.620 -4.468  1.00 29.78  ?  394 LEU B CD1 1 
ATOM   5757 C  CD2 . LEU B 1 394 ? -7.889  27.891 -5.157  1.00 29.30  ?  394 LEU B CD2 1 
ATOM   5758 N  N   . ALA B 1 395 ? -4.822  25.996 -2.026  1.00 27.04  ?  395 ALA B N   1 
ATOM   5759 C  CA  . ALA B 1 395 ? -4.314  25.703 -0.678  1.00 27.25  ?  395 ALA B CA  1 
ATOM   5760 C  C   . ALA B 1 395 ? -5.458  25.836 0.339   1.00 29.00  ?  395 ALA B C   1 
ATOM   5761 O  O   . ALA B 1 395 ? -5.979  26.953 0.560   1.00 29.59  ?  395 ALA B O   1 
ATOM   5762 C  CB  . ALA B 1 395 ? -3.169  26.608 -0.374  1.00 29.21  ?  395 ALA B CB  1 
ATOM   5763 N  N   . TRP B 1 396 ? -5.867  24.700 0.895   1.00 27.92  ?  396 TRP B N   1 
ATOM   5764 C  CA  . TRP B 1 396 ? -6.831  24.604 2.006   1.00 26.81  ?  396 TRP B CA  1 
ATOM   5765 C  C   . TRP B 1 396 ? -6.087  24.775 3.321   1.00 25.50  ?  396 TRP B C   1 
ATOM   5766 O  O   . TRP B 1 396 ? -5.086  24.079 3.536   1.00 22.76  ?  396 TRP B O   1 
ATOM   5767 C  CB  . TRP B 1 396 ? -7.593  23.291 1.882   1.00 28.68  ?  396 TRP B CB  1 
ATOM   5768 C  CG  . TRP B 1 396 ? -8.465  23.337 0.664   1.00 31.35  ?  396 TRP B CG  1 
ATOM   5769 C  CD1 . TRP B 1 396 ? -8.240  22.781 -0.567  1.00 29.43  ?  396 TRP B CD1 1 
ATOM   5770 C  CD2 . TRP B 1 396 ? -9.708  24.054 0.563   1.00 30.45  ?  396 TRP B CD2 1 
ATOM   5771 N  NE1 . TRP B 1 396 ? -9.295  23.043 -1.401  1.00 30.84  ?  396 TRP B NE1 1 
ATOM   5772 C  CE2 . TRP B 1 396 ? -10.194 23.847 -0.746  1.00 30.30  ?  396 TRP B CE2 1 
ATOM   5773 C  CE3 . TRP B 1 396 ? -10.458 24.811 1.462   1.00 27.17  ?  396 TRP B CE3 1 
ATOM   5774 C  CZ2 . TRP B 1 396 ? -11.393 24.401 -1.181  1.00 30.27  ?  396 TRP B CZ2 1 
ATOM   5775 C  CZ3 . TRP B 1 396 ? -11.656 25.335 1.035   1.00 28.79  ?  396 TRP B CZ3 1 
ATOM   5776 C  CH2 . TRP B 1 396 ? -12.110 25.140 -0.268  1.00 30.23  ?  396 TRP B CH2 1 
ATOM   5777 N  N   . ARG B 1 397 ? -6.558  25.735 4.118   1.00 28.73  ?  397 ARG B N   1 
ATOM   5778 C  CA  . ARG B 1 397 ? -6.057  26.052 5.481   1.00 30.04  ?  397 ARG B CA  1 
ATOM   5779 C  C   . ARG B 1 397 ? -6.225  24.831 6.390   1.00 31.67  ?  397 ARG B C   1 
ATOM   5780 O  O   . ARG B 1 397 ? -7.303  24.213 6.428   1.00 31.09  ?  397 ARG B O   1 
ATOM   5781 C  CB  . ARG B 1 397 ? -6.751  27.287 6.065   1.00 27.73  ?  397 ARG B CB  1 
ATOM   5782 C  CG  . ARG B 1 397 ? -6.077  27.749 7.344   1.00 27.74  ?  397 ARG B CG  1 
ATOM   5783 C  CD  . ARG B 1 397 ? -6.650  28.977 7.996   1.00 26.64  ?  397 ARG B CD  1 
ATOM   5784 N  NE  . ARG B 1 397 ? -6.252  30.164 7.295   1.00 27.10  ?  397 ARG B NE  1 
ATOM   5785 C  CZ  . ARG B 1 397 ? -6.503  31.388 7.724   1.00 28.83  ?  397 ARG B CZ  1 
ATOM   5786 N  NH1 . ARG B 1 397 ? -7.151  31.574 8.861   1.00 33.20  ?  397 ARG B NH1 1 
ATOM   5787 N  NH2 . ARG B 1 397 ? -6.129  32.428 7.017   1.00 27.31  ?  397 ARG B NH2 1 
ATOM   5788 N  N   . PRO B 1 398 ? -5.111  24.385 7.037   1.00 31.70  ?  398 PRO B N   1 
ATOM   5789 C  CA  . PRO B 1 398 ? -5.169  23.360 8.083   1.00 28.42  ?  398 PRO B CA  1 
ATOM   5790 C  C   . PRO B 1 398 ? -5.381  23.947 9.480   1.00 27.11  ?  398 PRO B C   1 
ATOM   5791 O  O   . PRO B 1 398 ? -5.146  25.146 9.660   1.00 27.50  ?  398 PRO B O   1 
ATOM   5792 C  CB  . PRO B 1 398 ? -3.771  22.696 8.003   1.00 26.66  ?  398 PRO B CB  1 
ATOM   5793 C  CG  . PRO B 1 398 ? -2.859  23.833 7.572   1.00 27.13  ?  398 PRO B CG  1 
ATOM   5794 C  CD  . PRO B 1 398 ? -3.708  24.744 6.694   1.00 28.15  ?  398 PRO B CD  1 
ATOM   5795 N  N   . GLY B 1 399 ? -5.721  23.087 10.446  1.00 26.10  ?  399 GLY B N   1 
ATOM   5796 C  CA  . GLY B 1 399 ? -5.660  23.433 11.884  1.00 25.39  ?  399 GLY B CA  1 
ATOM   5797 C  C   . GLY B 1 399 ? -6.555  24.626 12.182  1.00 27.75  ?  399 GLY B C   1 
ATOM   5798 O  O   . GLY B 1 399 ? -6.258  25.381 13.145  1.00 28.84  ?  399 GLY B O   1 
ATOM   5799 N  N   . PHE B 1 400 ? -7.646  24.779 11.420  1.00 24.39  ?  400 PHE B N   1 
ATOM   5800 C  CA  . PHE B 1 400 ? -8.618  25.879 11.627  1.00 25.82  ?  400 PHE B CA  1 
ATOM   5801 C  C   . PHE B 1 400 ? -10.039 25.326 11.768  1.00 23.53  ?  400 PHE B C   1 
ATOM   5802 O  O   . PHE B 1 400 ? -10.314 24.231 11.249  1.00 19.85  ?  400 PHE B O   1 
ATOM   5803 C  CB  . PHE B 1 400 ? -8.482  26.872 10.477  1.00 26.03  ?  400 PHE B CB  1 
ATOM   5804 C  CG  . PHE B 1 400 ? -8.872  28.281 10.816  1.00 25.52  ?  400 PHE B CG  1 
ATOM   5805 C  CD1 . PHE B 1 400 ? -8.112  29.030 11.695  1.00 27.24  ?  400 PHE B CD1 1 
ATOM   5806 C  CD2 . PHE B 1 400 ? -9.978  28.868 10.223  1.00 26.63  ?  400 PHE B CD2 1 
ATOM   5807 C  CE1 . PHE B 1 400 ? -8.472  30.343 11.979  1.00 29.99  ?  400 PHE B CE1 1 
ATOM   5808 C  CE2 . PHE B 1 400 ? -10.329 30.178 10.499  1.00 27.86  ?  400 PHE B CE2 1 
ATOM   5809 C  CZ  . PHE B 1 400 ? -9.581  30.914 11.384  1.00 27.98  ?  400 PHE B CZ  1 
ATOM   5810 N  N   . ILE B 1 401 ? -10.877 26.063 12.497  1.00 24.95  ?  401 ILE B N   1 
ATOM   5811 C  CA  . ILE B 1 401 ? -12.320 25.739 12.754  1.00 29.09  ?  401 ILE B CA  1 
ATOM   5812 C  C   . ILE B 1 401 ? -13.108 25.763 11.437  1.00 26.78  ?  401 ILE B C   1 
ATOM   5813 O  O   . ILE B 1 401 ? -13.948 24.902 11.232  1.00 23.13  ?  401 ILE B O   1 
ATOM   5814 C  CB  . ILE B 1 401 ? -12.880 26.671 13.846  1.00 35.09  ?  401 ILE B CB  1 
ATOM   5815 C  CG1 . ILE B 1 401 ? -12.186 26.379 15.179  1.00 41.07  ?  401 ILE B CG1 1 
ATOM   5816 C  CG2 . ILE B 1 401 ? -14.367 26.540 13.990  1.00 38.65  ?  401 ILE B CG2 1 
ATOM   5817 C  CD1 . ILE B 1 401 ? -12.444 27.385 16.278  1.00 43.31  ?  401 ILE B CD1 1 
