data_8R4H
# 
_entry.id   8R4H 
# 
_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   8R4H         pdb_00008r4h 10.2210/pdb8r4h/pdb 
WWPDB D_1292134626 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8R4H 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'native form' 
_pdbx_database_related.db_id          8R4F 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              pleone@imm.cnrs.fr 
_pdbx_contact_author.name_first         Philippe 
_pdbx_contact_author.name_last          Leone 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0425-5775 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Leone, P.'    1 ? 
'Contaldo, U.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of the copper efflux oxidase (CueO) from Hafnia alvei deleted of the Met-rich domain' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Leone, P.'    1 ? 
primary 'Contaldo, U.' 2 ? 
# 
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 'Copper efflux oxidase,Multicopper oxidase' 49844.332 2   ? ? ? ? 
2 non-polymer syn 'COPPER (II) ION'                           63.546    8   ? ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                              62.068    12  ? ? ? ? 
4 water       nat water                                       18.015    143 ? ? ? ? 
# 
_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       
;AEHPTLPIPALLTPDAAGKIALNVQTGSMKWKAGMQTPTWGINGPLLGPAMRLQRGKDVAINVTNALPEATTMHWHGMEI
PGTSDGGPQAVIEPGKMWTAEIKVDQPATTAWFHPHTHGLTGRQVAMGLGGLIIIDDEESTKLPLPKEWGVDDVPVILQD
KRLDAKGHIDYQLDIITAAVGWFGDMMLTNGTVYPQHLAPRGWLRLRFLNGCNARSLNLATSDGRPLYVVGSDGGLLGEP
VKLTELPILMGERFEVLVDTRDGKAFDIITLPVKQMGMTLPPFDRALPVLHIQPTLKSNEAKLPDALVNMPAVPAADNVK
TRWLQLMMDGGGNKINGIAFDMAKPMFDVKRGTYEKWTISGEGDMMLHPFHIHGTQFRILSENGKPPAAHRSGWKDTVRV
EGWRSEVLVKFDHEAPKERAYMAHCHLLEHEDTGMMMSFTVSSAWSHPQFEK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AEHPTLPIPALLTPDAAGKIALNVQTGSMKWKAGMQTPTWGINGPLLGPAMRLQRGKDVAINVTNALPEATTMHWHGMEI
PGTSDGGPQAVIEPGKMWTAEIKVDQPATTAWFHPHTHGLTGRQVAMGLGGLIIIDDEESTKLPLPKEWGVDDVPVILQD
KRLDAKGHIDYQLDIITAAVGWFGDMMLTNGTVYPQHLAPRGWLRLRFLNGCNARSLNLATSDGRPLYVVGSDGGLLGEP
VKLTELPILMGERFEVLVDTRDGKAFDIITLPVKQMGMTLPPFDRALPVLHIQPTLKSNEAKLPDALVNMPAVPAADNVK
TRWLQLMMDGGGNKINGIAFDMAKPMFDVKRGTYEKWTISGEGDMMLHPFHIHGTQFRILSENGKPPAAHRSGWKDTVRV
EGWRSEVLVKFDHEAPKERAYMAHCHLLEHEDTGMMMSFTVSSAWSHPQFEK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COPPER (II) ION' CU  
