data_9KW5
# 
_entry.id   9KW5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9KW5         pdb_00009kw5 10.2210/pdb9kw5/pdb 
WWPDB D_1300054166 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-21 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.title'          
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9KW5 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tamada.taro@qst.go.jp 
_pdbx_contact_author.name_first         Taro 
_pdbx_contact_author.name_last          Tamada 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1419-8022 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Hirano, Y.'            1 0000-0002-3007-6052 
'Yoneda, S.'            2 ?                   
'Yasuda, K.'            3 ?                   
'Takimoto-Kamimura, M.' 4 ?                   
'Sakaki, T.'            5 ?                   
'Tamada, T.'            6 0000-0003-1419-8022 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            301 
_citation.language                  ? 
_citation.page_first                108513 
_citation.page_last                 108513 
_citation.title                     
'Cooperative inhibition in cytochrome P450 between a substrate and an apparent noncompetitive inhibitor.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2025.108513 
_citation.pdbx_database_id_PubMed   40246023 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Hirano, Y.'            1  ? 
primary 'Yoneda, S.'            2  ? 
primary 'Yasuda, K.'            3  ? 
primary 'Kurita, N.'            4  ? 
primary 'Kawagoe, F.'           5  ? 
primary 'Mikami, B.'            6  ? 
primary 'Takita, T.'            7  ? 
primary 'Yasukawa, K.'          8  ? 
primary 'Ikushiro, S.'          9  ? 
primary 'Takimoto-Kamimura, M.' 10 ? 
primary 'Kittaka, A.'           11 ? 
primary 'Sakaki, T.'            12 ? 
primary 'Tamada, T.'            13 ? 
# 
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 'Vitamin D3 dihydroxylase'                                                                     44991.742 1   
1.14.15.- R84A ? '6xHis-tag fused to the C-terminus' 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                                              616.487   1   ? ? 
? ?                                   
3 non-polymer syn '2-[2,6-DICHLOROPHENYL)AMINO]BENZENEACETIC ACID'                                               296.149   1   ? ? 
? ?                                   
4 non-polymer syn '(2~{E})-2-[(4~{R})-4-(2-chlorophenyl)-1,3-dithiolan-2-ylidene]-2-imidazol-1-yl-ethanenitrile' 319.832   1   ? ? 
? ?                                   
5 water       nat water                                                                                          18.015    204 ? ? 
? ?                                   
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'CYP105A1,Cytochrome P450-CVA1,Cytochrome P450-SU1,Vitamin D3 hydroxylase,VD3 hydroxylase' 
# 
_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       
;MTDTATTPQTTDAPAFPSNRSCPYQLPDGYAQLRDTPGPLHRVTLYDGRQAWVVTKHEAARKLLGDPRLSSNRTDDNFPA
TSPAFEAVRESPQAFIGLDPPEHGTRRRMTISEFTVKRIKGMRPEVEEVVHGFLDEMLAAGPTADLVSQFALPVPSMVIC
RLLGVPYADHEFFQDASKRLVQSTDAQSALTARNDLAGYLDGLITQFQTEPGAGLVGALVADQLANGEIDREELISTAML
LLIAGHETTASMTSLSVITLLDHPEQYAALRADRSLVPGAVEELLRYLAIADIAGGRVATADIEVEGQLIRAGEGVIVVN
SIANRDGTVYEDPDALDIHRSARHHLAFGFGVHQCLGQNLARLELEVILNALMDRVPTLRLAVPVEQLVLRPGTTIQGVN
ELPVTWHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTDTATTPQTTDAPAFPSNRSCPYQLPDGYAQLRDTPGPLHRVTLYDGRQAWVVTKHEAARKLLGDPRLSSNRTDDNFPA
TSPAFEAVRESPQAFIGLDPPEHGTRRRMTISEFTVKRIKGMRPEVEEVVHGFLDEMLAAGPTADLVSQFALPVPSMVIC
RLLGVPYADHEFFQDASKRLVQSTDAQSALTARNDLAGYLDGLITQFQTEPGAGLVGALVADQLANGEIDREELISTAML
LLIAGHETTASMTSLSVITLLDHPEQYAALRADRSLVPGAVEELLRYLAIADIAGGRVATADIEVEGQLIRAGEGVIVVN
SIANRDGTVYEDPDALDIHRSARHHLAFGFGVHQCLGQNLARLELEVILNALMDRVPTLRLAVPVEQLVLRPGTTIQGVN
ELPVTWHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'                                                              HEM   
3 '2-[2,6-DICHLOROPHENYL)AMINO]BENZENEACETIC ACID'                                               DIF   
4 '(2~{E})-2-[(4~{R})-4-(2-chlorophenyl)-1,3-dithiolan-2-ylidene]-2-imidazol-1-yl-ethanenitrile' A1L6Q 
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   ASP n 
1 4   THR n 
1 5   ALA n 
1 6   THR n 
1 7   THR n 
1 8   PRO n 
1 9   GLN n 
1 10  THR n 
1 11  THR n 
1 12  ASP n 
1 13  ALA n 
1 14  PRO n 
1 15  ALA n 
1 16  PHE n 
1 17  PRO n 
1 18  SER n 
1 19  ASN n 
1 20  ARG n 
1 21  SER n 
1 22  CYS n 
1 23  PRO n 
1 24  TYR n 
1 25  GLN n 
1 26  LEU n 
1 27  PRO n 
1 28  ASP n 
1 29  GLY n 
1 30  TYR n 
1 31  ALA n 
1 32  GLN n 
1 33  LEU n 
1 34  ARG n 
1 35  ASP n 
1 36  THR n 
1 37  PRO n 
1 38  GLY n 
1 39  PRO n 
1 40  LEU n 
1 41  HIS n 
1 42  ARG n 
1 43  VAL n 
1 44  THR n 
1 45  LEU n 
1 46  TYR n 
1 47  ASP n 
1 48  GLY n 
1 49  ARG n 
1 50  GLN n 
1 51  ALA n 
1 52  TRP n 
1 53  VAL n 
1 54  VAL n 
1 55  THR n 
1 56  LYS n 
1 57  HIS n 
1 58  GLU n 
1 59  ALA n 
1 60  ALA n 
1 61  ARG n 
1 62  LYS n 
1 63  LEU n 
1 64  LEU n 
1 65  GLY n 
1 66  ASP n 
1 67  PRO n 
1 68  ARG n 
1 69  LEU n 
1 70  SER n 
1 71  SER n 
1 72  ASN n 
1 73  ARG n 
1 74  THR n 
1 75  ASP n 
1 76  ASP n 
1 77  ASN n 
1 78  PHE n 
1 79  PRO n 
1 80  ALA n 
1 81  THR n 
1 82  SER n 
1 83  PRO n 
1 84  ALA n 
1 85  PHE n 
1 86  GLU n 
1 87  ALA n 
1 88  VAL n 
1 89  ARG n 
1 90  GLU n 
1 91  SER n 
1 92  PRO n 
1 93  GLN n 
1 94  ALA n 
1 95  PHE n 
1 96  ILE n 
1 97  GLY n 
1 98  LEU n 
1 99  ASP n 
1 100 PRO n 
1 101 PRO n 
1 102 GLU n 
1 103 HIS n 
1 104 GLY n 
1 105 THR n 
1 106 ARG n 
1 107 ARG n 
1 108 ARG n 
1 109 MET n 
1 110 THR n 
1 111 ILE n 
1 112 SER n 
1 113 GLU n 
1 114 PHE n 
1 115 THR n 
1 116 VAL n 
1 117 LYS n 
1 118 ARG n 
1 119 ILE n 
1 120 LYS n 
1 121 GLY n 
1 122 MET n 
1 123 ARG n 
1 124 PRO n 
1 125 GLU n 
1 126 VAL n 
1 127 GLU n 
1 128 GLU n 
1 129 VAL n 
1 130 VAL n 
1 131 HIS n 
1 132 GLY n 
1 133 PHE n 
1 134 LEU n 
1 135 ASP n 
1 136 GLU n 
1 137 MET n 
1 138 LEU n 
1 139 ALA n 
1 140 ALA n 
1 141 GLY n 
1 142 PRO n 
1 143 THR n 
1 144 ALA n 
1 145 ASP n 
1 146 LEU n 
1 147 VAL n 
1 148 SER n 
1 149 GLN n 
1 150 PHE n 
1 151 ALA n 
1 152 LEU n 
1 153 PRO n 
1 154 VAL n 
1 155 PRO n 
1 156 SER n 
1 157 MET n 
1 158 VAL n 
1 159 ILE n 
1 160 CYS n 
1 161 ARG n 
1 162 LEU n 
1 163 LEU n 
1 164 GLY n 
1 165 VAL n 
1 166 PRO n 
1 167 TYR n 
1 168 ALA n 
1 169 ASP n 
1 170 HIS n 
1 171 GLU n 
1 172 PHE n 
1 173 PHE n 
1 174 GLN n 
1 175 ASP n 
1 176 ALA n 
1 177 SER n 
1 178 LYS n 
1 179 ARG n 
1 180 LEU n 
1 181 VAL n 
1 182 GLN n 
1 183 SER n 
1 184 THR n 
1 185 ASP n 
1 186 ALA n 
1 187 GLN n 
1 188 SER n 
1 189 ALA n 
1 190 LEU n 
1 191 THR n 
1 192 ALA n 
1 193 ARG n 
1 194 ASN n 
1 195 ASP n 
1 196 LEU n 
1 197 ALA n 
1 198 GLY n 
1 199 TYR n 
1 200 LEU n 
1 201 ASP n 
1 202 GLY n 
1 203 LEU n 
1 204 ILE n 
1 205 THR n 
1 206 GLN n 
1 207 PHE n 
1 208 GLN n 
1 209 THR n 
1 210 GLU n 
1 211 PRO n 
1 212 GLY n 
1 213 ALA n 
1 214 GLY n 
1 215 LEU n 
1 216 VAL n 
1 217 GLY n 
1 218 ALA n 
1 219 LEU n 
1 220 VAL n 
1 221 ALA n 
1 222 ASP n 
1 223 GLN n 
1 224 LEU n 
1 225 ALA n 
1 226 ASN n 
1 227 GLY n 
1 228 GLU n 
1 229 ILE n 
1 230 ASP n 
1 231 ARG n 
1 232 GLU n 
1 233 GLU n 
1 234 LEU n 
1 235 ILE n 
1 236 SER n 
1 237 THR n 
1 238 ALA n 
1 239 MET n 
1 240 LEU n 
1 241 LEU n 
1 242 LEU n 
1 243 ILE n 
1 244 ALA n 
1 245 GLY n 
1 246 HIS n 
1 247 GLU n 
1 248 THR n 
1 249 THR n 
1 250 ALA n 
1 251 SER n 
1 252 MET n 
1 253 THR n 
1 254 SER n 
1 255 LEU n 
1 256 SER n 
1 257 VAL n 
1 258 ILE n 
1 259 THR n 
1 260 LEU n 
1 261 LEU n 
1 262 ASP n 
1 263 HIS n 
1 264 PRO n 
1 265 GLU n 
1 266 GLN n 
1 267 TYR n 
1 268 ALA n 
1 269 ALA n 
1 270 LEU n 
1 271 ARG n 
1 272 ALA n 
1 273 ASP n 
1 274 ARG n 
1 275 SER n 
1 276 LEU n 
1 277 VAL n 
1 278 PRO n 
1 279 GLY n 
1 280 ALA n 
1 281 VAL n 
1 282 GLU n 
1 283 GLU n 
1 284 LEU n 
1 285 LEU n 
1 286 ARG n 
1 287 TYR n 
1 288 LEU n 
1 289 ALA n 
1 290 ILE n 
1 291 ALA n 
1 292 ASP n 
1 293 ILE n 
1 294 ALA n 
1 295 GLY n 
1 296 GLY n 
1 297 ARG n 
1 298 VAL n 
1 299 ALA n 
1 300 THR n 
1 301 ALA n 
1 302 ASP n 
1 303 ILE n 
1 304 GLU n 
1 305 VAL n 
1 306 GLU n 
1 307 GLY n 
1 308 GLN n 
1 309 LEU n 
1 310 ILE n 
1 311 ARG n 
1 312 ALA n 
1 313 GLY n 
1 314 GLU n 
1 315 GLY n 
1 316 VAL n 
1 317 ILE n 
1 318 VAL n 
1 319 VAL n 
1 320 ASN n 
1 321 SER n 
1 322 ILE n 
1 323 ALA n 
1 324 ASN n 
1 325 ARG n 
1 326 ASP n 
1 327 GLY n 
1 328 THR n 
1 329 VAL n 
1 330 TYR n 
1 331 GLU n 
1 332 ASP n 
1 333 PRO n 
1 334 ASP n 
1 335 ALA n 
1 336 LEU n 
1 337 ASP n 
1 338 ILE n 
1 339 HIS n 
1 340 ARG n 
1 341 SER n 
1 342 ALA n 
1 343 ARG n 
1 344 HIS n 
1 345 HIS n 
1 346 LEU n 
1 347 ALA n 
1 348 PHE n 
1 349 GLY n 
1 350 PHE n 
1 351 GLY n 
1 352 VAL n 
1 353 HIS n 
1 354 GLN n 
1 355 CYS n 
1 356 LEU n 
1 357 GLY n 
1 358 GLN n 
1 359 ASN n 
1 360 LEU n 
1 361 ALA n 
1 362 ARG n 
1 363 LEU n 
1 364 GLU n 
1 365 LEU n 
1 366 GLU n 
1 367 VAL n 
1 368 ILE n 
1 369 LEU n 
1 370 ASN n 
1 371 ALA n 
1 372 LEU n 
1 373 MET n 
1 374 ASP n 
1 375 ARG n 
1 376 VAL n 
1 377 PRO n 
1 378 THR n 
1 379 LEU n 
1 380 ARG n 
1 381 LEU n 
1 382 ALA n 
1 383 VAL n 
1 384 PRO n 
1 385 VAL n 
1 386 GLU n 
1 387 GLN n 
1 388 LEU n 
1 389 VAL n 
1 390 LEU n 
1 391 ARG n 
1 392 PRO n 
1 393 GLY n 
1 394 THR n 
1 395 THR n 
1 396 ILE n 
1 397 GLN n 
1 398 GLY n 
1 399 VAL n 
1 400 ASN n 
1 401 GLU n 
1 402 LEU n 
1 403 PRO n 
1 404 VAL n 
1 405 THR n 
1 406 TRP n 
1 407 HIS n 
1 408 HIS n 
1 409 HIS n 
1 410 HIS n 
1 411 HIS n 
1 412 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   412 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'cyp105A1, suaC' 
_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      'Streptomyces griseolus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1909 
_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 
A1L6Q non-polymer         . '(2~{E})-2-[(4~{R})-4-(2-chlorophenyl)-1,3-dithiolan-2-ylidene]-2-imidazol-1-yl-ethanenitrile' 
lanoconazole 'C14 H10 Cl N3 S2' 319.832 
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 
DIF   non-polymer         . '2-[2,6-DICHLOROPHENYL)AMINO]BENZENEACETIC ACID'                                               
DICLOFENAC   'C14 H11 Cl2 N O2' 296.149 
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 
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   ASP 3   3   ?   ?   ?   A . n 
A 1 4   THR 4   4   ?   ?   ?   A . n 
A 1 5   ALA 5   5   ?   ?   ?   A . n 
A 1 6   THR 6   6   ?   ?   ?   A . n 
A 1 7   THR 7   7   7   THR THR A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   GLN 9   9   9   GLN GLN A . n 
A 1 10  THR 10  10  10  THR THR A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  PHE 16  16  16  PHE PHE A . n 
A 1 17  PRO 17  17  17  PRO PRO A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  PRO 27  27  27  PRO PRO A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  TYR 30  30  30  TYR TYR A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  GLN 32  32  32  GLN GLN A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  ARG 42  42  42  ARG ARG A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  TYR 46  46  46  TYR TYR A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  GLN 50  50  50  GLN GLN A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  TRP 52  52  52  TRP TRP A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  VAL 54  54  54  VAL VAL A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  HIS 57  57  57  HIS HIS A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  PRO 67  67  67  PRO PRO A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  SER 71  71  71  SER SER A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  PHE 78  78  78  PHE PHE A . n 
A 1 79  PRO 79  79  79  PRO PRO A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  SER 82  82  82  SER SER A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  PHE 85  85  85  PHE PHE A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  GLN 93  93  93  GLN GLN A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 PRO 101 101 101 PRO PRO A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 HIS 103 103 103 HIS HIS A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 ARG 106 106 106 ARG ARG A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 MET 109 109 109 MET MET A . n 
A 1 110 THR 110 110 110 THR THR A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 THR 115 115 115 THR THR A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 ILE 119 119 119 ILE ILE A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 MET 122 122 122 MET MET A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 GLU 128 128 128 GLU GLU A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 HIS 131 131 131 HIS HIS A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 MET 137 137 137 MET MET A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 GLN 149 149 149 GLN GLN A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 VAL 154 154 154 VAL VAL A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 MET 157 157 157 MET MET A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 ASP 169 169 169 ASP ASP A . n 
A 1 170 HIS 170 170 170 HIS HIS A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 PHE 172 172 172 PHE PHE A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 GLN 174 174 174 GLN GLN A . n 
A 1 175 ASP 175 175 175 ASP ASP A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 SER 177 177 177 SER SER A . n 
A 1 178 LYS 178 178 178 LYS LYS A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 GLN 182 182 182 GLN GLN A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 THR 184 184 184 THR THR A . n 
A 1 185 ASP 185 185 185 ASP ASP A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 GLN 187 187 187 GLN GLN A . n 
A 1 188 SER 188 188 188 SER SER A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 THR 191 191 191 THR THR A . n 
A 1 192 ALA 192 192 192 ALA ALA A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 ASN 194 194 194 ASN ASN A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 LEU 196 196 196 LEU LEU A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 ASP 201 201 201 ASP ASP A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 ILE 204 204 204 ILE ILE A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 GLN 206 206 206 GLN GLN A . n 
A 1 207 PHE 207 207 207 PHE PHE A . n 
A 1 208 GLN 208 208 208 GLN GLN A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 GLY 212 212 212 GLY GLY A . n 
A 1 213 ALA 213 213 213 ALA ALA A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 ALA 218 218 218 ALA ALA A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 VAL 220 220 220 VAL VAL A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 GLN 223 223 223 GLN GLN A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 ASN 226 226 226 ASN ASN A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 ARG 231 231 231 ARG ARG A . n 
A 1 232 GLU 232 232 232 GLU GLU A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 SER 236 236 236 SER SER A . n 
A 1 237 THR 237 237 237 THR THR A . n 
A 1 238 ALA 238 238 238 ALA ALA A . n 
A 1 239 MET 239 239 239 MET MET A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 THR 248 248 248 THR THR A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 SER 251 251 251 SER SER A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 THR 253 253 253 THR THR A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 ASP 262 262 262 ASP ASP A . n 
A 1 263 HIS 263 263 263 HIS HIS A . n 
A 1 264 PRO 264 264 264 PRO PRO A . n 
A 1 265 GLU 265 265 265 GLU GLU A . n 
A 1 266 GLN 266 266 266 GLN GLN A . n 
A 1 267 TYR 267 267 267 TYR TYR A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 ARG 271 271 271 ARG ARG A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 ASP 273 273 273 ASP ASP A . n 
A 1 274 ARG 274 274 274 ARG ARG A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 VAL 277 277 277 VAL VAL A . n 
A 1 278 PRO 278 278 278 PRO PRO A . n 
A 1 279 GLY 279 279 279 GLY GLY A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 VAL 281 281 281 VAL VAL A . n 
A 1 282 GLU 282 282 282 GLU GLU A . n 
A 1 283 GLU 283 283 283 GLU GLU A . n 
A 1 284 LEU 284 284 284 LEU LEU A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 ARG 286 286 286 ARG ARG A . n 
A 1 287 TYR 287 287 287 TYR TYR A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 ILE 290 290 290 ILE ILE A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 ASP 292 292 292 ASP ASP A . n 
A 1 293 ILE 293 293 293 ILE ILE A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 GLY 295 295 295 GLY GLY A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 ARG 297 297 297 ARG ARG A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 THR 300 300 300 THR THR A . n 
A 1 301 ALA 301 301 301 ALA ALA A . n 
A 1 302 ASP 302 302 302 ASP ASP A . n 
A 1 303 ILE 303 303 303 ILE ILE A . n 
A 1 304 GLU 304 304 304 GLU GLU A . n 
A 1 305 VAL 305 305 305 VAL VAL A . n 
A 1 306 GLU 306 306 306 GLU GLU A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 GLN 308 308 308 GLN GLN A . n 
A 1 309 LEU 309 309 309 LEU LEU A . n 
A 1 310 ILE 310 310 310 ILE ILE A . n 
A 1 311 ARG 311 311 311 ARG ARG A . n 
A 1 312 ALA 312 312 312 ALA ALA A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 GLU 314 314 314 GLU GLU A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 ILE 317 317 317 ILE ILE A . n 
A 1 318 VAL 318 318 318 VAL VAL A . n 
A 1 319 VAL 319 319 319 VAL VAL A . n 
A 1 320 ASN 320 320 320 ASN ASN A . n 
A 1 321 SER 321 321 321 SER SER A . n 
A 1 322 ILE 322 322 322 ILE ILE A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 ASN 324 324 324 ASN ASN A . n 
A 1 325 ARG 325 325 325 ARG ARG A . n 
A 1 326 ASP 326 326 326 ASP ASP A . n 
A 1 327 GLY 327 327 327 GLY GLY A . n 
A 1 328 THR 328 328 328 THR THR A . n 
A 1 329 VAL 329 329 329 VAL VAL A . n 
A 1 330 TYR 330 330 330 TYR TYR A . n 
A 1 331 GLU 331 331 331 GLU GLU 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 ASP 334 334 334 ASP ASP A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 LEU 336 336 336 LEU LEU A . n 
A 1 337 ASP 337 337 337 ASP ASP A . n 
A 1 338 ILE 338 338 338 ILE ILE A . n 
A 1 339 HIS 339 339 339 HIS HIS A . n 
A 1 340 ARG 340 340 340 ARG ARG A . n 
A 1 341 SER 341 341 341 SER SER A . n 
A 1 342 ALA 342 342 342 ALA ALA A . n 
A 1 343 ARG 343 343 343 ARG ARG A . n 
A 1 344 HIS 344 344 344 HIS HIS A . n 
A 1 345 HIS 345 345 345 HIS HIS A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 PHE 348 348 348 PHE PHE A . n 
A 1 349 GLY 349 349 349 GLY GLY A . n 
A 1 350 PHE 350 350 350 PHE PHE A . n 
A 1 351 GLY 351 351 351 GLY GLY A . n 
A 1 352 VAL 352 352 352 VAL VAL A . n 
A 1 353 HIS 353 353 353 HIS HIS A . n 
A 1 354 GLN 354 354 354 GLN GLN A . n 
A 1 355 CYS 355 355 355 CYS CYS A . n 
A 1 356 LEU 356 356 356 LEU LEU 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 ASN 359 359 359 ASN ASN A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 ARG 362 362 362 ARG ARG A . n 
A 1 363 LEU 363 363 363 LEU LEU A . n 
A 1 364 GLU 364 364 364 GLU GLU A . n 
A 1 365 LEU 365 365 365 LEU LEU A . n 
A 1 366 GLU 366 366 366 GLU GLU A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 ILE 368 368 368 ILE ILE A . n 
A 1 369 LEU 369 369 369 LEU LEU A . n 
A 1 370 ASN 370 370 370 ASN ASN A . n 
A 1 371 ALA 371 371 371 ALA ALA A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 MET 373 373 373 MET MET A . n 
A 1 374 ASP 374 374 374 ASP ASP A . n 
A 1 375 ARG 375 375 375 ARG ARG A . n 
A 1 376 VAL 376 376 376 VAL VAL A . n 
A 1 377 PRO 377 377 377 PRO PRO A . n 
A 1 378 THR 378 378 378 THR THR A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 ARG 380 380 380 ARG ARG A . n 
A 1 381 LEU 381 381 381 LEU LEU A . n 
A 1 382 ALA 382 382 382 ALA ALA A . n 
A 1 383 VAL 383 383 383 VAL VAL A . n 
A 1 384 PRO 384 384 384 PRO PRO A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 GLU 386 386 386 GLU GLU A . n 
A 1 387 GLN 387 387 387 GLN GLN A . n 
A 1 388 LEU 388 388 388 LEU LEU A . n 
A 1 389 VAL 389 389 389 VAL VAL A . n 
A 1 390 LEU 390 390 390 LEU LEU A . n 
A 1 391 ARG 391 391 391 ARG ARG A . n 
A 1 392 PRO 392 392 392 PRO PRO A . n 
A 1 393 GLY 393 393 393 GLY GLY A . n 
A 1 394 THR 394 394 394 THR THR A . n 
A 1 395 THR 395 395 395 THR THR A . n 
A 1 396 ILE 396 396 396 ILE ILE A . n 
A 1 397 GLN 397 397 397 GLN GLN A . n 
A 1 398 GLY 398 398 398 GLY GLY A . n 
A 1 399 VAL 399 399 399 VAL VAL A . n 
A 1 400 ASN 400 400 400 ASN ASN A . n 
A 1 401 GLU 401 401 401 GLU GLU A . n 
A 1 402 LEU 402 402 402 LEU LEU A . n 
A 1 403 PRO 403 403 403 PRO PRO A . n 
A 1 404 VAL 404 404 404 VAL VAL A . n 
A 1 405 THR 405 405 405 THR THR A . n 
A 1 406 TRP 406 406 406 TRP TRP A . n 
A 1 407 HIS 407 407 407 HIS HIS A . n 
A 1 408 HIS 408 408 408 HIS HIS A . n 
A 1 409 HIS 409 409 ?   ?   ?   A . n 
A 1 410 HIS 410 410 ?   ?   ?   A . n 
A 1 411 HIS 411 411 ?   ?   ?   A . n 
A 1 412 HIS 412 412 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 DIF   ? ? DIF   ? ? 'SUBJECT OF INVESTIGATION' ? 
2 HEM   ? ? HEM   ? ? 'SUBJECT OF INVESTIGATION' ? 
3 A1L6Q ? ? A1L6Q ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
B 2 HEM   1   501 501 HEM   HEM A . 
C 3 DIF   1   502 502 DIF   DIF A . 
D 4 A1L6Q 1   503 503 A1L6Q LAN A . 
E 5 HOH   1   601 113 HOH   HOH A . 
E 5 HOH   2   602 157 HOH   HOH A . 
E 5 HOH   3   603 46  HOH   HOH A . 
E 5 HOH   4   604 117 HOH   HOH A . 
E 5 HOH   5   605 36  HOH   HOH A . 
E 5 HOH   6   606 44  HOH   HOH A . 
E 5 HOH   7   607 112 HOH   HOH A . 
E 5 HOH   8   608 37  HOH   HOH A . 
E 5 HOH   9   609 165 HOH   HOH A . 
E 5 HOH   10  610 21  HOH   HOH A . 
E 5 HOH   11  611 16  HOH   HOH A . 
E 5 HOH   12  612 167 HOH   HOH A . 
E 5 HOH   13  613 40  HOH   HOH A . 
E 5 HOH   14  614 177 HOH   HOH A . 
E 5 HOH   15  615 91  HOH   HOH A . 
E 5 HOH   16  616 108 HOH   HOH A . 
E 5 HOH   17  617 125 HOH   HOH A . 
E 5 HOH   18  618 71  HOH   HOH A . 
E 5 HOH   19  619 172 HOH   HOH A . 
E 5 HOH   20  620 51  HOH   HOH A . 
E 5 HOH   21  621 187 HOH   HOH A . 
E 5 HOH   22  622 7   HOH   HOH A . 
E 5 HOH   23  623 158 HOH   HOH A . 
E 5 HOH   24  624 140 HOH   HOH A . 
E 5 HOH   25  625 80  HOH   HOH A . 
E 5 HOH   26  626 26  HOH   HOH A . 
E 5 HOH   27  627 123 HOH   HOH A . 
E 5 HOH   28  628 59  HOH   HOH A . 
E 5 HOH   29  629 6   HOH   HOH A . 
E 5 HOH   30  630 119 HOH   HOH A . 
E 5 HOH   31  631 4   HOH   HOH A . 
E 5 HOH   32  632 103 HOH   HOH A . 
E 5 HOH   33  633 38  HOH   HOH A . 
E 5 HOH   34  634 20  HOH   HOH A . 
E 5 HOH   35  635 94  HOH   HOH A . 
E 5 HOH   36  636 86  HOH   HOH A . 
E 5 HOH   37  637 118 HOH   HOH A . 
E 5 HOH   38  638 78  HOH   HOH A . 
E 5 HOH   39  639 66  HOH   HOH A . 
E 5 HOH   40  640 47  HOH   HOH A . 
E 5 HOH   41  641 5   HOH   HOH A . 
E 5 HOH   42  642 85  HOH   HOH A . 
E 5 HOH   43  643 29  HOH   HOH A . 
E 5 HOH   44  644 60  HOH   HOH A . 
E 5 HOH   45  645 92  HOH   HOH A . 
E 5 HOH   46  646 131 HOH   HOH A . 
E 5 HOH   47  647 79  HOH   HOH A . 
E 5 HOH   48  648 9   HOH   HOH A . 
E 5 HOH   49  649 120 HOH   HOH A . 
E 5 HOH   50  650 100 HOH   HOH A . 
E 5 HOH   51  651 55  HOH   HOH A . 
E 5 HOH   52  652 1   HOH   HOH A . 
E 5 HOH   53  653 28  HOH   HOH A . 
E 5 HOH   54  654 32  HOH   HOH A . 
E 5 HOH   55  655 194 HOH   HOH A . 
E 5 HOH   56  656 196 HOH   HOH A . 
E 5 HOH   57  657 132 HOH   HOH A . 
E 5 HOH   58  658 201 HOH   HOH A . 
E 5 HOH   59  659 65  HOH   HOH A . 
E 5 HOH   60  660 90  HOH   HOH A . 
E 5 HOH   61  661 96  HOH   HOH A . 
E 5 HOH   62  662 115 HOH   HOH A . 
E 5 HOH   63  663 35  HOH   HOH A . 
E 5 HOH   64  664 195 HOH   HOH A . 
E 5 HOH   65  665 147 HOH   HOH A . 
E 5 HOH   66  666 22  HOH   HOH A . 
E 5 HOH   67  667 129 HOH   HOH A . 
E 5 HOH   68  668 57  HOH   HOH A . 
E 5 HOH   69  669 199 HOH   HOH A . 
E 5 HOH   70  670 64  HOH   HOH A . 
E 5 HOH   71  671 63  HOH   HOH A . 
E 5 HOH   72  672 105 HOH   HOH A . 
E 5 HOH   73  673 61  HOH   HOH A . 
E 5 HOH   74  674 54  HOH   HOH A . 
E 5 HOH   75  675 25  HOH   HOH A . 
E 5 HOH   76  676 136 HOH   HOH A . 
E 5 HOH   77  677 15  HOH   HOH A . 
E 5 HOH   78  678 181 HOH   HOH A . 
E 5 HOH   79  679 166 HOH   HOH A . 
E 5 HOH   80  680 95  HOH   HOH A . 
E 5 HOH   81  681 89  HOH   HOH A . 
E 5 HOH   82  682 126 HOH   HOH A . 
E 5 HOH   83  683 109 HOH   HOH A . 
E 5 HOH   84  684 84  HOH   HOH A . 
E 5 HOH   85  685 82  HOH   HOH A . 
E 5 HOH   86  686 88  HOH   HOH A . 
E 5 HOH   87  687 33  HOH   HOH A . 
E 5 HOH   88  688 97  HOH   HOH A . 
E 5 HOH   89  689 12  HOH   HOH A . 
E 5 HOH   90  690 99  HOH   HOH A . 
E 5 HOH   91  691 70  HOH   HOH A . 
E 5 HOH   92  692 171 HOH   HOH A . 
E 5 HOH   93  693 41  HOH   HOH A . 
E 5 HOH   94  694 188 HOH   HOH A . 
E 5 HOH   95  695 52  HOH   HOH A . 
E 5 HOH   96  696 75  HOH   HOH A . 
E 5 HOH   97  697 152 HOH   HOH A . 
E 5 HOH   98  698 122 HOH   HOH A . 
E 5 HOH   99  699 76  HOH   HOH A . 
E 5 HOH   100 700 81  HOH   HOH A . 
E 5 HOH   101 701 74  HOH   HOH A . 
E 5 HOH   102 702 121 HOH   HOH A . 
E 5 HOH   103 703 53  HOH   HOH A . 
E 5 HOH   104 704 178 HOH   HOH A . 
E 5 HOH   105 705 8   HOH   HOH A . 
E 5 HOH   106 706 43  HOH   HOH A . 
E 5 HOH   107 707 98  HOH   HOH A . 
E 5 HOH   108 708 110 HOH   HOH A . 
E 5 HOH   109 709 11  HOH   HOH A . 
E 5 HOH   110 710 42  HOH   HOH A . 
E 5 HOH   111 711 34  HOH   HOH A . 
E 5 HOH   112 712 48  HOH   HOH A . 
E 5 HOH   113 713 163 HOH   HOH A . 
E 5 HOH   114 714 17  HOH   HOH A . 
E 5 HOH   115 715 149 HOH   HOH A . 
E 5 HOH   116 716 160 HOH   HOH A . 
E 5 HOH   117 717 93  HOH   HOH A . 
E 5 HOH   118 718 50  HOH   HOH A . 
E 5 HOH   119 719 72  HOH   HOH A . 
E 5 HOH   120 720 153 HOH   HOH A . 
E 5 HOH   121 721 14  HOH   HOH A . 
E 5 HOH   122 722 27  HOH   HOH A . 
E 5 HOH   123 723 142 HOH   HOH A . 
E 5 HOH   124 724 24  HOH   HOH A . 
E 5 HOH   125 725 180 HOH   HOH A . 
E 5 HOH   126 726 58  HOH   HOH A . 
E 5 HOH   127 727 137 HOH   HOH A . 
E 5 HOH   128 728 69  HOH   HOH A . 
E 5 HOH   129 729 191 HOH   HOH A . 
E 5 HOH   130 730 68  HOH   HOH A . 
E 5 HOH   131 731 19  HOH   HOH A . 
E 5 HOH   132 732 144 HOH   HOH A . 
E 5 HOH   133 733 116 HOH   HOH A . 
E 5 HOH   134 734 13  HOH   HOH A . 
E 5 HOH   135 735 182 HOH   HOH A . 
E 5 HOH   136 736 31  HOH   HOH A . 
E 5 HOH   137 737 30  HOH   HOH A . 
E 5 HOH   138 738 173 HOH   HOH A . 
E 5 HOH   139 739 39  HOH   HOH A . 
E 5 HOH   140 740 128 HOH   HOH A . 
E 5 HOH   141 741 45  HOH   HOH A . 
E 5 HOH   142 742 197 HOH   HOH A . 
E 5 HOH   143 743 73  HOH   HOH A . 
E 5 HOH   144 744 174 HOH   HOH A . 
E 5 HOH   145 745 127 HOH   HOH A . 
E 5 HOH   146 746 176 HOH   HOH A . 
E 5 HOH   147 747 130 HOH   HOH A . 
E 5 HOH   148 748 133 HOH   HOH A . 
E 5 HOH   149 749 62  HOH   HOH A . 
E 5 HOH   150 750 202 HOH   HOH A . 
E 5 HOH   151 751 83  HOH   HOH A . 
E 5 HOH   152 752 141 HOH   HOH A . 
E 5 HOH   153 753 10  HOH   HOH A . 
E 5 HOH   154 754 184 HOH   HOH A . 
E 5 HOH   155 755 18  HOH   HOH A . 
E 5 HOH   156 756 102 HOH   HOH A . 
E 5 HOH   157 757 77  HOH   HOH A . 
E 5 HOH   158 758 3   HOH   HOH A . 
E 5 HOH   159 759 87  HOH   HOH A . 
E 5 HOH   160 760 145 HOH   HOH A . 
E 5 HOH   161 761 186 HOH   HOH A . 
E 5 HOH   162 762 146 HOH   HOH A . 
E 5 HOH   163 763 150 HOH   HOH A . 
E 5 HOH   164 764 56  HOH   HOH A . 
E 5 HOH   165 765 114 HOH   HOH A . 
E 5 HOH   166 766 200 HOH   HOH A . 
E 5 HOH   167 767 183 HOH   HOH A . 
E 5 HOH   168 768 175 HOH   HOH A . 
E 5 HOH   169 769 154 HOH   HOH A . 
E 5 HOH   170 770 67  HOH   HOH A . 
E 5 HOH   171 771 106 HOH   HOH A . 
E 5 HOH   172 772 2   HOH   HOH A . 
E 5 HOH   173 773 185 HOH   HOH A . 
E 5 HOH   174 774 204 HOH   HOH A . 
E 5 HOH   175 775 135 HOH   HOH A . 
E 5 HOH   176 776 193 HOH   HOH A . 
E 5 HOH   177 777 168 HOH   HOH A . 
E 5 HOH   178 778 151 HOH   HOH A . 
E 5 HOH   179 779 164 HOH   HOH A . 
E 5 HOH   180 780 198 HOH   HOH A . 
E 5 HOH   181 781 159 HOH   HOH A . 
E 5 HOH   182 782 107 HOH   HOH A . 
E 5 HOH   183 783 169 HOH   HOH A . 
E 5 HOH   184 784 111 HOH   HOH A . 
E 5 HOH   185 785 134 HOH   HOH A . 
E 5 HOH   186 786 203 HOH   HOH A . 
E 5 HOH   187 787 138 HOH   HOH A . 
E 5 HOH   188 788 170 HOH   HOH A . 
E 5 HOH   189 789 155 HOH   HOH A . 
E 5 HOH   190 790 162 HOH   HOH A . 
E 5 HOH   191 791 190 HOH   HOH A . 
E 5 HOH   192 792 161 HOH   HOH A . 
E 5 HOH   193 793 104 HOH   HOH A . 
E 5 HOH   194 794 124 HOH   HOH A . 
E 5 HOH   195 795 179 HOH   HOH A . 
E 5 HOH   196 796 156 HOH   HOH A . 
E 5 HOH   197 797 139 HOH   HOH A . 
E 5 HOH   198 798 148 HOH   HOH A . 
E 5 HOH   199 799 49  HOH   HOH A . 
E 5 HOH   200 800 189 HOH   HOH A . 
E 5 HOH   201 801 143 HOH   HOH A . 
E 5 HOH   202 802 101 HOH   HOH A . 
E 5 HOH   203 803 23  HOH   HOH A . 
E 5 HOH   204 804 192 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.18.2_3874 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KW5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.613 
_cell.length_a_esd                 ? 
_cell.length_b                     53.556 
_cell.length_b_esd                 ? 
_cell.length_c                     141.247 
_cell.length_c_esd                 ? 
_cell.volume                       397997.580 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9KW5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9KW5 
_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             2.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.38 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    '26% (w/v) PEG 2000 MME, 50mM Bis-Tris pH 6.5, 0.2M NaCl' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            283 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     95 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-05-25 
_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                    'SI(111)' 
_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   0.98 
_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                        'PHOTON FACTORY BEAMLINE BL-17A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL-17A 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
# 
_reflns.B_iso_Wilson_estimate                          33.89 
_reflns.entry_id                                       9KW5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.10 
_reflns.d_resolution_low                               49.30 
_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                                     24098 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.8 
_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                                0.126 
_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                              0.107 
_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                                    2.10 
_reflns_shell.d_res_low                                     2.16 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1925 
_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                               5.9 
_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                               0.893 
_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                                  0.815 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.740 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               38.42 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9KW5 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.10 
_refine.ls_d_res_low                             49.30 
_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                     24015 
_refine.ls_number_reflns_R_free                  1134 
_refine.ls_number_reflns_R_work                  22881 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.89 
_refine.ls_percent_reflns_R_free                 4.72 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2143 
_refine.ls_R_factor_R_free                       0.2552 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2123 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 27.0770 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2508 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        49.30 
_refine_hist.number_atoms_solvent             204 
_refine_hist.number_atoms_total               3367 
_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        3081 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         82 
_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' ? 0.0029  ? 3304 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5676  ? 4529 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0406  ? 507  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0035  ? 603  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 17.3369 ? 1214 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.10 2.20  . . 138 2785 99.63  . . . . 0.2675 . . . . . . . . . . . 0.2860 
'X-RAY DIFFRACTION' 2.20 2.31  . . 156 2787 99.83  . . . . 0.2651 . . . . . . . . . . . 0.3391 
'X-RAY DIFFRACTION' 2.31 2.46  . . 154 2803 99.86  . . . . 0.2405 . . . . . . . . . . . 0.3029 
'X-RAY DIFFRACTION' 2.46 2.65  . . 137 2839 99.97  . . . . 0.2422 . . . . . . . . . . . 0.3063 
'X-RAY DIFFRACTION' 2.65 2.91  . . 106 2881 99.90  . . . . 0.2398 . . . . . . . . . . . 0.2687 
'X-RAY DIFFRACTION' 2.91 3.33  . . 135 2863 99.97  . . . . 0.2231 . . . . . . . . . . . 0.2459 
'X-RAY DIFFRACTION' 3.33 4.20  . . 150 2889 100.00 . . . . 0.1906 . . . . . . . . . . . 0.2490 
'X-RAY DIFFRACTION' 4.20 49.30 . . 158 3034 99.97  . . . . 0.1846 . . . . . . . . . . . 0.2198 
# 
_struct.entry_id                     9KW5 
_struct.title                        'Crystal structure of CYP105A1 R84A, diclofenac and lanoconazole complex' 
_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        9KW5 
_struct_keywords.text            'Cytochrome P450, Substrate, Inhibitor, Heme, ESI complex, 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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CPXE_STRGO 
_struct_ref.pdbx_db_accession          P18326 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTDTATTPQTTDAPAFPSNRSCPYQLPDGYAQLRDTPGPLHRVTLYDGRQAWVVTKHEAARKLLGDPRLSSNRTDDNFPA
TSPRFEAVRESPQAFIGLDPPEHGTRRRMTISEFTVKRIKGMRPEVEEVVHGFLDEMLAAGPTADLVSQFALPVPSMVIC
RLLGVPYADHEFFQDASKRLVQSTDAQSALTARNDLAGYLDGLITQFQTEPGAGLVGALVADQLANGEIDREELISTAML
LLIAGHETTASMTSLSVITLLDHPEQYAALRADRSLVPGAVEELLRYLAIADIAGGRVATADIEVEGHLIRAGEGVIVVN
SIANRDGTVYEDPDALDIHRSARHHLAFGFGVHQCLGQNLARLELEVILNALMDRVPTLRLAVPVEQLVLRPGTTIQGVN
ELPVTW
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9KW5 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 406 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P18326 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  406 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       406 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9KW5 ALA A 84  ? UNP P18326 ARG 84  'engineered mutation' 84  1 
1 9KW5 GLN A 308 ? UNP P18326 HIS 308 variant               308 2 
1 9KW5 HIS A 407 ? UNP P18326 ?   ?   'expression tag'      407 3 
1 9KW5 HIS A 408 ? UNP P18326 ?   ?   'expression tag'      408 4 
1 9KW5 HIS A 409 ? UNP P18326 ?   ?   'expression tag'      409 5 
1 9KW5 HIS A 410 ? UNP P18326 ?   ?   'expression tag'      410 6 
1 9KW5 HIS A 411 ? UNP P18326 ?   ?   'expression tag'      411 7 
1 9KW5 HIS A 412 ? UNP P18326 ?   ?   'expression tag'      412 8 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 1890  ? 
1 MORE         -31   ? 
1 'SSA (A^2)'  16430 ? 
# 
_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 
# 
_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 27  ? THR A 36  ? PRO A 27  THR A 36  1 ? 10 
HELX_P HELX_P2  AA2 LYS A 56  ? GLY A 65  ? LYS A 56  GLY A 65  1 ? 10 
HELX_P HELX_P3  AA3 SER A 82  ? ALA A 84  ? SER A 82  ALA A 84  5 ? 3  
HELX_P HELX_P4  AA4 PHE A 85  ? GLU A 90  ? PHE A 85  GLU A 90  1 ? 6  
HELX_P HELX_P5  AA5 ALA A 94  ? LEU A 98  ? ALA A 94  LEU A 98  5 ? 5  
HELX_P HELX_P6  AA6 PRO A 101 ? ARG A 108 ? PRO A 101 ARG A 108 1 ? 8  
HELX_P HELX_P7  AA7 MET A 109 ? PHE A 114 ? MET A 109 PHE A 114 5 ? 6  
HELX_P HELX_P8  AA8 THR A 115 ? MET A 122 ? THR A 115 MET A 122 1 ? 8  
HELX_P HELX_P9  AA9 MET A 122 ? GLY A 141 ? MET A 122 GLY A 141 1 ? 20 
HELX_P HELX_P10 AB1 LEU A 146 ? PHE A 150 ? LEU A 146 PHE A 150 1 ? 5  
HELX_P HELX_P11 AB2 LEU A 152 ? GLY A 164 ? LEU A 152 GLY A 164 1 ? 13 
HELX_P HELX_P12 AB3 PRO A 166 ? ALA A 168 ? PRO A 166 ALA A 168 5 ? 3  
HELX_P HELX_P13 AB4 ASP A 169 ? SER A 183 ? ASP A 169 SER A 183 1 ? 15 
HELX_P HELX_P14 AB5 ASP A 185 ? GLU A 210 ? ASP A 185 GLU A 210 1 ? 26 
HELX_P HELX_P15 AB6 ALA A 213 ? ASP A 222 ? ALA A 213 ASP A 222 1 ? 10 
HELX_P HELX_P16 AB7 ASP A 230 ? ASP A 262 ? ASP A 230 ASP A 262 1 ? 33 
HELX_P HELX_P17 AB8 HIS A 263 ? ASP A 273 ? HIS A 263 ASP A 273 1 ? 11 
HELX_P HELX_P18 AB9 LEU A 276 ? ALA A 289 ? LEU A 276 ALA A 289 1 ? 14 
HELX_P HELX_P19 AC1 VAL A 319 ? ASN A 324 ? VAL A 319 ASN A 324 1 ? 6  
HELX_P HELX_P20 AC2 GLY A 357 ? VAL A 376 ? GLY A 357 VAL A 376 1 ? 20 
HELX_P HELX_P21 AC3 PRO A 384 ? LEU A 388 ? PRO A 384 LEU A 388 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 355 SG ? ? ? 1_555 B HEM   . FE ? ? A CYS 355 A HEM   501 1_555 ? ? ? ? ? ? ? 2.291 ? ? 
metalc2 metalc ? ? B HEM .   FE ? ? ? 1_555 D A1L6Q . N5 ? ? A HEM 501 A A1L6Q 503 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
# 
_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 355 ? A CYS 355 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 NA ? B HEM   . ? A HEM   501 ? 1_555 100.5 ? 
2  SG ? A CYS 355 ? A CYS 355 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 NB ? B HEM   . ? A HEM   501 ? 1_555 87.6  ? 
3  NA ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 NB ? B HEM   . ? A HEM   501 ? 1_555 88.7  ? 
4  SG ? A CYS 355 ? A CYS 355 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 NC ? B HEM   . ? A HEM   501 ? 1_555 82.7  ? 
5  NA ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 NC ? B HEM   . ? A HEM   501 ? 1_555 176.7 ? 
6  NB ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 NC ? B HEM   . ? A HEM   501 ? 1_555 91.4  ? 
7  SG ? A CYS 355 ? A CYS 355 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 ND ? B HEM   . ? A HEM   501 ? 1_555 95.5  ? 
8  NA ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 ND ? B HEM   . ? A HEM   501 ? 1_555 90.6  ? 
9  NB ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 ND ? B HEM   . ? A HEM   501 ? 1_555 176.9 ? 
10 NC ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 ND ? B HEM   . ? A HEM   501 ? 1_555 89.1  ? 
11 SG ? A CYS 355 ? A CYS 355 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 N5 ? D A1L6Q . ? A A1L6Q 503 ? 1_555 172.4 ? 
12 NA ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 N5 ? D A1L6Q . ? A A1L6Q 503 ? 1_555 86.9  ? 
13 NB ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 N5 ? D A1L6Q . ? A A1L6Q 503 ? 1_555 94.1  ? 
14 NC ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 N5 ? D A1L6Q . ? A A1L6Q 503 ? 1_555 89.8  ? 
15 ND ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 N5 ? D A1L6Q . ? A A1L6Q 503 ? 1_555 82.9  ? 
# 
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 16  A . ? PHE 16  A PRO 17  A ? PRO 17  A 1 2.90 
2 PRO 100 A . ? PRO 100 A PRO 101 A ? PRO 101 A 1 1.38 
3 PRO 142 A . ? PRO 142 A THR 143 A ? THR 143 A 1 2.09 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 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 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 40  ? THR A 44  ? LEU A 40  THR A 44  
AA1 2 GLN A 50  ? VAL A 54  ? GLN A 50  VAL A 54  
AA1 3 GLY A 315 ? VAL A 318 ? GLY A 315 VAL A 318 
AA1 4 GLY A 296 ? ALA A 299 ? GLY A 296 ALA A 299 
AA1 5 LEU A 69  ? SER A 70  ? LEU A 69  SER A 70  
AA2 1 ALA A 144 ? ASP A 145 ? ALA A 144 ASP A 145 
AA2 2 PRO A 403 ? THR A 405 ? PRO A 403 THR A 405 
AA2 3 ARG A 380 ? LEU A 381 ? ARG A 380 LEU A 381 
AA3 1 ILE A 303 ? VAL A 305 ? ILE A 303 VAL A 305 
AA3 2 GLN A 308 ? ILE A 310 ? GLN A 308 ILE A 310 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N HIS A 41  ? N HIS A 41  O VAL A 53  ? O VAL A 53  
AA1 2 3 N TRP A 52  ? N TRP A 52  O GLY A 315 ? O GLY A 315 
AA1 3 4 O VAL A 316 ? O VAL A 316 N ARG A 297 ? N ARG A 297 
AA1 4 5 O VAL A 298 ? O VAL A 298 N SER A 70  ? N SER A 70  
AA2 1 2 N ALA A 144 ? N ALA A 144 O VAL A 404 ? O VAL A 404 
AA2 2 3 O THR A 405 ? O THR A 405 N ARG A 380 ? N ARG A 380 
AA3 1 2 N ILE A 303 ? N ILE A 303 O ILE A 310 ? O ILE A 310 
# 
_pdbx_entry_details.entry_id                   9KW5 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
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 PHE A 150 ? ? -153.29 -49.75 
2 1 ASP A 222 ? ? -110.26 -78.35 
3 1 ALA A 289 ? ? 33.45   64.20  
4 1 ALA A 294 ? ? -89.07  45.66  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
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 ASP 3   ? A ASP 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 THR 6   ? A THR 6   
7  1 Y 1 A HIS 409 ? A HIS 409 
8  1 Y 1 A HIS 410 ? A HIS 410 
9  1 Y 1 A HIS 411 ? A HIS 411 
10 1 Y 1 A HIS 412 ? A HIS 412 
# 
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 
A1L6Q C10  C  N N 1   
A1L6Q C11  C  Y N 2   
A1L6Q C7   C  N R 3   
A1L6Q C8   C  N N 4   
A1L6Q C9   C  Y N 5   
A1L6Q C12  C  Y N 6   
A1L6Q C13  C  N N 7   
A1L6Q C20  C  Y N 8   
A1L6Q C14  C  Y N 9   
A1L6Q C15  C  Y N 10  
A1L6Q C16  C  Y N 11  
A1L6Q C17  C  Y N 12  
A1L6Q C19  C  N N 13  
A1L6Q C18  C  Y N 14  
A1L6Q N4   N  Y N 15  
A1L6Q N5   N  Y N 16  
A1L6Q N6   N  N N 17  
A1L6Q S2   S  N N 18  
A1L6Q S3   S  N N 19  
A1L6Q CL1  CL N N 20  
A1L6Q H1   H  N N 21  
A1L6Q H2   H  N N 22  
A1L6Q H3   H  N N 23  
A1L6Q H4   H  N N 24  
A1L6Q H5   H  N N 25  
A1L6Q H6   H  N N 26  
A1L6Q H7   H  N N 27  
A1L6Q H8   H  N N 28  
A1L6Q H9   H  N N 29  
A1L6Q H10  H  N N 30  
ALA   N    N  N N 31  
ALA   CA   C  N S 32  
ALA   C    C  N N 33  
ALA   O    O  N N 34  
ALA   CB   C  N N 35  
ALA   OXT  O  N N 36  
ALA   H    H  N N 37  
ALA   H2   H  N N 38  
ALA   HA   H  N N 39  
ALA   HB1  H  N N 40  
ALA   HB2  H  N N 41  
ALA   HB3  H  N N 42  
ALA   HXT  H  N N 43  
ARG   N    N  N N 44  
ARG   CA   C  N S 45  
ARG   C    C  N N 46  
ARG   O    O  N N 47  
ARG   CB   C  N N 48  
ARG   CG   C  N N 49  
ARG   CD   C  N N 50  
ARG   NE   N  N N 51  
ARG   CZ   C  N N 52  
ARG   NH1  N  N N 53  
ARG   NH2  N  N N 54  
ARG   OXT  O  N N 55  
ARG   H    H  N N 56  
ARG   H2   H  N N 57  
ARG   HA   H  N N 58  
ARG   HB2  H  N N 59  
ARG   HB3  H  N N 60  
ARG   HG2  H  N N 61  
ARG   HG3  H  N N 62  
ARG   HD2  H  N N 63  
ARG   HD3  H  N N 64  
ARG   HE   H  N N 65  
ARG   HH11 H  N N 66  
ARG   HH12 H  N N 67  
ARG   HH21 H  N N 68  
ARG   HH22 H  N N 69  
ARG   HXT  H  N N 70  
ASN   N    N  N N 71  
ASN   CA   C  N S 72  
ASN   C    C  N N 73  
ASN   O    O  N N 74  
ASN   CB   C  N N 75  
ASN   CG   C  N N 76  
ASN   OD1  O  N N 77  
ASN   ND2  N  N N 78  
ASN   OXT  O  N N 79  
ASN   H    H  N N 80  
ASN   H2   H  N N 81  
ASN   HA   H  N N 82  
ASN   HB2  H  N N 83  
ASN   HB3  H  N N 84  
ASN   HD21 H  N N 85  
ASN   HD22 H  N N 86  
ASN   HXT  H  N N 87  
ASP   N    N  N N 88  
ASP   CA   C  N S 89  
ASP   C    C  N N 90  
ASP   O    O  N N 91  
ASP   CB   C  N N 92  
ASP   CG   C  N N 93  
ASP   OD1  O  N N 94  
ASP   OD2  O  N N 95  
ASP   OXT  O  N N 96  
ASP   H    H  N N 97  
ASP   H2   H  N N 98  
ASP   HA   H  N N 99  
ASP   HB2  H  N N 100 
ASP   HB3  H  N N 101 
ASP   HD2  H  N N 102 
ASP   HXT  H  N N 103 
CYS   N    N  N N 104 
CYS   CA   C  N R 105 
CYS   C    C  N N 106 
CYS   O    O  N N 107 
CYS   CB   C  N N 108 
CYS   SG   S  N N 109 
CYS   OXT  O  N N 110 
CYS   H    H  N N 111 
CYS   H2   H  N N 112 
CYS   HA   H  N N 113 
CYS   HB2  H  N N 114 
CYS   HB3  H  N N 115 
CYS   HG   H  N N 116 
CYS   HXT  H  N N 117 
DIF   C1   C  Y N 118 
DIF   C2   C  Y N 119 
DIF   CL2  CL N N 120 
DIF   C3   C  Y N 121 
DIF   C4   C  Y N 122 
DIF   CL4  CL N N 123 
DIF   C5   C  Y N 124 
DIF   C6   C  Y N 125 
DIF   N1   N  N N 126 
DIF   C7   C  Y N 127 
DIF   C8   C  Y N 128 
DIF   C9   C  Y N 129 
DIF   C10  C  Y N 130 
DIF   C11  C  Y N 131 
DIF   C12  C  Y N 132 
DIF   C13  C  N N 133 
DIF   C14  C  N N 134 
DIF   O1   O  N N 135 
DIF   O2   O  N N 136 
DIF   H1   H  N N 137 
DIF   H5   H  N N 138 
DIF   H6   H  N N 139 
DIF   HN1  H  N N 140 
DIF   H9   H  N N 141 
DIF   H10  H  N N 142 
DIF   H11  H  N N 143 
DIF   H12  H  N N 144 
DIF   H131 H  N N 145 
DIF   H132 H  N N 146 
DIF   HO1  H  N N 147 
GLN   N    N  N N 148 
GLN   CA   C  N S 149 
GLN   C    C  N N 150 
GLN   O    O  N N 151 
GLN   CB   C  N N 152 
GLN   CG   C  N N 153 
GLN   CD   C  N N 154 
GLN   OE1  O  N N 155 
GLN   NE2  N  N N 156 
GLN   OXT  O  N N 157 
GLN   H    H  N N 158 
GLN   H2   H  N N 159 
GLN   HA   H  N N 160 
GLN   HB2  H  N N 161 
GLN   HB3  H  N N 162 
GLN   HG2  H  N N 163 
GLN   HG3  H  N N 164 
GLN   HE21 H  N N 165 
GLN   HE22 H  N N 166 
GLN   HXT  H  N N 167 
GLU   N    N  N N 168 
GLU   CA   C  N S 169 
GLU   C    C  N N 170 
GLU   O    O  N N 171 
GLU   CB   C  N N 172 
GLU   CG   C  N N 173 
GLU   CD   C  N N 174 
GLU   OE1  O  N N 175 
GLU   OE2  O  N N 176 
GLU   OXT  O  N N 177 
GLU   H    H  N N 178 
GLU   H2   H  N N 179 
GLU   HA   H  N N 180 
GLU   HB2  H  N N 181 
GLU   HB3  H  N N 182 
GLU   HG2  H  N N 183 
GLU   HG3  H  N N 184 
GLU   HE2  H  N N 185 
GLU   HXT  H  N N 186 
GLY   N    N  N N 187 
GLY   CA   C  N N 188 
GLY   C    C  N N 189 
GLY   O    O  N N 190 
GLY   OXT  O  N N 191 
GLY   H    H  N N 192 
GLY   H2   H  N N 193 
GLY   HA2  H  N N 194 
GLY   HA3  H  N N 195 
GLY   HXT  H  N N 196 
HEM   CHA  C  N N 197 
HEM   CHB  C  N N 198 
HEM   CHC  C  N N 199 
HEM   CHD  C  N N 200 
HEM   C1A  C  Y N 201 
HEM   C2A  C  Y N 202 
HEM   C3A  C  Y N 203 
HEM   C4A  C  Y N 204 
HEM   CMA  C  N N 205 
HEM   CAA  C  N N 206 
HEM   CBA  C  N N 207 
HEM   CGA  C  N N 208 
HEM   O1A  O  N N 209 
HEM   O2A  O  N N 210 
HEM   C1B  C  N N 211 
HEM   C2B  C  N N 212 
HEM   C3B  C  N N 213 
HEM   C4B  C  N N 214 
HEM   CMB  C  N N 215 
HEM   CAB  C  N N 216 
HEM   CBB  C  N N 217 
HEM   C1C  C  Y N 218 
HEM   C2C  C  Y N 219 
HEM   C3C  C  Y N 220 
HEM   C4C  C  Y N 221 
HEM   CMC  C  N N 222 
HEM   CAC  C  N N 223 
HEM   CBC  C  N N 224 
HEM   C1D  C  N N 225 
HEM   C2D  C  N N 226 
HEM   C3D  C  N N 227 
HEM   C4D  C  N N 228 
HEM   CMD  C  N N 229 
HEM   CAD  C  N N 230 
HEM   CBD  C  N N 231 
HEM   CGD  C  N N 232 
HEM   O1D  O  N N 233 
HEM   O2D  O  N N 234 
HEM   NA   N  Y N 235 
HEM   NB   N  N N 236 
HEM   NC   N  Y N 237 
HEM   ND   N  N N 238 
HEM   FE   FE N N 239 
HEM   HHB  H  N N 240 
HEM   HHC  H  N N 241 
HEM   HHD  H  N N 242 
HEM   HMA  H  N N 243 
HEM   HMAA H  N N 244 
HEM   HMAB H  N N 245 
HEM   HAA  H  N N 246 
HEM   HAAA H  N N 247 
HEM   HBA  H  N N 248 
HEM   HBAA H  N N 249 
HEM   HMB  H  N N 250 
HEM   HMBA H  N N 251 
HEM   HMBB H  N N 252 
HEM   HAB  H  N N 253 
HEM   HBB  H  N N 254 
HEM   HBBA H  N N 255 
HEM   HMC  H  N N 256 
HEM   HMCA H  N N 257 
HEM   HMCB H  N N 258 
HEM   HAC  H  N N 259 
HEM   HBC  H  N N 260 
HEM   HBCA H  N N 261 
HEM   HMD  H  N N 262 
HEM   HMDA H  N N 263 
HEM   HMDB H  N N 264 
HEM   HAD  H  N N 265 
HEM   HADA H  N N 266 
HEM   HBD  H  N N 267 
HEM   HBDA H  N N 268 
HEM   H2A  H  N N 269 
HEM   H2D  H  N N 270 
HEM   HHA  H  N N 271 
HIS   N    N  N N 272 
HIS   CA   C  N S 273 
HIS   C    C  N N 274 
HIS   O    O  N N 275 
HIS   CB   C  N N 276 
HIS   CG   C  Y N 277 
HIS   ND1  N  Y N 278 
HIS   CD2  C  Y N 279 
HIS   CE1  C  Y N 280 
HIS   NE2  N  Y N 281 
HIS   OXT  O  N N 282 
HIS   H    H  N N 283 
HIS   H2   H  N N 284 
HIS   HA   H  N N 285 
HIS   HB2  H  N N 286 
HIS   HB3  H  N N 287 
HIS   HD1  H  N N 288 
HIS   HD2  H  N N 289 
HIS   HE1  H  N N 290 
HIS   HE2  H  N N 291 
HIS   HXT  H  N N 292 
HOH   O    O  N N 293 
HOH   H1   H  N N 294 
HOH   H2   H  N N 295 
ILE   N    N  N N 296 
ILE   CA   C  N S 297 
ILE   C    C  N N 298 
ILE   O    O  N N 299 
ILE   CB   C  N S 300 
ILE   CG1  C  N N 301 
ILE   CG2  C  N N 302 
ILE   CD1  C  N N 303 
ILE   OXT  O  N N 304 
ILE   H    H  N N 305 
ILE   H2   H  N N 306 
ILE   HA   H  N N 307 
ILE   HB   H  N N 308 
ILE   HG12 H  N N 309 
ILE   HG13 H  N N 310 
ILE   HG21 H  N N 311 
ILE   HG22 H  N N 312 
ILE   HG23 H  N N 313 
ILE   HD11 H  N N 314 
ILE   HD12 H  N N 315 
ILE   HD13 H  N N 316 
ILE   HXT  H  N N 317 
LEU   N    N  N N 318 
LEU   CA   C  N S 319 
LEU   C    C  N N 320 
LEU   O    O  N N 321 
LEU   CB   C  N N 322 
LEU   CG   C  N N 323 
LEU   CD1  C  N N 324 
LEU   CD2  C  N N 325 
LEU   OXT  O  N N 326 
LEU   H    H  N N 327 
LEU   H2   H  N N 328 
LEU   HA   H  N N 329 
LEU   HB2  H  N N 330 
LEU   HB3  H  N N 331 
LEU   HG   H  N N 332 
LEU   HD11 H  N N 333 
LEU   HD12 H  N N 334 
LEU   HD13 H  N N 335 
LEU   HD21 H  N N 336 
LEU   HD22 H  N N 337 
LEU   HD23 H  N N 338 
LEU   HXT  H  N N 339 
LYS   N    N  N N 340 
LYS   CA   C  N S 341 
LYS   C    C  N N 342 
LYS   O    O  N N 343 
LYS   CB   C  N N 344 
LYS   CG   C  N N 345 
LYS   CD   C  N N 346 
LYS   CE   C  N N 347 
LYS   NZ   N  N N 348 
LYS   OXT  O  N N 349 
LYS   H    H  N N 350 
LYS   H2   H  N N 351 
LYS   HA   H  N N 352 
LYS   HB2  H  N N 353 
LYS   HB3  H  N N 354 
LYS   HG2  H  N N 355 
LYS   HG3  H  N N 356 
LYS   HD2  H  N N 357 
LYS   HD3  H  N N 358 
LYS   HE2  H  N N 359 
LYS   HE3  H  N N 360 
LYS   HZ1  H  N N 361 
LYS   HZ2  H  N N 362 
LYS   HZ3  H  N N 363 
LYS   HXT  H  N N 364 
MET   N    N  N N 365 
MET   CA   C  N S 366 
MET   C    C  N N 367 
MET   O    O  N N 368 
MET   CB   C  N N 369 
MET   CG   C  N N 370 
MET   SD   S  N N 371 
MET   CE   C  N N 372 
MET   OXT  O  N N 373 
MET   H    H  N N 374 
MET   H2   H  N N 375 
MET   HA   H  N N 376 
MET   HB2  H  N N 377 
MET   HB3  H  N N 378 
MET   HG2  H  N N 379 
MET   HG3  H  N N 380 
MET   HE1  H  N N 381 
MET   HE2  H  N N 382 
MET   HE3  H  N N 383 
MET   HXT  H  N N 384 
PHE   N    N  N N 385 
PHE   CA   C  N S 386 
PHE   C    C  N N 387 
PHE   O    O  N N 388 
PHE   CB   C  N N 389 
PHE   CG   C  Y N 390 
PHE   CD1  C  Y N 391 
PHE   CD2  C  Y N 392 
PHE   CE1  C  Y N 393 
PHE   CE2  C  Y N 394 
PHE   CZ   C  Y N 395 
PHE   OXT  O  N N 396 
PHE   H    H  N N 397 
PHE   H2   H  N N 398 
PHE   HA   H  N N 399 
PHE   HB2  H  N N 400 
PHE   HB3  H  N N 401 
PHE   HD1  H  N N 402 
PHE   HD2  H  N N 403 
PHE   HE1  H  N N 404 
PHE   HE2  H  N N 405 
PHE   HZ   H  N N 406 
PHE   HXT  H  N N 407 
PRO   N    N  N N 408 
PRO   CA   C  N S 409 
PRO   C    C  N N 410 
PRO   O    O  N N 411 
PRO   CB   C  N N 412 
PRO   CG   C  N N 413 
PRO   CD   C  N N 414 
PRO   OXT  O  N N 415 
PRO   H    H  N N 416 
PRO   HA   H  N N 417 
PRO   HB2  H  N N 418 
PRO   HB3  H  N N 419 
PRO   HG2  H  N N 420 
PRO   HG3  H  N N 421 
PRO   HD2  H  N N 422 
PRO   HD3  H  N N 423 
PRO   HXT  H  N N 424 
SER   N    N  N N 425 
SER   CA   C  N S 426 
SER   C    C  N N 427 
SER   O    O  N N 428 
SER   CB   C  N N 429 
SER   OG   O  N N 430 
SER   OXT  O  N N 431 
SER   H    H  N N 432 
SER   H2   H  N N 433 
SER   HA   H  N N 434 
SER   HB2  H  N N 435 
SER   HB3  H  N N 436 
SER   HG   H  N N 437 
SER   HXT  H  N N 438 
THR   N    N  N N 439 
THR   CA   C  N S 440 
THR   C    C  N N 441 
THR   O    O  N N 442 
THR   CB   C  N R 443 
THR   OG1  O  N N 444 
THR   CG2  C  N N 445 
THR   OXT  O  N N 446 
THR   H    H  N N 447 
THR   H2   H  N N 448 
THR   HA   H  N N 449 
THR   HB   H  N N 450 
THR   HG1  H  N N 451 
THR   HG21 H  N N 452 
THR   HG22 H  N N 453 
THR   HG23 H  N N 454 
THR   HXT  H  N N 455 
TRP   N    N  N N 456 
TRP   CA   C  N S 457 
TRP   C    C  N N 458 
TRP   O    O  N N 459 
TRP   CB   C  N N 460 
TRP   CG   C  Y N 461 
TRP   CD1  C  Y N 462 
TRP   CD2  C  Y N 463 
TRP   NE1  N  Y N 464 
TRP   CE2  C  Y N 465 
TRP   CE3  C  Y N 466 
TRP   CZ2  C  Y N 467 
TRP   CZ3  C  Y N 468 
TRP   CH2  C  Y N 469 
TRP   OXT  O  N N 470 
TRP   H    H  N N 471 
TRP   H2   H  N N 472 
TRP   HA   H  N N 473 
TRP   HB2  H  N N 474 
TRP   HB3  H  N N 475 
TRP   HD1  H  N N 476 
TRP   HE1  H  N N 477 
TRP   HE3  H  N N 478 
TRP   HZ2  H  N N 479 
TRP   HZ3  H  N N 480 
TRP   HH2  H  N N 481 
TRP   HXT  H  N N 482 
TYR   N    N  N N 483 
TYR   CA   C  N S 484 
TYR   C    C  N N 485 
TYR   O    O  N N 486 
TYR   CB   C  N N 487 
TYR   CG   C  Y N 488 
TYR   CD1  C  Y N 489 
TYR   CD2  C  Y N 490 