ATOM   5818 N  N   . LYS B 1 402 ? -12.721 26.629 10.505  1.00 31.14  ?  402 LYS B N   1 
ATOM   5819 C  CA  . LYS B 1 402 ? -13.286 26.715 9.132   1.00 29.21  ?  402 LYS B CA  1 
ATOM   5820 C  C   . LYS B 1 402 ? -12.354 26.044 8.112   1.00 30.35  ?  402 LYS B C   1 
ATOM   5821 O  O   . LYS B 1 402 ? -11.123 26.238 8.199   1.00 30.88  ?  402 LYS B O   1 
ATOM   5822 C  CB  . LYS B 1 402 ? -13.472 28.180 8.744   1.00 28.70  ?  402 LYS B CB  1 
ATOM   5823 C  CG  . LYS B 1 402 ? -14.339 28.996 9.688   1.00 31.01  ?  402 LYS B CG  1 
ATOM   5824 C  CD  . LYS B 1 402 ? -15.753 28.444 9.857   1.00 33.35  ?  402 LYS B CD  1 
ATOM   5825 C  CE  . LYS B 1 402 ? -16.578 29.277 10.821  1.00 36.77  ?  402 LYS B CE  1 
ATOM   5826 N  NZ  . LYS B 1 402 ? -17.932 28.721 11.058  1.00 35.40  ?  402 LYS B NZ  1 
ATOM   5827 N  N   . ARG B 1 403 ? -12.922 25.295 7.165   1.00 27.80  ?  403 ARG B N   1 
ATOM   5828 C  CA  . ARG B 1 403 ? -12.269 25.068 5.855   1.00 28.61  ?  403 ARG B CA  1 
ATOM   5829 C  C   . ARG B 1 403 ? -12.299 26.374 5.067   1.00 27.98  ?  403 ARG B C   1 
ATOM   5830 O  O   . ARG B 1 403 ? -13.357 27.024 5.007   1.00 30.04  ?  403 ARG B O   1 
ATOM   5831 C  CB  . ARG B 1 403 ? -12.992 24.004 5.039   1.00 27.08  ?  403 ARG B CB  1 
ATOM   5832 C  CG  . ARG B 1 403 ? -12.940 22.617 5.640   1.00 24.73  ?  403 ARG B CG  1 
ATOM   5833 C  CD  . ARG B 1 403 ? -13.434 21.659 4.593   1.00 26.99  ?  403 ARG B CD  1 
ATOM   5834 N  NE  . ARG B 1 403 ? -13.417 20.307 5.104   1.00 28.84  ?  403 ARG B NE  1 
ATOM   5835 C  CZ  . ARG B 1 403 ? -14.437 19.691 5.655   1.00 29.85  ?  403 ARG B CZ  1 
ATOM   5836 N  NH1 . ARG B 1 403 ? -15.603 20.300 5.752   1.00 32.39  ?  403 ARG B NH1 1 
ATOM   5837 N  NH2 . ARG B 1 403 ? -14.288 18.453 6.082   1.00 31.34  ?  403 ARG B NH2 1 
ATOM   5838 N  N   . LEU B 1 404 ? -11.189 26.745 4.470   1.00 29.12  ?  404 LEU B N   1 
ATOM   5839 C  CA  . LEU B 1 404 ? -11.152 27.889 3.525   1.00 30.80  ?  404 LEU B CA  1 
ATOM   5840 C  C   . LEU B 1 404 ? -9.865  27.851 2.722   1.00 30.82  ?  404 LEU B C   1 
ATOM   5841 O  O   . LEU B 1 404 ? -8.861  27.305 3.170   1.00 25.50  ?  404 LEU B O   1 
ATOM   5842 C  CB  . LEU B 1 404 ? -11.291 29.209 4.286   1.00 34.49  ?  404 LEU B CB  1 
ATOM   5843 C  CG  . LEU B 1 404 ? -12.605 29.473 5.010   1.00 33.40  ?  404 LEU B CG  1 
ATOM   5844 C  CD1 . LEU B 1 404 ? -12.537 30.744 5.832   1.00 38.19  ?  404 LEU B CD1 1 
ATOM   5845 C  CD2 . LEU B 1 404 ? -13.732 29.604 4.020   1.00 33.57  ?  404 LEU B CD2 1 
ATOM   5846 N  N   . PRO B 1 405 ? -9.910  28.390 1.486   1.00 35.12  ?  405 PRO B N   1 
ATOM   5847 C  CA  . PRO B 1 405 ? -8.714  28.577 0.668   1.00 33.76  ?  405 PRO B CA  1 
ATOM   5848 C  C   . PRO B 1 405 ? -7.862  29.713 1.256   1.00 31.57  ?  405 PRO B C   1 
ATOM   5849 O  O   . PRO B 1 405 ? -8.434  30.718 1.566   1.00 30.49  ?  405 PRO B O   1 
ATOM   5850 C  CB  . PRO B 1 405 ? -9.282  28.941 -0.708  1.00 35.48  ?  405 PRO B CB  1 
ATOM   5851 C  CG  . PRO B 1 405 ? -10.612 29.579 -0.420  1.00 37.90  ?  405 PRO B CG  1 
ATOM   5852 C  CD  . PRO B 1 405 ? -11.127 28.906 0.841   1.00 37.49  ?  405 PRO B CD  1 
ATOM   5853 N  N   . GLU B 1 406 ? -6.558  29.506 1.452   1.00 28.76  ?  406 GLU B N   1 
ATOM   5854 C  CA  . GLU B 1 406 ? -5.633  30.540 1.998   1.00 30.27  ?  406 GLU B CA  1 
ATOM   5855 C  C   . GLU B 1 406 ? -5.647  31.750 1.051   1.00 29.91  ?  406 GLU B C   1 
ATOM   5856 O  O   . GLU B 1 406 ? -5.549  32.890 1.534   1.00 28.59  ?  406 GLU B O   1 
ATOM   5857 C  CB  . GLU B 1 406 ? -4.197  30.026 2.140   1.00 31.02  ?  406 GLU B CB  1 
ATOM   5858 C  CG  . GLU B 1 406 ? -4.051  28.733 2.938   1.00 33.21  ?  406 GLU B CG  1 
ATOM   5859 C  CD  . GLU B 1 406 ? -3.936  28.920 4.439   1.00 34.21  ?  406 GLU B CD  1 
ATOM   5860 O  OE1 . GLU B 1 406 ? -4.384  29.997 4.901   1.00 33.53  ?  406 GLU B OE1 1 
ATOM   5861 O  OE2 . GLU B 1 406 ? -3.426  27.980 5.153   1.00 29.69  ?  406 GLU B OE2 1 
ATOM   5862 N  N   . ARG B 1 407 ? -5.747  31.474 -0.254  1.00 31.17  ?  407 ARG B N   1 
ATOM   5863 C  CA  . ARG B 1 407 ? -5.923  32.437 -1.366  1.00 29.15  ?  407 ARG B CA  1 
ATOM   5864 C  C   . ARG B 1 407 ? -6.976  31.884 -2.318  1.00 28.80  ?  407 ARG B C   1 
ATOM   5865 O  O   . ARG B 1 407 ? -6.987  30.644 -2.539  1.00 29.52  ?  407 ARG B O   1 
ATOM   5866 C  CB  . ARG B 1 407 ? -4.607  32.632 -2.108  1.00 28.78  ?  407 ARG B CB  1 
ATOM   5867 C  CG  . ARG B 1 407 ? -3.602  33.441 -1.309  1.00 29.69  ?  407 ARG B CG  1 
ATOM   5868 C  CD  . ARG B 1 407 ? -2.186  33.107 -1.721  1.00 30.35  ?  407 ARG B CD  1 
ATOM   5869 N  NE  . ARG B 1 407 ? -1.970  31.660 -1.682  1.00 33.65  ?  407 ARG B NE  1 
ATOM   5870 C  CZ  . ARG B 1 407 ? -1.644  30.980 -0.592  1.00 33.07  ?  407 ARG B CZ  1 
ATOM   5871 N  NH1 . ARG B 1 407 ? -1.520  31.621 0.554   1.00 33.59  ?  407 ARG B NH1 1 
ATOM   5872 N  NH2 . ARG B 1 407 ? -1.422  29.679 -0.650  1.00 31.37  ?  407 ARG B NH2 1 
ATOM   5873 N  N   . LEU B 1 408 ? -7.834  32.765 -2.844  1.00 27.63  ?  408 LEU B N   1 
ATOM   5874 C  CA  . LEU B 1 408 ? -8.947  32.409 -3.767  1.00 27.58  ?  408 LEU B CA  1 
ATOM   5875 C  C   . LEU B 1 408 ? -8.724  33.169 -5.059  1.00 29.17  ?  408 LEU B C   1 
ATOM   5876 O  O   . LEU B 1 408 ? -9.450  34.107 -5.360  1.00 34.00  ?  408 LEU B O   1 
ATOM   5877 C  CB  . LEU B 1 408 ? -10.316 32.731 -3.146  1.00 26.90  ?  408 LEU B CB  1 
ATOM   5878 C  CG  . LEU B 1 408 ? -11.552 32.181 -3.882  1.00 28.06  ?  408 LEU B CG  1 
ATOM   5879 C  CD1 . LEU B 1 408 ? -11.398 30.743 -4.309  1.00 26.92  ?  408 LEU B CD1 1 