3 1,2-ETHANEDIOL    EDO 
4 water             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   GLU n 
1 3   HIS n 
1 4   PRO n 
1 5   THR n 
1 6   LEU n 
1 7   PRO n 
1 8   ILE n 
1 9   PRO n 
1 10  ALA n 
1 11  LEU n 
1 12  LEU n 
1 13  THR n 
1 14  PRO n 
1 15  ASP n 
1 16  ALA n 
1 17  ALA n 
1 18  GLY n 
1 19  LYS n 
1 20  ILE n 
1 21  ALA n 
1 22  LEU n 
1 23  ASN n 
1 24  VAL n 
1 25  GLN n 
1 26  THR n 
1 27  GLY n 
1 28  SER n 
1 29  MET n 
1 30  LYS n 
1 31  TRP n 
1 32  LYS n 
1 33  ALA n 
1 34  GLY n 
1 35  MET n 
1 36  GLN n 
1 37  THR n 
1 38  PRO n 
1 39  THR n 
1 40  TRP n 
1 41  GLY n 
1 42  ILE n 
1 43  ASN n 
1 44  GLY n 
1 45  PRO n 
1 46  LEU n 
1 47  LEU n 
1 48  GLY n 
1 49  PRO n 
1 50  ALA n 
1 51  MET n 
1 52  ARG n 
1 53  LEU n 
1 54  GLN n 
1 55  ARG n 
1 56  GLY n 
1 57  LYS n 
1 58  ASP n 
1 59  VAL n 
1 60  ALA n 
1 61  ILE n 
1 62  ASN n 
1 63  VAL n 
1 64  THR n 
1 65  ASN n 
1 66  ALA n 
1 67  LEU n 
1 68  PRO n 
1 69  GLU n 
1 70  ALA n 
1 71  THR n 
1 72  THR n 
1 73  MET n 
1 74  HIS n 
1 75  TRP n 
1 76  HIS n 
1 77  GLY n 
1 78  MET n 
1 79  GLU n 
1 80  ILE n 
1 81  PRO n 
1 82  GLY n 
1 83  THR n 
1 84  SER n 
1 85  ASP n 
1 86  GLY n 
1 87  GLY n 
1 88  PRO n 
1 89  GLN n 
1 90  ALA n 
1 91  VAL n 
1 92  ILE n 
1 93  GLU n 
1 94  PRO n 
1 95  GLY n 
1 96  LYS n 
1 97  MET n 
1 98  TRP n 
1 99  THR n 
1 100 ALA n 
1 101 GLU n 
1 102 ILE n 
1 103 LYS n 
1 104 VAL n 
1 105 ASP n 
1 106 GLN n 
1 107 PRO n 
1 108 ALA n 
1 109 THR n 
1 110 THR n 
1 111 ALA n 
1 112 TRP n 
1 113 PHE n 
1 114 HIS n 
1 115 PRO n 
1 116 HIS n 
1 117 THR n 
1 118 HIS n 
1 119 GLY n 
1 120 LEU n 
1 121 THR n 
1 122 GLY n 
1 123 ARG n 
1 124 GLN n 
1 125 VAL n 
1 126 ALA n 
1 127 MET n 
1 128 GLY n 
1 129 LEU n 
1 130 GLY n 
1 131 GLY n 
1 132 LEU n 
1 133 ILE n 
1 134 ILE n 
1 135 ILE n 
1 136 ASP n 
1 137 ASP n 
1 138 GLU n 
1 139 GLU n 
1 140 SER n 
1 141 THR n 
1 142 LYS n 
1 143 LEU n 
1 144 PRO n 
1 145 LEU n 
1 146 PRO n 
1 147 LYS n 
1 148 GLU n 
1 149 TRP n 
1 150 GLY n 
1 151 VAL n 
1 152 ASP n 
1 153 ASP n 
1 154 VAL n 
1 155 PRO n 
1 156 VAL n 
1 157 ILE n 
1 158 LEU n 
1 159 GLN n 
1 160 ASP n 
1 161 LYS n 
1 162 ARG n 
1 163 LEU n 
1 164 ASP n 
1 165 ALA n 
1 166 LYS n 
1 167 GLY n 
1 168 HIS n 
1 169 ILE n 
1 170 ASP n 
1 171 TYR n 
1 172 GLN n 
1 173 LEU n 
1 174 ASP n 
1 175 ILE n 
1 176 ILE n 
1 177 THR n 
1 178 ALA n 
1 179 ALA n 
1 180 VAL n 