TYR   CE1  C  Y N 491 
TYR   CE2  C  Y N 492 
TYR   CZ   C  Y N 493 
TYR   OH   O  N N 494 
TYR   OXT  O  N N 495 
TYR   H    H  N N 496 
TYR   H2   H  N N 497 
TYR   HA   H  N N 498 
TYR   HB2  H  N N 499 
TYR   HB3  H  N N 500 
TYR   HD1  H  N N 501 
TYR   HD2  H  N N 502 
TYR   HE1  H  N N 503 
TYR   HE2  H  N N 504 
TYR   HH   H  N N 505 
TYR   HXT  H  N N 506 
VAL   N    N  N N 507 
VAL   CA   C  N S 508 
VAL   C    C  N N 509 
VAL   O    O  N N 510 
VAL   CB   C  N N 511 
VAL   CG1  C  N N 512 
VAL   CG2  C  N N 513 
VAL   OXT  O  N N 514 
VAL   H    H  N N 515 
VAL   H2   H  N N 516 
VAL   HA   H  N N 517 
VAL   HB   H  N N 518 
VAL   HG11 H  N N 519 
VAL   HG12 H  N N 520 
VAL   HG13 H  N N 521 
VAL   HG21 H  N N 522 
VAL   HG22 H  N N 523 
VAL   HG23 H  N N 524 
VAL   HXT  H  N N 525 
# 
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 
A1L6Q CL1 C11  sing N N 1   
A1L6Q N6  C19  trip N N 2   
A1L6Q C18 N5   doub Y N 3   
A1L6Q C18 N4   sing Y N 4   
A1L6Q C19 C13  sing N N 5   
A1L6Q C11 C14  doub Y N 6   
A1L6Q C11 C9   sing Y N 7   
A1L6Q C14 C16  sing Y N 8   
A1L6Q N5  C20  sing Y N 9   
A1L6Q S2  C10  sing N N 10  
A1L6Q S2  C7   sing N N 11  
A1L6Q C13 N4   sing N N 12  
A1L6Q C13 C10  doub N E 13  
A1L6Q N4  C17  sing Y N 14  
A1L6Q C10 S3   sing N N 15  
A1L6Q C8  C7   sing N N 16  
A1L6Q C8  S3   sing N N 17  
A1L6Q C9  C7   sing N N 18  
A1L6Q C9  C12  doub Y N 19  
A1L6Q C16 C15  doub Y N 20  
A1L6Q C20 C17  doub Y N 21  
A1L6Q C12 C15  sing Y N 22  
A1L6Q C7  H1   sing N N 23  
A1L6Q C8  H2   sing N N 24  
A1L6Q C8  H3   sing N N 25  
A1L6Q C12 H4   sing N N 26  
A1L6Q C20 H5   sing N N 27  
A1L6Q C14 H6   sing N N 28  
A1L6Q C15 H7   sing N N 29  
A1L6Q C16 H8   sing N N 30  
A1L6Q C17 H9   sing N N 31  
A1L6Q C18 H10  sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
DIF   C1  C2   doub Y N 115 
DIF   C1  C6   sing Y N 116 
DIF   C1  H1   sing N N 117 
DIF   C2  CL2  sing N N 118 
DIF   C2  C3   sing Y N 119 
DIF   C3  C4   doub Y N 120 
DIF   C3  N1   sing N N 121 
DIF   C4  CL4  sing N N 122 
DIF   C4  C5   sing Y N 123 
DIF   C5  C6   doub Y N 124 
DIF   C5  H5   sing N N 125 
DIF   C6  H6   sing N N 126 
DIF   N1  C8   sing N N 127 
DIF   N1  HN1  sing N N 128 
DIF   C7  C8   doub Y N 129 
DIF   C7  C12  sing Y N 130 
DIF   C7  C13  sing N N 131 
DIF   C8  C9   sing Y N 132 
DIF   C9  C10  doub Y N 133 
DIF   C9  H9   sing N N 134 
DIF   C10 C11  sing Y N 135 
DIF   C10 H10  sing N N 136 
DIF   C11 C12  doub Y N 137 
DIF   C11 H11  sing N N 138 
DIF   C12 H12  sing N N 139 
DIF   C13 C14  sing N N 140 
DIF   C13 H131 sing N N 141 
DIF   C13 H132 sing N N 142 
DIF   C14 O1   sing N N 143 
DIF   C14 O2   doub N N 144 
DIF   O1  HO1  sing N N 145 
GLN   N   CA   sing N N 146 
GLN   N   H    sing N N 147 
GLN   N   H2   sing N N 148 
GLN   CA  C    sing N N 149 
GLN   CA  CB   sing N N 150 
GLN   CA  HA   sing N N 151 
GLN   C   O    doub N N 152 
GLN   C   OXT  sing N N 153 
GLN   CB  CG   sing N N 154 
GLN   CB  HB2  sing N N 155 
GLN   CB  HB3  sing N N 156 
GLN   CG  CD   sing N N 157 
GLN   CG  HG2  sing N N 158 
GLN   CG  HG3  sing N N 159 
GLN   CD  OE1  doub N N 160 
GLN   CD  NE2  sing N N 161 
GLN   NE2 HE21 sing N N 162 
GLN   NE2 HE22 sing N N 163 
GLN   OXT HXT  sing N N 164 
GLU   N   CA   sing N N 165 
GLU   N   H    sing N N 166 
GLU   N   H2   sing N N 167 
GLU   CA  C    sing N N 168 
GLU   CA  CB   sing N N 169 
GLU   CA  HA   sing N N 170 
GLU   C   O    doub N N 171 
GLU   C   OXT  sing N N 172 
GLU   CB  CG   sing N N 173 
GLU   CB  HB2  sing N N 174 
GLU   CB  HB3  sing N N 175 
GLU   CG  CD   sing N N 176 
GLU   CG  HG2  sing N N 177 
GLU   CG  HG3  sing N N 178 
GLU   CD  OE1  doub N N 179 
GLU   CD  OE2  sing N N 180 
GLU   OE2 HE2  sing N N 181 
GLU   OXT HXT  sing N N 182 
GLY   N   CA   sing N N 183 
GLY   N   H    sing N N 184 
GLY   N   H2   sing N N 185 
GLY   CA  C    sing N N 186 
GLY   CA  HA2  sing N N 187 
GLY   CA  HA3  sing N N 188 
GLY   C   O    doub N N 189 
GLY   C   OXT  sing N N 190 
GLY   OXT HXT  sing N N 191 
HEM   CHA C1A  sing N N 192 
HEM   CHA C4D  doub N N 193 
HEM   CHA HHA  sing N N 194 
HEM   CHB C4A  sing N N 195 
HEM   CHB C1B  doub N N 196 
HEM   CHB HHB  sing N N 197 
HEM   CHC C4B  sing N N 198 
HEM   CHC C1C  doub N N 199 
HEM   CHC HHC  sing N N 200 
HEM   CHD C4C  doub N N 201 
HEM   CHD C1D  sing N N 202 
HEM   CHD HHD  sing N N 203 
HEM   C1A C2A  doub Y N 204 
HEM   C1A NA   sing Y N 205 
HEM   C2A C3A  sing Y N 206 
HEM   C2A CAA  sing N N 207 
HEM   C3A C4A  doub Y N 208 
HEM   C3A CMA  sing N N 209 
HEM   C4A NA   sing Y N 210 
HEM   CMA HMA  sing N N 211 
HEM   CMA HMAA sing N N 212 
HEM   CMA HMAB sing N N 213 
HEM   CAA CBA  sing N N 214 
HEM   CAA HAA  sing N N 215 
HEM   CAA HAAA sing N N 216 
HEM   CBA CGA  sing N N 217 
HEM   CBA HBA  sing N N 218 
HEM   CBA HBAA sing N N 219 
HEM   CGA O1A  doub N N 220 
HEM   CGA O2A  sing N N 221 
HEM   C1B C2B  sing N N 222 
HEM   C1B NB   sing N N 223 
HEM   C2B C3B  doub N N 224 
HEM   C2B CMB  sing N N 225 
HEM   C3B C4B  sing N N 226 
HEM   C3B CAB  sing N N 227 
HEM   C4B NB   doub N N 228 
HEM   CMB HMB  sing N N 229 
HEM   CMB HMBA sing N N 230 
HEM   CMB HMBB sing N N 231 
HEM   CAB CBB  doub N N 232 
HEM   CAB HAB  sing N N 233 
HEM   CBB HBB  sing N N 234 
HEM   CBB HBBA sing N N 235 
HEM   C1C C2C  sing Y N 236 
HEM   C1C NC   sing Y N 237 
HEM   C2C C3C  doub Y N 238 
HEM   C2C CMC  sing N N 239 
HEM   C3C C4C  sing Y N 240 
HEM   C3C CAC  sing N N 241 
HEM   C4C NC   sing Y N 242 
HEM   CMC HMC  sing N N 243 
HEM   CMC HMCA sing N N 244 
HEM   CMC HMCB sing N N 245 
HEM   CAC CBC  doub N N 246 
HEM   CAC HAC  sing N N 247 
HEM   CBC HBC  sing N N 248 
HEM   CBC HBCA sing N N 249 
HEM   C1D C2D  sing N N 250 
HEM   C1D ND   doub N N 251 
HEM   C2D C3D  doub N N 252 
HEM   C2D CMD  sing N N 253 
HEM   C3D C4D  sing N N 254 
HEM   C3D CAD  sing N N 255 
HEM   C4D ND   sing N N 256 
HEM   CMD HMD  sing N N 257 
HEM   CMD HMDA sing N N 258 
HEM   CMD HMDB sing N N 259 
HEM   CAD CBD  sing N N 260 
HEM   CAD HAD  sing N N 261 
HEM   CAD HADA sing N N 262 
HEM   CBD CGD  sing N N 263 
HEM   CBD HBD  sing N N 264 
HEM   CBD HBDA sing N N 265 
HEM   CGD O1D  doub N N 266 
HEM   CGD O2D  sing N N 267 
HEM   O2A H2A  sing N N 268 
HEM   O2D H2D  sing N N 269 
HEM   FE  NA   sing N N 270 
HEM   FE  NB   sing N N 271 
HEM   FE  NC   sing N N 272 
HEM   FE  ND   sing N N 273 
HIS   N   CA   sing N N 274 
HIS   N   H    sing N N 275 
HIS   N   H2   sing N N 276 
HIS   CA  C    sing N N 277 
HIS   CA  CB   sing N N 278 
HIS   CA  HA   sing N N 279 
HIS   C   O    doub N N 280 
HIS   C   OXT  sing N N 281 
HIS   CB  CG   sing N N 282 
HIS   CB  HB2  sing N N 283 
HIS   CB  HB3  sing N N 284 
HIS   CG  ND1  sing Y N 285 
HIS   CG  CD2  doub Y N 286 
HIS   ND1 CE1  doub Y N 287 
HIS   ND1 HD1  sing N N 288 
HIS   CD2 NE2  sing Y N 289 
HIS   CD2 HD2  sing N N 290 
HIS   CE1 NE2  sing Y N 291 
HIS   CE1 HE1  sing N N 292 
HIS   NE2 HE2  sing N N 293 
HIS   OXT HXT  sing N N 294 
HOH   O   H1   sing N N 295 
HOH   O   H2   sing N N 296 
ILE   N   CA   sing N N 297 
ILE   N   H    sing N N 298 
ILE   N   H2   sing N N 299 
ILE   CA  C    sing N N 300 
ILE   CA  CB   sing N N 301 
ILE   CA  HA   sing N N 302 
ILE   C   O    doub N N 303 
ILE   C   OXT  sing N N 304 
ILE   CB  CG1  sing N N 305 
ILE   CB  CG2  sing N N 306 
ILE   CB  HB   sing N N 307 
ILE   CG1 CD1  sing N N 308 
ILE   CG1 HG12 sing N N 309 
ILE   CG1 HG13 sing N N 310 
ILE   CG2 HG21 sing N N 311 
ILE   CG2 HG22 sing N N 312 
ILE   CG2 HG23 sing N N 313 
ILE   CD1 HD11 sing N N 314 
ILE   CD1 HD12 sing N N 315 
ILE   CD1 HD13 sing N N 316 
ILE   OXT HXT  sing N N 317 
LEU   N   CA   sing N N 318 
LEU   N   H    sing N N 319 
LEU   N   H2   sing N N 320 
LEU   CA  C    sing N N 321 
LEU   CA  CB   sing N N 322 
LEU   CA  HA   sing N N 323 
LEU   C   O    doub N N 324 
LEU   C   OXT  sing N N 325 
LEU   CB  CG   sing N N 326 
LEU   CB  HB2  sing N N 327 
LEU   CB  HB3  sing N N 328 
LEU   CG  CD1  sing N N 329 
LEU   CG  CD2  sing N N 330 
LEU   CG  HG   sing N N 331 
LEU   CD1 HD11 sing N N 332 
LEU   CD1 HD12 sing N N 333 
LEU   CD1 HD13 sing N N 334 
LEU   CD2 HD21 sing N N 335 
LEU   CD2 HD22 sing N N 336 
LEU   CD2 HD23 sing N N 337 
LEU   OXT HXT  sing N N 338 
LYS   N   CA   sing N N 339 
LYS   N   H    sing N N 340 
LYS   N   H2   sing N N 341 
LYS   CA  C    sing N N 342 
LYS   CA  CB   sing N N 343 
LYS   CA  HA   sing N N 344 
LYS   C   O    doub N N 345 
LYS   C   OXT  sing N N 346 
LYS   CB  CG   sing N N 347 
LYS   CB  HB2  sing N N 348 
LYS   CB  HB3  sing N N 349 
LYS   CG  CD   sing N N 350 
LYS   CG  HG2  sing N N 351 
LYS   CG  HG3  sing N N 352 
LYS   CD  CE   sing N N 353 
LYS   CD  HD2  sing N N 354 
LYS   CD  HD3  sing N N 355 
LYS   CE  NZ   sing N N 356 
LYS   CE  HE2  sing N N 357 
LYS   CE  HE3  sing N N 358 
LYS   NZ  HZ1  sing N N 359 
LYS   NZ  HZ2  sing N N 360 
LYS   NZ  HZ3  sing N N 361 
LYS   OXT HXT  sing N N 362 
MET   N   CA   sing N N 363 
MET   N   H    sing N N 364 
MET   N   H2   sing N N 365 
MET   CA  C    sing N N 366 
MET   CA  CB   sing N N 367 
MET   CA  HA   sing N N 368 
MET   C   O    doub N N 369 
MET   C   OXT  sing N N 370 
MET   CB  CG   sing N N 371 
MET   CB  HB2  sing N N 372 
MET   CB  HB3  sing N N 373 
MET   CG  SD   sing N N 374 
MET   CG  HG2  sing N N 375 
MET   CG  HG3  sing N N 376 
MET   SD  CE   sing N N 377 
MET   CE  HE1  sing N N 378 
MET   CE  HE2  sing N N 379 
MET   CE  HE3  sing N N 380 
MET   OXT HXT  sing N N 381 
PHE   N   CA   sing N N 382 
PHE   N   H    sing N N 383 
PHE   N   H2   sing N N 384 
PHE   CA  C    sing N N 385 
PHE   CA  CB   sing N N 386 
PHE   CA  HA   sing N N 387 
PHE   C   O    doub N N 388 
PHE   C   OXT  sing N N 389 
PHE   CB  CG   sing N N 390 
PHE   CB  HB2  sing N N 391 
PHE   CB  HB3  sing N N 392 
PHE   CG  CD1  doub Y N 393 
PHE   CG  CD2  sing Y N 394 
PHE   CD1 CE1  sing Y N 395 
PHE   CD1 HD1  sing N N 396 
PHE   CD2 CE2  doub Y N 397 
PHE   CD2 HD2  sing N N 398 
PHE   CE1 CZ   doub Y N 399 
PHE   CE1 HE1  sing N N 400 
PHE   CE2 CZ   sing Y N 401 
PHE   CE2 HE2  sing N N 402 
PHE   CZ  HZ   sing N N 403 
PHE   OXT HXT  sing N N 404 
PRO   N   CA   sing N N 405 
PRO   N   CD   sing N N 406 
PRO   N   H    sing N N 407 
PRO   CA  C    sing N N 408 
PRO   CA  CB   sing N N 409 
PRO   CA  HA   sing N N 410 
PRO   C   O    doub N N 411 
PRO   C   OXT  sing N N 412 
PRO   CB  CG   sing N N 413 
PRO   CB  HB2  sing N N 414 
PRO   CB  HB3  sing N N 415 
PRO   CG  CD   sing N N 416 
PRO   CG  HG2  sing N N 417 
PRO   CG  HG3  sing N N 418 
PRO   CD  HD2  sing N N 419 
PRO   CD  HD3  sing N N 420 
PRO   OXT HXT  sing N N 421 
SER   N   CA   sing N N 422 
SER   N   H    sing N N 423 
SER   N   H2   sing N N 424 
SER   CA  C    sing N N 425 
SER   CA  CB   sing N N 426 
SER   CA  HA   sing N N 427 
SER   C   O    doub N N 428 
SER   C   OXT  sing N N 429 
SER   CB  OG   sing N N 430 
SER   CB  HB2  sing N N 431 
SER   CB  HB3  sing N N 432 
SER   OG  HG   sing N N 433 
SER   OXT HXT  sing N N 434 
THR   N   CA   sing N N 435 
THR   N   H    sing N N 436 
THR   N   H2   sing N N 437 
THR   CA  C    sing N N 438 
THR   CA  CB   sing N N 439 
THR   CA  HA   sing N N 440 
THR   C   O    doub N N 441 
THR   C   OXT  sing N N 442 
THR   CB  OG1  sing N N 443 
THR   CB  CG2  sing N N 444 
THR   CB  HB   sing N N 445 
THR   OG1 HG1  sing N N 446 
THR   CG2 HG21 sing N N 447 
THR   CG2 HG22 sing N N 448 
THR   CG2 HG23 sing N N 449 
THR   OXT HXT  sing N N 450 
TRP   N   CA   sing N N 451 
TRP   N   H    sing N N 452 
TRP   N   H2   sing N N 453 
TRP   CA  C    sing N N 454 
TRP   CA  CB   sing N N 455 
TRP   CA  HA   sing N N 456 
TRP   C   O    doub N N 457 
TRP   C   OXT  sing N N 458 
TRP   CB  CG   sing N N 459 
TRP   CB  HB2  sing N N 460 
TRP   CB  HB3  sing N N 461 
TRP   CG  CD1  doub Y N 462 
TRP   CG  CD2  sing Y N 463 
TRP   CD1 NE1  sing Y N 464 
TRP   CD1 HD1  sing N N 465 
TRP   CD2 CE2  doub Y N 466 
TRP   CD2 CE3  sing Y N 467 
TRP   NE1 CE2  sing Y N 468 
TRP   NE1 HE1  sing N N 469 
TRP   CE2 CZ2  sing Y N 470 
TRP   CE3 CZ3  doub Y N 471 
TRP   CE3 HE3  sing N N 472 
TRP   CZ2 CH2  doub Y N 473 
TRP   CZ2 HZ2  sing N N 474 
TRP   CZ3 CH2  sing Y N 475 
TRP   CZ3 HZ3  sing N N 476 
TRP   CH2 HH2  sing N N 477 
TRP   OXT HXT  sing N N 478 
TYR   N   CA   sing N N 479 
TYR   N   H    sing N N 480 
TYR   N   H2   sing N N 481 
TYR   CA  C    sing N N 482 
TYR   CA  CB   sing N N 483 
TYR   CA  HA   sing N N 484 
TYR   C   O    doub N N 485 
TYR   C   OXT  sing N N 486 
TYR   CB  CG   sing N N 487 
TYR   CB  HB2  sing N N 488 
TYR   CB  HB3  sing N N 489 
TYR   CG  CD1  doub Y N 490 
TYR   CG  CD2  sing Y N 491 
TYR   CD1 CE1  sing Y N 492 
TYR   CD1 HD1  sing N N 493 
TYR   CD2 CE2  doub Y N 494 
TYR   CD2 HD2  sing N N 495 
TYR   CE1 CZ   doub Y N 496 
TYR   CE1 HE1  sing N N 497 
TYR   CE2 CZ   sing Y N 498 
TYR   CE2 HE2  sing N N 499 
TYR   CZ  OH   sing N N 500 
TYR   OH  HH   sing N N 501 
TYR   OXT HXT  sing N N 502 
VAL   N   CA   sing N N 503 
VAL   N   H    sing N N 504 
VAL   N   H2   sing N N 505 
VAL   CA  C    sing N N 506 
VAL   CA  CB   sing N N 507 
VAL   CA  HA   sing N N 508 
VAL   C   O    doub N N 509 
VAL   C   OXT  sing N N 510 
VAL   CB  CG1  sing N N 511 
VAL   CB  CG2  sing N N 512 
VAL   CB  HB   sing N N 513 
VAL   CG1 HG11 sing N N 514 
VAL   CG1 HG12 sing N N 515 
VAL   CG1 HG13 sing N N 516 
VAL   CG2 HG21 sing N N 517 
VAL   CG2 HG22 sing N N 518 
VAL   CG2 HG23 sing N N 519 
VAL   OXT HXT  sing N N 520 
# 
_pdbx_audit_support.funding_organization   'Ministry of Education, Culture, Sports, Science and Technology (Japan)' 
_pdbx_audit_support.country                Japan 
_pdbx_audit_support.grant_number           JPMXS0120330644 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2ZBY 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9KW5 
_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]   0.019007 
_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]   0.018672 
_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]   0.007080 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761  7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
FE ? ? 20.90327 4.99816 ? ? 2.55100  38.46870 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . THR   A 1 7   ? -0.10241  -29.55266 32.90459  1.000 62.07052 ? 7   THR   A N   1 
ATOM   2    C  CA  . THR   A 1 7   ? 0.23032   -29.64676 31.48786  1.000 61.89674 ? 7   THR   A CA  1 
ATOM   3    C  C   . THR   A 1 7   ? 1.11757   -28.47724 31.05859  1.000 61.66251 ? 7   THR   A C   1 
ATOM   4    O  O   . THR   A 1 7   ? 0.86707   -27.32774 31.43351  1.000 60.81529 ? 7   THR   A O   1 
ATOM   5    C  CB  . THR   A 1 7   ? -1.04467  -29.69717 30.61348  1.000 64.36462 ? 7   THR   A CB  1 
ATOM   6    O  OG1 . THR   A 1 7   ? -0.69577  -29.55355 29.22921  1.000 64.37625 ? 7   THR   A OG1 1 
ATOM   7    C  CG2 . THR   A 1 7   ? -2.02664  -28.60291 31.01656  1.000 61.80308 ? 7   THR   A CG2 1 
ATOM   8    N  N   . PRO   A 1 8   ? 2.15693   -28.77302 30.27950  1.000 57.94488 ? 8   PRO   A N   1 
ATOM   9    C  CA  . PRO   A 1 8   ? 3.12916   -27.73297 29.92193  1.000 57.08731 ? 8   PRO   A CA  1 
ATOM   10   C  C   . PRO   A 1 8   ? 2.52230   -26.66887 29.02004  1.000 56.93953 ? 8   PRO   A C   1 
ATOM   11   O  O   . PRO   A 1 8   ? 1.60293   -26.92894 28.23778  1.000 57.47826 ? 8   PRO   A O   1 
ATOM   12   C  CB  . PRO   A 1 8   ? 4.23420   -28.51043 29.19491  1.000 53.73576 ? 8   PRO   A CB  1 
ATOM   13   C  CG  . PRO   A 1 8   ? 4.00945   -29.95975 29.55878  1.000 50.00047 ? 8   PRO   A CG  1 
ATOM   14   C  CD  . PRO   A 1 8   ? 2.53204   -30.09072 29.74104  1.000 55.54412 ? 8   PRO   A CD  1 
ATOM   15   N  N   A GLN   A 1 9   ? 3.06466   -25.45526 29.12633  0.500 56.29379 ? 9   GLN   A N   1 
ATOM   16   N  N   B GLN   A 1 9   ? 3.05853   -25.45102 29.13960  0.500 56.28935 ? 9   GLN   A N   1 
ATOM   17   C  CA  A GLN   A 1 9   ? 2.55478   -24.31444 28.37838  0.500 56.43879 ? 9   GLN   A CA  1 
ATOM   18   C  CA  B GLN   A 1 9   ? 2.56325   -24.29823 28.39691  0.500 56.42440 ? 9   GLN   A CA  1 
ATOM   19   C  C   A GLN   A 1 9   ? 3.59902   -23.69449 27.45916  0.500 54.76494 ? 9   GLN   A C   1 
ATOM   20   C  C   B GLN   A 1 9   ? 3.61200   -23.67953 27.47865  0.500 54.76032 ? 9   GLN   A C   1 
ATOM   21   O  O   A GLN   A 1 9   ? 3.35326   -22.61433 26.90681  0.500 54.38093 ? 9   GLN   A O   1 
ATOM   22   O  O   B GLN   A 1 9   ? 3.37036   -22.60207 26.92142  0.500 54.38037 ? 9   GLN   A O   1 
ATOM   23   C  CB  A GLN   A 1 9   ? 2.01633   -23.24256 29.32961  0.500 57.57197 ? 9   GLN   A CB  1 
ATOM   24   C  CB  B GLN   A 1 9   ? 2.02997   -23.23868 29.36781  0.500 57.55560 ? 9   GLN   A CB  1 
ATOM   25   C  CG  A GLN   A 1 9   ? 0.54092   -22.94970 29.14373  0.500 59.43207 ? 9   GLN   A CG  1 
ATOM   26   C  CG  B GLN   A 1 9   ? 0.79072   -23.67561 30.13579  0.500 59.24596 ? 9   GLN   A CG  1 
ATOM   27   C  CD  A GLN   A 1 9   ? 0.21410   -21.47243 29.26596  0.500 60.84625 ? 9   GLN   A CD  1 
ATOM   28   C  CD  B GLN   A 1 9   ? -0.34716  -24.05915 29.21203  0.500 60.32333 ? 9   GLN   A CD  1 
ATOM   29   O  OE1 A GLN   A 1 9   ? 0.13941   -20.75792 28.26635  0.500 61.25408 ? 9   GLN   A OE1 1 
ATOM   30   O  OE1 B GLN   A 1 9   ? -0.58436  -23.39771 28.20159  0.500 61.03928 ? 9   GLN   A OE1 1 
ATOM   31   N  NE2 A GLN   A 1 9   ? 0.00843   -21.00964 30.49294  0.500 62.78218 ? 9   GLN   A NE2 1 
ATOM   32   N  NE2 B GLN   A 1 9   ? -1.04722  -25.13945 29.54310  0.500 62.57928 ? 9   GLN   A NE2 1 
ATOM   33   N  N   . THR   A 1 10  ? 4.76284   -24.32561 27.30089  1.000 52.74213 ? 10  THR   A N   1 
ATOM   34   C  CA  . THR   A 1 10  ? 5.77861   -23.81113 26.38826  1.000 49.73409 ? 10  THR   A CA  1 
ATOM   35   C  C   . THR   A 1 10  ? 5.22438   -23.75361 24.96826  1.000 48.83142 ? 10  THR   A C   1 
ATOM   36   O  O   . THR   A 1 10  ? 4.54973   -24.67990 24.50980  1.000 48.46464 ? 10  THR   A O   1 
ATOM   37   C  CB  . THR   A 1 10  ? 7.02732   -24.69660 26.43550  1.000 47.09516 ? 10  THR   A CB  1 
ATOM   38   O  OG1 . THR   A 1 10  ? 7.60358   -24.65418 27.74760  1.000 47.98202 ? 10  THR   A OG1 1 
ATOM   39   C  CG2 . THR   A 1 10  ? 8.06394   -24.23192 25.42498  1.000 44.94419 ? 10  THR   A CG2 1 
ATOM   40   N  N   . THR   A 1 11  ? 5.49907   -22.65253 24.27303  1.000 48.17530 ? 11  THR   A N   1 
ATOM   41   C  CA  . THR   A 1 11  ? 4.90335   -22.40245 22.97077  1.000 46.76352 ? 11  THR   A CA  1 
ATOM   42   C  C   . THR   A 1 11  ? 5.97428   -22.13023 21.92593  1.000 45.05010 ? 11  THR   A C   1 
ATOM   43   O  O   . THR   A 1 11  ? 7.07657   -21.66989 22.23608  1.000 44.80230 ? 11  THR   A O   1 
ATOM   44   C  CB  . THR   A 1 11  ? 3.92434   -21.22368 23.01236  1.000 46.39149 ? 11  THR   A CB  1 
ATOM   45   O  OG1 . THR   A 1 11  ? 3.42620   -20.97317 21.69150  1.000 49.54636 ? 11  THR   A OG1 1 
ATOM   46   C  CG2 . THR   A 1 11  ? 4.61447   -19.97087 23.53537  1.000 45.45863 ? 11  THR   A CG2 1 
ATOM   47   N  N   A ASP   A 1 12  ? 5.62876   -22.43481 20.67536  0.500 44.68410 ? 12  ASP   A N   1 
ATOM   48   N  N   B ASP   A 1 12  ? 5.63305   -22.42465 20.67227  0.500 44.68158 ? 12  ASP   A N   1 
ATOM   49   C  CA  A ASP   A 1 12  ? 6.50804   -22.15711 19.54731  0.500 44.72837 ? 12  ASP   A CA  1 
ATOM   50   C  CA  B ASP   A 1 12  ? 6.53155   -22.14766 19.56178  0.500 44.71753 ? 12  ASP   A CA  1 
ATOM   51   C  C   A ASP   A 1 12  ? 6.40390   -20.70944 19.08474  0.500 43.66349 ? 12  ASP   A C   1 
ATOM   52   C  C   B ASP   A 1 12  ? 6.39906   -20.71720 19.05799  0.500 43.66514 ? 12  ASP   A C   1 
ATOM   53   O  O   A ASP   A 1 12  ? 7.36383   -20.17195 18.52108  0.500 44.52767 ? 12  ASP   A O   1 
ATOM   54   O  O   B ASP   A 1 12  ? 7.33963   -20.20039 18.44239  0.500 44.51617 ? 12  ASP   A O   1 
ATOM   55   C  CB  A ASP   A 1 12  ? 6.16938   -23.09516 18.38928  0.500 44.24326 ? 12  ASP   A CB  1 
ATOM   56   C  CB  B ASP   A 1 12  ? 6.25608   -23.12747 18.41553  0.500 44.21254 ? 12  ASP   A CB  1 
ATOM   57   C  CG  A ASP   A 1 12  ? 4.68936   -23.10315 18.07516  0.500 44.48736 ? 12  ASP   A CG  1 
ATOM   58   C  CG  B ASP   A 1 12  ? 7.50954   -23.51894 17.66451  0.500 43.81271 ? 12  ASP   A CG  1 
ATOM   59   O  OD1 A ASP   A 1 12  ? 3.89491   -22.84898 19.00225  0.500 44.33911 ? 12  ASP   A OD1 1 
ATOM   60   O  OD1 B ASP   A 1 12  ? 8.60752   -23.07284 18.06570  0.500 43.72107 ? 12  ASP   A OD1 1 
ATOM   61   O  OD2 A ASP   A 1 12  ? 4.31349   -23.35033 16.91269  0.500 44.89503 ? 12  ASP   A OD2 1 
ATOM   62   O  OD2 B ASP   A 1 12  ? 7.39812   -24.27404 16.67971  0.500 42.25928 ? 12  ASP   A OD2 1 
ATOM   63   N  N   . ALA   A 1 13  ? 5.25557   -20.07276 19.30286  1.000 42.75148 ? 13  ALA   A N   1 
ATOM   64   C  CA  . ALA   A 1 13  ? 4.99479   -18.70377 18.85870  1.000 43.24217 ? 13  ALA   A CA  1 
ATOM   65   C  C   . ALA   A 1 13  ? 4.48855   -17.89464 20.04520  1.000 40.31652 ? 13  ALA   A C   1 
ATOM   66   O  O   . ALA   A 1 13  ? 3.27484   -17.72223 20.22374  1.000 40.70794 ? 13  ALA   A O   1 
ATOM   67   C  CB  . ALA   A 1 13  ? 3.98974   -18.68342 17.70667  1.000 42.24536 ? 13  ALA   A CB  1 
ATOM   68   N  N   . PRO   A 1 14  ? 5.39240   -17.37677 20.87565  1.000 41.48451 ? 14  PRO   A N   1 
ATOM   69   C  CA  . PRO   A 1 14  ? 4.95969   -16.62173 22.05689  1.000 40.80857 ? 14  PRO   A CA  1 
ATOM   70   C  C   . PRO   A 1 14  ? 4.19173   -15.36571 21.67464  1.000 38.57487 ? 14  PRO   A C   1 
ATOM   71   O  O   . PRO   A 1 14  ? 4.27615   -14.86599 20.55071  1.000 39.12298 ? 14  PRO   A O   1 
ATOM   72   C  CB  . PRO   A 1 14  ? 6.27648   -16.27599 22.76202  1.000 41.08588 ? 14  PRO   A CB  1 
ATOM   73   C  CG  . PRO   A 1 14  ? 7.31158   -16.34081 21.68040  1.000 40.97459 ? 14  PRO   A CG  1 
ATOM   74   C  CD  . PRO   A 1 14  ? 6.85963   -17.43400 20.75940  1.000 41.29524 ? 14  PRO   A CD  1 
ATOM   75   N  N   . ALA   A 1 15  ? 3.42519   -14.85978 22.63769  1.000 38.68236 ? 15  ALA   A N   1 
ATOM   76   C  CA  . ALA   A 1 15  ? 2.64008   -13.65519 22.40908  1.000 38.65805 ? 15  ALA   A CA  1 
ATOM   77   C  C   . ALA   A 1 15  ? 3.55354   -12.47503 22.10139  1.000 37.62476 ? 15  ALA   A C   1 
ATOM   78   O  O   . ALA   A 1 15  ? 4.63669   -12.33898 22.67708  1.000 37.12683 ? 15  ALA   A O   1 
ATOM   79   C  CB  . ALA   A 1 15  ? 1.76819   -13.35122 23.62732  1.000 36.62599 ? 15  ALA   A CB  1 
ATOM   80   N  N   . PHE   A 1 16  ? 3.11398   -11.62814 21.16878  1.000 37.76716 ? 16  PHE   A N   1 
ATOM   81   C  CA  . PHE   A 1 16  ? 3.84616   -10.44676 20.73430  1.000 38.16449 ? 16  PHE   A CA  1 
ATOM   82   C  C   . PHE   A 1 16  ? 2.83721   -9.33308  20.48862  1.000 37.99906 ? 16  PHE   A C   1 
ATOM   83   O  O   . PHE   A 1 16  ? 1.77452   -9.58144  19.89766  1.000 36.33779 ? 16  PHE   A O   1 
ATOM   84   C  CB  . PHE   A 1 16  ? 4.65554   -10.71602 19.45488  1.000 37.58785 ? 16  PHE   A CB  1 
ATOM   85   C  CG  . PHE   A 1 16  ? 5.43546   -9.52574  18.95846  1.000 37.64181 ? 16  PHE   A CG  1 
ATOM   86   C  CD1 . PHE   A 1 16  ? 4.85929   -8.60739  18.09044  1.000 37.71495 ? 16  PHE   A CD1 1 
ATOM   87   C  CD2 . PHE   A 1 16  ? 6.74900   -9.32936  19.35566  1.000 37.07222 ? 16  PHE   A CD2 1 
ATOM   88   C  CE1 . PHE   A 1 16  ? 5.57723   -7.51224  17.63763  1.000 38.41312 ? 16  PHE   A CE1 1 
ATOM   89   C  CE2 . PHE   A 1 16  ? 7.47251   -8.23755  18.90537  1.000 38.21937 ? 16  PHE   A CE2 1 
ATOM   90   C  CZ  . PHE   A 1 16  ? 6.88639   -7.32897  18.04434  1.000 37.35303 ? 16  PHE   A CZ  1 
ATOM   91   N  N   . PRO   A 1 17  ? 3.14206   -8.09273  20.90557  1.000 37.99362 ? 17  PRO   A N   1 
ATOM   92   C  CA  . PRO   A 1 17  ? 4.39486   -7.66095  21.53779  1.000 37.11403 ? 17  PRO   A CA  1 
ATOM   93   C  C   . PRO   A 1 17  ? 4.44809   -7.89097  23.04604  1.000 37.91306 ? 17  PRO   A C   1 
ATOM   94   O  O   . PRO   A 1 17  ? 3.45952   -8.31333  23.64600  1.000 36.30483 ? 17  PRO   A O   1 
ATOM   95   C  CB  . PRO   A 1 17  ? 4.43210   -6.16497  21.22366  1.000 38.53512 ? 17  PRO   A CB  1 
ATOM   96   C  CG  . PRO   A 1 17  ? 2.99737   -5.77155  21.19577  1.000 38.76998 ? 17  PRO   A CG  1 
ATOM   97   C  CD  . PRO   A 1 17  ? 2.24868   -6.95351  20.62760  1.000 38.09757 ? 17  PRO   A CD  1 
ATOM   98   N  N   . SER   A 1 18  ? 5.60635   -7.61785  23.64333  1.000 37.44042 ? 18  SER   A N   1 
ATOM   99   C  CA  . SER   A 1 18  ? 5.79622   -7.69198  25.08318  1.000 38.86578 ? 18  SER   A CA  1 
ATOM   100  C  C   . SER   A 1 18  ? 6.11025   -6.30524  25.63112  1.000 38.51373 ? 18  SER   A C   1 
ATOM   101  O  O   . SER   A 1 18  ? 6.59586   -5.42532  24.91475  1.000 36.96529 ? 18  SER   A O   1 
ATOM   102  C  CB  . SER   A 1 18  ? 6.92103   -8.67039  25.45289  1.000 37.69937 ? 18  SER   A CB  1 
ATOM   103  O  OG  . SER   A 1 18  ? 6.60216   -9.98903  25.04839  1.000 43.06755 ? 18  SER   A OG  1 
ATOM   104  N  N   . ASN   A 1 19  ? 5.82918   -6.11922  26.91685  1.000 39.11682 ? 19  ASN   A N   1 
ATOM   105  C  CA  . ASN   A 1 19  ? 6.01255   -4.83681  27.58113  1.000 39.05144 ? 19  ASN   A CA  1 
ATOM   106  C  C   . ASN   A 1 19  ? 7.36579   -4.78419  28.27818  1.000 38.72812 ? 19  ASN   A C   1 
ATOM   107  O  O   . ASN   A 1 19  ? 7.82078   -5.77807  28.85016  1.000 39.40537 ? 19  ASN   A O   1 
ATOM   108  C  CB  . ASN   A 1 19  ? 4.89747   -4.58858  28.59842  1.000 39.72262 ? 19  ASN   A CB  1 
ATOM   109  C  CG  . ASN   A 1 19  ? 3.52190   -4.56640  27.96311  1.000 40.46373 ? 19  ASN   A CG  1 
ATOM   110  O  OD1 . ASN   A 1 19  ? 3.37941   -4.29199  26.77408  1.000 38.17591 ? 19  ASN   A OD1 1 
ATOM   111  N  ND2 . ASN   A 1 19  ? 2.49756   -4.85622  28.75894  1.000 47.61305 ? 19  ASN   A ND2 1 
ATOM   112  N  N   . ARG   A 1 20  ? 8.00496   -3.61902  28.22594  1.000 38.42648 ? 20  ARG   A N   1 
ATOM   113  C  CA  . ARG   A 1 20  ? 9.22932   -3.40964  28.98216  1.000 40.52448 ? 20  ARG   A CA  1 
ATOM   114  C  C   . ARG   A 1 20  ? 8.91642   -3.27650  30.46845  1.000 39.73904 ? 20  ARG   A C   1 
ATOM   115  O  O   . ARG   A 1 20  ? 7.86595   -2.76221  30.86410  1.000 38.46108 ? 20  ARG   A O   1 
ATOM   116  C  CB  . ARG   A 1 20  ? 9.96856   -2.16049  28.48988  1.000 38.15425 ? 20  ARG   A CB  1 
ATOM   117  C  CG  . ARG   A 1 20  ? 10.56650  -2.28800  27.09380  1.000 36.98828 ? 20  ARG   A CG  1 
ATOM   118  C  CD  . ARG   A 1 20  ? 11.30201  -1.01670  26.67106  1.000 36.48493 ? 20  ARG   A CD  1 
ATOM   119  N  NE  . ARG   A 1 20  ? 11.65967  -1.05396  25.25497  1.000 34.24805 ? 20  ARG   A NE  1 
ATOM   120  C  CZ  . ARG   A 1 20  ? 12.31528  -0.09065  24.61624  1.000 33.83000 ? 20  ARG   A CZ  1 
ATOM   121  N  NH1 . ARG   A 1 20  ? 12.69751  1.00301   25.26351  1.000 32.55771 ? 20  ARG   A NH1 1 
ATOM   122  N  NH2 . ARG   A 1 20  ? 12.58907  -0.22310  23.32481  1.000 31.44958 ? 20  ARG   A NH2 1 
ATOM   123  N  N   . SER   A 1 21  ? 9.83373   -3.77406  31.29455  1.000 41.33119 ? 21  SER   A N   1 
ATOM   124  C  CA  . SER   A 1 21  ? 9.78263   -3.55808  32.73268  1.000 41.18071 ? 21  SER   A CA  1 
ATOM   125  C  C   . SER   A 1 21  ? 10.83628  -2.57635  33.21561  1.000 41.10873 ? 21  SER   A C   1 
ATOM   126  O  O   . SER   A 1 21  ? 10.63716  -1.93057  34.24384  1.000 44.42268 ? 21  SER   A O   1 
ATOM   127  C  CB  . SER   A 1 21  ? 9.94939   -4.88878  33.47894  1.000 41.75801 ? 21  SER   A CB  1 
ATOM   128  O  OG  . SER   A 1 21  ? 11.06919  -5.61233  32.99293  1.000 42.09364 ? 21  SER   A OG  1 
ATOM   129  N  N   . CYS   A 1 22  ? 11.95122  -2.45433  32.49148  1.000 40.28218 ? 22  CYS   A N   1 
ATOM   130  C  CA  . CYS   A 1 22  ? 13.01770  -1.46938  32.58703  1.000 39.66555 ? 22  CYS   A CA  1 
ATOM   131  C  C   . CYS   A 1 22  ? 13.01274  -0.59740  31.34050  1.000 40.42749 ? 22  CYS   A C   1 
ATOM   132  O  O   . CYS   A 1 22  ? 12.94843  -1.12720  30.22578  1.000 38.33809 ? 22  CYS   A O   1 
ATOM   133  C  CB  . CYS   A 1 22  ? 14.39386  -2.12703  32.73470  1.000 39.80096 ? 22  CYS   A CB  1 
ATOM   134  S  SG  . CYS   A 1 22  ? 15.75811  -0.97220  32.91955  1.000 41.43963 ? 22  CYS   A SG  1 
ATOM   135  N  N   . PRO   A 1 23  ? 13.04810  0.73000   31.49244  1.000 38.34331 ? 23  PRO   A N   1 
ATOM   136  C  CA  . PRO   A 1 23  ? 12.88302  1.60813   30.31909  1.000 37.68569 ? 23  PRO   A CA  1 
ATOM   137  C  C   . PRO   A 1 23  ? 13.90838  1.37310   29.22174  1.000 35.93255 ? 23  PRO   A C   1 
ATOM   138  O  O   . PRO   A 1 23  ? 13.59357  1.57872   28.04364  1.000 35.13979 ? 23  PRO   A O   1 
ATOM   139  C  CB  . PRO   A 1 23  ? 13.01652  3.01670   30.91759  1.000 37.23816 ? 23  PRO   A CB  1 
ATOM   140  C  CG  . PRO   A 1 23  ? 12.72371  2.84432   32.38155  1.000 37.82867 ? 23  PRO   A CG  1 
ATOM   141  C  CD  . PRO   A 1 23  ? 13.24878  1.49432   32.73632  1.000 38.88326 ? 23  PRO   A CD  1 
ATOM   142  N  N   . TYR   A 1 24  ? 15.12369  0.93942   29.56576  1.000 35.03237 ? 24  TYR   A N   1 
ATOM   143  C  CA  . TYR   A 1 24  ? 16.19696  0.79670   28.58749  1.000 36.13652 ? 24  TYR   A CA  1 
ATOM   144  C  C   . TYR   A 1 24  ? 16.65802  -0.64783  28.41617  1.000 37.84024 ? 24  TYR   A C   1 
ATOM   145  O  O   . TYR   A 1 24  ? 17.76727  -0.88206  27.92489  1.000 36.30303 ? 24  TYR   A O   1 
ATOM   146  C  CB  . TYR   A 1 24  ? 17.38357  1.68442   28.96565  1.000 36.21226 ? 24  TYR   A CB  1 
ATOM   147  C  CG  . TYR   A 1 24  ? 17.82664  1.55105   30.40473  1.000 37.15136 ? 24  TYR   A CG  1 
ATOM   148  C  CD1 . TYR   A 1 24  ? 18.72089  0.55873   30.78885  1.000 36.99025 ? 24  TYR   A CD1 1 
ATOM   149  C  CD2 . TYR   A 1 24  ? 17.36006  2.42635   31.37813  1.000 36.61174 ? 24  TYR   A CD2 1 
ATOM   150  C  CE1 . TYR   A 1 24  ? 19.13217  0.43668   32.10312  1.000 37.59123 ? 24  TYR   A CE1 1 
ATOM   151  C  CE2 . TYR   A 1 24  ? 17.76607  2.31297   32.69602  1.000 36.84232 ? 24  TYR   A CE2 1 
ATOM   152  C  CZ  . TYR   A 1 24  ? 18.65266  1.31703   33.05211  1.000 37.74588 ? 24  TYR   A CZ  1 
ATOM   153  O  OH  . TYR   A 1 24  ? 19.06053  1.20136   34.36112  1.000 39.69994 ? 24  TYR   A OH  1 
ATOM   154  N  N   . GLN   A 1 25  ? 15.83964  -1.62325  28.80041  1.000 35.70117 ? 25  GLN   A N   1 
ATOM   155  C  CA  . GLN   A 1 25  ? 16.15869  -3.02357  28.56505  1.000 39.57786 ? 25  GLN   A CA  1 
ATOM   156  C  C   . GLN   A 1 25  ? 15.04129  -3.70664  27.79015  1.000 36.22030 ? 25  GLN   A C   1 
ATOM   157  O  O   . GLN   A 1 25  ? 13.86249  -3.36288  27.92370  1.000 33.64659 ? 25  GLN   A O   1 
ATOM   158  C  CB  . GLN   A 1 25  ? 16.41467  -3.78184  29.87551  1.000 38.44631 ? 25  GLN   A CB  1 
ATOM   159  C  CG  . GLN   A 1 25  ? 17.88127  -3.82006  30.27782  1.000 40.09957 ? 25  GLN   A CG  1 
ATOM   160  C  CD  . GLN   A 1 25  ? 18.79372  -4.27390  29.14266  1.000 45.13872 ? 25  GLN   A CD  1 
ATOM   161  O  OE1 . GLN   A 1 25  ? 18.46781  -5.19644  28.39076  1.000 45.72144 ? 25  GLN   A OE1 1 
ATOM   162  N  NE2 . GLN   A 1 25  ? 19.94425  -3.62015  29.01445  1.000 42.86677 ? 25  GLN   A NE2 1 
ATOM   163  N  N   . LEU   A 1 26  ? 15.43171  -4.67674  26.97326  1.000 38.99147 ? 26  LEU   A N   1 
ATOM   164  C  CA  . LEU   A 1 26  ? 14.45471  -5.48571  26.26504  1.000 38.26246 ? 26  LEU   A CA  1 
ATOM   165  C  C   . LEU   A 1 26  ? 13.53922  -6.18500  27.26568  1.000 37.45939 ? 26  LEU   A C   1 
ATOM   166  O  O   . LEU   A 1 26  ? 13.98985  -6.58275  28.34718  1.000 41.60776 ? 26  LEU   A O   1 
ATOM   167  C  CB  . LEU   A 1 26  ? 15.15262  -6.53037  25.39201  1.000 38.45386 ? 26  LEU   A CB  1 
ATOM   168  C  CG  . LEU   A 1 26  ? 16.01333  -6.04775  24.22511  1.000 37.02188 ? 26  LEU   A CG  1 
ATOM   169  C  CD1 . LEU   A 1 26  ? 16.71963  -7.22839  23.57924  1.000 39.59306 ? 26  LEU   A CD1 1 
ATOM   170  C  CD2 . LEU   A 1 26  ? 15.16018  -5.30747  23.20714  1.000 36.62095 ? 26  LEU   A CD2 1 
ATOM   171  N  N   . PRO   A 1 27  ? 12.25533  -6.33812  26.95287  1.000 37.39655 ? 27  PRO   A N   1 
ATOM   172  C  CA  . PRO   A 1 27  ? 11.41861  -7.24876  27.73867  1.000 39.68732 ? 27  PRO   A CA  1 
ATOM   173  C  C   . PRO   A 1 27  ? 12.04965  -8.63343  27.75989  1.000 39.13283 ? 27  PRO   A C   1 
ATOM   174  O  O   . PRO   A 1 27  ? 12.78478  -9.01078  26.84449  1.000 37.72123 ? 27  PRO   A O   1 
ATOM   175  C  CB  . PRO   A 1 27  ? 10.08220  -7.24420  26.98788  1.000 38.62263 ? 27  PRO   A CB  1 
ATOM   176  C  CG  . PRO   A 1 27  ? 10.07593  -5.94067  26.23839  1.000 38.22030 ? 27  PRO   A CG  1 
ATOM   177  C  CD  . PRO   A 1 27  ? 11.50553  -5.67977  25.86943  1.000 37.97207 ? 27  PRO   A CD  1 
ATOM   178  N  N   . ASP   A 1 28  ? 11.77337  -9.38453  28.83048  1.000 40.79736 ? 28  ASP   A N   1 
ATOM   179  C  CA  . ASP   A 1 28  ? 12.36528  -10.71295 28.97135  1.000 41.44941 ? 28  ASP   A CA  1 
ATOM   180  C  C   . ASP   A 1 28  ? 12.10940  -11.57038 27.73905  1.000 40.11282 ? 28  ASP   A C   1 
ATOM   181  O  O   . ASP   A 1 28  ? 12.99884  -12.29886 27.28302  1.000 41.34137 ? 28  ASP   A O   1 
ATOM   182  C  CB  . ASP   A 1 28  ? 11.82248  -11.40675 30.22174  1.000 43.52650 ? 28  ASP   A CB  1 
ATOM   183  C  CG  . ASP   A 1 28  ? 12.37410  -10.81629 31.50405  1.000 47.42880 ? 28  ASP   A CG  1 
ATOM   184  O  OD1 . ASP   A 1 28  ? 13.47332  -10.22260 31.46706  1.000 45.77112 ? 28  ASP   A OD1 1 
ATOM   185  O  OD2 . ASP   A 1 28  ? 11.70874  -10.95282 32.55180  1.000 52.84718 ? 28  ASP   A OD2 1 
ATOM   186  N  N   . GLY   A 1 29  ? 10.90155  -11.48686 27.17906  1.000 38.70834 ? 29  GLY   A N   1 
ATOM   187  C  CA  . GLY   A 1 29  ? 10.59416  -12.26699 25.99138  1.000 39.37989 ? 29  GLY   A CA  1 
ATOM   188  C  C   . GLY   A 1 29  ? 11.42403  -11.86052 24.78868  1.000 39.86119 ? 29  GLY   A C   1 
ATOM   189  O  O   . GLY   A 1 29  ? 11.82595  -12.70747 23.98667  1.000 40.35890 ? 29  GLY   A O   1 
ATOM   190  N  N   . TYR   A 1 30  ? 11.69502  -10.55897 24.64630  1.000 38.12526 ? 30  TYR   A N   1 
ATOM   191  C  CA  . TYR   A 1 30  ? 12.49441  -10.09499 23.51523  1.000 39.23956 ? 30  TYR   A CA  1 
ATOM   192  C  C   . TYR   A 1 30  ? 13.93308  -10.58362 23.62030  1.000 38.73363 ? 30  TYR   A C   1 
ATOM   193  O  O   . TYR   A 1 30  ? 14.54196  -10.95856 22.61154  1.000 39.61171 ? 30  TYR   A O   1 
ATOM   194  C  CB  . TYR   A 1 30  ? 12.46120  -8.56858  23.42094  1.000 36.30196 ? 30  TYR   A CB  1 
ATOM   195  C  CG  . TYR   A 1 30  ? 11.15814  -7.98537  22.91722  1.000 36.39739 ? 30  TYR   A CG  1 
ATOM   196  C  CD1 . TYR   A 1 30  ? 9.99829   -8.74869  22.85883  1.000 36.31521 ? 30  TYR   A CD1 1 
ATOM   197  C  CD2 . TYR   A 1 30  ? 11.09373  -6.66389  22.49133  1.000 37.23366 ? 30  TYR   A CD2 1 
ATOM   198  C  CE1 . TYR   A 1 30  ? 8.81007   -8.20877  22.39971  1.000 36.95587 ? 30  TYR   A CE1 1 
ATOM   199  C  CE2 . TYR   A 1 30  ? 9.91295   -6.11701  22.03142  1.000 35.88909 ? 30  TYR   A CE2 1 
ATOM   200  C  CZ  . TYR   A 1 30  ? 8.77554   -6.89222  21.98598  1.000 36.80383 ? 30  TYR   A CZ  1 
ATOM   201  O  OH  . TYR   A 1 30  ? 7.60309   -6.34306  21.52684  1.000 36.04867 ? 30  TYR   A OH  1 
ATOM   202  N  N   . ALA   A 1 31  ? 14.49530  -10.58068 24.83230  1.000 40.09829 ? 31  ALA   A N   1 
ATOM   203  C  CA  . ALA   A 1 31  ? 15.84393  -11.10313 25.02093  1.000 40.97719 ? 31  ALA   A CA  1 
ATOM   204  C  C   . ALA   A 1 31  ? 15.91927  -12.58500 24.67738  1.000 42.67594 ? 31  ALA   A C   1 
ATOM   205  O  O   . ALA   A 1 31  ? 16.95129  -13.05743 24.18523  1.000 42.73625 ? 31  ALA   A O   1 
ATOM   206  C  CB  . ALA   A 1 31  ? 16.30375  -10.86025 26.45840  1.000 40.82459 ? 31  ALA   A CB  1 
ATOM   207  N  N   . GLN   A 1 32  ? 14.84137  -13.33186 24.92814  1.000 41.88747 ? 32  GLN   A N   1 
ATOM   208  C  CA  . GLN   A 1 32  ? 14.79214  -14.72701 24.50287  1.000 44.78757 ? 32  GLN   A CA  1 
ATOM   209  C  C   . GLN   A 1 32  ? 14.82301  -14.82831 22.98359  1.000 43.81680 ? 32  GLN   A C   1 
ATOM   210  O  O   . GLN   A 1 32  ? 15.57991  -15.62498 22.41718  1.000 45.20213 ? 32  GLN   A O   1 
ATOM   211  C  CB  . GLN   A 1 32  ? 13.54206  -15.40475 25.06745  1.000 45.14718 ? 32  GLN   A CB  1 
ATOM   212  C  CG  . GLN   A 1 32  ? 13.28951  -16.80437 24.51971  1.000 48.36172 ? 32  GLN   A CG  1 
ATOM   213  C  CD  . GLN   A 1 32  ? 14.39872  -17.78357 24.86824  1.000 50.37949 ? 32  GLN   A CD  1 
ATOM   214  O  OE1 . GLN   A 1 32  ? 15.09125  -18.29669 23.98694  1.000 50.72650 ? 32  GLN   A OE1 1 
ATOM   215  N  NE2 . GLN   A 1 32  ? 14.56824  -18.05104 26.15857  1.000 49.91028 ? 32  GLN   A NE2 1 
ATOM   216  N  N   . LEU   A 1 33  ? 14.00630  -14.01588 22.30588  1.000 43.17175 ? 33  LEU   A N   1 
ATOM   217  C  CA  . LEU   A 1 33  ? 14.03259  -13.98051 20.84683  1.000 42.45126 ? 33  LEU   A CA  1 
ATOM   218  C  C   . LEU   A 1 33  ? 15.40804  -13.57880 20.32971  1.000 42.05096 ? 33  LEU   A C   1 
ATOM   219  O  O   . LEU   A 1 33  ? 15.87996  -14.11239 19.31895  1.000 41.57030 ? 33  LEU   A O   1 
ATOM   220  C  CB  . LEU   A 1 33  ? 12.96456  -13.01753 20.32704  1.000 40.82185 ? 33  LEU   A CB  1 
ATOM   221  C  CG  . LEU   A 1 33  ? 11.50445  -13.36954 20.62066  1.000 39.72264 ? 33  LEU   A CG  1 
ATOM   222  C  CD1 . LEU   A 1 33  ? 10.57934  -12.25012 20.16147  1.000 38.82114 ? 33  LEU   A CD1 1 
ATOM   223  C  CD2 . LEU   A 1 33  ? 11.12715  -14.68745 19.95446  1.000 40.69288 ? 33  LEU   A CD2 1 
ATOM   224  N  N   . ARG   A 1 34  ? 16.06687  -12.63799 21.01169  1.000 42.63673 ? 34  ARG   A N   1 
ATOM   225  C  CA  . ARG   A 1 34  ? 17.39468  -12.20688 20.58612  1.000 42.19176 ? 34  ARG   A CA  1 
ATOM   226  C  C   . ARG   A 1 34  ? 18.39661  -13.35318 20.65647  1.000 43.78127 ? 34  ARG   A C   1 
ATOM   227  O  O   . ARG   A 1 34  ? 19.27406  -13.47485 19.79352  1.000 40.42348 ? 34  ARG   A O   1 
ATOM   228  C  CB  . ARG   A 1 34  ? 17.86060  -11.02861 21.44560  1.000 41.95610 ? 34  ARG   A CB  1 
ATOM   229  C  CG  . ARG   A 1 34  ? 19.18454  -10.40296 21.01221  1.000 41.18464 ? 34  ARG   A CG  1 
ATOM   230  C  CD  . ARG   A 1 34  ? 20.36686  -10.96893 21.79112  1.000 43.04539 ? 34  ARG   A CD  1 
ATOM   231  N  NE  . ARG   A 1 34  ? 20.15272  -10.90032 23.23378  1.000 43.59224 ? 34  ARG   A NE  1 
ATOM   232  C  CZ  . ARG   A 1 34  ? 20.42417  -9.83550  23.98095  1.000 43.37764 ? 34  ARG   A CZ  1 
ATOM   233  N  NH1 . ARG   A 1 34  ? 20.92401  -8.73953  23.42301  1.000 41.12430 ? 34  ARG   A NH1 1 
ATOM   234  N  NH2 . ARG   A 1 34  ? 20.19466  -9.86497  25.28675  1.000 43.89642 ? 34  ARG   A NH2 1 
ATOM   235  N  N   . ASP   A 1 35  ? 18.28126  -14.20574 21.67696  1.000 44.33036 ? 35  ASP   A N   1 
ATOM   236  C  CA  . ASP   A 1 35  ? 19.26323  -15.26546 21.87708  1.000 45.76995 ? 35  ASP   A CA  1 
ATOM   237  C  C   . ASP   A 1 35  ? 19.04438  -16.45102 20.94517  1.000 48.33113 ? 35  ASP   A C   1 
ATOM   238  O  O   . ASP   A 1 35  ? 20.01311  -17.12310 20.57376  1.000 48.70075 ? 35  ASP   A O   1 
ATOM   239  C  CB  . ASP   A 1 35  ? 19.23846  -15.73682 23.33079  1.000 46.87606 ? 35  ASP   A CB  1 
ATOM   240  C  CG  . ASP   A 1 35  ? 19.81093  -14.70937 24.28528  1.000 46.27012 ? 35  ASP   A CG  1 
ATOM   241  O  OD1 . ASP   A 1 35  ? 20.66627  -13.90551 23.85439  1.000 46.84629 ? 35  ASP   A OD1 1 
ATOM   242  O  OD2 . ASP   A 1 35  ? 19.40956  -14.70961 25.46866  1.000 46.53536 ? 35  ASP   A OD2 1 
ATOM   243  N  N   . THR   A 1 36  ? 17.80271  -16.72165 20.56070  1.000 46.02647 ? 36  THR   A N   1 
ATOM   244  C  CA  . THR   A 1 36  ? 17.51681  -17.88205 19.72433  1.000 46.33077 ? 36  THR   A CA  1 
ATOM   245  C  C   . THR   A 1 36  ? 18.16229  -17.71352 18.35354  1.000 45.93434 ? 36  THR   A C   1 
ATOM   246  O  O   . THR   A 1 36  ? 17.96034  -16.68158 17.70240  1.000 43.98380 ? 36  THR   A O   1 
ATOM   247  C  CB  . THR   A 1 36  ? 16.01043  -18.08009 19.57984  1.000 46.43112 ? 36  THR   A CB  1 
ATOM   248  O  OG1 . THR   A 1 36  ? 15.42621  -18.24858 20.87896  1.000 50.50166 ? 36  THR   A OG1 1 
ATOM   249  C  CG2 . THR   A 1 36  ? 15.71085  -19.31162 18.73305  1.000 46.49922 ? 36  THR   A CG2 1 
ATOM   250  N  N   . PRO   A 1 37  ? 18.94210  -18.69005 17.88739  1.000 45.75552 ? 37  PRO   A N   1 
ATOM   251  C  CA  . PRO   A 1 37  ? 19.61887  -18.54643 16.59365  1.000 45.62406 ? 37  PRO   A CA  1 
ATOM   252  C  C   . PRO   A 1 37  ? 18.62744  -18.45207 15.44358  1.000 43.62760 ? 37  PRO   A C   1 
ATOM   253  O  O   . PRO   A 1 37  ? 17.45822  -18.82596 15.55408  1.000 43.03655 ? 37  PRO   A O   1 
ATOM   254  C  CB  . PRO   A 1 37  ? 20.46978  -19.82064 16.48935  1.000 45.70949 ? 37  PRO   A CB  1 
ATOM   255  C  CG  . PRO   A 1 37  ? 20.60465  -20.31173 17.89681  1.000 46.08058 ? 37  PRO   A CG  1 
ATOM   256  C  CD  . PRO   A 1 37  ? 19.32444  -19.93323 18.57744  1.000 46.35651 ? 37  PRO   A CD  1 
ATOM   257  N  N   . GLY   A 1 38  ? 19.11770  -17.94024 14.32074  1.000 43.52742 ? 38  GLY   A N   1 
ATOM   258  C  CA  . GLY   A 1 38  ? 18.29353  -17.74903 13.15348  1.000 42.96139 ? 38  GLY   A CA  1 
ATOM   259  C  C   . GLY   A 1 38  ? 17.71292  -16.35143 13.10287  1.000 40.83548 ? 38  GLY   A C   1 
ATOM   260  O  O   . GLY   A 1 38  ? 17.53316  -15.68881 14.12928  1.000 39.63098 ? 38  GLY   A O   1 
ATOM   261  N  N   . PRO   A 1 39  ? 17.40333  -15.87639 11.89354  1.000 39.72250 ? 39  PRO   A N   1 
ATOM   262  C  CA  . PRO   A 1 39  ? 16.91149  -14.50156 11.73923  1.000 40.02704 ? 39  PRO   A CA  1 
ATOM   263  C  C   . PRO   A 1 39  ? 15.42908  -14.32654 12.01705  1.000 38.81731 ? 39  PRO   A C   1 
ATOM   264  O  O   . PRO   A 1 39  ? 14.97617  -13.18051 12.14786  1.000 37.20567 ? 39  PRO   A O   1 
ATOM   265  C  CB  . PRO   A 1 39  ? 17.21941  -14.19933 10.27078  1.000 40.36724 ? 39  PRO   A CB  1 
ATOM   266  C  CG  . PRO   A 1 39  ? 17.08261  -15.52700 9.60063   1.000 41.80263 ? 39  PRO   A CG  1 
ATOM   267  C  CD  . PRO   A 1 39  ? 17.59194  -16.54485 10.59342  1.000 42.61343 ? 39  PRO   A CD  1 
ATOM   268  N  N   . LEU   A 1 40  ? 14.66066  -15.40801 12.10226  1.000 38.33420 ? 40  LEU   A N   1 
ATOM   269  C  CA  . LEU   A 1 40  ? 13.21293  -15.32160 12.19200  1.000 37.58981 ? 40  LEU   A CA  1 
ATOM   270  C  C   . LEU   A 1 40  ? 12.71480  -16.12187 13.38447  1.000 38.74545 ? 40  LEU   A C   1 
ATOM   271  O  O   . LEU   A 1 40  ? 13.40457  -17.00227 13.90388  1.000 39.43018 ? 40  LEU   A O   1 
ATOM   272  C  CB  . LEU   A 1 40  ? 12.54322  -15.83062 10.90982  1.000 39.18579 ? 40  LEU   A CB  1 
ATOM   273  C  CG  . LEU   A 1 40  ? 12.90779  -15.08762 9.62505   1.000 39.99110 ? 40  LEU   A CG  1 
ATOM   274  C  CD1 . LEU   A 1 40  ? 12.38204  -15.83707 8.41094   1.000 41.19051 ? 40  LEU   A CD1 1 
ATOM   275  C  CD2 . LEU   A 1 40  ? 12.36479  -13.66938 9.66105   1.000 37.21692 ? 40  LEU   A CD2 1 
ATOM   276  N  N   . HIS   A 1 41  ? 11.49705  -15.80073 13.81214  1.000 37.09844 ? 41  HIS   A N   1 
ATOM   277  C  CA  . HIS   A 1 41  ? 10.84272  -16.54647 14.87484  1.000 38.18588 ? 41  HIS   A CA  1 
ATOM   278  C  C   . HIS   A 1 41  ? 9.34632   -16.29517 14.78923  1.000 39.48442 ? 41  HIS   A C   1 
ATOM   279  O  O   . HIS   A 1 41  ? 8.91723   -15.18917 14.45411  1.000 36.23878 ? 41  HIS   A O   1 
ATOM   280  C  CB  . HIS   A 1 41  ? 11.37350  -16.14546 16.25599  1.000 39.63486 ? 41  HIS   A CB  1 
ATOM   281  C  CG  . HIS   A 1 41  ? 11.13512  -17.17588 17.31542  1.000 39.72898 ? 41  HIS   A CG  1 
ATOM   282  N  ND1 . HIS   A 1 41  ? 9.87920   -17.46820 17.80202  1.000 39.78645 ? 41  HIS   A ND1 1 
ATOM   283  C  CD2 . HIS   A 1 41  ? 11.99351  -17.98574 17.97899  1.000 41.20848 ? 41  HIS   A CD2 1 
ATOM   284  C  CE1 . HIS   A 1 41  ? 9.97426   -18.41206 18.72104  1.000 41.57323 ? 41  HIS   A CE1 1 
ATOM   285  N  NE2 . HIS   A 1 41  ? 11.24649  -18.74385 18.84692  1.000 42.11575 ? 41  HIS   A NE2 1 
ATOM   286  N  N   . ARG   A 1 42  ? 8.56282   -17.32229 15.09336  1.000 38.47722 ? 42  ARG   A N   1 
ATOM   287  C  CA  . ARG   A 1 42  ? 7.11484   -17.19677 15.08062  1.000 38.95786 ? 42  ARG   A CA  1 
ATOM   288  C  C   . ARG   A 1 42  ? 6.62443   -16.50093 16.34380  1.000 39.40304 ? 42  ARG   A C   1 
ATOM   289  O  O   . ARG   A 1 42  ? 7.22990   -16.60819 17.41611  1.000 39.14292 ? 42  ARG   A O   1 
ATOM   290  C  CB  . ARG   A 1 42  ? 6.45881   -18.57241 14.95800  1.000 41.53051 ? 42  ARG   A CB  1 
ATOM   291  C  CG  . ARG   A 1 42  ? 6.79332   -19.30062 13.66818  1.000 41.49315 ? 42  ARG   A CG  1 
ATOM   292  C  CD  . ARG   A 1 42  ? 6.08916   -18.67256 12.47643  1.000 42.42295 ? 42  ARG   A CD  1 
ATOM   293  N  NE  . ARG   A 1 42  ? 4.70638   -19.12306 12.34128  1.000 43.95822 ? 42  ARG   A NE  1 
ATOM   294  C  CZ  . ARG   A 1 42  ? 3.86093   -18.65898 11.42686  1.000 47.10510 ? 42  ARG   A CZ  1 
ATOM   295  N  NH1 . ARG   A 1 42  ? 4.25716   -17.72518 10.57045  1.000 44.29110 ? 42  ARG   A NH1 1 
ATOM   296  N  NH2 . ARG   A 1 42  ? 2.62042   -19.12369 11.36788  1.000 46.16329 ? 42  ARG   A NH2 1 
ATOM   297  N  N   . VAL   A 1 43  ? 5.51071   -15.77801 16.20492  1.000 37.19932 ? 43  VAL   A N   1 
ATOM   298  C  CA  . VAL   A 1 43  ? 4.86834   -15.08567 17.31527  1.000 38.82544 ? 43  VAL   A CA  1 
ATOM   299  C  C   . VAL   A 1 43  ? 3.36337   -15.16374 17.11642  1.000 38.71205 ? 43  VAL   A C   1 
ATOM   300  O  O   . VAL   A 1 43  ? 2.87129   -15.41363 16.01418  1.000 36.81297 ? 43  VAL   A O   1 
ATOM   301  C  CB  . VAL   A 1 43  ? 5.29776   -13.60385 17.43688  1.000 36.82667 ? 43  VAL   A CB  1 
ATOM   302  C  CG1 . VAL   A 1 43  ? 6.77054   -13.48515 17.79181  1.000 35.17794 ? 43  VAL   A CG1 1 
ATOM   303  C  CG2 . VAL   A 1 43  ? 4.98744   -12.85543 16.14261  1.000 35.00985 ? 43  VAL   A CG2 1 
ATOM   304  N  N   . THR   A 1 44  ? 2.62831   -14.92297 18.20018  1.000 38.81090 ? 44  THR   A N   1 
ATOM   305  C  CA  . THR   A 1 44  ? 1.17089   -14.91399 18.18514  1.000 40.13050 ? 44  THR   A CA  1 
ATOM   306  C  C   . THR   A 1 44  ? 0.68479   -13.50462 18.49439  1.000 39.94273 ? 44  THR   A C   1 
ATOM   307  O  O   . THR   A 1 44  ? 0.95654   -12.97377 19.57698  1.000 40.23739 ? 44  THR   A O   1 
ATOM   308  C  CB  . THR   A 1 44  ? 0.60671   -15.91369 19.19538  1.000 40.30106 ? 44  THR   A CB  1 
ATOM   309  O  OG1 . THR   A 1 44  ? 1.09204   -17.22593 18.88769  1.000 39.34450 ? 44  THR   A OG1 1 
ATOM   310  C  CG2 . THR   A 1 44  ? -0.91679  -15.91682 19.15074  1.000 40.85455 ? 44  THR   A CG2 1 
ATOM   311  N  N   . LEU   A 1 45  ? -0.03405  -12.90618 17.54904  1.000 40.14690 ? 45  LEU   A N   1 
ATOM   312  C  CA  . LEU   A 1 45  ? -0.52812  -11.54587 17.69895  1.000 42.10051 ? 45  LEU   A CA  1 
ATOM   313  C  C   . LEU   A 1 45  ? -1.76534  -11.52885 18.59539  1.000 43.27356 ? 45  LEU   A C   1 
ATOM   314  O  O   . LEU   A 1 45  ? -2.27769  -12.57090 19.01567  1.000 42.93662 ? 45  LEU   A O   1 
ATOM   315  C  CB  . LEU   A 1 45  ? -0.81560  -10.93536 16.32620  1.000 42.21398 ? 45  LEU   A CB  1 
ATOM   316  C  CG  . LEU   A 1 45  ? 0.31851   -10.16519 15.62953  1.000 41.19585 ? 45  LEU   A CG  1 
ATOM   317  C  CD1 . LEU   A 1 45  ? 1.70552   -10.61295 16.07445  1.000 37.69764 ? 45  LEU   A CD1 1 
ATOM   318  C  CD2 . LEU   A 1 45  ? 0.18607   -10.27855 14.11788  1.000 41.29145 ? 45  LEU   A CD2 1 
ATOM   319  N  N   . TYR   A 1 46  ? -2.26416  -10.31949 18.87683  1.000 42.19828 ? 46  TYR   A N   1 
ATOM   320  C  CA  . TYR   A 1 46  ? -3.32551  -10.15080 19.86383  1.000 43.68175 ? 46  TYR   A CA  1 
ATOM   321  C  C   . TYR   A 1 46  ? -4.61976  -10.84724 19.46680  1.000 45.01271 ? 46  TYR   A C   1 
ATOM   322  O  O   . TYR   A 1 46  ? -5.43956  -11.14168 20.34326  1.000 45.15803 ? 46  TYR   A O   1 
ATOM   323  C  CB  . TYR   A 1 46  ? -3.59713  -8.66227  20.09911  1.000 44.36505 ? 46  TYR   A CB  1 
ATOM   324  C  CG  . TYR   A 1 46  ? -4.47964  -8.01359  19.04866  1.000 45.02438 ? 46  TYR   A CG  1 
ATOM   325  C  CD1 . TYR   A 1 46  ? -3.94736  -7.55694  17.84960  1.000 44.47761 ? 46  TYR   A CD1 1 
ATOM   326  C  CD2 . TYR   A 1 46  ? -5.84320  -7.84772  19.26263  1.000 45.67597 ? 46  TYR   A CD2 1 
ATOM   327  C  CE1 . TYR   A 1 46  ? -4.74879  -6.96411  16.89071  1.000 45.40514 ? 46  TYR   A CE1 1 
ATOM   328  C  CE2 . TYR   A 1 46  ? -6.65079  -7.25879  18.30866  1.000 46.99133 ? 46  TYR   A CE2 1 
ATOM   329  C  CZ  . TYR   A 1 46  ? -6.09964  -6.81769  17.12699  1.000 46.69035 ? 46  TYR   A CZ  1 
ATOM   330  O  OH  . TYR   A 1 46  ? -6.90676  -6.22829  16.18045  1.000 48.73802 ? 46  TYR   A OH  1 
ATOM   331  N  N   . ASP   A 1 47  ? -4.83033  -11.10692 18.17657  1.000 45.38596 ? 47  ASP   A N   1 
ATOM   332  C  CA  . ASP   A 1 47  ? -6.06642  -11.71086 17.69758  1.000 46.57106 ? 47  ASP   A CA  1 
ATOM   333  C  C   . ASP   A 1 47  ? -5.90925  -13.18361 17.33438  1.000 46.11928 ? 47  ASP   A C   1 
ATOM   334  O  O   . ASP   A 1 47  ? -6.79990  -13.75000 16.69352  1.000 47.03124 ? 47  ASP   A O   1 
ATOM   335  C  CB  . ASP   A 1 47  ? -6.60525  -10.93115 16.49545  1.000 46.26587 ? 47  ASP   A CB  1 
ATOM   336  C  CG  . ASP   A 1 47  ? -5.70980  -11.03991 15.27496  1.000 48.03799 ? 47  ASP   A CG  1 
ATOM   337  O  OD1 . ASP   A 1 47  ? -4.51647  -11.37976 15.42873  1.000 47.51867 ? 47  ASP   A OD1 1 
ATOM   338  O  OD2 . ASP   A 1 47  ? -6.20083  -10.77588 14.15651  1.000 49.66788 ? 47  ASP   A OD2 1 
ATOM   339  N  N   . GLY   A 1 48  ? -4.79903  -13.81320 17.71660  1.000 46.22747 ? 48  GLY   A N   1 
ATOM   340  C  CA  . GLY   A 1 48  ? -4.59202  -15.22835 17.50560  1.000 45.98986 ? 48  GLY   A CA  1 
ATOM   341  C  C   . GLY   A 1 48  ? -3.78430  -15.58827 16.27351  1.000 46.06463 ? 48  GLY   A C   1 
ATOM   342  O  O   . GLY   A 1 48  ? -3.20074  -16.67764 16.23538  1.000 45.74703 ? 48  GLY   A O   1 
ATOM   343  N  N   . ARG   A 1 49  ? -3.73578  -14.71680 15.26834  1.000 46.46301 ? 49  ARG   A N   1 
ATOM   344  C  CA  . ARG   A 1 49  ? -2.96498  -15.01735 14.06895  1.000 47.27081 ? 49  ARG   A CA  1 
ATOM   345  C  C   . ARG   A 1 49  ? -1.47758  -15.08099 14.38889  1.000 45.20501 ? 49  ARG   A C   1 
ATOM   346  O  O   . ARG   A 1 49  ? -0.97455  -14.33862 15.23531  1.000 42.94469 ? 49  ARG   A O   1 
ATOM   347  C  CB  . ARG   A 1 49  ? -3.21907  -13.96831 12.98606  1.000 49.38311 ? 49  ARG   A CB  1 
ATOM   348  C  CG  . ARG   A 1 49  ? -4.65319  -13.90237 12.49178  1.000 50.96501 ? 49  ARG   A CG  1 
ATOM   349  C  CD  . ARG   A 1 49  ? -4.82588  -12.82084 11.43159  1.000 53.51032 ? 49  ARG   A CD  1 
ATOM   350  N  NE  . ARG   A 1 49  ? -4.23522  -11.54883 11.84258  1.000 58.08716 ? 49  ARG   A NE  1 
ATOM   351  C  CZ  . ARG   A 1 49  ? -3.18363  -10.98676 11.25335  1.000 55.79243 ? 49  ARG   A CZ  1 
ATOM   352  N  NH1 . ARG   A 1 49  ? -2.60945  -11.57873 10.21389  1.000 50.85724 ? 49  ARG   A NH1 1 
ATOM   353  N  NH2 . ARG   A 1 49  ? -2.71054  -9.82891  11.69782  1.000 49.15852 ? 49  ARG   A NH2 1 
ATOM   354  N  N   . GLN   A 1 50  ? -0.77456  -15.97660 13.70888  1.000 44.56606 ? 50  GLN   A N   1 
ATOM   355  C  CA  . GLN   A 1 50  ? 0.66878   -16.07106 13.84670  1.000 43.64308 ? 50  GLN   A CA  1 
ATOM   356  C  C   . GLN   A 1 50  ? 1.35953   -15.19394 12.80924  1.000 42.26678 ? 50  GLN   A C   1 
ATOM   357  O  O   . GLN   A 1 50  ? 0.80306   -14.88998 11.75087  1.000 43.45954 ? 50  GLN   A O   1 
ATOM   358  C  CB  . GLN   A 1 50  ? 1.14122   -17.51941 13.70590  1.000 44.54009 ? 50  GLN   A CB  1 
ATOM   359  C  CG  . GLN   A 1 50  ? 0.90592   -18.37725 14.94139  1.000 44.91262 ? 50  GLN   A CG  1 
ATOM   360  C  CD  . GLN   A 1 50  ? 1.67492   -19.68961 14.90532  1.000 46.19525 ? 50  GLN   A CD  1 
ATOM   361  O  OE1 . GLN   A 1 50  ? 2.32304   -20.02082 13.91093  1.000 45.42549 ? 50  GLN   A OE1 1 
ATOM   362  N  NE2 . GLN   A 1 50  ? 1.60814   -20.44138 15.99737  1.000 46.18199 ? 50  GLN   A NE2 1 
ATOM   363  N  N   . ALA   A 1 51  ? 2.58438   -14.78401 13.12971  1.000 40.65175 ? 51  ALA   A N   1 
ATOM   364  C  CA  . ALA   A 1 51  ? 3.37562   -13.94938 12.24000  1.000 39.61917 ? 51  ALA   A CA  1 
ATOM   365  C  C   . ALA   A 1 51  ? 4.84995   -14.20735 12.51085  1.000 38.57595 ? 51  ALA   A C   1 
ATOM   366  O  O   . ALA   A 1 51  ? 5.21920   -14.86166 13.48857  1.000 39.01822 ? 51  ALA   A O   1 
ATOM   367  C  CB  . ALA   A 1 51  ? 3.03925   -12.46345 12.41530  1.000 39.37862 ? 51  ALA   A CB  1 
ATOM   368  N  N   . TRP   A 1 52  ? 5.69265   -13.68735 11.62486  1.000 37.52347 ? 52  TRP   A N   1 
ATOM   369  C  CA  . TRP   A 1 52  ? 7.13765   -13.76336 11.77816  1.000 37.23779 ? 52  TRP   A CA  1 
ATOM   370  C  C   . TRP   A 1 52  ? 7.66283   -12.49341 12.43424  1.000 37.45345 ? 52  TRP   A C   1 
ATOM   371  O  O   . TRP   A 1 52  ? 7.14289   -11.39836 12.20080  1.000 35.34719 ? 52  TRP   A O   1 