ATOM   5880 C  CD2 . LEU B 1 408 ? -12.824 32.316 -3.044  1.00 28.55  ?  408 LEU B CD2 1 
ATOM   5881 N  N   . PRO B 1 409 ? -7.689  32.789 -5.842  1.00 31.62  ?  409 PRO B N   1 
ATOM   5882 C  CA  . PRO B 1 409 ? -7.311  33.532 -7.037  1.00 28.88  ?  409 PRO B CA  1 
ATOM   5883 C  C   . PRO B 1 409 ? -8.322  33.251 -8.155  1.00 28.15  ?  409 PRO B C   1 
ATOM   5884 O  O   . PRO B 1 409 ? -8.559  32.071 -8.520  1.00 27.59  ?  409 PRO B O   1 
ATOM   5885 C  CB  . PRO B 1 409 ? -5.904  32.993 -7.381  1.00 27.42  ?  409 PRO B CB  1 
ATOM   5886 C  CG  . PRO B 1 409 ? -5.828  31.631 -6.772  1.00 27.78  ?  409 PRO B CG  1 
ATOM   5887 C  CD  . PRO B 1 409 ? -6.873  31.572 -5.676  1.00 29.79  ?  409 PRO B CD  1 
ATOM   5888 N  N   . VAL B 1 410 ? -8.864  34.328 -8.706  1.00 26.96  ?  410 VAL B N   1 
ATOM   5889 C  CA  . VAL B 1 410 ? -9.889  34.261 -9.782  1.00 27.20  ?  410 VAL B CA  1 
ATOM   5890 C  C   . VAL B 1 410 ? -9.454  35.145 -10.952 1.00 28.30  ?  410 VAL B C   1 
ATOM   5891 O  O   . VAL B 1 410 ? -8.567  35.980 -10.756 1.00 30.11  ?  410 VAL B O   1 
ATOM   5892 C  CB  . VAL B 1 410 ? -11.273 34.657 -9.230  1.00 25.70  ?  410 VAL B CB  1 
ATOM   5893 C  CG1 . VAL B 1 410 ? -11.673 33.742 -8.078  1.00 24.72  ?  410 VAL B CG1 1 
ATOM   5894 C  CG2 . VAL B 1 410 ? -11.330 36.115 -8.830  1.00 22.73  ?  410 VAL B CG2 1 
ATOM   5895 N  N   . LEU B 1 411 ? -10.098 34.950 -12.110 1.00 32.31  ?  411 LEU B N   1 
ATOM   5896 C  CA  . LEU B 1 411 ? -9.840  35.783 -13.311 1.00 31.61  ?  411 LEU B CA  1 
ATOM   5897 C  C   . LEU B 1 411 ? -11.196 36.320 -13.789 1.00 32.66  ?  411 LEU B C   1 
ATOM   5898 O  O   . LEU B 1 411 ? -12.228 35.718 -13.414 1.00 32.79  ?  411 LEU B O   1 
ATOM   5899 C  CB  . LEU B 1 411 ? -9.200  34.943 -14.411 1.00 32.58  ?  411 LEU B CB  1 
ATOM   5900 C  CG  . LEU B 1 411 ? -7.768  34.465 -14.164 1.00 33.34  ?  411 LEU B CG  1 
ATOM   5901 C  CD1 . LEU B 1 411 ? -7.443  33.380 -15.172 1.00 33.07  ?  411 LEU B CD1 1 
ATOM   5902 C  CD2 . LEU B 1 411 ? -6.810  35.629 -14.307 1.00 37.30  ?  411 LEU B CD2 1 
ATOM   5903 N  N   . TRP B 1 412 ? -11.195 37.383 -14.598 1.00 32.15  ?  412 TRP B N   1 
ATOM   5904 C  CA  . TRP B 1 412 ? -12.462 37.919 -15.159 1.00 34.90  ?  412 TRP B CA  1 
ATOM   5905 C  C   . TRP B 1 412 ? -12.158 38.795 -16.378 1.00 31.41  ?  412 TRP B C   1 
ATOM   5906 O  O   . TRP B 1 412 ? -11.056 38.620 -16.943 1.00 31.23  ?  412 TRP B O   1 
ATOM   5907 C  CB  . TRP B 1 412 ? -13.241 38.701 -14.092 1.00 34.28  ?  412 TRP B CB  1 
ATOM   5908 C  CG  . TRP B 1 412 ? -12.513 39.908 -13.563 1.00 37.15  ?  412 TRP B CG  1 
ATOM   5909 C  CD1 . TRP B 1 412 ? -12.558 41.178 -14.058 1.00 35.73  ?  412 TRP B CD1 1 
ATOM   5910 C  CD2 . TRP B 1 412 ? -11.633 39.954 -12.420 1.00 34.87  ?  412 TRP B CD2 1 
ATOM   5911 N  NE1 . TRP B 1 412 ? -11.768 42.009 -13.310 1.00 36.94  ?  412 TRP B NE1 1 
ATOM   5912 C  CE2 . TRP B 1 412 ? -11.189 41.288 -12.299 1.00 36.19  ?  412 TRP B CE2 1 
ATOM   5913 C  CE3 . TRP B 1 412 ? -11.181 39.006 -11.496 1.00 32.09  ?  412 TRP B CE3 1 
ATOM   5914 C  CZ2 . TRP B 1 412 ? -10.318 41.692 -11.292 1.00 33.89  ?  412 TRP B CZ2 1 
ATOM   5915 C  CZ3 . TRP B 1 412 ? -10.317 39.407 -10.502 1.00 32.55  ?  412 TRP B CZ3 1 
ATOM   5916 C  CH2 . TRP B 1 412 ? -9.895  40.732 -10.404 1.00 32.57  ?  412 TRP B CH2 1 
HETATM 5917 N  N9  . ADE C 2 .   ? 15.718  31.542 -6.314  1.00 73.03  ?  501 ADE A N9  1 
HETATM 5918 C  C8  . ADE C 2 .   ? 16.330  31.596 -7.484  1.00 73.88  ?  501 ADE A C8  1 
HETATM 5919 N  N7  . ADE C 2 .   ? 16.135  30.508 -8.253  1.00 76.20  ?  501 ADE A N7  1 
HETATM 5920 C  C5  . ADE C 2 .   ? 15.313  29.652 -7.544  1.00 75.41  ?  501 ADE A C5  1 
HETATM 5921 C  C6  . ADE C 2 .   ? 14.704  28.374 -7.741  1.00 65.99  ?  501 ADE A C6  1 
HETATM 5922 N  N6  . ADE C 2 .   ? 14.852  27.619 -8.839  1.00 60.47  ?  501 ADE A N6  1 
HETATM 5923 N  N1  . ADE C 2 .   ? 13.925  27.896 -6.751  1.00 67.12  ?  501 ADE A N1  1 
HETATM 5924 C  C2  . ADE C 2 .   ? 13.777  28.634 -5.638  1.00 73.19  ?  501 ADE A C2  1 
HETATM 5925 N  N3  . ADE C 2 .   ? 14.293  29.824 -5.345  1.00 82.95  ?  501 ADE A N3  1 
HETATM 5926 C  C4  . ADE C 2 .   ? 15.070  30.325 -6.335  1.00 79.95  ?  501 ADE A C4  1 
HETATM 5927 C  CHA . HEM D 3 .   ? 19.632  33.159 -8.720  1.00 35.57  ?  502 HEM A CHA 1 
HETATM 5928 C  CHB . HEM D 3 .   ? 18.886  32.167 -4.099  1.00 31.82  ?  502 HEM A CHB 1 
HETATM 5929 C  CHC . HEM D 3 .   ? 18.114  36.844 -3.463  1.00 34.22  ?  502 HEM A CHC 1 
HETATM 5930 C  CHD . HEM D 3 .   ? 17.761  37.519 -8.244  1.00 33.13  ?  502 HEM A CHD 1 
HETATM 5931 C  C1A . HEM D 3 .   ? 19.535  32.506 -7.529  1.00 30.46  ?  502 HEM A C1A 1 
HETATM 5932 C  C2A . HEM D 3 .   ? 19.975  31.176 -7.330  1.00 29.59  ?  502 HEM A C2A 1 
HETATM 5933 C  C3A . HEM D 3 .   ? 19.752  30.877 -6.034  1.00 32.22  ?  502 HEM A C3A 1 
HETATM 5934 C  C4A . HEM D 3 .   ? 19.232  32.057 -5.421  1.00 31.02  ?  502 HEM A C4A 1 
HETATM 5935 C  CMA . HEM D 3 .   ? 19.972  29.545 -5.376  1.00 33.92  ?  502 HEM A CMA 1 
HETATM 5936 C  CAA . HEM D 3 .   ? 20.584  30.299 -8.378  1.00 34.59  ?  502 HEM A CAA 1 
HETATM 5937 C  CBA . HEM D 3 .   ? 19.618  29.817 -9.465  1.00 36.17  ?  502 HEM A CBA 1 
HETATM 5938 C  CGA . HEM D 3 .   ? 20.022  28.501 -10.101 1.00 36.48  ?  502 HEM A CGA 1 
HETATM 5939 O  O1A . HEM D 3 .   ? 19.141  27.775 -10.621 1.00 38.10  ?  502 HEM A O1A 1 
HETATM 5940 O  O2A . HEM D 3 .   ? 21.234  28.221 -10.094 1.00 45.12  -1 502 HEM A O2A 1 
HETATM 5941 C  C1B . HEM D 3 .   ? 18.571  33.333 -3.492  1.00 33.18  ?  502 HEM A C1B 1 