1 181 GLY n 
1 182 TRP n 
1 183 PHE n 
1 184 GLY n 
1 185 ASP n 
1 186 MET n 
1 187 MET n 
1 188 LEU n 
1 189 THR n 
1 190 ASN n 
1 191 GLY n 
1 192 THR n 
1 193 VAL n 
1 194 TYR n 
1 195 PRO n 
1 196 GLN n 
1 197 HIS n 
1 198 LEU n 
1 199 ALA n 
1 200 PRO n 
1 201 ARG n 
1 202 GLY n 
1 203 TRP n 
1 204 LEU n 
1 205 ARG n 
1 206 LEU n 
1 207 ARG n 
1 208 PHE n 
1 209 LEU n 
1 210 ASN n 
1 211 GLY n 
1 212 CYS n 
1 213 ASN n 
1 214 ALA n 
1 215 ARG n 
1 216 SER n 
1 217 LEU n 
1 218 ASN n 
1 219 LEU n 
1 220 ALA n 
1 221 THR n 
1 222 SER n 
1 223 ASP n 
1 224 GLY n 
1 225 ARG n 
1 226 PRO n 
1 227 LEU n 
1 228 TYR n 
1 229 VAL n 
1 230 VAL n 
1 231 GLY n 
1 232 SER n 
1 233 ASP n 
1 234 GLY n 
1 235 GLY n 
1 236 LEU n 
1 237 LEU n 
1 238 GLY n 
1 239 GLU n 
1 240 PRO n 
1 241 VAL n 
1 242 LYS n 
1 243 LEU n 
1 244 THR n 
1 245 GLU n 
1 246 LEU n 
1 247 PRO n 
1 248 ILE n 
1 249 LEU n 
1 250 MET n 
1 251 GLY n 
1 252 GLU n 
1 253 ARG n 
1 254 PHE n 
1 255 GLU n 
1 256 VAL n 
1 257 LEU n 
1 258 VAL n 
1 259 ASP n 
1 260 THR n 
1 261 ARG n 
1 262 ASP n 
1 263 GLY n 
1 264 LYS n 
1 265 ALA n 
1 266 PHE n 
1 267 ASP n 
1 268 ILE n 
1 269 ILE n 
1 270 THR n 
1 271 LEU n 
1 272 PRO n 
1 273 VAL n 
1 274 LYS n 
1 275 GLN n 
1 276 MET n 
1 277 GLY n 
1 278 MET n 
1 279 THR n 
1 280 LEU n 
1 281 PRO n 
1 282 PRO n 
1 283 PHE n 
1 284 ASP n 
1 285 ARG n 
1 286 ALA n 
1 287 LEU n 
1 288 PRO n 
1 289 VAL n 
1 290 LEU n 
1 291 HIS n 
1 292 ILE n 
1 293 GLN n 
1 294 PRO n 
1 295 THR n 
1 296 LEU n 
1 297 LYS n 
1 298 SER n 
1 299 ASN n 
1 300 GLU n 
1 301 ALA n 
1 302 LYS n 
1 303 LEU n 
1 304 PRO n 
1 305 ASP n 
1 306 ALA n 
1 307 LEU n 
1 308 VAL n 
1 309 ASN n 
1 310 MET n 
1 311 PRO n 
1 312 ALA n 
1 313 VAL n 
1 314 PRO n 
1 315 ALA n 
1 316 ALA n 
1 317 ASP n 
1 318 ASN n 
1 319 VAL n 
1 320 LYS n 
1 321 THR n 
1 322 ARG n 
1 323 TRP n 
1 324 LEU n 
1 325 GLN n 
1 326 LEU n 
1 327 MET n 
1 328 MET n 
1 329 ASP n 
1 330 GLY n 
1 331 GLY n 
1 332 GLY n 
1 333 ASN n 
1 334 LYS n 
1 335 ILE n 
1 336 ASN n 
1 337 GLY n 
1 338 ILE n 
1 339 ALA n 
1 340 PHE n 
1 341 ASP n 
1 342 MET n 
1 343 ALA n 
1 344 LYS n 
1 345 PRO n 
1 346 MET n 
1 347 PHE n 
1 348 ASP n 
1 349 VAL n 
1 350 LYS n 
1 351 ARG n 
1 352 GLY n 
1 353 THR n 
1 354 TYR n 
1 355 GLU n 
1 356 LYS n 
1 357 TRP n 
1 358 THR n 
1 359 ILE n 
1 360 SER n 
1 361 GLY n 
1 362 GLU n 
1 363 GLY n 
1 364 ASP n 
1 365 MET n 