ATOM   372  C  CB  . TRP   A 1 52  ? 7.83038   -13.95560 10.42791  1.000 37.48576 ? 52  TRP   A CB  1 
ATOM   373  C  CG  . TRP   A 1 52  ? 7.59625   -15.28304 9.78000   1.000 40.19375 ? 52  TRP   A CG  1 
ATOM   374  C  CD1 . TRP   A 1 52  ? 6.81614   -15.53500 8.69010   1.000 41.01753 ? 52  TRP   A CD1 1 
ATOM   375  C  CD2 . TRP   A 1 52  ? 8.15935   -16.54273 10.17092  1.000 40.42628 ? 52  TRP   A CD2 1 
ATOM   376  N  NE1 . TRP   A 1 52  ? 6.85487   -16.87297 8.37935   1.000 41.00163 ? 52  TRP   A NE1 1 
ATOM   377  C  CE2 . TRP   A 1 52  ? 7.67280   -17.51344 9.27284   1.000 41.84027 ? 52  TRP   A CE2 1 
ATOM   378  C  CE3 . TRP   A 1 52  ? 9.02803   -16.94331 11.19229  1.000 40.93822 ? 52  TRP   A CE3 1 
ATOM   379  C  CZ2 . TRP   A 1 52  ? 8.02314   -18.86063 9.36599   1.000 42.96202 ? 52  TRP   A CZ2 1 
ATOM   380  C  CZ3 . TRP   A 1 52  ? 9.37671   -18.28309 11.28212  1.000 41.53553 ? 52  TRP   A CZ3 1 
ATOM   381  C  CH2 . TRP   A 1 52  ? 8.87415   -19.22406 10.37463  1.000 42.40380 ? 52  TRP   A CH2 1 
ATOM   382  N  N   . VAL   A 1 53  ? 8.69653   -12.64994 13.25508  1.000 35.23212 ? 53  VAL   A N   1 
ATOM   383  C  CA  . VAL   A 1 53  ? 9.45392   -11.53687 13.80981  1.000 35.82977 ? 53  VAL   A CA  1 
ATOM   384  C  C   . VAL   A 1 53  ? 10.91001  -11.72358 13.40937  1.000 36.51848 ? 53  VAL   A C   1 
ATOM   385  O  O   . VAL   A 1 53  ? 11.43140  -12.84313 13.45114  1.000 35.90864 ? 53  VAL   A O   1 
ATOM   386  C  CB  . VAL   A 1 53  ? 9.29734   -11.45077 15.34465  1.000 37.07542 ? 53  VAL   A CB  1 
ATOM   387  C  CG1 . VAL   A 1 53  ? 10.56276  -10.92306 15.99655  1.000 37.16044 ? 53  VAL   A CG1 1 
ATOM   388  C  CG2 . VAL   A 1 53  ? 8.11689   -10.56339 15.70766  1.000 35.38818 ? 53  VAL   A CG2 1 
ATOM   389  N  N   . VAL   A 1 54  ? 11.55622  -10.63583 12.99351  1.000 33.95036 ? 54  VAL   A N   1 
ATOM   390  C  CA  . VAL   A 1 54  ? 12.96311  -10.65298 12.60848  1.000 34.46162 ? 54  VAL   A CA  1 
ATOM   391  C  C   . VAL   A 1 54  ? 13.79259  -10.20431 13.80309  1.000 36.74954 ? 54  VAL   A C   1 
ATOM   392  O  O   . VAL   A 1 54  ? 13.55508  -9.12646  14.36488  1.000 33.23361 ? 54  VAL   A O   1 
ATOM   393  C  CB  . VAL   A 1 54  ? 13.21825  -9.75898  11.38338  1.000 34.28117 ? 54  VAL   A CB  1 
ATOM   394  C  CG1 . VAL   A 1 54  ? 14.61335  -10.00366 10.82980  1.000 34.05601 ? 54  VAL   A CG1 1 
ATOM   395  C  CG2 . VAL   A 1 54  ? 12.16895  -10.01528 10.31791  1.000 31.87692 ? 54  VAL   A CG2 1 
ATOM   396  N  N   . THR   A 1 55  ? 14.76970  -11.02741 14.19054  1.000 34.88643 ? 55  THR   A N   1 
ATOM   397  C  CA  . THR   A 1 55  ? 15.48839  -10.84123 15.44556  1.000 35.34038 ? 55  THR   A CA  1 
ATOM   398  C  C   . THR   A 1 55  ? 16.98139  -10.59390 15.26375  1.000 35.67761 ? 55  THR   A C   1 
ATOM   399  O  O   . THR   A 1 55  ? 17.70792  -10.53491 16.26276  1.000 37.09578 ? 55  THR   A O   1 
ATOM   400  C  CB  . THR   A 1 55  ? 15.28672  -12.05726 16.35593  1.000 36.88898 ? 55  THR   A CB  1 
ATOM   401  O  OG1 . THR   A 1 55  ? 15.88458  -13.20982 15.75009  1.000 37.51967 ? 55  THR   A OG1 1 
ATOM   402  C  CG2 . THR   A 1 55  ? 13.80804  -12.32347 16.57874  1.000 36.74125 ? 55  THR   A CG2 1 
ATOM   403  N  N   . LYS   A 1 56  ? 17.46500  -10.45184 14.03078  1.000 35.85714 ? 56  LYS   A N   1 
ATOM   404  C  CA  . LYS   A 1 56  ? 18.88759  -10.27357 13.77706  1.000 35.90791 ? 56  LYS   A CA  1 
ATOM   405  C  C   . LYS   A 1 56  ? 19.10569  -9.05071  12.89757  1.000 35.51427 ? 56  LYS   A C   1 
ATOM   406  O  O   . LYS   A 1 56  ? 18.26849  -8.71574  12.05544  1.000 35.79348 ? 56  LYS   A O   1 
ATOM   407  C  CB  . LYS   A 1 56  ? 19.50040  -11.52369 13.12174  1.000 36.88191 ? 56  LYS   A CB  1 
ATOM   408  C  CG  . LYS   A 1 56  ? 19.31333  -12.79723 13.93863  1.000 38.06967 ? 56  LYS   A CG  1 
ATOM   409  C  CD  . LYS   A 1 56  ? 19.97070  -12.69200 15.30931  1.000 38.30364 ? 56  LYS   A CD  1 
ATOM   410  C  CE  . LYS   A 1 56  ? 19.66719  -13.91158 16.17274  1.000 40.11570 ? 56  LYS   A CE  1 
ATOM   411  N  NZ  . LYS   A 1 56  ? 18.21754  -14.02193 16.50268  1.000 39.20591 ? 56  LYS   A NZ  1 
ATOM   412  N  N   . HIS   A 1 57  ? 20.25850  -8.40284  13.08883  1.000 35.54709 ? 57  HIS   A N   1 
ATOM   413  C  CA  . HIS   A 1 57  ? 20.48445  -7.07202  12.52683  1.000 34.76298 ? 57  HIS   A CA  1 
ATOM   414  C  C   . HIS   A 1 57  ? 20.58245  -7.10671  11.00488  1.000 35.69408 ? 57  HIS   A C   1 
ATOM   415  O  O   . HIS   A 1 57  ? 19.80269  -6.44764  10.30714  1.000 33.17712 ? 57  HIS   A O   1 
ATOM   416  C  CB  . HIS   A 1 57  ? 21.74762  -6.45897  13.13591  1.000 35.50030 ? 57  HIS   A CB  1 
ATOM   417  C  CG  . HIS   A 1 57  ? 22.07568  -5.09660  12.60937  1.000 35.08682 ? 57  HIS   A CG  1 
ATOM   418  N  ND1 . HIS   A 1 57  ? 22.83562  -4.89964  11.47602  1.000 37.28111 ? 57  HIS   A ND1 1 
ATOM   419  C  CD2 . HIS   A 1 57  ? 21.75475  -3.86209  13.06585  1.000 34.75326 ? 57  HIS   A CD2 1 
ATOM   420  C  CE1 . HIS   A 1 57  ? 22.96405  -3.60336  11.25364  1.000 34.58210 ? 57  HIS   A CE1 1 
ATOM   421  N  NE2 . HIS   A 1 57  ? 22.31697  -2.95156  12.20340  1.000 34.66513 ? 57  HIS   A NE2 1 
ATOM   422  N  N   . GLU   A 1 58  ? 21.54835  -7.85926  10.46746  1.000 36.38614 ? 58  GLU   A N   1 
ATOM   423  C  CA  . GLU   A 1 58  ? 21.76376  -7.84613  9.02224   1.000 37.92025 ? 58  GLU   A CA  1 
ATOM   424  C  C   . GLU   A 1 58  ? 20.57278  -8.42353  8.26631   1.000 35.48695 ? 58  GLU   A C   1 
ATOM   425  O  O   . GLU   A 1 58  ? 20.26831  -7.97224  7.15638   1.000 34.80984 ? 58  GLU   A O   1 
ATOM   426  C  CB  . GLU   A 1 58  ? 23.04521  -8.60470  8.66823   1.000 39.63275 ? 58  GLU   A CB  1 
ATOM   427  C  CG  . GLU   A 1 58  ? 23.39913  -8.58209  7.18232   1.000 41.84735 ? 58  GLU   A CG  1 
ATOM   428  C  CD  . GLU   A 1 58  ? 23.56710  -7.17427  6.62574   1.000 47.69338 ? 58  GLU   A CD  1 
ATOM   429  O  OE1 . GLU   A 1 58  ? 23.94679  -6.25748  7.38810   1.000 47.76179 ? 58  GLU   A OE1 1 
ATOM   430  O  OE2 . GLU   A 1 58  ? 23.31465  -6.98246  5.41722   1.000 47.82049 ? 58  GLU   A OE2 1 
ATOM   431  N  N   . ALA   A 1 59  ? 19.88613  -9.41005  8.84549   1.000 34.69999 ? 59  ALA   A N   1 
ATOM   432  C  CA  . ALA   A 1 59  ? 18.66887  -9.91580  8.22197   1.000 35.12854 ? 59  ALA   A CA  1 
ATOM   433  C  C   . ALA   A 1 59  ? 17.54977  -8.88612  8.26749   1.000 33.18949 ? 59  ALA   A C   1 
ATOM   434  O  O   . ALA   A 1 59  ? 16.69201  -8.86298  7.37676   1.000 30.78041 ? 59  ALA   A O   1 
ATOM   435  C  CB  . ALA   A 1 59  ? 18.22223  -11.20537 8.90189   1.000 34.65046 ? 59  ALA   A CB  1 
ATOM   436  N  N   . ALA   A 1 60  ? 17.53598  -8.03622  9.29563   1.000 33.66430 ? 60  ALA   A N   1 
ATOM   437  C  CA  . ALA   A 1 60  ? 16.55363  -6.95949  9.35142   1.000 32.92780 ? 60  ALA   A CA  1 
ATOM   438  C  C   . ALA   A 1 60  ? 16.78931  -5.94980  8.23462   1.000 32.03641 ? 60  ALA   A C   1 
ATOM   439  O  O   . ALA   A 1 60  ? 15.84661  -5.53255  7.55112   1.000 32.43028 ? 60  ALA   A O   1 
ATOM   440  C  CB  . ALA   A 1 60  ? 16.59948  -6.28233  10.71959  1.000 32.34316 ? 60  ALA   A CB  1 
ATOM   441  N  N   . ARG   A 1 61  ? 18.04986  -5.54812  8.03384   1.000 32.53181 ? 61  ARG   A N   1 
ATOM   442  C  CA  . ARG   A 1 61  ? 18.39041  -4.67537  6.91216   1.000 33.04758 ? 61  ARG   A CA  1 
ATOM   443  C  C   . ARG   A 1 61  ? 17.97574  -5.29479  5.58440   1.000 33.44275 ? 61  ARG   A C   1 
ATOM   444  O  O   . ARG   A 1 61  ? 17.43138  -4.60703  4.71189   1.000 31.14994 ? 61  ARG   A O   1 
ATOM   445  C  CB  . ARG   A 1 61  ? 19.89383  -4.38501  6.90230   1.000 33.28195 ? 61  ARG   A CB  1 
ATOM   446  C  CG  . ARG   A 1 61  ? 20.31734  -3.13922  7.65669   1.000 33.18310 ? 61  ARG   A CG  1 
ATOM   447  C  CD  . ARG   A 1 61  ? 21.83358  -3.05705  7.78174   1.000 34.26498 ? 61  ARG   A CD  1 
ATOM   448  N  NE  . ARG   A 1 61  ? 22.48911  -2.56663  6.56978   1.000 34.71618 ? 61  ARG   A NE  1 
ATOM   449  C  CZ  . ARG   A 1 61  ? 23.03173  -1.35695  6.44949   1.000 34.47097 ? 61  ARG   A CZ  1 
ATOM   450  N  NH1 . ARG   A 1 61  ? 22.99895  -0.50819  7.47019   1.000 31.56193 ? 61  ARG   A NH1 1 
ATOM   451  N  NH2 . ARG   A 1 61  ? 23.61490  -0.99688  5.31253   1.000 31.32258 ? 61  ARG   A NH2 1 
ATOM   452  N  N   . LYS   A 1 62  ? 18.23478  -6.59339  5.41476   1.000 31.16383 ? 62  LYS   A N   1 
ATOM   453  C  CA  . LYS   A 1 62  ? 17.93654  -7.26554  4.15383   1.000 31.34714 ? 62  LYS   A CA  1 
ATOM   454  C  C   . LYS   A 1 62  ? 16.43919  -7.26579  3.86921   1.000 30.97458 ? 62  LYS   A C   1 
ATOM   455  O  O   . LYS   A 1 62  ? 16.00770  -6.98040  2.74704   1.000 33.08962 ? 62  LYS   A O   1 
ATOM   456  C  CB  . LYS   A 1 62  ? 18.48284  -8.69513  4.19657   1.000 34.56748 ? 62  LYS   A CB  1 
ATOM   457  C  CG  . LYS   A 1 62  ? 18.34772  -9.47904  2.89707   1.000 36.29388 ? 62  LYS   A CG  1 
ATOM   458  C  CD  . LYS   A 1 62  ? 19.16644  -10.76474 2.97206   1.000 39.46790 ? 62  LYS   A CD  1 
ATOM   459  C  CE  . LYS   A 1 62  ? 18.98452  -11.63146 1.73770   1.000 44.18193 ? 62  LYS   A CE  1 
ATOM   460  N  NZ  . LYS   A 1 62  ? 19.33138  -10.90395 0.48577   1.000 46.36218 ? 62  LYS   A NZ  1 
ATOM   461  N  N   . LEU   A 1 63  ? 15.62706  -7.58186  4.88005   1.000 30.19985 ? 63  LEU   A N   1 
ATOM   462  C  CA  . LEU   A 1 63  ? 14.18487  -7.64933  4.67560   1.000 30.31788 ? 63  LEU   A CA  1 
ATOM   463  C  C   . LEU   A 1 63  ? 13.55755  -6.26202  4.57419   1.000 31.79142 ? 63  LEU   A C   1 
ATOM   464  O  O   . LEU   A 1 63  ? 12.57044  -6.08263  3.84803   1.000 27.59684 ? 63  LEU   A O   1 
ATOM   465  C  CB  . LEU   A 1 63  ? 13.54446  -8.46451  5.79974   1.000 29.03798 ? 63  LEU   A CB  1 
ATOM   466  C  CG  . LEU   A 1 63  ? 13.83834  -9.96799  5.68500   1.000 32.04316 ? 63  LEU   A CG  1 
ATOM   467  C  CD1 . LEU   A 1 63  ? 13.44739  -10.71012 6.95517   1.000 31.23033 ? 63  LEU   A CD1 1 
ATOM   468  C  CD2 . LEU   A 1 63  ? 13.11937  -10.54787 4.47821   1.000 30.29786 ? 63  LEU   A CD2 1 
ATOM   469  N  N   . LEU   A 1 64  ? 14.10555  -5.27355  5.29065   1.000 31.64124 ? 64  LEU   A N   1 
ATOM   470  C  CA  . LEU   A 1 64  ? 13.61191  -3.90491  5.15510   1.000 29.43475 ? 64  LEU   A CA  1 
ATOM   471  C  C   . LEU   A 1 64  ? 13.82513  -3.36896  3.74409   1.000 28.81635 ? 64  LEU   A C   1 
ATOM   472  O  O   . LEU   A 1 64  ? 13.04130  -2.53924  3.27083   1.000 32.82337 ? 64  LEU   A O   1 
ATOM   473  C  CB  . LEU   A 1 64  ? 14.28441  -2.99137  6.18324   1.000 29.94599 ? 64  LEU   A CB  1 
ATOM   474  C  CG  . LEU   A 1 64  ? 13.77428  -3.09452  7.62311   1.000 29.79455 ? 64  LEU   A CG  1 
ATOM   475  C  CD1 . LEU   A 1 64  ? 14.65369  -2.29288  8.56730   1.000 30.09957 ? 64  LEU   A CD1 1 
ATOM   476  C  CD2 . LEU   A 1 64  ? 12.32666  -2.63693  7.72005   1.000 30.19180 ? 64  LEU   A CD2 1 
ATOM   477  N  N   . GLY   A 1 65  ? 14.86434  -3.83588  3.05449   1.000 29.95762 ? 65  GLY   A N   1 
ATOM   478  C  CA  . GLY   A 1 65  ? 15.11464  -3.44486  1.68237   1.000 32.49552 ? 65  GLY   A CA  1 
ATOM   479  C  C   . GLY   A 1 65  ? 14.47083  -4.31368  0.62565   1.000 31.20699 ? 65  GLY   A C   1 
ATOM   480  O  O   . GLY   A 1 65  ? 14.53879  -3.97953  -0.56020  1.000 31.95107 ? 65  GLY   A O   1 
ATOM   481  N  N   . ASP   A 1 66  ? 13.84506  -5.42128  1.02481   1.000 33.62781 ? 66  ASP   A N   1 
ATOM   482  C  CA  . ASP   A 1 66  ? 13.21148  -6.35935  0.10557   1.000 33.09093 ? 66  ASP   A CA  1 
ATOM   483  C  C   . ASP   A 1 66  ? 11.84457  -5.83118  -0.31432  1.000 32.12256 ? 66  ASP   A C   1 
ATOM   484  O  O   . ASP   A 1 66  ? 10.94314  -5.71041  0.52525   1.000 32.12041 ? 66  ASP   A O   1 
ATOM   485  C  CB  . ASP   A 1 66  ? 13.08171  -7.73655  0.76431   1.000 32.22658 ? 66  ASP   A CB  1 
ATOM   486  C  CG  . ASP   A 1 66  ? 12.77376  -8.84403  -0.23027  1.000 34.92176 ? 66  ASP   A CG  1 
ATOM   487  O  OD1 . ASP   A 1 66  ? 12.17635  -8.56337  -1.29051  1.000 32.63654 ? 66  ASP   A OD1 1 
ATOM   488  O  OD2 . ASP   A 1 66  ? 13.12704  -10.00819 0.05812   1.000 36.09757 ? 66  ASP   A OD2 1 
ATOM   489  N  N   . PRO   A 1 67  ? 11.64629  -5.51731  -1.59792  1.000 33.99328 ? 67  PRO   A N   1 
ATOM   490  C  CA  . PRO   A 1 67  ? 10.33791  -4.99884  -2.03205  1.000 33.62739 ? 67  PRO   A CA  1 
ATOM   491  C  C   . PRO   A 1 67  ? 9.20240   -5.98974  -1.85428  1.000 34.56613 ? 67  PRO   A C   1 
ATOM   492  O  O   . PRO   A 1 67  ? 8.03531   -5.57682  -1.85643  1.000 34.52044 ? 67  PRO   A O   1 
ATOM   493  C  CB  . PRO   A 1 67  ? 10.56102  -4.66921  -3.51648  1.000 35.22921 ? 67  PRO   A CB  1 
ATOM   494  C  CG  . PRO   A 1 67  ? 12.04893  -4.59593  -3.68593  1.000 35.24650 ? 67  PRO   A CG  1 
ATOM   495  C  CD  . PRO   A 1 67  ? 12.61209  -5.57607  -2.70692  1.000 34.25719 ? 67  PRO   A CD  1 
ATOM   496  N  N   . ARG   A 1 68  ? 9.50258   -7.28212  -1.69965  1.000 33.01564 ? 68  ARG   A N   1 
ATOM   497  C  CA  . ARG   A 1 68  ? 8.45220   -8.27522  -1.50994  1.000 35.05172 ? 68  ARG   A CA  1 
ATOM   498  C  C   . ARG   A 1 68  ? 7.79791   -8.17644  -0.13735  1.000 34.02770 ? 68  ARG   A C   1 
ATOM   499  O  O   . ARG   A 1 68  ? 6.70603   -8.72253  0.05206   1.000 33.86531 ? 68  ARG   A O   1 
ATOM   500  C  CB  . ARG   A 1 68  ? 9.01202   -9.68214  -1.73090  1.000 34.88227 ? 68  ARG   A CB  1 
ATOM   501  C  CG  . ARG   A 1 68  ? 9.33539   -9.99256  -3.18560  1.000 35.99453 ? 68  ARG   A CG  1 
ATOM   502  C  CD  . ARG   A 1 68  ? 10.11910  -11.29227 -3.31665  1.000 37.23503 ? 68  ARG   A CD  1 
ATOM   503  N  NE  . ARG   A 1 68  ? 11.35365  -11.24531 -2.53971  1.000 37.35538 ? 68  ARG   A NE  1 
ATOM   504  C  CZ  . ARG   A 1 68  ? 12.28077  -12.19706 -2.54074  1.000 40.33057 ? 68  ARG   A CZ  1 
ATOM   505  N  NH1 . ARG   A 1 68  ? 12.12346  -13.28494 -3.28418  1.000 39.67831 ? 68  ARG   A NH1 1 
ATOM   506  N  NH2 . ARG   A 1 68  ? 13.36990  -12.05859 -1.79803  1.000 38.70580 ? 68  ARG   A NH2 1 
ATOM   507  N  N   . LEU   A 1 69  ? 8.43213   -7.50209  0.82066   1.000 32.42031 ? 69  LEU   A N   1 
ATOM   508  C  CA  . LEU   A 1 69  ? 7.79459   -7.18396  2.09556   1.000 32.27124 ? 69  LEU   A CA  1 
ATOM   509  C  C   . LEU   A 1 69  ? 7.14804   -5.80789  1.97243   1.000 32.39715 ? 69  LEU   A C   1 
ATOM   510  O  O   . LEU   A 1 69  ? 7.84269   -4.78631  1.92487   1.000 31.88506 ? 69  LEU   A O   1 
ATOM   511  C  CB  . LEU   A 1 69  ? 8.79878   -7.23407  3.24552   1.000 32.03092 ? 69  LEU   A CB  1 
ATOM   512  C  CG  . LEU   A 1 69  ? 9.10758   -8.63123  3.79680   1.000 32.85684 ? 69  LEU   A CG  1 
ATOM   513  C  CD1 . LEU   A 1 69  ? 9.96865   -8.55358  5.04929   1.000 32.81921 ? 69  LEU   A CD1 1 
ATOM   514  C  CD2 . LEU   A 1 69  ? 7.82188   -9.39594  4.07904   1.000 32.97170 ? 69  LEU   A CD2 1 
ATOM   515  N  N   . SER   A 1 70  ? 5.81976   -5.78511  1.92283   1.000 31.02974 ? 70  SER   A N   1 
ATOM   516  C  CA  . SER   A 1 70  ? 5.06252   -4.57702  1.63519   1.000 32.35958 ? 70  SER   A CA  1 
ATOM   517  C  C   . SER   A 1 70  ? 4.66118   -3.85326  2.91610   1.000 33.28552 ? 70  SER   A C   1 
ATOM   518  O  O   . SER   A 1 70  ? 4.38409   -4.47436  3.94594   1.000 30.78668 ? 70  SER   A O   1 
ATOM   519  C  CB  . SER   A 1 70  ? 3.81167   -4.92046  0.82542   1.000 33.21066 ? 70  SER   A CB  1 
ATOM   520  O  OG  . SER   A 1 70  ? 2.90845   -3.82940  0.78902   1.000 31.94772 ? 70  SER   A OG  1 
ATOM   521  N  N   . SER   A 1 71  ? 4.61888   -2.52285  2.83427   1.000 31.45981 ? 71  SER   A N   1 
ATOM   522  C  CA  . SER   A 1 71  ? 4.20138   -1.67784  3.94440   1.000 31.46465 ? 71  SER   A CA  1 
ATOM   523  C  C   . SER   A 1 71  ? 2.72326   -1.31303  3.88618   1.000 34.08986 ? 71  SER   A C   1 
ATOM   524  O  O   . SER   A 1 71  ? 2.28461   -0.44162  4.64407   1.000 33.90739 ? 71  SER   A O   1 
ATOM   525  C  CB  . SER   A 1 71  ? 5.04535   -0.39990  3.98060   1.000 31.77004 ? 71  SER   A CB  1 
ATOM   526  O  OG  . SER   A 1 71  ? 6.40085   -0.68168  4.28043   1.000 32.32496 ? 71  SER   A OG  1 
ATOM   527  N  N   . ASN   A 1 72  ? 1.95230   -1.95561  3.01055   1.000 33.03716 ? 72  ASN   A N   1 
ATOM   528  C  CA  . ASN   A 1 72  ? 0.53786   -1.63491  2.81828   1.000 34.21485 ? 72  ASN   A CA  1 
ATOM   529  C  C   . ASN   A 1 72  ? -0.24306  -2.05188  4.05851   1.000 37.38593 ? 72  ASN   A C   1 
ATOM   530  O  O   . ASN   A 1 72  ? -0.52884  -3.23388  4.26570   1.000 35.28548 ? 72  ASN   A O   1 
ATOM   531  C  CB  . ASN   A 1 72  ? 0.00771   -2.32815  1.56727   1.000 35.29701 ? 72  ASN   A CB  1 
ATOM   532  C  CG  . ASN   A 1 72  ? -1.48360  -2.11216  1.35803   1.000 37.75946 ? 72  ASN   A CG  1 
ATOM   533  O  OD1 . ASN   A 1 72  ? -2.08631  -1.21372  1.94368   1.000 37.57676 ? 72  ASN   A OD1 1 
ATOM   534  N  ND2 . ASN   A 1 72  ? -2.08440  -2.94190  0.51394   1.000 39.04994 ? 72  ASN   A ND2 1 
ATOM   535  N  N   . ARG   A 1 73  ? -0.60492  -1.07271  4.88635   1.000 36.82383 ? 73  ARG   A N   1 
ATOM   536  C  CA  . ARG   A 1 73  ? -1.30216  -1.35413  6.13236   1.000 37.59134 ? 73  ARG   A CA  1 
ATOM   537  C  C   . ARG   A 1 73  ? -2.78359  -1.65231  5.93215   1.000 38.29137 ? 73  ARG   A C   1 
ATOM   538  O  O   . ARG   A 1 73  ? -3.44118  -2.09373  6.88046   1.000 41.71734 ? 73  ARG   A O   1 
ATOM   539  C  CB  . ARG   A 1 73  ? -1.11815  -0.18095  7.10338   1.000 38.07530 ? 73  ARG   A CB  1 
ATOM   540  C  CG  . ARG   A 1 73  ? 0.34714   0.15991   7.36310   1.000 37.46619 ? 73  ARG   A CG  1 
ATOM   541  C  CD  . ARG   A 1 73  ? 0.53875   1.11772   8.52594   1.000 38.73057 ? 73  ARG   A CD  1 
ATOM   542  N  NE  . ARG   A 1 73  ? 0.17115   2.49396   8.22973   1.000 38.86310 ? 73  ARG   A NE  1 
ATOM   543  C  CZ  . ARG   A 1 73  ? 0.44601   3.51916   9.02955   1.000 39.11713 ? 73  ARG   A CZ  1 
ATOM   544  N  NH1 . ARG   A 1 73  ? 0.06658   4.74328   8.68644   1.000 38.67990 ? 73  ARG   A NH1 1 
ATOM   545  N  NH2 . ARG   A 1 73  ? 1.09704   3.32299   10.17035  1.000 39.16941 ? 73  ARG   A NH2 1 
ATOM   546  N  N   . THR   A 1 74  ? -3.32037  -1.43256  4.73050   1.000 39.32458 ? 74  THR   A N   1 
ATOM   547  C  CA  . THR   A 1 74  ? -4.69749  -1.80219  4.42572   1.000 40.74903 ? 74  THR   A CA  1 
ATOM   548  C  C   . THR   A 1 74  ? -4.84067  -3.26500  4.02612   1.000 41.46107 ? 74  THR   A C   1 
ATOM   549  O  O   . THR   A 1 74  ? -5.97162  -3.73971  3.88224   1.000 43.23646 ? 74  THR   A O   1 
ATOM   550  C  CB  . THR   A 1 74  ? -5.26011  -0.91799  3.30613   1.000 39.89877 ? 74  THR   A CB  1 
ATOM   551  O  OG1 . THR   A 1 74  ? -4.56063  -1.18319  2.08347   1.000 40.53949 ? 74  THR   A OG1 1 
ATOM   552  C  CG2 . THR   A 1 74  ? -5.10748  0.55158   3.66031   1.000 41.44734 ? 74  THR   A CG2 1 
ATOM   553  N  N   . ASP   A 1 75  ? -3.73261  -3.97993  3.83895   1.000 40.14626 ? 75  ASP   A N   1 
ATOM   554  C  CA  . ASP   A 1 75  ? -3.78953  -5.39437  3.49324   1.000 41.73478 ? 75  ASP   A CA  1 
ATOM   555  C  C   . ASP   A 1 75  ? -4.35609  -6.19833  4.65881   1.000 42.11289 ? 75  ASP   A C   1 
ATOM   556  O  O   . ASP   A 1 75  ? -3.94533  -6.01821  5.80915   1.000 42.32238 ? 75  ASP   A O   1 
ATOM   557  C  CB  . ASP   A 1 75  ? -2.39479  -5.89663  3.11803   1.000 39.64793 ? 75  ASP   A CB  1 
ATOM   558  C  CG  . ASP   A 1 75  ? -2.40504  -7.31560  2.57387   1.000 41.23492 ? 75  ASP   A CG  1 
ATOM   559  O  OD1 . ASP   A 1 75  ? -2.61069  -8.26235  3.36121   1.000 39.46211 ? 75  ASP   A OD1 1 
ATOM   560  O  OD2 . ASP   A 1 75  ? -2.20770  -7.48122  1.35189   1.000 40.25208 ? 75  ASP   A OD2 1 
ATOM   561  N  N   . ASP   A 1 76  ? -5.30206  -7.09262  4.35458   1.000 43.43976 ? 76  ASP   A N   1 
ATOM   562  C  CA  . ASP   A 1 76  ? -5.97373  -7.86238  5.40008   1.000 45.63984 ? 76  ASP   A CA  1 
ATOM   563  C  C   . ASP   A 1 76  ? -5.00074  -8.71311  6.20596   1.000 43.61064 ? 76  ASP   A C   1 
ATOM   564  O  O   . ASP   A 1 76  ? -5.27305  -9.03053  7.36994   1.000 43.84228 ? 76  ASP   A O   1 
ATOM   565  C  CB  . ASP   A 1 76  ? -7.05270  -8.75737  4.78826   1.000 49.95164 ? 76  ASP   A CB  1 
ATOM   566  C  CG  . ASP   A 1 76  ? -8.27438  -7.98232  4.34369   1.000 55.40510 ? 76  ASP   A CG  1 
ATOM   567  O  OD1 . ASP   A 1 76  ? -8.36004  -6.77531  4.65225   1.000 53.15482 ? 76  ASP   A OD1 1 
ATOM   568  O  OD2 . ASP   A 1 76  ? -9.14143  -8.58095  3.67360   1.000 62.72376 ? 76  ASP   A OD2 1 
ATOM   569  N  N   . ASN   A 1 77  ? -3.87473  -9.09909  5.61395   1.000 41.47196 ? 77  ASN   A N   1 
ATOM   570  C  CA  . ASN   A 1 77  ? -2.89497  -9.92446  6.30354   1.000 41.59731 ? 77  ASN   A CA  1 
ATOM   571  C  C   . ASN   A 1 77  ? -1.78252  -9.11014  6.95260   1.000 40.78400 ? 77  ASN   A C   1 
ATOM   572  O  O   . ASN   A 1 77  ? -0.78144  -9.68898  7.38938   1.000 39.60924 ? 77  ASN   A O   1 
ATOM   573  C  CB  . ASN   A 1 77  ? -2.29730  -10.94623 5.33701   1.000 40.77571 ? 77  ASN   A CB  1 
ATOM   574  C  CG  . ASN   A 1 77  ? -3.27811  -12.04414 4.96561   1.000 41.66755 ? 77  ASN   A CG  1 
ATOM   575  O  OD1 . ASN   A 1 77  ? -3.98530  -12.57856 5.81971   1.000 41.25194 ? 77  ASN   A OD1 1 
ATOM   576  N  ND2 . ASN   A 1 77  ? -3.32507  -12.38433 3.68274   1.000 41.46221 ? 77  ASN   A ND2 1 
ATOM   577  N  N   . PHE   A 1 78  ? -1.93340  -7.79360  7.03115   1.000 39.13601 ? 78  PHE   A N   1 
ATOM   578  C  CA  . PHE   A 1 78  ? -0.91844  -6.98173  7.67794   1.000 38.72602 ? 78  PHE   A CA  1 
ATOM   579  C  C   . PHE   A 1 78  ? -0.87715  -7.29393  9.17226   1.000 38.64853 ? 78  PHE   A C   1 
ATOM   580  O  O   . PHE   A 1 78  ? -1.92649  -7.41939  9.81235   1.000 39.13026 ? 78  PHE   A O   1 
ATOM   581  C  CB  . PHE   A 1 78  ? -1.18874  -5.49280  7.46224   1.000 38.38497 ? 78  PHE   A CB  1 
ATOM   582  C  CG  . PHE   A 1 78  ? -0.02683  -4.61292  7.82451   1.000 37.78527 ? 78  PHE   A CG  1 
ATOM   583  C  CD1 . PHE   A 1 78  ? 0.12476   -4.13508  9.11714   1.000 36.51203 ? 78  PHE   A CD1 1 
ATOM   584  C  CD2 . PHE   A 1 78  ? 0.92632   -4.28046  6.87691   1.000 35.39846 ? 78  PHE   A CD2 1 
ATOM   585  C  CE1 . PHE   A 1 78  ? 1.19941   -3.33558  9.45138   1.000 37.18522 ? 78  PHE   A CE1 1 
ATOM   586  C  CE2 . PHE   A 1 78  ? 2.00175   -3.47764  7.20803   1.000 35.56436 ? 78  PHE   A CE2 1 
ATOM   587  C  CZ  . PHE   A 1 78  ? 2.13657   -3.00500  8.49470   1.000 35.86547 ? 78  PHE   A CZ  1 
ATOM   588  N  N   . PRO   A 1 79  ? 0.31493   -7.42560  9.75315   1.000 37.75717 ? 79  PRO   A N   1 
ATOM   589  C  CA  . PRO   A 1 79  ? 0.41417   -7.78541  11.17358  1.000 39.50006 ? 79  PRO   A CA  1 
ATOM   590  C  C   . PRO   A 1 79  ? 0.02610   -6.65267  12.11081  1.000 39.87769 ? 79  PRO   A C   1 
ATOM   591  O  O   . PRO   A 1 79  ? 0.89087   -5.95392  12.64906  1.000 39.86482 ? 79  PRO   A O   1 
ATOM   592  C  CB  . PRO   A 1 79  ? 1.89292   -8.16103  11.33152  1.000 38.55422 ? 79  PRO   A CB  1 
ATOM   593  C  CG  . PRO   A 1 79  ? 2.58998   -7.37667  10.27238  1.000 37.15055 ? 79  PRO   A CG  1 
ATOM   594  C  CD  . PRO   A 1 79  ? 1.63661   -7.32392  9.10975   1.000 36.21685 ? 79  PRO   A CD  1 
ATOM   595  N  N   . ALA   A 1 80  ? -1.27539  -6.46937  12.31406  1.000 40.69788 ? 80  ALA   A N   1 
ATOM   596  C  CA  . ALA   A 1 80  ? -1.75290  -5.51383  13.30292  1.000 41.22832 ? 80  ALA   A CA  1 
ATOM   597  C  C   . ALA   A 1 80  ? -1.50060  -6.05451  14.70382  1.000 42.07325 ? 80  ALA   A C   1 
ATOM   598  O  O   . ALA   A 1 80  ? -1.86858  -7.19041  15.01728  1.000 40.57412 ? 80  ALA   A O   1 
ATOM   599  C  CB  . ALA   A 1 80  ? -3.24067  -5.23546  13.09955  1.000 43.03422 ? 80  ALA   A CB  1 
ATOM   600  N  N   . THR   A 1 81  ? -0.86911  -5.24228  15.54828  1.000 41.73580 ? 81  THR   A N   1 
ATOM   601  C  CA  . THR   A 1 81  ? -0.47407  -5.67541  16.88033  1.000 41.85310 ? 81  THR   A CA  1 
ATOM   602  C  C   . THR   A 1 81  ? -1.39541  -5.16713  17.98269  1.000 42.06718 ? 81  THR   A C   1 
ATOM   603  O  O   . THR   A 1 81  ? -1.15740  -5.47532  19.15412  1.000 40.41996 ? 81  THR   A O   1 
ATOM   604  C  CB  . THR   A 1 81  ? 0.96570   -5.23971  17.17088  1.000 41.22339 ? 81  THR   A CB  1 
ATOM   605  O  OG1 . THR   A 1 81  ? 1.10564   -3.83585  16.91587  1.000 43.94420 ? 81  THR   A OG1 1 
ATOM   606  C  CG2 . THR   A 1 81  ? 1.93854   -6.00951  16.29258  1.000 39.08607 ? 81  THR   A CG2 1 
ATOM   607  N  N   . SER   A 1 82  ? -2.43474  -4.40814  17.64600  1.000 43.30205 ? 82  SER   A N   1 
ATOM   608  C  CA  . SER   A 1 82  ? -3.37766  -3.90876  18.63741  1.000 44.70246 ? 82  SER   A CA  1 
ATOM   609  C  C   . SER   A 1 82  ? -4.65595  -3.49885  17.92180  1.000 46.73932 ? 82  SER   A C   1 
ATOM   610  O  O   . SER   A 1 82  ? -4.63715  -3.23727  16.71261  1.000 46.17746 ? 82  SER   A O   1 
ATOM   611  C  CB  . SER   A 1 82  ? -2.79373  -2.71872  19.41824  1.000 44.83469 ? 82  SER   A CB  1 
ATOM   612  O  OG  . SER   A 1 82  ? -2.79530  -1.54055  18.62880  1.000 45.92678 ? 82  SER   A OG  1 
ATOM   613  N  N   . PRO   A 1 83  ? -5.78450  -3.44587  18.63512  1.000 47.14392 ? 83  PRO   A N   1 
ATOM   614  C  CA  . PRO   A 1 83  ? -7.01278  -2.93029  18.01002  1.000 48.00576 ? 83  PRO   A CA  1 
ATOM   615  C  C   . PRO   A 1 83  ? -6.91012  -1.47137  17.60843  1.000 49.24896 ? 83  PRO   A C   1 
ATOM   616  O  O   . PRO   A 1 83  ? -7.55228  -1.05991  16.63421  1.000 48.77895 ? 83  PRO   A O   1 
ATOM   617  C  CB  . PRO   A 1 83  ? -8.07570  -3.13985  19.09850  1.000 48.83899 ? 83  PRO   A CB  1 
ATOM   618  C  CG  . PRO   A 1 83  ? -7.51685  -4.19942  19.98215  1.000 47.93283 ? 83  PRO   A CG  1 
ATOM   619  C  CD  . PRO   A 1 83  ? -6.03589  -3.97795  19.98464  1.000 47.52929 ? 83  PRO   A CD  1 
ATOM   620  N  N   . ALA   A 1 84  ? -6.11949  -0.67379  18.33126  1.000 48.59059 ? 84  ALA   A N   1 
ATOM   621  C  CA  . ALA   A 1 84  ? -5.94846  0.72994   17.97548  1.000 49.26814 ? 84  ALA   A CA  1 
ATOM   622  C  C   . ALA   A 1 84  ? -5.32908  0.90340   16.59574  1.000 49.37640 ? 84  ALA   A C   1 
ATOM   623  O  O   . ALA   A 1 84  ? -5.49129  1.96601   15.98465  1.000 49.17322 ? 84  ALA   A O   1 
ATOM   624  C  CB  . ALA   A 1 84  ? -5.09037  1.43654   19.02507  1.000 49.58092 ? 84  ALA   A CB  1 
ATOM   625  N  N   . PHE   A 1 85  ? -4.63097  -0.11810  16.09142  1.000 49.16708 ? 85  PHE   A N   1 
ATOM   626  C  CA  . PHE   A 1 85  ? -4.06029  -0.05725  14.75079  1.000 49.11312 ? 85  PHE   A CA  1 
ATOM   627  C  C   . PHE   A 1 85  ? -5.12549  0.15046   13.68080  1.000 49.93352 ? 85  PHE   A C   1 
ATOM   628  O  O   . PHE   A 1 85  ? -4.80650  0.62945   12.58750  1.000 49.50902 ? 85  PHE   A O   1 
ATOM   629  C  CB  . PHE   A 1 85  ? -3.26556  -1.33609  14.47060  1.000 48.18871 ? 85  PHE   A CB  1 
ATOM   630  C  CG  . PHE   A 1 85  ? -2.47736  -1.29597  13.19318  1.000 47.14820 ? 85  PHE   A CG  1 
ATOM   631  C  CD1 . PHE   A 1 85  ? -1.19463  -0.77490  13.17204  1.000 47.03575 ? 85  PHE   A CD1 1 
ATOM   632  C  CD2 . PHE   A 1 85  ? -3.01586  -1.78621  12.01546  1.000 47.44288 ? 85  PHE   A CD2 1 
ATOM   633  C  CE1 . PHE   A 1 85  ? -0.46816  -0.73692  11.99978  1.000 44.47919 ? 85  PHE   A CE1 1 
ATOM   634  C  CE2 . PHE   A 1 85  ? -2.29589  -1.74875  10.84084  1.000 44.95869 ? 85  PHE   A CE2 1 
ATOM   635  C  CZ  . PHE   A 1 85  ? -1.02049  -1.22376  10.83238  1.000 43.34537 ? 85  PHE   A CZ  1 
ATOM   636  N  N   . GLU   A 1 86  ? -6.38418  -0.18355  13.97645  1.000 50.72203 ? 86  GLU   A N   1 
ATOM   637  C  CA  . GLU   A 1 86  ? -7.46212  -0.00997  13.00916  1.000 52.25742 ? 86  GLU   A CA  1 
ATOM   638  C  C   . GLU   A 1 86  ? -7.69613  1.45446   12.65258  1.000 51.62906 ? 86  GLU   A C   1 
ATOM   639  O  O   . GLU   A 1 86  ? -8.28313  1.73934   11.60237  1.000 51.59647 ? 86  GLU   A O   1 
ATOM   640  C  CB  . GLU   A 1 86  ? -8.74918  -0.63249  13.56003  1.000 53.57312 ? 86  GLU   A CB  1 
ATOM   641  C  CG  . GLU   A 1 86  ? -9.88560  -0.74156  12.55551  1.000 56.78460 ? 86  GLU   A CG  1 
ATOM   642  C  CD  . GLU   A 1 86  ? -9.58987  -1.72416  11.43850  1.000 61.33644 ? 86  GLU   A CD  1 
ATOM   643  O  OE1 . GLU   A 1 86  ? -8.73304  -2.61477  11.63157  1.000 57.61776 ? 86  GLU   A OE1 1 
ATOM   644  O  OE2 . GLU   A 1 86  ? -10.21635 -1.60518  10.36421  1.000 66.44317 ? 86  GLU   A OE2 1 
ATOM   645  N  N   . ALA   A 1 87  ? -7.24523  2.38758   13.49556  1.000 50.11466 ? 87  ALA   A N   1 
ATOM   646  C  CA  . ALA   A 1 87  ? -7.48280  3.80344   13.23073  1.000 49.31710 ? 87  ALA   A CA  1 
ATOM   647  C  C   . ALA   A 1 87  ? -6.82097  4.24623   11.93152  1.000 48.32735 ? 87  ALA   A C   1 
ATOM   648  O  O   . ALA   A 1 87  ? -7.38770  5.04799   11.17984  1.000 47.82138 ? 87  ALA   A O   1 
ATOM   649  C  CB  . ALA   A 1 87  ? -6.98049  4.64898   14.40098  1.000 48.66435 ? 87  ALA   A CB  1 
ATOM   650  N  N   . VAL   A 1 88  ? -5.62180  3.73004   11.64317  1.000 49.00009 ? 88  VAL   A N   1 
ATOM   651  C  CA  . VAL   A 1 88  ? -4.90488  4.12763   10.43397  1.000 47.84819 ? 88  VAL   A CA  1 
ATOM   652  C  C   . VAL   A 1 88  ? -5.28050  3.28871   9.22274   1.000 48.08341 ? 88  VAL   A C   1 
ATOM   653  O  O   . VAL   A 1 88  ? -4.95064  3.67309   8.09036   1.000 46.30790 ? 88  VAL   A O   1 
ATOM   654  C  CB  . VAL   A 1 88  ? -3.37986  4.05495   10.65168  1.000 46.50341 ? 88  VAL   A CB  1 
ATOM   655  C  CG1 . VAL   A 1 88  ? -2.97703  4.86290   11.88153  1.000 45.97892 ? 88  VAL   A CG1 1 
ATOM   656  C  CG2 . VAL   A 1 88  ? -2.92898  2.61055   10.78238  1.000 46.76655 ? 88  VAL   A CG2 1 
ATOM   657  N  N   . ARG   A 1 89  ? -5.97502  2.16575   9.41760   1.000 49.47657 ? 89  ARG   A N   1 
ATOM   658  C  CA  . ARG   A 1 89  ? -6.24467  1.24966   8.31442   1.000 49.59673 ? 89  ARG   A CA  1 
ATOM   659  C  C   . ARG   A 1 89  ? -7.41269  1.70853   7.44561   1.000 50.88228 ? 89  ARG   A C   1 
ATOM   660  O  O   . ARG   A 1 89  ? -7.44212  1.40344   6.24770   1.000 50.29766 ? 89  ARG   A O   1 
ATOM   661  C  CB  . ARG   A 1 89  ? -6.51128  -0.15784  8.86099   1.000 51.16186 ? 89  ARG   A CB  1 
ATOM   662  C  CG  . ARG   A 1 89  ? -6.50355  -1.24945  7.79721   1.000 50.02493 ? 89  ARG   A CG  1 
ATOM   663  C  CD  . ARG   A 1 89  ? -7.21338  -2.50793  8.26729   1.000 53.33821 ? 89  ARG   A CD  1 
ATOM   664  N  NE  . ARG   A 1 89  ? -6.57917  -3.10193  9.43907   1.000 53.72355 ? 89  ARG   A NE  1 
ATOM   665  C  CZ  . ARG   A 1 89  ? -5.71965  -4.11409  9.39024   1.000 52.68041 ? 89  ARG   A CZ  1 
ATOM   666  N  NH1 . ARG   A 1 89  ? -5.38758  -4.65009  8.22359   1.000 47.91761 ? 89  ARG   A NH1 1 
ATOM   667  N  NH2 . ARG   A 1 89  ? -5.19524  -4.59322  10.50932  1.000 50.11682 ? 89  ARG   A NH2 1 
ATOM   668  N  N   . GLU   A 1 90  ? -8.36574  2.44855   8.01547   1.000 51.79797 ? 90  GLU   A N   1 
ATOM   669  C  CA  . GLU   A 1 90  ? -9.59887  2.80721   7.31870   1.000 52.98507 ? 90  GLU   A CA  1 
ATOM   670  C  C   . GLU   A 1 90  ? -9.46939  4.01138   6.39112   1.000 51.43362 ? 90  GLU   A C   1 
ATOM   671  O  O   . GLU   A 1 90  ? -10.20793 4.09799   5.40422   1.000 53.88692 ? 90  GLU   A O   1 
ATOM   672  C  CB  . GLU   A 1 90  ? -10.70370 3.09200   8.33611   1.000 56.93770 ? 90  GLU   A CB  1 
ATOM   673  C  CG  . GLU   A 1 90  ? -11.29364 1.85601   9.00503   1.000 59.96346 ? 90  GLU   A CG  1 
ATOM   674  C  CD  . GLU   A 1 90  ? -12.36496 1.19112   8.16273   1.000 66.69046 ? 90  GLU   A CD  1 
ATOM   675  O  OE1 . GLU   A 1 90  ? -12.13374 0.96024   6.95577   1.000 64.70540 ? 90  GLU   A OE1 1 
ATOM   676  O  OE2 . GLU   A 1 90  ? -13.45003 0.91125   8.71075   1.000 71.59519 ? 90  GLU   A OE2 1 
ATOM   677  N  N   . SER   A 1 91  ? -8.55966  4.92884   6.66658   1.000 48.58582 ? 91  SER   A N   1 
ATOM   678  C  CA  . SER   A 1 91  ? -8.41169  6.15643   5.90204   1.000 45.60581 ? 91  SER   A CA  1 
ATOM   679  C  C   . SER   A 1 91  ? -7.26270  6.03494   4.91268   1.000 43.51272 ? 91  SER   A C   1 
ATOM   680  O  O   . SER   A 1 91  ? -6.45273  5.10707   4.99252   1.000 42.66180 ? 91  SER   A O   1 
ATOM   681  C  CB  . SER   A 1 91  ? -8.17957  7.32985   6.85372   1.000 43.96484 ? 91  SER   A CB  1 
ATOM   682  O  OG  . SER   A 1 91  ? -6.90220  7.23897   7.45554   1.000 47.07798 ? 91  SER   A OG  1 
ATOM   683  N  N   . PRO   A 1 92  ? -7.16715  6.95567   3.94366   1.000 41.40887 ? 92  PRO   A N   1 
ATOM   684  C  CA  . PRO   A 1 92  ? -6.02531  6.93992   3.01742   1.000 39.67792 ? 92  PRO   A CA  1 
ATOM   685  C  C   . PRO   A 1 92  ? -4.68923  6.91087   3.74656   1.000 38.73013 ? 92  PRO   A C   1 
ATOM   686  O  O   . PRO   A 1 92  ? -4.53127  7.48376   4.82414   1.000 38.09895 ? 92  PRO   A O   1 
ATOM   687  C  CB  . PRO   A 1 92  ? -6.19828  8.23864   2.22077   1.000 38.09126 ? 92  PRO   A CB  1 
ATOM   688  C  CG  . PRO   A 1 92  ? -7.66429  8.43566   2.18523   1.000 38.44195 ? 92  PRO   A CG  1 
ATOM   689  C  CD  . PRO   A 1 92  ? -8.18088  7.94221   3.52400   1.000 40.25648 ? 92  PRO   A CD  1 
ATOM   690  N  N   . GLN   A 1 93  ? -3.71969  6.23564   3.13559   1.000 38.03566 ? 93  GLN   A N   1 
ATOM   691  C  CA  . GLN   A 1 93  ? -2.43266  5.97731   3.76687   1.000 36.71212 ? 93  GLN   A CA  1 
ATOM   692  C  C   . GLN   A 1 93  ? -1.44029  7.08693   3.45030   1.000 35.26192 ? 93  GLN   A C   1 
ATOM   693  O  O   . GLN   A 1 93  ? -1.22177  7.41680   2.28167   1.000 35.38896 ? 93  GLN   A O   1 
ATOM   694  C  CB  . GLN   A 1 93  ? -1.87063  4.63532   3.29888   1.000 36.09451 ? 93  GLN   A CB  1 
ATOM   695  C  CG  . GLN   A 1 93  ? -2.65124  3.43149   3.79150   1.000 37.74573 ? 93  GLN   A CG  1 
ATOM   696  C  CD  . GLN   A 1 93  ? -2.57914  3.28165   5.29706   1.000 37.89558 ? 93  GLN   A CD  1 
ATOM   697  O  OE1 . GLN   A 1 93  ? -1.49331  3.25390   5.87629   1.000 37.04655 ? 93  GLN   A OE1 1 
ATOM   698  N  NE2 . GLN   A 1 93  ? -3.73795  3.20170   5.94210   1.000 40.50500 ? 93  GLN   A NE2 1 
ATOM   699  N  N   . ALA   A 1 94  ? -0.84637  7.66158   4.49408   1.000 35.04319 ? 94  ALA   A N   1 
ATOM   700  C  CA  . ALA   A 1 94  ? 0.36768   8.43286   4.30240   1.000 33.21105 ? 94  ALA   A CA  1 
ATOM   701  C  C   . ALA   A 1 94  ? 1.47145   7.50760   3.78734   1.000 32.61973 ? 94  ALA   A C   1 
ATOM   702  O  O   . ALA   A 1 94  ? 1.36850   6.27809   3.84755   1.000 32.28826 ? 94  ALA   A O   1 
ATOM   703  C  CB  . ALA   A 1 94  ? 0.78309   9.11886   5.60366   1.000 29.99940 ? 94  ALA   A CB  1 
ATOM   704  N  N   . PHE   A 1 95  ? 2.54563   8.10801   3.27191   1.000 28.68942 ? 95  PHE   A N   1 
ATOM   705  C  CA  . PHE   A 1 95  ? 3.51631   7.30144   2.53975   1.000 31.83911 ? 95  PHE   A CA  1 
ATOM   706  C  C   . PHE   A 1 95  ? 4.26237   6.30355   3.42085   1.000 32.93835 ? 95  PHE   A C   1 
ATOM   707  O  O   . PHE   A 1 95  ? 4.96366   5.43930   2.88247   1.000 31.28253 ? 95  PHE   A O   1 
ATOM   708  C  CB  . PHE   A 1 95  ? 4.50405   8.19788   1.78430   1.000 32.85683 ? 95  PHE   A CB  1 
ATOM   709  C  CG  . PHE   A 1 95  ? 5.20222   9.21654   2.63991   1.000 30.59942 ? 95  PHE   A CG  1 
ATOM   710  C  CD1 . PHE   A 1 95  ? 6.39856   8.91023   3.26683   1.000 30.47834 ? 95  PHE   A CD1 1 
ATOM   711  C  CD2 . PHE   A 1 95  ? 4.68383   10.49174  2.78394   1.000 30.99590 ? 95  PHE   A CD2 1 
ATOM   712  C  CE1 . PHE   A 1 95  ? 7.05527   9.84893   4.03943   1.000 31.37535 ? 95  PHE   A CE1 1 
ATOM   713  C  CE2 . PHE   A 1 95  ? 5.33719   11.43724  3.55623   1.000 31.37663 ? 95  PHE   A CE2 1 
ATOM   714  C  CZ  . PHE   A 1 95  ? 6.52467   11.11337  4.18498   1.000 30.03688 ? 95  PHE   A CZ  1 
ATOM   715  N  N   . ILE   A 1 96  ? 4.10758   6.37187   4.74620   1.000 31.27223 ? 96  ILE   A N   1 
ATOM   716  C  CA  . ILE   A 1 96  ? 4.64584   5.32248   5.60354   1.000 31.37266 ? 96  ILE   A CA  1 
ATOM   717  C  C   . ILE   A 1 96  ? 3.94339   3.99357   5.35017   1.000 33.06747 ? 96  ILE   A C   1 
ATOM   718  O  O   . ILE   A 1 96  ? 4.50849   2.92773   5.62590   1.000 30.48113 ? 96  ILE   A O   1 
ATOM   719  C  CB  . ILE   A 1 96  ? 4.54311   5.73342   7.08915   1.000 30.71694 ? 96  ILE   A CB  1 
ATOM   720  C  CG1 . ILE   A 1 96  ? 5.29832   4.73865   7.97729   1.000 31.07017 ? 96  ILE   A CG1 1 
ATOM   721  C  CG2 . ILE   A 1 96  ? 3.08482   5.83835   7.52210   1.000 32.33928 ? 96  ILE   A CG2 1 
ATOM   722  C  CD1 . ILE   A 1 96  ? 5.30429   5.10391   9.44495   1.000 31.46579 ? 96  ILE   A CD1 1 
ATOM   723  N  N   . GLY   A 1 97  ? 2.72440   4.02830   4.81467   1.000 33.80241 ? 97  GLY   A N   1 
ATOM   724  C  CA  . GLY   A 1 97  ? 1.98867   2.81416   4.52560   1.000 31.95901 ? 97  GLY   A CA  1 
ATOM   725  C  C   . GLY   A 1 97  ? 1.82302   2.56243   3.04174   1.000 34.17612 ? 97  GLY   A C   1 
ATOM   726  O  O   . GLY   A 1 97  ? 0.90129   1.85491   2.62359   1.000 32.09091 ? 97  GLY   A O   1 
ATOM   727  N  N   . LEU   A 1 98  ? 2.71539   3.13376   2.23740   1.000 32.66284 ? 98  LEU   A N   1 
ATOM   728  C  CA  . LEU   A 1 98  ? 2.68204   2.99368   0.79068   1.000 33.53081 ? 98  LEU   A CA  1 
ATOM   729  C  C   . LEU   A 1 98  ? 3.93754   2.28424   0.30294   1.000 34.79063 ? 98  LEU   A C   1 
ATOM   730  O  O   . LEU   A 1 98  ? 4.99417   2.34639   0.93637   1.000 34.04160 ? 98  LEU   A O   1 
ATOM   731  C  CB  . LEU   A 1 98  ? 2.56542   4.35795   0.09846   1.000 32.47397 ? 98  LEU   A CB  1 
ATOM   732  C  CG  . LEU   A 1 98  ? 1.25551   5.13454   0.24913   1.000 33.77074 ? 98  LEU   A CG  1 
ATOM   733  C  CD1 . LEU   A 1 98  ? 1.37876   6.49626   -0.40821  1.000 34.34174 ? 98  LEU   A CD1 1 
ATOM   734  C  CD2 . LEU   A 1 98  ? 0.09756   4.35705   -0.35495  1.000 34.37382 ? 98  LEU   A CD2 1 
ATOM   735  N  N   . ASP   A 1 99  ? 3.80957   1.61165   -0.82272  1.000 32.92172 ? 99  ASP   A N   1 
ATOM   736  C  CA  . ASP   A 1 99  ? 4.92268   0.99545   -1.51968  1.000 35.26085 ? 99  ASP   A CA  1 
ATOM   737  C  C   . ASP   A 1 99  ? 5.29349   1.81993   -2.74179  1.000 35.48974 ? 99  ASP   A C   1 
ATOM   738  O  O   . ASP   A 1 99  ? 4.51198   2.66371   -3.19168  1.000 34.19738 ? 99  ASP   A O   1 
ATOM   739  C  CB  . ASP   A 1 99  ? 4.55671   -0.43132  -1.94634  1.000 34.78754 ? 99  ASP   A CB  1 
ATOM   740  C  CG  . ASP   A 1 99  ? 4.22090   -1.32528  -0.76772  1.000 33.37176 ? 99  ASP   A CG  1 
ATOM   741  O  OD1 . ASP   A 1 99  ? 4.89698   -1.21500  0.27524   1.000 32.78527 ? 99  ASP   A OD1 1 
ATOM   742  O  OD2 . ASP   A 1 99  ? 3.27776   -2.13598  -0.88448  1.000 32.84913 ? 99  ASP   A OD2 1 
ATOM   743  N  N   . PRO   A 1 100 ? 6.48496   1.62456   -3.29973  1.000 37.44799 ? 100 PRO   A N   1 
ATOM   744  C  CA  . PRO   A 1 100 ? 6.79983   2.25362   -4.57454  1.000 36.56669 ? 100 PRO   A CA  1 
ATOM   745  C  C   . PRO   A 1 100 ? 5.80578   1.81019   -5.64181  1.000 37.26364 ? 100 PRO   A C   1 
ATOM   746  O  O   . PRO   A 1 100 ? 5.28799   0.68172   -5.59171  1.000 36.59027 ? 100 PRO   A O   1 
ATOM   747  C  CB  . PRO   A 1 100 ? 8.21461   1.75374   -4.88224  1.000 36.68012 ? 100 PRO   A CB  1 
ATOM   748  C  CG  . PRO   A 1 100 ? 8.80343   1.49248   -3.54467  1.000 36.55810 ? 100 PRO   A CG  1 
ATOM   749  C  CD  . PRO   A 1 100 ? 7.66900   0.97556   -2.70292  1.000 35.88558 ? 100 PRO   A CD  1 
ATOM   750  N  N   . PRO   A 1 101 ? 5.51374   2.67903   -6.62022  1.000 36.94364 ? 101 PRO   A N   1 
ATOM   751  C  CA  . PRO   A 1 101 ? 6.07880   4.02080   -6.79061  1.000 36.61063 ? 101 PRO   A CA  1 
ATOM   752  C  C   . PRO   A 1 101 ? 5.32209   5.11570   -6.03355  1.000 35.94828 ? 101 PRO   A C   1 
ATOM   753  O  O   . PRO   A 1 101 ? 5.81014   6.24329   -5.95464  1.000 36.34087 ? 101 PRO   A O   1 
ATOM   754  C  CB  . PRO   A 1 101 ? 5.96863   4.23818   -8.29928  1.000 36.13830 ? 101 PRO   A CB  1 
ATOM   755  C  CG  . PRO   A 1 101 ? 4.71193   3.51906   -8.66130  1.000 37.18272 ? 101 PRO   A CG  1 
ATOM   756  C  CD  . PRO   A 1 101 ? 4.62391   2.31963   -7.74181  1.000 37.58336 ? 101 PRO   A CD  1 
ATOM   757  N  N   . GLU   A 1 102 ? 4.14738   4.78757   -5.49070  1.000 35.84069 ? 102 GLU   A N   1 
ATOM   758  C  CA  . GLU   A 1 102 ? 3.34280   5.79271   -4.80312  1.000 36.49423 ? 102 GLU   A CA  1 
ATOM   759  C  C   . GLU   A 1 102 ? 4.06824   6.36327   -3.59496  1.000 36.45624 ? 102 GLU   A C   1 
ATOM   760  O  O   . GLU   A 1 102 ? 3.92391   7.55495   -3.29380  1.000 36.90718 ? 102 GLU   A O   1 
ATOM   761  C  CB  . GLU   A 1 102 ? 1.99798   5.20152   -4.37285  1.000 37.37482 ? 102 GLU   A CB  1 
ATOM   762  C  CG  . GLU   A 1 102 ? 1.07295   4.81865   -5.52107  1.000 38.81389 ? 102 GLU   A CG  1 
ATOM   763  C  CD  . GLU   A 1 102 ? 1.37817   3.45002   -6.08442  1.000 40.33952 ? 102 GLU   A CD  1 
ATOM   764  O  OE1 . GLU   A 1 102 ? 1.99346   2.63611   -5.36500  1.000 39.68316 ? 102 GLU   A OE1 1 
ATOM   765  O  OE2 . GLU   A 1 102 ? 1.01061   3.19216   -7.24896  1.000 48.12556 ? 102 GLU   A OE2 1 
ATOM   766  N  N   . HIS   A 1 103 ? 4.86743   5.54090   -2.91006  1.000 33.97409 ? 103 HIS   A N   1 
ATOM   767  C  CA  . HIS   A 1 103 ? 5.57712   6.00990   -1.72232  1.000 36.33146 ? 103 HIS   A CA  1 
ATOM   768  C  C   . HIS   A 1 103 ? 6.50828   7.16653   -2.05046  1.000 32.23675 ? 103 HIS   A C   1 
ATOM   769  O  O   . HIS   A 1 103 ? 6.53882   8.17194   -1.33611  1.000 33.43103 ? 103 HIS   A O   1 
ATOM   770  C  CB  . HIS   A 1 103 ? 6.36675   4.86828   -1.08504  1.000 32.38678 ? 103 HIS   A CB  1 
ATOM   771  C  CG  . HIS   A 1 103 ? 7.49710   5.33124   -0.21992  1.000 31.23422 ? 103 HIS   A CG  1 
ATOM   772  N  ND1 . HIS   A 1 103 ? 8.77943   5.50092   -0.69787  1.000 31.73360 ? 103 HIS   A ND1 1 
ATOM   773  C  CD2 . HIS   A 1 103 ? 7.53575   5.66879   1.09083   1.000 31.95559 ? 103 HIS   A CD2 1 
ATOM   774  C  CE1 . HIS   A 1 103 ? 9.56020   5.91597   0.28385   1.000 30.90746 ? 103 HIS   A CE1 1 
ATOM   775  N  NE2 . HIS   A 1 103 ? 8.83029   6.02612   1.37954   1.000 29.94701 ? 103 HIS   A NE2 1 
ATOM   776  N  N   . GLY   A 1 104 ? 7.28256   7.03714   -3.12731  1.000 34.33521 ? 104 GLY   A N   1 
ATOM   777  C  CA  . GLY   A 1 104 ? 8.25328   8.06701   -3.45693  1.000 33.82665 ? 104 GLY   A CA  1 
ATOM   778  C  C   . GLY   A 1 104 ? 7.60911   9.35114   -3.94229  1.000 36.09108 ? 104 GLY   A C   1 
ATOM   779  O  O   . GLY   A 1 104 ? 8.09862   10.44705  -3.65407  1.000 34.93474 ? 104 GLY   A O   1 
ATOM   780  N  N   A THR   A 1 105 ? 6.50546   9.23905   -4.68424  0.500 35.70481 ? 105 THR   A N   1 
ATOM   781  N  N   B THR   A 1 105 ? 6.50802   9.24072   -4.68531  0.500 35.68361 ? 105 THR   A N   1 
ATOM   782  C  CA  A THR   A 1 105 ? 5.82032   10.43087  -5.17356  0.500 35.70463 ? 105 THR   A CA  1 
ATOM   783  C  CA  B THR   A 1 105 ? 5.82380   10.43579  -5.16999  0.500 35.67978 ? 105 THR   A CA  1 
ATOM   784  C  C   A THR   A 1 105 ? 5.25390   11.25224  -4.02196  0.500 34.28654 ? 105 THR   A C   1 
ATOM   785  C  C   B THR   A 1 105 ? 5.26398   11.25432  -4.01450  0.500 34.26183 ? 105 THR   A C   1 
ATOM   786  O  O   A THR   A 1 105 ? 5.28638   12.48733  -4.05489  0.500 35.07095 ? 105 THR   A O   1 
ATOM   787  O  O   B THR   A 1 105 ? 5.30986   12.48950  -4.03977  0.500 35.09443 ? 105 THR   A O   1 
ATOM   788  C  CB  A THR   A 1 105 ? 4.71062   10.03362  -6.14559  0.500 35.81274 ? 105 THR   A CB  1 
ATOM   789  C  CB  B THR   A 1 105 ? 4.70668   10.05503  -6.14810  0.500 35.75855 ? 105 THR   A CB  1 
ATOM   790  O  OG1 A THR   A 1 105 ? 5.25272   9.18864   -7.16935  0.500 35.81483 ? 105 THR   A OG1 1 
ATOM   791  O  OG1 B THR   A 1 105 ? 3.74545   9.22379   -5.48596  0.500 35.64087 ? 105 THR   A OG1 1 
ATOM   792  C  CG2 A THR   A 1 105 ? 4.09859   11.27079  -6.79134  0.500 36.13467 ? 105 THR   A CG2 1 
ATOM   793  C  CG2 B THR   A 1 105 ? 5.27458   9.31264   -7.34790  0.500 35.70170 ? 105 THR   A CG2 1 
ATOM   794  N  N   . ARG   A 1 106 ? 4.73990   10.58215  -2.98882  1.000 36.34490 ? 106 ARG   A N   1 
ATOM   795  C  CA  . ARG   A 1 106 ? 4.18600   11.28758  -1.83803  1.000 32.93001 ? 106 ARG   A CA  1 
ATOM   796  C  C   . ARG   A 1 106 ? 5.28846   11.80790  -0.92573  1.000 33.48090 ? 106 ARG   A C   1 
ATOM   797  O  O   . ARG   A 1 106 ? 5.24254   12.96101  -0.48241  1.000 33.65006 ? 106 ARG   A O   1 
ATOM   798  C  CB  . ARG   A 1 106 ? 3.24171   10.37166  -1.05352  1.000 34.22944 ? 106 ARG   A CB  1 
ATOM   799  C  CG  . ARG   A 1 106 ? 2.05007   9.83396   -1.83999  1.000 38.55317 ? 106 ARG   A CG  1 
ATOM   800  C  CD  . ARG   A 1 106 ? 1.56499   10.82404  -2.88113  1.000 40.58903 ? 106 ARG   A CD  1 
ATOM   801  N  NE  . ARG   A 1 106 ? 0.15527   10.64551  -3.21217  1.000 36.29598 ? 106 ARG   A NE  1 
ATOM   802  C  CZ  . ARG   A 1 106 ? -0.37663  10.97174  -4.38444  1.000 36.76696 ? 106 ARG   A CZ  1 
ATOM   803  N  NH1 . ARG   A 1 106 ? 0.39175   11.46934  -5.34337  1.000 41.05120 ? 106 ARG   A NH1 1 
ATOM   804  N  NH2 . ARG   A 1 106 ? -1.67078  10.78881  -4.60467  1.000 36.96520 ? 106 ARG   A NH2 1 
ATOM   805  N  N   . ARG   A 1 107 ? 6.28302   10.96519  -0.62903  1.000 33.11244 ? 107 ARG   A N   1 
ATOM   806  C  CA  . ARG   A 1 107 ? 7.36577   11.37847  0.25909   1.000 32.26615 ? 107 ARG   A CA  1 
ATOM   807  C  C   . ARG   A 1 107 ? 8.11009   12.58273  -0.30119  1.000 33.12592 ? 107 ARG   A C   1 
ATOM   808  O  O   . ARG   A 1 107 ? 8.44005   13.51511  0.44086   1.000 32.03842 ? 107 ARG   A O   1 
ATOM   809  C  CB  . ARG   A 1 107 ? 8.33236   10.21655  0.49944   1.000 32.54738 ? 107 ARG   A CB  1 
ATOM   810  C  CG  . ARG   A 1 107 ? 9.54495   10.57889  1.36228   1.000 32.10873 ? 107 ARG   A CG  1 
ATOM   811  C  CD  . ARG   A 1 107 ? 10.52066  9.40825   1.48897   1.000 31.88906 ? 107 ARG   A CD  1 
ATOM   812  N  NE  . ARG   A 1 107 ? 11.82170  9.82102   2.01728   1.000 32.45257 ? 107 ARG   A NE  1 
ATOM   813  C  CZ  . ARG   A 1 107 ? 12.30780  9.46432   3.20337   1.000 30.43596 ? 107 ARG   A CZ  1 
ATOM   814  N  NH1 . ARG   A 1 107 ? 11.61158  8.66903   4.00465   1.000 32.53459 ? 107 ARG   A NH1 1 
ATOM   815  N  NH2 . ARG   A 1 107 ? 13.50204  9.89871   3.58786   1.000 31.12821 ? 107 ARG   A NH2 1 
ATOM   816  N  N   . ARG   A 1 108 ? 8.36837   12.59057  -1.61263  1.000 33.35322 ? 108 ARG   A N   1 
ATOM   817  C  CA  . ARG   A 1 108 ? 9.07116   13.71073  -2.22850  1.000 33.54439 ? 108 ARG   A CA  1 
ATOM   818  C  C   . ARG   A 1 108 ? 8.29682   15.01858  -2.13488  1.000 32.84933 ? 108 ARG   A C   1 
ATOM   819  O  O   . ARG   A 1 108 ? 8.88397   16.08133  -2.36778  1.000 33.01198 ? 108 ARG   A O   1 
ATOM   820  C  CB  . ARG   A 1 108 ? 9.39219   13.39889  -3.69371  1.000 35.03075 ? 108 ARG   A CB  1 
ATOM   821  C  CG  . ARG   A 1 108 ? 10.53256  12.40213  -3.86596  1.000 35.58649 ? 108 ARG   A CG  1 
ATOM   822  C  CD  . ARG   A 1 108 ? 11.00749  12.31835  -5.31214  1.000 36.54298 ? 108 ARG   A CD  1 
ATOM   823  N  NE  . ARG   A 1 108 ? 10.01030  11.72909  -6.20274  1.000 36.48527 ? 108 ARG   A NE  1 
ATOM   824  C  CZ  . ARG   A 1 108 ? 9.84975   10.42026  -6.38321  1.000 38.22098 ? 108 ARG   A CZ  1 
ATOM   825  N  NH1 . ARG   A 1 108 ? 8.92127   9.97204   -7.21858  1.000 37.18836 ? 108 ARG   A NH1 1 
ATOM   826  N  NH2 . ARG   A 1 108 ? 10.61260  9.55754   -5.72358  1.000 35.60586 ? 108 ARG   A NH2 1 
ATOM   827  N  N   . MET   A 1 109 ? 7.00553   14.97350  -1.79844  1.000 32.03880 ? 109 MET   A N   1 
ATOM   828  C  CA  . MET   A 1 109 ? 6.26240   16.20363  -1.55465  1.000 32.48684 ? 109 MET   A CA  1 
ATOM   829  C  C   . MET   A 1 109 ? 6.64257   16.85431  -0.23012  1.000 31.00120 ? 109 MET   A C   1 
ATOM   830  O  O   . MET   A 1 109 ? 6.34064   18.03458  -0.02562  1.000 30.82790 ? 109 MET   A O   1 
ATOM   831  C  CB  . MET   A 1 109 ? 4.75687   15.92555  -1.58392  1.000 31.57938 ? 109 MET   A CB  1 
ATOM   832  C  CG  . MET   A 1 109 ? 4.25336   15.36805  -2.90987  1.000 33.49239 ? 109 MET   A CG  1 
ATOM   833  S  SD  . MET   A 1 109 ? 2.47591   15.05028  -2.92046  1.000 32.87201 ? 109 MET   A SD  1 
ATOM   834  C  CE  . MET   A 1 109 ? 2.23858   14.48509  -4.60389  1.000 34.37778 ? 109 MET   A CE  1 
ATOM   835  N  N   . THR   A 1 110 ? 7.30322   16.11832  0.66696   1.000 31.38107 ? 110 THR   A N   1 
ATOM   836  C  CA  . THR   A 1 110 ? 7.59077   16.60228  2.00808   1.000 31.91534 ? 110 THR   A CA  1 
ATOM   837  C  C   . THR   A 1 110 ? 9.07446   16.74684  2.31990   1.000 32.01797 ? 110 THR   A C   1 
ATOM   838  O  O   . THR   A 1 110 ? 9.41099   17.40781  3.30833   1.000 31.30342 ? 110 THR   A O   1 
ATOM   839  C  CB  . THR   A 1 110 ? 6.96075   15.67038  3.05926   1.000 30.93240 ? 110 THR   A CB  1 
ATOM   840  O  OG1 . THR   A 1 110 ? 7.60953   14.39187  3.02428   1.000 30.96084 ? 110 THR   A OG1 1 
ATOM   841  C  CG2 . THR   A 1 110 ? 5.47543   15.48060  2.78577   1.000 30.57572 ? 110 THR   A CG2 1 
ATOM   842  N  N   . ILE   A 1 111 ? 9.96749   16.16839  1.51027   1.000 31.12346 ? 111 ILE   A N   1 
ATOM   843  C  CA  . ILE   A 1 111 ? 11.37567  16.07035  1.89022   1.000 33.41894 ? 111 ILE   A CA  1 
ATOM   844  C  C   . ILE   A 1 111 ? 12.06406  17.42569  1.99572   1.000 33.94685 ? 111 ILE   A C   1 
ATOM   845  O  O   . ILE   A 1 111 ? 13.08844  17.53707  2.68033   1.000 32.58902 ? 111 ILE   A O   1 
ATOM   846  C  CB  . ILE   A 1 111 ? 12.15061  15.18600  0.89703   1.000 33.52020 ? 111 ILE   A CB  1 
ATOM   847  C  CG1 . ILE   A 1 111 ? 12.12086  15.81022  -0.50059  1.000 33.52256 ? 111 ILE   A CG1 1 
ATOM   848  C  CG2 . ILE   A 1 111 ? 11.59511  13.76946  0.88821   1.000 32.94407 ? 111 ILE   A CG2 1 
ATOM   849  C  CD1 . ILE   A 1 111 ? 12.82265  14.98773  -1.54832  1.000 34.92636 ? 111 ILE   A CD1 1 
ATOM   850  N  N   . SER   A 1 112 ? 11.54056  18.45957  1.33052   1.000 34.25461 ? 112 SER   A N   1 
ATOM   851  C  CA  . SER   A 1 112 ? 12.21598  19.75456  1.33208   1.000 34.91712 ? 112 SER   A CA  1 
ATOM   852  C  C   . SER   A 1 112 ? 12.34895  20.32167  2.73924   1.000 36.32621 ? 112 SER   A C   1 
ATOM   853  O  O   . SER   A 1 112 ? 13.32756  21.01391  3.03875   1.000 38.80565 ? 112 SER   A O   1 
ATOM   854  C  CB  . SER   A 1 112 ? 11.46766  20.73870  0.43165   1.000 36.97135 ? 112 SER   A CB  1 
ATOM   855  O  OG  . SER   A 1 112 ? 10.12783  20.90340  0.86810   1.000 39.01191 ? 112 SER   A OG  1 
ATOM   856  N  N   . GLU   A 1 113 ? 11.39211  20.02940  3.61408   1.000 35.74951 ? 113 GLU   A N   1 
ATOM   857  C  CA  . GLU   A 1 113 ? 11.38014  20.57153  4.96589   1.000 36.64169 ? 113 GLU   A CA  1 
ATOM   858  C  C   . GLU   A 1 113 ? 12.28394  19.81336  5.93164   1.000 35.90264 ? 113 GLU   A C   1 
ATOM   859  O  O   . GLU   A 1 113 ? 12.41598  20.23642  7.08430   1.000 33.53235 ? 113 GLU   A O   1 
ATOM   860  C  CB  . GLU   A 1 113 ? 9.94695   20.57946  5.50486   1.000 36.40857 ? 113 GLU   A CB  1 
ATOM   861  C  CG  . GLU   A 1 113 ? 8.92065   21.10099  4.50656   1.000 37.37951 ? 113 GLU   A CG  1 
ATOM   862  C  CD  . GLU   A 1 113 ? 9.22201   22.51253  4.04500   1.000 41.61909 ? 113 GLU   A CD  1 
ATOM   863  O  OE1 . GLU   A 1 113 ? 9.54439   23.36200  4.90260   1.000 48.99392 ? 113 GLU   A OE1 1 
ATOM   864  O  OE2 . GLU   A 1 113 ? 9.14775   22.77099  2.82484   1.000 49.69968 ? 113 GLU   A OE2 1 
ATOM   865  N  N   . PHE   A 1 114 ? 12.91153  18.71751  5.50155   1.000 32.53068 ? 114 PHE   A N   1 
ATOM   866  C  CA  . PHE   A 1 114 ? 13.69702  17.87764  6.39887   1.000 34.10462 ? 114 PHE   A CA  1 
ATOM   867  C  C   . PHE   A 1 114 ? 15.13770  17.68707  5.93689   1.000 33.67287 ? 114 PHE   A C   1 
ATOM   868  O  O   . PHE   A 1 114 ? 15.82967  16.80367  6.45734   1.000 33.97046 ? 114 PHE   A O   1 
ATOM   869  C  CB  . PHE   A 1 114 ? 13.01524  16.51632  6.57421   1.000 32.03134 ? 114 PHE   A CB  1 
ATOM   870  C  CG  . PHE   A 1 114 ? 11.66093  16.59958  7.22397   1.000 31.05825 ? 114 PHE   A CG  1 
ATOM   871  C  CD1 . PHE   A 1 114 ? 10.52100  16.79930  6.46083   1.000 31.56066 ? 114 PHE   A CD1 1 
ATOM   872  C  CD2 . PHE   A 1 114 ? 11.52832  16.48894  8.59803   1.000 30.96810 ? 114 PHE   A CD2 1 
ATOM   873  C  CE1 . PHE   A 1 114 ? 9.27344   16.88056  7.05494   1.000 31.46418 ? 114 PHE   A CE1 1 
ATOM   874  C  CE2 . PHE   A 1 114 ? 10.28234  16.57073  9.19994   1.000 31.36820 ? 114 PHE   A CE2 1 
ATOM   875  C  CZ  . PHE   A 1 114 ? 9.15345   16.76768  8.42568   1.000 30.67822 ? 114 PHE   A CZ  1 
ATOM   876  N  N   . THR   A 1 115 ? 15.61244  18.49571  4.99121   1.000 35.31296 ? 115 THR   A N   1 
ATOM   877  C  CA  . THR   A 1 115 ? 16.97203  18.36903  4.48927   1.000 36.73353 ? 115 THR   A CA  1 
ATOM   878  C  C   . THR   A 1 115 ? 17.98434  18.74523  5.57248   1.000 37.91801 ? 115 THR   A C   1 
ATOM   879  O  O   . THR   A 1 115 ? 17.65318  19.35155  6.59577   1.000 36.89745 ? 115 THR   A O   1 
ATOM   880  C  CB  . THR   A 1 115 ? 17.17902  19.25891  3.26365   1.000 36.99837 ? 115 THR   A CB  1 