HETATM 5942 C  C2B . HEM D 3 .   ? 18.294  33.491 -2.073  1.00 36.18  ?  502 HEM A C2B 1 
HETATM 5943 C  C3B . HEM D 3 .   ? 18.016  34.878 -1.949  1.00 37.40  ?  502 HEM A C3B 1 
HETATM 5944 C  C4B . HEM D 3 .   ? 18.162  35.484 -3.198  1.00 33.92  ?  502 HEM A C4B 1 
HETATM 5945 C  CMB . HEM D 3 .   ? 18.196  32.426 -1.013  1.00 36.31  ?  502 HEM A CMB 1 
HETATM 5946 C  CAB . HEM D 3 .   ? 17.629  35.580 -0.812  1.00 40.32  ?  502 HEM A CAB 1 
HETATM 5947 C  CBB . HEM D 3 .   ? 18.344  35.674 0.277   1.00 45.97  ?  502 HEM A CBB 1 
HETATM 5948 C  C1C . HEM D 3 .   ? 17.921  37.450 -4.687  1.00 34.43  ?  502 HEM A C1C 1 
HETATM 5949 C  C2C . HEM D 3 .   ? 17.678  38.870 -4.868  1.00 33.78  ?  502 HEM A C2C 1 
HETATM 5950 C  C3C . HEM D 3 .   ? 17.635  39.044 -6.256  1.00 35.25  ?  502 HEM A C3C 1 
HETATM 5951 C  C4C . HEM D 3 .   ? 17.789  37.796 -6.863  1.00 34.44  ?  502 HEM A C4C 1 
HETATM 5952 C  CMC . HEM D 3 .   ? 17.567  39.907 -3.790  1.00 34.51  ?  502 HEM A CMC 1 
HETATM 5953 C  CAC . HEM D 3 .   ? 17.504  40.222 -7.002  1.00 40.48  ?  502 HEM A CAC 1 
HETATM 5954 C  CBC . HEM D 3 .   ? 16.660  41.191 -6.777  1.00 41.80  ?  502 HEM A CBC 1 
HETATM 5955 C  C1D . HEM D 3 .   ? 18.305  36.397 -8.807  1.00 37.45  ?  502 HEM A C1D 1 
HETATM 5956 C  C2D . HEM D 3 .   ? 18.543  36.179 -10.221 1.00 37.22  ?  502 HEM A C2D 1 
HETATM 5957 C  C3D . HEM D 3 .   ? 19.002  34.911 -10.353 1.00 37.46  ?  502 HEM A C3D 1 
HETATM 5958 C  C4D . HEM D 3 .   ? 19.148  34.382 -9.011  1.00 33.66  ?  502 HEM A C4D 1 
HETATM 5959 C  CMD . HEM D 3 .   ? 18.316  37.163 -11.324 1.00 40.41  ?  502 HEM A CMD 1 
HETATM 5960 C  CAD . HEM D 3 .   ? 19.335  34.172 -11.621 1.00 43.13  ?  502 HEM A CAD 1 
HETATM 5961 C  CBD . HEM D 3 .   ? 20.815  34.276 -12.034 1.00 48.83  ?  502 HEM A CBD 1 
HETATM 5962 C  CGD . HEM D 3 .   ? 21.207  33.475 -13.267 1.00 52.25  ?  502 HEM A CGD 1 
HETATM 5963 O  O1D . HEM D 3 .   ? 20.332  32.771 -13.808 1.00 60.65  ?  502 HEM A O1D 1 
HETATM 5964 O  O2D . HEM D 3 .   ? 22.389  33.559 -13.690 1.00 51.33  -1 502 HEM A O2D 1 
HETATM 5965 N  NA  . HEM D 3 .   ? 19.094  33.050 -6.363  1.00 28.91  ?  502 HEM A NA  1 
HETATM 5966 N  NB  . HEM D 3 .   ? 18.393  34.532 -4.152  1.00 32.52  ?  502 HEM A NB  1 
HETATM 5967 N  NC  . HEM D 3 .   ? 17.963  36.824 -5.901  1.00 34.08  ?  502 HEM A NC  1 
HETATM 5968 N  ND  . HEM D 3 .   ? 18.762  35.295 -8.083  1.00 37.87  ?  502 HEM A ND  1 
HETATM 5969 FE FE  . HEM D 3 .   ? 18.983  35.095 -6.051  1.00 40.17  ?  502 HEM A FE  1 
HETATM 5970 N  N9  . ADE E 2 .   ? -20.167 28.022 13.438  1.00 49.96  ?  501 ADE B N9  1 
HETATM 5971 C  C8  . ADE E 2 .   ? -20.757 28.039 14.623  1.00 56.31  ?  501 ADE B C8  1 
HETATM 5972 N  N7  . ADE E 2 .   ? -20.314 27.105 15.485  1.00 57.43  ?  501 ADE B N7  1 
HETATM 5973 C  C5  . ADE E 2 .   ? -19.319 26.411 14.832  1.00 61.71  ?  501 ADE B C5  1 
HETATM 5974 C  C6  . ADE E 2 .   ? -18.436 25.342 15.126  1.00 61.05  ?  501 ADE B C6  1 
HETATM 5975 N  N6  . ADE E 2 .   ? -18.378 24.704 16.301  1.00 60.96  ?  501 ADE B N6  1 
HETATM 5976 N  N1  . ADE E 2 .   ? -17.603 24.949 14.149  1.00 58.82  ?  501 ADE B N1  1 
HETATM 5977 C  C2  . ADE E 2 .   ? -17.632 25.599 12.972  1.00 55.46  ?  501 ADE B C2  1 
HETATM 5978 N  N3  . ADE E 2 .   ? -18.405 26.605 12.589  1.00 59.90  ?  501 ADE B N3  1 
HETATM 5979 C  C4  . ADE E 2 .   ? -19.257 26.999 13.554  1.00 56.68  ?  501 ADE B C4  1 
HETATM 5980 C  CHA . HEM F 3 .   ? -24.249 29.572 16.247  1.00 27.31  ?  502 HEM B CHA 1 
HETATM 5981 C  CHB . HEM F 3 .   ? -23.449 28.917 11.544  1.00 25.37  ?  502 HEM B CHB 1 
HETATM 5982 C  CHC . HEM F 3 .   ? -23.077 33.691 10.951  1.00 28.07  ?  502 HEM B CHC 1 
HETATM 5983 C  CHD . HEM F 3 .   ? -22.996 34.220 15.790  1.00 26.76  ?  502 HEM B CHD 1 
HETATM 5984 C  C1A . HEM F 3 .   ? -24.041 28.975 15.040  1.00 25.48  ?  502 HEM B C1A 1 
HETATM 5985 C  C2A . HEM F 3 .   ? -24.158 27.571 14.796  1.00 26.34  ?  502 HEM B C2A 1 
HETATM 5986 C  C3A . HEM F 3 .   ? -23.965 27.379 13.470  1.00 25.73  ?  502 HEM B C3A 1 
HETATM 5987 C  C4A . HEM F 3 .   ? -23.711 28.683 12.876  1.00 25.93  ?  502 HEM B C4A 1 
HETATM 5988 C  CMA . HEM F 3 .   ? -24.015 26.055 12.767  1.00 26.82  ?  502 HEM B CMA 1 
HETATM 5989 C  CAA . HEM F 3 .   ? -24.507 26.530 15.819  1.00 30.28  ?  502 HEM B CAA 1 
HETATM 5990 C  CBA . HEM F 3 .   ? -23.350 26.076 16.705  1.00 29.67  ?  502 HEM B CBA 1 
HETATM 5991 C  CGA . HEM F 3 .   ? -23.693 24.900 17.576  1.00 29.25  ?  502 HEM B CGA 1 
HETATM 5992 O  O1A . HEM F 3 .   ? -24.830 24.462 17.528  1.00 31.97  ?  502 HEM B O1A 1 
HETATM 5993 O  O2A . HEM F 3 .   ? -22.808 24.435 18.288  1.00 39.14  -1 502 HEM B O2A 1 
HETATM 5994 C  C1B . HEM F 3 .   ? -23.238 30.132 10.970  1.00 26.49  ?  502 HEM B C1B 1 
HETATM 5995 C  C2B . HEM F 3 .   ? -23.032 30.355 9.550   1.00 28.54  ?  502 HEM B C2B 1 
HETATM 5996 C  C3B . HEM F 3 .   ? -22.977 31.768 9.415   1.00 27.74  ?  502 HEM B C3B 1 
HETATM 5997 C  C4B . HEM F 3 .   ? -23.073 32.326 10.671  1.00 26.19  ?  502 HEM B C4B 1 
HETATM 5998 C  CMB . HEM F 3 .   ? -22.860 29.327 8.469   1.00 27.79  ?  502 HEM B CMB 1 
HETATM 5999 C  CAB . HEM F 3 .   ? -22.781 32.532 8.264   1.00 33.38  ?  502 HEM B CAB 1 
HETATM 6000 C  CBB . HEM F 3 .   ? -23.039 32.173 6.994   1.00 37.15  ?  502 HEM B CBB 1 
HETATM 6001 C  C1C . HEM F 3 .   ? -23.070 34.266 12.209  1.00 27.45  ?  502 HEM B C1C 1 
HETATM 6002 C  C2C . HEM F 3 .   ? -22.923 35.687 12.465  1.00 29.13  ?  502 HEM B C2C 1 
HETATM 6003 C  C3C . HEM F 3 .   ? -22.884 35.796 13.861  1.00 28.00  ?  502 HEM B C3C 1 