1 366 MET n 
1 367 LEU n 
1 368 HIS n 
1 369 PRO n 
1 370 PHE n 
1 371 HIS n 
1 372 ILE n 
1 373 HIS n 
1 374 GLY n 
1 375 THR n 
1 376 GLN n 
1 377 PHE n 
1 378 ARG n 
1 379 ILE n 
1 380 LEU n 
1 381 SER n 
1 382 GLU n 
1 383 ASN n 
1 384 GLY n 
1 385 LYS n 
1 386 PRO n 
1 387 PRO n 
1 388 ALA n 
1 389 ALA n 
1 390 HIS n 
1 391 ARG n 
1 392 SER n 
1 393 GLY n 
1 394 TRP n 
1 395 LYS n 
1 396 ASP n 
1 397 THR n 
1 398 VAL n 
1 399 ARG n 
1 400 VAL n 
1 401 GLU n 
1 402 GLY n 
1 403 TRP n 
1 404 ARG n 
1 405 SER n 
1 406 GLU n 
1 407 VAL n 
1 408 LEU n 
1 409 VAL n 
1 410 LYS n 
1 411 PHE n 
1 412 ASP n 
1 413 HIS n 
1 414 GLU n 
1 415 ALA n 
1 416 PRO n 
1 417 LYS n 
1 418 GLU n 
1 419 ARG n 
1 420 ALA n 
1 421 TYR n 
1 422 MET n 
1 423 ALA n 
1 424 HIS n 
1 425 CYS n 
1 426 HIS n 
1 427 LEU n 
1 428 LEU n 
1 429 GLU n 
1 430 HIS n 
1 431 GLU n 
1 432 ASP n 
1 433 THR n 
1 434 GLY n 
1 435 MET n 
1 436 MET n 
1 437 MET n 
1 438 SER n 
1 439 PHE n 
1 440 THR n 
1 441 VAL n 
1 442 SER n 
1 443 SER n 
1 444 ALA n 
1 445 TRP n 
1 446 SER n 
1 447 HIS n 
1 448 PRO n 
1 449 GLN n 
1 450 PHE n 
1 451 GLU n 
1 452 LYS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1   329 ? ? cueO       ? ? ? ? ? ? 'Hafnia alvei' 569 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 330 452 ? ? AT03_17850 ? ? ? ? ? ? 'Hafnia alvei' 569 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE           ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE          ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE        ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'   ?                 'C4 H7 N O4'     133.103 
CU  non-polymer         . 'COPPER (II) ION' ?                 'Cu 2'           63.546  
CYS 'L-peptide linking' y CYSTEINE          ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL    'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE         ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'   ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE           ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE         ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER             ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE        ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE     ?                 'C9 H11 N O2'    165.189 
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   ALA 1   30  30  ALA ALA A . n 