ATOM   881  O  OG1 . THR   A 1 115 ? 17.22299  20.63242  3.67054   1.000 38.13374 ? 115 THR   A OG1 1 
ATOM   882  C  CG2 . THR   A 1 115 ? 16.04844  19.06769  2.26656   1.000 35.94577 ? 115 THR   A CG2 1 
ATOM   883  N  N   . VAL   A 1 116 ? 19.24708  18.38705  5.32568   1.000 37.84306 ? 116 VAL   A N   1 
ATOM   884  C  CA  . VAL   A 1 116 ? 20.31989  18.76808  6.24269   1.000 38.16717 ? 116 VAL   A CA  1 
ATOM   885  C  C   . VAL   A 1 116 ? 20.42243  20.28512  6.34263   1.000 39.64644 ? 116 VAL   A C   1 
ATOM   886  O  O   . VAL   A 1 116 ? 20.70050  20.83543  7.41530   1.000 39.23187 ? 116 VAL   A O   1 
ATOM   887  C  CB  . VAL   A 1 116 ? 21.65502  18.13852  5.79886   1.000 42.80150 ? 116 VAL   A CB  1 
ATOM   888  C  CG1 . VAL   A 1 116 ? 21.61621  16.62648  5.97272   1.000 38.15772 ? 116 VAL   A CG1 1 
ATOM   889  C  CG2 . VAL   A 1 116 ? 21.97189  18.51053  4.35199   1.000 40.84506 ? 116 VAL   A CG2 1 
ATOM   890  N  N   . LYS   A 1 117 ? 20.18517  20.98447  5.23044   1.000 39.19036 ? 117 LYS   A N   1 
ATOM   891  C  CA  . LYS   A 1 117 ? 20.30028  22.43801  5.22728   1.000 40.41220 ? 117 LYS   A CA  1 
ATOM   892  C  C   . LYS   A 1 117 ? 19.17875  23.08196  6.03038   1.000 39.86821 ? 117 LYS   A C   1 
ATOM   893  O  O   . LYS   A 1 117 ? 19.41095  24.04579  6.76819   1.000 41.27536 ? 117 LYS   A O   1 
ATOM   894  C  CB  . LYS   A 1 117 ? 20.30153  22.95227  3.78767   1.000 40.99992 ? 117 LYS   A CB  1 
ATOM   895  C  CG  . LYS   A 1 117 ? 20.47900  24.45420  3.64556   1.000 41.89709 ? 117 LYS   A CG  1 
ATOM   896  C  CD  . LYS   A 1 117 ? 20.60577  24.84579  2.17808   1.000 43.17791 ? 117 LYS   A CD  1 
ATOM   897  C  CE  . LYS   A 1 117 ? 20.64847  26.35601  2.00650   1.000 44.71192 ? 117 LYS   A CE  1 
ATOM   898  N  NZ  . LYS   A 1 117 ? 20.80524  26.74395  0.57466   1.000 44.05142 ? 117 LYS   A NZ  1 
ATOM   899  N  N   . ARG   A 1 118 ? 17.95546  22.56553  5.89732   1.000 39.86684 ? 118 ARG   A N   1 
ATOM   900  C  CA  . ARG   A 1 118 ? 16.83341  23.11977  6.64704   1.000 40.68571 ? 118 ARG   A CA  1 
ATOM   901  C  C   . ARG   A 1 118 ? 16.96151  22.82032  8.13523   1.000 40.08990 ? 118 ARG   A C   1 
ATOM   902  O  O   . ARG   A 1 118 ? 16.66206  23.67874  8.97344   1.000 41.06530 ? 118 ARG   A O   1 
ATOM   903  C  CB  . ARG   A 1 118 ? 15.51605  22.57079  6.09985   1.000 40.04060 ? 118 ARG   A CB  1 
ATOM   904  C  CG  . ARG   A 1 118 ? 15.22925  22.96205  4.66145   1.000 41.82366 ? 118 ARG   A CG  1 
ATOM   905  C  CD  . ARG   A 1 118 ? 14.92981  24.44574  4.53851   1.000 44.26614 ? 118 ARG   A CD  1 
ATOM   906  N  NE  . ARG   A 1 118 ? 13.89354  24.86421  5.47793   1.000 49.78452 ? 118 ARG   A NE  1 
ATOM   907  C  CZ  . ARG   A 1 118 ? 12.58918  24.80975  5.22775   1.000 51.61248 ? 118 ARG   A CZ  1 
ATOM   908  N  NH1 . ARG   A 1 118 ? 12.15250  24.35367  4.06130   1.000 47.64379 ? 118 ARG   A NH1 1 
ATOM   909  N  NH2 . ARG   A 1 118 ? 11.72008  25.21265  6.14551   1.000 58.70348 ? 118 ARG   A NH2 1 
ATOM   910  N  N   . ILE   A 1 119 ? 17.40945  21.61129  8.48136   1.000 38.21567 ? 119 ILE   A N   1 
ATOM   911  C  CA  . ILE   A 1 119 ? 17.53279  21.23162  9.88686   1.000 38.29644 ? 119 ILE   A CA  1 
ATOM   912  C  C   . ILE   A 1 119 ? 18.58535  22.08968  10.57901  1.000 40.54028 ? 119 ILE   A C   1 
ATOM   913  O  O   . ILE   A 1 119 ? 18.35502  22.62657  11.66929  1.000 38.23130 ? 119 ILE   A O   1 
ATOM   914  C  CB  . ILE   A 1 119 ? 17.84989  19.73022  10.01160  1.000 37.20539 ? 119 ILE   A CB  1 
ATOM   915  C  CG1 . ILE   A 1 119 ? 16.66347  18.89342  9.52516   1.000 35.24836 ? 119 ILE   A CG1 1 
ATOM   916  C  CG2 . ILE   A 1 119 ? 18.21392  19.37109  11.44311  1.000 35.52105 ? 119 ILE   A CG2 1 
ATOM   917  C  CD1 . ILE   A 1 119 ? 15.32400  19.36308  10.05473  1.000 34.39776 ? 119 ILE   A CD1 1 
ATOM   918  N  N   . LYS   A 1 120 ? 19.75834  22.23221  9.95533   1.000 40.11595 ? 120 LYS   A N   1 
ATOM   919  C  CA  . LYS   A 1 120 ? 20.76643  23.14144  10.49132  1.000 42.20231 ? 120 LYS   A CA  1 
ATOM   920  C  C   . LYS   A 1 120 ? 20.22998  24.56435  10.57711  1.000 41.96397 ? 120 LYS   A C   1 
ATOM   921  O  O   . LYS   A 1 120 ? 20.54392  25.29937  11.52036  1.000 45.63973 ? 120 LYS   A O   1 
ATOM   922  C  CB  . LYS   A 1 120 ? 22.03198  23.09880  9.63463   1.000 46.15961 ? 120 LYS   A CB  1 
ATOM   923  C  CG  . LYS   A 1 120 ? 23.06419  24.15189  10.02049  1.000 46.39561 ? 120 LYS   A CG  1 
ATOM   924  C  CD  . LYS   A 1 120 ? 24.38412  23.95069  9.29356   1.000 49.30788 ? 120 LYS   A CD  1 
ATOM   925  C  CE  . LYS   A 1 120 ? 24.66538  25.09022  8.32668   1.000 50.59489 ? 120 LYS   A CE  1 
ATOM   926  N  NZ  . LYS   A 1 120 ? 24.62671  26.41546  9.00348   1.000 52.88819 ? 120 LYS   A NZ  1 
ATOM   927  N  N   . GLY   A 1 121 ? 19.41134  24.96884  9.60500   1.000 41.32785 ? 121 GLY   A N   1 
ATOM   928  C  CA  . GLY   A 1 121 ? 18.80705  26.28746  9.66706   1.000 41.61621 ? 121 GLY   A CA  1 
ATOM   929  C  C   . GLY   A 1 121 ? 17.85504  26.45001  10.83530  1.000 41.66179 ? 121 GLY   A C   1 
ATOM   930  O  O   . GLY   A 1 121 ? 17.67189  27.56048  11.34151  1.000 44.34734 ? 121 GLY   A O   1 
ATOM   931  N  N   . MET   A 1 122 ? 17.23883  25.35447  11.28065  1.000 40.86797 ? 122 MET   A N   1 
ATOM   932  C  CA  . MET   A 1 122 ? 16.31523  25.38986  12.40731  1.000 41.52790 ? 122 MET   A CA  1 
ATOM   933  C  C   . MET   A 1 122 ? 17.02003  25.33515  13.75509  1.000 40.44055 ? 122 MET   A C   1 
ATOM   934  O  O   . MET   A 1 122 ? 16.34661  25.43004  14.78776  1.000 38.96783 ? 122 MET   A O   1 
ATOM   935  C  CB  . MET   A 1 122 ? 15.31363  24.23496  12.30545  1.000 39.90184 ? 122 MET   A CB  1 
ATOM   936  C  CG  . MET   A 1 122 ? 14.36330  24.33981  11.12629  1.000 40.91903 ? 122 MET   A CG  1 
ATOM   937  S  SD  . MET   A 1 122 ? 13.43292  22.82216  10.84329  1.000 44.92634 ? 122 MET   A SD  1 
ATOM   938  C  CE  . MET   A 1 122 ? 12.66414  22.60529  12.44284  1.000 37.92481 ? 122 MET   A CE  1 
ATOM   939  N  N   . ARG   A 1 123 ? 18.34380  25.17829  13.76819  1.000 39.33539 ? 123 ARG   A N   1 
ATOM   940  C  CA  . ARG   A 1 123 ? 19.09293  25.10575  15.02192  1.000 40.27218 ? 123 ARG   A CA  1 
ATOM   941  C  C   . ARG   A 1 123 ? 18.82121  26.27506  15.96183  1.000 40.45332 ? 123 ARG   A C   1 
ATOM   942  O  O   . ARG   A 1 123 ? 18.54127  26.02554  17.14555  1.000 39.05725 ? 123 ARG   A O   1 
ATOM   943  C  CB  . ARG   A 1 123 ? 20.59035  24.98405  14.70743  1.000 41.55780 ? 123 ARG   A CB  1 
ATOM   944  C  CG  . ARG   A 1 123 ? 21.49983  25.52934  15.79562  1.000 43.07511 ? 123 ARG   A CG  1 
ATOM   945  C  CD  . ARG   A 1 123 ? 22.01129  24.42090  16.67994  1.000 43.60993 ? 123 ARG   A CD  1 
ATOM   946  N  NE  . ARG   A 1 123 ? 22.74162  23.42911  15.90165  1.000 46.59870 ? 123 ARG   A NE  1 
ATOM   947  C  CZ  . ARG   A 1 123 ? 23.26890  22.32436  16.41394  1.000 46.03283 ? 123 ARG   A CZ  1 
ATOM   948  N  NH1 . ARG   A 1 123 ? 23.14447  22.07442  17.70752  1.000 43.85793 ? 123 ARG   A NH1 1 
ATOM   949  N  NH2 . ARG   A 1 123 ? 23.91743  21.47050  15.63386  1.000 45.68216 ? 123 ARG   A NH2 1 
ATOM   950  N  N   . PRO   A 1 124 ? 18.87575  27.54537  15.52853  1.000 40.12708 ? 124 PRO   A N   1 
ATOM   951  C  CA  . PRO   A 1 124 ? 18.59967  28.63575  16.48154  1.000 40.06428 ? 124 PRO   A CA  1 
ATOM   952  C  C   . PRO   A 1 124 ? 17.18908  28.60644  17.04130  1.000 38.82966 ? 124 PRO   A C   1 
ATOM   953  O  O   . PRO   A 1 124 ? 17.00178  28.85576  18.23791  1.000 39.78111 ? 124 PRO   A O   1 
ATOM   954  C  CB  . PRO   A 1 124 ? 18.85333  29.90430  15.64983  1.000 39.97101 ? 124 PRO   A CB  1 
ATOM   955  C  CG  . PRO   A 1 124 ? 19.72042  29.46518  14.52640  1.000 41.15749 ? 124 PRO   A CG  1 
ATOM   956  C  CD  . PRO   A 1 124 ? 19.26049  28.07506  14.20726  1.000 39.93774 ? 124 PRO   A CD  1 
ATOM   957  N  N   A GLU   A 1 125 ? 16.17903  28.29868  16.22684  0.500 39.07869 ? 125 GLU   A N   1 
ATOM   958  N  N   B GLU   A 1 125 ? 16.19301  28.32177  16.19638  0.500 38.84865 ? 125 GLU   A N   1 
ATOM   959  C  CA  A GLU   A 1 125 ? 14.82684  28.30431  16.77219  0.500 39.72250 ? 125 GLU   A CA  1 
ATOM   960  C  CA  B GLU   A 1 125 ? 14.81200  28.24438  16.65996  0.500 39.67587 ? 125 GLU   A CA  1 
ATOM   961  C  C   A GLU   A 1 125 ? 14.57033  27.09218  17.66217  0.500 39.69868 ? 125 GLU   A C   1 
ATOM   962  C  C   B GLU   A 1 125 ? 14.63546  27.12334  17.67295  0.500 39.01790 ? 125 GLU   A C   1 
ATOM   963  O  O   A GLU   A 1 125 ? 13.76459  27.17789  18.59550  0.500 36.34089 ? 125 GLU   A O   1 
ATOM   964  O  O   B GLU   A 1 125 ? 13.95359  27.29518  18.69040  0.500 36.42051 ? 125 GLU   A O   1 
ATOM   965  C  CB  A GLU   A 1 125 ? 13.78946  28.39866  15.65072  0.500 41.21211 ? 125 GLU   A CB  1 
ATOM   966  C  CB  B GLU   A 1 125 ? 13.87350  28.04036  15.46961  0.500 40.82487 ? 125 GLU   A CB  1 
ATOM   967  C  CG  A GLU   A 1 125 ? 14.01910  27.50076  14.45742  0.500 41.19663 ? 125 GLU   A CG  1 
ATOM   968  C  CG  B GLU   A 1 125 ? 12.39877  27.88351  15.82982  0.500 41.77472 ? 125 GLU   A CG  1 
ATOM   969  C  CD  A GLU   A 1 125 ? 13.08517  27.83467  13.30812  0.500 43.66928 ? 125 GLU   A CD  1 
ATOM   970  C  CD  B GLU   A 1 125 ? 11.89868  26.45802  15.67313  0.500 43.66928 ? 125 GLU   A CD  1 
ATOM   971  O  OE1 A GLU   A 1 125 ? 12.22601  28.72617  13.47866  0.500 50.68928 ? 125 GLU   A OE1 1 
ATOM   972  O  OE1 B GLU   A 1 125 ? 12.71619  25.57262  15.34557  0.500 50.68928 ? 125 GLU   A OE1 1 
ATOM   973  O  OE2 A GLU   A 1 125 ? 13.21002  27.21335  12.23363  0.500 43.00335 ? 125 GLU   A OE2 1 
ATOM   974  O  OE2 B GLU   A 1 125 ? 10.68722  26.22447  15.87506  0.500 40.89928 ? 125 GLU   A OE2 1 
ATOM   975  N  N   . VAL   A 1 126 ? 15.24743  25.96642  17.41064  1.000 38.03399 ? 126 VAL   A N   1 
ATOM   976  C  CA  . VAL   A 1 126 ? 15.13286  24.83409  18.32646  1.000 37.17457 ? 126 VAL   A CA  1 
ATOM   977  C  C   . VAL   A 1 126 ? 15.75647  25.17799  19.67238  1.000 35.16341 ? 126 VAL   A C   1 
ATOM   978  O  O   . VAL   A 1 126 ? 15.17921  24.89760  20.72966  1.000 32.71172 ? 126 VAL   A O   1 
ATOM   979  C  CB  . VAL   A 1 126 ? 15.76707  23.57265  17.70958  1.000 36.46536 ? 126 VAL   A CB  1 
ATOM   980  C  CG1 . VAL   A 1 126 ? 15.86011  22.45798  18.74231  1.000 33.30590 ? 126 VAL   A CG1 1 
ATOM   981  C  CG2 . VAL   A 1 126 ? 14.96001  23.11181  16.50868  1.000 35.68270 ? 126 VAL   A CG2 1 
ATOM   982  N  N   . GLU   A 1 127 ? 16.93240  25.81037  19.65625  1.000 35.27020 ? 127 GLU   A N   1 
ATOM   983  C  CA  . GLU   A 1 127 ? 17.54534  26.24888  20.90558  1.000 37.61843 ? 127 GLU   A CA  1 
ATOM   984  C  C   . GLU   A 1 127 ? 16.66840  27.26901  21.62161  1.000 36.53791 ? 127 GLU   A C   1 
ATOM   985  O  O   . GLU   A 1 127 ? 16.56180  27.25104  22.85323  1.000 34.08580 ? 127 GLU   A O   1 
ATOM   986  C  CB  . GLU   A 1 127 ? 18.93649  26.82492  20.63905  1.000 39.34060 ? 127 GLU   A CB  1 
ATOM   987  C  CG  . GLU   A 1 127 ? 19.91340  25.81760  20.05327  1.000 40.18674 ? 127 GLU   A CG  1 
ATOM   988  C  CD  . GLU   A 1 127 ? 21.36340  26.20981  20.26670  1.000 43.90938 ? 127 GLU   A CD  1 
ATOM   989  O  OE1 . GLU   A 1 127 ? 21.61037  27.32633  20.77041  1.000 50.81262 ? 127 GLU   A OE1 1 
ATOM   990  O  OE2 . GLU   A 1 127 ? 22.25608  25.39654  19.93888  1.000 44.59158 ? 127 GLU   A OE2 1 
ATOM   991  N  N   . GLU   A 1 128 ? 16.02090  28.15940  20.86553  1.000 36.62980 ? 128 GLU   A N   1 
ATOM   992  C  CA  . GLU   A 1 128 ? 15.14298  29.15221  21.47732  1.000 36.40916 ? 128 GLU   A CA  1 
ATOM   993  C  C   . GLU   A 1 128 ? 13.95146  28.49085  22.15911  1.000 36.34750 ? 128 GLU   A C   1 
ATOM   994  O  O   . GLU   A 1 128 ? 13.58211  28.86098  23.28034  1.000 33.69759 ? 128 GLU   A O   1 
ATOM   995  C  CB  . GLU   A 1 128 ? 14.66460  30.15226  20.42457  1.000 37.71340 ? 128 GLU   A CB  1 
ATOM   996  C  CG  . GLU   A 1 128 ? 13.73654  31.22058  20.97731  1.000 40.27299 ? 128 GLU   A CG  1 
ATOM   997  C  CD  . GLU   A 1 128 ? 13.07850  32.04090  19.88815  1.000 45.41795 ? 128 GLU   A CD  1 
ATOM   998  O  OE1 . GLU   A 1 128 ? 13.39397  31.81083  18.70030  1.000 48.73001 ? 128 GLU   A OE1 1 
ATOM   999  O  OE2 . GLU   A 1 128 ? 12.24460  32.91073  20.21892  1.000 46.46619 ? 128 GLU   A OE2 1 
ATOM   1000 N  N   . VAL   A 1 129 ? 13.33566  27.50681  21.49843  1.000 34.07009 ? 129 VAL   A N   1 
ATOM   1001 C  CA  . VAL   A 1 129 ? 12.18798  26.82680  22.09394  1.000 34.24929 ? 129 VAL   A CA  1 
ATOM   1002 C  C   . VAL   A 1 129 ? 12.61539  26.02618  23.31788  1.000 34.24819 ? 129 VAL   A C   1 
ATOM   1003 O  O   . VAL   A 1 129 ? 11.91699  26.00442  24.33937  1.000 35.20120 ? 129 VAL   A O   1 
ATOM   1004 C  CB  . VAL   A 1 129 ? 11.49074  25.93316  21.05125  1.000 35.13375 ? 129 VAL   A CB  1 
ATOM   1005 C  CG1 . VAL   A 1 129 ? 10.38535  25.12533  21.70069  1.000 30.71565 ? 129 VAL   A CG1 1 
ATOM   1006 C  CG2 . VAL   A 1 129 ? 10.93132  26.77793  19.91238  1.000 35.83212 ? 129 VAL   A CG2 1 
ATOM   1007 N  N   . VAL   A 1 130 ? 13.76961  25.36136  23.23844  1.000 34.15636 ? 130 VAL   A N   1 
ATOM   1008 C  CA  . VAL   A 1 130 ? 14.24616  24.55327  24.35928  1.000 33.95090 ? 130 VAL   A CA  1 
ATOM   1009 C  C   . VAL   A 1 130 ? 14.51206  25.43050  25.57622  1.000 35.67085 ? 130 VAL   A C   1 
ATOM   1010 O  O   . VAL   A 1 130 ? 14.01646  25.16396  26.67838  1.000 34.66228 ? 130 VAL   A O   1 
ATOM   1011 C  CB  . VAL   A 1 130 ? 15.50235  23.76096  23.95707  1.000 33.29964 ? 130 VAL   A CB  1 
ATOM   1012 C  CG1 . VAL   A 1 130 ? 16.17970  23.20382  25.19014  1.000 33.26244 ? 130 VAL   A CG1 1 
ATOM   1013 C  CG2 . VAL   A 1 130 ? 15.13925  22.64211  22.99041  1.000 31.95897 ? 130 VAL   A CG2 1 
ATOM   1014 N  N   . HIS   A 1 131 ? 15.30881  26.48558  25.39820  1.000 35.93278 ? 131 HIS   A N   1 
ATOM   1015 C  CA  . HIS   A 1 131 ? 15.60713  27.37039  26.51578  1.000 36.73781 ? 131 HIS   A CA  1 
ATOM   1016 C  C   . HIS   A 1 131 ? 14.38454  28.15010  26.97907  1.000 37.64448 ? 131 HIS   A C   1 
ATOM   1017 O  O   . HIS   A 1 131 ? 14.33757  28.57298  28.13831  1.000 38.35910 ? 131 HIS   A O   1 
ATOM   1018 C  CB  . HIS   A 1 131 ? 16.73970  28.32461  26.13948  1.000 38.60174 ? 131 HIS   A CB  1 
ATOM   1019 C  CG  . HIS   A 1 131 ? 18.07927  27.66226  26.04872  1.000 39.55190 ? 131 HIS   A CG  1 
ATOM   1020 N  ND1 . HIS   A 1 131 ? 18.78733  27.26167  27.16134  1.000 40.05387 ? 131 HIS   A ND1 1 
ATOM   1021 C  CD2 . HIS   A 1 131 ? 18.83688  27.32434  24.97865  1.000 41.18586 ? 131 HIS   A CD2 1 
ATOM   1022 C  CE1 . HIS   A 1 131 ? 19.92452  26.70832  26.78096  1.000 42.25471 ? 131 HIS   A CE1 1 
ATOM   1023 N  NE2 . HIS   A 1 131 ? 19.97930  26.73415  25.46133  1.000 44.93139 ? 131 HIS   A NE2 1 
ATOM   1024 N  N   . GLY   A 1 132 ? 13.38730  28.32738  26.11380  1.000 36.51367 ? 132 GLY   A N   1 
ATOM   1025 C  CA  . GLY   A 1 132 ? 12.16501  28.98658  26.54358  1.000 36.30135 ? 132 GLY   A CA  1 
ATOM   1026 C  C   . GLY   A 1 132 ? 11.36432  28.15194  27.52684  1.000 38.89579 ? 132 GLY   A C   1 
ATOM   1027 O  O   . GLY   A 1 132 ? 10.96242  28.63566  28.58977  1.000 37.57987 ? 132 GLY   A O   1 
ATOM   1028 N  N   . PHE   A 1 133 ? 11.11770  26.88377  27.18527  1.000 37.24586 ? 133 PHE   A N   1 
ATOM   1029 C  CA  . PHE   A 1 133 ? 10.37530  26.01650  28.09273  1.000 36.76127 ? 133 PHE   A CA  1 
ATOM   1030 C  C   . PHE   A 1 133 ? 11.19030  25.67346  29.33361  1.000 38.23330 ? 133 PHE   A C   1 
ATOM   1031 O  O   . PHE   A 1 133 ? 10.61501  25.36907  30.38344  1.000 36.54481 ? 133 PHE   A O   1 
ATOM   1032 C  CB  . PHE   A 1 133 ? 9.93161   24.74286  27.37096  1.000 37.34531 ? 133 PHE   A CB  1 
ATOM   1033 C  CG  . PHE   A 1 133 ? 8.76704   24.94694  26.44195  1.000 37.04467 ? 133 PHE   A CG  1 
ATOM   1034 C  CD1 . PHE   A 1 133 ? 7.48958   25.13165  26.94536  1.000 39.49139 ? 133 PHE   A CD1 1 
ATOM   1035 C  CD2 . PHE   A 1 133 ? 8.94703   24.94650  25.06755  1.000 37.09104 ? 133 PHE   A CD2 1 
ATOM   1036 C  CE1 . PHE   A 1 133 ? 6.41482   25.31903  26.09784  1.000 40.30123 ? 133 PHE   A CE1 1 
ATOM   1037 C  CE2 . PHE   A 1 133 ? 7.87426   25.13351  24.21269  1.000 35.42315 ? 133 PHE   A CE2 1 
ATOM   1038 C  CZ  . PHE   A 1 133 ? 6.60678   25.31917  24.72930  1.000 37.29144 ? 133 PHE   A CZ  1 
ATOM   1039 N  N   . LEU   A 1 134 ? 12.52148  25.71573  29.23896  1.000 38.11841 ? 134 LEU   A N   1 
ATOM   1040 C  CA  . LEU   A 1 134 ? 13.34311  25.55151  30.43412  1.000 37.75920 ? 134 LEU   A CA  1 
ATOM   1041 C  C   . LEU   A 1 134 ? 13.22900  26.76419  31.34904  1.000 41.10522 ? 134 LEU   A C   1 
ATOM   1042 O  O   . LEU   A 1 134 ? 13.16729  26.61609  32.57528  1.000 43.56758 ? 134 LEU   A O   1 
ATOM   1043 C  CB  . LEU   A 1 134 ? 14.80102  25.30490  30.04916  1.000 37.76057 ? 134 LEU   A CB  1 
ATOM   1044 C  CG  . LEU   A 1 134 ? 15.20750  23.84101  29.87124  1.000 36.28991 ? 134 LEU   A CG  1 
ATOM   1045 C  CD1 . LEU   A 1 134 ? 16.69027  23.72538  29.55466  1.000 35.44964 ? 134 LEU   A CD1 1 
ATOM   1046 C  CD2 . LEU   A 1 134 ? 14.86307  23.03705  31.11431  1.000 36.03461 ? 134 LEU   A CD2 1 
ATOM   1047 N  N   . ASP   A 1 135 ? 13.21333  27.97113  30.77102  1.000 39.44981 ? 135 ASP   A N   1 
ATOM   1048 C  CA  . ASP   A 1 135 ? 12.96552  29.17765  31.55612  1.000 41.51693 ? 135 ASP   A CA  1 
ATOM   1049 C  C   . ASP   A 1 135 ? 11.71337  29.02016  32.40643  1.000 43.44285 ? 135 ASP   A C   1 
ATOM   1050 O  O   . ASP   A 1 135 ? 11.73714  29.24090  33.62205  1.000 43.73960 ? 135 ASP   A O   1 
ATOM   1051 C  CB  . ASP   A 1 135 ? 12.82064  30.39535  30.63692  1.000 41.08320 ? 135 ASP   A CB  1 
ATOM   1052 C  CG  . ASP   A 1 135 ? 14.14241  30.86360  30.06113  1.000 41.46540 ? 135 ASP   A CG  1 
ATOM   1053 O  OD1 . ASP   A 1 135 ? 15.20038  30.49584  30.61177  1.000 43.34852 ? 135 ASP   A OD1 1 
ATOM   1054 O  OD2 . ASP   A 1 135 ? 14.11727  31.61150  29.06120  1.000 41.68164 ? 135 ASP   A OD2 1 
ATOM   1055 N  N   . GLU   A 1 136 ? 10.61083  28.61276  31.77429  1.000 41.99498 ? 136 GLU   A N   1 
ATOM   1056 C  CA  . GLU   A 1 136 ? 9.33623   28.50894  32.47309  1.000 43.74577 ? 136 GLU   A CA  1 
ATOM   1057 C  C   . GLU   A 1 136 ? 9.37248   27.42590  33.54348  1.000 44.61606 ? 136 GLU   A C   1 
ATOM   1058 O  O   . GLU   A 1 136 ? 8.83981   27.61642  34.64279  1.000 44.76578 ? 136 GLU   A O   1 
ATOM   1059 C  CB  . GLU   A 1 136 ? 8.22392   28.23584  31.46456  1.000 45.38211 ? 136 GLU   A CB  1 
ATOM   1060 C  CG  . GLU   A 1 136 ? 6.82697   28.30928  32.03517  1.000 48.14646 ? 136 GLU   A CG  1 
ATOM   1061 C  CD  . GLU   A 1 136 ? 5.76822   28.27753  30.95381  1.000 50.92892 ? 136 GLU   A CD  1 
ATOM   1062 O  OE1 . GLU   A 1 136 ? 6.12975   28.10062  29.77045  1.000 51.13693 ? 136 GLU   A OE1 1 
ATOM   1063 O  OE2 . GLU   A 1 136 ? 4.57558   28.43286  31.28690  1.000 53.49653 ? 136 GLU   A OE2 1 
ATOM   1064 N  N   . MET   A 1 137 ? 9.99919   26.28532  33.24683  1.000 42.54838 ? 137 MET   A N   1 
ATOM   1065 C  CA  . MET   A 1 137 ? 10.03271  25.19365  34.21604  1.000 44.11413 ? 137 MET   A CA  1 
ATOM   1066 C  C   . MET   A 1 137 ? 10.90732  25.54534  35.41286  1.000 44.95762 ? 137 MET   A C   1 
ATOM   1067 O  O   . MET   A 1 137 ? 10.51048  25.33941  36.56559  1.000 45.17822 ? 137 MET   A O   1 
ATOM   1068 C  CB  . MET   A 1 137 ? 10.52643  23.90615  33.55425  1.000 42.02192 ? 137 MET   A CB  1 
ATOM   1069 C  CG  . MET   A 1 137 ? 10.50415  22.70143  34.48640  1.000 42.62317 ? 137 MET   A CG  1 
ATOM   1070 S  SD  . MET   A 1 137 ? 11.08593  21.17162  33.72475  1.000 36.21506 ? 137 MET   A SD  1 
ATOM   1071 C  CE  . MET   A 1 137 ? 12.85504  21.44493  33.69800  1.000 39.63115 ? 137 MET   A CE  1 
ATOM   1072 N  N   . LEU   A 1 138 ? 12.10652  26.07503  35.15870  1.000 44.96490 ? 138 LEU   A N   1 
ATOM   1073 C  CA  . LEU   A 1 138 ? 13.01705  26.39288  36.25433  1.000 45.38980 ? 138 LEU   A CA  1 
ATOM   1074 C  C   . LEU   A 1 138 ? 12.50058  27.56145  37.08525  1.000 47.71393 ? 138 LEU   A C   1 
ATOM   1075 O  O   . LEU   A 1 138 ? 12.68686  27.58994  38.30739  1.000 47.72248 ? 138 LEU   A O   1 
ATOM   1076 C  CB  . LEU   A 1 138 ? 14.41289  26.69391  35.70858  1.000 44.97869 ? 138 LEU   A CB  1 
ATOM   1077 C  CG  . LEU   A 1 138 ? 15.07436  25.57217  34.90343  1.000 44.03847 ? 138 LEU   A CG  1 
ATOM   1078 C  CD1 . LEU   A 1 138 ? 16.50959  25.93635  34.54686  1.000 42.66747 ? 138 LEU   A CD1 1 
ATOM   1079 C  CD2 . LEU   A 1 138 ? 15.01540  24.25042  35.65682  1.000 43.64855 ? 138 LEU   A CD2 1 
ATOM   1080 N  N   . ALA   A 1 139 ? 11.85047  28.53598  36.44343  1.000 46.80221 ? 139 ALA   A N   1 
ATOM   1081 C  CA  . ALA   A 1 139 ? 11.27843  29.65072  37.19169  1.000 47.48530 ? 139 ALA   A CA  1 
ATOM   1082 C  C   . ALA   A 1 139 ? 10.13471  29.19436  38.08804  1.000 48.47139 ? 139 ALA   A C   1 
ATOM   1083 O  O   . ALA   A 1 139 ? 9.92545   29.76362  39.16662  1.000 49.84882 ? 139 ALA   A O   1 
ATOM   1084 C  CB  . ALA   A 1 139 ? 10.80259  30.74328  36.23367  1.000 47.29514 ? 139 ALA   A CB  1 
ATOM   1085 N  N   . ALA   A 1 140 ? 9.38999   28.16987  37.66554  1.000 47.82753 ? 140 ALA   A N   1 
ATOM   1086 C  CA  . ALA   A 1 140 ? 8.29920   27.64572  38.47921  1.000 48.76248 ? 140 ALA   A CA  1 
ATOM   1087 C  C   . ALA   A 1 140 ? 8.80525   26.81518  39.65257  1.000 49.16733 ? 140 ALA   A C   1 
ATOM   1088 O  O   . ALA   A 1 140 ? 8.13361   26.73793  40.68671  1.000 49.61452 ? 140 ALA   A O   1 
ATOM   1089 C  CB  . ALA   A 1 140 ? 7.35800   26.80922  37.61375  1.000 47.94343 ? 140 ALA   A CB  1 
ATOM   1090 N  N   . GLY   A 1 141 ? 9.97775   26.19985  39.51922  1.000 49.08590 ? 141 GLY   A N   1 
ATOM   1091 C  CA  . GLY   A 1 141 ? 10.56947  25.44470  40.59759  1.000 50.14652 ? 141 GLY   A CA  1 
ATOM   1092 C  C   . GLY   A 1 141 ? 10.08668  24.00894  40.66437  1.000 49.19316 ? 141 GLY   A C   1 
ATOM   1093 O  O   . GLY   A 1 141 ? 9.03779   23.65206  40.11770  1.000 48.83121 ? 141 GLY   A O   1 
ATOM   1094 N  N   . PRO   A 1 142 ? 10.84868  23.15827  41.34765  1.000 50.44264 ? 142 PRO   A N   1 
ATOM   1095 C  CA  . PRO   A 1 142 ? 10.45648  21.75347  41.49750  1.000 49.07367 ? 142 PRO   A CA  1 
ATOM   1096 C  C   . PRO   A 1 142 ? 9.33016   21.60307  42.51220  1.000 50.69885 ? 142 PRO   A C   1 
ATOM   1097 O  O   . PRO   A 1 142 ? 9.09145   22.48048  43.34418  1.000 52.84973 ? 142 PRO   A O   1 
ATOM   1098 C  CB  . PRO   A 1 142 ? 11.74704  21.08998  41.99381  1.000 48.03742 ? 142 PRO   A CB  1 
ATOM   1099 C  CG  . PRO   A 1 142 ? 12.42911  22.16218  42.76373  1.000 48.56113 ? 142 PRO   A CG  1 
ATOM   1100 C  CD  . PRO   A 1 142 ? 12.10536  23.46124  42.05726  1.000 50.34470 ? 142 PRO   A CD  1 
ATOM   1101 N  N   . THR   A 1 143 ? 8.62727   20.46913  42.44103  1.000 49.92163 ? 143 THR   A N   1 
ATOM   1102 C  CA  . THR   A 1 143 ? 8.88098   19.36683  41.51082  1.000 48.35821 ? 143 THR   A CA  1 
ATOM   1103 C  C   . THR   A 1 143 ? 8.02676   19.49479  40.24839  1.000 48.80447 ? 143 THR   A C   1 
ATOM   1104 O  O   . THR   A 1 143 ? 6.87361   19.91699  40.31641  1.000 48.77707 ? 143 THR   A O   1 
ATOM   1105 C  CB  . THR   A 1 143 ? 8.61231   18.00267  42.20278  1.000 48.78397 ? 143 THR   A CB  1 
ATOM   1106 O  OG1 . THR   A 1 143 ? 9.72308   17.66475  43.04377  1.000 48.67050 ? 143 THR   A OG1 1 
ATOM   1107 C  CG2 . THR   A 1 143 ? 8.38249   16.88337  41.19089  1.000 48.25557 ? 143 THR   A CG2 1 
ATOM   1108 N  N   . ALA   A 1 144 ? 8.59563   19.13845  39.09633  1.000 46.13630 ? 144 ALA   A N   1 
ATOM   1109 C  CA  . ALA   A 1 144 ? 7.90747   19.24669  37.81913  1.000 44.31586 ? 144 ALA   A CA  1 
ATOM   1110 C  C   . ALA   A 1 144 ? 7.83179   17.89242  37.12454  1.000 42.97084 ? 144 ALA   A C   1 
ATOM   1111 O  O   . ALA   A 1 144 ? 8.65288   17.00094  37.36441  1.000 41.82382 ? 144 ALA   A O   1 
ATOM   1112 C  CB  . ALA   A 1 144 ? 8.60601   20.25637  36.89952  1.000 43.98876 ? 144 ALA   A CB  1 
ATOM   1113 N  N   . ASP   A 1 145 ? 6.82493   17.75042  36.26341  1.000 41.80376 ? 145 ASP   A N   1 
ATOM   1114 C  CA  . ASP   A 1 145 ? 6.71594   16.61735  35.34872  1.000 39.90386 ? 145 ASP   A CA  1 
ATOM   1115 C  C   . ASP   A 1 145 ? 7.46067   16.98516  34.07078  1.000 39.05308 ? 145 ASP   A C   1 
ATOM   1116 O  O   . ASP   A 1 145 ? 7.00408   17.83828  33.30327  1.000 38.11478 ? 145 ASP   A O   1 
ATOM   1117 C  CB  . ASP   A 1 145 ? 5.25004   16.28774  35.07005  1.000 39.41786 ? 145 ASP   A CB  1 
ATOM   1118 C  CG  . ASP   A 1 145 ? 5.06617   15.28582  33.93504  1.000 38.86518 ? 145 ASP   A CG  1 
ATOM   1119 O  OD1 . ASP   A 1 145 ? 6.02380   14.56627  33.58277  1.000 38.58290 ? 145 ASP   A OD1 1 
ATOM   1120 O  OD2 . ASP   A 1 145 ? 3.94507   15.22328  33.38986  1.000 39.24515 ? 145 ASP   A OD2 1 
ATOM   1121 N  N   . LEU   A 1 146 ? 8.60665   16.33869  33.84259  1.000 37.65796 ? 146 LEU   A N   1 
ATOM   1122 C  CA  . LEU   A 1 146 ? 9.44288   16.68900  32.69885  1.000 37.70481 ? 146 LEU   A CA  1 
ATOM   1123 C  C   . LEU   A 1 146 ? 8.71987   16.47436  31.37306  1.000 35.95538 ? 146 LEU   A C   1 
ATOM   1124 O  O   . LEU   A 1 146 ? 9.02783   17.14981  30.38345  1.000 33.51711 ? 146 LEU   A O   1 
ATOM   1125 C  CB  . LEU   A 1 146 ? 10.74086  15.87904  32.73284  1.000 36.87375 ? 146 LEU   A CB  1 
ATOM   1126 C  CG  . LEU   A 1 146 ? 11.81689  16.27231  31.71832  1.000 35.44601 ? 146 LEU   A CG  1 
ATOM   1127 C  CD1 . LEU   A 1 146 ? 12.32000  17.68592  31.98506  1.000 35.66398 ? 146 LEU   A CD1 1 
ATOM   1128 C  CD2 . LEU   A 1 146 ? 12.96561  15.27984  31.72601  1.000 34.95204 ? 146 LEU   A CD2 1 
ATOM   1129 N  N   . VAL   A 1 147 ? 7.75429   15.55588  31.33010  1.000 36.77866 ? 147 VAL   A N   1 
ATOM   1130 C  CA  . VAL   A 1 147 ? 7.09269   15.23626  30.06694  1.000 35.84040 ? 147 VAL   A CA  1 
ATOM   1131 C  C   . VAL   A 1 147 ? 6.17700   16.37875  29.63793  1.000 36.39289 ? 147 VAL   A C   1 
ATOM   1132 O  O   . VAL   A 1 147 ? 6.35447   16.97274  28.56792  1.000 33.55156 ? 147 VAL   A O   1 
ATOM   1133 C  CB  . VAL   A 1 147 ? 6.32531   13.90684  30.17677  1.000 37.82509 ? 147 VAL   A CB  1 
ATOM   1134 C  CG1 . VAL   A 1 147 ? 5.52788   13.65379  28.90800  1.000 36.55759 ? 147 VAL   A CG1 1 
ATOM   1135 C  CG2 . VAL   A 1 147 ? 7.28904   12.75511  30.43398  1.000 37.01887 ? 147 VAL   A CG2 1 
ATOM   1136 N  N   . SER   A 1 148 ? 5.18568   16.70634  30.46889  1.000 36.99282 ? 148 SER   A N   1 
ATOM   1137 C  CA  . SER   A 1 148 ? 4.21072   17.72287  30.09081  1.000 37.94466 ? 148 SER   A CA  1 
ATOM   1138 C  C   . SER   A 1 148 ? 4.78104   19.13404  30.14350  1.000 38.44620 ? 148 SER   A C   1 
ATOM   1139 O  O   . SER   A 1 148 ? 4.19857   20.04452  29.54518  1.000 37.59957 ? 148 SER   A O   1 
ATOM   1140 C  CB  . SER   A 1 148 ? 2.97826   17.63186  30.99195  1.000 40.44635 ? 148 SER   A CB  1 
ATOM   1141 O  OG  . SER   A 1 148 ? 3.31780   17.87345  32.34668  1.000 39.25593 ? 148 SER   A OG  1 
ATOM   1142 N  N   . GLN   A 1 149 ? 5.89953   19.34041  30.83702  1.000 36.17017 ? 149 GLN   A N   1 
ATOM   1143 C  CA  . GLN   A 1 149 ? 6.45410   20.67657  31.00110  1.000 39.16296 ? 149 GLN   A CA  1 
ATOM   1144 C  C   . GLN   A 1 149 ? 7.65140   20.95383  30.10323  1.000 36.77807 ? 149 GLN   A C   1 
ATOM   1145 O  O   . GLN   A 1 149 ? 8.07316   22.11020  30.00893  1.000 36.68700 ? 149 GLN   A O   1 
ATOM   1146 C  CB  . GLN   A 1 149 ? 6.85891   20.91178  32.46343  1.000 39.63056 ? 149 GLN   A CB  1 
ATOM   1147 C  CG  . GLN   A 1 149 ? 5.71807   20.75449  33.45208  1.000 41.02932 ? 149 GLN   A CG  1 
ATOM   1148 C  CD  . GLN   A 1 149 ? 4.49660   21.55869  33.05948  1.000 43.89221 ? 149 GLN   A CD  1 
ATOM   1149 O  OE1 . GLN   A 1 149 ? 3.42761   21.00169  32.80554  1.000 44.92745 ? 149 GLN   A OE1 1 
ATOM   1150 N  NE2 . GLN   A 1 149 ? 4.64725   22.87720  33.00958  1.000 47.34624 ? 149 GLN   A NE2 1 
ATOM   1151 N  N   . PHE   A 1 150 ? 8.20784   19.93839  29.44581  1.000 33.15822 ? 150 PHE   A N   1 
ATOM   1152 C  CA  . PHE   A 1 150 ? 9.41128   20.14820  28.65224  1.000 32.89857 ? 150 PHE   A CA  1 
ATOM   1153 C  C   . PHE   A 1 150 ? 9.53197   19.14436  27.51176  1.000 33.14253 ? 150 PHE   A C   1 
ATOM   1154 O  O   . PHE   A 1 150 ? 9.76328   19.53344  26.36209  1.000 30.57906 ? 150 PHE   A O   1 
ATOM   1155 C  CB  . PHE   A 1 150 ? 10.64906  20.07557  29.54848  1.000 32.56844 ? 150 PHE   A CB  1 
ATOM   1156 C  CG  . PHE   A 1 150 ? 11.94534  20.18955  28.80124  1.000 32.75476 ? 150 PHE   A CG  1 
ATOM   1157 C  CD1 . PHE   A 1 150 ? 12.38204  21.41792  28.32970  1.000 32.16150 ? 150 PHE   A CD1 1 
ATOM   1158 C  CD2 . PHE   A 1 150 ? 12.73073  19.06930  28.57473  1.000 28.95728 ? 150 PHE   A CD2 1 
ATOM   1159 C  CE1 . PHE   A 1 150 ? 13.57601  21.52913  27.64112  1.000 30.87068 ? 150 PHE   A CE1 1 
ATOM   1160 C  CE2 . PHE   A 1 150 ? 13.92691  19.17138  27.88770  1.000 30.26448 ? 150 PHE   A CE2 1 
ATOM   1161 C  CZ  . PHE   A 1 150 ? 14.35069  20.40394  27.41921  1.000 32.43173 ? 150 PHE   A CZ  1 
ATOM   1162 N  N   . ALA   A 1 151 ? 9.37642   17.85307  27.81963  1.000 30.98517 ? 151 ALA   A N   1 
ATOM   1163 C  CA  . ALA   A 1 151 ? 9.64791   16.81648  26.82709  1.000 32.90349 ? 151 ALA   A CA  1 
ATOM   1164 C  C   . ALA   A 1 151 ? 8.65725   16.86624  25.67002  1.000 30.54247 ? 151 ALA   A C   1 
ATOM   1165 O  O   . ALA   A 1 151 ? 9.04332   16.67329  24.51371  1.000 29.24883 ? 151 ALA   A O   1 
ATOM   1166 C  CB  . ALA   A 1 151 ? 9.63225   15.43547  27.48350  1.000 31.26427 ? 151 ALA   A CB  1 
ATOM   1167 N  N   . LEU   A 1 152 ? 7.38311   17.11105  25.95549  1.000 31.06617 ? 152 LEU   A N   1 
ATOM   1168 C  CA  . LEU   A 1 152 ? 6.36353   17.15095  24.91188  1.000 32.27329 ? 152 LEU   A CA  1 
ATOM   1169 C  C   . LEU   A 1 152 ? 6.23444   18.52003  24.23974  1.000 32.40509 ? 152 LEU   A C   1 
ATOM   1170 O  O   . LEU   A 1 152 ? 6.16550   18.57854  23.00558  1.000 32.74630 ? 152 LEU   A O   1 
ATOM   1171 C  CB  . LEU   A 1 152 ? 5.00658   16.72054  25.47378  1.000 33.83756 ? 152 LEU   A CB  1 
ATOM   1172 C  CG  . LEU   A 1 152 ? 3.88175   16.62246  24.44152  1.000 35.57387 ? 152 LEU   A CG  1 
ATOM   1173 C  CD1 . LEU   A 1 152 ? 4.18752   15.52392  23.42746  1.000 34.20942 ? 152 LEU   A CD1 1 
ATOM   1174 C  CD2 . LEU   A 1 152 ? 2.53763   16.38457  25.11303  1.000 42.65320 ? 152 LEU   A CD2 1 
ATOM   1175 N  N   . PRO   A 1 153 ? 6.18295   19.63716  24.98214  1.000 32.68112 ? 153 PRO   A N   1 
ATOM   1176 C  CA  . PRO   A 1 153 ? 5.93801   20.92653  24.31027  1.000 33.86494 ? 153 PRO   A CA  1 
ATOM   1177 C  C   . PRO   A 1 153 ? 7.05130   21.35752  23.36942  1.000 32.29556 ? 153 PRO   A C   1 
ATOM   1178 O  O   . PRO   A 1 153 ? 6.76505   22.02270  22.36544  1.000 32.73796 ? 153 PRO   A O   1 
ATOM   1179 C  CB  . PRO   A 1 153 ? 5.78282   21.91383  25.47833  1.000 35.25311 ? 153 PRO   A CB  1 
ATOM   1180 C  CG  . PRO   A 1 153 ? 5.49134   21.07380  26.66689  1.000 34.19367 ? 153 PRO   A CG  1 
ATOM   1181 C  CD  . PRO   A 1 153 ? 6.24973   19.80916  26.44455  1.000 34.49272 ? 153 PRO   A CD  1 
ATOM   1182 N  N   . VAL   A 1 154 ? 8.30280   21.00870  23.65457  1.000 30.60392 ? 154 VAL   A N   1 
ATOM   1183 C  CA  . VAL   A 1 154 ? 9.42998   21.46331  22.84043  1.000 29.99208 ? 154 VAL   A CA  1 
ATOM   1184 C  C   . VAL   A 1 154 ? 9.30122   20.93611  21.41098  1.000 31.49662 ? 154 VAL   A C   1 
ATOM   1185 O  O   . VAL   A 1 154 ? 9.25093   21.74933  20.47464  1.000 29.92151 ? 154 VAL   A O   1 
ATOM   1186 C  CB  . VAL   A 1 154 ? 10.77457  21.07453  23.48113  1.000 29.24124 ? 154 VAL   A CB  1 
ATOM   1187 C  CG1 . VAL   A 1 154 ? 11.88545  21.11536  22.45236  1.000 30.46226 ? 154 VAL   A CG1 1 
ATOM   1188 C  CG2 . VAL   A 1 154 ? 11.09364  21.99685  24.64275  1.000 31.26261 ? 154 VAL   A CG2 1 
ATOM   1189 N  N   . PRO   A 1 155 ? 9.22344   19.61757  21.17118  1.000 29.86552 ? 155 PRO   A N   1 
ATOM   1190 C  CA  . PRO   A 1 155 ? 9.06961   19.16435  19.78012  1.000 31.57809 ? 155 PRO   A CA  1 
ATOM   1191 C  C   . PRO   A 1 155 ? 7.70987   19.49487  19.20030  1.000 29.38336 ? 155 PRO   A C   1 
ATOM   1192 O  O   . PRO   A 1 155 ? 7.58574   19.61038  17.97582  1.000 28.33267 ? 155 PRO   A O   1 
ATOM   1193 C  CB  . PRO   A 1 155 ? 9.29157   17.64984  19.87486  1.000 28.20647 ? 155 PRO   A CB  1 
ATOM   1194 C  CG  . PRO   A 1 155 ? 8.83419   17.30480  21.23554  1.000 29.85133 ? 155 PRO   A CG  1 
ATOM   1195 C  CD  . PRO   A 1 155 ? 9.24265   18.47175  22.10022  1.000 30.41128 ? 155 PRO   A CD  1 
ATOM   1196 N  N   . SER   A 1 156 ? 6.68576   19.64127  20.04353  1.000 29.85001 ? 156 SER   A N   1 
ATOM   1197 C  CA  . SER   A 1 156 ? 5.37955   20.07959  19.56377  1.000 31.07003 ? 156 SER   A CA  1 
ATOM   1198 C  C   . SER   A 1 156 ? 5.47432   21.44498  18.89259  1.000 33.18802 ? 156 SER   A C   1 
ATOM   1199 O  O   . SER   A 1 156 ? 5.03053   21.62512  17.75254  1.000 29.76386 ? 156 SER   A O   1 
ATOM   1200 C  CB  . SER   A 1 156 ? 4.38879   20.12162  20.72626  1.000 33.73438 ? 156 SER   A CB  1 
ATOM   1201 O  OG  . SER   A 1 156 ? 3.11024   20.54879  20.28925  1.000 36.59125 ? 156 SER   A OG  1 
ATOM   1202 N  N   . MET   A 1 157 ? 6.05981   22.42170  19.58858  1.000 33.68460 ? 157 MET   A N   1 
ATOM   1203 C  CA  . MET   A 1 157 ? 6.18667   23.75857  19.01925  1.000 31.93566 ? 157 MET   A CA  1 
ATOM   1204 C  C   . MET   A 1 157 ? 7.04465   23.74601  17.75950  1.000 32.51546 ? 157 MET   A C   1 
ATOM   1205 O  O   . MET   A 1 157 ? 6.73955   24.44174  16.78396  1.000 31.52850 ? 157 MET   A O   1 
ATOM   1206 C  CB  . MET   A 1 157 ? 6.76815   24.71540  20.05879  1.000 33.61476 ? 157 MET   A CB  1 
ATOM   1207 C  CG  . MET   A 1 157 ? 6.95296   26.13547  19.54234  1.000 35.71808 ? 157 MET   A CG  1 
ATOM   1208 S  SD  . MET   A 1 157 ? 7.20129   27.32701  20.86716  1.000 40.63678 ? 157 MET   A SD  1 
ATOM   1209 C  CE  . MET   A 1 157 ? 5.65654   27.16235  21.73994  1.000 40.47832 ? 157 MET   A CE  1 
ATOM   1210 N  N   . VAL   A 1 158 ? 8.11408   22.95012  17.75593  1.000 29.83116 ? 158 VAL   A N   1 
ATOM   1211 C  CA  . VAL   A 1 158 ? 9.00254   22.90194  16.59761  1.000 33.17919 ? 158 VAL   A CA  1 
ATOM   1212 C  C   . VAL   A 1 158 ? 8.27047   22.34623  15.37932  1.000 33.05154 ? 158 VAL   A C   1 
ATOM   1213 O  O   . VAL   A 1 158 ? 8.33240   22.91936  14.28499  1.000 31.95318 ? 158 VAL   A O   1 
ATOM   1214 C  CB  . VAL   A 1 158 ? 10.26414  22.08379  16.92361  1.000 32.19236 ? 158 VAL   A CB  1 
ATOM   1215 C  CG1 . VAL   A 1 158 ? 11.05070  21.79446  15.65517  1.000 32.01721 ? 158 VAL   A CG1 1 
ATOM   1216 C  CG2 . VAL   A 1 158 ? 11.12716  22.83072  17.92862  1.000 33.30403 ? 158 VAL   A CG2 1 
ATOM   1217 N  N   . ILE   A 1 159 ? 7.55890   21.22700  15.54946  1.000 31.17722 ? 159 ILE   A N   1 
ATOM   1218 C  CA  . ILE   A 1 159 ? 6.91223   20.59266  14.40093  1.000 30.99421 ? 159 ILE   A CA  1 
ATOM   1219 C  C   . ILE   A 1 159 ? 5.74162   21.43419  13.90382  1.000 31.94733 ? 159 ILE   A C   1 
ATOM   1220 O  O   . ILE   A 1 159 ? 5.44969   21.45313  12.70069  1.000 29.15598 ? 159 ILE   A O   1 
ATOM   1221 C  CB  . ILE   A 1 159 ? 6.47366   19.15151  14.74163  1.000 29.58210 ? 159 ILE   A CB  1 
ATOM   1222 C  CG1 . ILE   A 1 159 ? 6.03550   18.40899  13.47546  1.000 30.27226 ? 159 ILE   A CG1 1 
ATOM   1223 C  CG2 . ILE   A 1 159 ? 5.33817   19.13692  15.74731  1.000 30.17510 ? 159 ILE   A CG2 1 
ATOM   1224 C  CD1 . ILE   A 1 159 ? 7.14380   18.20832  12.46702  1.000 29.67919 ? 159 ILE   A CD1 1 
ATOM   1225 N  N   . CYS   A 1 160 ? 5.05947   22.14739  14.80550  1.000 30.02852 ? 160 CYS   A N   1 
ATOM   1226 C  CA  . CYS   A 1 160 ? 3.96263   23.01382  14.38588  1.000 33.03497 ? 160 CYS   A CA  1 
ATOM   1227 C  C   . CYS   A 1 160 ? 4.45798   24.12637  13.47014  1.000 34.01478 ? 160 CYS   A C   1 
ATOM   1228 O  O   . CYS   A 1 160 ? 3.82683   24.42778  12.45067  1.000 32.45819 ? 160 CYS   A O   1 
ATOM   1229 C  CB  . CYS   A 1 160 ? 3.25057   23.59789  15.60746  1.000 34.09787 ? 160 CYS   A CB  1 
ATOM   1230 S  SG  . CYS   A 1 160 ? 2.26641   22.40045  16.54259  1.000 36.11036 ? 160 CYS   A SG  1 
ATOM   1231 N  N   A ARG   A 1 161 ? 5.59156   24.74001  13.81890  0.500 34.26686 ? 161 ARG   A N   1 
ATOM   1232 N  N   B ARG   A 1 161 ? 5.58375   24.76178  13.82060  0.500 34.32372 ? 161 ARG   A N   1 
ATOM   1233 C  CA  A ARG   A 1 161 ? 6.15287   25.78802  12.97575  0.500 36.22753 ? 161 ARG   A CA  1 
ATOM   1234 C  CA  B ARG   A 1 161 ? 6.14880   25.79367  12.95215  0.500 36.48399 ? 161 ARG   A CA  1 
ATOM   1235 C  C   A ARG   A 1 161 ? 6.61447   25.22385  11.63663  0.500 35.90637 ? 161 ARG   A C   1 
ATOM   1236 C  C   B ARG   A 1 161 ? 6.57572   25.20501  11.61567  0.500 35.86276 ? 161 ARG   A C   1 
ATOM   1237 O  O   A ARG   A 1 161 ? 6.50924   25.89407  10.60314  0.500 34.58150 ? 161 ARG   A O   1 
ATOM   1238 O  O   B ARG   A 1 161 ? 6.40656   25.83656  10.56532  0.500 34.55512 ? 161 ARG   A O   1 
ATOM   1239 C  CB  A ARG   A 1 161 ? 7.30204   26.48524  13.70553  0.500 34.81448 ? 161 ARG   A CB  1 
ATOM   1240 C  CB  B ARG   A 1 161 ? 7.32796   26.48853  13.64526  0.500 34.85310 ? 161 ARG   A CB  1 
ATOM   1241 C  CG  A ARG   A 1 161 ? 7.84953   27.69316  12.96753  0.500 38.97936 ? 161 ARG   A CG  1 
ATOM   1242 C  CG  B ARG   A 1 161 ? 8.35804   27.12477  12.70642  0.500 38.83932 ? 161 ARG   A CG  1 
ATOM   1243 C  CD  A ARG   A 1 161 ? 6.73607   28.67809  12.63197  0.500 39.72244 ? 161 ARG   A CD  1 
ATOM   1244 C  CD  B ARG   A 1 161 ? 8.70656   28.54239  13.09835  0.500 39.92922 ? 161 ARG   A CD  1 
ATOM   1245 N  NE  A ARG   A 1 161 ? 6.23860   29.38914  13.80814  0.500 40.82632 ? 161 ARG   A NE  1 
ATOM   1246 N  NE  B ARG   A 1 161 ? 7.86286   29.54337  12.48651  0.500 43.67716 ? 161 ARG   A NE  1 
ATOM   1247 C  CZ  A ARG   A 1 161 ? 5.21916   30.24305  13.78825  0.500 42.49562 ? 161 ARG   A CZ  1 
ATOM   1248 C  CZ  B ARG   A 1 161 ? 8.20484   30.81645  12.35967  0.500 42.51475 ? 161 ARG   A CZ  1 
ATOM   1249 N  NH1 A ARG   A 1 161 ? 4.58094   30.49288  12.65389  0.500 41.98351 ? 161 ARG   A NH1 1 
ATOM   1250 N  NH1 B ARG   A 1 161 ? 9.38028   31.26383  12.79877  0.500 43.67265 ? 161 ARG   A NH1 1 
ATOM   1251 N  NH2 A ARG   A 1 161 ? 4.83586   30.84995  14.90161  0.500 43.31304 ? 161 ARG   A NH2 1 
ATOM   1252 N  NH2 B ARG   A 1 161 ? 7.33993   31.64011  11.79239  0.500 43.01753 ? 161 ARG   A NH2 1 
ATOM   1253 N  N   . LEU   A 1 162 ? 7.10772   23.98172  11.63135  1.000 33.57613 ? 162 LEU   A N   1 
ATOM   1254 C  CA  . LEU   A 1 162 ? 7.49477   23.34211  10.37891  1.000 33.15771 ? 162 LEU   A CA  1 
ATOM   1255 C  C   . LEU   A 1 162 ? 6.27182   23.04062  9.52260   1.000 33.54335 ? 162 LEU   A C   1 
ATOM   1256 O  O   . LEU   A 1 162 ? 6.28440   23.26848  8.30735   1.000 31.12872 ? 162 LEU   A O   1 
ATOM   1257 C  CB  . LEU   A 1 162 ? 8.28818   22.06249  10.66199  1.000 33.50734 ? 162 LEU   A CB  1 
ATOM   1258 C  CG  . LEU   A 1 162 ? 8.87694   21.28476  9.47840   1.000 33.31911 ? 162 LEU   A CG  1 
ATOM   1259 C  CD1 . LEU   A 1 162 ? 10.19255  20.64382  9.88556   1.000 32.79198 ? 162 LEU   A CD1 1 
ATOM   1260 C  CD2 . LEU   A 1 162 ? 7.91465   20.22298  8.95576   1.000 31.22386 ? 162 LEU   A CD2 1 
ATOM   1261 N  N   . LEU   A 1 163 ? 5.20027   22.54262  10.14213  1.000 30.93138 ? 163 LEU   A N   1 
ATOM   1262 C  CA  . LEU   A 1 163 ? 4.00724   22.15558  9.40169   1.000 31.27038 ? 163 LEU   A CA  1 
ATOM   1263 C  C   . LEU   A 1 163 ? 3.11933   23.33559  9.03984   1.000 34.05239 ? 163 LEU   A C   1 
ATOM   1264 O  O   . LEU   A 1 163 ? 2.34260   23.23449  8.08518   1.000 29.66045 ? 163 LEU   A O   1 
ATOM   1265 C  CB  . LEU   A 1 163 ? 3.19091   21.14470  10.20889  1.000 31.30881 ? 163 LEU   A CB  1 
ATOM   1266 C  CG  . LEU   A 1 163 ? 3.83467   19.77290  10.40897  1.000 29.36117 ? 163 LEU   A CG  1 
ATOM   1267 C  CD1 . LEU   A 1 163 ? 2.93791   18.88398  11.25434  1.000 28.86125 ? 163 LEU   A CD1 1 
ATOM   1268 C  CD2 . LEU   A 1 163 ? 4.13090   19.13448  9.06283   1.000 29.41296 ? 163 LEU   A CD2 1 
ATOM   1269 N  N   . GLY   A 1 164 ? 3.21989   24.44821  9.76232   1.000 31.12738 ? 164 GLY   A N   1 
ATOM   1270 C  CA  . GLY   A 1 164 ? 2.23791   25.50093  9.61853   1.000 33.05684 ? 164 GLY   A CA  1 
ATOM   1271 C  C   . GLY   A 1 164 ? 0.98657   25.28066  10.43227  1.000 33.47447 ? 164 GLY   A C   1 
ATOM   1272 O  O   . GLY   A 1 164 ? -0.06130  25.84590  10.10692  1.000 31.84280 ? 164 GLY   A O   1 
ATOM   1273 N  N   . VAL   A 1 165 ? 1.05904   24.45297  11.47010  1.000 30.40432 ? 165 VAL   A N   1 
ATOM   1274 C  CA  . VAL   A 1 165 ? -0.05559  24.22432  12.38406  1.000 33.00893 ? 165 VAL   A CA  1 
ATOM   1275 C  C   . VAL   A 1 165 ? 0.00345   25.28119  13.48023  1.000 33.29105 ? 165 VAL   A C   1 
ATOM   1276 O  O   . VAL   A 1 165 ? 1.05631   25.45509  14.10945  1.000 31.81423 ? 165 VAL   A O   1 
ATOM   1277 C  CB  . VAL   A 1 165 ? -0.01147  22.80445  12.97038  1.000 31.47756 ? 165 VAL   A CB  1 
ATOM   1278 C  CG1 . VAL   A 1 165 ? -0.98915  22.67564  14.11785  1.000 32.92564 ? 165 VAL   A CG1 1 
ATOM   1279 C  CG2 . VAL   A 1 165 ? -0.31223  21.77260  11.88808  1.000 32.46619 ? 165 VAL   A CG2 1 
ATOM   1280 N  N   . PRO   A 1 166 ? -1.08612  26.00480  13.73975  1.000 33.44790 ? 166 PRO   A N   1 
ATOM   1281 C  CA  . PRO   A 1 166 ? -1.03693  27.09141  14.73003  1.000 36.22441 ? 166 PRO   A CA  1 
ATOM   1282 C  C   . PRO   A 1 166 ? -0.87249  26.53234  16.13560  1.000 35.78755 ? 166 PRO   A C   1 
ATOM   1283 O  O   . PRO   A 1 166 ? -1.65493  25.68815  16.57545  1.000 35.13674 ? 166 PRO   A O   1 
ATOM   1284 C  CB  . PRO   A 1 166 ? -2.39064  27.79693  14.55965  1.000 36.02566 ? 166 PRO   A CB  1 
ATOM   1285 C  CG  . PRO   A 1 166 ? -2.96910  27.26652  13.26384  1.000 35.77688 ? 166 PRO   A CG  1 
ATOM   1286 C  CD  . PRO   A 1 166 ? -2.41214  25.88628  13.11421  1.000 35.08614 ? 166 PRO   A CD  1 
ATOM   1287 N  N   . TYR   A 1 167 ? 0.15674   27.00619  16.84271  1.000 37.07030 ? 167 TYR   A N   1 
ATOM   1288 C  CA  . TYR   A 1 167 ? 0.41128   26.48280  18.18034  1.000 38.96177 ? 167 TYR   A CA  1 
ATOM   1289 C  C   . TYR   A 1 167 ? -0.66907  26.87849  19.17620  1.000 39.17304 ? 167 TYR   A C   1 
ATOM   1290 O  O   . TYR   A 1 167 ? -0.76780  26.25833  20.23962  1.000 40.02850 ? 167 TYR   A O   1 
ATOM   1291 C  CB  . TYR   A 1 167 ? 1.77177   26.94336  18.70378  1.000 38.95343 ? 167 TYR   A CB  1 
ATOM   1292 C  CG  . TYR   A 1 167 ? 2.21001   26.14653  19.90969  1.000 40.14008 ? 167 TYR   A CG  1 
ATOM   1293 C  CD1 . TYR   A 1 167 ? 2.70552   24.85932  19.76228  1.000 37.37669 ? 167 TYR   A CD1 1 
ATOM   1294 C  CD2 . TYR   A 1 167 ? 2.10745   26.66778  21.19516  1.000 40.81805 ? 167 TYR   A CD2 1 
ATOM   1295 C  CE1 . TYR   A 1 167 ? 3.09708   24.11417  20.85479  1.000 37.91101 ? 167 TYR   A CE1 1 
ATOM   1296 C  CE2 . TYR   A 1 167 ? 2.49692   25.92626  22.30113  1.000 39.75625 ? 167 TYR   A CE2 1 
ATOM   1297 C  CZ  . TYR   A 1 167 ? 2.99139   24.64823  22.12161  1.000 39.82926 ? 167 TYR   A CZ  1 
ATOM   1298 O  OH  . TYR   A 1 167 ? 3.38405   23.89586  23.20646  1.000 40.85775 ? 167 TYR   A OH  1 
ATOM   1299 N  N   . ALA   A 1 168 ? -1.48273  27.88769  18.85935  1.000 37.31938 ? 168 ALA   A N   1 
ATOM   1300 C  CA  . ALA   A 1 168 ? -2.55919  28.27607  19.76330  1.000 39.90537 ? 168 ALA   A CA  1 
ATOM   1301 C  C   . ALA   A 1 168 ? -3.55955  27.14815  19.98175  1.000 39.07175 ? 168 ALA   A C   1 
ATOM   1302 O  O   . ALA   A 1 168 ? -4.29569  27.16907  20.97367  1.000 38.79347 ? 168 ALA   A O   1 
ATOM   1303 C  CB  . ALA   A 1 168 ? -3.27333  29.52016  19.23058  1.000 37.36921 ? 168 ALA   A CB  1 
ATOM   1304 N  N   . ASP   A 1 169 ? -3.59577  26.15939  19.08841  1.000 39.23155 ? 169 ASP   A N   1 
ATOM   1305 C  CA  . ASP   A 1 169 ? -4.47964  25.01133  19.22268  1.000 39.47316 ? 169 ASP   A CA  1 
ATOM   1306 C  C   . ASP   A 1 169 ? -3.80498  23.82459  19.89802  1.000 39.84139 ? 169 ASP   A C   1 
ATOM   1307 O  O   . ASP   A 1 169 ? -4.31847  22.70333  19.80743  1.000 40.44946 ? 169 ASP   A O   1 
ATOM   1308 C  CB  . ASP   A 1 169 ? -5.00296  24.58647  17.84897  1.000 39.38544 ? 169 ASP   A CB  1 
ATOM   1309 C  CG  . ASP   A 1 169 ? -5.79833  25.67574  17.16492  1.000 39.37932 ? 169 ASP   A CG  1 
ATOM   1310 O  OD1 . ASP   A 1 169 ? -6.60665  26.33517  17.84774  1.000 39.77705 ? 169 ASP   A OD1 1 
ATOM   1311 O  OD2 . ASP   A 1 169 ? -5.61585  25.87136  15.94406  1.000 38.75863 ? 169 ASP   A OD2 1 
ATOM   1312 N  N   . HIS   A 1 170 ? -2.67424  24.04288  20.57706  1.000 40.06264 ? 170 HIS   A N   1 
ATOM   1313 C  CA  . HIS   A 1 170 ? -1.83855  22.91594  20.98281  1.000 40.75084 ? 170 HIS   A CA  1 
ATOM   1314 C  C   . HIS   A 1 170 ? -2.54803  22.01507  21.98426  1.000 42.30502 ? 170 HIS   A C   1 
ATOM   1315 O  O   . HIS   A 1 170 ? -2.39244  20.79083  21.93550  1.000 37.70992 ? 170 HIS   A O   1 
ATOM   1316 C  CB  . HIS   A 1 170 ? -0.50141  23.40700  21.54165  1.000 40.42970 ? 170 HIS   A CB  1 
ATOM   1317 C  CG  . HIS   A 1 170 ? -0.61796  24.20361  22.80238  1.000 41.36196 ? 170 HIS   A CG  1 
ATOM   1318 N  ND1 . HIS   A 1 170 ? -0.77367  25.57310  22.80639  1.000 41.20652 ? 170 HIS   A ND1 1 
ATOM   1319 C  CD2 . HIS   A 1 170 ? -0.57821  23.82574  24.10188  1.000 42.32585 ? 170 HIS   A CD2 1 
ATOM   1320 C  CE1 . HIS   A 1 170 ? -0.83514  26.00336  24.05394  1.000 42.99091 ? 170 HIS   A CE1 1 
ATOM   1321 N  NE2 . HIS   A 1 170 ? -0.71958  24.96290  24.85938  1.000 43.77713 ? 170 HIS   A NE2 1 
ATOM   1322 N  N   . GLU   A 1 171 ? -3.34507  22.59147  22.88762  1.000 41.82580 ? 171 GLU   A N   1 
ATOM   1323 C  CA  . GLU   A 1 171 ? -4.03917  21.76067  23.86819  1.000 43.01397 ? 171 GLU   A CA  1 
ATOM   1324 C  C   . GLU   A 1 171 ? -4.97065  20.76197  23.19099  1.000 41.38745 ? 171 GLU   A C   1 
ATOM   1325 O  O   . GLU   A 1 171 ? -5.12059  19.62783  23.66051  1.000 40.97583 ? 171 GLU   A O   1 
ATOM   1326 C  CB  . GLU   A 1 171 ? -4.81335  22.62855  24.85909  1.000 45.57098 ? 171 GLU   A CB  1 
ATOM   1327 C  CG  . GLU   A 1 171 ? -3.98006  23.11586  26.03140  1.000 48.75425 ? 171 GLU   A CG  1 
ATOM   1328 C  CD  . GLU   A 1 171 ? -4.83025  23.54111  27.21442  1.000 58.04091 ? 171 GLU   A CD  1 
ATOM   1329 O  OE1 . GLU   A 1 171 ? -5.44155  22.66184  27.86105  1.000 57.01880 ? 171 GLU   A OE1 1 
ATOM   1330 O  OE2 . GLU   A 1 171 ? -4.89367  24.75678  27.49201  1.000 55.54531 ? 171 GLU   A OE2 1 
ATOM   1331 N  N   . PHE   A 1 172 ? -5.59253  21.15403  22.07725  1.000 40.51181 ? 172 PHE   A N   1 
ATOM   1332 C  CA  . PHE   A 1 172 ? -6.48691  20.23435  21.38180  1.000 40.93168 ? 172 PHE   A CA  1 
ATOM   1333 C  C   . PHE   A 1 172 ? -5.71430  19.08821  20.73854  1.000 39.85687 ? 172 PHE   A C   1 
ATOM   1334 O  O   . PHE   A 1 172 ? -5.95111  17.91476  21.04852  1.000 39.24750 ? 172 PHE   A O   1 
ATOM   1335 C  CB  . PHE   A 1 172 ? -7.31354  20.96918  20.32674  1.000 39.37245 ? 172 PHE   A CB  1 
ATOM   1336 C  CG  . PHE   A 1 172 ? -8.01043  20.04228  19.37110  1.000 40.30712 ? 172 PHE   A CG  1 
ATOM   1337 C  CD1 . PHE   A 1 172 ? -9.15771  19.36477  19.75490  1.000 40.94007 ? 172 PHE   A CD1 1 
ATOM   1338 C  CD2 . PHE   A 1 172 ? -7.50468  19.82574  18.09904  1.000 39.16919 ? 172 PHE   A CD2 1 
ATOM   1339 C  CE1 . PHE   A 1 172 ? -9.79413  18.49870  18.88365  1.000 40.38145 ? 172 PHE   A CE1 1 
ATOM   1340 C  CE2 . PHE   A 1 172 ? -8.13574  18.96099  17.22607  1.000 39.64662 ? 172 PHE   A CE2 1 
ATOM   1341 C  CZ  . PHE   A 1 172 ? -9.28312  18.29751  17.61635  1.000 39.99059 ? 172 PHE   A CZ  1 
ATOM   1342 N  N   . PHE   A 1 173 ? -4.79013  19.40359  19.82527  1.000 39.71024 ? 173 PHE   A N   1 
ATOM   1343 C  CA  . PHE   A 1 173 ? -4.16720  18.33264  19.05882  1.000 39.56490 ? 173 PHE   A CA  1 
ATOM   1344 C  C   . PHE   A 1 173 ? -3.08641  17.59118  19.83546  1.000 40.11339 ? 173 PHE   A C   1 
ATOM   1345 O  O   . PHE   A 1 173 ? -2.77136  16.45183  19.47778  1.000 37.42058 ? 173 PHE   A O   1 
ATOM   1346 C  CB  . PHE   A 1 173 ? -3.61644  18.84914  17.71859  1.000 38.38251 ? 173 PHE   A CB  1 
ATOM   1347 C  CG  . PHE   A 1 173 ? -2.63805  19.99379  17.82245  1.000 39.23995 ? 173 PHE   A CG  1 
ATOM   1348 C  CD1 . PHE   A 1 173 ? -1.33800  19.78863  18.26144  1.000 38.37681 ? 173 PHE   A CD1 1 
ATOM   1349 C  CD2 . PHE   A 1 173 ? -3.00179  21.26409  17.40087  1.000 38.83276 ? 173 PHE   A CD2 1 
ATOM   1350 C  CE1 . PHE   A 1 173 ? -0.43726  20.83730  18.32477  1.000 38.84007 ? 173 PHE   A CE1 1 
ATOM   1351 C  CE2 . PHE   A 1 173 ? -2.10493  22.31785  17.46047  1.000 38.62050 ? 173 PHE   A CE2 1 
ATOM   1352 C  CZ  . PHE   A 1 173 ? -0.82085  22.10305  17.91661  1.000 38.52936 ? 173 PHE   A CZ  1 
ATOM   1353 N  N   . GLN   A 1 174 ? -2.52201  18.18682  20.89103  1.000 37.68707 ? 174 GLN   A N   1 
ATOM   1354 C  CA  . GLN   A 1 174 ? -1.65777  17.40256  21.76932  1.000 39.35102 ? 174 GLN   A CA  1 
ATOM   1355 C  C   . GLN   A 1 174 ? -2.46206  16.35055  22.51963  1.000 39.78459 ? 174 GLN   A C   1 
ATOM   1356 O  O   . GLN   A 1 174 ? -1.97837  15.23565  22.74563  1.000 38.61135 ? 174 GLN   A O   1 
ATOM   1357 C  CB  . GLN   A 1 174 ? -0.91288  18.30534  22.75318  1.000 39.79569 ? 174 GLN   A CB  1 
ATOM   1358 C  CG  . GLN   A 1 174 ? 0.22917   19.09520  22.12970  1.000 39.34307 ? 174 GLN   A CG  1 
ATOM   1359 C  CD  . GLN   A 1 174 ? 0.88643   20.04603  23.10964  1.000 40.52059 ? 174 GLN   A CD  1 
ATOM   1360 O  OE1 . GLN   A 1 174 ? 1.76458   20.82512  22.74090  1.000 39.01432 ? 174 GLN   A OE1 1 
ATOM   1361 N  NE2 . GLN   A 1 174 ? 0.46308   19.98786  24.36689  1.000 40.88340 ? 174 GLN   A NE2 1 
ATOM   1362 N  N   . ASP   A 1 175 ? -3.69641  16.68403  22.90357  1.000 39.19967 ? 175 ASP   A N   1 
ATOM   1363 C  CA  . ASP   A 1 175 ? -4.54369  15.71265  23.58613  1.000 40.51127 ? 175 ASP   A CA  1 
ATOM   1364 C  C   . ASP   A 1 175 ? -5.02713  14.63334  22.62762  1.000 39.93056 ? 175 ASP   A C   1 
ATOM   1365 O  O   . ASP   A 1 175 ? -5.05540  13.44940  22.98258  1.000 41.31814 ? 175 ASP   A O   1 
ATOM   1366 C  CB  . ASP   A 1 175 ? -5.73178  16.41504  24.24172  1.000 40.43216 ? 175 ASP   A CB  1 
ATOM   1367 C  CG  . ASP   A 1 175 ? -6.70137  15.44122  24.87775  1.000 41.67608 ? 175 ASP   A CG  1 
ATOM   1368 O  OD1 . ASP   A 1 175 ? -6.37869  14.89832  25.95626  1.000 42.57879 ? 175 ASP   A OD1 1 
ATOM   1369 O  OD2 . ASP   A 1 175 ? -7.78391  15.21514  24.29638  1.000 40.94030 ? 175 ASP   A OD2 1 
ATOM   1370 N  N   . ALA   A 1 176 ? -5.42233  15.02389  21.41297  1.000 39.57879 ? 176 ALA   A N   1 
ATOM   1371 C  CA  . ALA   A 1 176 ? -5.82279  14.03736  20.41519  1.000 40.51502 ? 176 ALA   A CA  1 
ATOM   1372 C  C   . ALA   A 1 176 ? -4.65520  13.13547  20.04172  1.000 40.11026 ? 176 ALA   A C   1 
ATOM   1373 O  O   . ALA   A 1 176 ? -4.83148  11.92713  19.84711  1.000 40.44040 ? 176 ALA   A O   1 
ATOM   1374 C  CB  . ALA   A 1 176 ? -6.38390  14.73522  19.17629  1.000 38.61297 ? 176 ALA   A CB  1 
ATOM   1375 N  N   . SER   A 1 177 ? -3.45086  13.70377  19.94916  1.000 38.44747 ? 177 SER   A N   1 
ATOM   1376 C  CA  . SER   A 1 177 ? -2.26714  12.89492  19.67891  1.000 39.35369 ? 177 SER   A CA  1 
ATOM   1377 C  C   . SER   A 1 177 ? -2.02379  11.89367  20.80158  1.000 41.89970 ? 177 SER   A C   1 
ATOM   1378 O  O   . SER   A 1 177 ? -1.77482  10.70854  20.54943  1.000 40.73171 ? 177 SER   A O   1 
ATOM   1379 C  CB  . SER   A 1 177 ? -1.04728  13.79746  19.48750  1.000 38.27574 ? 177 SER   A CB  1 
ATOM   1380 O  OG  . SER   A 1 177 ? 0.10873   13.03989  19.17717  1.000 37.94872 ? 177 SER   A OG  1 
ATOM   1381 N  N   . LYS   A 1 178 ? -2.09585  12.35548  22.05411  1.000 40.86378 ? 178 LYS   A N   1 
ATOM   1382 C  CA  . LYS   A 1 178 ? -1.87089  11.46243  23.18635  1.000 42.69710 ? 178 LYS   A CA  1 
ATOM   1383 C  C   . LYS   A 1 178 ? -2.93439  10.37379  23.24989  1.000 44.95637 ? 178 LYS   A C   1 
ATOM   1384 O  O   . LYS   A 1 178 ? -2.61952  9.20333   23.49664  1.000 45.09045 ? 178 LYS   A O   1 
ATOM   1385 C  CB  . LYS   A 1 178 ? -1.84346  12.25801  24.49135  1.000 44.32493 ? 178 LYS   A CB  1 
ATOM   1386 C  CG  . LYS   A 1 178 ? -1.64516  11.39222  25.73026  1.000 47.92472 ? 178 LYS   A CG  1 
ATOM   1387 C  CD  . LYS   A 1 178 ? -2.07568  12.12127  26.99567  1.000 50.48854 ? 178 LYS   A CD  1 
ATOM   1388 C  CE  . LYS   A 1 178 ? -1.06625  13.17603  27.42230  1.000 54.21782 ? 178 LYS   A CE  1 
ATOM   1389 N  NZ  . LYS   A 1 178 ? 0.06233   12.58576  28.19740  1.000 56.88364 ? 178 LYS   A NZ  1 
ATOM   1390 N  N   . ARG   A 1 179 ? -4.19974  10.73989  23.02343  1.000 43.98587 ? 179 ARG   A N   1 