HETATM 6004 C  C4C . HEM F 3 .   ? -23.044 34.543 14.408  1.00 27.33  ?  502 HEM B C4C 1 
HETATM 6005 C  CMC . HEM F 3 .   ? -22.890 36.790 11.448  1.00 30.64  ?  502 HEM B CMC 1 
HETATM 6006 C  CAC . HEM F 3 .   ? -22.751 36.929 14.629  1.00 30.08  ?  502 HEM B CAC 1 
HETATM 6007 C  CBC . HEM F 3 .   ? -22.488 38.117 14.152  1.00 33.48  ?  502 HEM B CBC 1 
HETATM 6008 C  C1D . HEM F 3 .   ? -23.370 33.011 16.331  1.00 26.70  ?  502 HEM B C1D 1 
HETATM 6009 C  C2D . HEM F 3 .   ? -23.567 32.760 17.743  1.00 28.55  ?  502 HEM B C2D 1 
HETATM 6010 C  C3D . HEM F 3 .   ? -23.818 31.428 17.888  1.00 29.79  ?  502 HEM B C3D 1 
HETATM 6011 C  C4D . HEM F 3 .   ? -23.922 30.886 16.544  1.00 28.58  ?  502 HEM B C4D 1 
HETATM 6012 C  CMD . HEM F 3 .   ? -23.505 33.794 18.828  1.00 28.64  ?  502 HEM B CMD 1 
HETATM 6013 C  CAD . HEM F 3 .   ? -24.000 30.639 19.159  1.00 32.05  ?  502 HEM B CAD 1 
HETATM 6014 C  CBD . HEM F 3 .   ? -25.486 30.474 19.516  1.00 36.54  ?  502 HEM B CBD 1 
HETATM 6015 C  CGD . HEM F 3 .   ? -25.800 29.595 20.719  1.00 39.13  ?  502 HEM B CGD 1 
HETATM 6016 O  O1D . HEM F 3 .   ? -24.862 28.965 21.230  1.00 43.57  ?  502 HEM B O1D 1 
HETATM 6017 O  O2D . HEM F 3 .   ? -27.000 29.535 21.139  1.00 39.07  -1 502 HEM B O2D 1 
HETATM 6018 N  NA  . HEM F 3 .   ? -23.773 29.651 13.855  1.00 25.37  ?  502 HEM B NA  1 
HETATM 6019 N  NB  . HEM F 3 .   ? -23.166 31.336 11.634  1.00 24.47  ?  502 HEM B NB  1 
HETATM 6020 N  NC  . HEM F 3 .   ? -23.233 33.607 13.395  1.00 26.03  ?  502 HEM B NC  1 
HETATM 6021 N  ND  . HEM F 3 .   ? -23.633 31.871 15.603  1.00 25.48  ?  502 HEM B ND  1 
HETATM 6022 FE FE  . HEM F 3 .   ? -23.680 31.545 13.603  1.00 29.32  ?  502 HEM B FE  1 
HETATM 6023 N  N   . UYM G 4 .   ? -14.218 33.255 19.450  1.00 70.99  ?  503 UYM B N   1 
HETATM 6024 C  C   . UYM G 4 .   ? -19.840 31.890 20.696  1.00 73.95  ?  503 UYM B C   1 
HETATM 6025 O  O   . UYM G 4 .   ? -20.284 33.047 20.673  1.00 61.77  ?  503 UYM B O   1 
HETATM 6026 C  C1  . UYM G 4 .   ? -18.338 31.671 20.720  1.00 77.60  ?  503 UYM B C1  1 
HETATM 6027 C  C10 . UYM G 4 .   ? -12.738 31.209 19.355  1.00 78.80  ?  503 UYM B C10 1 
HETATM 6028 C  C11 . UYM G 4 .   ? -20.203 29.415 20.679  1.00 79.70  ?  503 UYM B C11 1 
HETATM 6029 C  C12 . UYM G 4 .   ? -20.535 28.734 19.323  1.00 80.99  ?  503 UYM B C12 1 
HETATM 6030 C  C15 . UYM G 4 .   ? -18.735 29.217 21.007  1.00 79.81  ?  503 UYM B C15 1 
HETATM 6031 C  C2  . UYM G 4 .   ? -17.717 32.074 19.355  1.00 72.54  ?  503 UYM B C2  1 
HETATM 6032 C  C3  . UYM G 4 .   ? -16.226 32.257 19.373  1.00 76.41  ?  503 UYM B C3  1 
HETATM 6033 C  C34 . UYM G 4 .   ? -20.060 29.444 18.083  1.00 74.34  ?  503 UYM B C34 1 
HETATM 6034 C  C35 . UYM G 4 .   ? -20.696 30.497 17.489  1.00 69.14  ?  503 UYM B C35 1 
HETATM 6035 C  C37 . UYM G 4 .   ? -18.914 30.099 16.206  1.00 79.01  ?  503 UYM B C37 1 
HETATM 6036 C  C38 . UYM G 4 .   ? -18.900 29.167 17.270  1.00 77.80  ?  503 UYM B C38 1 
HETATM 6037 C  C39 . UYM G 4 .   ? -17.864 28.225 17.338  1.00 77.07  ?  503 UYM B C39 1 
HETATM 6038 C  C4  . UYM G 4 .   ? -15.576 33.460 19.442  1.00 68.04  ?  503 UYM B C4  1 
HETATM 6039 C  C40 . UYM G 4 .   ? -16.892 28.238 16.363  1.00 72.57  ?  503 UYM B C40 1 
HETATM 6040 C  C41 . UYM G 4 .   ? -16.926 29.175 15.324  1.00 77.37  ?  503 UYM B C41 1 
HETATM 6041 C  C42 . UYM G 4 .   ? -17.925 30.118 15.221  1.00 72.63  ?  503 UYM B C42 1 
HETATM 6042 C  C5  . UYM G 4 .   ? -13.953 31.906 19.375  1.00 79.27  ?  503 UYM B C5  1 
HETATM 6043 C  C6  . UYM G 4 .   ? -15.198 31.234 19.320  1.00 78.53  ?  503 UYM B C6  1 
HETATM 6044 C  C7  . UYM G 4 .   ? -15.206 29.828 19.249  1.00 74.93  ?  503 UYM B C7  1 
HETATM 6045 C  C8  . UYM G 4 .   ? -14.004 29.144 19.230  1.00 71.14  ?  503 UYM B C8  1 
HETATM 6046 C  C9  . UYM G 4 .   ? -12.790 29.829 19.288  1.00 76.12  ?  503 UYM B C9  1 
HETATM 6047 N  N1  . UYM G 4 .   ? -17.963 30.305 21.087  1.00 79.68  ?  503 UYM B N1  1 
HETATM 6048 N  N2  . UYM G 4 .   ? -20.627 30.816 20.695  1.00 77.80  ?  503 UYM B N2  1 
HETATM 6049 N  N36 . UYM G 4 .   ? -20.025 30.886 16.364  1.00 72.83  ?  503 UYM B N36 1 
HETATM 6050 O  O1  . UYM G 4 .   ? -18.313 28.059 21.177  1.00 61.23  ?  503 UYM B O1  1 
HETATM 6051 O  O   . HOH H 5 .   ? 25.992  47.536 -20.705 1.00 48.47  ?  601 HOH A O   1 
HETATM 6052 O  O   . HOH H 5 .   ? 29.689  8.972  -19.983 1.00 41.40  ?  602 HOH A O   1 
HETATM 6053 O  O   . HOH H 5 .   ? -1.121  31.407 -18.606 1.00 34.05  ?  603 HOH A O   1 
HETATM 6054 O  O   . HOH H 5 .   ? 5.621   12.403 -8.536  1.00 50.06  ?  604 HOH A O   1 
HETATM 6055 O  O   . HOH H 5 .   ? 2.787   39.448 -11.412 1.00 37.62  ?  605 HOH A O   1 
HETATM 6056 O  O   . HOH H 5 .   ? 23.555  42.948 14.296  1.00 30.20  ?  606 HOH A O   1 
HETATM 6057 O  O   . HOH H 5 .   ? 15.109  6.400  -8.151  1.00 39.70  ?  607 HOH A O   1 
HETATM 6058 O  O   . HOH H 5 .   ? -2.466  36.606 -3.183  1.00 25.11  ?  608 HOH A O   1 
HETATM 6059 O  O   . HOH H 5 .   ? 30.353  12.112 -21.231 1.00 45.50  ?  609 HOH A O   1 
HETATM 6060 O  O   . HOH H 5 .   ? 3.996   35.613 -1.210  1.00 33.08  ?  610 HOH A O   1 
HETATM 6061 O  O   . HOH H 5 .   ? 22.845  7.592  -6.742  1.00 31.11  ?  611 HOH A O   1 
HETATM 6062 O  O   . HOH H 5 .   ? 6.214   22.535 11.077  1.00 38.04  ?  612 HOH A O   1 
HETATM 6063 O  O   . HOH H 5 .   ? 15.545  15.614 9.443   1.00 31.04  ?  613 HOH A O   1 
HETATM 6064 O  O   . HOH H 5 .   ? 14.993  13.851 -17.283 1.00 29.42  ?  614 HOH A O   1 
HETATM 6065 O  O   . HOH H 5 .   ? 12.155  32.052 21.868  1.00 20.33  ?  615 HOH A O   1 