A 1 2   GLU 2   31  31  GLU GLU A . n 
A 1 3   HIS 3   32  32  HIS HIS A . n 
A 1 4   PRO 4   33  33  PRO PRO A . n 
A 1 5   THR 5   34  34  THR THR A . n 
A 1 6   LEU 6   35  35  LEU LEU A . n 
A 1 7   PRO 7   36  36  PRO PRO A . n 
A 1 8   ILE 8   37  37  ILE ILE A . n 
A 1 9   PRO 9   38  38  PRO PRO A . n 
A 1 10  ALA 10  39  39  ALA ALA A . n 
A 1 11  LEU 11  40  40  LEU LEU A . n 
A 1 12  LEU 12  41  41  LEU LEU A . n 
A 1 13  THR 13  42  42  THR THR A . n 
A 1 14  PRO 14  43  43  PRO PRO A . n 
A 1 15  ASP 15  44  44  ASP ASP A . n 
A 1 16  ALA 16  45  45  ALA ALA A . n 
A 1 17  ALA 17  46  46  ALA ALA A . n 
A 1 18  GLY 18  47  47  GLY GLY A . n 
A 1 19  LYS 19  48  48  LYS LYS A . n 
A 1 20  ILE 20  49  49  ILE ILE A . n 
A 1 21  ALA 21  50  50  ALA ALA A . n 
A 1 22  LEU 22  51  51  LEU LEU A . n 
A 1 23  ASN 23  52  52  ASN ASN A . n 
A 1 24  VAL 24  53  53  VAL VAL A . n 
A 1 25  GLN 25  54  54  GLN GLN A . n 
A 1 26  THR 26  55  55  THR THR A . n 
A 1 27  GLY 27  56  56  GLY GLY A . n 
A 1 28  SER 28  57  57  SER SER A . n 
A 1 29  MET 29  58  58  MET MET A . n 
A 1 30  LYS 30  59  59  LYS LYS A . n 
A 1 31  TRP 31  60  60  TRP TRP A . n 
A 1 32  LYS 32  61  61  LYS LYS A . n 
A 1 33  ALA 33  62  62  ALA ALA A . n 
A 1 34  GLY 34  63  63  GLY GLY A . n 
A 1 35  MET 35  64  64  MET MET A . n 
A 1 36  GLN 36  65  65  GLN GLN A . n 
A 1 37  THR 37  66  66  THR THR A . n 
A 1 38  PRO 38  67  67  PRO PRO A . n 
A 1 39  THR 39  68  68  THR THR A . n 
A 1 40  TRP 40  69  69  TRP TRP A . n 
A 1 41  GLY 41  70  70  GLY GLY A . n 
A 1 42  ILE 42  71  71  ILE ILE A . n 
A 1 43  ASN 43  72  72  ASN ASN A . n 
A 1 44  GLY 44  73  73  GLY GLY A . n 
A 1 45  PRO 45  74  74  PRO PRO A . n 
A 1 46  LEU 46  75  75  LEU LEU A . n 
A 1 47  LEU 47  76  76  LEU LEU A . n 
A 1 48  GLY 48  77  77  GLY GLY A . n 
A 1 49  PRO 49  78  78  PRO PRO A . n 
A 1 50  ALA 50  79  79  ALA ALA A . n 
A 1 51  MET 51  80  80  MET MET A . n 
A 1 52  ARG 52  81  81  ARG ARG A . n 
A 1 53  LEU 53  82  82  LEU LEU A . n 
A 1 54  GLN 54  83  83  GLN GLN A . n 
A 1 55  ARG 55  84  84  ARG ARG A . n 
A 1 56  GLY 56  85  85  GLY GLY A . n 
A 1 57  LYS 57  86  86  LYS LYS A . n 
A 1 58  ASP 58  87  87  ASP ASP A . n 
A 1 59  VAL 59  88  88  VAL VAL A . n 
A 1 60  ALA 60  89  89  ALA ALA A . n 
A 1 61  ILE 61  90  90  ILE ILE A . n 
A 1 62  ASN 62  91  91  ASN ASN A . n 
A 1 63  VAL 63  92  92  VAL VAL A . n 