ATOM   1391 C  CA  . ARG   A 1 179 ? -5.27193  9.74945   23.05105  1.000 43.77864 ? 179 ARG   A CA  1 
ATOM   1392 C  C   . ARG   A 1 179 ? -5.04477  8.65613   22.01448  1.000 45.74597 ? 179 ARG   A C   1 
ATOM   1393 O  O   . ARG   A 1 179 ? -5.33607  7.48155   22.26883  1.000 46.45899 ? 179 ARG   A O   1 
ATOM   1394 C  CB  . ARG   A 1 179 ? -6.62641  10.42830  22.83864  1.000 42.95017 ? 179 ARG   A CB  1 
ATOM   1395 C  CG  . ARG   A 1 179 ? -7.20472  11.04403  24.10866  1.000 43.08760 ? 179 ARG   A CG  1 
ATOM   1396 C  CD  . ARG   A 1 179 ? -8.62472  11.56275  23.91069  1.000 42.06292 ? 179 ARG   A CD  1 
ATOM   1397 N  NE  . ARG   A 1 179 ? -8.67048  12.77418  23.09414  1.000 41.67924 ? 179 ARG   A NE  1 
ATOM   1398 C  CZ  . ARG   A 1 179 ? -9.29330  12.86697  21.92350  1.000 41.39905 ? 179 ARG   A CZ  1 
ATOM   1399 N  NH1 . ARG   A 1 179 ? -9.93849  11.82102  21.42851  1.000 40.87444 ? 179 ARG   A NH1 1 
ATOM   1400 N  NH2 . ARG   A 1 179 ? -9.27976  14.01086  21.25066  1.000 40.49846 ? 179 ARG   A NH2 1 
ATOM   1401 N  N   . LEU   A 1 180 ? -4.51284  9.01749   20.84396  1.000 44.35166 ? 180 LEU   A N   1 
ATOM   1402 C  CA  . LEU   A 1 180 ? -4.18753  8.00775   19.84110  1.000 45.61522 ? 180 LEU   A CA  1 
ATOM   1403 C  C   . LEU   A 1 180 ? -3.00941  7.14795   20.28512  1.000 46.37528 ? 180 LEU   A C   1 
ATOM   1404 O  O   . LEU   A 1 180 ? -3.03006  5.92252   20.12053  1.000 47.13239 ? 180 LEU   A O   1 
ATOM   1405 C  CB  . LEU   A 1 180 ? -3.88279  8.67636   18.50143  1.000 44.96452 ? 180 LEU   A CB  1 
ATOM   1406 C  CG  . LEU   A 1 180 ? -4.76851  8.28844   17.31650  1.000 44.96505 ? 180 LEU   A CG  1 
ATOM   1407 C  CD1 . LEU   A 1 180 ? -4.16357  8.76541   16.00486  1.000 44.16717 ? 180 LEU   A CD1 1 
ATOM   1408 C  CD2 . LEU   A 1 180 ? -5.00468  6.78700   17.27973  1.000 46.35904 ? 180 LEU   A CD2 1 
ATOM   1409 N  N   . VAL   A 1 181 ? -1.98190  7.77284   20.86736  1.000 46.02835 ? 181 VAL   A N   1 
ATOM   1410 C  CA  . VAL   A 1 181 ? -0.76686  7.04782   21.23723  1.000 46.28661 ? 181 VAL   A CA  1 
ATOM   1411 C  C   . VAL   A 1 181 ? -1.06231  6.00756   22.31135  1.000 47.07257 ? 181 VAL   A C   1 
ATOM   1412 O  O   . VAL   A 1 181 ? -0.54773  4.88337   22.26810  1.000 46.00421 ? 181 VAL   A O   1 
ATOM   1413 C  CB  . VAL   A 1 181 ? 0.32331   8.03959   21.68767  1.000 44.76312 ? 181 VAL   A CB  1 
ATOM   1414 C  CG1 . VAL   A 1 181 ? 1.44247   7.32121   22.42364  1.000 43.11877 ? 181 VAL   A CG1 1 
ATOM   1415 C  CG2 . VAL   A 1 181 ? 0.87005   8.78830   20.48533  1.000 43.27252 ? 181 VAL   A CG2 1 
ATOM   1416 N  N   A GLN   A 1 182 ? -1.90535  6.35864   23.27887  0.500 47.29323 ? 182 GLN   A N   1 
ATOM   1417 N  N   B GLN   A 1 182 ? -1.89944  6.35850   23.28228  0.500 47.28783 ? 182 GLN   A N   1 
ATOM   1418 C  CA  A GLN   A 1 182 ? -2.22260  5.48629   24.40066  0.500 48.52177 ? 182 GLN   A CA  1 
ATOM   1419 C  CA  B GLN   A 1 182 ? -2.21828  5.47879   24.39878  0.500 48.54477 ? 182 GLN   A CA  1 
ATOM   1420 C  C   A GLN   A 1 182 ? -3.49629  4.67895   24.18867  0.500 49.03627 ? 182 GLN   A C   1 
ATOM   1421 C  C   B GLN   A 1 182 ? -3.50332  4.68633   24.19295  0.500 49.04400 ? 182 GLN   A C   1 
ATOM   1422 O  O   A GLN   A 1 182 ? -3.88203  3.91698   25.08049  0.500 49.58905 ? 182 GLN   A O   1 
ATOM   1423 O  O   B GLN   A 1 182 ? -3.90452  3.94110   25.09344  0.500 49.60677 ? 182 GLN   A O   1 
ATOM   1424 C  CB  A GLN   A 1 182 ? -2.34746  6.31221   25.68544  0.500 48.70688 ? 182 GLN   A CB  1 
ATOM   1425 C  CB  B GLN   A 1 182 ? -2.31691  6.29191   25.69423  0.500 48.69910 ? 182 GLN   A CB  1 
ATOM   1426 C  CG  A GLN   A 1 182 ? -3.60211  7.17159   25.74039  0.500 48.66546 ? 182 GLN   A CG  1 
ATOM   1427 C  CG  B GLN   A 1 182 ? -1.01384  6.96264   26.10299  0.500 48.63132 ? 182 GLN   A CG  1 
ATOM   1428 C  CD  A GLN   A 1 182 ? -3.56941  8.18507   26.86857  0.500 48.88642 ? 182 GLN   A CD  1 
ATOM   1429 C  CD  B GLN   A 1 182 ? -1.17052  7.87220   27.30816  0.500 49.55332 ? 182 GLN   A CD  1 
ATOM   1430 O  OE1 A GLN   A 1 182 ? -2.54914  8.35420   27.53631  0.500 49.36434 ? 182 GLN   A OE1 1 
ATOM   1431 O  OE1 B GLN   A 1 182 ? -2.26845  8.34369   27.61025  0.500 49.46606 ? 182 GLN   A OE1 1 
ATOM   1432 N  NE2 A GLN   A 1 182 ? -4.68918  8.86788   27.08520  0.500 48.67101 ? 182 GLN   A NE2 1 
ATOM   1433 N  NE2 B GLN   A 1 182 ? -0.06802  8.12426   28.00328  0.500 49.41809 ? 182 GLN   A NE2 1 
ATOM   1434 N  N   . SER   A 1 183 ? -4.15124  4.82411   23.03701  1.000 48.23654 ? 183 SER   A N   1 
ATOM   1435 C  CA  . SER   A 1 183 ? -5.43039  4.16144   22.80256  1.000 49.51541 ? 183 SER   A CA  1 
ATOM   1436 C  C   . SER   A 1 183 ? -5.29163  2.64427   22.85352  1.000 50.09412 ? 183 SER   A C   1 
ATOM   1437 O  O   . SER   A 1 183 ? -4.40010  2.06624   22.22484  1.000 49.20831 ? 183 SER   A O   1 
ATOM   1438 C  CB  . SER   A 1 183 ? -6.00157  4.58342   21.44907  1.000 49.67353 ? 183 SER   A CB  1 
ATOM   1439 O  OG  . SER   A 1 183 ? -7.21449  3.90310   21.18175  1.000 55.18976 ? 183 SER   A OG  1 
ATOM   1440 N  N   . THR   A 1 184 ? -6.19013  2.00140   23.60104  1.000 51.29941 ? 184 THR   A N   1 
ATOM   1441 C  CA  . THR   A 1 184 ? -6.17508  0.55727   23.78811  1.000 51.61026 ? 184 THR   A CA  1 
ATOM   1442 C  C   . THR   A 1 184 ? -7.33022  -0.14866  23.09129  1.000 52.00899 ? 184 THR   A C   1 
ATOM   1443 O  O   . THR   A 1 184 ? -7.41082  -1.37955  23.15343  1.000 52.34124 ? 184 THR   A O   1 
ATOM   1444 C  CB  . THR   A 1 184 ? -6.19605  0.21824   25.28325  1.000 51.92687 ? 184 THR   A CB  1 
ATOM   1445 O  OG1 . THR   A 1 184 ? -7.40543  0.71461   25.87001  1.000 51.96510 ? 184 THR   A OG1 1 
ATOM   1446 C  CG2 . THR   A 1 184 ? -5.00421  0.84940   25.98847  1.000 51.94550 ? 184 THR   A CG2 1 
ATOM   1447 N  N   . ASP   A 1 185 ? -8.22649  0.58881   22.43761  1.000 52.55598 ? 185 ASP   A N   1 
ATOM   1448 C  CA  . ASP   A 1 185 ? -9.31921  -0.00496  21.68062  1.000 53.12633 ? 185 ASP   A CA  1 
ATOM   1449 C  C   . ASP   A 1 185 ? -9.46102  0.72911   20.35480  1.000 51.61837 ? 185 ASP   A C   1 
ATOM   1450 O  O   . ASP   A 1 185 ? -8.90257  1.81102   20.15416  1.000 51.13103 ? 185 ASP   A O   1 
ATOM   1451 C  CB  . ASP   A 1 185 ? -10.63904 0.03151   22.46165  1.000 54.11074 ? 185 ASP   A CB  1 
ATOM   1452 C  CG  . ASP   A 1 185 ? -10.97681 1.41831   22.96769  1.000 55.40862 ? 185 ASP   A CG  1 
ATOM   1453 O  OD1 . ASP   A 1 185 ? -10.10921 2.03813   23.61719  1.000 58.30692 ? 185 ASP   A OD1 1 
ATOM   1454 O  OD2 . ASP   A 1 185 ? -12.10351 1.89322   22.70968  1.000 61.91855 ? 185 ASP   A OD2 1 
ATOM   1455 N  N   . ALA   A 1 186 ? -10.22722 0.12672   19.44261  1.000 51.21402 ? 186 ALA   A N   1 
ATOM   1456 C  CA  . ALA   A 1 186 ? -10.36796 0.69513   18.10581  1.000 50.13676 ? 186 ALA   A CA  1 
ATOM   1457 C  C   . ALA   A 1 186 ? -11.21785 1.96093   18.12011  1.000 50.26666 ? 186 ALA   A C   1 
ATOM   1458 O  O   . ALA   A 1 186 ? -10.88287 2.94584   17.45180  1.000 48.72818 ? 186 ALA   A O   1 
ATOM   1459 C  CB  . ALA   A 1 186 ? -10.96588 -0.34230  17.15596  1.000 49.96014 ? 186 ALA   A CB  1 
ATOM   1460 N  N   . GLN   A 1 187 ? -12.32084 1.95426   18.87287  1.000 51.68783 ? 187 GLN   A N   1 
ATOM   1461 C  CA  . GLN   A 1 187 ? -13.22565 3.10069   18.87298  1.000 52.71600 ? 187 GLN   A CA  1 
ATOM   1462 C  C   . GLN   A 1 187 ? -12.55080 4.34549   19.43761  1.000 50.91168 ? 187 GLN   A C   1 
ATOM   1463 O  O   . GLN   A 1 187 ? -12.73581 5.45130   18.91535  1.000 48.64221 ? 187 GLN   A O   1 
ATOM   1464 C  CB  . GLN   A 1 187 ? -14.48852 2.77063   19.66834  1.000 55.27360 ? 187 GLN   A CB  1 
ATOM   1465 C  CG  . GLN   A 1 187 ? -15.46580 3.92907   19.78794  1.000 56.94545 ? 187 GLN   A CG  1 
ATOM   1466 C  CD  . GLN   A 1 187 ? -16.54811 3.67325   20.81820  1.000 59.78822 ? 187 GLN   A CD  1 
ATOM   1467 O  OE1 . GLN   A 1 187 ? -16.76927 2.53558   21.23384  1.000 59.54424 ? 187 GLN   A OE1 1 
ATOM   1468 N  NE2 . GLN   A 1 187 ? -17.22504 4.73505   21.24190  1.000 59.88275 ? 187 GLN   A NE2 1 
ATOM   1469 N  N   . SER   A 1 188 ? -11.77188 4.18937   20.51092  1.000 51.05133 ? 188 SER   A N   1 
ATOM   1470 C  CA  . SER   A 1 188 ? -11.07112 5.33592   21.08059  1.000 49.78234 ? 188 SER   A CA  1 
ATOM   1471 C  C   . SER   A 1 188 ? -10.02779 5.87652   20.11282  1.000 48.19474 ? 188 SER   A C   1 
ATOM   1472 O  O   . SER   A 1 188 ? -9.86783  7.09556   19.97659  1.000 45.37237 ? 188 SER   A O   1 
ATOM   1473 C  CB  . SER   A 1 188 ? -10.41865 4.95248   22.40815  1.000 51.99608 ? 188 SER   A CB  1 
ATOM   1474 O  OG  . SER   A 1 188 ? -11.38718 4.53321   23.35346  1.000 55.81051 ? 188 SER   A OG  1 
ATOM   1475 N  N   . ALA   A 1 189 ? -9.30900  4.98250   19.43102  1.000 48.24585 ? 189 ALA   A N   1 
ATOM   1476 C  CA  . ALA   A 1 189 ? -8.30866  5.41577   18.46190  1.000 47.18133 ? 189 ALA   A CA  1 
ATOM   1477 C  C   . ALA   A 1 189 ? -8.96126  6.12915   17.28538  1.000 46.55342 ? 189 ALA   A C   1 
ATOM   1478 O  O   . ALA   A 1 189 ? -8.48709  7.18097   16.84016  1.000 44.50516 ? 189 ALA   A O   1 
ATOM   1479 C  CB  . ALA   A 1 189 ? -7.49225  4.21567   17.98098  1.000 48.23892 ? 189 ALA   A CB  1 
ATOM   1480 N  N   . LEU   A 1 190 ? -10.06031 5.57105   16.77104  1.000 46.76119 ? 190 LEU   A N   1 
ATOM   1481 C  CA  . LEU   A 1 190 ? -10.72876 6.17657   15.62390  1.000 46.13318 ? 190 LEU   A CA  1 
ATOM   1482 C  C   . LEU   A 1 190 ? -11.34465 7.52200   15.98263  1.000 45.37580 ? 190 LEU   A C   1 
ATOM   1483 O  O   . LEU   A 1 190 ? -11.34797 8.44481   15.15967  1.000 43.09026 ? 190 LEU   A O   1 
ATOM   1484 C  CB  . LEU   A 1 190 ? -11.78751 5.22469   15.07127  1.000 47.68086 ? 190 LEU   A CB  1 
ATOM   1485 C  CG  . LEU   A 1 190 ? -11.27812 4.29612   13.96830  1.000 51.16432 ? 190 LEU   A CG  1 
ATOM   1486 C  CD1 . LEU   A 1 190 ? -12.25697 3.16254   13.71348  1.000 51.36869 ? 190 LEU   A CD1 1 
ATOM   1487 C  CD2 . LEU   A 1 190 ? -11.03253 5.09673   12.69750  1.000 48.92432 ? 190 LEU   A CD2 1 
ATOM   1488 N  N   . THR   A 1 191 ? -11.87052 7.65459   17.20259  1.000 44.78145 ? 191 THR   A N   1 
ATOM   1489 C  CA  . THR   A 1 191 ? -12.39144 8.94480   17.64393  1.000 44.42568 ? 191 THR   A CA  1 
ATOM   1490 C  C   . THR   A 1 191 ? -11.28433 9.99057   17.68852  1.000 42.20128 ? 191 THR   A C   1 
ATOM   1491 O  O   . THR   A 1 191 ? -11.44560 11.10720  17.18266  1.000 41.48924 ? 191 THR   A O   1 
ATOM   1492 C  CB  . THR   A 1 191 ? -13.05806 8.80661   19.01505  1.000 43.95741 ? 191 THR   A CB  1 
ATOM   1493 O  OG1 . THR   A 1 191 ? -14.26507 8.04544   18.88977  1.000 45.65338 ? 191 THR   A OG1 1 
ATOM   1494 C  CG2 . THR   A 1 191 ? -13.39041 10.17568  19.58871  1.000 42.69578 ? 191 THR   A CG2 1 
ATOM   1495 N  N   . ALA   A 1 192 ? -10.14405 9.64049   18.28807  1.000 42.86148 ? 192 ALA   A N   1 
ATOM   1496 C  CA  . ALA   A 1 192 ? -9.02453  10.57327  18.35005  1.000 42.15178 ? 192 ALA   A CA  1 
ATOM   1497 C  C   . ALA   A 1 192 ? -8.46867  10.88037  16.96460  1.000 42.01582 ? 192 ALA   A C   1 
ATOM   1498 O  O   . ALA   A 1 192 ? -7.99693  11.99817  16.72226  1.000 39.72500 ? 192 ALA   A O   1 
ATOM   1499 C  CB  . ALA   A 1 192 ? -7.92646  10.01400  19.25373  1.000 41.96953 ? 192 ALA   A CB  1 
ATOM   1500 N  N   . ARG   A 1 193 ? -8.52183  9.91536   16.04276  1.000 41.44777 ? 193 ARG   A N   1 
ATOM   1501 C  CA  . ARG   A 1 193 ? -8.03015  10.16970  14.69259  1.000 42.19282 ? 193 ARG   A CA  1 
ATOM   1502 C  C   . ARG   A 1 193 ? -8.97028  11.09775  13.93494  1.000 40.75700 ? 193 ARG   A C   1 
ATOM   1503 O  O   . ARG   A 1 193 ? -8.52382  12.02888  13.25462  1.000 38.90961 ? 193 ARG   A O   1 
ATOM   1504 C  CB  . ARG   A 1 193 ? -7.84669  8.85904   13.92922  1.000 42.84374 ? 193 ARG   A CB  1 
ATOM   1505 C  CG  . ARG   A 1 193 ? -6.98499  9.02497   12.68697  1.000 42.34464 ? 193 ARG   A CG  1 
ATOM   1506 C  CD  . ARG   A 1 193 ? -7.61484  8.41404   11.44795  1.000 43.03375 ? 193 ARG   A CD  1 
ATOM   1507 N  NE  . ARG   A 1 193 ? -6.87288  8.79286   10.24844  1.000 41.87506 ? 193 ARG   A NE  1 
ATOM   1508 C  CZ  . ARG   A 1 193 ? -7.34248  9.58910   9.29328   1.000 41.10862 ? 193 ARG   A CZ  1 
ATOM   1509 N  NH1 . ARG   A 1 193 ? -6.58504  9.88182   8.24482   1.000 38.81969 ? 193 ARG   A NH1 1 
ATOM   1510 N  NH2 . ARG   A 1 193 ? -8.57368  10.07497  9.37274   1.000 40.66801 ? 193 ARG   A NH2 1 
ATOM   1511 N  N   . ASN   A 1 194 ? -10.28071 10.85643  14.03827  1.000 41.05551 ? 194 ASN   A N   1 
ATOM   1512 C  CA  . ASN   A 1 194 ? -11.24309 11.73359  13.37976  1.000 42.16472 ? 194 ASN   A CA  1 
ATOM   1513 C  C   . ASN   A 1 194 ? -11.22020 13.13579  13.97364  1.000 39.66742 ? 194 ASN   A C   1 
ATOM   1514 O  O   . ASN   A 1 194 ? -11.51128 14.11013  13.27008  1.000 40.22128 ? 194 ASN   A O   1 
ATOM   1515 C  CB  . ASN   A 1 194 ? -12.64850 11.13981  13.46909  1.000 43.75920 ? 194 ASN   A CB  1 
ATOM   1516 C  CG  . ASN   A 1 194 ? -12.76068 9.80181   12.76704  1.000 46.11753 ? 194 ASN   A CG  1 
ATOM   1517 O  OD1 . ASN   A 1 194 ? -11.91709 9.44467   11.94359  1.000 49.59371 ? 194 ASN   A OD1 1 
ATOM   1518 N  ND2 . ASN   A 1 194 ? -13.81052 9.05512   13.08566  1.000 48.52657 ? 194 ASN   A ND2 1 
ATOM   1519 N  N   . ASP   A 1 195 ? -10.88440 13.25802  15.26101  1.000 37.88783 ? 195 ASP   A N   1 
ATOM   1520 C  CA  . ASP   A 1 195 ? -10.69575 14.57747  15.85782  1.000 40.40755 ? 195 ASP   A CA  1 
ATOM   1521 C  C   . ASP   A 1 195 ? -9.57399  15.33402  15.15797  1.000 37.55945 ? 195 ASP   A C   1 
ATOM   1522 O  O   . ASP   A 1 195 ? -9.71693  16.51694  14.82782  1.000 38.16493 ? 195 ASP   A O   1 
ATOM   1523 C  CB  . ASP   A 1 195 ? -10.40023 14.44464  17.35370  1.000 39.26564 ? 195 ASP   A CB  1 
ATOM   1524 C  CG  . ASP   A 1 195 ? -11.61850 14.03551  18.15792  1.000 39.78711 ? 195 ASP   A CG  1 
ATOM   1525 O  OD1 . ASP   A 1 195 ? -12.73145 14.04045  17.59074  1.000 39.97465 ? 195 ASP   A OD1 1 
ATOM   1526 O  OD2 . ASP   A 1 195 ? -11.46056 13.70704  19.35493  1.000 39.18179 ? 195 ASP   A OD2 1 
ATOM   1527 N  N   . LEU   A 1 196 ? -8.44342  14.66212  14.92551  1.000 36.39571 ? 196 LEU   A N   1 
ATOM   1528 C  CA  . LEU   A 1 196 ? -7.33927  15.29127  14.20922  1.000 37.30915 ? 196 LEU   A CA  1 
ATOM   1529 C  C   . LEU   A 1 196 ? -7.69865  15.54235  12.75163  1.000 36.45813 ? 196 LEU   A C   1 
ATOM   1530 O  O   . LEU   A 1 196 ? -7.39507  16.61164  12.20729  1.000 34.36975 ? 196 LEU   A O   1 
ATOM   1531 C  CB  . LEU   A 1 196 ? -6.08607  14.42260  14.30971  1.000 36.60622 ? 196 LEU   A CB  1 
ATOM   1532 C  CG  . LEU   A 1 196 ? -5.31288  14.50315  15.62346  1.000 36.90196 ? 196 LEU   A CG  1 
ATOM   1533 C  CD1 . LEU   A 1 196 ? -4.12294  13.55503  15.60479  1.000 36.79092 ? 196 LEU   A CD1 1 
ATOM   1534 C  CD2 . LEU   A 1 196 ? -4.86062  15.93080  15.87089  1.000 36.70465 ? 196 LEU   A CD2 1 
ATOM   1535 N  N   . ALA   A 1 197 ? -8.34312  14.56651  12.10505  1.000 35.90042 ? 197 ALA   A N   1 
ATOM   1536 C  CA  . ALA   A 1 197 ? -8.74030  14.73218  10.71043  1.000 35.90874 ? 197 ALA   A CA  1 
ATOM   1537 C  C   . ALA   A 1 197 ? -9.66523  15.93094  10.53556  1.000 34.81940 ? 197 ALA   A C   1 
ATOM   1538 O  O   . ALA   A 1 197 ? -9.50843  16.71195  9.58996   1.000 34.43944 ? 197 ALA   A O   1 
ATOM   1539 C  CB  . ALA   A 1 197 ? -9.41300  13.45744  10.20129  1.000 35.44859 ? 197 ALA   A CB  1 
ATOM   1540 N  N   . GLY   A 1 198 ? -10.63767 16.09045  11.43579  1.000 35.06920 ? 198 GLY   A N   1 
ATOM   1541 C  CA  . GLY   A 1 198 ? -11.53822 17.22659  11.33926  1.000 35.60137 ? 198 GLY   A CA  1 
ATOM   1542 C  C   . GLY   A 1 198 ? -10.82361 18.55108  11.52096  1.000 34.16700 ? 198 GLY   A C   1 
ATOM   1543 O  O   . GLY   A 1 198 ? -11.12484 19.53042  10.83447  1.000 36.99698 ? 198 GLY   A O   1 
ATOM   1544 N  N   . TYR   A 1 199 ? -9.86058  18.59655  12.44131  1.000 34.48617 ? 199 TYR   A N   1 
ATOM   1545 C  CA  . TYR   A 1 199 ? -9.09821  19.82067  12.65533  1.000 35.31766 ? 199 TYR   A CA  1 
ATOM   1546 C  C   . TYR   A 1 199 ? -8.23478  20.14838  11.44458  1.000 34.61189 ? 199 TYR   A C   1 
ATOM   1547 O  O   . TYR   A 1 199 ? -8.20564  21.29442  10.98209  1.000 31.71347 ? 199 TYR   A O   1 
ATOM   1548 C  CB  . TYR   A 1 199 ? -8.23607  19.68568  13.90807  1.000 35.03340 ? 199 TYR   A CB  1 
ATOM   1549 C  CG  . TYR   A 1 199 ? -7.24651  20.81040  14.08119  1.000 36.35575 ? 199 TYR   A CG  1 
ATOM   1550 C  CD1 . TYR   A 1 199 ? -7.67476  22.09415  14.39171  1.000 37.17948 ? 199 TYR   A CD1 1 
ATOM   1551 C  CD2 . TYR   A 1 199 ? -5.88351  20.59086  13.93439  1.000 35.89526 ? 199 TYR   A CD2 1 
ATOM   1552 C  CE1 . TYR   A 1 199 ? -6.77372  23.12840  14.55075  1.000 37.38921 ? 199 TYR   A CE1 1 
ATOM   1553 C  CE2 . TYR   A 1 199 ? -4.97451  21.61941  14.08989  1.000 37.00754 ? 199 TYR   A CE2 1 
ATOM   1554 C  CZ  . TYR   A 1 199 ? -5.42561  22.88552  14.39824  1.000 37.31784 ? 199 TYR   A CZ  1 
ATOM   1555 O  OH  . TYR   A 1 199 ? -4.52598  23.91418  14.55574  1.000 37.28703 ? 199 TYR   A OH  1 
ATOM   1556 N  N   . LEU   A 1 200 ? -7.52462  19.14914  10.91483  1.000 32.27886 ? 200 LEU   A N   1 
ATOM   1557 C  CA  . LEU   A 1 200 ? -6.63632  19.39334  9.78449   1.000 33.83365 ? 200 LEU   A CA  1 
ATOM   1558 C  C   . LEU   A 1 200 ? -7.41214  19.74679  8.52248   1.000 32.02997 ? 200 LEU   A C   1 
ATOM   1559 O  O   . LEU   A 1 200 ? -6.93484  20.54957  7.71273   1.000 32.96798 ? 200 LEU   A O   1 
ATOM   1560 C  CB  . LEU   A 1 200 ? -5.74340  18.17384  9.54809   1.000 32.08802 ? 200 LEU   A CB  1 
ATOM   1561 C  CG  . LEU   A 1 200 ? -4.75939  17.87041  10.68029  1.000 30.74738 ? 200 LEU   A CG  1 
ATOM   1562 C  CD1 . LEU   A 1 200 ? -4.12779  16.49475  10.50766  1.000 30.99305 ? 200 LEU   A CD1 1 
ATOM   1563 C  CD2 . LEU   A 1 200 ? -3.68883  18.94625  10.75496  1.000 30.78977 ? 200 LEU   A CD2 1 
ATOM   1564 N  N   . ASP   A 1 201 ? -8.60501  19.17158  8.34007   1.000 33.93536 ? 201 ASP   A N   1 
ATOM   1565 C  CA  . ASP   A 1 201 ? -9.41400  19.50950  7.17175   1.000 33.23015 ? 201 ASP   A CA  1 
ATOM   1566 C  C   . ASP   A 1 201 ? -9.81625  20.97924  7.18468   1.000 33.26964 ? 201 ASP   A C   1 
ATOM   1567 O  O   . ASP   A 1 201 ? -9.78099  21.64989  6.14561   1.000 33.75146 ? 201 ASP   A O   1 
ATOM   1568 C  CB  . ASP   A 1 201 ? -10.65507 18.61905  7.10897   1.000 34.42963 ? 201 ASP   A CB  1 
ATOM   1569 C  CG  . ASP   A 1 201 ? -11.46629 18.84133  5.84512   1.000 36.86728 ? 201 ASP   A CG  1 
ATOM   1570 O  OD1 . ASP   A 1 201 ? -11.08870 18.29453  4.78667   1.000 35.97097 ? 201 ASP   A OD1 1 
ATOM   1571 O  OD2 . ASP   A 1 201 ? -12.47619 19.57271  5.90622   1.000 44.68854 ? 201 ASP   A OD2 1 
ATOM   1572 N  N   . GLY   A 1 202 ? -10.20999 21.49594  8.35087   1.000 33.77202 ? 202 GLY   A N   1 
ATOM   1573 C  CA  . GLY   A 1 202 ? -10.51443 22.91178  8.45779   1.000 33.73001 ? 202 GLY   A CA  1 
ATOM   1574 C  C   . GLY   A 1 202 ? -9.29500  23.78912  8.27320   1.000 32.40351 ? 202 GLY   A C   1 
ATOM   1575 O  O   . GLY   A 1 202 ? -9.40079  24.90378  7.75453   1.000 33.67879 ? 202 GLY   A O   1 
ATOM   1576 N  N   . LEU   A 1 203 ? -8.12419  23.30371  8.69248   1.000 34.59682 ? 203 LEU   A N   1 
ATOM   1577 C  CA  . LEU   A 1 203 ? -6.88872  24.03984  8.44880   1.000 33.26404 ? 203 LEU   A CA  1 
ATOM   1578 C  C   . LEU   A 1 203 ? -6.59035  24.12183  6.95723   1.000 34.91543 ? 203 LEU   A C   1 
ATOM   1579 O  O   . LEU   A 1 203 ? -6.07235  25.13632  6.47383   1.000 34.31192 ? 203 LEU   A O   1 
ATOM   1580 C  CB  . LEU   A 1 203 ? -5.73311  23.37782  9.20023   1.000 33.24990 ? 203 LEU   A CB  1 
ATOM   1581 C  CG  . LEU   A 1 203 ? -4.41126  24.14073  9.29699   1.000 34.60038 ? 203 LEU   A CG  1 
ATOM   1582 C  CD1 . LEU   A 1 203 ? -4.62824  25.49447  9.94872   1.000 35.11879 ? 203 LEU   A CD1 1 
ATOM   1583 C  CD2 . LEU   A 1 203 ? -3.38012  23.33079  10.07413  1.000 34.01824 ? 203 LEU   A CD2 1 
ATOM   1584 N  N   . ILE   A 1 204 ? -6.91754  23.06330  6.21093   1.000 30.93731 ? 204 ILE   A N   1 
ATOM   1585 C  CA  . ILE   A 1 204 ? -6.74899  23.08990  4.75971   1.000 32.59214 ? 204 ILE   A CA  1 
ATOM   1586 C  C   . ILE   A 1 204 ? -7.63084  24.16985  4.14699   1.000 31.19821 ? 204 ILE   A C   1 
ATOM   1587 O  O   . ILE   A 1 204 ? -7.17746  24.97677  3.32690   1.000 31.27254 ? 204 ILE   A O   1 
ATOM   1588 C  CB  . ILE   A 1 204 ? -7.05004  21.70542  4.15626   1.000 30.23430 ? 204 ILE   A CB  1 
ATOM   1589 C  CG1 . ILE   A 1 204 ? -5.97244  20.70070  4.56479   1.000 32.11879 ? 204 ILE   A CG1 1 
ATOM   1590 C  CG2 . ILE   A 1 204 ? -7.15242  21.79108  2.63842   1.000 31.39582 ? 204 ILE   A CG2 1 
ATOM   1591 C  CD1 . ILE   A 1 204 ? -6.26670  19.27363  4.13026   1.000 31.16758 ? 204 ILE   A CD1 1 
ATOM   1592 N  N   . THR   A 1 205 ? -8.90711  24.19738  4.53768   1.000 29.28509 ? 205 THR   A N   1 
ATOM   1593 C  CA  . THR   A 1 205 ? -9.81454  25.23015  4.05027   1.000 32.68641 ? 205 THR   A CA  1 
ATOM   1594 C  C   . THR   A 1 205 ? -9.31391  26.61981  4.42344   1.000 33.86950 ? 205 THR   A C   1 
ATOM   1595 O  O   . THR   A 1 205 ? -9.42055  27.56117  3.62940   1.000 32.48799 ? 205 THR   A O   1 
ATOM   1596 C  CB  . THR   A 1 205 ? -11.21871 24.99859  4.61087   1.000 33.43473 ? 205 THR   A CB  1 
ATOM   1597 O  OG1 . THR   A 1 205 ? -11.69673 23.70916  4.20364   1.000 33.06834 ? 205 THR   A OG1 1 
ATOM   1598 C  CG2 . THR   A 1 205 ? -12.17756 26.07088  4.11840   1.000 33.24179 ? 205 THR   A CG2 1 
ATOM   1599 N  N   . GLN   A 1 206 ? -8.75781  26.76294  5.62887   1.000 33.76635 ? 206 GLN   A N   1 
ATOM   1600 C  CA  . GLN   A 1 206 ? -8.19368  28.04368  6.04294   1.000 37.54843 ? 206 GLN   A CA  1 
ATOM   1601 C  C   . GLN   A 1 206 ? -7.04790  28.46224  5.13021   1.000 36.04066 ? 206 GLN   A C   1 
ATOM   1602 O  O   . GLN   A 1 206 ? -6.93296  29.63810  4.76312   1.000 35.48541 ? 206 GLN   A O   1 
ATOM   1603 C  CB  . GLN   A 1 206 ? -7.71938  27.95805  7.49420   1.000 37.57939 ? 206 GLN   A CB  1 
ATOM   1604 C  CG  . GLN   A 1 206 ? -7.13990  29.25022  8.03752   1.000 43.19411 ? 206 GLN   A CG  1 
ATOM   1605 C  CD  . GLN   A 1 206 ? -8.20663  30.28389  8.33829   1.000 51.78799 ? 206 GLN   A CD  1 
ATOM   1606 O  OE1 . GLN   A 1 206 ? -8.30087  31.31098  7.66609   1.000 48.41128 ? 206 GLN   A OE1 1 
ATOM   1607 N  NE2 . GLN   A 1 206 ? -9.01533  30.01858  9.35872   1.000 60.30809 ? 206 GLN   A NE2 1 
ATOM   1608 N  N   . PHE   A 1 207 ? -6.19011  27.51157  4.75089   1.000 32.93790 ? 207 PHE   A N   1 
ATOM   1609 C  CA  . PHE   A 1 207 ? -5.08435  27.82660  3.85276   1.000 34.38493 ? 207 PHE   A CA  1 
ATOM   1610 C  C   . PHE   A 1 207 ? -5.57291  28.12635  2.44325   1.000 33.53642 ? 207 PHE   A C   1 
ATOM   1611 O  O   . PHE   A 1 207 ? -4.92801  28.88752  1.71179   1.000 31.94922 ? 207 PHE   A O   1 
ATOM   1612 C  CB  . PHE   A 1 207 ? -4.08064  26.67417  3.82829   1.000 34.10886 ? 207 PHE   A CB  1 
ATOM   1613 C  CG  . PHE   A 1 207 ? -3.13413  26.66908  4.99314   1.000 33.53359 ? 207 PHE   A CG  1 
ATOM   1614 C  CD1 . PHE   A 1 207 ? -2.75644  27.85187  5.60093   1.000 36.85417 ? 207 PHE   A CD1 1 
ATOM   1615 C  CD2 . PHE   A 1 207 ? -2.62036  25.47976  5.48008   1.000 35.88117 ? 207 PHE   A CD2 1 
ATOM   1616 C  CE1 . PHE   A 1 207 ? -1.88419  27.84920  6.67239   1.000 40.72898 ? 207 PHE   A CE1 1 
ATOM   1617 C  CE2 . PHE   A 1 207 ? -1.74615  25.47245  6.55174   1.000 34.57032 ? 207 PHE   A CE2 1 
ATOM   1618 C  CZ  . PHE   A 1 207 ? -1.37897  26.65705  7.14637   1.000 35.44339 ? 207 PHE   A CZ  1 
ATOM   1619 N  N   . GLN   A 1 208 ? -6.70066  27.53898  2.04222   1.000 31.98026 ? 208 GLN   A N   1 
ATOM   1620 C  CA  . GLN   A 1 208 ? -7.24698  27.83406  0.72332   1.000 33.43709 ? 208 GLN   A CA  1 
ATOM   1621 C  C   . GLN   A 1 208 ? -7.83403  29.23795  0.66749   1.000 31.19685 ? 208 GLN   A C   1 
ATOM   1622 O  O   . GLN   A 1 208 ? -7.79760  29.88156  -0.38793  1.000 31.74486 ? 208 GLN   A O   1 
ATOM   1623 C  CB  . GLN   A 1 208 ? -8.28838  26.78085  0.34533   1.000 29.43850 ? 208 GLN   A CB  1 
ATOM   1624 C  CG  . GLN   A 1 208 ? -7.66753  25.40820  0.12412   1.000 30.84495 ? 208 GLN   A CG  1 
ATOM   1625 C  CD  . GLN   A 1 208 ? -8.68593  24.30387  -0.06129  1.000 29.70567 ? 208 GLN   A CD  1 
ATOM   1626 O  OE1 . GLN   A 1 208 ? -9.76458  24.32563  0.53350   1.000 30.09514 ? 208 GLN   A OE1 1 
ATOM   1627 N  NE2 . GLN   A 1 208 ? -8.34295  23.32203  -0.88879  1.000 28.85874 ? 208 GLN   A NE2 1 
ATOM   1628 N  N   . THR   A 1 209 ? -8.36782  29.73048  1.78761   1.000 32.21103 ? 209 THR   A N   1 
ATOM   1629 C  CA  . THR   A 1 209 ? -8.77031  31.13189  1.86072   1.000 33.86646 ? 209 THR   A CA  1 
ATOM   1630 C  C   . THR   A 1 209 ? -7.55121  32.04509  1.87744   1.000 34.33769 ? 209 THR   A C   1 
ATOM   1631 O  O   . THR   A 1 209 ? -7.44048  32.96876  1.06249   1.000 36.33907 ? 209 THR   A O   1 
ATOM   1632 C  CB  . THR   A 1 209 ? -9.63115  31.37217  3.10144   1.000 33.88198 ? 209 THR   A CB  1 
ATOM   1633 O  OG1 . THR   A 1 209 ? -10.86838 30.65907  2.97772   1.000 33.45461 ? 209 THR   A OG1 1 
ATOM   1634 C  CG2 . THR   A 1 209 ? -9.91974  32.86127  3.27284   1.000 35.46302 ? 209 THR   A CG2 1 
ATOM   1635 N  N   . GLU   A 1 210 ? -6.61960  31.79136  2.79259   1.000 36.17448 ? 210 GLU   A N   1 
ATOM   1636 C  CA  . GLU   A 1 210 ? -5.42899  32.61970  2.96949   1.000 37.64863 ? 210 GLU   A CA  1 
ATOM   1637 C  C   . GLU   A 1 210 ? -4.19716  31.72609  2.92376   1.000 36.68942 ? 210 GLU   A C   1 
ATOM   1638 O  O   . GLU   A 1 210 ? -3.90701  31.02271  3.90829   1.000 36.53932 ? 210 GLU   A O   1 
ATOM   1639 C  CB  . GLU   A 1 210 ? -5.49085  33.38471  4.28568   1.000 40.45375 ? 210 GLU   A CB  1 
ATOM   1640 C  CG  . GLU   A 1 210 ? -4.42182  34.44776  4.42967   1.000 44.91744 ? 210 GLU   A CG  1 
ATOM   1641 C  CD  . GLU   A 1 210 ? -4.68555  35.64797  3.54671   1.000 47.51353 ? 210 GLU   A CD  1 
ATOM   1642 O  OE1 . GLU   A 1 210 ? -5.84819  36.10341  3.49561   1.000 52.78463 ? 210 GLU   A OE1 1 
ATOM   1643 O  OE2 . GLU   A 1 210 ? -3.73455  36.12974  2.89646   1.000 53.69747 ? 210 GLU   A OE2 1 
ATOM   1644 N  N   . PRO   A 1 211 ? -3.46611  31.71080  1.80788   1.000 37.05468 ? 211 PRO   A N   1 
ATOM   1645 C  CA  . PRO   A 1 211 ? -2.23885  30.90904  1.73274   1.000 36.96530 ? 211 PRO   A CA  1 
ATOM   1646 C  C   . PRO   A 1 211 ? -1.32478  31.17851  2.91886   1.000 38.42749 ? 211 PRO   A C   1 
ATOM   1647 O  O   . PRO   A 1 211 ? -1.13757  32.32236  3.33559   1.000 40.94766 ? 211 PRO   A O   1 
ATOM   1648 C  CB  . PRO   A 1 211 ? -1.60821  31.36132  0.41247   1.000 35.82218 ? 211 PRO   A CB  1 
ATOM   1649 C  CG  . PRO   A 1 211 ? -2.77820  31.74763  -0.42906  1.000 35.77216 ? 211 PRO   A CG  1 
ATOM   1650 C  CD  . PRO   A 1 211 ? -3.77960  32.36151  0.52285   1.000 37.24548 ? 211 PRO   A CD  1 
ATOM   1651 N  N   . GLY   A 1 212 ? -0.76605  30.10321  3.47586   1.000 38.95961 ? 212 GLY   A N   1 
ATOM   1652 C  CA  . GLY   A 1 212 ? -0.05174  30.17495  4.73222   1.000 42.00522 ? 212 GLY   A CA  1 
ATOM   1653 C  C   . GLY   A 1 212 ? 1.31751   29.52543  4.65099   1.000 39.99017 ? 212 GLY   A C   1 
ATOM   1654 O  O   . GLY   A 1 212 ? 1.71488   28.98357  3.61824   1.000 38.15501 ? 212 GLY   A O   1 
ATOM   1655 N  N   . ALA   A 1 213 ? 2.02266   29.59348  5.77328   1.000 40.30238 ? 213 ALA   A N   1 
ATOM   1656 C  CA  . ALA   A 1 213 ? 3.37437   29.07414  5.88512   1.000 41.04041 ? 213 ALA   A CA  1 
ATOM   1657 C  C   . ALA   A 1 213 ? 3.35038   27.59721  6.26704   1.000 35.44435 ? 213 ALA   A C   1 
ATOM   1658 O  O   . ALA   A 1 213 ? 2.30055   27.01079  6.53716   1.000 35.32721 ? 213 ALA   A O   1 
ATOM   1659 C  CB  . ALA   A 1 213 ? 4.17178   29.87823  6.91210   1.000 40.33067 ? 213 ALA   A CB  1 
ATOM   1660 N  N   . GLY   A 1 214 ? 4.53373   26.99345  6.28275   1.000 34.45932 ? 214 GLY   A N   1 
ATOM   1661 C  CA  . GLY   A 1 214 ? 4.67763   25.61562  6.69490   1.000 34.06924 ? 214 GLY   A CA  1 
ATOM   1662 C  C   . GLY   A 1 214 ? 4.41307   24.63747  5.56589   1.000 33.38863 ? 214 GLY   A C   1 
ATOM   1663 O  O   . GLY   A 1 214 ? 3.91495   24.98100  4.49212   1.000 32.64251 ? 214 GLY   A O   1 
ATOM   1664 N  N   . LEU   A 1 215 ? 4.76109   23.37579  5.83184   1.000 29.28489 ? 215 LEU   A N   1 
ATOM   1665 C  CA  . LEU   A 1 215 ? 4.61119   22.32908  4.82524   1.000 31.09612 ? 215 LEU   A CA  1 
ATOM   1666 C  C   . LEU   A 1 215 ? 3.15347   22.14722  4.41657   1.000 30.42586 ? 215 LEU   A C   1 
ATOM   1667 O  O   . LEU   A 1 215 ? 2.85306   21.97514  3.22936   1.000 28.97369 ? 215 LEU   A O   1 
ATOM   1668 C  CB  . LEU   A 1 215 ? 5.18917   21.01612  5.35283   1.000 30.99943 ? 215 LEU   A CB  1 
ATOM   1669 C  CG  . LEU   A 1 215 ? 5.02053   19.78458  4.46366   1.000 30.01559 ? 215 LEU   A CG  1 
ATOM   1670 C  CD1 . LEU   A 1 215 ? 5.61229   20.02627  3.08726   1.000 30.54157 ? 215 LEU   A CD1 1 
ATOM   1671 C  CD2 . LEU   A 1 215 ? 5.67346   18.58137  5.12111   1.000 30.90886 ? 215 LEU   A CD2 1 
ATOM   1672 N  N   . VAL   A 1 216 ? 2.23318   22.18003  5.38438   1.000 29.80059 ? 216 VAL   A N   1 
ATOM   1673 C  CA  . VAL   A 1 216 ? 0.81632   22.01043  5.06719   1.000 30.33892 ? 216 VAL   A CA  1 
ATOM   1674 C  C   . VAL   A 1 216 ? 0.35243   23.09623  4.10482   1.000 32.27706 ? 216 VAL   A C   1 
ATOM   1675 O  O   . VAL   A 1 216 ? -0.35840  22.81993  3.13019   1.000 28.55050 ? 216 VAL   A O   1 
ATOM   1676 C  CB  . VAL   A 1 216 ? -0.02823  21.99739  6.35598   1.000 29.57382 ? 216 VAL   A CB  1 
ATOM   1677 C  CG1 . VAL   A 1 216 ? -1.50872  21.98188  6.02096   1.000 29.82103 ? 216 VAL   A CG1 1 
ATOM   1678 C  CG2 . VAL   A 1 216 ? 0.33583   20.79911  7.22117   1.000 30.17466 ? 216 VAL   A CG2 1 
ATOM   1679 N  N   . GLY   A 1 217 ? 0.75367   24.34503  4.35673   1.000 30.44782 ? 217 GLY   A N   1 
ATOM   1680 C  CA  . GLY   A 1 217 ? 0.39952   25.42195  3.44673   1.000 31.84684 ? 217 GLY   A CA  1 
ATOM   1681 C  C   . GLY   A 1 217 ? 0.97343   25.22140  2.05757   1.000 32.11824 ? 217 GLY   A C   1 
ATOM   1682 O  O   . GLY   A 1 217 ? 0.31215   25.50376  1.05453   1.000 29.90110 ? 217 GLY   A O   1 
ATOM   1683 N  N   . ALA   A 1 218 ? 2.20851   24.72038  1.97890   1.000 30.35106 ? 218 ALA   A N   1 
ATOM   1684 C  CA  . ALA   A 1 218 ? 2.81452   24.44337  0.68055   1.000 30.44092 ? 218 ALA   A CA  1 
ATOM   1685 C  C   . ALA   A 1 218 ? 2.05371   23.34786  -0.05643  1.000 31.46099 ? 218 ALA   A C   1 
ATOM   1686 O  O   . ALA   A 1 218 ? 1.77803   23.46735  -1.25590  1.000 31.79759 ? 218 ALA   A O   1 
ATOM   1687 C  CB  . ALA   A 1 218 ? 4.28256   24.05638  0.85876   1.000 31.17809 ? 218 ALA   A CB  1 
ATOM   1688 N  N   . LEU   A 1 219 ? 1.70410   22.26786  0.65112   1.000 30.14879 ? 219 LEU   A N   1 
ATOM   1689 C  CA  . LEU   A 1 219 ? 0.96237   21.17624  0.02592   1.000 29.75868 ? 219 LEU   A CA  1 
ATOM   1690 C  C   . LEU   A 1 219 ? -0.41113  21.63839  -0.44647  1.000 31.01304 ? 219 LEU   A C   1 
ATOM   1691 O  O   . LEU   A 1 219 ? -0.90878  21.17801  -1.48120  1.000 29.44262 ? 219 LEU   A O   1 
ATOM   1692 C  CB  . LEU   A 1 219 ? 0.82517   20.00635  1.00311   1.000 28.27343 ? 219 LEU   A CB  1 
ATOM   1693 C  CG  . LEU   A 1 219 ? 2.11275   19.33005  1.47747   1.000 28.88692 ? 219 LEU   A CG  1 
ATOM   1694 C  CD1 . LEU   A 1 219 ? 1.80905   18.27637  2.53489   1.000 29.91111 ? 219 LEU   A CD1 1 
ATOM   1695 C  CD2 . LEU   A 1 219 ? 2.85849   18.71399  0.30832   1.000 31.07711 ? 219 LEU   A CD2 1 
ATOM   1696 N  N   . VAL   A 1 220 ? -1.04318  22.54289  0.30276   1.000 28.20473 ? 220 VAL   A N   1 
ATOM   1697 C  CA  . VAL   A 1 220 ? -2.35299  23.05025  -0.09341  1.000 29.17970 ? 220 VAL   A CA  1 
ATOM   1698 C  C   . VAL   A 1 220 ? -2.23214  23.94519  -1.32184  1.000 30.69883 ? 220 VAL   A C   1 
ATOM   1699 O  O   . VAL   A 1 220 ? -3.04245  23.86018  -2.25238  1.000 32.45493 ? 220 VAL   A O   1 
ATOM   1700 C  CB  . VAL   A 1 220 ? -3.01373  23.78946  1.08581   1.000 30.03403 ? 220 VAL   A CB  1 
ATOM   1701 C  CG1 . VAL   A 1 220 ? -4.23280  24.56261  0.61682   1.000 30.62427 ? 220 VAL   A CG1 1 
ATOM   1702 C  CG2 . VAL   A 1 220 ? -3.40064  22.80810  2.17918   1.000 30.45391 ? 220 VAL   A CG2 1 
ATOM   1703 N  N   . ALA   A 1 221 ? -1.21289  24.80498  -1.35402  1.000 28.85519 ? 221 ALA   A N   1 
ATOM   1704 C  CA  . ALA   A 1 221 ? -1.09991  25.77287  -2.43829  1.000 31.83277 ? 221 ALA   A CA  1 
ATOM   1705 C  C   . ALA   A 1 221 ? -0.63472  25.12742  -3.73757  1.000 32.49975 ? 221 ALA   A C   1 
ATOM   1706 O  O   . ALA   A 1 221 ? -0.94971  25.63124  -4.82044  1.000 30.19020 ? 221 ALA   A O   1 
ATOM   1707 C  CB  . ALA   A 1 221 ? -0.14738  26.90024  -2.03893  1.000 31.94872 ? 221 ALA   A CB  1 
ATOM   1708 N  N   . ASP   A 1 222 ? 0.10541   24.02177  -3.65881  1.000 31.83461 ? 222 ASP   A N   1 
ATOM   1709 C  CA  . ASP   A 1 222 ? 0.67752   23.42301  -4.85790  1.000 30.82118 ? 222 ASP   A CA  1 
ATOM   1710 C  C   . ASP   A 1 222 ? 0.01715   22.09443  -5.21033  1.000 32.14984 ? 222 ASP   A C   1 
ATOM   1711 O  O   . ASP   A 1 222 ? -0.82338  22.04125  -6.11412  1.000 31.59902 ? 222 ASP   A O   1 
ATOM   1712 C  CB  . ASP   A 1 222 ? 2.18595   23.23237  -4.68622  1.000 33.03282 ? 222 ASP   A CB  1 
ATOM   1713 C  CG  . ASP   A 1 222 ? 2.88577   22.90013  -5.99389  1.000 35.56299 ? 222 ASP   A CG  1 
ATOM   1714 O  OD1 . ASP   A 1 222 ? 2.21684   22.88850  -7.05004  1.000 36.15306 ? 222 ASP   A OD1 1 
ATOM   1715 O  OD2 . ASP   A 1 222 ? 4.10912   22.65235  -5.96609  1.000 37.17470 ? 222 ASP   A OD2 1 
ATOM   1716 N  N   . GLN   A 1 223 ? 0.39234   21.02169  -4.50492  1.000 30.45877 ? 223 GLN   A N   1 
ATOM   1717 C  CA  . GLN   A 1 223 ? -0.01776  19.67649  -4.90699  1.000 32.62807 ? 223 GLN   A CA  1 
ATOM   1718 C  C   . GLN   A 1 223 ? -1.53247  19.50622  -4.85559  1.000 31.76970 ? 223 GLN   A C   1 
ATOM   1719 O  O   . GLN   A 1 223 ? -2.13425  18.94405  -5.77828  1.000 30.61155 ? 223 GLN   A O   1 
ATOM   1720 C  CB  . GLN   A 1 223 ? 0.66516   18.62703  -4.02785  1.000 30.73783 ? 223 GLN   A CB  1 
ATOM   1721 C  CG  . GLN   A 1 223 ? 2.11680   18.35197  -4.38412  1.000 31.47127 ? 223 GLN   A CG  1 
ATOM   1722 C  CD  . GLN   A 1 223 ? 3.07248   19.33810  -3.75034  1.000 32.67286 ? 223 GLN   A CD  1 
ATOM   1723 O  OE1 . GLN   A 1 223 ? 2.65426   20.30720  -3.11856  1.000 29.89426 ? 223 GLN   A OE1 1 
ATOM   1724 N  NE2 . GLN   A 1 223 ? 4.36719   19.09140  -3.90955  1.000 32.15826 ? 223 GLN   A NE2 1 
ATOM   1725 N  N   . LEU   A 1 224 ? -2.16897  19.96892  -3.77613  1.000 31.10622 ? 224 LEU   A N   1 
ATOM   1726 C  CA  . LEU   A 1 224 ? -3.61797  19.81603  -3.67112  1.000 29.94801 ? 224 LEU   A CA  1 
ATOM   1727 C  C   . LEU   A 1 224 ? -4.33317  20.59053  -4.77226  1.000 29.62321 ? 224 LEU   A C   1 
ATOM   1728 O  O   . LEU   A 1 224 ? -5.27463  20.07959  -5.39125  1.000 30.33720 ? 224 LEU   A O   1 
ATOM   1729 C  CB  . LEU   A 1 224 ? -4.10463  20.26396  -2.29174  1.000 28.53398 ? 224 LEU   A CB  1 
ATOM   1730 C  CG  . LEU   A 1 224 ? -5.61522  20.14155  -2.06126  1.000 30.25735 ? 224 LEU   A CG  1 
ATOM   1731 C  CD1 . LEU   A 1 224 ? -6.08136  18.70193  -2.26202  1.000 28.41931 ? 224 LEU   A CD1 1 
ATOM   1732 C  CD2 . LEU   A 1 224 ? -5.99954  20.64384  -0.67906  1.000 27.19757 ? 224 LEU   A CD2 1 
ATOM   1733 N  N   . ALA   A 1 225 ? -3.88934  21.81948  -5.04197  1.000 29.38149 ? 225 ALA   A N   1 
ATOM   1734 C  CA  . ALA   A 1 225 ? -4.51346  22.63367  -6.07816  1.000 30.29929 ? 225 ALA   A CA  1 
ATOM   1735 C  C   . ALA   A 1 225 ? -4.29796  22.06821  -7.47691  1.000 28.86199 ? 225 ALA   A C   1 
ATOM   1736 O  O   . ALA   A 1 225 ? -5.07118  22.38751  -8.38672  1.000 27.59962 ? 225 ALA   A O   1 
ATOM   1737 C  CB  . ALA   A 1 225 ? -3.98362  24.06539  -6.00824  1.000 29.62220 ? 225 ALA   A CB  1 
ATOM   1738 N  N   . ASN   A 1 226 ? -3.27002  21.24533  -7.67265  1.000 31.36875 ? 226 ASN   A N   1 
ATOM   1739 C  CA  . ASN   A 1 226 ? -3.03221  20.57686  -8.94452  1.000 32.04391 ? 226 ASN   A CA  1 
ATOM   1740 C  C   . ASN   A 1 226 ? -3.58240  19.15558  -8.97494  1.000 30.95171 ? 226 ASN   A C   1 
ATOM   1741 O  O   . ASN   A 1 226 ? -3.36675  18.44038  -9.95886  1.000 32.44125 ? 226 ASN   A O   1 
ATOM   1742 C  CB  . ASN   A 1 226 ? -1.53482  20.56684  -9.26284  1.000 33.35896 ? 226 ASN   A CB  1 
ATOM   1743 C  CG  . ASN   A 1 226 ? -1.03667  21.90680  -9.76929  1.000 35.66910 ? 226 ASN   A CG  1 
ATOM   1744 O  OD1 . ASN   A 1 226 ? -0.98840  22.14718  -10.97664 1.000 35.67765 ? 226 ASN   A OD1 1 
ATOM   1745 N  ND2 . ASN   A 1 226 ? -0.66349  22.78862  -8.84744  1.000 35.08352 ? 226 ASN   A ND2 1 
ATOM   1746 N  N   . GLY   A 1 227 ? -4.28672  18.73267  -7.92709  1.000 30.27117 ? 227 GLY   A N   1 
ATOM   1747 C  CA  . GLY   A 1 227 ? -4.87876  17.40559  -7.90531  1.000 31.98973 ? 227 GLY   A CA  1 
ATOM   1748 C  C   . GLY   A 1 227 ? -3.88704  16.26734  -7.86766  1.000 32.81669 ? 227 GLY   A C   1 
ATOM   1749 O  O   . GLY   A 1 227 ? -4.22650  15.14479  -8.25444  1.000 34.31006 ? 227 GLY   A O   1 
ATOM   1750 N  N   . GLU   A 1 228 ? -2.66228  16.52606  -7.41297  1.000 32.70186 ? 228 GLU   A N   1 
ATOM   1751 C  CA  . GLU   A 1 228 ? -1.62404  15.50858  -7.35183  1.000 35.11569 ? 228 GLU   A CA  1 
ATOM   1752 C  C   . GLU   A 1 228 ? -1.59912  14.77872  -6.01824  1.000 34.05607 ? 228 GLU   A C   1 
ATOM   1753 O  O   . GLU   A 1 228 ? -0.96241  13.72428  -5.91180  1.000 35.94349 ? 228 GLU   A O   1 
ATOM   1754 C  CB  . GLU   A 1 228 ? -0.26083  16.14226  -7.63646  1.000 34.88402 ? 228 GLU   A CB  1 
ATOM   1755 C  CG  . GLU   A 1 228 ? -0.11903  16.61292  -9.07375  1.000 35.94395 ? 228 GLU   A CG  1 
ATOM   1756 C  CD  . GLU   A 1 228 ? 1.03962   17.56649  -9.27134  1.000 38.60122 ? 228 GLU   A CD  1 
ATOM   1757 O  OE1 . GLU   A 1 228 ? 1.55679   18.09221  -8.26479  1.000 37.08397 ? 228 GLU   A OE1 1 
ATOM   1758 O  OE2 . GLU   A 1 228 ? 1.43265   17.79047  -10.43568 1.000 43.97824 ? 228 GLU   A OE2 1 
ATOM   1759 N  N   . ILE   A 1 229 ? -2.27309  15.31521  -5.00727  1.000 31.42788 ? 229 ILE   A N   1 
ATOM   1760 C  CA  . ILE   A 1 229 ? -2.52216  14.61736  -3.75553  1.000 31.28423 ? 229 ILE   A CA  1 
ATOM   1761 C  C   . ILE   A 1 229 ? -4.00368  14.77211  -3.44158  1.000 32.31406 ? 229 ILE   A C   1 
ATOM   1762 O  O   . ILE   A 1 229 ? -4.60657  15.80490  -3.75150  1.000 31.77986 ? 229 ILE   A O   1 
ATOM   1763 C  CB  . ILE   A 1 229 ? -1.63755  15.15764  -2.60553  1.000 33.83045 ? 229 ILE   A CB  1 
ATOM   1764 C  CG1 . ILE   A 1 229 ? -1.76953  14.28956  -1.35287  1.000 32.61423 ? 229 ILE   A CG1 1 
ATOM   1765 C  CG2 . ILE   A 1 229 ? -1.98406  16.60351  -2.27126  1.000 29.70236 ? 229 ILE   A CG2 1 
ATOM   1766 C  CD1 . ILE   A 1 229 ? -0.77906  14.64082  -0.24944  1.000 30.14001 ? 229 ILE   A CD1 1 
ATOM   1767 N  N   . ASP   A 1 230 ? -4.60072  13.73301  -2.86985  1.000 32.16772 ? 230 ASP   A N   1 
ATOM   1768 C  CA  . ASP   A 1 230 ? -5.97937  13.83536  -2.42071  1.000 32.72554 ? 230 ASP   A CA  1 
ATOM   1769 C  C   . ASP   A 1 230 ? -6.05156  14.65107  -1.13639  1.000 33.20822 ? 230 ASP   A C   1 
ATOM   1770 O  O   . ASP   A 1 230 ? -5.08866  14.72240  -0.36613  1.000 30.91711 ? 230 ASP   A O   1 
ATOM   1771 C  CB  . ASP   A 1 230 ? -6.58299  12.44975  -2.19398  1.000 34.14668 ? 230 ASP   A CB  1 
ATOM   1772 C  CG  . ASP   A 1 230 ? -6.76367  11.67260  -3.48874  1.000 34.35384 ? 230 ASP   A CG  1 
ATOM   1773 O  OD1 . ASP   A 1 230 ? -6.84100  12.30994  -4.56383  1.000 36.03380 ? 230 ASP   A OD1 1 
ATOM   1774 O  OD2 . ASP   A 1 230 ? -6.83265  10.42579  -3.43083  1.000 35.01000 ? 230 ASP   A OD2 1 
ATOM   1775 N  N   . ARG   A 1 231 ? -7.21090  15.27579  -0.91315  1.000 31.84105 ? 231 ARG   A N   1 
ATOM   1776 C  CA  . ARG   A 1 231 ? -7.40487  16.06012  0.30317   1.000 34.44430 ? 231 ARG   A CA  1 
ATOM   1777 C  C   . ARG   A 1 231 ? -7.24524  15.19991  1.55093   1.000 33.47418 ? 231 ARG   A C   1 
ATOM   1778 O  O   . ARG   A 1 231 ? -6.75566  15.67768  2.57907   1.000 32.17248 ? 231 ARG   A O   1 
ATOM   1779 C  CB  . ARG   A 1 231 ? -8.78392  16.72128  0.28312   1.000 33.95953 ? 231 ARG   A CB  1 
ATOM   1780 C  CG  . ARG   A 1 231 ? -9.00410  17.73802  1.38344   1.000 33.51743 ? 231 ARG   A CG  1 
ATOM   1781 C  CD  . ARG   A 1 231 ? -10.34541 18.44286  1.22842   1.000 33.48093 ? 231 ARG   A CD  1 
ATOM   1782 N  NE  . ARG   A 1 231 ? -10.54536 19.45261  2.26541   1.000 34.42323 ? 231 ARG   A NE  1 
ATOM   1783 C  CZ  . ARG   A 1 231 ? -10.52713 20.76541  2.05804   1.000 32.47002 ? 231 ARG   A CZ  1 
ATOM   1784 N  NH1 . ARG   A 1 231 ? -10.33664 21.25296  0.84000   1.000 29.94910 ? 231 ARG   A NH1 1 
ATOM   1785 N  NH2 . ARG   A 1 231 ? -10.71556 21.59528  3.07520   1.000 34.20686 ? 231 ARG   A NH2 1 
ATOM   1786 N  N   A GLU   A 1 232 ? -7.64427  13.92856  1.48151   0.500 34.26493 ? 232 GLU   A N   1 
ATOM   1787 N  N   B GLU   A 1 232 ? -7.63182  13.92893  1.47223   0.500 34.26967 ? 232 GLU   A N   1 
ATOM   1788 C  CA  A GLU   A 1 232 ? -7.52758  13.04256  2.63249   0.500 34.92629 ? 232 GLU   A CA  1 
ATOM   1789 C  CA  B GLU   A 1 232 ? -7.53587  13.03064  2.61338   0.500 34.92106 ? 232 GLU   A CA  1 
ATOM   1790 C  C   A GLU   A 1 232 ? -6.13447  12.44165  2.77215   0.500 32.85803 ? 232 GLU   A C   1 
ATOM   1791 C  C   B GLU   A 1 232 ? -6.14219  12.43778  2.76811   0.500 32.86424 ? 232 GLU   A C   1 
ATOM   1792 O  O   A GLU   A 1 232 ? -5.75543  12.04653  3.87991   0.500 33.39466 ? 232 GLU   A O   1 
ATOM   1793 O  O   B GLU   A 1 232 ? -5.76602  12.05913  3.88306   0.500 33.08377 ? 232 GLU   A O   1 
ATOM   1794 C  CB  A GLU   A 1 232 ? -8.57152  11.92841  2.54520   0.500 35.36731 ? 232 GLU   A CB  1 
ATOM   1795 C  CB  B GLU   A 1 232 ? -8.58242  11.92015  2.49018   0.500 34.95845 ? 232 GLU   A CB  1 
ATOM   1796 C  CG  A GLU   A 1 232 ? -10.01116 12.42858  2.55381   0.500 35.82075 ? 232 GLU   A CG  1 
ATOM   1797 C  CG  B GLU   A 1 232 ? -10.02166 12.41684  2.62476   0.500 35.82196 ? 232 GLU   A CG  1 
ATOM   1798 C  CD  A GLU   A 1 232 ? -10.40447 13.09598  3.86277   0.500 35.75141 ? 232 GLU   A CD  1 
ATOM   1799 C  CD  B GLU   A 1 232 ? -10.45008 13.29895  1.46535   0.500 35.94844 ? 232 GLU   A CD  1 
ATOM   1800 O  OE1 A GLU   A 1 232 ? -9.98457  12.61253  4.93629   0.500 35.89494 ? 232 GLU   A OE1 1 
ATOM   1801 O  OE1 B GLU   A 1 232 ? -10.05423 12.99632  0.31919   0.500 34.24928 ? 232 GLU   A OE1 1 
ATOM   1802 O  OE2 A GLU   A 1 232 ? -11.13546 14.10741  3.81671   0.500 43.74928 ? 232 GLU   A OE2 1 
ATOM   1803 O  OE2 B GLU   A 1 232 ? -11.16219 14.30008  1.69887   0.500 43.74928 ? 232 GLU   A OE2 1 
ATOM   1804 N  N   . GLU   A 1 233 ? -5.36723  12.35817  1.68222   1.000 33.01227 ? 233 GLU   A N   1 
ATOM   1805 C  CA  . GLU   A 1 233 ? -3.96234  11.98378  1.80647   1.000 32.54403 ? 233 GLU   A CA  1 
ATOM   1806 C  C   . GLU   A 1 233 ? -3.16907  13.08476  2.49904   1.000 30.24578 ? 233 GLU   A C   1 
ATOM   1807 O  O   . GLU   A 1 233 ? -2.27117  12.80209  3.30069   1.000 30.16730 ? 233 GLU   A O   1 
ATOM   1808 C  CB  . GLU   A 1 233 ? -3.35532  11.70290  0.43659   1.000 32.03855 ? 233 GLU   A CB  1 
ATOM   1809 C  CG  . GLU   A 1 233 ? -3.86543  10.47819  -0.28376  1.000 32.54743 ? 233 GLU   A CG  1 
ATOM   1810 C  CD  . GLU   A 1 233 ? -3.11616  10.24909  -1.58278  1.000 35.80405 ? 233 GLU   A CD  1 
ATOM   1811 O  OE1 . GLU   A 1 233 ? -2.21885  9.37778   -1.61104  1.000 36.13116 ? 233 GLU   A OE1 1 
ATOM   1812 O  OE2 . GLU   A 1 233 ? -3.40654  10.96617  -2.56596  1.000 33.54595 ? 233 GLU   A OE2 1 
ATOM   1813 N  N   . LEU   A 1 234 ? -3.46670  14.34695  2.17378   1.000 32.19611 ? 234 LEU   A N   1 
ATOM   1814 C  CA  . LEU   A 1 234 ? -2.82899  15.46484  2.86091   1.000 29.31003 ? 234 LEU   A CA  1 
ATOM   1815 C  C   . LEU   A 1 234 ? -3.11248  15.40794  4.35494   1.000 26.81497 ? 234 LEU   A C   1 
ATOM   1816 O  O   . LEU   A 1 234 ? -2.21013  15.61103  5.17584   1.000 28.46132 ? 234 LEU   A O   1 
ATOM   1817 C  CB  . LEU   A 1 234 ? -3.31493  16.78981  2.26284   1.000 28.49954 ? 234 LEU   A CB  1 
ATOM   1818 C  CG  . LEU   A 1 234 ? -2.39145  18.01881  2.27773   1.000 29.41744 ? 234 LEU   A CG  1 
ATOM   1819 C  CD1 . LEU   A 1 234 ? -2.99585  19.15605  1.45999   1.000 27.40729 ? 234 LEU   A CD1 1 
ATOM   1820 C  CD2 . LEU   A 1 234 ? -2.07316  18.50236  3.68527   1.000 28.83209 ? 234 LEU   A CD2 1 
ATOM   1821 N  N   . ILE   A 1 235 ? -4.36312  15.12332  4.72187   1.000 29.58417 ? 235 ILE   A N   1 
ATOM   1822 C  CA  . ILE   A 1 235 ? -4.72680  14.99332  6.12943   1.000 29.24236 ? 235 ILE   A CA  1 
ATOM   1823 C  C   . ILE   A 1 235 ? -3.91737  13.88292  6.78917   1.000 31.83994 ? 235 ILE   A C   1 
ATOM   1824 O  O   . ILE   A 1 235 ? -3.34959  14.06456  7.87348   1.000 29.52650 ? 235 ILE   A O   1 
ATOM   1825 C  CB  . ILE   A 1 235 ? -6.23973  14.74848  6.26412   1.000 30.56574 ? 235 ILE   A CB  1 
ATOM   1826 C  CG1 . ILE   A 1 235 ? -7.01759  16.01800  5.90675   1.000 32.86393 ? 235 ILE   A CG1 1 
ATOM   1827 C  CG2 . ILE   A 1 235 ? -6.58623  14.27085  7.66386   1.000 33.46944 ? 235 ILE   A CG2 1 
ATOM   1828 C  CD1 . ILE   A 1 235 ? -8.52013  15.86123  6.00781   1.000 33.37608 ? 235 ILE   A CD1 1 
ATOM   1829 N  N   . SER   A 1 236 ? -3.84632  12.71705  6.13926   1.000 29.54668 ? 236 SER   A N   1 
ATOM   1830 C  CA  . SER   A 1 236 ? -3.10239  11.59526  6.70695   1.000 31.30643 ? 236 SER   A CA  1 
ATOM   1831 C  C   . SER   A 1 236 ? -1.61457  11.90678  6.80725   1.000 28.79275 ? 236 SER   A C   1 
ATOM   1832 O  O   . SER   A 1 236 ? -0.96154  11.53882  7.79125   1.000 30.36816 ? 236 SER   A O   1 
ATOM   1833 C  CB  . SER   A 1 236 ? -3.32260  10.33625  5.86749   1.000 31.66672 ? 236 SER   A CB  1 
ATOM   1834 O  OG  . SER   A 1 236 ? -4.68998  9.97294   5.84154   1.000 33.86974 ? 236 SER   A OG  1 
ATOM   1835 N  N   . THR   A 1 237 ? -1.05931  12.57713  5.79458   1.000 29.04551 ? 237 THR   A N   1 
ATOM   1836 C  CA  . THR   A 1 237 ? 0.36300   12.90408  5.81102   1.000 29.14517 ? 237 THR   A CA  1 
ATOM   1837 C  C   . THR   A 1 237 ? 0.67874   13.91864  6.90349   1.000 28.75239 ? 237 THR   A C   1 
ATOM   1838 O  O   . THR   A 1 237 ? 1.60847   13.72432  7.69629   1.000 28.60130 ? 237 THR   A O   1 
ATOM   1839 C  CB  . THR   A 1 237 ? 0.79424   13.43707  4.44438   1.000 29.27288 ? 237 THR   A CB  1 
ATOM   1840 O  OG1 . THR   A 1 237 ? 0.40614   12.50887  3.42476   1.000 29.41040 ? 237 THR   A OG1 1 
ATOM   1841 C  CG2 . THR   A 1 237 ? 2.30303   13.62990  4.40089   1.000 27.94936 ? 237 THR   A CG2 1 
ATOM   1842 N  N   . ALA   A 1 238 ? -0.08503  15.01425  6.95340   1.000 28.40141 ? 238 ALA   A N   1 
ATOM   1843 C  CA  . ALA   A 1 238 ? 0.10477   16.00898  8.00440   1.000 28.81886 ? 238 ALA   A CA  1 
ATOM   1844 C  C   . ALA   A 1 238 ? -0.06444  15.38931  9.38469   1.000 27.74889 ? 238 ALA   A C   1 
ATOM   1845 O  O   . ALA   A 1 238 ? 0.69649   15.69778  10.30992  1.000 29.57598 ? 238 ALA   A O   1 
ATOM   1846 C  CB  . ALA   A 1 238 ? -0.87682  17.16483  7.81525   1.000 27.01563 ? 238 ALA   A CB  1 
ATOM   1847 N  N   . MET   A 1 239 ? -1.05386  14.50490  9.54060   1.000 27.64435 ? 239 MET   A N   1 
ATOM   1848 C  CA  . MET   A 1 239 ? -1.26645  13.85823  10.83174  1.000 28.02661 ? 239 MET   A CA  1 
ATOM   1849 C  C   . MET   A 1 239 ? -0.08841  12.96895  11.20271  1.000 29.14642 ? 239 MET   A C   1 
ATOM   1850 O  O   . MET   A 1 239 ? 0.33286   12.94418  12.36481  1.000 28.01458 ? 239 MET   A O   1 
ATOM   1851 C  CB  . MET   A 1 239 ? -2.56052  13.04593  10.81435  1.000 29.74044 ? 239 MET   A CB  1 
ATOM   1852 C  CG  . MET   A 1 239 ? -2.92833  12.46664  12.17245  1.000 31.72915 ? 239 MET   A CG  1 
ATOM   1853 S  SD  . MET   A 1 239 ? -4.40164  11.43266  12.14494  1.000 38.33678 ? 239 MET   A SD  1 
ATOM   1854 C  CE  . MET   A 1 239 ? -5.53839  12.48956  11.25667  1.000 35.42417 ? 239 MET   A CE  1 
ATOM   1855 N  N   . LEU   A 1 240 ? 0.45095   12.22574  10.23110  1.000 28.40221 ? 240 LEU   A N   1 
ATOM   1856 C  CA  . LEU   A 1 240 ? 1.63067   11.40700  10.49259  1.000 26.89686 ? 240 LEU   A CA  1 
ATOM   1857 C  C   . LEU   A 1 240 ? 2.78493   12.26246  10.99969  1.000 30.48766 ? 240 LEU   A C   1 
ATOM   1858 O  O   . LEU   A 1 240 ? 3.41213   11.94210  12.01455  1.000 28.30642 ? 240 LEU   A O   1 
ATOM   1859 C  CB  . LEU   A 1 240 ? 2.03829   10.65097  9.22748   1.000 29.51732 ? 240 LEU   A CB  1 
ATOM   1860 C  CG  . LEU   A 1 240 ? 3.38008   9.91247   9.26989   1.000 30.81680 ? 240 LEU   A CG  1 
ATOM   1861 C  CD1 . LEU   A 1 240 ? 3.35385   8.76790   10.27732  1.000 31.20962 ? 240 LEU   A CD1 1 
ATOM   1862 C  CD2 . LEU   A 1 240 ? 3.76510   9.40518   7.88186   1.000 27.50456 ? 240 LEU   A CD2 1 
ATOM   1863 N  N   . LEU   A 1 241 ? 3.06909   13.36904  10.30935  1.000 27.20957 ? 241 LEU   A N   1 
ATOM   1864 C  CA  . LEU   A 1 241 ? 4.17266   14.23236  10.71855  1.000 27.75586 ? 241 LEU   A CA  1 
ATOM   1865 C  C   . LEU   A 1 241 ? 3.88415   14.91171  12.05168  1.000 27.46154 ? 241 LEU   A C   1 
ATOM   1866 O  O   . LEU   A 1 241 ? 4.79480   15.09907  12.86793  1.000 27.56060 ? 241 LEU   A O   1 
ATOM   1867 C  CB  . LEU   A 1 241 ? 4.44987   15.27374  9.63570   1.000 26.83890 ? 241 LEU   A CB  1 
ATOM   1868 C  CG  . LEU   A 1 241 ? 4.74066   14.74302  8.23256   1.000 29.23094 ? 241 LEU   A CG  1 
ATOM   1869 C  CD1 . LEU   A 1 241 ? 4.85915   15.89068  7.24863   1.000 26.64714 ? 241 LEU   A CD1 1 
ATOM   1870 C  CD2 . LEU   A 1 241 ? 6.00039   13.89528  8.21416   1.000 28.03056 ? 241 LEU   A CD2 1 
ATOM   1871 N  N   . LEU   A 1 242 ? 2.62418   15.28469  12.29013  1.000 27.43876 ? 242 LEU   A N   1 
ATOM   1872 C  CA  . LEU   A 1 242 ? 2.26510   15.96708  13.53105  1.000 29.80984 ? 242 LEU   A CA  1 
ATOM   1873 C  C   . LEU   A 1 242 ? 2.45918   15.05773  14.74010  1.000 30.48398 ? 242 LEU   A C   1 
ATOM   1874 O  O   . LEU   A 1 242 ? 3.12141   15.43301  15.71471  1.000 30.68385 ? 242 LEU   A O   1 
ATOM   1875 C  CB  . LEU   A 1 242 ? 0.81909   16.45565  13.45280  1.000 28.07519 ? 242 LEU   A CB  1 
ATOM   1876 C  CG  . LEU   A 1 242 ? 0.32265   17.36900  14.57394  1.000 31.80931 ? 242 LEU   A CG  1 
ATOM   1877 C  CD1 . LEU   A 1 242 ? 1.16271   18.63263  14.63604  1.000 32.39148 ? 242 LEU   A CD1 1 
ATOM   1878 C  CD2 . LEU   A 1 242 ? -1.14090  17.71681  14.36720  1.000 30.81420 ? 242 LEU   A CD2 1 
ATOM   1879 N  N   . ILE   A 1 243 ? 1.87871   13.85662  14.69775  1.000 30.68347 ? 243 ILE   A N   1 
ATOM   1880 C  CA  . ILE   A 1 243 ? 2.01423   12.92241  15.81439  1.000 29.87064 ? 243 ILE   A CA  1 
ATOM   1881 C  C   . ILE   A 1 243 ? 3.47028   12.50626  15.98288  1.000 29.07652 ? 243 ILE   A C   1 
ATOM   1882 O  O   . ILE   A 1 243 ? 4.01876   12.53231  17.09115  1.000 30.70302 ? 243 ILE   A O   1 
ATOM   1883 C  CB  . ILE   A 1 243 ? 1.09476   11.70532  15.60748  1.000 32.19127 ? 243 ILE   A CB  1 
ATOM   1884 C  CG1 . ILE   A 1 243 ? -0.36850  12.15026  15.55783  1.000 31.99585 ? 243 ILE   A CG1 1 
ATOM   1885 C  CG2 . ILE   A 1 243 ? 1.30436   10.67311  16.71111  1.000 35.41058 ? 243 ILE   A CG2 1 
ATOM   1886 C  CD1 . ILE   A 1 243 ? -1.32400  11.03791  15.18779  1.000 36.31908 ? 243 ILE   A CD1 1 
ATOM   1887 N  N   . ALA   A 1 244 ? 4.12221   12.12583  14.88093  1.000 31.79784 ? 244 ALA   A N   1 
ATOM   1888 C  CA  . ALA   A 1 244 ? 5.52904   11.74108  14.94730  1.000 30.47808 ? 244 ALA   A CA  1 
ATOM   1889 C  C   . ALA   A 1 244 ? 6.38797   12.86696  15.50541  1.000 29.81896 ? 244 ALA   A C   1 
ATOM   1890 O  O   . ALA   A 1 244 ? 7.27828   12.62749  16.33000  1.000 29.32024 ? 244 ALA   A O   1 
ATOM   1891 C  CB  . ALA   A 1 244 ? 6.03294   11.34154  13.56361  1.000 29.15826 ? 244 ALA   A CB  1 
ATOM   1892 N  N   . GLY   A 1 245 ? 6.14938   14.09916  15.05003  1.000 28.81165 ? 245 GLY   A N   1 
ATOM   1893 C  CA  . GLY   A 1 245 ? 6.91628   15.22357  15.55885  1.000 30.30664 ? 245 GLY   A CA  1 
ATOM   1894 C  C   . GLY   A 1 245 ? 6.73945   15.41991  17.05110  1.000 29.58855 ? 245 GLY   A C   1 
ATOM   1895 O  O   . GLY   A 1 245 ? 7.70204   15.70477  17.76475  1.000 34.39856 ? 245 GLY   A O   1 
ATOM   1896 N  N   . HIS   A 1 246 ? 5.51015   15.24922  17.54429  1.000 31.11942 ? 246 HIS   A N   1 
ATOM   1897 C  CA  . HIS   A 1 246 ? 5.25090   15.35805  18.97822  1.000 31.73659 ? 246 HIS   A CA  1 
ATOM   1898 C  C   . HIS   A 1 246 ? 5.88225   14.20553  19.74905  1.000 32.49035 ? 246 HIS   A C   1 
ATOM   1899 O  O   . HIS   A 1 246 ? 6.70571   14.41352  20.64767  1.000 29.24502 ? 246 HIS   A O   1 
ATOM   1900 C  CB  . HIS   A 1 246 ? 3.74592   15.37465  19.24811  1.000 33.83995 ? 246 HIS   A CB  1 