HETATM 6066 O  O   . HOH H 5 .   ? -3.538  23.832 -15.135 1.00 30.15  ?  616 HOH A O   1 
HETATM 6067 O  O   . HOH H 5 .   ? 3.914   45.293 22.296  1.00 29.24  ?  617 HOH A O   1 
HETATM 6068 O  O   . HOH H 5 .   ? 24.427  50.822 1.570   1.00 41.33  ?  618 HOH A O   1 
HETATM 6069 O  O   . HOH H 5 .   ? 27.702  12.495 2.062   1.00 39.41  ?  619 HOH A O   1 
HETATM 6070 O  O   . HOH H 5 .   ? -3.184  41.493 6.702   1.00 34.49  ?  620 HOH A O   1 
HETATM 6071 O  O   . HOH H 5 .   ? 12.271  24.013 15.631  1.00 27.51  ?  621 HOH A O   1 
HETATM 6072 O  O   . HOH H 5 .   ? 3.613   52.716 -22.980 1.00 39.07  ?  622 HOH A O   1 
HETATM 6073 O  O   . HOH H 5 .   ? 30.945  15.616 9.612   1.00 46.33  ?  623 HOH A O   1 
HETATM 6074 O  O   . HOH H 5 .   ? 13.091  21.955 -17.660 1.00 31.94  ?  624 HOH A O   1 
HETATM 6075 O  O   . HOH H 5 .   ? 23.664  28.595 -9.119  1.00 36.38  ?  625 HOH A O   1 
HETATM 6076 O  O   . HOH H 5 .   ? 28.690  27.288 -14.227 1.00 46.01  ?  626 HOH A O   1 
HETATM 6077 O  O   . HOH H 5 .   ? 7.407   22.485 19.227  1.00 37.10  ?  627 HOH A O   1 
HETATM 6078 O  O   . HOH H 5 .   ? 5.608   25.326 2.613   1.00 24.19  ?  628 HOH A O   1 
HETATM 6079 O  O   . HOH H 5 .   ? 11.664  21.888 14.492  1.00 36.82  ?  629 HOH A O   1 
HETATM 6080 O  O   . HOH H 5 .   ? 4.072   46.083 10.634  1.00 32.75  ?  630 HOH A O   1 
HETATM 6081 O  O   . HOH H 5 .   ? 4.564   40.973 -9.180  1.00 39.44  ?  631 HOH A O   1 
HETATM 6082 O  O   . HOH H 5 .   ? 19.315  11.842 -4.834  1.00 30.49  ?  632 HOH A O   1 
HETATM 6083 O  O   . HOH H 5 .   ? 1.908   39.481 1.080   1.00 32.12  ?  633 HOH A O   1 
HETATM 6084 O  O   . HOH H 5 .   ? 1.037   28.322 -16.186 1.00 28.58  ?  634 HOH A O   1 
HETATM 6085 O  O   . HOH H 5 .   ? 25.251  27.622 -12.218 1.00 40.19  ?  635 HOH A O   1 
HETATM 6086 O  O   . HOH H 5 .   ? 0.545   35.823 6.260   1.00 22.94  ?  636 HOH A O   1 
HETATM 6087 O  O   . HOH H 5 .   ? 0.362   33.244 3.169   1.00 29.55  ?  637 HOH A O   1 
HETATM 6088 O  O   . HOH H 5 .   ? 28.776  31.347 9.136   1.00 37.07  ?  638 HOH A O   1 
HETATM 6089 O  O   . HOH H 5 .   ? 30.800  12.775 -11.002 1.00 43.46  ?  639 HOH A O   1 
HETATM 6090 O  O   . HOH H 5 .   ? 14.199  32.108 -0.783  1.00 31.84  ?  640 HOH A O   1 
HETATM 6091 O  O   . HOH H 5 .   ? 5.330   25.196 -1.616  1.00 32.67  ?  641 HOH A O   1 
HETATM 6092 O  O   . HOH H 5 .   ? 25.767  37.294 5.636   1.00 30.07  ?  642 HOH A O   1 
HETATM 6093 O  O   . HOH H 5 .   ? 14.494  38.156 19.784  1.00 24.59  ?  643 HOH A O   1 
HETATM 6094 O  O   . HOH H 5 .   ? 22.269  44.687 20.889  1.00 32.05  ?  644 HOH A O   1 
HETATM 6095 O  O   . HOH H 5 .   ? 25.879  29.535 -2.502  1.00 24.78  ?  645 HOH A O   1 
HETATM 6096 O  O   . HOH H 5 .   ? 21.042  15.534 9.112   1.00 45.75  ?  646 HOH A O   1 
HETATM 6097 O  O   . HOH H 5 .   ? -0.410  47.729 -1.183  1.00 29.51  ?  647 HOH A O   1 
HETATM 6098 O  O   . HOH H 5 .   ? 27.762  37.333 -0.911  1.00 40.41  ?  648 HOH A O   1 
HETATM 6099 O  O   . HOH H 5 .   ? 16.774  22.636 -3.448  1.00 31.52  ?  649 HOH A O   1 
HETATM 6100 O  O   . HOH H 5 .   ? 11.635  54.842 6.117   1.00 54.47  ?  650 HOH A O   1 
HETATM 6101 O  O   . HOH H 5 .   ? -0.545  21.696 20.786  1.00 36.61  ?  651 HOH A O   1 
HETATM 6102 O  O   . HOH H 5 .   ? 0.669   37.948 -0.086  1.00 32.37  ?  652 HOH A O   1 
HETATM 6103 O  O   . HOH H 5 .   ? 7.033   22.151 -24.253 1.00 38.29  ?  653 HOH A O   1 
HETATM 6104 O  O   . HOH H 5 .   ? 2.234   59.698 -16.167 1.00 30.28  ?  654 HOH A O   1 
HETATM 6105 O  O   . HOH H 5 .   ? 25.208  24.507 -14.198 1.00 45.45  ?  655 HOH A O   1 
HETATM 6106 O  O   . HOH H 5 .   ? -1.197  41.659 23.965  1.00 27.36  ?  656 HOH A O   1 
HETATM 6107 O  O   . HOH H 5 .   ? 1.448   21.809 2.517   1.00 42.85  ?  657 HOH A O   1 
HETATM 6108 O  O   . HOH H 5 .   ? 1.344   22.458 6.621   1.00 32.11  ?  658 HOH A O   1 
HETATM 6109 O  O   . HOH H 5 .   ? 9.176   9.269  -2.144  1.00 48.19  ?  659 HOH A O   1 
HETATM 6110 O  O   . HOH H 5 .   ? 26.164  39.957 -4.934  1.00 40.60  ?  660 HOH A O   1 
HETATM 6111 O  O   . HOH H 5 .   ? 19.817  39.582 25.637  1.00 27.29  ?  661 HOH A O   1 
HETATM 6112 O  O   . HOH H 5 .   ? -1.636  47.128 -3.311  1.00 22.61  ?  662 HOH A O   1 
HETATM 6113 O  O   . HOH H 5 .   ? 15.227  35.698 22.231  1.00 33.45  ?  663 HOH A O   1 
HETATM 6114 O  O   . HOH H 5 .   ? 6.347   37.613 26.988  1.00 48.88  ?  664 HOH A O   1 
HETATM 6115 O  O   . HOH H 5 .   ? 31.597  24.032 8.877   1.00 41.89  ?  665 HOH A O   1 
HETATM 6116 O  O   . HOH H 5 .   ? 18.802  29.038 0.040   1.00 27.74  ?  666 HOH A O   1 
HETATM 6117 O  O   . HOH H 5 .   ? -3.120  27.669 10.114  1.00 29.92  ?  667 HOH A O   1 
HETATM 6118 O  O   . HOH H 5 .   ? 26.048  29.165 17.435  1.00 32.13  ?  668 HOH A O   1 
HETATM 6119 O  O   . HOH H 5 .   ? 4.245   41.979 25.563  1.00 35.28  ?  669 HOH A O   1 
HETATM 6120 O  O   . HOH H 5 .   ? 17.720  6.111  -9.132  1.00 36.82  ?  670 HOH A O   1 
HETATM 6121 O  O   . HOH H 5 .   ? 13.125  21.498 -1.844  1.00 33.36  ?  671 HOH A O   1 
HETATM 6122 O  O   . HOH H 5 .   ? -0.733  23.228 5.080   1.00 34.72  ?  672 HOH A O   1 
HETATM 6123 O  O   . HOH H 5 .   ? 21.520  15.545 6.946   1.00 39.81  ?  673 HOH A O   1 
HETATM 6124 O  O   . HOH H 5 .   ? -1.865  29.696 11.527  1.00 25.02  ?  674 HOH A O   1 
HETATM 6125 O  O   . HOH H 5 .   ? -3.491  47.725 21.573  1.00 33.65  ?  675 HOH A O   1 
HETATM 6126 O  O   . HOH H 5 .   ? -2.100  27.355 12.119  1.00 33.51  ?  676 HOH A O   1 
HETATM 6127 O  O   . HOH H 5 .   ? 4.278   17.987 1.263   1.00 38.37  ?  677 HOH A O   1 