ATOM   1901 C  CG  . HIS   A 1 246 ? 3.09313   16.69251  18.99500  1.000 33.40773 ? 246 HIS   A CG  1 
ATOM   1902 N  ND1 . HIS   A 1 246 ? 3.03303   17.26835  17.74430  1.000 38.96075 ? 246 HIS   A ND1 1 
ATOM   1903 C  CD2 . HIS   A 1 246 ? 2.44142   17.53469  19.83029  1.000 38.49277 ? 246 HIS   A CD2 1 
ATOM   1904 C  CE1 . HIS   A 1 246 ? 2.38606   18.41827  17.82391  1.000 37.32491 ? 246 HIS   A CE1 1 
ATOM   1905 N  NE2 . HIS   A 1 246 ? 2.01608   18.60314  19.07836  1.000 37.99863 ? 246 HIS   A NE2 1 
ATOM   1906 N  N   . GLU   A 1 247 ? 5.50005   12.97300  19.40936  1.000 30.67239 ? 247 GLU   A N   1 
ATOM   1907 C  CA  . GLU   A 1 247 ? 5.58600   11.88103  20.37216  1.000 31.15456 ? 247 GLU   A CA  1 
ATOM   1908 C  C   . GLU   A 1 247 ? 6.95544   11.20961  20.39650  1.000 31.12670 ? 247 GLU   A C   1 
ATOM   1909 O  O   . GLU   A 1 247 ? 7.44649   10.85364  21.47416  1.000 32.84643 ? 247 GLU   A O   1 
ATOM   1910 C  CB  . GLU   A 1 247 ? 4.48865   10.85610  20.08305  1.000 32.89326 ? 247 GLU   A CB  1 
ATOM   1911 C  CG  . GLU   A 1 247 ? 3.11042   11.47338  20.01774  1.000 34.89335 ? 247 GLU   A CG  1 
ATOM   1912 C  CD  . GLU   A 1 247 ? 2.62864   11.98914  21.36615  1.000 36.04236 ? 247 GLU   A CD  1 
ATOM   1913 O  OE1 . GLU   A 1 247 ? 3.19382   11.58466  22.40636  1.000 34.18952 ? 247 GLU   A OE1 1 
ATOM   1914 O  OE2 . GLU   A 1 247 ? 1.67356   12.79635  21.38397  1.000 37.72363 ? 247 GLU   A OE2 1 
ATOM   1915 N  N   . THR   A 1 248 ? 7.56775   10.98512  19.23276  1.000 30.11136 ? 248 THR   A N   1 
ATOM   1916 C  CA  . THR   A 1 248 ? 8.83754   10.26671  19.19696  1.000 29.62453 ? 248 THR   A CA  1 
ATOM   1917 C  C   . THR   A 1 248 ? 9.92258   11.02320  19.95571  1.000 29.11125 ? 248 THR   A C   1 
ATOM   1918 O  O   . THR   A 1 248 ? 10.61679  10.45086  20.80315  1.000 31.33040 ? 248 THR   A O   1 
ATOM   1919 C  CB  . THR   A 1 248 ? 9.25477   10.02866  17.74809  1.000 30.42812 ? 248 THR   A CB  1 
ATOM   1920 O  OG1 . THR   A 1 248 ? 9.50440   11.28855  17.11443  1.000 31.08238 ? 248 THR   A OG1 1 
ATOM   1921 C  CG2 . THR   A 1 248 ? 8.15506   9.28897   16.99037  1.000 28.75243 ? 248 THR   A CG2 1 
ATOM   1922 N  N   . THR   A 1 249 ? 10.07853  12.31759  19.66667  1.000 29.07433 ? 249 THR   A N   1 
ATOM   1923 C  CA  . THR   A 1 249 ? 11.12415  13.10121  20.31630  1.000 28.72121 ? 249 THR   A CA  1 
ATOM   1924 C  C   . THR   A 1 249 ? 10.88264  13.21882  21.81572  1.000 25.96676 ? 249 THR   A C   1 
ATOM   1925 O  O   . THR   A 1 249 ? 11.82680  13.11842  22.60740  1.000 29.00595 ? 249 THR   A O   1 
ATOM   1926 C  CB  . THR   A 1 249 ? 11.21768  14.48419  19.67234  1.000 28.63938 ? 249 THR   A CB  1 
ATOM   1927 O  OG1 . THR   A 1 249 ? 11.80741  14.36328  18.37219  1.000 29.82781 ? 249 THR   A OG1 1 
ATOM   1928 C  CG2 . THR   A 1 249 ? 12.07021  15.42623  20.52661  1.000 29.20934 ? 249 THR   A CG2 1 
ATOM   1929 N  N   . ALA   A 1 250 ? 9.62694   13.42107  22.22609  1.000 27.61485 ? 250 ALA   A N   1 
ATOM   1930 C  CA  . ALA   A 1 250 ? 9.32093   13.50423  23.65207  1.000 30.45514 ? 250 ALA   A CA  1 
ATOM   1931 C  C   . ALA   A 1 250 ? 9.70600   12.22023  24.37354  1.000 29.73827 ? 250 ALA   A C   1 
ATOM   1932 O  O   . ALA   A 1 250 ? 10.21740  12.25998  25.49886  1.000 29.99780 ? 250 ALA   A O   1 
ATOM   1933 C  CB  . ALA   A 1 250 ? 7.83677   13.80502  23.85984  1.000 29.72738 ? 250 ALA   A CB  1 
ATOM   1934 N  N   . SER   A 1 251 ? 9.47332   11.07089  23.73627  1.000 29.76739 ? 251 SER   A N   1 
ATOM   1935 C  CA  . SER   A 1 251 ? 9.81794   9.79381   24.35331  1.000 29.81611 ? 251 SER   A CA  1 
ATOM   1936 C  C   . SER   A 1 251 ? 11.32690  9.60216   24.42939  1.000 30.82546 ? 251 SER   A C   1 
ATOM   1937 O  O   . SER   A 1 251 ? 11.84087  9.08045   25.42521  1.000 28.53129 ? 251 SER   A O   1 
ATOM   1938 C  CB  . SER   A 1 251 ? 9.17230   8.64861   23.57642  1.000 30.10159 ? 251 SER   A CB  1 
ATOM   1939 O  OG  . SER   A 1 251 ? 7.75888   8.72067   23.64052  1.000 31.71356 ? 251 SER   A OG  1 
ATOM   1940 N  N   . MET   A 1 252 ? 12.05439  10.00692  23.38464  1.000 27.93313 ? 252 MET   A N   1 
ATOM   1941 C  CA  . MET   A 1 252 ? 13.50922  9.91149   23.43287  1.000 28.65746 ? 252 MET   A CA  1 
ATOM   1942 C  C   . MET   A 1 252 ? 14.08148  10.80506  24.52193  1.000 29.59105 ? 252 MET   A C   1 
ATOM   1943 O  O   . MET   A 1 252 ? 15.06524  10.44238  25.17379  1.000 28.91158 ? 252 MET   A O   1 
ATOM   1944 C  CB  . MET   A 1 252 ? 14.11667  10.26717  22.07723  1.000 28.94454 ? 252 MET   A CB  1 
ATOM   1945 C  CG  . MET   A 1 252 ? 14.18412  9.09912   21.12105  1.000 28.68459 ? 252 MET   A CG  1 
ATOM   1946 S  SD  . MET   A 1 252 ? 15.09176  7.67520   21.76696  1.000 30.16613 ? 252 MET   A SD  1 
ATOM   1947 C  CE  . MET   A 1 252 ? 16.72472  8.37657   22.00556  1.000 29.22499 ? 252 MET   A CE  1 
ATOM   1948 N  N   . THR   A 1 253 ? 13.47577  11.97520  24.73782  1.000 28.45710 ? 253 THR   A N   1 
ATOM   1949 C  CA  . THR   A 1 253 ? 13.95738  12.87553  25.78154  1.000 30.42868 ? 253 THR   A CA  1 
ATOM   1950 C  C   . THR   A 1 253 ? 13.77455  12.26418  27.16660  1.000 29.70137 ? 253 THR   A C   1 
ATOM   1951 O  O   . THR   A 1 253 ? 14.73309  12.16303  27.94180  1.000 30.14030 ? 253 THR   A O   1 
ATOM   1952 C  CB  . THR   A 1 253 ? 13.24001  14.22358  25.69064  1.000 28.99033 ? 253 THR   A CB  1 
ATOM   1953 O  OG1 . THR   A 1 253 ? 13.58338  14.86580  24.45595  1.000 29.23131 ? 253 THR   A OG1 1 
ATOM   1954 C  CG2 . THR   A 1 253 ? 13.64521  15.12101  26.85766  1.000 29.55619 ? 253 THR   A CG2 1 
ATOM   1955 N  N   . SER   A 1 254 ? 12.54878  11.84633  27.49421  1.000 28.75051 ? 254 SER   A N   1 
ATOM   1956 C  CA  . SER   A 1 254 ? 12.28130  11.32157  28.82905  1.000 30.66108 ? 254 SER   A CA  1 
ATOM   1957 C  C   . SER   A 1 254 ? 13.09408  10.06242  29.09963  1.000 33.15462 ? 254 SER   A C   1 
ATOM   1958 O  O   . SER   A 1 254 ? 13.67849  9.91134   30.17868  1.000 33.69375 ? 254 SER   A O   1 
ATOM   1959 C  CB  . SER   A 1 254 ? 10.78700  11.04218  28.99435  1.000 32.73082 ? 254 SER   A CB  1 
ATOM   1960 O  OG  . SER   A 1 254 ? 10.43866  9.78634   28.43233  1.000 41.18310 ? 254 SER   A OG  1 
ATOM   1961 N  N   . LEU   A 1 255 ? 13.15676  9.15218   28.12621  1.000 31.93196 ? 255 LEU   A N   1 
ATOM   1962 C  CA  . LEU   A 1 255 ? 13.89679  7.91473   28.33915  1.000 31.96171 ? 255 LEU   A CA  1 
ATOM   1963 C  C   . LEU   A 1 255 ? 15.40333  8.14990   28.35272  1.000 31.42452 ? 255 LEU   A C   1 
ATOM   1964 O  O   . LEU   A 1 255 ? 16.12381  7.46274   29.08516  1.000 32.76837 ? 255 LEU   A O   1 
ATOM   1965 C  CB  . LEU   A 1 255 ? 13.51171  6.88402   27.27791  1.000 29.56026 ? 255 LEU   A CB  1 
ATOM   1966 C  CG  . LEU   A 1 255 ? 12.03696  6.46456   27.30260  1.000 31.53410 ? 255 LEU   A CG  1 
ATOM   1967 C  CD1 . LEU   A 1 255 ? 11.73387  5.46854   26.19678  1.000 31.67446 ? 255 LEU   A CD1 1 
ATOM   1968 C  CD2 . LEU   A 1 255 ? 11.64613  5.89315   28.65874  1.000 34.28783 ? 255 LEU   A CD2 1 
ATOM   1969 N  N   . SER   A 1 256 ? 15.90124  9.11144   27.56827  1.000 31.18466 ? 256 SER   A N   1 
ATOM   1970 C  CA  . SER   A 1 256 ? 17.32345  9.43866   27.63969  1.000 30.52119 ? 256 SER   A CA  1 
ATOM   1971 C  C   . SER   A 1 256 ? 17.68880  9.99885   29.00755  1.000 32.77292 ? 256 SER   A C   1 
ATOM   1972 O  O   . SER   A 1 256 ? 18.75942  9.69364   29.54354  1.000 33.17297 ? 256 SER   A O   1 
ATOM   1973 C  CB  . SER   A 1 256 ? 17.71030  10.43179  26.54381  1.000 31.89147 ? 256 SER   A CB  1 
ATOM   1974 O  OG  . SER   A 1 256 ? 17.67574  9.83188   25.25818  1.000 30.69536 ? 256 SER   A OG  1 
ATOM   1975 N  N   . VAL   A 1 257 ? 16.81046  10.81872  29.58851  1.000 31.88558 ? 257 VAL   A N   1 
ATOM   1976 C  CA  . VAL   A 1 257 ? 17.06693  11.36767  30.91918  1.000 33.30463 ? 257 VAL   A CA  1 
ATOM   1977 C  C   . VAL   A 1 257 ? 17.08985  10.25320  31.95872  1.000 33.64527 ? 257 VAL   A C   1 
ATOM   1978 O  O   . VAL   A 1 257 ? 18.01097  10.16593  32.77904  1.000 35.69726 ? 257 VAL   A O   1 
ATOM   1979 C  CB  . VAL   A 1 257 ? 16.02189  12.44084  31.26868  1.000 32.39350 ? 257 VAL   A CB  1 
ATOM   1980 C  CG1 . VAL   A 1 257 ? 16.06977  12.76317  32.75788  1.000 36.08435 ? 257 VAL   A CG1 1 
ATOM   1981 C  CG2 . VAL   A 1 257 ? 16.25794  13.69662  30.44179  1.000 32.76943 ? 257 VAL   A CG2 1 
ATOM   1982 N  N   . ILE   A 1 258 ? 16.06856  9.39147   31.94315  1.000 30.95252 ? 258 ILE   A N   1 
ATOM   1983 C  CA  . ILE   A 1 258 ? 16.03155  8.24535   32.85111  1.000 35.14481 ? 258 ILE   A CA  1 
ATOM   1984 C  C   . ILE   A 1 258 ? 17.29169  7.40590   32.69360  1.000 34.73140 ? 258 ILE   A C   1 
ATOM   1985 O  O   . ILE   A 1 258 ? 17.95716  7.05653   33.67568  1.000 36.36778 ? 258 ILE   A O   1 
ATOM   1986 C  CB  . ILE   A 1 258 ? 14.77048  7.40008   32.59846  1.000 33.55721 ? 258 ILE   A CB  1 
ATOM   1987 C  CG1 . ILE   A 1 258 ? 13.49929  8.21559   32.83540  1.000 33.65519 ? 258 ILE   A CG1 1 
ATOM   1988 C  CG2 . ILE   A 1 258 ? 14.77377  6.16632   33.48835  1.000 35.54386 ? 258 ILE   A CG2 1 
ATOM   1989 C  CD1 . ILE   A 1 258 ? 12.23829  7.48979   32.41804  1.000 34.14865 ? 258 ILE   A CD1 1 
ATOM   1990 N  N   . THR   A 1 259 ? 17.64661  7.08544   31.44595  1.000 29.35676 ? 259 THR   A N   1 
ATOM   1991 C  CA  . THR   A 1 259 ? 18.76645  6.18191   31.19971  1.000 36.00485 ? 259 THR   A CA  1 
ATOM   1992 C  C   . THR   A 1 259 ? 20.09231  6.80993   31.61161  1.000 35.16641 ? 259 THR   A C   1 
ATOM   1993 O  O   . THR   A 1 259 ? 20.92411  6.15255   32.24695  1.000 36.43256 ? 259 THR   A O   1 
ATOM   1994 C  CB  . THR   A 1 259 ? 18.79887  5.77732   29.72507  1.000 33.73799 ? 259 THR   A CB  1 
ATOM   1995 O  OG1 . THR   A 1 259 ? 17.54681  5.17921   29.36495  1.000 32.53652 ? 259 THR   A OG1 1 
ATOM   1996 C  CG2 . THR   A 1 259 ? 19.91976  4.79070   29.46132  1.000 35.22878 ? 259 THR   A CG2 1 
ATOM   1997 N  N   . LEU   A 1 260 ? 20.30773  8.08039   31.26614  1.000 33.56621 ? 260 LEU   A N   1 
ATOM   1998 C  CA  . LEU   A 1 260 ? 21.57518  8.72545   31.59884  1.000 36.11045 ? 260 LEU   A CA  1 
ATOM   1999 C  C   . LEU   A 1 260 ? 21.77316  8.82439   33.10728  1.000 36.22509 ? 260 LEU   A C   1 
ATOM   2000 O  O   . LEU   A 1 260 ? 22.89955  8.69681   33.60196  1.000 36.58832 ? 260 LEU   A O   1 
ATOM   2001 C  CB  . LEU   A 1 260 ? 21.64646  10.10996  30.95799  1.000 35.32462 ? 260 LEU   A CB  1 
ATOM   2002 C  CG  . LEU   A 1 260 ? 21.96743  10.14002  29.46135  1.000 35.58346 ? 260 LEU   A CG  1 
ATOM   2003 C  CD1 . LEU   A 1 260 ? 21.60121  11.48557  28.85554  1.000 34.49208 ? 260 LEU   A CD1 1 
ATOM   2004 C  CD2 . LEU   A 1 260 ? 23.43779  9.82928   29.22828  1.000 36.34797 ? 260 LEU   A CD2 1 
ATOM   2005 N  N   . LEU   A 1 261 ? 20.69012  9.04570   33.85610  1.000 34.83945 ? 261 LEU   A N   1 
ATOM   2006 C  CA  . LEU   A 1 261 ? 20.80016  9.14470   35.30786  1.000 35.74222 ? 261 LEU   A CA  1 
ATOM   2007 C  C   . LEU   A 1 261 ? 21.05371  7.79279   35.96811  1.000 37.13089 ? 261 LEU   A C   1 
ATOM   2008 O  O   . LEU   A 1 261 ? 21.57853  7.75331   37.08648  1.000 37.33721 ? 261 LEU   A O   1 
ATOM   2009 C  CB  . LEU   A 1 261 ? 19.54047  9.79136   35.88571  1.000 35.26170 ? 261 LEU   A CB  1 
ATOM   2010 C  CG  . LEU   A 1 261 ? 19.39344  11.28982  35.60224  1.000 37.00711 ? 261 LEU   A CG  1 
ATOM   2011 C  CD1 . LEU   A 1 261 ? 18.03837  11.79596  36.06915  1.000 38.47547 ? 261 LEU   A CD1 1 
ATOM   2012 C  CD2 . LEU   A 1 261 ? 20.51672  12.07187  36.26679  1.000 36.70545 ? 261 LEU   A CD2 1 
ATOM   2013 N  N   . ASP   A 1 262 ? 20.69560  6.69003   35.31036  1.000 36.45901 ? 262 ASP   A N   1 
ATOM   2014 C  CA  . ASP   A 1 262 ? 21.04165  5.36031   35.79956  1.000 37.69568 ? 262 ASP   A CA  1 
ATOM   2015 C  C   . ASP   A 1 262 ? 22.44961  4.93857   35.40745  1.000 38.09296 ? 262 ASP   A C   1 
ATOM   2016 O  O   . ASP   A 1 262 ? 22.89480  3.86150   35.82017  1.000 38.22706 ? 262 ASP   A O   1 
ATOM   2017 C  CB  . ASP   A 1 262 ? 20.03774  4.32212   35.28937  1.000 37.44254 ? 262 ASP   A CB  1 
ATOM   2018 C  CG  . ASP   A 1 262 ? 18.91207  4.06462   36.27248  1.000 38.52196 ? 262 ASP   A CG  1 
ATOM   2019 O  OD1 . ASP   A 1 262 ? 18.85930  4.75055   37.31413  1.000 36.91039 ? 262 ASP   A OD1 1 
ATOM   2020 O  OD2 . ASP   A 1 262 ? 18.08302  3.17013   36.00290  1.000 39.06957 ? 262 ASP   A OD2 1 
ATOM   2021 N  N   . HIS   A 1 263 ? 23.15006  5.75066   34.61936  1.000 37.08219 ? 263 HIS   A N   1 
ATOM   2022 C  CA  . HIS   A 1 263 ? 24.54528  5.51430   34.25746  1.000 39.08737 ? 263 HIS   A CA  1 
ATOM   2023 C  C   . HIS   A 1 263 ? 25.32594  6.79455   34.52962  1.000 40.75728 ? 263 HIS   A C   1 
ATOM   2024 O  O   . HIS   A 1 263 ? 25.83322  7.44135   33.60487  1.000 39.95990 ? 263 HIS   A O   1 
ATOM   2025 C  CB  . HIS   A 1 263 ? 24.66324  5.07659   32.79739  1.000 39.17182 ? 263 HIS   A CB  1 
ATOM   2026 C  CG  . HIS   A 1 263 ? 23.82275  3.88416   32.45725  1.000 38.33395 ? 263 HIS   A CG  1 
ATOM   2027 N  ND1 . HIS   A 1 263 ? 22.44963  3.94455   32.33824  1.000 36.81213 ? 263 HIS   A ND1 1 
ATOM   2028 C  CD2 . HIS   A 1 263 ? 24.16417  2.59666   32.21477  1.000 38.31952 ? 263 HIS   A CD2 1 
ATOM   2029 C  CE1 . HIS   A 1 263 ? 21.98316  2.74642   32.03215  1.000 38.16498 ? 263 HIS   A CE1 1 
ATOM   2030 N  NE2 . HIS   A 1 263 ? 23.00287  1.91087   31.95137  1.000 37.51967 ? 263 HIS   A NE2 1 
ATOM   2031 N  N   . PRO   A 1 264 ? 25.47136  7.16803   35.80707  1.000 40.80103 ? 264 PRO   A N   1 
ATOM   2032 C  CA  . PRO   A 1 264 ? 25.99692  8.50803   36.12387  1.000 41.87906 ? 264 PRO   A CA  1 
ATOM   2033 C  C   . PRO   A 1 264 ? 27.43177  8.72355   35.68397  1.000 43.09984 ? 264 PRO   A C   1 
ATOM   2034 O  O   . PRO   A 1 264 ? 27.82261  9.87012   35.42728  1.000 45.40414 ? 264 PRO   A O   1 
ATOM   2035 C  CB  . PRO   A 1 264 ? 25.85793  8.59103   37.65125  1.000 42.08429 ? 264 PRO   A CB  1 
ATOM   2036 C  CG  . PRO   A 1 264 ? 24.92350  7.46644   38.03049  1.000 40.55219 ? 264 PRO   A CG  1 
ATOM   2037 C  CD  . PRO   A 1 264 ? 25.15190  6.39704   37.01916  1.000 40.05446 ? 264 PRO   A CD  1 
ATOM   2038 N  N   . GLU   A 1 265 ? 28.23395  7.66178   35.59191  1.000 43.58427 ? 265 GLU   A N   1 
ATOM   2039 C  CA  . GLU   A 1 265 ? 29.59406  7.81477   35.08763  1.000 45.40724 ? 265 GLU   A CA  1 
ATOM   2040 C  C   . GLU   A 1 265 ? 29.58485  8.32056   33.65230  1.000 44.75036 ? 265 GLU   A C   1 
ATOM   2041 O  O   . GLU   A 1 265 ? 30.33514  9.23780   33.29839  1.000 44.50743 ? 265 GLU   A O   1 
ATOM   2042 C  CB  . GLU   A 1 265 ? 30.35070  6.48862   35.17893  1.000 48.25904 ? 265 GLU   A CB  1 
ATOM   2043 C  CG  . GLU   A 1 265 ? 30.80070  6.10186   36.57643  1.000 51.41174 ? 265 GLU   A CG  1 
ATOM   2044 C  CD  . GLU   A 1 265 ? 31.96945  5.13445   36.55320  1.000 56.03193 ? 265 GLU   A CD  1 
ATOM   2045 O  OE1 . GLU   A 1 265 ? 32.85429  5.29444   35.68556  1.000 58.94741 ? 265 GLU   A OE1 1 
ATOM   2046 O  OE2 . GLU   A 1 265 ? 32.00182  4.21243   37.39470  1.000 58.05989 ? 265 GLU   A OE2 1 
ATOM   2047 N  N   . GLN   A 1 266 ? 28.73118  7.73367   32.80938  1.000 42.96521 ? 266 GLN   A N   1 
ATOM   2048 C  CA  . GLN   A 1 266 ? 28.68189  8.13795   31.40973  1.000 43.71768 ? 266 GLN   A CA  1 
ATOM   2049 C  C   . GLN   A 1 266 ? 28.03233  9.50500   31.23775  1.000 43.40922 ? 266 GLN   A C   1 
ATOM   2050 O  O   . GLN   A 1 266 ? 28.39347  10.24670  30.31713  1.000 44.06756 ? 266 GLN   A O   1 
ATOM   2051 C  CB  . GLN   A 1 266 ? 27.94093  7.08641   30.58623  1.000 42.51084 ? 266 GLN   A CB  1 
ATOM   2052 C  CG  . GLN   A 1 266 ? 28.68894  5.77200   30.45421  1.000 42.02713 ? 266 GLN   A CG  1 
ATOM   2053 C  CD  . GLN   A 1 266 ? 27.94945  4.76659   29.59667  1.000 40.67746 ? 266 GLN   A CD  1 
ATOM   2054 O  OE1 . GLN   A 1 266 ? 27.82006  4.94184   28.38507  1.000 40.24997 ? 266 GLN   A OE1 1 
ATOM   2055 N  NE2 . GLN   A 1 266 ? 27.45289  3.70662   30.22464  1.000 40.60490 ? 266 GLN   A NE2 1 
ATOM   2056 N  N   . TYR   A 1 267 ? 27.07898  9.85648   32.10396  1.000 41.96875 ? 267 TYR   A N   1 
ATOM   2057 C  CA  . TYR   A 1 267 ? 26.47146  11.18119  32.03066  1.000 42.37405 ? 267 TYR   A CA  1 
ATOM   2058 C  C   . TYR   A 1 267 ? 27.48360  12.26100  32.39079  1.000 43.39890 ? 267 TYR   A C   1 
ATOM   2059 O  O   . TYR   A 1 267 ? 27.61705  13.26453  31.67954  1.000 42.80521 ? 267 TYR   A O   1 
ATOM   2060 C  CB  . TYR   A 1 267 ? 25.25244  11.25647  32.95171  1.000 41.04762 ? 267 TYR   A CB  1 
ATOM   2061 C  CG  . TYR   A 1 267 ? 24.33538  12.42280  32.65288  1.000 39.30421 ? 267 TYR   A CG  1 
ATOM   2062 C  CD1 . TYR   A 1 267 ? 24.40299  13.08820  31.43584  1.000 39.55447 ? 267 TYR   A CD1 1 
ATOM   2063 C  CD2 . TYR   A 1 267 ? 23.41004  12.86488  33.59003  1.000 38.70975 ? 267 TYR   A CD2 1 
ATOM   2064 C  CE1 . TYR   A 1 267 ? 23.57106  14.15423  31.15566  1.000 38.72337 ? 267 TYR   A CE1 1 
ATOM   2065 C  CE2 . TYR   A 1 267 ? 22.57446  13.93400  33.31953  1.000 39.16830 ? 267 TYR   A CE2 1 
ATOM   2066 C  CZ  . TYR   A 1 267 ? 22.65991  14.57483  32.10125  1.000 38.82593 ? 267 TYR   A CZ  1 
ATOM   2067 O  OH  . TYR   A 1 267 ? 21.83146  15.63807  31.82461  1.000 38.21666 ? 267 TYR   A OH  1 
ATOM   2068 N  N   . ALA   A 1 268 ? 28.21016  12.06762  33.49522  1.000 42.81389 ? 268 ALA   A N   1 
ATOM   2069 C  CA  . ALA   A 1 268 ? 29.22900  13.03452  33.89019  1.000 44.37468 ? 268 ALA   A CA  1 
ATOM   2070 C  C   . ALA   A 1 268 ? 30.31908  13.14248  32.83324  1.000 44.88696 ? 268 ALA   A C   1 
ATOM   2071 O  O   . ALA   A 1 268 ? 30.81557  14.24022  32.55115  1.000 44.22231 ? 268 ALA   A O   1 
ATOM   2072 C  CB  . ALA   A 1 268 ? 29.82632  12.64648  35.24224  1.000 45.78436 ? 268 ALA   A CB  1 
ATOM   2073 N  N   . ALA   A 1 269 ? 30.70048  12.01140  32.23280  1.000 44.22194 ? 269 ALA   A N   1 
ATOM   2074 C  CA  . ALA   A 1 269 ? 31.65616  12.04800  31.13097  1.000 44.72011 ? 269 ALA   A CA  1 
ATOM   2075 C  C   . ALA   A 1 269 ? 31.09410  12.82263  29.94598  1.000 44.51854 ? 269 ALA   A C   1 
ATOM   2076 O  O   . ALA   A 1 269 ? 31.81589  13.58742  29.29474  1.000 44.38219 ? 269 ALA   A O   1 
ATOM   2077 C  CB  . ALA   A 1 269 ? 32.03638  10.62626  30.71626  1.000 45.02484 ? 269 ALA   A CB  1 
ATOM   2078 N  N   . LEU   A 1 270 ? 29.80120  12.64499  29.65912  1.000 44.47130 ? 270 LEU   A N   1 
ATOM   2079 C  CA  . LEU   A 1 270 ? 29.16981  13.37799  28.56660  1.000 43.36227 ? 270 LEU   A CA  1 
ATOM   2080 C  C   . LEU   A 1 270 ? 29.15772  14.87658  28.84341  1.000 44.14613 ? 270 LEU   A C   1 
ATOM   2081 O  O   . LEU   A 1 270 ? 29.42460  15.68450  27.94606  1.000 42.92584 ? 270 LEU   A O   1 
ATOM   2082 C  CB  . LEU   A 1 270 ? 27.75039  12.85542  28.34822  1.000 43.21476 ? 270 LEU   A CB  1 
ATOM   2083 C  CG  . LEU   A 1 270 ? 26.94959  13.39545  27.16285  1.000 42.66749 ? 270 LEU   A CG  1 
ATOM   2084 C  CD1 . LEU   A 1 270 ? 27.68942  13.16127  25.85697  1.000 40.82789 ? 270 LEU   A CD1 1 
ATOM   2085 C  CD2 . LEU   A 1 270 ? 25.57303  12.75328  27.12002  1.000 40.59318 ? 270 LEU   A CD2 1 
ATOM   2086 N  N   . ARG   A 1 271 ? 28.86636  15.26731  30.08610  1.000 44.08159 ? 271 ARG   A N   1 
ATOM   2087 C  CA  . ARG   A 1 271 ? 28.84560  16.68780  30.41765  1.000 44.68021 ? 271 ARG   A CA  1 
ATOM   2088 C  C   . ARG   A 1 271 ? 30.23791  17.29713  30.31799  1.000 45.19210 ? 271 ARG   A C   1 
ATOM   2089 O  O   . ARG   A 1 271 ? 30.39210  18.44998  29.89730  1.000 44.28830 ? 271 ARG   A O   1 
ATOM   2090 C  CB  . ARG   A 1 271 ? 28.27550  16.90157  31.81844  1.000 45.38248 ? 271 ARG   A CB  1 
ATOM   2091 C  CG  . ARG   A 1 271 ? 28.00958  18.36481  32.12598  1.000 47.52726 ? 271 ARG   A CG  1 
ATOM   2092 C  CD  . ARG   A 1 271 ? 27.58624  18.59952  33.56732  1.000 47.61380 ? 271 ARG   A CD  1 
ATOM   2093 N  NE  . ARG   A 1 271 ? 26.92850  19.89593  33.70498  1.000 48.33525 ? 271 ARG   A NE  1 
ATOM   2094 C  CZ  . ARG   A 1 271 ? 27.56916  21.06043  33.73729  1.000 52.07764 ? 271 ARG   A CZ  1 
ATOM   2095 N  NH1 . ARG   A 1 271 ? 26.88648  22.19024  33.85611  1.000 49.57106 ? 271 ARG   A NH1 1 
ATOM   2096 N  NH2 . ARG   A 1 271 ? 28.89217  21.09817  33.64877  1.000 53.68336 ? 271 ARG   A NH2 1 
ATOM   2097 N  N   . ALA   A 1 272 ? 31.26585  16.53466  30.69565  1.000 44.40598 ? 272 ALA   A N   1 
ATOM   2098 C  CA  . ALA   A 1 272 ? 32.63391  17.03185  30.66263  1.000 44.85086 ? 272 ALA   A CA  1 
ATOM   2099 C  C   . ALA   A 1 272 ? 33.17504  17.17996  29.24659  1.000 44.84420 ? 272 ALA   A C   1 
ATOM   2100 O  O   . ALA   A 1 272 ? 34.22044  17.81413  29.06574  1.000 45.52594 ? 272 ALA   A O   1 
ATOM   2101 C  CB  . ALA   A 1 272 ? 33.54651  16.10703  31.46809  1.000 45.08705 ? 272 ALA   A CB  1 
ATOM   2102 N  N   . ASP   A 1 273 ? 32.49925  16.61872  28.24481  1.000 44.59892 ? 273 ASP   A N   1 
ATOM   2103 C  CA  . ASP   A 1 273 ? 32.97722  16.70761  26.86770  1.000 44.45896 ? 273 ASP   A CA  1 
ATOM   2104 C  C   . ASP   A 1 273 ? 31.75898  16.67929  25.95462  1.000 44.02223 ? 273 ASP   A C   1 
ATOM   2105 O  O   . ASP   A 1 273 ? 31.18537  15.60904  25.71269  1.000 43.15378 ? 273 ASP   A O   1 
ATOM   2106 C  CB  . ASP   A 1 273 ? 33.93966  15.57341  26.54423  1.000 45.12725 ? 273 ASP   A CB  1 
ATOM   2107 C  CG  . ASP   A 1 273 ? 34.67102  15.78819  25.23193  1.000 45.92144 ? 273 ASP   A CG  1 
ATOM   2108 O  OD1 . ASP   A 1 273 ? 34.52573  16.87040  24.63357  1.000 45.93031 ? 273 ASP   A OD1 1 
ATOM   2109 O  OD2 . ASP   A 1 273 ? 35.40086  14.86962  24.80377  1.000 47.41580 ? 273 ASP   A OD2 1 
ATOM   2110 N  N   . ARG   A 1 274 ? 31.37943  17.84846  25.43110  1.000 43.46518 ? 274 ARG   A N   1 
ATOM   2111 C  CA  . ARG   A 1 274 ? 30.25468  17.95208  24.51415  1.000 42.60437 ? 274 ARG   A CA  1 
ATOM   2112 C  C   . ARG   A 1 274 ? 30.58470  17.42145  23.12673  1.000 41.65516 ? 274 ARG   A C   1 
ATOM   2113 O  O   . ARG   A 1 274 ? 29.67165  17.20199  22.32682  1.000 39.63008 ? 274 ARG   A O   1 
ATOM   2114 C  CB  . ARG   A 1 274 ? 29.78293  19.40397  24.42512  1.000 42.16486 ? 274 ARG   A CB  1 
ATOM   2115 C  CG  . ARG   A 1 274 ? 29.48181  20.00552  25.79612  1.000 41.88671 ? 274 ARG   A CG  1 
ATOM   2116 C  CD  . ARG   A 1 274 ? 28.64116  19.04915  26.63039  1.000 42.56436 ? 274 ARG   A CD  1 
ATOM   2117 N  NE  . ARG   A 1 274 ? 28.46081  19.52715  27.99492  1.000 42.80984 ? 274 ARG   A NE  1 
ATOM   2118 C  CZ  . ARG   A 1 274 ? 27.54851  20.42413  28.35315  1.000 41.34524 ? 274 ARG   A CZ  1 
ATOM   2119 N  NH1 . ARG   A 1 274 ? 26.73542  20.94428  27.44404  1.000 40.61247 ? 274 ARG   A NH1 1 
ATOM   2120 N  NH2 . ARG   A 1 274 ? 27.45101  20.80660  29.61783  1.000 42.73679 ? 274 ARG   A NH2 1 
ATOM   2121 N  N   . SER   A 1 275 ? 31.86845  17.19403  22.83630  1.000 42.32151 ? 275 SER   A N   1 
ATOM   2122 C  CA  . SER   A 1 275 ? 32.25299  16.46922  21.63120  1.000 43.90364 ? 275 SER   A CA  1 
ATOM   2123 C  C   . SER   A 1 275 ? 31.55752  15.11967  21.54693  1.000 41.79285 ? 275 SER   A C   1 
ATOM   2124 O  O   . SER   A 1 275 ? 31.35007  14.60323  20.44363  1.000 39.44783 ? 275 SER   A O   1 
ATOM   2125 C  CB  . SER   A 1 275 ? 33.78264  16.29064  21.59440  1.000 44.57598 ? 275 SER   A CB  1 
ATOM   2126 O  OG  . SER   A 1 275 ? 34.20888  15.79040  20.33395  1.000 52.95226 ? 275 SER   A OG  1 
ATOM   2127 N  N   . LEU   A 1 276 ? 31.13619  14.56254  22.68515  1.000 40.34820 ? 276 LEU   A N   1 
ATOM   2128 C  CA  . LEU   A 1 276 ? 30.56187  13.22760  22.74000  1.000 40.46016 ? 276 LEU   A CA  1 
ATOM   2129 C  C   . LEU   A 1 276 ? 29.05623  13.19767  22.52451  1.000 38.91293 ? 276 LEU   A C   1 
ATOM   2130 O  O   . LEU   A 1 276 ? 28.50128  12.10607  22.35818  1.000 37.71446 ? 276 LEU   A O   1 
ATOM   2131 C  CB  . LEU   A 1 276 ? 30.87318  12.57293  24.08725  1.000 40.89874 ? 276 LEU   A CB  1 
ATOM   2132 C  CG  . LEU   A 1 276 ? 32.33581  12.56765  24.53321  1.000 42.49369 ? 276 LEU   A CG  1 
ATOM   2133 C  CD1 . LEU   A 1 276 ? 32.49156  11.89312  25.88708  1.000 42.91227 ? 276 LEU   A CD1 1 
ATOM   2134 C  CD2 . LEU   A 1 276 ? 33.21522  11.89776  23.49049  1.000 42.49333 ? 276 LEU   A CD2 1 
ATOM   2135 N  N   . VAL   A 1 277 ? 28.38377  14.35213  22.52611  1.000 39.03270 ? 277 VAL   A N   1 
ATOM   2136 C  CA  . VAL   A 1 277 ? 26.91738  14.36826  22.44205  1.000 37.84292 ? 277 VAL   A CA  1 
ATOM   2137 C  C   . VAL   A 1 277 ? 26.40186  13.69242  21.17414  1.000 36.45859 ? 277 VAL   A C   1 
ATOM   2138 O  O   . VAL   A 1 277 ? 25.46557  12.87847  21.27221  1.000 35.07505 ? 277 VAL   A O   1 
ATOM   2139 C  CB  . VAL   A 1 277 ? 26.39108  15.79003  22.61348  1.000 38.31367 ? 277 VAL   A CB  1 
ATOM   2140 C  CG1 . VAL   A 1 277 ? 24.89247  15.84315  22.37458  1.000 36.83838 ? 277 VAL   A CG1 1 
ATOM   2141 C  CG2 . VAL   A 1 277 ? 26.72945  16.31773  24.00145  1.000 39.43585 ? 277 VAL   A CG2 1 
ATOM   2142 N  N   . PRO   A 1 278 ? 26.92618  13.97516  19.97074  1.000 36.23548 ? 278 PRO   A N   1 
ATOM   2143 C  CA  . PRO   A 1 278 ? 26.42400  13.26131  18.78189  1.000 36.73289 ? 278 PRO   A CA  1 
ATOM   2144 C  C   . PRO   A 1 278 ? 26.49512  11.74703  18.90624  1.000 34.73434 ? 278 PRO   A C   1 
ATOM   2145 O  O   . PRO   A 1 278 ? 25.48899  11.06415  18.68086  1.000 35.06877 ? 278 PRO   A O   1 
ATOM   2146 C  CB  . PRO   A 1 278 ? 27.32377  13.79190  17.65823  1.000 37.40836 ? 278 PRO   A CB  1 
ATOM   2147 C  CG  . PRO   A 1 278 ? 27.71545  15.14797  18.11027  1.000 38.26417 ? 278 PRO   A CG  1 
ATOM   2148 C  CD  . PRO   A 1 278 ? 27.89873  15.02154  19.59568  1.000 38.29588 ? 278 PRO   A CD  1 
ATOM   2149 N  N   . GLY   A 1 279 ? 27.65919  11.20319  19.27261  1.000 35.72140 ? 279 GLY   A N   1 
ATOM   2150 C  CA  . GLY   A 1 279 ? 27.77831  9.76460   19.44108  1.000 34.34255 ? 279 GLY   A CA  1 
ATOM   2151 C  C   . GLY   A 1 279 ? 26.92292  9.21966   20.56603  1.000 33.91540 ? 279 GLY   A C   1 
ATOM   2152 O  O   . GLY   A 1 279 ? 26.43063  8.08966   20.48522  1.000 33.06970 ? 279 GLY   A O   1 
ATOM   2153 N  N   . ALA   A 1 280 ? 26.73823  10.00308  21.62964  1.000 34.22084 ? 280 ALA   A N   1 
ATOM   2154 C  CA  . ALA   A 1 280 ? 25.84138  9.58862   22.70102  1.000 34.99118 ? 280 ALA   A CA  1 
ATOM   2155 C  C   . ALA   A 1 280 ? 24.39833  9.52686   22.22253  1.000 33.23965 ? 280 ALA   A C   1 
ATOM   2156 O  O   . ALA   A 1 280 ? 23.63007  8.67385   22.67976  1.000 31.51248 ? 280 ALA   A O   1 
ATOM   2157 C  CB  . ALA   A 1 280 ? 25.96533  10.54089  23.88986  1.000 35.17288 ? 280 ALA   A CB  1 
ATOM   2158 N  N   . VAL   A 1 281 ? 24.01821  10.41207  21.29987  1.000 31.30364 ? 281 VAL   A N   1 
ATOM   2159 C  CA  . VAL   A 1 281 ? 22.65330  10.41148  20.78480  1.000 32.74852 ? 281 VAL   A CA  1 
ATOM   2160 C  C   . VAL   A 1 281 ? 22.39786  9.16301   19.94823  1.000 29.98480 ? 281 VAL   A C   1 
ATOM   2161 O  O   . VAL   A 1 281 ? 21.33317  8.54152   20.04892  1.000 30.47240 ? 281 VAL   A O   1 
ATOM   2162 C  CB  . VAL   A 1 281 ? 22.38624  11.70601  19.99054  1.000 31.91117 ? 281 VAL   A CB  1 
ATOM   2163 C  CG1 . VAL   A 1 281 ? 21.09051  11.60216  19.20410  1.000 29.36477 ? 281 VAL   A CG1 1 
ATOM   2164 C  CG2 . VAL   A 1 281 ? 22.32672  12.89959  20.93583  1.000 32.47619 ? 281 VAL   A CG2 1 
ATOM   2165 N  N   . GLU   A 1 282 ? 23.36937  8.76964   19.11711  1.000 31.44492 ? 282 GLU   A N   1 
ATOM   2166 C  CA  . GLU   A 1 282 ? 23.23067  7.53934   18.34012  1.000 30.72206 ? 282 GLU   A CA  1 
ATOM   2167 C  C   . GLU   A 1 282 ? 23.11072  6.32248   19.24843  1.000 32.12519 ? 282 GLU   A C   1 
ATOM   2168 O  O   . GLU   A 1 282 ? 22.27326  5.44178   19.01513  1.000 31.68075 ? 282 GLU   A O   1 
ATOM   2169 C  CB  . GLU   A 1 282 ? 24.41684  7.37611   17.38868  1.000 29.57780 ? 282 GLU   A CB  1 
ATOM   2170 C  CG  . GLU   A 1 282 ? 24.48875  8.44084   16.31189  1.000 33.03029 ? 282 GLU   A CG  1 
ATOM   2171 C  CD  . GLU   A 1 282 ? 23.19585  8.55027   15.53699  1.000 31.28072 ? 282 GLU   A CD  1 
ATOM   2172 O  OE1 . GLU   A 1 282 ? 22.74731  7.52869   14.97329  1.000 27.60694 ? 282 GLU   A OE1 1 
ATOM   2173 O  OE2 . GLU   A 1 282 ? 22.61461  9.65218   15.51973  1.000 30.37563 ? 282 GLU   A OE2 1 
ATOM   2174 N  N   . GLU   A 1 283 ? 23.94066  6.25415   20.29114  1.000 32.84025 ? 283 GLU   A N   1 
ATOM   2175 C  CA  . GLU   A 1 283 ? 23.88185  5.11049   21.19477  1.000 30.71894 ? 283 GLU   A CA  1 
ATOM   2176 C  C   . GLU   A 1 283 ? 22.54556  5.05551   21.92055  1.000 31.94373 ? 283 GLU   A C   1 
ATOM   2177 O  O   . GLU   A 1 283 ? 21.96865  3.97539   22.08976  1.000 30.45043 ? 283 GLU   A O   1 
ATOM   2178 C  CB  . GLU   A 1 283 ? 25.04168  5.15763   22.19042  1.000 32.55494 ? 283 GLU   A CB  1 
ATOM   2179 C  CG  . GLU   A 1 283 ? 24.93997  4.15477   23.34586  1.000 33.91258 ? 283 GLU   A CG  1 
ATOM   2180 C  CD  . GLU   A 1 283 ? 25.17509  2.70559   22.92959  1.000 36.16384 ? 283 GLU   A CD  1 
ATOM   2181 O  OE1 . GLU   A 1 283 ? 25.23964  2.41956   21.71430  1.000 32.30937 ? 283 GLU   A OE1 1 
ATOM   2182 O  OE2 . GLU   A 1 283 ? 25.30202  1.84639   23.83082  1.000 33.04162 ? 283 GLU   A OE2 1 
ATOM   2183 N  N   . LEU   A 1 284 ? 22.02285  6.21483   22.33145  1.000 31.45128 ? 284 LEU   A N   1 
ATOM   2184 C  CA  . LEU   A 1 284 ? 20.71406  6.24566   22.97716  1.000 30.63671 ? 284 LEU   A CA  1 
ATOM   2185 C  C   . LEU   A 1 284 ? 19.61240  5.81879   22.01449  1.000 29.34400 ? 284 LEU   A C   1 
ATOM   2186 O  O   . LEU   A 1 284 ? 18.65217  5.15113   22.41469  1.000 30.27513 ? 284 LEU   A O   1 
ATOM   2187 C  CB  . LEU   A 1 284 ? 20.43535  7.64242   23.53433  1.000 30.13935 ? 284 LEU   A CB  1 
ATOM   2188 C  CG  . LEU   A 1 284 ? 21.22171  8.01553   24.79228  1.000 31.39104 ? 284 LEU   A CG  1 
ATOM   2189 C  CD1 . LEU   A 1 284 ? 21.01623  9.47790   25.14685  1.000 31.53412 ? 284 LEU   A CD1 1 
ATOM   2190 C  CD2 . LEU   A 1 284 ? 20.81568  7.11839   25.95309  1.000 31.21518 ? 284 LEU   A CD2 1 
ATOM   2191 N  N   . LEU   A 1 285 ? 19.73358  6.19397   20.73974  1.000 29.61896 ? 285 LEU   A N   1 
ATOM   2192 C  CA  . LEU   A 1 285 ? 18.75122  5.77300   19.74523  1.000 29.81922 ? 285 LEU   A CA  1 
ATOM   2193 C  C   . LEU   A 1 285 ? 18.78619  4.26152   19.54378  1.000 28.43422 ? 285 LEU   A C   1 
ATOM   2194 O  O   . LEU   A 1 285 ? 17.74037  3.60147   19.53669  1.000 27.96698 ? 285 LEU   A O   1 
ATOM   2195 C  CB  . LEU   A 1 285 ? 18.99996  6.50516   18.42696  1.000 28.80999 ? 285 LEU   A CB  1 
ATOM   2196 C  CG  . LEU   A 1 285 ? 18.64829  7.99552   18.42187  1.000 28.88478 ? 285 LEU   A CG  1 
ATOM   2197 C  CD1 . LEU   A 1 285 ? 19.31250  8.70330   17.25458  1.000 28.83652 ? 285 LEU   A CD1 1 
ATOM   2198 C  CD2 . LEU   A 1 285 ? 17.14355  8.18296   18.37290  1.000 27.25402 ? 285 LEU   A CD2 1 
ATOM   2199 N  N   . ARG   A 1 286 ? 19.98505  3.69655   19.37716  1.000 27.92754 ? 286 ARG   A N   1 
ATOM   2200 C  CA  . ARG   A 1 286 ? 20.11860  2.24603   19.27588  1.000 31.38765 ? 286 ARG   A CA  1 
ATOM   2201 C  C   . ARG   A 1 286 ? 19.60897  1.55844   20.53372  1.000 30.96795 ? 286 ARG   A C   1 
ATOM   2202 O  O   . ARG   A 1 286 ? 18.87914  0.56276   20.45542  1.000 32.00447 ? 286 ARG   A O   1 
ATOM   2203 C  CB  . ARG   A 1 286 ? 21.57890  1.86311   19.03511  1.000 30.15226 ? 286 ARG   A CB  1 
ATOM   2204 C  CG  . ARG   A 1 286 ? 21.84059  0.36488   19.11405  1.000 32.80095 ? 286 ARG   A CG  1 
ATOM   2205 C  CD  . ARG   A 1 286 ? 23.30852  0.04268   19.33988  1.000 32.50803 ? 286 ARG   A CD  1 
ATOM   2206 N  NE  . ARG   A 1 286 ? 23.69889  0.17574   20.74134  1.000 32.69249 ? 286 ARG   A NE  1 
ATOM   2207 C  CZ  . ARG   A 1 286 ? 23.64604  -0.81096  21.63234  1.000 35.72880 ? 286 ARG   A CZ  1 
ATOM   2208 N  NH1 . ARG   A 1 286 ? 23.21067  -2.01311  21.27377  1.000 34.39314 ? 286 ARG   A NH1 1 
ATOM   2209 N  NH2 . ARG   A 1 286 ? 24.02979  -0.59667  22.88460  1.000 33.87165 ? 286 ARG   A NH2 1 
ATOM   2210 N  N   . TYR   A 1 287 ? 19.96859  2.09408   21.70421  1.000 29.17611 ? 287 TYR   A N   1 
ATOM   2211 C  CA  . TYR   A 1 287 ? 19.71832  1.40338   22.96563  1.000 30.15839 ? 287 TYR   A CA  1 
ATOM   2212 C  C   . TYR   A 1 287 ? 18.24517  1.45247   23.34784  1.000 31.56505 ? 287 TYR   A C   1 
ATOM   2213 O  O   . TYR   A 1 287 ? 17.69133  0.46107   23.83690  1.000 30.03028 ? 287 TYR   A O   1 
ATOM   2214 C  CB  . TYR   A 1 287 ? 20.57784  2.02870   24.06520  1.000 33.58286 ? 287 TYR   A CB  1 
ATOM   2215 C  CG  . TYR   A 1 287 ? 20.80331  1.16604   25.28452  1.000 35.25082 ? 287 TYR   A CG  1 
ATOM   2216 C  CD1 . TYR   A 1 287 ? 21.47658  -0.04620  25.18814  1.000 35.92480 ? 287 TYR   A CD1 1 
ATOM   2217 C  CD2 . TYR   A 1 287 ? 20.37451  1.57988   26.53855  1.000 36.03495 ? 287 TYR   A CD2 1 
ATOM   2218 C  CE1 . TYR   A 1 287 ? 21.69551  -0.83234  26.30377  1.000 37.23305 ? 287 TYR   A CE1 1 
ATOM   2219 C  CE2 . TYR   A 1 287 ? 20.59106  0.80167   27.66010  1.000 36.46475 ? 287 TYR   A CE2 1 
ATOM   2220 C  CZ  . TYR   A 1 287 ? 21.25108  -0.40359  27.53647  1.000 38.28627 ? 287 TYR   A CZ  1 
ATOM   2221 O  OH  . TYR   A 1 287 ? 21.47039  -1.18474  28.64826  1.000 38.92641 ? 287 TYR   A OH  1 
ATOM   2222 N  N   . LEU   A 1 288 ? 17.59536  2.59754   23.14173  1.000 32.28154 ? 288 LEU   A N   1 
ATOM   2223 C  CA  . LEU   A 1 288 ? 16.21631  2.77575   23.57880  1.000 29.81750 ? 288 LEU   A CA  1 
ATOM   2224 C  C   . LEU   A 1 288 ? 15.19845  2.33666   22.53503  1.000 29.47119 ? 288 LEU   A C   1 
ATOM   2225 O  O   . LEU   A 1 288 ? 14.10187  1.90401   22.90886  1.000 29.07713 ? 288 LEU   A O   1 
ATOM   2226 C  CB  . LEU   A 1 288 ? 15.97681  4.24118   23.95845  1.000 30.91411 ? 288 LEU   A CB  1 
ATOM   2227 C  CG  . LEU   A 1 288 ? 16.81236  4.71216   25.15267  1.000 31.64206 ? 288 LEU   A CG  1 
ATOM   2228 C  CD1 . LEU   A 1 288 ? 16.69468  6.21264   25.36926  1.000 31.11948 ? 288 LEU   A CD1 1 
ATOM   2229 C  CD2 . LEU   A 1 288 ? 16.40568  3.95429   26.41150  1.000 31.41077 ? 288 LEU   A CD2 1 
ATOM   2230 N  N   . ALA   A 1 289 ? 15.54078  2.45110   21.24536  1.000 29.33165 ? 289 ALA   A N   1 
ATOM   2231 C  CA  . ALA   A 1 289 ? 14.72570  1.99966   20.11740  1.000 30.21127 ? 289 ALA   A CA  1 
ATOM   2232 C  C   . ALA   A 1 289 ? 13.22845  2.13236   20.37011  1.000 31.60197 ? 289 ALA   A C   1 
ATOM   2233 O  O   . ALA   A 1 289 ? 12.51303  1.12696   20.42147  1.000 26.64321 ? 289 ALA   A O   1 
ATOM   2234 C  CB  . ALA   A 1 289 ? 15.07113  0.54976   19.77579  1.000 28.94095 ? 289 ALA   A CB  1 
ATOM   2235 N  N   . ILE   A 1 290 ? 12.74767  3.36835   20.53186  1.000 29.29762 ? 290 ILE   A N   1 
ATOM   2236 C  CA  . ILE   A 1 290 ? 11.37927  3.59848   20.98212  1.000 30.46295 ? 290 ILE   A CA  1 
ATOM   2237 C  C   . ILE   A 1 290 ? 10.32917  3.29556   19.92572  1.000 31.07069 ? 290 ILE   A C   1 
ATOM   2238 O  O   . ILE   A 1 290 ? 9.14081   3.22250   20.25656  1.000 32.09123 ? 290 ILE   A O   1 
ATOM   2239 C  CB  . ILE   A 1 290 ? 11.20742  5.05346   21.45961  1.000 30.31035 ? 290 ILE   A CB  1 
ATOM   2240 C  CG1 . ILE   A 1 290 ? 11.38046  6.01336   20.27991  1.000 29.86149 ? 290 ILE   A CG1 1 
ATOM   2241 C  CG2 . ILE   A 1 290 ? 12.20950  5.36674   22.55983  1.000 29.17455 ? 290 ILE   A CG2 1 
ATOM   2242 C  CD1 . ILE   A 1 290 ? 10.61954  7.29048   20.42689  1.000 30.22271 ? 290 ILE   A CD1 1 
ATOM   2243 N  N   . ALA   A 1 291 ? 10.72453  3.11998   18.66431  1.000 33.04223 ? 291 ALA   A N   1 
ATOM   2244 C  CA  . ALA   A 1 291 ? 9.78625   2.81387   17.59108  1.000 31.64461 ? 291 ALA   A CA  1 
ATOM   2245 C  C   . ALA   A 1 291 ? 9.85102   1.35155   17.16239  1.000 35.19593 ? 291 ALA   A C   1 
ATOM   2246 O  O   . ALA   A 1 291 ? 9.63444   1.03918   15.98459  1.000 30.00431 ? 291 ALA   A O   1 
ATOM   2247 C  CB  . ALA   A 1 291 ? 10.03298  3.72746   16.39070  1.000 30.67727 ? 291 ALA   A CB  1 
ATOM   2248 N  N   . ASP   A 1 292 ? 10.13595  0.44256   18.09810  1.000 33.81187 ? 292 ASP   A N   1 
ATOM   2249 C  CA  . ASP   A 1 292 ? 10.29554  -0.96048  17.73056  1.000 35.99556 ? 292 ASP   A CA  1 
ATOM   2250 C  C   . ASP   A 1 292 ? 8.97492   -1.64758  17.41423  1.000 36.40178 ? 292 ASP   A C   1 
ATOM   2251 O  O   . ASP   A 1 292 ? 8.98907   -2.82278  17.02936  1.000 37.33200 ? 292 ASP   A O   1 
ATOM   2252 C  CB  . ASP   A 1 292 ? 11.03867  -1.72281  18.83447  1.000 34.86321 ? 292 ASP   A CB  1 
ATOM   2253 C  CG  . ASP   A 1 292 ? 10.33611  -1.66209  20.18187  1.000 34.07476 ? 292 ASP   A CG  1 
ATOM   2254 O  OD1 . ASP   A 1 292 ? 9.25702   -1.04337  20.28184  1.000 34.63450 ? 292 ASP   A OD1 1 
ATOM   2255 O  OD2 . ASP   A 1 292 ? 10.87089  -2.24286  21.15071  1.000 38.69489 ? 292 ASP   A OD2 1 
ATOM   2256 N  N   . ILE   A 1 293 ? 7.84549   -0.95327  17.56905  1.000 38.57370 ? 293 ILE   A N   1 
ATOM   2257 C  CA  . ILE   A 1 293 ? 6.56268   -1.49889  17.13896  1.000 38.95819 ? 293 ILE   A CA  1 
ATOM   2258 C  C   . ILE   A 1 293 ? 6.28128   -1.21218  15.66643  1.000 39.86286 ? 293 ILE   A C   1 
ATOM   2259 O  O   . ILE   A 1 293 ? 5.46093   -1.91234  15.05526  1.000 38.78320 ? 293 ILE   A O   1 
ATOM   2260 C  CB  . ILE   A 1 293 ? 5.41819   -0.95709  18.01785  1.000 38.88364 ? 293 ILE   A CB  1 
ATOM   2261 C  CG1 . ILE   A 1 293 ? 4.16957   -1.83259  17.89486  1.000 39.68406 ? 293 ILE   A CG1 1 
ATOM   2262 C  CG2 . ILE   A 1 293 ? 5.09012   0.49171   17.65563  1.000 39.69605 ? 293 ILE   A CG2 1 
ATOM   2263 C  CD1 . ILE   A 1 293 ? 4.41020   -3.28784  18.23540  1.000 39.83731 ? 293 ILE   A CD1 1 
ATOM   2264 N  N   . ALA   A 1 294 ? 6.95955   -0.22771  15.07385  1.000 38.54333 ? 294 ALA   A N   1 
ATOM   2265 C  CA  . ALA   A 1 294 ? 6.70266   0.20289   13.69860  1.000 37.10084 ? 294 ALA   A CA  1 
ATOM   2266 C  C   . ALA   A 1 294 ? 7.52372   -0.56808  12.67253  1.000 37.40286 ? 294 ALA   A C   1 
ATOM   2267 O  O   . ALA   A 1 294 ? 8.09559   0.02302   11.75192  1.000 39.62922 ? 294 ALA   A O   1 
ATOM   2268 C  CB  . ALA   A 1 294 ? 6.95770   1.70174   13.57354  1.000 39.41015 ? 294 ALA   A CB  1 
ATOM   2269 N  N   . GLY   A 1 295 ? 7.59370   -1.89240  12.78632  1.000 34.72455 ? 295 GLY   A N   1 
ATOM   2270 C  CA  . GLY   A 1 295 ? 8.30320   -2.70287  11.81812  1.000 35.51034 ? 295 GLY   A CA  1 
ATOM   2271 C  C   . GLY   A 1 295 ? 7.43632   -3.57508  10.94326  1.000 32.36421 ? 295 GLY   A C   1 
ATOM   2272 O  O   . GLY   A 1 295 ? 7.97052   -4.47138  10.27234  1.000 34.64546 ? 295 GLY   A O   1 
ATOM   2273 N  N   . GLY   A 1 296 ? 6.12844   -3.34118  10.89555  1.000 34.25144 ? 296 GLY   A N   1 
ATOM   2274 C  CA  . GLY   A 1 296 ? 5.22652   -4.29179  10.26884  1.000 32.83806 ? 296 GLY   A CA  1 
ATOM   2275 C  C   . GLY   A 1 296 ? 5.36046   -4.31485  8.75551   1.000 34.74951 ? 296 GLY   A C   1 
ATOM   2276 O  O   . GLY   A 1 296 ? 5.48360   -3.27860  8.10010   1.000 31.46931 ? 296 GLY   A O   1 
ATOM   2277 N  N   . ARG   A 1 297 ? 5.32855   -5.52632  8.20211   1.000 31.08777 ? 297 ARG   A N   1 
ATOM   2278 C  CA  . ARG   A 1 297 ? 5.37273   -5.75800  6.76547   1.000 31.25805 ? 297 ARG   A CA  1 
ATOM   2279 C  C   . ARG   A 1 297 ? 4.48239   -6.95134  6.44723   1.000 34.97036 ? 297 ARG   A C   1 
ATOM   2280 O  O   . ARG   A 1 297 ? 4.18160   -7.77189  7.31803   1.000 29.84158 ? 297 ARG   A O   1 
ATOM   2281 C  CB  . ARG   A 1 297 ? 6.80367   -6.02258  6.27308   1.000 31.19753 ? 297 ARG   A CB  1 
ATOM   2282 C  CG  . ARG   A 1 297 ? 7.79675   -4.88346  6.48895   1.000 32.80395 ? 297 ARG   A CG  1 
ATOM   2283 C  CD  . ARG   A 1 297 ? 7.44660   -3.67022  5.64267   1.000 29.95805 ? 297 ARG   A CD  1 
ATOM   2284 N  NE  . ARG   A 1 297 ? 8.53205   -2.69414  5.57739   1.000 28.85415 ? 297 ARG   A NE  1 
ATOM   2285 C  CZ  . ARG   A 1 297 ? 8.70410   -1.69753  6.44165   1.000 31.50610 ? 297 ARG   A CZ  1 
ATOM   2286 N  NH1 . ARG   A 1 297 ? 7.86855   -1.54023  7.46208   1.000 28.06863 ? 297 ARG   A NH1 1 
ATOM   2287 N  NH2 . ARG   A 1 297 ? 9.71869   -0.85638  6.28553   1.000 29.01309 ? 297 ARG   A NH2 1 
ATOM   2288 N  N   . VAL   A 1 298 ? 4.06103   -7.04562  5.18801   1.000 33.44779 ? 298 VAL   A N   1 
ATOM   2289 C  CA  . VAL   A 1 298 ? 3.30479   -8.19632  4.70449   1.000 33.56329 ? 298 VAL   A CA  1 
ATOM   2290 C  C   . VAL   A 1 298 ? 3.94997   -8.68738  3.41494   1.000 32.63204 ? 298 VAL   A C   1 
ATOM   2291 O  O   . VAL   A 1 298 ? 4.28684   -7.88559  2.53639   1.000 32.42460 ? 298 VAL   A O   1 
ATOM   2292 C  CB  . VAL   A 1 298 ? 1.81176   -7.86691  4.49264   1.000 35.08402 ? 298 VAL   A CB  1 
ATOM   2293 C  CG1 . VAL   A 1 298 ? 1.62887   -6.69715  3.51785   1.000 32.37339 ? 298 VAL   A CG1 1 
ATOM   2294 C  CG2 . VAL   A 1 298 ? 1.04967   -9.10565  4.02254   1.000 35.29821 ? 298 VAL   A CG2 1 
ATOM   2295 N  N   . ALA   A 1 299 ? 4.14132   -10.00024 3.31240   1.000 34.05079 ? 299 ALA   A N   1 
ATOM   2296 C  CA  . ALA   A 1 299 ? 4.80435   -10.58482 2.15473   1.000 34.94847 ? 299 ALA   A CA  1 
ATOM   2297 C  C   . ALA   A 1 299 ? 3.82982   -10.71339 0.99124   1.000 33.65351 ? 299 ALA   A C   1 
ATOM   2298 O  O   . ALA   A 1 299 ? 2.74646   -11.28570 1.13795   1.000 35.42622 ? 299 ALA   A O   1 
ATOM   2299 C  CB  . ALA   A 1 299 ? 5.38797   -11.95262 2.51024   1.000 34.64375 ? 299 ALA   A CB  1 
ATOM   2300 N  N   . THR   A 1 300 ? 4.21315   -10.17255 -0.16335  1.000 35.22026 ? 300 THR   A N   1 
ATOM   2301 C  CA  . THR   A 1 300 ? 3.44024   -10.32671 -1.38777  1.000 35.78063 ? 300 THR   A CA  1 
ATOM   2302 C  C   . THR   A 1 300 ? 3.96779   -11.44894 -2.27164  1.000 36.81747 ? 300 THR   A C   1 
ATOM   2303 O  O   . THR   A 1 300 ? 3.40867   -11.69138 -3.34491  1.000 36.24199 ? 300 THR   A O   1 
ATOM   2304 C  CB  . THR   A 1 300 ? 3.41579   -9.01210  -2.17779  1.000 36.55817 ? 300 THR   A CB  1 
ATOM   2305 O  OG1 . THR   A 1 300 ? 4.75269   -8.62410  -2.51349  1.000 34.94365 ? 300 THR   A OG1 1 
ATOM   2306 C  CG2 . THR   A 1 300 ? 2.76579   -7.90915  -1.35604  1.000 35.34363 ? 300 THR   A CG2 1 
ATOM   2307 N  N   . ALA   A 1 301 ? 5.02931   -12.12901 -1.84735  1.000 36.82314 ? 301 ALA   A N   1 
ATOM   2308 C  CA  . ALA   A 1 301 ? 5.57095   -13.27903 -2.55798  1.000 38.44492 ? 301 ALA   A CA  1 
ATOM   2309 C  C   . ALA   A 1 301 ? 6.42018   -14.07472 -1.57713  1.000 39.07337 ? 301 ALA   A C   1 
ATOM   2310 O  O   . ALA   A 1 301 ? 6.74231   -13.60524 -0.48301  1.000 36.41912 ? 301 ALA   A O   1 
ATOM   2311 C  CB  . ALA   A 1 301 ? 6.38682   -12.85618 -3.78508  1.000 37.59662 ? 301 ALA   A CB  1 
ATOM   2312 N  N   . ASP   A 1 302 ? 6.77843   -15.28983 -1.98201  1.000 40.56060 ? 302 ASP   A N   1 
ATOM   2313 C  CA  . ASP   A 1 302 ? 7.60185   -16.14090 -1.13453  1.000 41.04646 ? 302 ASP   A CA  1 
ATOM   2314 C  C   . ASP   A 1 302 ? 8.99447   -15.54674 -0.96193  1.000 40.76207 ? 302 ASP   A C   1 
ATOM   2315 O  O   . ASP   A 1 302 ? 9.59759   -15.03973 -1.91289  1.000 38.12121 ? 302 ASP   A O   1 
ATOM   2316 C  CB  . ASP   A 1 302 ? 7.70470   -17.54616 -1.72337  1.000 42.66603 ? 302 ASP   A CB  1 
ATOM   2317 C  CG  . ASP   A 1 302 ? 6.43544   -18.35152 -1.53103  1.000 45.84896 ? 302 ASP   A CG  1 
ATOM   2318 O  OD1 . ASP   A 1 302 ? 5.41473   -17.76462 -1.11205  1.000 42.89649 ? 302 ASP   A OD1 1 
ATOM   2319 O  OD2 . ASP   A 1 302 ? 6.46228   -19.57346 -1.79005  1.000 46.68810 ? 302 ASP   A OD2 1 
ATOM   2320 N  N   . ILE   A 1 303 ? 9.49999   -15.60633 0.26805   1.000 40.85872 ? 303 ILE   A N   1 
ATOM   2321 C  CA  . ILE   A 1 303 ? 10.83147  -15.11893 0.61222   1.000 41.94255 ? 303 ILE   A CA  1 
ATOM   2322 C  C   . ILE   A 1 303 ? 11.49562  -16.17521 1.48158   1.000 43.43938 ? 303 ILE   A C   1 
ATOM   2323 O  O   . ILE   A 1 303 ? 10.98667  -16.49984 2.56058   1.000 44.00442 ? 303 ILE   A O   1 
ATOM   2324 C  CB  . ILE   A 1 303 ? 10.78583  -13.77113 1.35576   1.000 40.65000 ? 303 ILE   A CB  1 
ATOM   2325 C  CG1 . ILE   A 1 303 ? 9.96120   -12.74506 0.57838   1.000 39.25793 ? 303 ILE   A CG1 1 
ATOM   2326 C  CG2 . ILE   A 1 303 ? 12.19762  -13.25201 1.61067   1.000 39.85104 ? 303 ILE   A CG2 1 
ATOM   2327 C  CD1 . ILE   A 1 303 ? 9.56838   -11.53115 1.39673   1.000 36.97782 ? 303 ILE   A CD1 1 
ATOM   2328 N  N   . GLU   A 1 304 ? 12.62101  -16.71172 1.02181   1.000 44.77492 ? 304 GLU   A N   1 
ATOM   2329 C  CA  . GLU   A 1 304 ? 13.39433  -17.66235 1.80856   1.000 47.30563 ? 304 GLU   A CA  1 
ATOM   2330 C  C   . GLU   A 1 304 ? 14.53446  -16.92698 2.50005   1.000 46.79347 ? 304 GLU   A C   1 
ATOM   2331 O  O   . GLU   A 1 304 ? 15.29732  -16.19982 1.85335   1.000 46.43371 ? 304 GLU   A O   1 
ATOM   2332 C  CB  . GLU   A 1 304 ? 13.92591  -18.80608 0.94183   1.000 50.72989 ? 304 GLU   A CB  1 
ATOM   2333 C  CG  . GLU   A 1 304 ? 14.66452  -18.39293 -0.31795  1.000 55.47739 ? 304 GLU   A CG  1 
ATOM   2334 C  CD  . GLU   A 1 304 ? 14.89533  -19.56631 -1.25277  1.000 63.48668 ? 304 GLU   A CD  1 
ATOM   2335 O  OE1 . GLU   A 1 304 ? 13.92944  -20.31321 -1.52006  1.000 63.94534 ? 304 GLU   A OE1 1 
ATOM   2336 O  OE2 . GLU   A 1 304 ? 16.04316  -19.75169 -1.70820  1.000 66.26550 ? 304 GLU   A OE2 1 
ATOM   2337 N  N   . VAL   A 1 305 ? 14.63125  -17.10234 3.81488   1.000 46.53535 ? 305 VAL   A N   1 
ATOM   2338 C  CA  . VAL   A 1 305 ? 15.58969  -16.38472 4.64674   1.000 46.64114 ? 305 VAL   A CA  1 
ATOM   2339 C  C   . VAL   A 1 305 ? 16.40593  -17.43124 5.39569   1.000 47.26933 ? 305 VAL   A C   1 
ATOM   2340 O  O   . VAL   A 1 305 ? 15.93373  -18.00921 6.38372   1.000 47.36628 ? 305 VAL   A O   1 
ATOM   2341 C  CB  . VAL   A 1 305 ? 14.90259  -15.42207 5.62235   1.000 45.41794 ? 305 VAL   A CB  1 
ATOM   2342 C  CG1 . VAL   A 1 305 ? 15.91206  -14.44961 6.21419   1.000 43.80851 ? 305 VAL   A CG1 1 
ATOM   2343 C  CG2 . VAL   A 1 305 ? 13.76597  -14.67791 4.93552   1.000 42.77437 ? 305 VAL   A CG2 1 
ATOM   2344 N  N   . GLU   A 1 306 ? 17.62820  -17.68035 4.92754   1.000 48.50207 ? 306 GLU   A N   1 
ATOM   2345 C  CA  . GLU   A 1 306 ? 18.58459  -18.56441 5.60283   1.000 47.84968 ? 306 GLU   A CA  1 
ATOM   2346 C  C   . GLU   A 1 306 ? 17.96297  -19.92104 5.93213   1.000 48.40447 ? 306 GLU   A C   1 
ATOM   2347 O  O   . GLU   A 1 306 ? 18.06210  -20.42605 7.05312   1.000 47.12477 ? 306 GLU   A O   1 
ATOM   2348 C  CB  . GLU   A 1 306 ? 19.14150  -17.89826 6.86293   1.000 47.64662 ? 306 GLU   A CB  1 
ATOM   2349 C  CG  . GLU   A 1 306 ? 19.90881  -16.61769 6.58855   1.000 48.33680 ? 306 GLU   A CG  1 
ATOM   2350 C  CD  . GLU   A 1 306 ? 20.33684  -15.90522 7.85616   1.000 48.55154 ? 306 GLU   A CD  1 
ATOM   2351 O  OE1 . GLU   A 1 306 ? 20.56553  -16.58119 8.88298   1.000 51.32511 ? 306 GLU   A OE1 1 
ATOM   2352 O  OE2 . GLU   A 1 306 ? 20.43741  -14.66208 7.82487   1.000 47.23437 ? 306 GLU   A OE2 1 
ATOM   2353 N  N   . GLY   A 1 307 ? 17.29914  -20.51080 4.93792   1.000 49.02481 ? 307 GLY   A N   1 
ATOM   2354 C  CA  . GLY   A 1 307 ? 16.66786  -21.80196 5.09354   1.000 48.94468 ? 307 GLY   A CA  1 
ATOM   2355 C  C   . GLY   A 1 307 ? 15.23868  -21.76736 5.59521   1.000 49.05471 ? 307 GLY   A C   1 
ATOM   2356 O  O   . GLY   A 1 307 ? 14.51525  -22.75460 5.42720   1.000 50.68134 ? 307 GLY   A O   1 
ATOM   2357 N  N   . GLN   A 1 308 ? 14.80901  -20.66721 6.20437   1.000 48.88924 ? 308 GLN   A N   1 
ATOM   2358 C  CA  . GLN   A 1 308 ? 13.41897  -20.50676 6.60534   1.000 48.81831 ? 308 GLN   A CA  1 
ATOM   2359 C  C   . GLN   A 1 308 ? 12.64315  -19.79874 5.50063   1.000 47.59947 ? 308 GLN   A C   1 
ATOM   2360 O  O   . GLN   A 1 308 ? 13.17106  -18.90885 4.82760   1.000 47.38930 ? 308 GLN   A O   1 
ATOM   2361 C  CB  . GLN   A 1 308 ? 13.31762  -19.72481 7.91788   1.000 48.49210 ? 308 GLN   A CB  1 
ATOM   2362 C  CG  . GLN   A 1 308 ? 11.93614  -19.76610 8.55779   1.000 49.42295 ? 308 GLN   A CG  1 
ATOM   2363 C  CD  . GLN   A 1 308 ? 11.42120  -21.18169 8.74940   1.000 51.10487 ? 308 GLN   A CD  1 
ATOM   2364 O  OE1 . GLN   A 1 308 ? 10.74291  -21.72994 7.87971   1.000 49.37027 ? 308 GLN   A OE1 1 
ATOM   2365 N  NE2 . GLN   A 1 308 ? 11.74121  -21.78031 9.89178   1.000 49.51829 ? 308 GLN   A NE2 1 
ATOM   2366 N  N   . LEU   A 1 309 ? 11.38994  -20.20048 5.31134   1.000 47.55577 ? 309 LEU   A N   1 
ATOM   2367 C  CA  . LEU   A 1 309 ? 10.58060  -19.72777 4.19444   1.000 46.59183 ? 309 LEU   A CA  1 
ATOM   2368 C  C   . LEU   A 1 309 ? 9.45735   -18.83024 4.69703   1.000 44.40112 ? 309 LEU   A C   1 
ATOM   2369 O  O   . LEU   A 1 309 ? 8.61042   -19.26694 5.48454   1.000 44.90623 ? 309 LEU   A O   1 
ATOM   2370 C  CB  . LEU   A 1 309 ? 10.00043  -20.89876 3.40406   1.000 46.41817 ? 309 LEU   A CB  1 
ATOM   2371 C  CG  . LEU   A 1 309 ? 9.01215   -20.49005 2.30826   1.000 47.05196 ? 309 LEU   A CG  1 
ATOM   2372 C  CD1 . LEU   A 1 309 ? 9.68708   -19.59317 1.27695   1.000 45.72981 ? 309 LEU   A CD1 1 
ATOM   2373 C  CD2 . LEU   A 1 309 ? 8.38869   -21.71276 1.64386   1.000 48.93604 ? 309 LEU   A CD2 1 
ATOM   2374 N  N   . ILE   A 1 310 ? 9.44561   -17.58830 4.22478   1.000 44.51255 ? 310 ILE   A N   1 
ATOM   2375 C  CA  . ILE   A 1 310 ? 8.32317   -16.67965 4.42500   1.000 42.63247 ? 310 ILE   A CA  1 
ATOM   2376 C  C   . ILE   A 1 310 ? 7.37145   -16.85146 3.24765   1.000 41.47479 ? 310 ILE   A C   1 
ATOM   2377 O  O   . ILE   A 1 310 ? 7.77553   -16.72128 2.08715   1.000 42.18754 ? 310 ILE   A O   1 
ATOM   2378 C  CB  . ILE   A 1 310 ? 8.79998   -15.22395 4.54570   1.000 41.96142 ? 310 ILE   A CB  1 
ATOM   2379 C  CG1 . ILE   A 1 310 ? 9.52690   -15.00217 5.87630   1.000 42.06476 ? 310 ILE   A CG1 1 
ATOM   2380 C  CG2 . ILE   A 1 310 ? 7.62951   -14.25258 4.38156   1.000 40.43571 ? 310 ILE   A CG2 1 
ATOM   2381 C  CD1 . ILE   A 1 310 ? 10.20425  -13.65419 5.97958   1.000 39.86651 ? 310 ILE   A CD1 1 
ATOM   2382 N  N   . ARG   A 1 311 ? 6.11312   -17.15490 3.54135   1.000 41.49133 ? 311 ARG   A N   1 
ATOM   2383 C  CA  . ARG   A 1 311 ? 5.11757   -17.36800 2.50318   1.000 41.69914 ? 311 ARG   A CA  1 
ATOM   2384 C  C   . ARG   A 1 311 ? 4.40132   -16.06625 2.17181   1.000 40.57407 ? 311 ARG   A C   1 
ATOM   2385 O  O   . ARG   A 1 311 ? 4.26166   -15.18051 3.01799   1.000 39.40481 ? 311 ARG   A O   1 
ATOM   2386 C  CB  . ARG   A 1 311 ? 4.09639   -18.42164 2.93672   1.000 43.17951 ? 311 ARG   A CB  1 
ATOM   2387 C  CG  . ARG   A 1 311 ? 4.68111   -19.80958 3.13130   1.000 44.25362 ? 311 ARG   A CG  1 
ATOM   2388 C  CD  . ARG   A 1 311 ? 3.59058   -20.84844 3.37126   1.000 46.15283 ? 311 ARG   A CD  1 
ATOM   2389 N  NE  . ARG   A 1 311 ? 3.35673   -21.10133 4.79124   1.000 51.23908 ? 311 ARG   A NE  1 
ATOM   2390 C  CZ  . ARG   A 1 311 ? 2.31446   -20.64131 5.47686   1.000 48.08813 ? 311 ARG   A CZ  1 
ATOM   2391 N  NH1 . ARG   A 1 311 ? 1.39479   -19.89874 4.87551   1.000 55.81368 ? 311 ARG   A NH1 1 
ATOM   2392 N  NH2 . ARG   A 1 311 ? 2.18800   -20.92970 6.76472   1.000 44.86616 ? 311 ARG   A NH2 1 
ATOM   2393 N  N   . ALA   A 1 312 ? 3.95277   -15.95743 0.92241   1.000 40.13446 ? 312 ALA   A N   1 
ATOM   2394 C  CA  . ALA   A 1 312 ? 3.12839   -14.82516 0.52556   1.000 39.05117 ? 312 ALA   A CA  1 
ATOM   2395 C  C   . ALA   A 1 312 ? 1.87678   -14.76595 1.39093   1.000 38.95208 ? 312 ALA   A C   1 
ATOM   2396 O  O   . ALA   A 1 312 ? 1.25943   -15.79166 1.69315   1.000 38.30960 ? 312 ALA   A O   1 
ATOM   2397 C  CB  . ALA   A 1 312 ? 2.74601   -14.92978 -0.95167  1.000 38.27747 ? 312 ALA   A CB  1 
ATOM   2398 N  N   . GLY   A 1 313 ? 1.51210   -13.55540 1.80405   1.000 36.24732 ? 313 GLY   A N   1 
ATOM   2399 C  CA  . GLY   A 1 313 ? 0.37515   -13.36199 2.67513   1.000 37.22075 ? 313 GLY   A CA  1 
ATOM   2400 C  C   . GLY   A 1 313 ? 0.68162   -13.43245 4.15409   1.000 37.48113 ? 313 GLY   A C   1 
ATOM   2401 O  O   . GLY   A 1 313 ? -0.23195  -13.24588 4.96737   1.000 38.02566 ? 313 GLY   A O   1 
ATOM   2402 N  N   . GLU   A 1 314 ? 1.92782   -13.70545 4.53090   1.000 35.69190 ? 314 GLU   A N   1 
ATOM   2403 C  CA  . GLU   A 1 314 ? 2.31693   -13.75783 5.93235   1.000 37.33558 ? 314 GLU   A CA  1 
ATOM   2404 C  C   . GLU   A 1 314 ? 2.76676   -12.38583 6.41353   1.000 35.88911 ? 314 GLU   A C   1 
ATOM   2405 O  O   . GLU   A 1 314 ? 3.41002   -11.63347 5.67574   1.000 34.68292 ? 314 GLU   A O   1 
ATOM   2406 C  CB  . GLU   A 1 314 ? 3.44229   -14.77061 6.15043   1.000 38.44543 ? 314 GLU   A CB  1 
ATOM   2407 C  CG  . GLU   A 1 314 ? 2.99242   -16.21982 6.14782   1.000 40.25161 ? 314 GLU   A CG  1 
ATOM   2408 C  CD  . GLU   A 1 314 ? 3.96487   -17.11776 6.88023   1.000 41.82830 ? 314 GLU   A CD  1 
ATOM   2409 O  OE1 . GLU   A 1 314 ? 5.05992   -17.37768 6.33772   1.000 42.00193 ? 314 GLU   A OE1 1 
ATOM   2410 O  OE2 . GLU   A 1 314 ? 3.64005   -17.54419 8.01014   1.000 42.01414 ? 314 GLU   A OE2 1 
ATOM   2411 N  N   . GLY   A 1 315 ? 2.42221   -12.06839 7.65915   1.000 35.80163 ? 315 GLY   A N   1 
ATOM   2412 C  CA  . GLY   A 1 315 ? 2.90198   -10.84399 8.27051   1.000 35.30492 ? 315 GLY   A CA  1 
ATOM   2413 C  C   . GLY   A 1 315 ? 4.29710   -11.03032 8.84637   1.000 36.14809 ? 315 GLY   A C   1 
ATOM   2414 O  O   . GLY   A 1 315 ? 4.63164   -12.07627 9.40314   1.000 36.29611 ? 315 GLY   A O   1 
ATOM   2415 N  N   . VAL   A 1 316 ? 5.12200   -9.99844  8.68579   1.000 33.74795 ? 316 VAL   A N   1 
ATOM   2416 C  CA  . VAL   A 1 316 ? 6.48013   -9.97305  9.21337   1.000 33.77743 ? 316 VAL   A CA  1 
ATOM   2417 C  C   . VAL   A 1 316 ? 6.66618   -8.67082  9.97931   1.000 34.74018 ? 316 VAL   A C   1 
ATOM   2418 O  O   . VAL   A 1 316 ? 6.21981   -7.60968  9.53040   1.000 34.77725 ? 316 VAL   A O   1 
ATOM   2419 C  CB  . VAL   A 1 316 ? 7.53407   -10.10041 8.09252   1.000 34.19715 ? 316 VAL   A CB  1 
ATOM   2420 C  CG1 . VAL   A 1 316 ? 8.92910   -10.22157 8.68452   1.000 34.16978 ? 316 VAL   A CG1 1 
ATOM   2421 C  CG2 . VAL   A 1 316 ? 7.22694   -11.29098 7.19622   1.000 35.57956 ? 316 VAL   A CG2 1 
ATOM   2422 N  N   . ILE   A 1 317 ? 7.31753   -8.75025  11.13701  1.000 33.87774 ? 317 ILE   A N   1 
ATOM   2423 C  CA  . ILE   A 1 317 ? 7.58033   -7.58691  11.97790  1.000 33.91484 ? 317 ILE   A CA  1 
ATOM   2424 C  C   . ILE   A 1 317 ? 9.08409   -7.50888  12.21328  1.000 34.48555 ? 317 ILE   A C   1 
ATOM   2425 O  O   . ILE   A 1 317 ? 9.66176   -8.37478  12.88397  1.000 30.33055 ? 317 ILE   A O   1 
ATOM   2426 C  CB  . ILE   A 1 317 ? 6.81564   -7.65171  13.30707  1.000 34.97493 ? 317 ILE   A CB  1 
ATOM   2427 C  CG1 . ILE   A 1 317 ? 5.31460   -7.80155  13.05596  1.000 36.30092 ? 317 ILE   A CG1 1 
ATOM   2428 C  CG2 . ILE   A 1 317 ? 7.08452   -6.40620  14.13229  1.000 34.83666 ? 317 ILE   A CG2 1 
ATOM   2429 C  CD1 . ILE   A 1 317 ? 4.49188   -7.91894  14.31749  1.000 36.84245 ? 317 ILE   A CD1 1 
ATOM   2430 N  N   . VAL   A 1 318 ? 9.71804   -6.47566  11.66133  1.000 32.33537 ? 318 VAL   A N   1 
ATOM   2431 C  CA  . VAL   A 1 318 ? 11.14076  -6.22141  11.86554  1.000 31.16964 ? 318 VAL   A CA  1 
ATOM   2432 C  C   . VAL   A 1 318 ? 11.27274  -5.42446  13.16066  1.000 33.10829 ? 318 VAL   A C   1 
ATOM   2433 O  O   . VAL   A 1 318 ? 11.03289  -4.21745  13.18804  1.000 31.07679 ? 318 VAL   A O   1 
ATOM   2434 C  CB  . VAL   A 1 318 ? 11.75527  -5.48219  10.67559  1.000 32.68866 ? 318 VAL   A CB  1 
ATOM   2435 C  CG1 . VAL   A 1 318 ? 13.22329  -5.17931  10.92930  1.000 28.21735 ? 318 VAL   A CG1 1 
ATOM   2436 C  CG2 . VAL   A 1 318 ? 11.57810  -6.29101  9.39330   1.000 31.38455 ? 318 VAL   A CG2 1 
ATOM   2437 N  N   . VAL   A 1 319 ? 11.65970  -6.10449  14.23863  1.000 30.35626 ? 319 VAL   A N   1 
ATOM   2438 C  CA  . VAL   A 1 319 ? 11.71560  -5.50575  15.57161  1.000 32.69281 ? 319 VAL   A CA  1 
ATOM   2439 C  C   . VAL   A 1 319 ? 13.09888  -4.88300  15.74233  1.000 32.03885 ? 319 VAL   A C   1 
ATOM   2440 O  O   . VAL   A 1 319 ? 14.06581  -5.57203  16.07387  1.000 30.82954 ? 319 VAL   A O   1 
ATOM   2441 C  CB  . VAL   A 1 319 ? 11.42209  -6.53646  16.66296  1.000 32.79071 ? 319 VAL   A CB  1 
ATOM   2442 C  CG1 . VAL   A 1 319 ? 11.27530  -5.85693  18.01911  1.000 32.93708 ? 319 VAL   A CG1 1 
ATOM   2443 C  CG2 . VAL   A 1 319 ? 10.17279  -7.32863  16.31385  1.000 32.37492 ? 319 VAL   A CG2 1 
ATOM   2444 N  N   . ASN   A 1 320 ? 13.19424  -3.56322  15.54232  1.000 31.29744 ? 320 ASN   A N   1 
ATOM   2445 C  CA  . ASN   A 1 320 ? 14.51129  -2.93590  15.49312  1.000 30.27507 ? 320 ASN   A CA  1 
ATOM   2446 C  C   . ASN   A 1 320 ? 15.19121  -2.87887  16.85574  1.000 30.29674 ? 320 ASN   A C   1 
ATOM   2447 O  O   . ASN   A 1 320 ? 16.42222  -2.80675  16.90753  1.000 31.58385 ? 320 ASN   A O   1 
ATOM   2448 C  CB  . ASN   A 1 320 ? 14.42753  -1.53065  14.87757  1.000 29.61357 ? 320 ASN   A CB  1 
ATOM   2449 C  CG  . ASN   A 1 320 ? 13.42480  -0.62616  15.57931  1.000 30.43624 ? 320 ASN   A CG  1 
ATOM   2450 O  OD1 . ASN   A 1 320 ? 13.63079  -0.21404  16.72133  1.000 29.76040 ? 320 ASN   A OD1 1 
ATOM   2451 N  ND2 . ASN   A 1 320 ? 12.34714  -0.28845  14.88204  1.000 32.10239 ? 320 ASN   A ND2 1 
ATOM   2452 N  N   . SER   A 1 321 ? 14.43465  -2.92044  17.95531  1.000 31.38011 ? 321 SER   A N   1 
ATOM   2453 C  CA  . SER   A 1 321 ? 15.06592  -2.97751  19.27307  1.000 29.93434 ? 321 SER   A CA  1 
ATOM   2454 C  C   . SER   A 1 321 ? 15.86616  -4.26470  19.44555  1.000 32.04407 ? 321 SER   A C   1 
ATOM   2455 O  O   . SER   A 1 321 ? 17.00082  -4.24464  19.93672  1.000 31.40873 ? 321 SER   A O   1 
ATOM   2456 C  CB  . SER   A 1 321 ? 14.01555  -2.84863  20.37757  1.000 32.14585 ? 321 SER   A CB  1 
ATOM   2457 O  OG  . SER   A 1 321 ? 13.03554  -3.86350  20.28065  1.000 29.25428 ? 321 SER   A OG  1 
ATOM   2458 N  N   . ILE   A 1 322 ? 15.28787  -5.39779  19.04705  1.000 32.13046 ? 322 ILE   A N   1 
ATOM   2459 C  CA  . ILE   A 1 322 ? 15.99935  -6.66967  19.13699  1.000 30.84272 ? 322 ILE   A CA  1 
ATOM   2460 C  C   . ILE   A 1 322 ? 17.19945  -6.67749  18.19784  1.000 31.23164 ? 322 ILE   A C   1 
ATOM   2461 O  O   . ILE   A 1 322 ? 18.29974  -7.09904  18.57300  1.000 30.82314 ? 322 ILE   A O   1 
ATOM   2462 C  CB  . ILE   A 1 322 ? 15.04295  -7.83645  18.83697  1.000 33.52396 ? 322 ILE   A CB  1 
ATOM   2463 C  CG1 . ILE   A 1 322 ? 13.95698  -7.92026  19.90924  1.000 33.25741 ? 322 ILE   A CG1 1 
ATOM   2464 C  CG2 . ILE   A 1 322 ? 15.81476  -9.14720  18.72659  1.000 33.85850 ? 322 ILE   A CG2 1 
ATOM   2465 C  CD1 . ILE   A 1 322 ? 12.87189  -8.92499  19.59365  1.000 34.60486 ? 322 ILE   A CD1 1 
ATOM   2466 N  N   . ALA   A 1 323 ? 17.00478  -6.21250  16.96022  1.000 30.92312 ? 323 ALA   A N   1 
ATOM   2467 C  CA  . ALA   A 1 323 ? 18.10939  -6.15454  16.00791  1.000 32.85350 ? 323 ALA   A CA  1 
ATOM   2468 C  C   . ALA   A 1 323 ? 19.21721  -5.22101  16.48151  1.000 33.99619 ? 323 ALA   A C   1 
ATOM   2469 O  O   . ALA   A 1 323 ? 20.39437  -5.45529  16.18374  1.000 33.38863 ? 323 ALA   A O   1 
ATOM   2470 C  CB  . ALA   A 1 323 ? 17.59710  -5.71692  14.63492  1.000 32.05482 ? 323 ALA   A CB  1 
ATOM   2471 N  N   . ASN   A 1 324 ? 18.86671  -4.15932  17.21258  1.000 29.42613 ? 324 ASN   A N   1 
ATOM   2472 C  CA  . ASN   A 1 324 ? 19.87960  -3.25764  17.74701  1.000 32.85857 ? 324 ASN   A CA  1 
ATOM   2473 C  C   . ASN   A 1 324 ? 20.65358  -3.86562  18.91020  1.000 34.51250 ? 324 ASN   A C   1 
ATOM   2474 O  O   . ASN   A 1 324 ? 21.67905  -3.30350  19.30872  1.000 32.64236 ? 324 ASN   A O   1 
ATOM   2475 C  CB  . ASN   A 1 324 ? 19.23782  -1.93469  18.17563  1.000 29.98944 ? 324 ASN   A CB  1 
ATOM   2476 C  CG  . ASN   A 1 324 ? 18.90051  -1.04346  16.99307  1.000 31.27681 ? 324 ASN   A CG  1 
ATOM   2477 O  OD1 . ASN   A 1 324 ? 19.40767  -1.24381  15.88886  1.000 32.54620 ? 324 ASN   A OD1 1 
ATOM   2478 N  ND2 . ASN   A 1 324 ? 18.04836  -0.04895  17.22010  1.000 31.40792 ? 324 ASN   A ND2 1 
ATOM   2479 N  N   . ARG   A 1 325 ? 20.19481  -4.99171  19.45946  1.000 32.42052 ? 325 ARG   A N   1 
ATOM   2480 C  CA  . ARG   A 1 325 ? 20.93030  -5.73072  20.47828  1.000 35.97787 ? 325 ARG   A CA  1 
ATOM   2481 C  C   . ARG   A 1 325 ? 21.60180  -6.97750  19.90840  1.000 36.30760 ? 325 ARG   A C   1 
ATOM   2482 O  O   . ARG   A 1 325 ? 21.74131  -7.98610  20.60834  1.000 38.58357 ? 325 ARG   A O   1 
ATOM   2483 C  CB  . ARG   A 1 325 ? 20.00642  -6.10522  21.63748  1.000 35.20306 ? 325 ARG   A CB  1 
ATOM   2484 C  CG  . ARG   A 1 325 ? 19.27035  -4.92791  22.25822  1.000 36.18058 ? 325 ARG   A CG  1 
ATOM   2485 C  CD  . ARG   A 1 325 ? 20.23328  -3.87853  22.78429  1.000 35.61911 ? 325 ARG   A CD  1 
ATOM   2486 N  NE  . ARG   A 1 325 ? 19.52795  -2.78288  23.44265  1.000 36.06094 ? 325 ARG   A NE  1 
ATOM   2487 C  CZ  . ARG   A 1 325 ? 19.22750  -2.75776  24.73781  1.000 38.05306 ? 325 ARG   A CZ  1 
ATOM   2488 N  NH1 . ARG   A 1 325 ? 19.57238  -3.77081  25.52183  1.000 37.22156 ? 325 ARG   A NH1 1 
ATOM   2489 N  NH2 . ARG   A 1 325 ? 18.58228  -1.71810  25.25024  1.000 35.49211 ? 325 ARG   A NH2 1 
ATOM   2490 N  N   . ASP   A 1 326 ? 22.01610  -6.92843  18.64419  1.000 36.81265 ? 326 ASP   A N   1 
ATOM   2491 C  CA  . ASP   A 1 326 ? 22.70333  -8.04853  18.00933  1.000 37.62319 ? 326 ASP   A CA  1 
ATOM   2492 C  C   . ASP   A 1 326 ? 24.17038  -8.01313  18.42112  1.000 39.23853 ? 326 ASP   A C   1 
ATOM   2493 O  O   . ASP   A 1 326 ? 24.91327  -7.11003  18.02243  1.000 37.45183 ? 326 ASP   A O   1 
ATOM   2494 C  CB  . ASP   A 1 326 ? 22.54944  -7.97694  16.49220  1.000 36.64599 ? 326 ASP   A CB  1 
ATOM   2495 C  CG  . ASP   A 1 326 ? 22.97529  -9.26025  15.79210  1.000 38.12292 ? 326 ASP   A CG  1 
ATOM   2496 O  OD1 . ASP   A 1 326 ? 23.80596  -10.01151 16.34732  1.000 39.55344 ? 326 ASP   A OD1 1 
ATOM   2497 O  OD2 . ASP   A 1 326 ? 22.47660  -9.51612  14.67578  1.000 37.43397 ? 326 ASP   A OD2 1 
ATOM   2498 N  N   . GLY   A 1 327 ? 24.59160  -9.00484  19.20935  1.000 38.97282 ? 327 GLY   A N   1 
ATOM   2499 C  CA  . GLY   A 1 327 ? 25.95586  -9.04488  19.70618  1.000 38.89186 ? 327 GLY   A CA  1 
ATOM   2500 C  C   . GLY   A 1 327 ? 27.01099  -9.16705  18.62711  1.000 39.96136 ? 327 GLY   A C   1 
ATOM   2501 O  O   . GLY   A 1 327 ? 28.17373  -8.82794  18.87046  1.000 40.80440 ? 327 GLY   A O   1 
ATOM   2502 N  N   . THR   A 1 328 ? 26.63947  -9.64898  17.44026  1.000 39.67211 ? 328 THR   A N   1 
ATOM   2503 C  CA  . THR   A 1 328 ? 27.58350  -9.72695  16.33382  1.000 39.64710 ? 328 THR   A CA  1 
ATOM   2504 C  C   . THR   A 1 328 ? 27.81159  -8.38084  15.65983  1.000 40.10524 ? 328 THR   A C   1 
ATOM   2505 O  O   . THR   A 1 328 ? 28.68748  -8.27945  14.79372  1.000 43.82170 ? 328 THR   A O   1 
ATOM   2506 C  CB  . THR   A 1 328 ? 27.10498  -10.74452 15.29236  1.000 40.73666 ? 328 THR   A CB  1 
ATOM   2507 O  OG1 . THR   A 1 328 ? 26.10662  -10.14824 14.45398  1.000 39.98713 ? 328 THR   A OG1 1 
ATOM   2508 C  CG2 . THR   A 1 328 ? 26.51633  -11.96992 15.97931  1.000 39.68607 ? 328 THR   A CG2 1 
ATOM   2509 N  N   . VAL   A 1 329 ? 27.04892  -7.35477  16.02829  1.000 39.49925 ? 329 VAL   A N   1 
ATOM   2510 C  CA  . VAL   A 1 329 ? 27.23806  -6.01063  15.51032  1.000 38.82454 ? 329 VAL   A CA  1 
ATOM   2511 C  C   . VAL   A 1 329 ? 27.75741  -5.06514  16.58530  1.000 38.96748 ? 329 VAL   A C   1 
ATOM   2512 O  O   . VAL   A 1 329 ? 28.67205  -4.27760  16.33429  1.000 39.63172 ? 329 VAL   A O   1 
ATOM   2513 C  CB  . VAL   A 1 329 ? 25.92966  -5.47051  14.89218  1.000 38.43701 ? 329 VAL   A CB  1 
ATOM   2514 C  CG1 . VAL   A 1 329 ? 26.18156  -4.13936  14.20005  1.000 35.26348 ? 329 VAL   A CG1 1 
ATOM   2515 C  CG2 . VAL   A 1 329 ? 25.33246  -6.48907  13.92849  1.000 38.20934 ? 329 VAL   A CG2 1 
ATOM   2516 N  N   . TYR   A 1 330 ? 27.19152  -5.13368  17.78737  1.000 38.20742 ? 330 TYR   A N   1 
ATOM   2517 C  CA  . TYR   A 1 330 ? 27.55362  -4.24928  18.88915  1.000 40.43112 ? 330 TYR   A CA  1 
ATOM   2518 C  C   . TYR   A 1 330 ? 28.06845  -5.10997  20.03284  1.000 40.15861 ? 330 TYR   A C   1 
ATOM   2519 O  O   . TYR   A 1 330 ? 27.28519  -5.78795  20.70659  1.000 40.87106 ? 330 TYR   A O   1 
ATOM   2520 C  CB  . TYR   A 1 330 ? 26.35900  -3.39456  19.31212  1.000 37.95220 ? 330 TYR   A CB  1 
ATOM   2521 C  CG  . TYR   A 1 330 ? 25.72199  -2.70082  18.13117  1.000 37.62192 ? 330 TYR   A CG  1 
ATOM   2522 C  CD1 . TYR   A 1 330 ? 26.36796  -1.65097  17.49359  1.000 37.10396 ? 330 TYR   A CD1 1 
ATOM   2523 C  CD2 . TYR   A 1 330 ? 24.49450  -3.11675  17.63122  1.000 38.34622 ? 330 TYR   A CD2 1 
ATOM   2524 C  CE1 . TYR   A 1 330 ? 25.80469  -1.02370  16.40144  1.000 36.65289 ? 330 TYR   A CE1 1 
ATOM   2525 C  CE2 . TYR   A 1 330 ? 23.92055  -2.49208  16.53897  1.000 35.72270 ? 330 TYR   A CE2 1 
ATOM   2526 C  CZ  . TYR   A 1 330 ? 24.58182  -1.44683  15.92878  1.000 35.35576 ? 330 TYR   A CZ  1 
ATOM   2527 O  OH  . TYR   A 1 330 ? 24.02210  -0.82226  14.84001  1.000 33.89362 ? 330 TYR   A OH  1 
ATOM   2528 N  N   . GLU   A 1 331 ? 29.38469  -5.08689  20.23555  1.000 42.12720 ? 331 GLU   A N   1 
ATOM   2529 C  CA  . GLU   A 1 331 ? 30.01017  -5.89779  21.27114  1.000 45.57310 ? 331 GLU   A CA  1 
ATOM   2530 C  C   . GLU   A 1 331 ? 29.42502  -5.55767  22.63418  1.000 44.36847 ? 331 GLU   A C   1 
ATOM   2531 O  O   . GLU   A 1 331 ? 29.36854  -4.38654  23.02219  1.000 43.01946 ? 331 GLU   A O   1 
ATOM   2532 C  CB  . GLU   A 1 331 ? 31.52186  -5.67284  21.26591  1.000 49.18823 ? 331 GLU   A CB  1 
ATOM   2533 C  CG  . GLU   A 1 331 ? 32.30341  -6.64553  22.12868  1.000 53.83317 ? 331 GLU   A CG  1 
ATOM   2534 C  CD  . GLU   A 1 331 ? 33.79983  -6.40810  22.06046  1.000 61.78143 ? 331 GLU   A CD  1 
ATOM   2535 O  OE1 . GLU   A 1 331 ? 34.22615  -5.48724  21.33077  1.000 67.02609 ? 331 GLU   A OE1 1 
ATOM   2536 O  OE2 . GLU   A 1 331 ? 34.54967  -7.14318  22.73692  1.000 71.30460 ? 331 GLU   A OE2 1 
ATOM   2537 N  N   . ASP   A 1 332 ? 28.98538  -6.59318  23.35701  1.000 42.93460 ? 332 ASP   A N   1 
ATOM   2538 C  CA  . ASP   A 1 332 ? 28.27797  -6.43710  24.62189  1.000 42.36132 ? 332 ASP   A CA  1 
ATOM   2539 C  C   . ASP   A 1 332 ? 27.06573  -5.54501  24.38030  1.000 41.03786 ? 332 ASP   A C   1 
ATOM   2540 O  O   . ASP   A 1 332 ? 27.02315  -4.40151  24.85477  1.000 41.12382 ? 332 ASP   A O   1 
ATOM   2541 C  CB  . ASP   A 1 332 ? 29.21039  -5.86287  25.68990  1.000 44.63477 ? 332 ASP   A CB  1 
ATOM   2542 C  CG  . ASP   A 1 332 ? 30.53742  -6.60039  25.75281  1.000 48.08322 ? 332 ASP   A CG  1 
ATOM   2543 O  OD1 . ASP   A 1 332 ? 30.54712  -7.78466  26.15539  1.000 45.43683 ? 332 ASP   A OD1 1 
ATOM   2544 O  OD2 . ASP   A 1 332 ? 31.56705  -6.00732  25.36829  1.000 48.23933 ? 332 ASP   A OD2 1 
ATOM   2545 N  N   . PRO   A 1 333 ? 26.06149  -6.03858  23.64735  1.000 40.96931 ? 333 PRO   A N   1 
ATOM   2546 C  CA  . PRO   A 1 333 ? 25.02506  -5.13866  23.11397  1.000 39.05723 ? 333 PRO   A CA  1 
ATOM   2547 C  C   . PRO   A 1 333 ? 24.09031  -4.56780  24.16390  1.000 39.80555 ? 333 PRO   A C   1 
ATOM   2548 O  O   . PRO   A 1 333 ? 23.51264  -3.49948  23.92864  1.000 36.63728 ? 333 PRO   A O   1 
ATOM   2549 C  CB  . PRO   A 1 333 ? 24.26427  -6.03223  22.12536  1.000 38.34695 ? 333 PRO   A CB  1 
ATOM   2550 C  CG  . PRO   A 1 333 ? 24.43569  -7.41630  22.68106  1.000 39.63152 ? 333 PRO   A CG  1 
ATOM   2551 C  CD  . PRO   A 1 333 ? 25.82370  -7.44493  23.27245  1.000 39.85571 ? 333 PRO   A CD  1 
ATOM   2552 N  N   . ASP   A 1 334 ? 23.90882  -5.23254  25.30165  1.000 38.02028 ? 334 ASP   A N   1 
ATOM   2553 C  CA  . ASP   A 1 334 ? 22.99304  -4.74616  26.32337  1.000 39.09412 ? 334 ASP   A CA  1 
ATOM   2554 C  C   . ASP   A 1 334 ? 23.64757  -3.75286  27.27626  1.000 39.19176 ? 334 ASP   A C   1 
ATOM   2555 O  O   . ASP   A 1 334 ? 23.02187  -3.35117  28.26276  1.000 37.05268 ? 334 ASP   A O   1 
ATOM   2556 C  CB  . ASP   A 1 334 ? 22.39930  -5.92376  27.09709  1.000 40.20057 ? 334 ASP   A CB  1 
ATOM   2557 C  CG  . ASP   A 1 334 ? 21.50874  -6.79155  26.22956  1.000 40.09497 ? 334 ASP   A CG  1 
ATOM   2558 O  OD1 . ASP   A 1 334 ? 20.81223  -6.23402  25.35686  1.000 38.86029 ? 334 ASP   A OD1 1 
ATOM   2559 O  OD2 . ASP   A 1 334 ? 21.50932  -8.02766  26.40828  1.000 41.51963 ? 334 ASP   A OD2 1 
ATOM   2560 N  N   . ALA   A 1 335 ? 24.87959  -3.33972  26.99567  1.000 38.71301 ? 335 ALA   A N   1 
ATOM   2561 C  CA  . ALA   A 1 335 ? 25.57849  -2.34306  27.79360  1.000 39.00208 ? 335 ALA   A CA  1 
ATOM   2562 C  C   . ALA   A 1 335 ? 25.48650  -0.99402  27.09195  1.000 38.67925 ? 335 ALA   A C   1 
ATOM   2563 O  O   . ALA   A 1 335 ? 25.85198  -0.87393  25.91631  1.000 37.44397 ? 335 ALA   A O   1 
ATOM   2564 C  CB  . ALA   A 1 335 ? 27.03920  -2.73807  28.00828  1.000 39.47400 ? 335 ALA   A CB  1 
ATOM   2565 N  N   . LEU   A 1 336 ? 24.98570  0.01088   27.80638  1.000 38.70378 ? 336 LEU   A N   1 
ATOM   2566 C  CA  . LEU   A 1 336 ? 24.99606  1.37494   27.29499  1.000 37.38621 ? 336 LEU   A CA  1 
ATOM   2567 C  C   . LEU   A 1 336 ? 26.43002  1.88672   27.25863  1.000 38.78650 ? 336 LEU   A C   1 
ATOM   2568 O  O   . LEU   A 1 336 ? 27.11062  1.91556   28.28916  1.000 40.19126 ? 336 LEU   A O   1 
ATOM   2569 C  CB  . LEU   A 1 336 ? 24.12667  2.27593   28.16811  1.000 38.48468 ? 336 LEU   A CB  1 
ATOM   2570 C  CG  . LEU   A 1 336 ? 24.09925  3.75883   27.78817  1.000 37.89877 ? 336 LEU   A CG  1 
ATOM   2571 C  CD1 . LEU   A 1 336 ? 23.19092  3.99717   26.59156  1.000 35.30974 ? 336 LEU   A CD1 1 
ATOM   2572 C  CD2 . LEU   A 1 336 ? 23.67817  4.61660   28.97084  1.000 38.03276 ? 336 LEU   A CD2 1 
ATOM   2573 N  N   . ASP   A 1 337 ? 26.89278  2.28372   26.07502  1.000 38.87579 ? 337 ASP   A N   1 
ATOM   2574 C  CA  . ASP   A 1 337 ? 28.25804  2.78059   25.89564  1.000 39.45245 ? 337 ASP   A CA  1 
ATOM   2575 C  C   . ASP   A 1 337 ? 28.20004  3.97039   24.94115  1.000 38.65821 ? 337 ASP   A C   1 
ATOM   2576 O  O   . ASP   A 1 337 ? 28.17958  3.79137   23.71955  1.000 37.49533 ? 337 ASP   A O   1 
ATOM   2577 C  CB  . ASP   A 1 337 ? 29.17902  1.68400   25.36817  1.000 39.94635 ? 337 ASP   A CB  1 
ATOM   2578 C  CG  . ASP   A 1 337 ? 30.61773  2.15110   25.20226  1.000 41.09893 ? 337 ASP   A CG  1 
ATOM   2579 O  OD1 . ASP   A 1 337 ? 30.93470  3.29319   25.59361  1.000 40.81355 ? 337 ASP   A OD1 1 
ATOM   2580 O  OD2 . ASP   A 1 337 ? 31.43710  1.36854   24.67481  1.000 42.67403 ? 337 ASP   A OD2 1 
ATOM   2581 N  N   . ILE   A 1 338 ? 28.19319  5.18421   25.50103  1.000 40.08953 ? 338 ILE   A N   1 
ATOM   2582 C  CA  . ILE   A 1 338 ? 28.15742  6.39126   24.68037  1.000 38.90614 ? 338 ILE   A CA  1 
ATOM   2583 C  C   . ILE   A 1 338 ? 29.43140  6.59176   23.87501  1.000 40.05078 ? 338 ILE   A C   1 
ATOM   2584 O  O   . ILE   A 1 338 ? 29.45577  7.44026   22.97618  1.000 39.43132 ? 338 ILE   A O   1 
ATOM   2585 C  CB  . ILE   A 1 338 ? 27.89368  7.64091   25.54712  1.000 39.62796 ? 338 ILE   A CB  1 
ATOM   2586 C  CG1 . ILE   A 1 338 ? 29.09195  7.92777   26.45117  1.000 40.93037 ? 338 ILE   A CG1 1 
ATOM   2587 C  CG2 . ILE   A 1 338 ? 26.62810  7.45500   26.37276  1.000 38.98002 ? 338 ILE   A CG2 1 
ATOM   2588 C  CD1 . ILE   A 1 338 ? 28.97497  9.21298   27.23754  1.000 41.49434 ? 338 ILE   A CD1 1 
ATOM   2589 N  N   . HIS   A 1 339 ? 30.48845  5.83201   24.16633  1.000 41.32670 ? 339 HIS   A N   1 
ATOM   2590 C  CA  . HIS   A 1 339 ? 31.73612  5.91750   23.41866  1.000 42.15008 ? 339 HIS   A CA  1 
ATOM   2591 C  C   . HIS   A 1 339 ? 31.81016  4.92585   22.26466  1.000 43.22471 ? 339 HIS   A C   1 
ATOM   2592 O  O   . HIS   A 1 339 ? 32.68919  5.06585   21.40709  1.000 44.64564 ? 339 HIS   A O   1 
ATOM   2593 C  CB  . HIS   A 1 339 ? 32.93642  5.68764   24.34687  1.000 42.89630 ? 339 HIS   A CB  1 
ATOM   2594 C  CG  . HIS   A 1 339 ? 32.96501  6.59076   25.54097  1.000 42.99405 ? 339 HIS   A CG  1 
ATOM   2595 N  ND1 . HIS   A 1 339 ? 33.72118  7.74189   25.58645  1.000 44.19707 ? 339 HIS   A ND1 1 
ATOM   2596 C  CD2 . HIS   A 1 339 ? 32.33721  6.50642   26.73748  1.000 42.30474 ? 339 HIS   A CD2 1 
ATOM   2597 C  CE1 . HIS   A 1 339 ? 33.55424  8.33037   26.75740  1.000 46.23025 ? 339 HIS   A CE1 1 
ATOM   2598 N  NE2 . HIS   A 1 339 ? 32.71905  7.60079   27.47467  1.000 44.04292 ? 339 HIS   A NE2 1 
ATOM   2599 N  N   . ARG   A 1 340 ? 30.92629  3.93066   22.22329  1.000 42.24817 ? 340 ARG   A N   1 
ATOM   2600 C  CA  . ARG   A 1 340 ? 30.99303  2.91838   21.18072  1.000 42.05795 ? 340 ARG   A CA  1 
ATOM   2601 C  C   . ARG   A 1 340 ? 30.53577  3.48876   19.84303  1.000 41.82078 ? 340 ARG   A C   1 
ATOM   2602 O  O   . ARG   A 1 340 ? 29.93462  4.56273   19.76293  1.000 39.79530 ? 340 ARG   A O   1 
ATOM   2603 C  CB  . ARG   A 1 340 ? 30.11947  1.71226   21.53045  1.000 40.73983 ? 340 ARG   A CB  1 
ATOM   2604 C  CG  . ARG   A 1 340 ? 28.64587  1.92704   21.21418  1.000 39.68173 ? 340 ARG   A CG  1 
ATOM   2605 C  CD  . ARG   A 1 340 ? 27.88241  0.62453   21.01213  1.000 38.12169 ? 340 ARG   A CD  1 
ATOM   2606 N  NE  . ARG   A 1 340 ? 27.44391  0.02153   22.26757  1.000 37.60735 ? 340 ARG   A NE  1 
ATOM   2607 C  CZ  . ARG   A 1 340 ? 27.86814  -1.15355  22.72404  1.000 39.27474 ? 340 ARG   A CZ  1 
ATOM   2608 N  NH1 . ARG   A 1 340 ? 28.74329  -1.86617  22.02673  1.000 39.64151 ? 340 ARG   A NH1 1 
ATOM   2609 N  NH2 . ARG   A 1 340 ? 27.40771  -1.62220  23.87536  1.000 39.28267 ? 340 ARG   A NH2 1 
ATOM   2610 N  N   . SER   A 1 341 ? 30.83656  2.74908   18.78063  1.000 45.16729 ? 341 SER   A N   1 
ATOM   2611 C  CA  . SER   A 1 341 ? 30.29110  3.03921   17.46114  1.000 41.84737 ? 341 SER   A CA  1 
ATOM   2612 C  C   . SER   A 1 341 ? 28.88694  2.45247   17.38431  1.000 40.67146 ? 341 SER   A C   1 
ATOM   2613 O  O   . SER   A 1 341 ? 28.71920  1.23356   17.27456  1.000 40.77525 ? 341 SER   A O   1 
ATOM   2614 C  CB  . SER   A 1 341 ? 31.19102  2.46547   16.37107  1.000 44.39219 ? 341 SER   A CB  1 
ATOM   2615 O  OG  . SER   A 1 341 ? 30.55813  2.52985   15.10534  1.000 50.88995 ? 341 SER   A OG  1 
ATOM   2616 N  N   . ALA   A 1 342 ? 27.87398  3.31371   17.46523  1.000 39.77540 ? 342 ALA   A N   1 
ATOM   2617 C  CA  . ALA   A 1 342 ? 26.48823  2.90185   17.29776  1.000 38.03480 ? 342 ALA   A CA  1 
ATOM   2618 C  C   . ALA   A 1 342 ? 26.05598  2.90037   15.83511  1.000 37.08853 ? 342 ALA   A C   1 
ATOM   2619 O  O   . ALA   A 1 342 ? 24.85174  2.88122   15.55346  1.000 35.70555 ? 342 ALA   A O   1 
ATOM   2620 C  CB  . ALA   A 1 342 ? 25.56641  3.80296   18.12221  1.000 34.56406 ? 342 ALA   A CB  1 
ATOM   2621 N  N   . ARG   A 1 343 ? 27.01212  2.90899   14.90654  1.000 38.17531 ? 343 ARG   A N   1 
ATOM   2622 C  CA  . ARG   A 1 343 ? 26.69753  3.01653   13.48864  1.000 37.23042 ? 343 ARG   A CA  1 
ATOM   2623 C  C   . ARG   A 1 343 ? 25.81381  1.86351   13.02704  1.000 37.17831 ? 343 ARG   A C   1 
ATOM   2624 O  O   . ARG   A 1 343 ? 25.82351  0.76861   13.59867  1.000 34.80398 ? 343 ARG   A O   1 
ATOM   2625 C  CB  . ARG   A 1 343 ? 27.97944  3.04344   12.65290  1.000 38.42801 ? 343 ARG   A CB  1 
ATOM   2626 C  CG  . ARG   A 1 343 ? 28.89247  4.22200   12.93196  1.000 41.84752 ? 343 ARG   A CG  1 
ATOM   2627 C  CD  . ARG   A 1 343 ? 29.98668  4.33662   11.87549  1.000 44.14293 ? 343 ARG   A CD  1 
ATOM   2628 N  NE  . ARG   A 1 343 ? 29.44412  4.62447   10.54998  1.000 39.98068 ? 343 ARG   A NE  1 
ATOM   2629 C  CZ  . ARG   A 1 343 ? 29.03019  5.82671   10.16291  1.000 40.01577 ? 343 ARG   A CZ  1 
ATOM   2630 N  NH1 . ARG   A 1 343 ? 29.09026  6.84951   11.00556  1.000 40.33669 ? 343 ARG   A NH1 1 
ATOM   2631 N  NH2 . ARG   A 1 343 ? 28.55030  6.00845   8.93964   1.000 37.84644 ? 343 ARG   A NH2 1 
ATOM   2632 N  N   . HIS   A 1 344 ? 25.03214  2.13804   11.98212  1.000 34.83615 ? 344 HIS   A N   1 
ATOM   2633 C  CA  . HIS   A 1 344 ? 24.19402  1.16784   11.28685  1.000 36.16754 ? 344 HIS   A CA  1 
ATOM   2634 C  C   . HIS   A 1 344 ? 23.05431  0.64178   12.14726  1.000 32.47357 ? 344 HIS   A C   1 
ATOM   2635 O  O   . HIS   A 1 344 ? 22.47465  -0.39947  11.83028  1.000 34.14001 ? 344 HIS   A O   1 
ATOM   2636 C  CB  . HIS   A 1 344 ? 25.03007  0.00277   10.74328  1.000 35.79190 ? 344 HIS   A CB  1 
ATOM   2637 C  CG  . HIS   A 1 344 ? 26.21458  0.44165   9.94112   1.000 39.85940 ? 344 HIS   A CG  1 
ATOM   2638 N  ND1 . HIS   A 1 344 ? 26.12466  0.78985   8.61028   1.000 42.00758 ? 344 HIS   A ND1 1 
ATOM   2639 C  CD2 . HIS   A 1 344 ? 27.51415  0.60414   10.28551  1.000 39.07764 ? 344 HIS   A CD2 1 
ATOM   2640 C  CE1 . HIS   A 1 344 ? 27.31881  1.14143   8.16777   1.000 40.82823 ? 344 HIS   A CE1 1 
ATOM   2641 N  NE2 . HIS   A 1 344 ? 28.17963  1.03869   9.16466   1.000 42.48687 ? 344 HIS   A NE2 1 
ATOM   2642 N  N   . HIS   A 1 345 ? 22.70209  1.34256   13.22231  1.000 32.28529 ? 345 HIS   A N   1 
ATOM   2643 C  CA  . HIS   A 1 345 ? 21.55982  0.92208   14.01674  1.000 31.89085 ? 345 HIS   A CA  1 
ATOM   2644 C  C   . HIS   A 1 345 ? 20.26626  1.15305   13.24185  1.000 30.75414 ? 345 HIS   A C   1 
ATOM   2645 O  O   . HIS   A 1 345 ? 20.21037  1.93455   12.28745  1.000 30.56404 ? 345 HIS   A O   1 
ATOM   2646 C  CB  . HIS   A 1 345 ? 21.52442  1.65643   15.35910  1.000 29.94099 ? 345 HIS   A CB  1 
ATOM   2647 C  CG  . HIS   A 1 345 ? 21.21851  3.11771   15.24817  1.000 31.08770 ? 345 HIS   A CG  1 
ATOM   2648 N  ND1 . HIS   A 1 345 ? 19.93509  3.60252   15.11577  1.000 30.23348 ? 345 HIS   A ND1 1 
ATOM   2649 C  CD2 . HIS   A 1 345 ? 22.03043  4.20140   15.26271  1.000 30.64596 ? 345 HIS   A CD2 1 
ATOM   2650 C  CE1 . HIS   A 1 345 ? 19.96999  4.92176   15.04807  1.000 29.20160 ? 345 HIS   A CE1 1 
ATOM   2651 N  NE2 . HIS   A 1 345 ? 21.22973  5.30997   15.13294  1.000 28.77681 ? 345 HIS   A NE2 1 
ATOM   2652 N  N   . LEU   A 1 346 ? 19.21402  0.45177   13.66651  1.000 29.75355 ? 346 LEU   A N   1 
ATOM   2653 C  CA  . LEU   A 1 346 ? 17.94524  0.43028   12.95037  1.000 29.18506 ? 346 LEU   A CA  1 
ATOM   2654 C  C   . LEU   A 1 346 ? 16.83074  1.14991   13.70159  1.000 28.63599 ? 346 LEU   A C   1 
ATOM   2655 O  O   . LEU   A 1 346 ? 15.65220  0.92590   13.41075  1.000 27.19348 ? 346 LEU   A O   1 
ATOM   2656 C  CB  . LEU   A 1 346 ? 17.53700  -1.01208  12.65647  1.000 29.24399 ? 346 LEU   A CB  1 
ATOM   2657 C  CG  . LEU   A 1 346 ? 18.43804  -1.75489  11.67353  1.000 30.39328 ? 346 LEU   A CG  1 
ATOM   2658 C  CD1 . LEU   A 1 346 ? 18.16751  -3.24280  11.74581  1.000 31.09190 ? 346 LEU   A CD1 1 
ATOM   2659 C  CD2 . LEU   A 1 346 ? 18.20991  -1.22853  10.26392  1.000 28.70531 ? 346 LEU   A CD2 1 
ATOM   2660 N  N   . ALA   A 1 347 ? 17.17763  2.01785   14.65598  1.000 27.64668 ? 347 ALA   A N   1 
ATOM   2661 C  CA  . ALA   A 1 347 ? 16.15084  2.76139   15.38006  1.000 29.90747 ? 347 ALA   A CA  1 
ATOM   2662 C  C   . ALA   A 1 347 ? 15.30127  3.60337   14.43875  1.000 27.90179 ? 347 ALA   A C   1 
ATOM   2663 O  O   . ALA   A 1 347 ? 14.12129  3.84428   14.71714  1.000 28.52838 ? 347 ALA   A O   1 
ATOM   2664 C  CB  . ALA   A 1 347 ? 16.78998  3.64414   16.45194  1.000 27.68343 ? 347 ALA   A CB  1 
ATOM   2665 N  N   . PHE   A 1 348 ? 15.87639  4.05038   13.32306  1.000 25.78052 ? 348 PHE   A N   1 
ATOM   2666 C  CA  . PHE   A 1 348 ? 15.15371  4.80125   12.30646  1.000 28.84033 ? 348 PHE   A CA  1 
ATOM   2667 C  C   . PHE   A 1 348 ? 14.75028  3.94738   11.11205  1.000 28.29450 ? 348 PHE   A C   1 
ATOM   2668 O  O   . PHE   A 1 348 ? 14.15459  4.47233   10.16638  1.000 26.92676 ? 348 PHE   A O   1 
ATOM   2669 C  CB  . PHE   A 1 348 ? 15.99750  5.98045   11.81228  1.000 26.70856 ? 348 PHE   A CB  1 
ATOM   2670 C  CG  . PHE   A 1 348 ? 16.20200  7.05906   12.83535  1.000 26.32359 ? 348 PHE   A CG  1 
ATOM   2671 C  CD1 . PHE   A 1 348 ? 15.12167  7.71913   13.39170  1.000 27.34418 ? 348 PHE   A CD1 1 
ATOM   2672 C  CD2 . PHE   A 1 348 ? 17.47716  7.43320   13.21866  1.000 28.66638 ? 348 PHE   A CD2 1 
ATOM   2673 C  CE1 . PHE   A 1 348 ? 15.30808  8.72051   14.32317  1.000 25.08047 ? 348 PHE   A CE1 1 
ATOM   2674 C  CE2 . PHE   A 1 348 ? 17.66936  8.43724   14.14705  1.000 27.74192 ? 348 PHE   A CE2 1 
ATOM   2675 C  CZ  . PHE   A 1 348 ? 16.58343  9.07803   14.70085  1.000 27.13713 ? 348 PHE   A CZ  1 
ATOM   2676 N  N   . GLY   A 1 349 ? 15.06873  2.65990   11.12088  1.000 29.38872 ? 349 GLY   A N   1 
ATOM   2677 C  CA  . GLY   A 1 349 ? 14.78735  1.80888   9.98175   1.000 27.34207 ? 349 GLY   A CA  1 
ATOM   2678 C  C   . GLY   A 1 349 ? 15.91888  1.79369   8.97016   1.000 28.80656 ? 349 GLY   A C   1 
ATOM   2679 O  O   . GLY   A 1 349 ? 17.06394  2.15871   9.25063   1.000 27.73844 ? 349 GLY   A O   1 
ATOM   2680 N  N   . PHE   A 1 350 ? 15.57680  1.35566   7.76140   1.000 29.05742 ? 350 PHE   A N   1 
ATOM   2681 C  CA  . PHE   A 1 350 ? 16.54897  1.22182   6.68554   1.000 29.12214 ? 350 PHE   A CA  1 
ATOM   2682 C  C   . PHE   A 1 350 ? 15.79854  1.13249   5.36700   1.000 28.22112 ? 350 PHE   A C   1 
ATOM   2683 O  O   . PHE   A 1 350 ? 14.72158  0.53688   5.30391   1.000 28.67323 ? 350 PHE   A O   1 
ATOM   2684 C  CB  . PHE   A 1 350 ? 17.43659  -0.01935  6.87732   1.000 29.30538 ? 350 PHE   A CB  1 
ATOM   2685 C  CG  . PHE   A 1 350 ? 18.25943  -0.37506  5.66539   1.000 30.20525 ? 350 PHE   A CG  1 
ATOM   2686 C  CD1 . PHE   A 1 350 ? 19.50516  0.19687   5.46317   1.000 29.78420 ? 350 PHE   A CD1 1 
ATOM   2687 C  CD2 . PHE   A 1 350 ? 17.78406  -1.28062  4.72764   1.000 29.27439 ? 350 PHE   A CD2 1 
ATOM   2688 C  CE1 . PHE   A 1 350 ? 20.25788  -0.12483  4.34822   1.000 31.06952 ? 350 PHE   A CE1 1 
ATOM   2689 C  CE2 . PHE   A 1 350 ? 18.53200  -1.60301  3.60955   1.000 30.13532 ? 350 PHE   A CE2 1 
ATOM   2690 C  CZ  . PHE   A 1 350 ? 19.77070  -1.02730  3.42213   1.000 30.45702 ? 350 PHE   A CZ  1 
ATOM   2691 N  N   . GLY   A 1 351 ? 16.37575  1.71800   4.32078   1.000 29.26722 ? 351 GLY   A N   1 
ATOM   2692 C  CA  . GLY   A 1 351 ? 15.79296  1.62546   2.99719   1.000 27.14631 ? 351 GLY   A CA  1 
ATOM   2693 C  C   . GLY   A 1 351 ? 14.91809  2.80141   2.61675   1.000 31.11463 ? 351 GLY   A C   1 
ATOM   2694 O  O   . GLY   A 1 351 ? 15.14551  3.93023   3.06597   1.000 25.98087 ? 351 GLY   A O   1 
ATOM   2695 N  N   . VAL   A 1 352 ? 13.90164  2.54174   1.78972   1.000 29.23738 ? 352 VAL   A N   1 
ATOM   2696 C  CA  . VAL   A 1 352 ? 13.06881  3.61752   1.26923   1.000 29.86953 ? 352 VAL   A CA  1 
ATOM   2697 C  C   . VAL   A 1 352 ? 12.21025  4.25680   2.35210   1.000 29.53729 ? 352 VAL   A C   1 
ATOM   2698 O  O   . VAL   A 1 352 ? 11.78718  5.40676   2.19722   1.000 29.69500 ? 352 VAL   A O   1 
ATOM   2699 C  CB  . VAL   A 1 352 ? 12.18267  3.10809   0.11614   1.000 30.48202 ? 352 VAL   A CB  1 
ATOM   2700 C  CG1 . VAL   A 1 352 ? 13.03333  2.46752   -0.96401  1.000 32.00146 ? 352 VAL   A CG1 1 
ATOM   2701 C  CG2 . VAL   A 1 352 ? 11.14711  2.12909   0.62990   1.000 30.90393 ? 352 VAL   A CG2 1 
ATOM   2702 N  N   . HIS   A 1 353 ? 11.94642  3.55379   3.45161   1.000 29.01181 ? 353 HIS   A N   1 
ATOM   2703 C  CA  . HIS   A 1 353 ? 11.07634  4.06368   4.50206   1.000 28.35941 ? 353 HIS   A CA  1 
ATOM   2704 C  C   . HIS   A 1 353 ? 11.83942  4.59862   5.70885   1.000 28.38250 ? 353 HIS   A C   1 
ATOM   2705 O  O   . HIS   A 1 353 ? 11.21225  4.93148   6.71866   1.000 30.26861 ? 353 HIS   A O   1 
ATOM   2706 C  CB  . HIS   A 1 353 ? 10.09636  2.97679   4.95343   1.000 29.24804 ? 353 HIS   A CB  1 
ATOM   2707 C  CG  . HIS   A 1 353 ? 9.02336   2.67360   3.95460   1.000 31.13036 ? 353 HIS   A CG  1 
ATOM   2708 N  ND1 . HIS   A 1 353 ? 7.96888   3.52774   3.71424   1.000 27.97201 ? 353 HIS   A ND1 1 
ATOM   2709 C  CD2 . HIS   A 1 353 ? 8.83671   1.60655   3.14104   1.000 30.58166 ? 353 HIS   A CD2 1 
ATOM   2710 C  CE1 . HIS   A 1 353 ? 7.18040   3.00101   2.79436   1.000 30.19482 ? 353 HIS   A CE1 1 
ATOM   2711 N  NE2 . HIS   A 1 353 ? 7.68519   1.83678   2.42849   1.000 28.71114 ? 353 HIS   A NE2 1 
ATOM   2712 N  N   . GLN   A 1 354 ? 13.16651  4.69057   5.63257   1.000 26.94880 ? 354 GLN   A N   1 
ATOM   2713 C  CA  . GLN   A 1 354 ? 13.93817  5.15928   6.77579   1.000 27.63816 ? 354 GLN   A CA  1 
ATOM   2714 C  C   . GLN   A 1 354 ? 13.45512  6.54142   7.20324   1.000 28.91062 ? 354 GLN   A C   1 
ATOM   2715 O  O   . GLN   A 1 354 ? 13.16026  7.40210   6.36860   1.000 27.33142 ? 354 GLN   A O   1 
ATOM   2716 C  CB  . GLN   A 1 354 ? 15.43423  5.19125   6.45019   1.000 28.42593 ? 354 GLN   A CB  1 
ATOM   2717 C  CG  . GLN   A 1 354 ? 16.29150  5.63633   7.63165   1.000 27.41034 ? 354 GLN   A CG  1 
ATOM   2718 C  CD  . GLN   A 1 354 ? 17.75728  5.25969   7.49894   1.000 30.47079 ? 354 GLN   A CD  1 
ATOM   2719 O  OE1 . GLN   A 1 354 ? 18.12127  4.36097   6.73880   1.000 26.72070 ? 354 GLN   A OE1 1 
ATOM   2720 N  NE2 . GLN   A 1 354 ? 18.60796  5.94768   8.25000   1.000 29.82270 ? 354 GLN   A NE2 1 
ATOM   2721 N  N   . CYS   A 1 355 ? 13.37143  6.73743   8.51685   1.000 28.27425 ? 355 CYS   A N   1 
ATOM   2722 C  CA  . CYS   A 1 355 ? 12.68859  7.86460   9.14040   1.000 30.25039 ? 355 CYS   A CA  1 
ATOM   2723 C  C   . CYS   A 1 355 ? 13.01526  9.19338   8.46999   1.000 25.63208 ? 355 CYS   A C   1 
ATOM   2724 O  O   . CYS   A 1 355 ? 14.16707  9.64209   8.46671   1.000 25.67878 ? 355 CYS   A O   1 
ATOM   2725 C  CB  . CYS   A 1 355 ? 13.06471  7.92172   10.61849  1.000 28.32592 ? 355 CYS   A CB  1 
ATOM   2726 S  SG  . CYS   A 1 355 ? 12.29701  9.27540   11.48041  1.000 29.02194 ? 355 CYS   A SG  1 
ATOM   2727 N  N   . LEU   A 1 356 ? 11.99062  9.82422   7.89655   1.000 26.77389 ? 356 LEU   A N   1 
ATOM   2728 C  CA  . LEU   A 1 356 ? 12.17415  11.14027  7.29260   1.000 27.74236 ? 356 LEU   A CA  1 
ATOM   2729 C  C   . LEU   A 1 356 ? 12.62244  12.17737  8.31628   1.000 28.70920 ? 356 LEU   A C   1 
ATOM   2730 O  O   . LEU   A 1 356 ? 13.38668  13.09021  7.98121   1.000 30.54432 ? 356 LEU   A O   1 
ATOM   2731 C  CB  . LEU   A 1 356 ? 10.87466  11.58856  6.62297   1.000 28.24130 ? 356 LEU   A CB  1 
ATOM   2732 C  CG  . LEU   A 1 356 ? 10.83563  13.01005  6.05457   1.000 30.83800 ? 356 LEU   A CG  1 
ATOM   2733 C  CD1 . LEU   A 1 356 ? 11.72537  13.12858  4.82441   1.000 30.61872 ? 356 LEU   A CD1 1 
ATOM   2734 C  CD2 . LEU   A 1 356 ? 9.40089   13.41872  5.74123   1.000 29.03611 ? 356 LEU   A CD2 1 
ATOM   2735 N  N   . GLY   A 1 357 ? 12.16945  12.05559  9.56144   1.000 27.45428 ? 357 GLY   A N   1 
ATOM   2736 C  CA  . GLY   A 1 357 ? 12.49765  13.03862  10.57427  1.000 29.38135 ? 357 GLY   A CA  1 
ATOM   2737 C  C   . GLY   A 1 357 ? 13.72971  12.71135  11.39259  1.000 28.45735 ? 357 GLY   A C   1 
ATOM   2738 O  O   . GLY   A 1 357 ? 13.89455  13.23262  12.49915  1.000 29.63824 ? 357 GLY   A O   1 
ATOM   2739 N  N   . GLN   A 1 358 ? 14.61145  11.86097  10.86113  1.000 28.12212 ? 358 GLN   A N   1 
ATOM   2740 C  CA  . GLN   A 1 358 ? 15.76279  11.41836  11.64357  1.000 29.93804 ? 358 GLN   A CA  1 
ATOM   2741 C  C   . GLN   A 1 358 ? 16.74135  12.56042  11.89756  1.000 29.46271 ? 358 GLN   A C   1 
ATOM   2742 O  O   . GLN   A 1 358 ? 17.30828  12.66049  12.99048  1.000 30.68841 ? 358 GLN   A O   1 
ATOM   2743 C  CB  . GLN   A 1 358 ? 16.46293  10.24825  10.94843  1.000 28.07075 ? 358 GLN   A CB  1 
ATOM   2744 C  CG  . GLN   A 1 358 ? 16.97655  10.54249  9.54487   1.000 26.90434 ? 358 GLN   A CG  1 
ATOM   2745 C  CD  . GLN   A 1 358 ? 17.66288  9.34015   8.91457   1.000 30.70871 ? 358 GLN   A CD  1 
ATOM   2746 O  OE1 . GLN   A 1 358 ? 18.18490  8.47171   9.61467   1.000 26.44603 ? 358 GLN   A OE1 1 
ATOM   2747 N  NE2 . GLN   A 1 358 ? 17.66233  9.28437   7.58637   1.000 29.31256 ? 358 GLN   A NE2 1 
ATOM   2748 N  N   . ASN   A 1 359 ? 16.95698  13.43050  10.90612  1.000 29.82788 ? 359 ASN   A N   1 
ATOM   2749 C  CA  . ASN   A 1 359 ? 17.84165  14.57251  11.11922  1.000 30.78931 ? 359 ASN   A CA  1 
ATOM   2750 C  C   . ASN   A 1 359 ? 17.27197  15.52004  12.16711  1.000 30.86955 ? 359 ASN   A C   1 
ATOM   2751 O  O   . ASN   A 1 359 ? 18.01935  16.10176  12.96320  1.000 27.45295 ? 359 ASN   A O   1 
ATOM   2752 C  CB  . ASN   A 1 359 ? 18.07860  15.31392  9.80338   1.000 31.71080 ? 359 ASN   A CB  1 
ATOM   2753 C  CG  . ASN   A 1 359 ? 18.77122  14.45438  8.76520   1.000 39.44457 ? 359 ASN   A CG  1 
ATOM   2754 O  OD1 . ASN   A 1 359 ? 19.40241  13.44931  9.09503   1.000 34.20097 ? 359 ASN   A OD1 1 
ATOM   2755 N  ND2 . ASN   A 1 359 ? 18.66436  14.85235  7.50036   1.000 37.30825 ? 359 ASN   A ND2 1 
ATOM   2756 N  N   . LEU   A 1 360 ? 15.94760  15.68706  12.18216  1.000 31.14094 ? 360 LEU   A N   1 
ATOM   2757 C  CA  . LEU   A 1 360 ? 15.32427  16.58107  13.15199  1.000 28.32014 ? 360 LEU   A CA  1 
ATOM   2758 C  C   . LEU   A 1 360 ? 15.38903  15.99889  14.55852  1.000 29.28494 ? 360 LEU   A C   1 
ATOM   2759 O  O   . LEU   A 1 360 ? 15.69183  16.71561  15.52022  1.000 27.87574 ? 360 LEU   A O   1 
ATOM   2760 C  CB  . LEU   A 1 360 ? 13.87686  16.85802  12.74851  1.000 26.71041 ? 360 LEU   A CB  1 
ATOM   2761 C  CG  . LEU   A 1 360 ? 13.04015  17.74031  13.67725  1.000 28.74549 ? 360 LEU   A CG  1 
ATOM   2762 C  CD1 . LEU   A 1 360 ? 13.57171  19.17045  13.70810  1.000 25.35001 ? 360 LEU   A CD1 1 
ATOM   2763 C  CD2 . LEU   A 1 360 ? 11.57532  17.71132  13.26644  1.000 26.17132 ? 360 LEU   A CD2 1 
ATOM   2764 N  N   . ALA   A 1 361 ? 15.10627  14.70055  14.69827  1.000 27.79077 ? 361 ALA   A N   1 
ATOM   2765 C  CA  . ALA   A 1 361 ? 15.18907  14.06173  16.00849  1.000 27.56232 ? 361 ALA   A CA  1 
ATOM   2766 C  C   . ALA   A 1 361 ? 16.60804  14.11772  16.55771  1.000 27.48218 ? 361 ALA   A C   1 
ATOM   2767 O  O   . ALA   A 1 361 ? 16.80992  14.37524  17.75023  1.000 28.77890 ? 361 ALA   A O   1 
ATOM   2768 C  CB  . ALA   A 1 361 ? 14.70328  12.61505  15.92163  1.000 28.73560 ? 361 ALA   A CB  1 
ATOM   2769 N  N   . ARG   A 1 362 ? 17.60536  13.88541  15.69840  1.000 29.53684 ? 362 ARG   A N   1 
ATOM   2770 C  CA  . ARG   A 1 362 ? 18.99634  13.98769  16.12834  1.000 29.58285 ? 362 ARG   A CA  1 
ATOM   2771 C  C   . ARG   A 1 362 ? 19.33156  15.40142  16.59011  1.000 29.31204 ? 362 ARG   A C   1 
ATOM   2772 O  O   . ARG   A 1 362 ? 20.00503  15.58385  17.61049  1.000 29.79752 ? 362 ARG   A O   1 
ATOM   2773 C  CB  . ARG   A 1 362 ? 19.93057  13.55718  14.99668  1.000 28.55461 ? 362 ARG   A CB  1 
ATOM   2774 C  CG  . ARG   A 1 362 ? 19.95655  12.05311  14.73700  1.000 29.23414 ? 362 ARG   A CG  1 
ATOM   2775 C  CD  . ARG   A 1 362 ? 20.95238  11.70118  13.63687  1.000 29.39402 ? 362 ARG   A CD  1 
ATOM   2776 N  NE  . ARG   A 1 362 ? 21.21425  10.26397  13.56896  1.000 30.83958 ? 362 ARG   A NE  1 
ATOM   2777 C  CZ  . ARG   A 1 362 ? 20.69227  9.44496   12.66012  1.000 30.07255 ? 362 ARG   A CZ  1 
ATOM   2778 N  NH1 . ARG   A 1 362 ? 19.87899  9.91472   11.72400  1.000 27.04852 ? 362 ARG   A NH1 1 
ATOM   2779 N  NH2 . ARG   A 1 362 ? 20.98910  8.15257   12.68340  1.000 29.53039 ? 362 ARG   A NH2 1 
ATOM   2780 N  N   . LEU   A 1 363 ? 18.87052  16.41572  15.85334  1.000 29.46563 ? 363 LEU   A N   1 
ATOM   2781 C  CA  . LEU   A 1 363 ? 19.14219  17.79609  16.24568  1.000 30.74566 ? 363 LEU   A CA  1 
ATOM   2782 C  C   . LEU   A 1 363 ? 18.48508  18.12738  17.57882  1.000 30.00521 ? 363 LEU   A C   1 
ATOM   2783 O  O   . LEU   A 1 363 ? 19.13358  18.65335  18.49027  1.000 29.49075 ? 363 LEU   A O   1 
ATOM   2784 C  CB  . LEU   A 1 363 ? 18.66108  18.76389  15.16195  1.000 29.60364 ? 363 LEU   A CB  1 
ATOM   2785 C  CG  . LEU   A 1 363 ? 18.63377  20.23465  15.59904  1.000 32.16741 ? 363 LEU   A CG  1 
ATOM   2786 C  CD1 . LEU   A 1 363 ? 20.04230  20.75425  15.85352  1.000 35.14262 ? 363 LEU   A CD1 1 
ATOM   2787 C  CD2 . LEU   A 1 363 ? 17.90977  21.11167  14.58513  1.000 31.98159 ? 363 LEU   A CD2 1 
ATOM   2788 N  N   . GLU   A 1 364 ? 17.19171  17.82662  17.70933  1.000 28.41324 ? 364 GLU   A N   1 
ATOM   2789 C  CA  . GLU   A 1 364 ? 16.47371  18.17229  18.93108  1.000 29.71475 ? 364 GLU   A CA  1 
ATOM   2790 C  C   . GLU   A 1 364 ? 17.09198  17.50043  20.15178  1.000 31.70439 ? 364 GLU   A C   1 
ATOM   2791 O  O   . GLU   A 1 364 ? 17.23738  18.13005  21.20624  1.000 28.73137 ? 364 GLU   A O   1 
ATOM   2792 C  CB  . GLU   A 1 364 ? 14.99884  17.79514  18.79448  1.000 28.43075 ? 364 GLU   A CB  1 
ATOM   2793 C  CG  . GLU   A 1 364 ? 14.23997  18.62520  17.76417  1.000 26.51754 ? 364 GLU   A CG  1 
ATOM   2794 C  CD  . GLU   A 1 364 ? 12.84899  18.08872  17.49108  1.000 29.06221 ? 364 GLU   A CD  1 
ATOM   2795 O  OE1 . GLU   A 1 364 ? 12.63186  16.86740  17.65982  1.000 29.58078 ? 364 GLU   A OE1 1 
ATOM   2796 O  OE2 . GLU   A 1 364 ? 11.97198  18.88706  17.10233  1.000 27.19317 ? 364 GLU   A OE2 1 
ATOM   2797 N  N   . LEU   A 1 365 ? 17.47942  16.22800  20.02667  1.000 30.25402 ? 365 LEU   A N   1 
ATOM   2798 C  CA  . LEU   A 1 365 ? 18.02770  15.51943  21.17865  1.000 30.66511 ? 365 LEU   A CA  1 
ATOM   2799 C  C   . LEU   A 1 365 ? 19.37478  16.09727  21.59487  1.000 29.87159 ? 365 LEU   A C   1 
ATOM   2800 O  O   . LEU   A 1 365 ? 19.64195  16.25802  22.79112  1.000 28.79441 ? 365 LEU   A O   1 
ATOM   2801 C  CB  . LEU   A 1 365 ? 18.14920  14.02628  20.87446  1.000 30.77403 ? 365 LEU   A CB  1 
ATOM   2802 C  CG  . LEU   A 1 365 ? 18.28910  13.16533  22.13033  1.000 34.02119 ? 365 LEU   A CG  1 
ATOM   2803 C  CD1 . LEU   A 1 365 ? 17.11435  13.40799  23.06489  1.000 32.81333 ? 365 LEU   A CD1 1 
ATOM   2804 C  CD2 . LEU   A 1 365 ? 18.39766  11.69047  21.77839  1.000 34.56474 ? 365 LEU   A CD2 1 
ATOM   2805 N  N   . GLU   A 1 366 ? 20.23463  16.41509  20.62452  1.000 31.10806 ? 366 GLU   A N   1 
ATOM   2806 C  CA  . GLU   A 1 366 ? 21.50473  17.05908  20.94275  1.000 31.25606 ? 366 GLU   A CA  1 
ATOM   2807 C  C   . GLU   A 1 366 ? 21.27786  18.36858  21.68865  1.000 34.55510 ? 366 GLU   A C   1 
ATOM   2808 O  O   . GLU   A 1 366 ? 21.87843  18.60929  22.74331  1.000 31.43309 ? 366 GLU   A O   1 
ATOM   2809 C  CB  . GLU   A 1 366 ? 22.30622  17.29748  19.66077  1.000 33.49556 ? 366 GLU   A CB  1 
ATOM   2810 C  CG  . GLU   A 1 366 ? 23.54603  18.16957  19.84995  1.000 36.68004 ? 366 GLU   A CG  1 
ATOM   2811 C  CD  . GLU   A 1 366 ? 23.26713  19.65176  19.64808  1.000 42.07455 ? 366 GLU   A CD  1 
ATOM   2812 O  OE1 . GLU   A 1 366 ? 22.60998  20.00706  18.64484  1.000 38.17288 ? 366 GLU   A OE1 1 
ATOM   2813 O  OE2 . GLU   A 1 366 ? 23.69872  20.46168  20.49667  1.000 43.98948 ? 366 GLU   A OE2 1 
ATOM   2814 N  N   . VAL   A 1 367 ? 20.40436  19.22751  21.15323  1.000 33.03730 ? 367 VAL   A N   1 
ATOM   2815 C  CA  . VAL   A 1 367 ? 20.13540  20.51672  21.78400  1.000 33.63421 ? 367 VAL   A CA  1 
ATOM   2816 C  C   . VAL   A 1 367 ? 19.56240  20.31647  23.18125  1.000 32.70074 ? 367 VAL   A C   1 
ATOM   2817 O  O   . VAL   A 1 367 ? 19.97400  20.98221  24.13949  1.000 31.03623 ? 367 VAL   A O   1 
ATOM   2818 C  CB  . VAL   A 1 367 ? 19.19173  21.35336  20.89965  1.000 32.73918 ? 367 VAL   A CB  1 
ATOM   2819 C  CG1 . VAL   A 1 367 ? 18.80327  22.64389  21.60497  1.000 33.17907 ? 367 VAL   A CG1 1 
ATOM   2820 C  CG2 . VAL   A 1 367 ? 19.83882  21.63785  19.55018  1.000 33.08398 ? 367 VAL   A CG2 1 
ATOM   2821 N  N   . ILE   A 1 368 ? 18.61321  19.38633  23.31892  1.000 31.21453 ? 368 ILE   A N   1 
ATOM   2822 C  CA  . ILE   A 1 368 ? 17.96579  19.15419  24.60976  1.000 31.75856 ? 368 ILE   A CA  1 
ATOM   2823 C  C   . ILE   A 1 368 ? 18.97359  18.65937  25.64142  1.000 31.87728 ? 368 ILE   A C   1 
ATOM   2824 O  O   . ILE   A 1 368 ? 19.00332  19.13827  26.78338  1.000 33.14433 ? 368 ILE   A O   1 
ATOM   2825 C  CB  . ILE   A 1 368 ? 16.78896  18.17207  24.44675  1.000 31.01058 ? 368 ILE   A CB  1 
ATOM   2826 C  CG1 . ILE   A 1 368 ? 15.59018  18.87542  23.80845  1.000 30.93993 ? 368 ILE   A CG1 1 
ATOM   2827 C  CG2 . ILE   A 1 368 ? 16.40573  17.55216  25.78446  1.000 30.39540 ? 368 ILE   A CG2 1 
ATOM   2828 C  CD1 . ILE   A 1 368 ? 14.54222  17.91792  23.27173  1.000 29.68338 ? 368 ILE   A CD1 1 
ATOM   2829 N  N   . LEU   A 1 369 ? 19.81019  17.69259  25.26097  1.000 32.71125 ? 369 LEU   A N   1 
ATOM   2830 C  CA  . LEU   A 1 369 ? 20.78675  17.15310  26.20303  1.000 32.99371 ? 369 LEU   A CA  1 
ATOM   2831 C  C   . LEU   A 1 369 ? 21.79288  18.21500  26.62555  1.000 35.29048 ? 369 LEU   A C   1 
ATOM   2832 O  O   . LEU   A 1 369 ? 22.12047  18.33101  27.81282  1.000 34.97645 ? 369 LEU   A O   1 
ATOM   2833 C  CB  . LEU   A 1 369 ? 21.50762  15.95237  25.59309  1.000 32.83034 ? 369 LEU   A CB  1 
ATOM   2834 C  CG  . LEU   A 1 369 ? 20.70015  14.66361  25.46025  1.000 32.03756 ? 369 LEU   A CG  1 
ATOM   2835 C  CD1 . LEU   A 1 369 ? 21.56201  13.55702  24.86552  1.000 33.16864 ? 369 LEU   A CD1 1 
ATOM   2836 C  CD2 . LEU   A 1 369 ? 20.13266  14.23965  26.80770  1.000 32.42927 ? 369 LEU   A CD2 1 
ATOM   2837 N  N   . ASN   A 1 370 ? 22.28899  19.00398  25.67109  1.000 33.86810 ? 370 ASN   A N   1 
ATOM   2838 C  CA  . ASN   A 1 370 ? 23.22646  20.06685  26.01629  1.000 35.78669 ? 370 ASN   A CA  1 
ATOM   2839 C  C   . ASN   A 1 370 ? 22.56937  21.10863  26.91027  1.000 36.73052 ? 370 ASN   A C   1 
ATOM   2840 O  O   . ASN   A 1 370 ? 23.20802  21.64863  27.82133  1.000 36.52276 ? 370 ASN   A O   1 
ATOM   2841 C  CB  . ASN   A 1 370 ? 23.78086  20.71583  24.74856  1.000 36.31356 ? 370 ASN   A CB  1 
ATOM   2842 C  CG  . ASN   A 1 370 ? 25.03248  20.02436  24.23985  1.000 37.58894 ? 370 ASN   A CG  1 
ATOM   2843 O  OD1 . ASN   A 1 370 ? 25.94393  19.72141  25.01116  1.000 38.68760 ? 370 ASN   A OD1 1 
ATOM   2844 N  ND2 . ASN   A 1 370 ? 25.08362  19.77217  22.93564  1.000 35.40815 ? 370 ASN   A ND2 1 
ATOM   2845 N  N   . ALA   A 1 371 ? 21.28657  21.39200  26.67535  1.000 34.92515 ? 371 ALA   A N   1 
ATOM   2846 C  CA  . ALA   A 1 371 ? 20.59758  22.39842  27.47539  1.000 36.66699 ? 371 ALA   A CA  1 
ATOM   2847 C  C   . ALA   A 1 371 ? 20.35903  21.91168  28.89861  1.000 36.76488 ? 371 ALA   A C   1 
ATOM   2848 O  O   . ALA   A 1 371 ? 20.49757  22.68424  29.85470  1.000 37.09799 ? 371 ALA   A O   1 
ATOM   2849 C  CB  . ALA   A 1 371 ? 19.27674  22.78402  26.81430  1.000 35.01463 ? 371 ALA   A CB  1 
ATOM   2850 N  N   . LEU   A 1 372 ? 19.99286  20.63811  29.06103  1.000 34.81209 ? 372 LEU   A N   1 
ATOM   2851 C  CA  . LEU   A 1 372 ? 19.77135  20.10274  30.40109  1.000 36.72902 ? 372 LEU   A CA  1 
ATOM   2852 C  C   . LEU   A 1 372 ? 21.06472  20.06938  31.20721  1.000 38.62127 ? 372 LEU   A C   1 
ATOM   2853 O  O   . LEU   A 1 372 ? 21.05802  20.34307  32.41275  1.000 38.31401 ? 372 LEU   A O   1 
ATOM   2854 C  CB  . LEU   A 1 372 ? 19.15678  18.70526  30.31788  1.000 35.29797 ? 372 LEU   A CB  1 
ATOM   2855 C  CG  . LEU   A 1 372 ? 17.71659  18.60303  29.80966  1.000 34.16439 ? 372 LEU   A CG  1 
ATOM   2856 C  CD1 . LEU   A 1 372 ? 17.29086  17.14276  29.72079  1.000 33.22291 ? 372 LEU   A CD1 1 
ATOM   2857 C  CD2 . LEU   A 1 372 ? 16.76648  19.38173  30.70575  1.000 34.43236 ? 372 LEU   A CD2 1 
ATOM   2858 N  N   . MET   A 1 373 ? 22.18368  19.73050  30.56305  1.000 37.67164 ? 373 MET   A N   1 
ATOM   2859 C  CA  . MET   A 1 373 ? 23.46304  19.72722  31.26407  1.000 38.85492 ? 373 MET   A CA  1 
ATOM   2860 C  C   . MET   A 1 373 ? 23.94799  21.14224  31.56266  1.000 41.45165 ? 373 MET   A C   1 
ATOM   2861 O  O   . MET   A 1 373 ? 24.68440  21.35169  32.53407  1.000 42.23195 ? 373 MET   A O   1 
ATOM   2862 C  CB  . MET   A 1 373 ? 24.50383  18.96763  30.44495  1.000 39.24349 ? 373 MET   A CB  1 
ATOM   2863 C  CG  . MET   A 1 373 ? 24.19765  17.48768  30.29583  1.000 39.59131 ? 373 MET   A CG  1 
ATOM   2864 S  SD  . MET   A 1 373 ? 25.45731  16.58188  29.38058  1.000 38.78332 ? 373 MET   A SD  1 
ATOM   2865 C  CE  . MET   A 1 373 ? 25.22296  17.22239  27.72277  1.000 36.82164 ? 373 MET   A CE  1 
ATOM   2866 N  N   . ASP   A 1 374 ? 23.55337  22.12059  30.74427  1.000 37.78145 ? 374 ASP   A N   1 
ATOM   2867 C  CA  . ASP   A 1 374 ? 23.94774  23.50421  30.99010  1.000 40.54435 ? 374 ASP   A CA  1 
ATOM   2868 C  C   . ASP   A 1 374 ? 23.05877  24.15715  32.04232  1.000 39.43005 ? 374 ASP   A C   1 
ATOM   2869 O  O   . ASP   A 1 374 ? 23.55650  24.72522  33.02038  1.000 39.80419 ? 374 ASP   A O   1 
ATOM   2870 C  CB  . ASP   A 1 374 ? 23.90241  24.30978  29.68836  1.000 37.58908 ? 374 ASP   A CB  1 
ATOM   2871 C  CG  . ASP   A 1 374 ? 25.03552  23.96414  28.74240  1.000 39.31751 ? 374 ASP   A CG  1 
ATOM   2872 O  OD1 . ASP   A 1 374 ? 25.96693  23.24447  29.15750  1.000 40.68589 ? 374 ASP   A OD1 1 
ATOM   2873 O  OD2 . ASP   A 1 374 ? 24.99117  24.41370  27.57760  1.000 38.63647 ? 374 ASP   A OD2 1 
ATOM   2874 N  N   . ARG   A 1 375 ? 21.74022  24.07386  31.86245  1.000 38.38340 ? 375 ARG   A N   1 
ATOM   2875 C  CA  . ARG   A 1 375 ? 20.80061  24.84039  32.67070  1.000 40.19080 ? 375 ARG   A CA  1 
ATOM   2876 C  C   . ARG   A 1 375 ? 20.38526  24.14030  33.95598  1.000 40.39429 ? 375 ARG   A C   1 
ATOM   2877 O  O   . ARG   A 1 375 ? 19.96863  24.81602  34.90320  1.000 39.28380 ? 375 ARG   A O   1 
ATOM   2878 C  CB  . ARG   A 1 375 ? 19.54546  25.16006  31.85276  1.000 39.78025 ? 375 ARG   A CB  1 
ATOM   2879 C  CG  . ARG   A 1 375 ? 19.80437  25.98814  30.60015  1.000 40.02778 ? 375 ARG   A CG  1 
ATOM   2880 C  CD  . ARG   A 1 375 ? 19.84731  27.47472  30.91022  1.000 41.45359 ? 375 ARG   A CD  1 
ATOM   2881 N  NE  . ARG   A 1 375 ? 18.61467  27.93401  31.54417  1.000 41.26549 ? 375 ARG   A NE  1 
ATOM   2882 C  CZ  . ARG   A 1 375 ? 17.52087  28.29517  30.88069  1.000 40.63764 ? 375 ARG   A CZ  1 
ATOM   2883 N  NH1 . ARG   A 1 375 ? 17.49900  28.24836  29.55655  1.000 40.42936 ? 375 ARG   A NH1 1 
ATOM   2884 N  NH2 . ARG   A 1 375 ? 16.44480  28.69842  31.54112  1.000 40.04077 ? 375 ARG   A NH2 1 
ATOM   2885 N  N   . VAL   A 1 376 ? 20.47220  22.81625  34.01804  1.000 40.80322 ? 376 VAL   A N   1 
ATOM   2886 C  CA  . VAL   A 1 376 ? 20.01864  22.10607  35.21068  1.000 40.67137 ? 376 VAL   A CA  1 
ATOM   2887 C  C   . VAL   A 1 376 ? 20.92458  20.89720  35.44540  1.000 42.41425 ? 376 VAL   A C   1 
ATOM   2888 O  O   . VAL   A 1 376 ? 20.50173  19.74243  35.28281  1.000 40.50460 ? 376 VAL   A O   1 
ATOM   2889 C  CB  . VAL   A 1 376 ? 18.52114  21.75680  35.08667  1.000 41.00738 ? 376 VAL   A CB  1 
ATOM   2890 C  CG1 . VAL   A 1 376 ? 18.21658  20.98219  33.79845  1.000 40.23431 ? 376 VAL   A CG1 1 
ATOM   2891 C  CG2 . VAL   A 1 376 ? 18.00034  21.04409  36.33012  1.000 42.22849 ? 376 VAL   A CG2 1 
ATOM   2892 N  N   . PRO   A 1 377 ? 22.18577  21.11604  35.83275  1.000 41.87386 ? 377 PRO   A N   1 
ATOM   2893 C  CA  . PRO   A 1 377 ? 23.08290  19.97617  36.08440  1.000 42.91363 ? 377 PRO   A CA  1 
ATOM   2894 C  C   . PRO   A 1 377 ? 22.68885  19.15521  37.29832  1.000 42.87591 ? 377 PRO   A C   1 
ATOM   2895 O  O   . PRO   A 1 377 ? 23.03756  17.96953  37.36467  1.000 42.19255 ? 377 PRO   A O   1 
ATOM   2896 C  CB  . PRO   A 1 377 ? 24.45426  20.64011  36.28829  1.000 44.28014 ? 377 PRO   A CB  1 
ATOM   2897 C  CG  . PRO   A 1 377 ? 24.28997  22.05565  35.81021  1.000 45.78860 ? 377 PRO   A CG  1 
ATOM   2898 C  CD  . PRO   A 1 377 ? 22.86362  22.40261  36.04877  1.000 43.33811 ? 377 PRO   A CD  1 
ATOM   2899 N  N   . THR   A 1 378 ? 21.97932  19.74351  38.25726  1.000 42.73290 ? 378 THR   A N   1 
ATOM   2900 C  CA  . THR   A 1 378 ? 21.51757  19.03340  39.44063  1.000 43.03377 ? 378 THR   A CA  1 
ATOM   2901 C  C   . THR   A 1 378 ? 20.19918  18.30722  39.20852  1.000 42.64861 ? 378 THR   A C   1 
ATOM   2902 O  O   . THR   A 1 378 ? 19.54339  17.91208  40.17781  1.000 43.09061 ? 378 THR   A O   1 
ATOM   2903 C  CB  . THR   A 1 378 ? 21.37705  20.00476  40.61745  1.000 43.91175 ? 378 THR   A CB  1 
ATOM   2904 O  OG1 . THR   A 1 378 ? 20.40583  21.01150  40.30068  1.000 43.21997 ? 378 THR   A OG1 1 
ATOM   2905 C  CG2 . THR   A 1 378 ? 22.71204  20.67649  40.91059  1.000 43.97257 ? 378 THR   A CG2 1 
ATOM   2906 N  N   . LEU   A 1 379 ? 19.79742  18.12974  37.95193  1.000 42.35996 ? 379 LEU   A N   1 
ATOM   2907 C  CA  . LEU   A 1 379 ? 18.55649  17.43040  37.65293  1.000 42.30456 ? 379 LEU   A CA  1 
ATOM   2908 C  C   . LEU   A 1 379 ? 18.63315  15.98437  38.12608  1.000 42.93293 ? 379 LEU   A C   1 
ATOM   2909 O  O   . LEU   A 1 379 ? 19.64937  15.30715  37.94902  1.000 41.97313 ? 379 LEU   A O   1 
ATOM   2910 C  CB  . LEU   A 1 379 ? 18.27351  17.47451  36.15035  1.000 41.75912 ? 379 LEU   A CB  1 
ATOM   2911 C  CG  . LEU   A 1 379 ? 16.95177  16.86443  35.68025  1.000 42.52192 ? 379 LEU   A CG  1 
ATOM   2912 C  CD1 . LEU   A 1 379 ? 15.77921  17.72021  36.12882  1.000 41.97246 ? 379 LEU   A CD1 1 
ATOM   2913 C  CD2 . LEU   A 1 379 ? 16.94574  16.68394  34.16743  1.000 40.38766 ? 379 LEU   A CD2 1 
ATOM   2914 N  N   . ARG   A 1 380 ? 17.54780  15.51573  38.73493  1.000 43.09353 ? 380 ARG   A N   1 
ATOM   2915 C  CA  . ARG   A 1 380 ? 17.45670  14.13865  39.19424  1.000 44.21941 ? 380 ARG   A CA  1 
ATOM   2916 C  C   . ARG   A 1 380 ? 15.98606  13.76758  39.28701  1.000 44.06630 ? 380 ARG   A C   1 
ATOM   2917 O  O   . ARG   A 1 380 ? 15.11395  14.63319  39.40223  1.000 43.25695 ? 380 ARG   A O   1 
ATOM   2918 C  CB  . ARG   A 1 380 ? 18.15387  13.94282  40.54502  1.000 45.98769 ? 380 ARG   A CB  1 
ATOM   2919 C  CG  . ARG   A 1 380 ? 17.52494  14.73346  41.67350  1.000 47.38166 ? 380 ARG   A CG  1 