HETATM 6128 O  O   . HOH H 5 .   ? -2.276  32.457 -5.438  1.00 28.07  ?  678 HOH A O   1 
HETATM 6129 O  O   . HOH H 5 .   ? -4.588  47.785 15.573  1.00 44.50  ?  679 HOH A O   1 
HETATM 6130 O  O   . HOH H 5 .   ? -2.300  37.728 7.490   1.00 42.89  ?  680 HOH A O   1 
HETATM 6131 O  O   . HOH H 5 .   ? 3.757   37.628 28.133  1.00 38.56  ?  681 HOH A O   1 
HETATM 6132 O  O   . HOH H 5 .   ? -1.463  34.856 12.399  1.00 21.69  ?  682 HOH A O   1 
HETATM 6133 O  O   . HOH H 5 .   ? -4.165  49.284 19.958  1.00 31.62  ?  683 HOH A O   1 
HETATM 6134 O  O   . HOH H 5 .   ? -3.373  34.784 -4.898  1.00 24.44  ?  684 HOH A O   1 
HETATM 6135 O  O   . HOH H 5 .   ? 24.775  11.640 3.877   1.00 32.28  ?  685 HOH A O   1 
HETATM 6136 O  O   . HOH H 5 .   ? 6.049   20.142 -22.756 1.00 46.21  ?  686 HOH A O   1 
HETATM 6137 O  O   . HOH H 5 .   ? 4.189   16.630 3.441   1.00 38.19  ?  687 HOH A O   1 
HETATM 6138 O  O   . HOH H 5 .   ? 1.508   19.414 1.892   1.00 37.34  ?  688 HOH A O   1 
HETATM 6139 O  O   . HOH I 5 .   ? -5.029  43.418 -7.735  1.00 27.14  ?  601 HOH B O   1 
HETATM 6140 O  O   . HOH I 5 .   ? -26.940 24.383 16.632  1.00 28.23  ?  602 HOH B O   1 
HETATM 6141 O  O   . HOH I 5 .   ? -7.195  14.016 14.562  1.00 48.57  ?  603 HOH B O   1 
HETATM 6142 O  O   . HOH I 5 .   ? -20.666 8.899  11.846  1.00 23.86  ?  604 HOH B O   1 
HETATM 6143 O  O   . HOH I 5 .   ? -2.843  36.347 10.396  1.00 30.51  ?  605 HOH B O   1 
HETATM 6144 O  O   . HOH I 5 .   ? -6.167  35.497 1.236   1.00 25.02  ?  606 HOH B O   1 
HETATM 6145 O  O   . HOH I 5 .   ? -20.457 30.702 13.567  1.00 46.63  ?  607 HOH B O   1 
HETATM 6146 O  O   . HOH I 5 .   ? -14.565 19.984 -7.219  1.00 43.43  ?  608 HOH B O   1 
HETATM 6147 O  O   . HOH I 5 .   ? -16.624 29.965 -14.590 1.00 32.85  ?  609 HOH B O   1 
HETATM 6148 O  O   . HOH I 5 .   ? -20.446 25.288 18.039  1.00 31.71  ?  610 HOH B O   1 
HETATM 6149 O  O   . HOH I 5 .   ? -27.595 12.410 -8.361  1.00 49.39  ?  611 HOH B O   1 
HETATM 6150 O  O   . HOH I 5 .   ? -31.617 33.189 13.833  1.00 29.30  ?  612 HOH B O   1 
HETATM 6151 O  O   . HOH I 5 .   ? -13.356 28.401 -12.298 1.00 24.44  ?  613 HOH B O   1 
HETATM 6152 O  O   . HOH I 5 .   ? -29.893 44.540 26.755  1.00 48.92  ?  614 HOH B O   1 
HETATM 6153 O  O   . HOH I 5 .   ? -32.746 33.060 8.565   1.00 51.22  ?  615 HOH B O   1 
HETATM 6154 O  O   . HOH I 5 .   ? 0.020   23.946 22.142  1.00 37.82  ?  616 HOH B O   1 
HETATM 6155 O  O   . HOH I 5 .   ? -5.383  45.939 23.295  1.00 38.34  ?  617 HOH B O   1 
HETATM 6156 O  O   . HOH I 5 .   ? -33.466 35.803 2.504   1.00 46.42  ?  618 HOH B O   1 
HETATM 6157 O  O   . HOH I 5 .   ? -23.037 20.929 -8.087  1.00 34.75  ?  619 HOH B O   1 
HETATM 6158 O  O   . HOH I 5 .   ? -9.470  24.100 4.659   1.00 29.63  ?  620 HOH B O   1 
HETATM 6159 O  O   . HOH I 5 .   ? -32.128 24.249 -11.127 1.00 34.53  ?  621 HOH B O   1 
HETATM 6160 O  O   . HOH I 5 .   ? -18.739 29.322 8.106   1.00 30.86  ?  622 HOH B O   1 
HETATM 6161 O  O   . HOH I 5 .   ? -22.542 35.226 4.909   1.00 23.85  ?  623 HOH B O   1 
HETATM 6162 O  O   . HOH I 5 .   ? -12.870 16.954 1.266   1.00 21.93  ?  624 HOH B O   1 
HETATM 6163 O  O   . HOH I 5 .   ? -20.031 35.695 -11.982 1.00 21.27  ?  625 HOH B O   1 
HETATM 6164 O  O   . HOH I 5 .   ? -23.475 6.715  32.278  1.00 40.47  ?  626 HOH B O   1 
HETATM 6165 O  O   . HOH I 5 .   ? -3.198  30.458 25.905  1.00 30.26  ?  627 HOH B O   1 
HETATM 6166 O  O   . HOH I 5 .   ? -9.187  21.699 -3.766  1.00 41.05  ?  628 HOH B O   1 
HETATM 6167 O  O   . HOH I 5 .   ? -5.117  28.770 -2.594  1.00 28.73  ?  629 HOH B O   1 
HETATM 6168 O  O   . HOH I 5 .   ? -0.354  23.918 -7.867  1.00 26.35  ?  630 HOH B O   1 
HETATM 6169 O  O   . HOH I 5 .   ? -9.123  38.060 18.764  1.00 35.54  ?  631 HOH B O   1 
HETATM 6170 O  O   . HOH I 5 .   ? -35.743 33.130 -14.964 1.00 42.71  ?  632 HOH B O   1 
HETATM 6171 O  O   . HOH I 5 .   ? -25.637 21.112 -10.075 1.00 36.87  ?  633 HOH B O   1 
HETATM 6172 O  O   . HOH I 5 .   ? -16.222 19.259 9.121   1.00 34.10  ?  634 HOH B O   1 
HETATM 6173 O  O   . HOH I 5 .   ? -17.397 12.473 -2.168  1.00 36.18  ?  635 HOH B O   1 
HETATM 6174 O  O   . HOH I 5 .   ? -27.595 35.394 -17.257 1.00 28.31  ?  636 HOH B O   1 
HETATM 6175 O  O   . HOH I 5 .   ? -29.006 8.235  5.384   1.00 28.68  ?  637 HOH B O   1 
HETATM 6176 O  O   . HOH I 5 .   ? -12.542 54.561 19.216  1.00 39.29  ?  638 HOH B O   1 
HETATM 6177 O  O   . HOH I 5 .   ? -10.717 45.174 -3.115  1.00 26.59  ?  639 HOH B O   1 
HETATM 6178 O  O   . HOH I 5 .   ? -7.625  48.590 27.968  1.00 42.51  ?  640 HOH B O   1 
HETATM 6179 O  O   . HOH I 5 .   ? -6.771  47.469 8.875   1.00 26.39  ?  641 HOH B O   1 
HETATM 6180 O  O   . HOH I 5 .   ? -5.251  32.900 4.242   1.00 29.75  ?  642 HOH B O   1 
HETATM 6181 O  O   . HOH I 5 .   ? -35.234 18.865 -1.397  1.00 32.48  ?  643 HOH B O   1 
HETATM 6182 O  O   . HOH I 5 .   ? -7.592  24.855 19.532  1.00 25.16  ?  644 HOH B O   1 
HETATM 6183 O  O   . HOH I 5 .   ? -18.907 32.688 -12.616 1.00 26.19  ?  645 HOH B O   1 
HETATM 6184 O  O   . HOH I 5 .   ? -12.414 36.776 -19.034 1.00 32.37  ?  646 HOH B O   1 
HETATM 6185 O  O   . HOH I 5 .   ? -1.859  26.448 3.520   1.00 32.07  ?  647 HOH B O   1 
HETATM 6186 O  O   . HOH I 5 .   ? -15.682 19.284 24.701  1.00 30.48  ?  648 HOH B O   1 
HETATM 6187 O  O   . HOH I 5 .   ? -4.797  29.935 11.397  1.00 38.09  ?  649 HOH B O   1 
HETATM 6188 O  O   . HOH I 5 .   ? -32.055 7.559  17.626  1.00 29.48  ?  650 HOH B O   1 
HETATM 6189 O  O   . HOH I 5 .   ? -5.828  40.188 -4.588  1.00 26.60  ?  651 HOH B O   1 