ATOM   2920 C  CD  . ARG   A 1 380 ? 18.36790  14.68166  42.93355  1.000 53.20762 ? 380 ARG   A CD  1 
ATOM   2921 N  NE  . ARG   A 1 380 ? 18.01902  15.76840  43.84377  1.000 53.50787 ? 380 ARG   A NE  1 
ATOM   2922 C  CZ  . ARG   A 1 380 ? 17.11693  15.67202  44.81480  1.000 56.46292 ? 380 ARG   A CZ  1 
ATOM   2923 N  NH1 . ARG   A 1 380 ? 16.46916  14.53020  45.01158  1.000 54.32526 ? 380 ARG   A NH1 1 
ATOM   2924 N  NH2 . ARG   A 1 380 ? 16.86352  16.71874  45.59036  1.000 53.64238 ? 380 ARG   A NH2 1 
ATOM   2925 N  N   . LEU   A 1 381 ? 15.72257  12.46709  39.22426  1.000 43.62218 ? 381 LEU   A N   1 
ATOM   2926 C  CA  . LEU   A 1 381 ? 14.35474  11.98271  39.32730  1.000 44.11740 ? 381 LEU   A CA  1 
ATOM   2927 C  C   . LEU   A 1 381 ? 13.80208  12.23138  40.72432  1.000 48.74498 ? 381 LEU   A C   1 
ATOM   2928 O  O   . LEU   A 1 381 ? 14.51529  12.11073  41.72556  1.000 45.79354 ? 381 LEU   A O   1 
ATOM   2929 C  CB  . LEU   A 1 381 ? 14.29170  10.49357  38.98719  1.000 43.60130 ? 381 LEU   A CB  1 
ATOM   2930 C  CG  . LEU   A 1 381 ? 13.87526  10.10472  37.56607  1.000 42.76834 ? 381 LEU   A CG  1 
ATOM   2931 C  CD1 . LEU   A 1 381 ? 14.46433  11.05615  36.53102  1.000 40.60136 ? 381 LEU   A CD1 1 
ATOM   2932 C  CD2 . LEU   A 1 381 ? 14.29334  8.67080   37.27501  1.000 40.20950 ? 381 LEU   A CD2 1 
ATOM   2933 N  N   . ALA   A 1 382 ? 12.52388  12.59565  40.78350  1.000 45.68179 ? 382 ALA   A N   1 
ATOM   2934 C  CA  . ALA   A 1 382 ? 11.83744  12.80948  42.04766  1.000 45.78994 ? 382 ALA   A CA  1 
ATOM   2935 C  C   . ALA   A 1 382 ? 11.24880  11.52882  42.62598  1.000 46.82418 ? 382 ALA   A C   1 
ATOM   2936 O  O   . ALA   A 1 382 ? 10.71728  11.56233  43.74237  1.000 46.82708 ? 382 ALA   A O   1 
ATOM   2937 C  CB  . ALA   A 1 382 ? 10.73176  13.85858  41.88003  1.000 45.31312 ? 382 ALA   A CB  1 
ATOM   2938 N  N   . VAL   A 1 383 ? 11.33011  10.41386  41.90412  1.000 47.58383 ? 383 VAL   A N   1 
ATOM   2939 C  CA  . VAL   A 1 383 ? 10.85078  9.11559   42.38177  1.000 48.86996 ? 383 VAL   A CA  1 
ATOM   2940 C  C   . VAL   A 1 383 ? 11.80730  8.03271   41.90749  1.000 48.41971 ? 383 VAL   A C   1 
ATOM   2941 O  O   . VAL   A 1 383 ? 12.57028  8.23069   40.95242  1.000 47.46527 ? 383 VAL   A O   1 
ATOM   2942 C  CB  . VAL   A 1 383 ? 9.42301   8.80399   41.88374  1.000 52.43833 ? 383 VAL   A CB  1 
ATOM   2943 C  CG1 . VAL   A 1 383 ? 8.39835   9.72643   42.54235  1.000 49.92614 ? 383 VAL   A CG1 1 
ATOM   2944 C  CG2 . VAL   A 1 383 ? 9.34686   8.93583   40.36322  1.000 48.93771 ? 383 VAL   A CG2 1 
ATOM   2945 N  N   . PRO   A 1 384 ? 11.81130  6.87967   42.57908  1.000 50.01206 ? 384 PRO   A N   1 
ATOM   2946 C  CA  . PRO   A 1 384 ? 12.51767  5.71965   42.01999  1.000 49.19653 ? 384 PRO   A CA  1 
ATOM   2947 C  C   . PRO   A 1 384 ? 11.93916  5.33708   40.66436  1.000 49.11582 ? 384 PRO   A C   1 
ATOM   2948 O  O   . PRO   A 1 384 ? 10.73950  5.48620   40.41291  1.000 49.03947 ? 384 PRO   A O   1 
ATOM   2949 C  CB  . PRO   A 1 384 ? 12.27951  4.61541   43.05785  1.000 49.79137 ? 384 PRO   A CB  1 
ATOM   2950 C  CG  . PRO   A 1 384 ? 12.06140  5.34908   44.33031  1.000 50.37211 ? 384 PRO   A CG  1 
ATOM   2951 C  CD  . PRO   A 1 384 ? 11.37567  6.64091   43.96426  1.000 50.18340 ? 384 PRO   A CD  1 
ATOM   2952 N  N   . VAL   A 1 385 ? 12.81254  4.84220   39.78024  1.000 48.99315 ? 385 VAL   A N   1 
ATOM   2953 C  CA  . VAL   A 1 385 ? 12.38060  4.46958   38.43647  1.000 49.06525 ? 385 VAL   A CA  1 
ATOM   2954 C  C   . VAL   A 1 385 ? 11.36160  3.34186   38.47723  1.000 50.14795 ? 385 VAL   A C   1 
ATOM   2955 O  O   . VAL   A 1 385 ? 10.57827  3.18227   37.53462  1.000 50.06817 ? 385 VAL   A O   1 
ATOM   2956 C  CB  . VAL   A 1 385 ? 13.59616  4.09214   37.55680  1.000 47.88418 ? 385 VAL   A CB  1 
ATOM   2957 C  CG1 . VAL   A 1 385 ? 14.87603  4.68522   38.12057  1.000 46.11892 ? 385 VAL   A CG1 1 
ATOM   2958 C  CG2 . VAL   A 1 385 ? 13.71956  2.57967   37.39084  1.000 50.16245 ? 385 VAL   A CG2 1 
ATOM   2959 N  N   . GLU   A 1 386 ? 11.34038  2.56158   39.56326  1.000 51.52689 ? 386 GLU   A N   1 
ATOM   2960 C  CA  . GLU   A 1 386 ? 10.35711  1.49208   39.69800  1.000 52.27505 ? 386 GLU   A CA  1 
ATOM   2961 C  C   . GLU   A 1 386 ? 8.94197   2.04165   39.81452  1.000 51.56328 ? 386 GLU   A C   1 
ATOM   2962 O  O   . GLU   A 1 386 ? 7.98041   1.35407   39.45213  1.000 51.18756 ? 386 GLU   A O   1 
ATOM   2963 C  CB  . GLU   A 1 386 ? 10.68649  0.61986   40.91169  1.000 53.56660 ? 386 GLU   A CB  1 
ATOM   2964 C  CG  . GLU   A 1 386 ? 12.00298  -0.15005  40.80673  1.000 57.35172 ? 386 GLU   A CG  1 
ATOM   2965 C  CD  . GLU   A 1 386 ? 13.22349  0.71305   41.08168  1.000 64.55053 ? 386 GLU   A CD  1 
ATOM   2966 O  OE1 . GLU   A 1 386 ? 13.05124  1.89705   41.44302  1.000 55.42487 ? 386 GLU   A OE1 1 
ATOM   2967 O  OE2 . GLU   A 1 386 ? 14.35636  0.20555   40.93606  1.000 71.50487 ? 386 GLU   A OE2 1 
ATOM   2968 N  N   . GLN   A 1 387 ? 8.79364   3.27178   40.31147  1.000 50.59496 ? 387 GLN   A N   1 
ATOM   2969 C  CA  . GLN   A 1 387 ? 7.48002   3.89606   40.40688  1.000 51.31375 ? 387 GLN   A CA  1 
ATOM   2970 C  C   . GLN   A 1 387 ? 7.01397   4.48268   39.08308  1.000 50.61767 ? 387 GLN   A C   1 
ATOM   2971 O  O   . GLN   A 1 387 ? 5.82636   4.79222   38.94262  1.000 50.69388 ? 387 GLN   A O   1 
ATOM   2972 C  CB  . GLN   A 1 387 ? 7.48896   4.99265   41.47574  1.000 52.69849 ? 387 GLN   A CB  1 
ATOM   2973 C  CG  . GLN   A 1 387 ? 7.67507   4.47665   42.89356  1.000 53.82879 ? 387 GLN   A CG  1 
ATOM   2974 C  CD  . GLN   A 1 387 ? 7.78853   5.59466   43.91349  1.000 56.65909 ? 387 GLN   A CD  1 
ATOM   2975 O  OE1 . GLN   A 1 387 ? 7.20029   6.66573   43.75234  1.000 59.15815 ? 387 GLN   A OE1 1 
ATOM   2976 N  NE2 . GLN   A 1 387 ? 8.55303   5.35065   44.97071  1.000 59.52055 ? 387 GLN   A NE2 1 
ATOM   2977 N  N   . LEU   A 1 388 ? 7.91485   4.64773   38.11957  1.000 49.43082 ? 388 LEU   A N   1 
ATOM   2978 C  CA  . LEU   A 1 388 ? 7.53084   5.16870   36.81696  1.000 49.81881 ? 388 LEU   A CA  1 
ATOM   2979 C  C   . LEU   A 1 388 ? 6.67285   4.15422   36.06806  1.000 48.30714 ? 388 LEU   A C   1 
ATOM   2980 O  O   . LEU   A 1 388 ? 6.85154   2.93991   36.19406  1.000 48.30081 ? 388 LEU   A O   1 
ATOM   2981 C  CB  . LEU   A 1 388 ? 8.77292   5.52279   35.99935  1.000 47.73353 ? 388 LEU   A CB  1 
ATOM   2982 C  CG  . LEU   A 1 388 ? 9.65726   6.62409   36.58798  1.000 46.14436 ? 388 LEU   A CG  1 
ATOM   2983 C  CD1 . LEU   A 1 388 ? 10.89536  6.84458   35.73279  1.000 44.28977 ? 388 LEU   A CD1 1 
ATOM   2984 C  CD2 . LEU   A 1 388 ? 8.86860   7.91737   36.73950  1.000 45.65252 ? 388 LEU   A CD2 1 
ATOM   2985 N  N   . VAL   A 1 389 ? 5.72848   4.66845   35.28447  1.000 46.93863 ? 389 VAL   A N   1 
ATOM   2986 C  CA  . VAL   A 1 389 ? 4.76002   3.85339   34.55852  1.000 45.98309 ? 389 VAL   A CA  1 
ATOM   2987 C  C   . VAL   A 1 389 ? 5.16744   3.81910   33.09195  1.000 44.47905 ? 389 VAL   A C   1 
ATOM   2988 O  O   . VAL   A 1 389 ? 5.21819   4.86133   32.42736  1.000 43.89310 ? 389 VAL   A O   1 
ATOM   2989 C  CB  . VAL   A 1 389 ? 3.33111   4.39189   34.72403  1.000 46.48186 ? 389 VAL   A CB  1 
ATOM   2990 C  CG1 . VAL   A 1 389 ? 2.37608   3.65199   33.79987  1.000 45.73920 ? 389 VAL   A CG1 1 
ATOM   2991 C  CG2 . VAL   A 1 389 ? 2.88469   4.26680   36.17554  1.000 47.29437 ? 389 VAL   A CG2 1 
ATOM   2992 N  N   . LEU   A 1 390 ? 5.44811   2.62208   32.58775  1.000 42.82899 ? 390 LEU   A N   1 
ATOM   2993 C  CA  . LEU   A 1 390 ? 5.90789   2.44159   31.21826  1.000 41.71340 ? 390 LEU   A CA  1 
ATOM   2994 C  C   . LEU   A 1 390 ? 4.72694   2.20621   30.28525  1.000 40.78200 ? 390 LEU   A C   1 
ATOM   2995 O  O   . LEU   A 1 390 ? 3.74232   1.56157   30.65921  1.000 40.11601 ? 390 LEU   A O   1 
ATOM   2996 C  CB  . LEU   A 1 390 ? 6.88295   1.26351   31.13318  1.000 41.38282 ? 390 LEU   A CB  1 
ATOM   2997 C  CG  . LEU   A 1 390 ? 8.38192   1.50820   31.35319  1.000 42.42154 ? 390 LEU   A CG  1 
ATOM   2998 C  CD1 . LEU   A 1 390 ? 8.64283   2.61926   32.35743  1.000 42.17239 ? 390 LEU   A CD1 1 
ATOM   2999 C  CD2 . LEU   A 1 390 ? 9.06911   0.22511   31.80419  1.000 39.63304 ? 390 LEU   A CD2 1 
ATOM   3000 N  N   . ARG   A 1 391 ? 4.82887   2.74033   29.06942  1.000 38.69353 ? 391 ARG   A N   1 
ATOM   3001 C  CA  . ARG   A 1 391 ? 3.84405   2.43593   28.04607  1.000 38.05900 ? 391 ARG   A CA  1 
ATOM   3002 C  C   . ARG   A 1 391 ? 4.02877   0.99880   27.55831  1.000 36.98555 ? 391 ARG   A C   1 
ATOM   3003 O  O   . ARG   A 1 391 ? 5.14678   0.47668   27.55161  1.000 36.21586 ? 391 ARG   A O   1 
ATOM   3004 C  CB  . ARG   A 1 391 ? 3.96688   3.39642   26.86607  1.000 37.55694 ? 391 ARG   A CB  1 
ATOM   3005 C  CG  . ARG   A 1 391 ? 3.75082   4.86035   27.20009  1.000 39.54493 ? 391 ARG   A CG  1 
ATOM   3006 C  CD  . ARG   A 1 391 ? 3.22692   5.61400   25.98153  1.000 40.10125 ? 391 ARG   A CD  1 
ATOM   3007 N  NE  . ARG   A 1 391 ? 3.32667   7.06161   26.13837  1.000 43.78243 ? 391 ARG   A NE  1 
ATOM   3008 C  CZ  . ARG   A 1 391 ? 4.16686   7.83050   25.45390  1.000 39.64124 ? 391 ARG   A CZ  1 
ATOM   3009 N  NH1 . ARG   A 1 391 ? 4.97808   7.29322   24.55034  1.000 36.36562 ? 391 ARG   A NH1 1 
ATOM   3010 N  NH2 . ARG   A 1 391 ? 4.19044   9.13857   25.66706  1.000 40.12301 ? 391 ARG   A NH2 1 
ATOM   3011 N  N   . PRO   A 1 392 ? 2.94891   0.33783   27.14685  1.000 36.89667 ? 392 PRO   A N   1 
ATOM   3012 C  CA  . PRO   A 1 392 ? 3.06326   -1.04904  26.68066  1.000 36.60901 ? 392 PRO   A CA  1 
ATOM   3013 C  C   . PRO   A 1 392 ? 3.76665   -1.12997  25.33334  1.000 36.95636 ? 392 PRO   A C   1 
ATOM   3014 O  O   . PRO   A 1 392 ? 3.96541   -0.13596  24.63226  1.000 34.64711 ? 392 PRO   A O   1 
ATOM   3015 C  CB  . PRO   A 1 392 ? 1.60651   -1.50830  26.57832  1.000 36.56080 ? 392 PRO   A CB  1 
ATOM   3016 C  CG  . PRO   A 1 392 ? 0.84003   -0.24716  26.34550  1.000 37.21634 ? 392 PRO   A CG  1 
ATOM   3017 C  CD  . PRO   A 1 392 ? 1.54862   0.79775   27.16295  1.000 35.22130 ? 392 PRO   A CD  1 
ATOM   3018 N  N   . GLY   A 1 393 ? 4.14252   -2.35659  24.97157  1.000 36.90523 ? 393 GLY   A N   1 
ATOM   3019 C  CA  . GLY   A 1 393 ? 4.82414   -2.59837  23.71154  1.000 36.31750 ? 393 GLY   A CA  1 
ATOM   3020 C  C   . GLY   A 1 393 ? 3.95816   -2.41961  22.48131  1.000 35.59502 ? 393 GLY   A C   1 
ATOM   3021 O  O   . GLY   A 1 393 ? 4.47199   -2.53157  21.36302  1.000 36.28205 ? 393 GLY   A O   1 
ATOM   3022 N  N   . THR   A 1 394 ? 2.66425   -2.15345  22.65790  1.000 33.90347 ? 394 THR   A N   1 
ATOM   3023 C  CA  . THR   A 1 394 ? 1.74973   -1.91631  21.54446  1.000 36.75427 ? 394 THR   A CA  1 
ATOM   3024 C  C   . THR   A 1 394 ? 1.80259   -0.48423  21.01686  1.000 36.31517 ? 394 THR   A C   1 
ATOM   3025 O  O   . THR   A 1 394 ? 1.07460   -0.16055  20.07173  1.000 35.39393 ? 394 THR   A O   1 
ATOM   3026 C  CB  . THR   A 1 394 ? 0.31232   -2.24935  21.96356  1.000 37.42485 ? 394 THR   A CB  1 
ATOM   3027 O  OG1 . THR   A 1 394 ? 0.07003   -1.73775  23.27915  1.000 38.26384 ? 394 THR   A OG1 1 
ATOM   3028 C  CG2 . THR   A 1 394 ? 0.08648   -3.75902  21.96463  1.000 38.70026 ? 394 THR   A CG2 1 
ATOM   3029 N  N   . THR   A 1 395 ? 2.63644   0.38043   21.58754  1.000 36.09252 ? 395 THR   A N   1 
ATOM   3030 C  CA  . THR   A 1 395 ? 2.67759   1.77992   21.17701  1.000 36.86604 ? 395 THR   A CA  1 
ATOM   3031 C  C   . THR   A 1 395 ? 4.11722   2.27736   21.26810  1.000 35.41571 ? 395 THR   A C   1 
ATOM   3032 O  O   . THR   A 1 395 ? 5.06097   1.49633   21.42758  1.000 32.15208 ? 395 THR   A O   1 
ATOM   3033 C  CB  . THR   A 1 395 ? 1.72242   2.62538   22.03154  1.000 36.70311 ? 395 THR   A CB  1 
ATOM   3034 O  OG1 . THR   A 1 395 ? 1.70597   3.97333   21.54401  1.000 39.88370 ? 395 THR   A OG1 1 
ATOM   3035 C  CG2 . THR   A 1 395 ? 2.16409   2.62784   23.49004  1.000 36.31083 ? 395 THR   A CG2 1 
ATOM   3036 N  N   . ILE   A 1 396 ? 4.28054   3.59814   21.15921  1.000 34.97223 ? 396 ILE   A N   1 
ATOM   3037 C  CA  . ILE   A 1 396 ? 5.59706   4.20637   21.29399  1.000 33.80291 ? 396 ILE   A CA  1 
ATOM   3038 C  C   . ILE   A 1 396 ? 6.09676   4.02424   22.71891  1.000 33.46566 ? 396 ILE   A C   1 
ATOM   3039 O  O   . ILE   A 1 396 ? 5.37682   4.29707   23.68740  1.000 33.57077 ? 396 ILE   A O   1 
ATOM   3040 C  CB  . ILE   A 1 396 ? 5.53279   5.69133   20.90969  1.000 33.32898 ? 396 ILE   A CB  1 
ATOM   3041 C  CG1 . ILE   A 1 396 ? 5.00427   5.84840   19.48325  1.000 35.75197 ? 396 ILE   A CG1 1 
ATOM   3042 C  CG2 . ILE   A 1 396 ? 6.89663   6.34205   21.05848  1.000 31.65663 ? 396 ILE   A CG2 1 
ATOM   3043 C  CD1 . ILE   A 1 396 ? 4.80317   7.29204   19.06904  1.000 36.32103 ? 396 ILE   A CD1 1 
ATOM   3044 N  N   . GLN   A 1 397 ? 7.33629   3.55754   22.85310  1.000 31.59275 ? 397 GLN   A N   1 
ATOM   3045 C  CA  . GLN   A 1 397 ? 7.92968   3.38504   24.17171  1.000 33.02983 ? 397 GLN   A CA  1 
ATOM   3046 C  C   . GLN   A 1 397 ? 8.08724   4.73401   24.86328  1.000 34.32921 ? 397 GLN   A C   1 
ATOM   3047 O  O   . GLN   A 1 397 ? 8.46208   5.72892   24.23974  1.000 28.45803 ? 397 GLN   A O   1 
ATOM   3048 C  CB  . GLN   A 1 397 ? 9.29198   2.69968   24.05339  1.000 32.91336 ? 397 GLN   A CB  1 
ATOM   3049 C  CG  . GLN   A 1 397 ? 9.28570   1.40167   23.25511  1.000 32.68647 ? 397 GLN   A CG  1 
ATOM   3050 C  CD  . GLN   A 1 397 ? 8.73163   0.22599   24.03957  1.000 34.89018 ? 397 GLN   A CD  1 
ATOM   3051 O  OE1 . GLN   A 1 397 ? 8.54695   0.30441   25.25415  1.000 34.13048 ? 397 GLN   A OE1 1 
ATOM   3052 N  NE2 . GLN   A 1 397 ? 8.46530   -0.87447  23.34487  1.000 33.68422 ? 397 GLN   A NE2 1 
ATOM   3053 N  N   . GLY   A 1 398 ? 7.80487   4.76374   26.15976  1.000 35.66138 ? 398 GLY   A N   1 
ATOM   3054 C  CA  . GLY   A 1 398 ? 7.94909   5.98840   26.91848  1.000 35.72451 ? 398 GLY   A CA  1 
ATOM   3055 C  C   . GLY   A 1 398 ? 7.29793   5.85851   28.28096  1.000 39.20359 ? 398 GLY   A C   1 
ATOM   3056 O  O   . GLY   A 1 398 ? 6.82328   4.78721   28.66595  1.000 36.81116 ? 398 GLY   A O   1 
ATOM   3057 N  N   . VAL   A 1 399 ? 7.29332   6.97654   29.00392  1.000 39.61241 ? 399 VAL   A N   1 
ATOM   3058 C  CA  . VAL   A 1 399 ? 6.67074   7.07554   30.31767  1.000 40.82393 ? 399 VAL   A CA  1 
ATOM   3059 C  C   . VAL   A 1 399 ? 5.59419   8.14973   30.25873  1.000 42.40517 ? 399 VAL   A C   1 
ATOM   3060 O  O   . VAL   A 1 399 ? 5.74500   9.15601   29.55680  1.000 42.57894 ? 399 VAL   A O   1 
ATOM   3061 C  CB  . VAL   A 1 399 ? 7.70477   7.38949   31.42080  1.000 40.67865 ? 399 VAL   A CB  1 
ATOM   3062 C  CG1 . VAL   A 1 399 ? 8.71442   6.25891   31.53692  1.000 40.48767 ? 399 VAL   A CG1 1 
ATOM   3063 C  CG2 . VAL   A 1 399 ? 8.41432   8.71022   31.13636  1.000 39.66476 ? 399 VAL   A CG2 1 
ATOM   3064 N  N   . ASN   A 1 400 ? 4.50224   7.93326   30.99559  1.000 43.03544 ? 400 ASN   A N   1 
ATOM   3065 C  CA  . ASN   A 1 400 ? 3.39831   8.88764   30.95944  1.000 45.28249 ? 400 ASN   A CA  1 
ATOM   3066 C  C   . ASN   A 1 400 ? 3.73499   10.17183  31.70908  1.000 44.44527 ? 400 ASN   A C   1 
ATOM   3067 O  O   . ASN   A 1 400 ? 3.18941   11.23426  31.38875  1.000 43.36312 ? 400 ASN   A O   1 
ATOM   3068 C  CB  . ASN   A 1 400 ? 2.13151   8.24935   31.52855  1.000 48.37688 ? 400 ASN   A CB  1 
ATOM   3069 C  CG  . ASN   A 1 400 ? 1.67921   7.04155   30.72842  1.000 50.51506 ? 400 ASN   A CG  1 
ATOM   3070 O  OD1 . ASN   A 1 400 ? 1.32312   7.15902   29.55503  1.000 50.21168 ? 400 ASN   A OD1 1 
ATOM   3071 N  ND2 . ASN   A 1 400 ? 1.68377   5.87472   31.36212  1.000 51.66246 ? 400 ASN   A ND2 1 
ATOM   3072 N  N   . GLU   A 1 401 ? 4.62042   10.09862  32.70038  1.000 43.01919 ? 401 GLU   A N   1 
ATOM   3073 C  CA  . GLU   A 1 401 ? 5.08666   11.28911  33.39613  1.000 43.92111 ? 401 GLU   A CA  1 
ATOM   3074 C  C   . GLU   A 1 401 ? 6.43010   10.98152  34.03795  1.000 42.16918 ? 401 GLU   A C   1 
ATOM   3075 O  O   . GLU   A 1 401 ? 6.71274   9.83676   34.39967  1.000 41.62662 ? 401 GLU   A O   1 
ATOM   3076 C  CB  . GLU   A 1 401 ? 4.07456   11.76885  34.44417  1.000 45.08714 ? 401 GLU   A CB  1 
ATOM   3077 C  CG  . GLU   A 1 401 ? 3.62707   10.70612  35.43069  1.000 47.75916 ? 401 GLU   A CG  1 
ATOM   3078 C  CD  . GLU   A 1 401 ? 2.51143   11.19367  36.33966  1.000 55.10109 ? 401 GLU   A CD  1 
ATOM   3079 O  OE1 . GLU   A 1 401 ? 1.51259   11.73951  35.82318  1.000 57.24694 ? 401 GLU   A OE1 1 
ATOM   3080 O  OE2 . GLU   A 1 401 ? 2.63748   11.04051  37.57241  1.000 58.18293 ? 401 GLU   A OE2 1 
ATOM   3081 N  N   . LEU   A 1 402 ? 7.26012   12.01549  34.16027  1.000 39.96525 ? 402 LEU   A N   1 
ATOM   3082 C  CA  . LEU   A 1 402 ? 8.60892   11.88377  34.70699  1.000 40.40901 ? 402 LEU   A CA  1 
ATOM   3083 C  C   . LEU   A 1 402 ? 8.81479   12.96293  35.76089  1.000 40.27171 ? 402 LEU   A C   1 
ATOM   3084 O  O   . LEU   A 1 402 ? 9.29659   14.06371  35.45687  1.000 38.62728 ? 402 LEU   A O   1 
ATOM   3085 C  CB  . LEU   A 1 402 ? 9.66174   11.97117  33.60420  1.000 38.63368 ? 402 LEU   A CB  1 
ATOM   3086 C  CG  . LEU   A 1 402 ? 11.10768  11.69744  34.01798  1.000 38.60099 ? 402 LEU   A CG  1 
ATOM   3087 C  CD1 . LEU   A 1 402 ? 11.20336  10.39132  34.78847  1.000 38.97060 ? 402 LEU   A CD1 1 
ATOM   3088 C  CD2 . LEU   A 1 402 ? 12.01010  11.66346  32.79539  1.000 36.72104 ? 402 LEU   A CD2 1 
ATOM   3089 N  N   . PRO   A 1 403 ? 8.44935   12.68636  37.01235  1.000 41.47554 ? 403 PRO   A N   1 
ATOM   3090 C  CA  . PRO   A 1 403 ? 8.69289   13.65640  38.09202  1.000 40.88729 ? 403 PRO   A CA  1 
ATOM   3091 C  C   . PRO   A 1 403 ? 10.18319  13.85913  38.31120  1.000 41.03909 ? 403 PRO   A C   1 
ATOM   3092 O  O   . PRO   A 1 403 ? 10.92221  12.91374  38.59532  1.000 42.56074 ? 403 PRO   A O   1 
ATOM   3093 C  CB  . PRO   A 1 403 ? 8.02352   13.00594  39.31012  1.000 42.93445 ? 403 PRO   A CB  1 
ATOM   3094 C  CG  . PRO   A 1 403 ? 7.07036   11.99678  38.74370  1.000 43.51660 ? 403 PRO   A CG  1 
ATOM   3095 C  CD  . PRO   A 1 403 ? 7.71056   11.50409  37.48404  1.000 41.36472 ? 403 PRO   A CD  1 
ATOM   3096 N  N   . VAL   A 1 404 ? 10.62505  15.10808  38.16917  1.000 41.63587 ? 404 VAL   A N   1 
ATOM   3097 C  CA  . VAL   A 1 404 ? 12.02370  15.46890  38.34276  1.000 42.00589 ? 404 VAL   A CA  1 
ATOM   3098 C  C   . VAL   A 1 404 ? 12.11520  16.60901  39.34780  1.000 43.40603 ? 404 VAL   A C   1 
ATOM   3099 O  O   . VAL   A 1 404 ? 11.15013  17.33589  39.59381  1.000 41.16203 ? 404 VAL   A O   1 
ATOM   3100 C  CB  . VAL   A 1 404 ? 12.69936  15.87242  37.01211  1.000 41.09149 ? 404 VAL   A CB  1 
ATOM   3101 C  CG1 . VAL   A 1 404 ? 12.62993  14.73111  36.00837  1.000 40.29880 ? 404 VAL   A CG1 1 
ATOM   3102 C  CG2 . VAL   A 1 404 ? 12.05245  17.12516  36.44503  1.000 40.80873 ? 404 VAL   A CG2 1 
ATOM   3103 N  N   . THR   A 1 405 ? 13.30144  16.75229  39.93370  1.000 42.89192 ? 405 THR   A N   1 
ATOM   3104 C  CA  . THR   A 1 405 ? 13.59626  17.84433  40.84739  1.000 44.19941 ? 405 THR   A CA  1 
ATOM   3105 C  C   . THR   A 1 405 ? 15.02623  18.30528  40.59932  1.000 43.47685 ? 405 THR   A C   1 
ATOM   3106 O  O   . THR   A 1 405 ? 15.79095  17.66095  39.87437  1.000 42.58094 ? 405 THR   A O   1 
ATOM   3107 C  CB  . THR   A 1 405 ? 13.39717  17.43018  42.31158  1.000 45.18116 ? 405 THR   A CB  1 
ATOM   3108 O  OG1 . THR   A 1 405 ? 13.48112  18.58644  43.15365  1.000 46.87024 ? 405 THR   A OG1 1 
ATOM   3109 C  CG2 . THR   A 1 405 ? 14.45926  16.43120  42.72722  1.000 46.06367 ? 405 THR   A CG2 1 
ATOM   3110 N  N   . TRP   A 1 406 ? 15.38135  19.43663  41.19933  1.000 43.94385 ? 406 TRP   A N   1 
ATOM   3111 C  CA  . TRP   A 1 406 ? 16.69316  20.04091  40.99285  1.000 44.31663 ? 406 TRP   A CA  1 
ATOM   3112 C  C   . TRP   A 1 406 ? 16.90916  21.09742  42.07141  1.000 44.06530 ? 406 TRP   A C   1 
ATOM   3113 O  O   . TRP   A 1 406 ? 16.01935  21.38510  42.87557  1.000 44.28238 ? 406 TRP   A O   1 
ATOM   3114 C  CB  . TRP   A 1 406 ? 16.80952  20.64338  39.59358  1.000 42.36189 ? 406 TRP   A CB  1 
ATOM   3115 C  CG  . TRP   A 1 406 ? 15.84002  21.75491  39.35388  1.000 44.32836 ? 406 TRP   A CG  1 
ATOM   3116 C  CD1 . TRP   A 1 406 ? 16.06142  23.09086  39.53670  1.000 44.01929 ? 406 TRP   A CD1 1 
ATOM   3117 C  CD2 . TRP   A 1 406 ? 14.48464  21.63059  38.90576  1.000 44.27851 ? 406 TRP   A CD2 1 
ATOM   3118 N  NE1 . TRP   A 1 406 ? 14.93053  23.80449  39.22410  1.000 44.17043 ? 406 TRP   A NE1 1 
ATOM   3119 C  CE2 . TRP   A 1 406 ? 13.94848  22.93186  38.83381  1.000 45.05646 ? 406 TRP   A CE2 1 
ATOM   3120 C  CE3 . TRP   A 1 406 ? 13.67350  20.54639  38.55302  1.000 44.08611 ? 406 TRP   A CE3 1 
ATOM   3121 C  CZ2 . TRP   A 1 406 ? 12.63904  23.17816  38.42407  1.000 46.01107 ? 406 TRP   A CZ2 1 
ATOM   3122 C  CZ3 . TRP   A 1 406 ? 12.37173  20.79404  38.14774  1.000 44.32733 ? 406 TRP   A CZ3 1 
ATOM   3123 C  CH2 . TRP   A 1 406 ? 11.86898  22.09950  38.08571  1.000 45.15304 ? 406 TRP   A CH2 1 
ATOM   3124 N  N   . HIS   A 1 407 ? 18.10216  21.68770  42.06185  1.000 45.01471 ? 407 HIS   A N   1 
ATOM   3125 C  CA  . HIS   A 1 407 ? 18.50133  22.68951  43.05031  1.000 47.65852 ? 407 HIS   A CA  1 
ATOM   3126 C  C   . HIS   A 1 407 ? 17.83452  24.01447  42.70787  1.000 48.94578 ? 407 HIS   A C   1 
ATOM   3127 O  O   . HIS   A 1 407 ? 18.25248  24.71439  41.78259  1.000 48.76258 ? 407 HIS   A O   1 
ATOM   3128 C  CB  . HIS   A 1 407 ? 20.01992  22.82791  43.08166  1.000 47.29465 ? 407 HIS   A CB  1 
ATOM   3129 C  CG  . HIS   A 1 407 ? 20.51561  23.87725  44.02995  1.000 50.76167 ? 407 HIS   A CG  1 
ATOM   3130 N  ND1 . HIS   A 1 407 ? 20.78371  23.61689  45.35724  1.000 47.30267 ? 407 HIS   A ND1 1 
ATOM   3131 C  CD2 . HIS   A 1 407 ? 20.79569  25.18928  43.84067  1.000 48.31242 ? 407 HIS   A CD2 1 
ATOM   3132 C  CE1 . HIS   A 1 407 ? 21.20445  24.72322  45.94491  1.000 46.62310 ? 407 HIS   A CE1 1 
ATOM   3133 N  NE2 . HIS   A 1 407 ? 21.22097  25.69179  45.04683  1.000 46.49362 ? 407 HIS   A NE2 1 
ATOM   3134 N  N   . HIS   A 1 408 ? 16.79808  24.36864  43.46056  1.000 51.22023 ? 408 HIS   A N   1 
ATOM   3135 C  CA  . HIS   A 1 408 ? 16.11278  25.63817  43.25050  1.000 54.62202 ? 408 HIS   A CA  1 
ATOM   3136 C  C   . HIS   A 1 408 ? 16.88941  26.77818  43.90947  1.000 58.23190 ? 408 HIS   A C   1 
ATOM   3137 O  O   . HIS   A 1 408 ? 16.32693  27.59354  44.64390  1.000 63.83575 ? 408 HIS   A O   1 
ATOM   3138 C  CB  . HIS   A 1 408 ? 14.68075  25.57929  43.79203  1.000 57.39282 ? 408 HIS   A CB  1 
ATOM   3139 C  CG  . HIS   A 1 408 ? 13.82604  26.73522  43.36811  1.000 60.28143 ? 408 HIS   A CG  1 
ATOM   3140 N  ND1 . HIS   A 1 408 ? 13.53027  27.79005  44.20530  1.000 63.87662 ? 408 HIS   A ND1 1 
ATOM   3141 C  CD2 . HIS   A 1 408 ? 13.20970  27.00482  42.19274  1.000 58.63915 ? 408 HIS   A CD2 1 
ATOM   3142 C  CE1 . HIS   A 1 408 ? 12.76542  28.65711  43.56559  1.000 62.29050 ? 408 HIS   A CE1 1 
ATOM   3143 N  NE2 . HIS   A 1 408 ? 12.55571  28.20413  42.34268  1.000 59.49160 ? 408 HIS   A NE2 1 
HETATM 3144 C  CHA . HEM   B 2 .   ? 9.65448   6.33794   9.67586   1.000 27.21882 ? 501 HEM   A CHA 1 
HETATM 3145 C  CHB . HEM   B 2 .   ? 11.61155  5.81203   14.08001  1.000 26.10872 ? 501 HEM   A CHB 1 
HETATM 3146 C  CHC . HEM   B 2 .   ? 11.21817  10.60424  14.73511  1.000 27.81119 ? 501 HEM   A CHC 1 
HETATM 3147 C  CHD . HEM   B 2 .   ? 8.60836   10.99707  10.68717  1.000 27.86291 ? 501 HEM   A CHD 1 
HETATM 3148 C  C1A . HEM   B 2 .   ? 10.25031  5.76018   10.77492  1.000 26.69138 ? 501 HEM   A C1A 1 
HETATM 3149 C  C2A . HEM   B 2 .   ? 10.65249  4.37197   10.92769  1.000 27.40928 ? 501 HEM   A C2A 1 
HETATM 3150 C  C3A . HEM   B 2 .   ? 11.18875  4.23248   12.14387  1.000 29.40246 ? 501 HEM   A C3A 1 
HETATM 3151 C  C4A . HEM   B 2 .   ? 11.15406  5.52246   12.81054  1.000 28.80724 ? 501 HEM   A C4A 1 
HETATM 3152 C  CMA . HEM   B 2 .   ? 11.74588  2.91625   12.73236  1.000 29.02719 ? 501 HEM   A CMA 1 
HETATM 3153 C  CAA . HEM   B 2 .   ? 10.49865  3.23509   9.88799   1.000 29.23475 ? 501 HEM   A CAA 1 
HETATM 3154 C  CBA . HEM   B 2 .   ? 9.03686   2.85069   9.67688   1.000 29.66421 ? 501 HEM   A CBA 1 
HETATM 3155 C  CGA . HEM   B 2 .   ? 8.95834   1.68878   8.71706   1.000 30.42787 ? 501 HEM   A CGA 1 
HETATM 3156 O  O1A . HEM   B 2 .   ? 10.02700  1.21354   8.25131   1.000 29.95849 ? 501 HEM   A O1A 1 
HETATM 3157 O  O2A . HEM   B 2 .   ? 7.82618   1.23314   8.41512   1.000 28.95826 ? 501 HEM   A O2A 1 
HETATM 3158 C  C1B . HEM   B 2 .   ? 11.72043  7.07213   14.63067  1.000 29.61759 ? 501 HEM   A C1B 1 
HETATM 3159 C  C2B . HEM   B 2 .   ? 12.37385  7.42346   15.88093  1.000 29.00840 ? 501 HEM   A C2B 1 
HETATM 3160 C  C3B . HEM   B 2 .   ? 12.23517  8.74947   16.05353  1.000 28.03618 ? 501 HEM   A C3B 1 
HETATM 3161 C  C4B . HEM   B 2 .   ? 11.52600  9.27630   14.91435  1.000 29.46534 ? 501 HEM   A C4B 1 
HETATM 3162 C  CMB . HEM   B 2 .   ? 13.05942  6.41194   16.82994  1.000 28.46270 ? 501 HEM   A CMB 1 
HETATM 3163 C  CAB . HEM   B 2 .   ? 12.74720  9.67522   17.18130  1.000 28.62603 ? 501 HEM   A CAB 1 
HETATM 3164 C  CBB . HEM   B 2 .   ? 13.86149  9.42506   17.86656  1.000 31.48472 ? 501 HEM   A CBB 1 
HETATM 3165 C  C1C . HEM   B 2 .   ? 10.48033  11.14485  13.71279  1.000 27.86564 ? 501 HEM   A C1C 1 
HETATM 3166 C  C2C . HEM   B 2 .   ? 10.13491  12.54005  13.56211  1.000 29.53312 ? 501 HEM   A C2C 1 
HETATM 3167 C  C3C . HEM   B 2 .   ? 9.41276   12.67337  12.44519  1.000 28.90348 ? 501 HEM   A C3C 1 
HETATM 3168 C  C4C . HEM   B 2 .   ? 9.27089   11.35052  11.84552  1.000 28.24255 ? 501 HEM   A C4C 1 
HETATM 3169 C  CMC . HEM   B 2 .   ? 10.54103  13.67031  14.53197  1.000 28.94704 ? 501 HEM   A CMC 1 
HETATM 3170 C  CAC . HEM   B 2 .   ? 8.85556   14.02681  11.94709  1.000 28.58215 ? 501 HEM   A CAC 1 
HETATM 3171 C  CBC . HEM   B 2 .   ? 8.19523   14.16473  10.79495  1.000 31.61314 ? 501 HEM   A CBC 1 
HETATM 3172 C  C1D . HEM   B 2 .   ? 8.69535   9.77645   10.04620  1.000 30.35560 ? 501 HEM   A C1D 1 
HETATM 3173 C  C2D . HEM   B 2 .   ? 8.14879   9.45553   8.74251   1.000 29.72056 ? 501 HEM   A C2D 1 
HETATM 3174 C  C3D . HEM   B 2 .   ? 8.43507   8.18041   8.47383   1.000 28.88547 ? 501 HEM   A C3D 1 
HETATM 3175 C  C4D . HEM   B 2 .   ? 9.17897   7.63263   9.58784   1.000 29.67020 ? 501 HEM   A C4D 1 
HETATM 3176 C  CMD . HEM   B 2 .   ? 7.36835   10.41788  7.82161   1.000 28.05352 ? 501 HEM   A CMD 1 
HETATM 3177 C  CAD . HEM   B 2 .   ? 8.05209   7.41082   7.19173   1.000 28.40025 ? 501 HEM   A CAD 1 
HETATM 3178 C  CBD . HEM   B 2 .   ? 9.14381   7.62018   6.14861   1.000 29.40096 ? 501 HEM   A CBD 1 
HETATM 3179 C  CGD . HEM   B 2 .   ? 8.80748   6.83758   4.90744   1.000 28.75520 ? 501 HEM   A CGD 1 
HETATM 3180 O  O1D . HEM   B 2 .   ? 7.92806   5.94734   4.98700   1.000 28.42543 ? 501 HEM   A O1D 1 
HETATM 3181 O  O2D . HEM   B 2 .   ? 9.42035   7.10457   3.84318   1.000 27.36715 ? 501 HEM   A O2D 1 
HETATM 3182 N  NA  . HEM   B 2 .   ? 10.57650  6.42549   11.93960  1.000 28.73391 ? 501 HEM   A NA  1 
HETATM 3183 N  NB  . HEM   B 2 .   ? 11.21772  8.23217   14.06900  1.000 27.45015 ? 501 HEM   A NB  1 
HETATM 3184 N  NC  . HEM   B 2 .   ? 9.93967   10.45420  12.65353  1.000 26.21722 ? 501 HEM   A NC  1 
HETATM 3185 N  ND  . HEM   B 2 .   ? 9.31646   8.63580   10.53010  1.000 25.08805 ? 501 HEM   A ND  1 
HETATM 3186 FE FE  . HEM   B 2 .   ? 10.30998  8.45650   12.27381  1.000 26.50995 ? 501 HEM   A FE  1 
HETATM 3187 C  C1  . DIF   C 3 .   ? -1.59233  4.75411   17.50816  1.000 46.83781 ? 502 DIF   A C1  1 
HETATM 3188 C  C2  . DIF   C 3 .   ? -0.94634  5.60640   16.61262  1.000 46.04958 ? 502 DIF   A C2  1 
HETATM 3189 CL CL2 . DIF   C 3 .   ? -0.67423  7.23540   17.12470  1.000 46.49800 ? 502 DIF   A CL2 1 
HETATM 3190 C  C3  . DIF   C 3 .   ? -0.54201  5.13421   15.35308  1.000 44.73037 ? 502 DIF   A C3  1 
HETATM 3191 C  C4  . DIF   C 3 .   ? -0.80303  3.80281   15.00926  1.000 45.80007 ? 502 DIF   A C4  1 
HETATM 3192 CL CL4 . DIF   C 3 .   ? -0.33283  3.16019   13.47519  1.000 45.88532 ? 502 DIF   A CL4 1 
HETATM 3193 C  C5  . DIF   C 3 .   ? -1.44865  2.95395   15.90767  1.000 46.82741 ? 502 DIF   A C5  1 
HETATM 3194 C  C6  . DIF   C 3 .   ? -1.84428  3.42895   17.15739  1.000 47.50929 ? 502 DIF   A C6  1 
HETATM 3195 N  N1  . DIF   C 3 .   ? 0.10877   5.97779   14.43131  1.000 42.85661 ? 502 DIF   A N1  1 
HETATM 3196 C  C7  . DIF   C 3 .   ? 1.35221   7.90310   13.59929  1.000 38.78057 ? 502 DIF   A C7  1 
HETATM 3197 C  C8  . DIF   C 3 .   ? 1.19630   6.87828   14.53104  1.000 41.61712 ? 502 DIF   A C8  1 
HETATM 3198 C  C9  . DIF   C 3 .   ? 2.11212   6.74955   15.57565  1.000 40.79805 ? 502 DIF   A C9  1 
HETATM 3199 C  C10 . DIF   C 3 .   ? 3.18285   7.63763   15.68050  1.000 40.87935 ? 502 DIF   A C10 1 
HETATM 3200 C  C11 . DIF   C 3 .   ? 3.34277   8.65684   14.74035  1.000 36.34765 ? 502 DIF   A C11 1 
HETATM 3201 C  C12 . DIF   C 3 .   ? 2.42656   8.78662   13.69835  1.000 36.72228 ? 502 DIF   A C12 1 
HETATM 3202 C  C13 . DIF   C 3 .   ? 0.38944   8.05616   12.46801  1.000 37.90680 ? 502 DIF   A C13 1 
HETATM 3203 C  C14 . DIF   C 3 .   ? 0.59680   6.98087   11.42167  1.000 37.98182 ? 502 DIF   A C14 1 
HETATM 3204 O  O1  . DIF   C 3 .   ? 0.05139   7.32565   10.22675  1.000 36.55783 ? 502 DIF   A O1  1 
HETATM 3205 O  O2  . DIF   C 3 .   ? 1.19455   5.92856   11.60701  1.000 38.99896 ? 502 DIF   A O2  1 
HETATM 3206 C  C10 . A1L6Q D 4 .   ? 5.26571   5.06316   14.58685  1.000 39.90409 ? 503 A1L6Q A C10 1 
HETATM 3207 C  C11 . A1L6Q D 4 .   ? 1.93306   1.92080   16.35266  1.000 44.02585 ? 503 A1L6Q A C11 1 
HETATM 3208 C  C7  . A1L6Q D 4 .   ? 3.16288   3.46160   14.75535  1.000 42.38007 ? 503 A1L6Q A C7  1 
HETATM 3209 C  C8  . A1L6Q D 4 .   ? 3.51924   3.58119   13.27230  1.000 41.22724 ? 503 A1L6Q A C8  1 
HETATM 3210 C  C9  . A1L6Q D 4 .   ? 2.59170   2.11322   15.13809  1.000 43.61338 ? 503 A1L6Q A C9  1 
HETATM 3211 C  C12 . A1L6Q D 4 .   ? 2.73787   1.04999   14.24426  1.000 43.26897 ? 503 A1L6Q A C12 1 
HETATM 3212 C  C13 . A1L6Q D 4 .   ? 6.30226   5.86391   14.88257  1.000 36.58826 ? 503 A1L6Q A C13 1 
HETATM 3213 C  C20 . A1L6Q D 4 .   ? 7.18178   8.43703   12.64188  1.000 32.36191 ? 503 A1L6Q A C20 1 
HETATM 3214 C  C14 . A1L6Q D 4 .   ? 1.41962   0.66361   16.67263  1.000 43.62437 ? 503 A1L6Q A C14 1 
HETATM 3215 C  C15 . A1L6Q D 4 .   ? 2.22464   -0.20741  14.56526  1.000 45.20000 ? 503 A1L6Q A C15 1 
HETATM 3216 C  C16 . A1L6Q D 4 .   ? 1.56579   -0.40082  15.78056  1.000 44.00036 ? 503 A1L6Q A C16 1 
HETATM 3217 C  C17 . A1L6Q D 4 .   ? 6.18819   7.73998   13.28627  1.000 32.75510 ? 503 A1L6Q A C17 1 
HETATM 3218 C  C19 . A1L6Q D 4 .   ? 6.89825   5.68762   16.18023  1.000 36.19885 ? 503 A1L6Q A C19 1 
HETATM 3219 C  C18 . A1L6Q D 4 .   ? 8.18458   6.99767   13.84986  1.000 30.88699 ? 503 A1L6Q A C18 1 
HETATM 3220 N  N4  . A1L6Q D 4 .   ? 6.86890   6.85083   14.02161  1.000 31.73124 ? 503 A1L6Q A N4  1 
HETATM 3221 N  N5  . A1L6Q D 4 .   ? 8.41590   7.97368   13.00470  1.000 31.18962 ? 503 A1L6Q A N5  1 
HETATM 3222 N  N6  . A1L6Q D 4 .   ? 7.37302   5.57050   17.23367  1.000 37.63453 ? 503 A1L6Q A N6  1 
HETATM 3223 S  S2  . A1L6Q D 4 .   ? 4.66749   3.88518   15.71738  1.000 41.03830 ? 503 A1L6Q A S2  1 
HETATM 3224 S  S3  . A1L6Q D 4 .   ? 4.43303   5.14017   13.05872  1.000 40.25754 ? 503 A1L6Q A S3  1 
HETATM 3225 CL CL1 . A1L6Q D 4 .   ? 1.73585   3.21641   17.48069  1.000 44.82536 ? 503 A1L6Q A CL1 1 
HETATM 3226 O  O   . HOH   E 5 .   ? -2.42047  2.50230   21.30944  1.000 47.40929 ? 601 HOH   A O   1 
HETATM 3227 O  O   . HOH   E 5 .   ? 2.60709   -23.48723 20.75005  1.000 44.73139 ? 602 HOH   A O   1 
HETATM 3228 O  O   . HOH   E 5 .   ? -8.87451  5.63495   9.57716   1.000 48.64510 ? 603 HOH   A O   1 
HETATM 3229 O  O   . HOH   E 5 .   ? 3.30217   -18.62456 -1.45803  1.000 47.20469 ? 604 HOH   A O   1 
HETATM 3230 O  O   . HOH   E 5 .   ? 8.80802   23.89582  37.19909  1.000 45.30430 ? 605 HOH   A O   1 
HETATM 3231 O  O   . HOH   E 5 .   ? 0.20306   -2.23893  18.41602  1.000 40.06859 ? 606 HOH   A O   1 
HETATM 3232 O  O   . HOH   E 5 .   ? 5.44285   27.80908  9.66061   1.000 37.21655 ? 607 HOH   A O   1 
HETATM 3233 O  O   . HOH   E 5 .   ? 5.88997   1.32335   9.80625   1.000 34.54490 ? 608 HOH   A O   1 
HETATM 3234 O  O   . HOH   E 5 .   ? 9.54585   -14.81051 -4.31048  1.000 40.13186 ? 609 HOH   A O   1 
HETATM 3235 O  O   . HOH   E 5 .   ? 21.33826  0.04933   9.15935   1.000 34.30497 ? 610 HOH   A O   1 
HETATM 3236 O  O   . HOH   E 5 .   ? -14.06626 23.39232  4.73489   1.000 37.22134 ? 611 HOH   A O   1 
HETATM 3237 O  O   . HOH   E 5 .   ? 12.05421  9.49462   -3.72945  1.000 41.14993 ? 612 HOH   A O   1 
HETATM 3238 O  O   . HOH   E 5 .   ? 19.52524  -9.47812  17.55543  1.000 32.88850 ? 613 HOH   A O   1 
HETATM 3239 O  O   . HOH   E 5 .   ? 19.78035  -12.53142 26.59006  1.000 44.70206 ? 614 HOH   A O   1 
HETATM 3240 O  O   . HOH   E 5 .   ? 21.64481  16.07084  36.49686  1.000 41.73372 ? 615 HOH   A O   1 
HETATM 3241 O  O   . HOH   E 5 .   ? -1.56440  -2.98867  24.72160  1.000 41.28904 ? 616 HOH   A O   1 
HETATM 3242 O  O   . HOH   E 5 .   ? 5.65052   -9.03104  -4.82716  1.000 41.39472 ? 617 HOH   A O   1 
HETATM 3243 O  O   . HOH   E 5 .   ? -6.92806  -3.66029  13.04677  1.000 53.80270 ? 618 HOH   A O   1 
HETATM 3244 O  O   . HOH   E 5 .   ? -13.76843 21.32265  7.20917   1.000 41.49823 ? 619 HOH   A O   1 
HETATM 3245 O  O   . HOH   E 5 .   ? -10.25657 8.91635   21.70485  1.000 42.51180 ? 620 HOH   A O   1 
HETATM 3246 O  O   . HOH   E 5 .   ? 14.98837  7.46544   40.75479  1.000 45.24579 ? 621 HOH   A O   1 
HETATM 3247 O  O   . HOH   E 5 .   ? 18.71385  3.79560   4.32846   1.000 28.21908 ? 622 HOH   A O   1 
HETATM 3248 O  O   . HOH   E 5 .   ? 2.61921   27.28817  13.28068  1.000 37.20917 ? 623 HOH   A O   1 
HETATM 3249 O  O   . HOH   E 5 .   ? 5.75096   7.52152   34.89328  1.000 44.21971 ? 624 HOH   A O   1 
HETATM 3250 O  O   . HOH   E 5 .   ? -0.17483  -10.79996 10.07114  1.000 42.71441 ? 625 HOH   A O   1 
HETATM 3251 O  O   . HOH   E 5 .   ? 10.76590  -1.45359  3.71667   1.000 29.94203 ? 626 HOH   A O   1 
HETATM 3252 O  O   . HOH   E 5 .   ? 19.38031  17.75047  42.93941  1.000 47.38451 ? 627 HOH   A O   1 
HETATM 3253 O  O   . HOH   E 5 .   ? 17.19901  22.58453  2.00006   1.000 41.48724 ? 628 HOH   A O   1 
HETATM 3254 O  O   . HOH   E 5 .   ? 16.44558  -6.96476  0.21403   1.000 30.69343 ? 629 HOH   A O   1 
HETATM 3255 O  O   . HOH   E 5 .   ? 24.80973  -5.82946  9.77924   1.000 40.32795 ? 630 HOH   A O   1 
HETATM 3256 O  O   . HOH   E 5 .   ? 12.36285  0.72563   4.26585   1.000 27.00123 ? 631 HOH   A O   1 
HETATM 3257 O  O   . HOH   E 5 .   ? 15.80880  26.06056  8.43054   1.000 41.45487 ? 632 HOH   A O   1 
HETATM 3258 O  O   . HOH   E 5 .   ? -4.15239  6.05054   7.43104   1.000 41.12295 ? 633 HOH   A O   1 
HETATM 3259 O  O   . HOH   E 5 .   ? 19.61095  2.15941   8.75728   1.000 26.96743 ? 634 HOH   A O   1 
HETATM 3260 O  O   . HOH   E 5 .   ? 11.57229  16.65866  23.93078  1.000 31.30909 ? 635 HOH   A O   1 
HETATM 3261 O  O   . HOH   E 5 .   ? 8.00754   24.61354  30.70086  1.000 39.71601 ? 636 HOH   A O   1 
HETATM 3262 O  O   . HOH   E 5 .   ? 10.15094  24.43416  13.20770  1.000 36.84329 ? 637 HOH   A O   1 
HETATM 3263 O  O   . HOH   E 5 .   ? 7.09152   -11.10125 22.74516  1.000 37.92167 ? 638 HOH   A O   1 
HETATM 3264 O  O   . HOH   E 5 .   ? 1.16339   -0.90118  -1.77368  1.000 35.33134 ? 639 HOH   A O   1 
HETATM 3265 O  O   . HOH   E 5 .   ? 9.54651   18.29746  16.35487  1.000 29.57577 ? 640 HOH   A O   1 
HETATM 3266 O  O   . HOH   E 5 .   ? 18.27260  3.51102   11.54561  1.000 26.82757 ? 641 HOH   A O   1 
HETATM 3267 O  O   . HOH   E 5 .   ? -1.54976  8.99602   9.02614   1.000 34.29921 ? 642 HOH   A O   1 
HETATM 3268 O  O   . HOH   E 5 .   ? 17.04544  5.66038   2.62527   1.000 30.70015 ? 643 HOH   A O   1 
HETATM 3269 O  O   . HOH   E 5 .   ? 20.59709  16.45678  12.76956  1.000 30.88446 ? 644 HOH   A O   1 
HETATM 3270 O  O   . HOH   E 5 .   ? 0.79572   12.70370  -7.61026  1.000 38.90042 ? 645 HOH   A O   1 
HETATM 3271 O  O   . HOH   E 5 .   ? 23.84671  11.75703  16.46020  1.000 32.19305 ? 646 HOH   A O   1 
HETATM 3272 O  O   . HOH   E 5 .   ? -11.65193 30.48636  5.46649   1.000 41.65454 ? 647 HOH   A O   1 
HETATM 3273 O  O   . HOH   E 5 .   ? 7.39297   -0.09294  0.68402   1.000 29.60812 ? 648 HOH   A O   1 
HETATM 3274 O  O   . HOH   E 5 .   ? -6.64941  31.18353  -2.34768  1.000 33.11072 ? 649 HOH   A O   1 
HETATM 3275 O  O   . HOH   E 5 .   ? 0.72199   14.81353  22.75913  1.000 36.07113 ? 650 HOH   A O   1 
HETATM 3276 O  O   . HOH   E 5 .   ? -9.890    10.474    -0.382    1.000 36.05246 ? 651 HOH   A O   1 
HETATM 3277 O  O   . HOH   E 5 .   ? 6.90558   1.44822   5.96671   1.000 29.19994 ? 652 HOH   A O   1 
HETATM 3278 O  O   . HOH   E 5 .   ? 5.46476   -6.00199  -2.17521  1.000 35.76179 ? 653 HOH   A O   1 
HETATM 3279 O  O   . HOH   E 5 .   ? 7.26532   -1.39958  26.79860  1.000 36.57767 ? 654 HOH   A O   1 
HETATM 3280 O  O   . HOH   E 5 .   ? 6.77430   24.41350  33.25764  1.000 43.90201 ? 655 HOH   A O   1 
HETATM 3281 O  O   . HOH   E 5 .   ? 1.38606   21.79223  26.07941  1.000 41.89575 ? 656 HOH   A O   1 
HETATM 3282 O  O   . HOH   E 5 .   ? -9.28217  23.49765  12.00158  1.000 35.05829 ? 657 HOH   A O   1 
HETATM 3283 O  O   . HOH   E 5 .   ? 5.74076   0.41123   34.04539  1.000 43.05557 ? 658 HOH   A O   1 
HETATM 3284 O  O   . HOH   E 5 .   ? -0.31672  -8.28658  18.85879  1.000 38.57476 ? 659 HOH   A O   1 
HETATM 3285 O  O   . HOH   E 5 .   ? -7.37543  11.00054  5.95282   1.000 35.27743 ? 660 HOH   A O   1 
HETATM 3286 O  O   . HOH   E 5 .   ? 8.72099   -10.51544 28.37587  1.000 38.80114 ? 661 HOH   A O   1 
HETATM 3287 O  O   . HOH   E 5 .   ? 23.15803  -10.02446 12.14028  1.000 38.14706 ? 662 HOH   A O   1 
HETATM 3288 O  O   . HOH   E 5 .   ? 30.27232  12.38755  19.40137  1.000 36.42277 ? 663 HOH   A O   1 
HETATM 3289 O  O   . HOH   E 5 .   ? 23.34870  -12.57676 16.99527  1.000 47.35510 ? 664 HOH   A O   1 
HETATM 3290 O  O   . HOH   E 5 .   ? 15.33704  -11.03511 1.19446   1.000 38.15401 ? 665 HOH   A O   1 
HETATM 3291 O  O   . HOH   E 5 .   ? 21.92746  3.49028   10.92317  1.000 32.18800 ? 666 HOH   A O   1 
HETATM 3292 O  O   . HOH   E 5 .   ? 8.38450   -3.49653  23.93649  1.000 34.21354 ? 667 HOH   A O   1 
HETATM 3293 O  O   . HOH   E 5 .   ? 15.09204  15.73927  2.76206   1.000 34.53421 ? 668 HOH   A O   1 
HETATM 3294 O  O   . HOH   E 5 .   ? -0.21789  -19.50546 17.75059  1.000 44.47463 ? 669 HOH   A O   1 
HETATM 3295 O  O   . HOH   E 5 .   ? -1.52792  6.97047   7.01329   1.000 36.04028 ? 670 HOH   A O   1 
HETATM 3296 O  O   . HOH   E 5 .   ? 14.96145  14.99519  9.06905   1.000 30.72049 ? 671 HOH   A O   1 
HETATM 3297 O  O   . HOH   E 5 .   ? 12.71736  -4.22846  30.22600  1.000 39.00612 ? 672 HOH   A O   1 
HETATM 3298 O  O   . HOH   E 5 .   ? 7.40641   1.16063   19.92020  1.000 33.12438 ? 673 HOH   A O   1 
HETATM 3299 O  O   . HOH   E 5 .   ? 21.95497  19.65203  9.51583   1.000 39.31119 ? 674 HOH   A O   1 
HETATM 3300 O  O   . HOH   E 5 .   ? 4.82481   -19.98974 7.94145   1.000 42.74541 ? 675 HOH   A O   1 
HETATM 3301 O  O   . HOH   E 5 .   ? -3.81725  30.84149  6.61992   1.000 40.05285 ? 676 HOH   A O   1 
HETATM 3302 O  O   . HOH   E 5 .   ? 1.61364   10.66680  1.81429   1.000 30.92858 ? 677 HOH   A O   1 
HETATM 3303 O  O   . HOH   E 5 .   ? 29.88336  7.23178   13.59082  1.000 44.28898 ? 678 HOH   A O   1 
HETATM 3304 O  O   . HOH   E 5 .   ? -0.80841  28.46151  10.36605  1.000 36.21011 ? 679 HOH   A O   1 
HETATM 3305 O  O   . HOH   E 5 .   ? -8.33009  16.48958  21.92137  1.000 42.87473 ? 680 HOH   A O   1 
HETATM 3306 O  O   . HOH   E 5 .   ? 21.25575  -11.46257 10.03383  1.000 40.36700 ? 681 HOH   A O   1 
HETATM 3307 O  O   . HOH   E 5 .   ? -6.80254  16.56363  -5.20892  1.000 35.12847 ? 682 HOH   A O   1 
HETATM 3308 O  O   . HOH   E 5 .   ? 4.52439   -0.92336  9.12830   1.000 34.34567 ? 683 HOH   A O   1 
HETATM 3309 O  O   . HOH   E 5 .   ? 1.64919   1.73614   -2.79621  1.000 36.58388 ? 684 HOH   A O   1 
HETATM 3310 O  O   . HOH   E 5 .   ? 10.96184  -3.24538  23.70645  1.000 34.09885 ? 685 HOH   A O   1 
HETATM 3311 O  O   . HOH   E 5 .   ? 15.34214  9.49618   5.58968   1.000 31.02867 ? 686 HOH   A O   1 
HETATM 3312 O  O   . HOH   E 5 .   ? 25.03295  -3.87711  6.54236   1.000 40.23184 ? 687 HOH   A O   1 
HETATM 3313 O  O   . HOH   E 5 .   ? -1.16547  27.78779  1.45683   1.000 34.10716 ? 688 HOH   A O   1 
HETATM 3314 O  O   . HOH   E 5 .   ? 8.26692   -1.92250  2.68528   1.000 29.44296 ? 689 HOH   A O   1 
HETATM 3315 O  O   . HOH   E 5 .   ? -7.36853  9.49871   -0.89339  1.000 35.05990 ? 690 HOH   A O   1 
HETATM 3316 O  O   . HOH   E 5 .   ? -4.157    -2.299    -1.187    1.000 45.60015 ? 691 HOH   A O   1 
HETATM 3317 O  O   . HOH   E 5 .   ? 23.80738  -11.37195 20.39281  1.000 43.46292 ? 692 HOH   A O   1 
HETATM 3318 O  O   . HOH   E 5 .   ? 12.59918  1.49100   7.28858   1.000 28.99441 ? 693 HOH   A O   1 
HETATM 3319 O  O   . HOH   E 5 .   ? 2.27619   28.43445  15.77726  1.000 39.21279 ? 694 HOH   A O   1 
HETATM 3320 O  O   . HOH   E 5 .   ? 7.85870   7.33653   -7.46546  1.000 36.06220 ? 695 HOH   A O   1 
HETATM 3321 O  O   . HOH   E 5 .   ? 5.71877   14.19852  -6.19013  1.000 34.81769 ? 696 HOH   A O   1 
HETATM 3322 O  O   . HOH   E 5 .   ? 25.79029  -9.61863  11.75287  1.000 39.38549 ? 697 HOH   A O   1 
HETATM 3323 O  O   . HOH   E 5 .   ? 3.11148   -26.61867 25.87047  1.000 49.83771 ? 698 HOH   A O   1 
HETATM 3324 O  O   . HOH   E 5 .   ? 19.76887  -12.72833 5.94919   1.000 42.51920 ? 699 HOH   A O   1 
HETATM 3325 O  O   . HOH   E 5 .   ? -2.84915  7.14646   -0.07925  1.000 36.99383 ? 700 HOH   A O   1 
HETATM 3326 O  O   . HOH   E 5 .   ? 7.44124   -2.88224  -2.19206  1.000 36.27084 ? 701 HOH   A O   1 
HETATM 3327 O  O   . HOH   E 5 .   ? 23.13161  18.74952  16.22127  1.000 38.74198 ? 702 HOH   A O   1 
HETATM 3328 O  O   . HOH   E 5 .   ? 14.38137  -1.40431  -1.59535  1.000 31.97673 ? 703 HOH   A O   1 
HETATM 3329 O  O   . HOH   E 5 .   ? 19.02890  -16.30967 2.95328   1.000 48.22698 ? 704 HOH   A O   1 
HETATM 3330 O  O   . HOH   E 5 .   ? -0.52180  9.64231   0.76015   1.000 32.79349 ? 705 HOH   A O   1 
HETATM 3331 O  O   . HOH   E 5 .   ? 17.64880  -1.65501  21.61376  1.000 28.86985 ? 706 HOH   A O   1 
HETATM 3332 O  O   . HOH   E 5 .   ? 21.57694  23.24933  23.88309  1.000 35.32330 ? 707 HOH   A O   1 
HETATM 3333 O  O   . HOH   E 5 .   ? 22.76940  23.13288  21.48482  1.000 39.94814 ? 708 HOH   A O   1 
HETATM 3334 O  O   . HOH   E 5 .   ? -9.03778  15.62910  -2.99396  1.000 31.90564 ? 709 HOH   A O   1 
HETATM 3335 O  O   . HOH   E 5 .   ? 9.96140   18.25798  -0.96540  1.000 33.68271 ? 710 HOH   A O   1 
HETATM 3336 O  O   . HOH   E 5 .   ? 7.51306   1.95494   27.25815  1.000 34.57524 ? 711 HOH   A O   1 
HETATM 3337 O  O   . HOH   E 5 .   ? 11.27963  -0.40559  10.15920  1.000 30.28426 ? 712 HOH   A O   1 
HETATM 3338 O  O   . HOH   E 5 .   ? 21.48561  17.50339  33.88641  1.000 39.42632 ? 713 HOH   A O   1 
HETATM 3339 O  O   . HOH   E 5 .   ? -5.82737  23.70925  -2.54082  1.000 29.55498 ? 714 HOH   A O   1 
HETATM 3340 O  O   . HOH   E 5 .   ? 3.10588   1.48512   10.87391  1.000 42.20084 ? 715 HOH   A O   1 
HETATM 3341 O  O   . HOH   E 5 .   ? 22.57376  24.99826  26.25908  1.000 43.48610 ? 716 HOH   A O   1 
HETATM 3342 O  O   . HOH   E 5 .   ? -3.10067  15.62803  -10.79406 1.000 41.74376 ? 717 HOH   A O   1 
HETATM 3343 O  O   . HOH   E 5 .   ? 23.52965  -2.45082  2.88440   1.000 33.61444 ? 718 HOH   A O   1 
HETATM 3344 O  O   . HOH   E 5 .   ? -7.924    19.068    -5.322    1.000 31.97096 ? 719 HOH   A O   1 
HETATM 3345 O  O   . HOH   E 5 .   ? 5.287     32.296    9.935     1.000 42.61260 ? 720 HOH   A O   1 
HETATM 3346 O  O   . HOH   E 5 .   ? 12.06992  -1.58969  12.35749  1.000 31.28771 ? 721 HOH   A O   1 
HETATM 3347 O  O   . HOH   E 5 .   ? -1.331    20.256    -13.092   1.000 33.88980 ? 722 HOH   A O   1 
HETATM 3348 O  O   . HOH   E 5 .   ? -0.40759  17.89203  -12.62062 1.000 39.15438 ? 723 HOH   A O   1 
HETATM 3349 O  O   . HOH   E 5 .   ? 13.15691  2.57763   17.14084  1.000 28.88715 ? 724 HOH   A O   1 
HETATM 3350 O  O   . HOH   E 5 .   ? 14.52061  22.53983  0.92391   1.000 39.62350 ? 725 HOH   A O   1 
HETATM 3351 O  O   . HOH   E 5 .   ? 4.05390   27.32196  2.83824   1.000 34.61657 ? 726 HOH   A O   1 
HETATM 3352 O  O   . HOH   E 5 .   ? -7.58773  24.97487  20.17776  1.000 41.70930 ? 727 HOH   A O   1 
HETATM 3353 O  O   . HOH   E 5 .   ? 27.49496  19.14489  21.50210  1.000 37.23908 ? 728 HOH   A O   1 
HETATM 3354 O  O   . HOH   E 5 .   ? 8.24260   24.95379  7.03628   1.000 38.38352 ? 729 HOH   A O   1 
HETATM 3355 O  O   . HOH   E 5 .   ? 3.73480   -3.83480  -3.16520  1.000 42.65804 ? 730 HOH   A O   1 
HETATM 3356 O  O   . HOH   E 5 .   ? 13.96783  -0.23101  1.00576   1.000 29.97254 ? 731 HOH   A O   1 
HETATM 3357 O  O   . HOH   E 5 .   ? 15.29870  -18.30671 28.93541  1.000 49.01580 ? 732 HOH   A O   1 
HETATM 3358 O  O   . HOH   E 5 .   ? 17.72831  -17.02538 0.54176   1.000 47.64682 ? 733 HOH   A O   1 
HETATM 3359 O  O   . HOH   E 5 .   ? -3.25438  28.03335  -0.48217  1.000 31.10672 ? 734 HOH   A O   1 
HETATM 3360 O  O   . HOH   E 5 .   ? 1.58797   8.19803   -7.11180  1.000 37.57075 ? 735 HOH   A O   1 
HETATM 3361 O  O   . HOH   E 5 .   ? 3.58933   0.66505   7.19261   1.000 34.04125 ? 736 HOH   A O   1 
HETATM 3362 O  O   . HOH   E 5 .   ? -0.83432  29.98855  16.95956  1.000 37.19258 ? 737 HOH   A O   1 
HETATM 3363 O  O   . HOH   E 5 .   ? -0.48800  -11.20913 21.39418  1.000 39.93611 ? 738 HOH   A O   1 
HETATM 3364 O  O   . HOH   E 5 .   ? 10.24316  -4.33109  3.68810   1.000 31.46760 ? 739 HOH   A O   1 
HETATM 3365 O  O   . HOH   E 5 .   ? 29.70969  -1.37179  19.31573  1.000 38.55470 ? 740 HOH   A O   1 
HETATM 3366 O  O   . HOH   E 5 .   ? 3.19661   25.67465  -2.54186  1.000 36.33764 ? 741 HOH   A O   1 
HETATM 3367 O  O   . HOH   E 5 .   ? 13.960    6.859     0.887     1.000 35.50137 ? 742 HOH   A O   1 
HETATM 3368 O  O   . HOH   E 5 .   ? -6.36245  23.97757  21.88803  1.000 40.14570 ? 743 HOH   A O   1 
HETATM 3369 O  O   . HOH   E 5 .   ? 32.41611  0.35423   19.46233  1.000 42.59716 ? 744 HOH   A O   1 
HETATM 3370 O  O   . HOH   E 5 .   ? 24.36191  -0.50188  30.91481  1.000 37.83389 ? 745 HOH   A O   1 
HETATM 3371 O  O   . HOH   E 5 .   ? 1.25335   -18.44706 0.39142   1.000 42.86673 ? 746 HOH   A O   1 
HETATM 3372 O  O   . HOH   E 5 .   ? 11.21460  -2.76622  0.61308   1.000 33.00770 ? 747 HOH   A O   1 
HETATM 3373 O  O   . HOH   E 5 .   ? 18.18037  10.83762  39.47928  1.000 40.89174 ? 748 HOH   A O   1 
HETATM 3374 O  O   . HOH   E 5 .   ? 27.57440  4.78656   35.34086  1.000 43.40041 ? 749 HOH   A O   1 
HETATM 3375 O  O   . HOH   E 5 .   ? 4.66019   19.77148  36.34627  1.000 44.60627 ? 750 HOH   A O   1 
HETATM 3376 O  O   . HOH   E 5 .   ? -3.82011  25.47469  23.39430  1.000 42.16305 ? 751 HOH   A O   1 
HETATM 3377 O  O   . HOH   E 5 .   ? 0.92025   -22.76715 19.15869  1.000 43.77337 ? 752 HOH   A O   1 
HETATM 3378 O  O   . HOH   E 5 .   ? 25.70938  -7.17305  26.67652  1.000 39.24117 ? 753 HOH   A O   1 
HETATM 3379 O  O   . HOH   E 5 .   ? 10.36835  -7.81053  31.09003  1.000 42.42036 ? 754 HOH   A O   1 
HETATM 3380 O  O   . HOH   E 5 .   ? 20.25978  5.66612   11.15944  1.000 27.36694 ? 755 HOH   A O   1 
HETATM 3381 O  O   . HOH   E 5 .   ? 0.42426   -4.86528  -0.56135  1.000 36.22487 ? 756 HOH   A O   1 
HETATM 3382 O  O   . HOH   E 5 .   ? 15.13248  5.15520   19.67554  1.000 28.14547 ? 757 HOH   A O   1 
HETATM 3383 O  O   . HOH   E 5 .   ? 9.98549   5.06348   -3.46895  1.000 32.76602 ? 758 HOH   A O   1 
HETATM 3384 O  O   . HOH   E 5 .   ? -11.624   14.773    -1.617    1.000 36.51068 ? 759 HOH   A O   1 
HETATM 3385 O  O   . HOH   E 5 .   ? -11.37543 -2.68868  19.99598  1.000 47.76184 ? 760 HOH   A O   1 
HETATM 3386 O  O   . HOH   E 5 .   ? 5.22184   -16.24344 -4.49684  1.000 41.10801 ? 761 HOH   A O   1 
HETATM 3387 O  O   . HOH   E 5 .   ? -13.23007 -0.53468  20.49862  1.000 52.34322 ? 762 HOH   A O   1 
HETATM 3388 O  O   . HOH   E 5 .   ? 22.12304  -4.25941  3.97703   1.000 34.46280 ? 763 HOH   A O   1 
HETATM 3389 O  O   . HOH   E 5 .   ? -3.99733  8.19128   9.18715   1.000 38.93913 ? 764 HOH   A O   1 
HETATM 3390 O  O   . HOH   E 5 .   ? -6.70935  -6.84113  1.57695   1.000 48.81268 ? 765 HOH   A O   1 
HETATM 3391 O  O   . HOH   E 5 .   ? 7.06931   -1.85514  -5.06940  1.000 41.31139 ? 766 HOH   A O   1 
HETATM 3392 O  O   . HOH   E 5 .   ? 21.86135  -16.20497 14.92475  1.000 46.10792 ? 767 HOH   A O   1 
HETATM 3393 O  O   . HOH   E 5 .   ? 23.53115  -11.11362 23.06681  1.000 44.37766 ? 768 HOH   A O   1 
HETATM 3394 O  O   . HOH   E 5 .   ? -0.61556  7.90980   -6.14102  1.000 38.44918 ? 769 HOH   A O   1 
HETATM 3395 O  O   . HOH   E 5 .   ? 1.15756   29.20895  0.13751   1.000 37.50598 ? 770 HOH   A O   1 
HETATM 3396 O  O   . HOH   E 5 .   ? 16.73861  8.34589   3.20041   1.000 35.66230 ? 771 HOH   A O   1 
HETATM 3397 O  O   . HOH   E 5 .   ? 15.76803  -0.11492  35.15784  1.000 34.81065 ? 772 HOH   A O   1 
HETATM 3398 O  O   . HOH   E 5 .   ? 22.19864  -11.94712 27.54513  1.000 47.94505 ? 773 HOH   A O   1 
HETATM 3399 O  O   . HOH   E 5 .   ? 26.18605  -5.99695  29.33196  1.000 47.02099 ? 774 HOH   A O   1 
HETATM 3400 O  O   . HOH   E 5 .   ? 3.28833   -0.86257  11.26082  1.000 38.62670 ? 775 HOH   A O   1 
HETATM 3401 O  O   . HOH   E 5 .   ? 3.47018   -8.24641  -6.06604  1.000 50.58548 ? 776 HOH   A O   1 
HETATM 3402 O  O   . HOH   E 5 .   ? -2.186    -2.198    -3.211    1.000 44.07560 ? 777 HOH   A O   1 
HETATM 3403 O  O   . HOH   E 5 .   ? -8.64760  22.92502  23.51188  1.000 41.32866 ? 778 HOH   A O   1 
HETATM 3404 O  O   . HOH   E 5 .   ? 2.73697   26.78664  -4.70370  1.000 37.71709 ? 779 HOH   A O   1 
HETATM 3405 O  O   . HOH   E 5 .   ? 23.29225  -12.03903 7.75661   1.000 43.06080 ? 780 HOH   A O   1 
HETATM 3406 O  O   . HOH   E 5 .   ? -7.977    5.125     0.589     1.000 41.90860 ? 781 HOH   A O   1 
HETATM 3407 O  O   . HOH   E 5 .   ? 17.17390  7.93978   38.91633  1.000 40.68696 ? 782 HOH   A O   1 
HETATM 3408 O  O   . HOH   E 5 .   ? 17.39438  25.64203  2.29017   1.000 44.96134 ? 783 HOH   A O   1 
HETATM 3409 O  O   . HOH   E 5 .   ? 22.07003  18.15167  14.25546  1.000 37.58539 ? 784 HOH   A O   1 
HETATM 3410 O  O   . HOH   E 5 .   ? -10.33465 6.03539   1.68931   1.000 45.30549 ? 785 HOH   A O   1 
HETATM 3411 O  O   . HOH   E 5 .   ? -1.17592  2.63380   -2.87105  1.000 39.03028 ? 786 HOH   A O   1 
HETATM 3412 O  O   . HOH   E 5 .   ? 3.24846   27.93523  -0.44152  1.000 37.03065 ? 787 HOH   A O   1 
HETATM 3413 O  O   . HOH   E 5 .   ? 0.42353   29.44421  12.01479  1.000 37.94232 ? 788 HOH   A O   1 
HETATM 3414 O  O   . HOH   E 5 .   ? -14.73209 25.44978  6.48188   1.000 40.36827 ? 789 HOH   A O   1 
HETATM 3415 O  O   . HOH   E 5 .   ? 24.29808  16.52425  17.05865  1.000 42.15917 ? 790 HOH   A O   1 
HETATM 3416 O  O   . HOH   E 5 .   ? 28.78844  21.53123  21.94411  1.000 42.47533 ? 791 HOH   A O   1 
HETATM 3417 O  O   . HOH   E 5 .   ? -9.32027  8.10894   24.51616  1.000 44.99513 ? 792 HOH   A O   1 
HETATM 3418 O  O   . HOH   E 5 .   ? -11.13624 8.94553   1.35676   1.000 37.40655 ? 793 HOH   A O   1 
HETATM 3419 O  O   . HOH   E 5 .   ? 26.48805  -3.51372  9.59456   1.000 41.78582 ? 794 HOH   A O   1 
HETATM 3420 O  O   . HOH   E 5 .   ? -10.77411 -4.06600  22.47836  1.000 51.55541 ? 795 HOH   A O   1 
HETATM 3421 O  O   . HOH   E 5 .   ? 26.29056  -3.55182  3.00553   1.000 34.25543 ? 796 HOH   A O   1 
HETATM 3422 O  O   . HOH   E 5 .   ? 28.16259  -3.15294  7.70896   1.000 42.55917 ? 797 HOH   A O   1 
HETATM 3423 O  O   . HOH   E 5 .   ? 11.85611  -0.98025  -2.44200  1.000 33.74586 ? 798 HOH   A O   1 
HETATM 3424 O  O   . HOH   E 5 .   ? 9.71321   -1.57029  -0.81116  1.000 31.62094 ? 799 HOH   A O   1 
HETATM 3425 O  O   . HOH   E 5 .   ? 24.294    21.793    3.238     1.000 37.95844 ? 800 HOH   A O   1 
HETATM 3426 O  O   . HOH   E 5 .   ? 22.58341  14.80755  12.43362  1.000 36.97241 ? 801 HOH   A O   1 
HETATM 3427 O  O   . HOH   E 5 .   ? 18.10104  -3.43738  35.93285  1.000 43.20501 ? 802 HOH   A O   1 
HETATM 3428 O  O   . HOH   E 5 .   ? 15.52668  -3.20679  36.54118  1.000 45.97760 ? 803 HOH   A O   1 
HETATM 3429 O  O   . HOH   E 5 .   ? 26.03932  15.90789  14.92321  1.000 40.30917 ? 804 HOH   A O   1 
# 