HETATM 6190 O  O   . HOH I 5 .   ? -8.848  23.819 8.920   1.00 26.65  ?  652 HOH B O   1 
HETATM 6191 O  O   . HOH I 5 .   ? -20.472 23.895 6.446   1.00 24.33  ?  653 HOH B O   1 
HETATM 6192 O  O   . HOH I 5 .   ? -5.112  41.810 -16.087 1.00 33.62  ?  654 HOH B O   1 
HETATM 6193 O  O   . HOH I 5 .   ? -7.265  6.827  15.270  1.00 42.45  ?  655 HOH B O   1 
HETATM 6194 O  O   . HOH I 5 .   ? -28.683 23.144 19.636  1.00 25.16  ?  656 HOH B O   1 
HETATM 6195 O  O   . HOH I 5 .   ? -32.708 4.558  18.210  1.00 36.39  ?  657 HOH B O   1 
HETATM 6196 O  O   . HOH I 5 .   ? -8.992  21.493 12.110  1.00 31.25  ?  658 HOH B O   1 
HETATM 6197 O  O   . HOH I 5 .   ? -5.174  27.246 23.574  1.00 32.26  ?  659 HOH B O   1 
HETATM 6198 O  O   . HOH I 5 .   ? -10.669 21.261 -11.910 1.00 44.06  ?  660 HOH B O   1 
HETATM 6199 O  O   . HOH I 5 .   ? -1.870  23.183 -3.786  1.00 35.80  ?  661 HOH B O   1 
HETATM 6200 O  O   . HOH I 5 .   ? -32.025 22.035 21.381  1.00 31.47  ?  662 HOH B O   1 
HETATM 6201 O  O   . HOH I 5 .   ? -22.852 21.064 4.393   1.00 29.36  ?  663 HOH B O   1 
HETATM 6202 O  O   . HOH I 5 .   ? -19.023 51.707 11.652  1.00 43.35  ?  664 HOH B O   1 
HETATM 6203 O  O   . HOH I 5 .   ? -30.962 32.976 1.863   1.00 23.97  ?  665 HOH B O   1 
HETATM 6204 O  O   . HOH I 5 .   ? -11.419 23.668 -11.527 1.00 29.75  ?  666 HOH B O   1 
HETATM 6205 O  O   . HOH I 5 .   ? -31.092 10.656 7.965   1.00 30.20  ?  667 HOH B O   1 
HETATM 6206 O  O   . HOH I 5 .   ? -22.682 25.905 7.419   1.00 23.49  ?  668 HOH B O   1 
HETATM 6207 O  O   . HOH I 5 .   ? -25.768 43.540 -4.090  1.00 23.11  ?  669 HOH B O   1 
HETATM 6208 O  O   . HOH I 5 .   ? -29.762 25.163 9.800   1.00 21.27  ?  670 HOH B O   1 
HETATM 6209 O  O   . HOH I 5 .   ? -2.265  21.883 -13.570 1.00 33.00  ?  671 HOH B O   1 
HETATM 6210 O  O   . HOH I 5 .   ? -10.414 39.730 16.564  1.00 28.36  ?  672 HOH B O   1 
HETATM 6211 O  O   . HOH I 5 .   ? -27.916 19.842 21.508  1.00 27.37  ?  673 HOH B O   1 
HETATM 6212 O  O   . HOH I 5 .   ? -28.390 38.752 -9.624  1.00 25.63  ?  674 HOH B O   1 
HETATM 6213 O  O   . HOH I 5 .   ? -18.117 3.117  16.124  1.00 37.07  ?  675 HOH B O   1 
HETATM 6214 O  O   . HOH I 5 .   ? -30.895 40.545 -0.378  1.00 34.06  ?  676 HOH B O   1 
HETATM 6215 O  O   . HOH I 5 .   ? -5.324  46.756 10.980  1.00 32.01  ?  677 HOH B O   1 
HETATM 6216 O  O   . HOH I 5 .   ? -30.280 25.213 -10.082 1.00 30.67  ?  678 HOH B O   1 
HETATM 6217 O  O   . HOH I 5 .   ? -21.954 0.997  26.934  1.00 44.04  ?  679 HOH B O   1 
HETATM 6218 O  O   . HOH I 5 .   ? -19.329 18.636 -2.575  1.00 28.97  ?  680 HOH B O   1 
HETATM 6219 O  O   . HOH I 5 .   ? -4.547  22.118 0.468   1.00 37.59  ?  681 HOH B O   1 
HETATM 6220 O  O   . HOH I 5 .   ? -32.823 26.276 -1.580  1.00 29.33  ?  682 HOH B O   1 
HETATM 6221 O  O   . HOH I 5 .   ? -15.896 39.509 -16.088 1.00 26.12  ?  683 HOH B O   1 
HETATM 6222 O  O   . HOH I 5 .   ? -11.442 20.705 13.129  1.00 32.71  ?  684 HOH B O   1 
HETATM 6223 O  O   . HOH I 5 .   ? -7.504  19.483 -3.465  1.00 37.29  ?  685 HOH B O   1 
HETATM 6224 O  O   . HOH I 5 .   ? -29.605 45.404 -1.086  1.00 46.13  ?  686 HOH B O   1 
HETATM 6225 O  O   . HOH I 5 .   ? -7.432  39.145 6.293   1.00 30.51  ?  687 HOH B O   1 
HETATM 6226 O  O   . HOH I 5 .   ? -26.239 4.200  14.737  1.00 31.49  ?  688 HOH B O   1 
HETATM 6227 O  O   . HOH I 5 .   ? -15.459 22.333 -7.950  1.00 36.15  ?  689 HOH B O   1 
HETATM 6228 O  O   . HOH I 5 .   ? -25.289 36.486 -17.947 1.00 27.82  ?  690 HOH B O   1 
HETATM 6229 O  O   . HOH I 5 .   ? -15.675 3.358  14.529  1.00 36.13  ?  691 HOH B O   1 
HETATM 6230 O  O   . HOH I 5 .   ? -30.036 27.554 -11.608 1.00 24.87  ?  692 HOH B O   1 
HETATM 6231 O  O   . HOH I 5 .   ? -2.547  29.997 -4.185  1.00 36.48  ?  693 HOH B O   1 
HETATM 6232 O  O   . HOH I 5 .   ? -31.471 35.682 12.594  1.00 40.79  ?  694 HOH B O   1 
HETATM 6233 O  O   . HOH I 5 .   ? -11.804 18.560 15.163  1.00 39.57  ?  695 HOH B O   1 
HETATM 6234 O  O   . HOH I 5 .   ? -20.429 2.403  16.122  1.00 54.23  ?  696 HOH B O   1 
HETATM 6235 O  O   . HOH I 5 .   ? -6.642  16.926 5.415   1.00 42.38  ?  697 HOH B O   1 
HETATM 6236 O  O   . HOH I 5 .   ? -2.261  32.357 12.788  1.00 27.49  ?  698 HOH B O   1 
HETATM 6237 O  O   . HOH I 5 .   ? -3.389  37.509 -0.548  1.00 36.49  ?  699 HOH B O   1 
HETATM 6238 O  O   . HOH I 5 .   ? -6.026  38.261 7.731   1.00 30.08  ?  700 HOH B O   1 
HETATM 6239 O  O   . HOH I 5 .   ? -30.501 10.890 -5.294  1.00 34.06  ?  701 HOH B O   1 
HETATM 6240 O  O   . HOH I 5 .   ? -6.911  15.112 3.194   1.00 49.22  ?  702 HOH B O   1 
HETATM 6241 O  O   . HOH I 5 .   ? -5.696  40.769 7.293   1.00 35.07  ?  703 HOH B O   1 
HETATM 6242 O  O   . HOH I 5 .   ? -1.245  27.980 -3.523  1.00 34.22  ?  704 HOH B O   1 
HETATM 6243 O  O   . HOH I 5 .   ? -28.380 43.719 -3.624  1.00 26.57  ?  705 HOH B O   1 
HETATM 6244 O  O   . HOH I 5 .   ? -9.598  40.072 32.765  1.00 62.87  ?  706 HOH B O   1 
HETATM 6245 O  O   . HOH I 5 .   ? -29.498 41.006 -2.665  1.00 46.80  ?  707 HOH B O   1 
HETATM 6246 O  O   . HOH I 5 .   ? -20.034 16.593 -3.845  1.00 40.66  ?  708 HOH B O   1 
HETATM 6247 O  O   . HOH I 5 .   ? -30.766 47.127 -0.336  1.00 45.21  ?  709 HOH B O   1 
HETATM 6248 O  O   . HOH I 5 .   ? -2.234  43.377 11.216  1.00 34.76  ?  710 HOH B O   1 
HETATM 6249 O  O   . HOH I 5 .   ? -19.678 52.255 9.208   1.00 42.22  ?  711 HOH B O   1 
HETATM 6250 O  O   . HOH I 5 .   ? -20.175 4.942  0.681   1.00 38.03  ?  712 HOH B O   1 
HETATM 6251 O  O   . HOH I 5 .   ? -4.242  39.089 6.323   1.00 32.45  ?  713 HOH B O   1 
# 