A 1 64  THR 64  93  93  THR THR A . n 
A 1 65  ASN 65  94  94  ASN ASN A . n 
A 1 66  ALA 66  95  95  ALA ALA A . n 
A 1 67  LEU 67  96  96  LEU LEU A . n 
A 1 68  PRO 68  97  97  PRO PRO A . n 
A 1 69  GLU 69  98  98  GLU GLU A . n 
A 1 70  ALA 70  99  99  ALA ALA A . n 
A 1 71  THR 71  100 100 THR THR A . n 
A 1 72  THR 72  101 101 THR THR A . n 
A 1 73  MET 73  102 102 MET MET A . n 
A 1 74  HIS 74  103 103 HIS HIS A . n 
A 1 75  TRP 75  104 104 TRP TRP A . n 
A 1 76  HIS 76  105 105 HIS HIS A . n 
A 1 77  GLY 77  106 106 GLY GLY A . n 
A 1 78  MET 78  107 107 MET MET A . n 
A 1 79  GLU 79  108 108 GLU GLU A . n 
A 1 80  ILE 80  109 109 ILE ILE A . n 
A 1 81  PRO 81  110 110 PRO PRO A . n 
A 1 82  GLY 82  111 111 GLY GLY A . n 
A 1 83  THR 83  112 112 THR THR A . n 
A 1 84  SER 84  113 113 SER SER A . n 
A 1 85  ASP 85  114 114 ASP ASP A . n 
A 1 86  GLY 86  115 115 GLY GLY A . n 
A 1 87  GLY 87  116 116 GLY GLY A . n 
A 1 88  PRO 88  117 117 PRO PRO A . n 
A 1 89  GLN 89  118 118 GLN GLN A . n 
A 1 90  ALA 90  119 119 ALA ALA A . n 
A 1 91  VAL 91  120 120 VAL VAL A . n 
A 1 92  ILE 92  121 121 ILE ILE A . n 
A 1 93  GLU 93  122 122 GLU GLU A . n 
A 1 94  PRO 94  123 123 PRO PRO A . n 
A 1 95  GLY 95  124 124 GLY GLY A . n 
A 1 96  LYS 96  125 125 LYS LYS A . n 
A 1 97  MET 97  126 126 MET MET A . n 
A 1 98  TRP 98  127 127 TRP TRP A . n 
A 1 99  THR 99  128 128 THR THR A . n 
A 1 100 ALA 100 129 129 ALA ALA A . n 
A 1 101 GLU 101 130 130 GLU GLU A . n 
A 1 102 ILE 102 131 131 ILE ILE A . n 
A 1 103 LYS 103 132 132 LYS LYS A . n 
A 1 104 VAL 104 133 133 VAL VAL A . n 
A 1 105 ASP 105 134 134 ASP ASP A . n 
A 1 106 GLN 106 135 135 GLN GLN A . n 
A 1 107 PRO 107 136 136 PRO PRO A . n 
A 1 108 ALA 108 137 137 ALA ALA A . n 
A 1 109 THR 109 138 138 THR THR A . n 
A 1 110 THR 110 139 139 THR THR A . n 
A 1 111 ALA 111 140 140 ALA ALA A . n 
A 1 112 TRP 112 141 141 TRP TRP A . n 
A 1 113 PHE 113 142 142 PHE PHE A . n 
A 1 114 HIS 114 143 143 HIS HIS A . n 
A 1 115 PRO 115 144 144 PRO PRO A . n 
A 1 116 HIS 116 145 145 HIS HIS A . n 
A 1 117 THR 117 146 146 THR THR A . n 
A 1 118 HIS 118 147 147 HIS HIS A . n 
A 1 119 GLY 119 148 148 GLY GLY A . n 
A 1 120 LEU 120 149 149 LEU LEU A . n 
A 1 121 THR 121 150 150 THR THR A . n 
A 1 122 GLY 122 151 151 GLY GLY A . n 
A 1 123 ARG 123 152 152 ARG ARG A . n 
A 1 124 GLN 124 153 153 GLN GLN A . n 
A 1 125 VAL 125 154 154 VAL VAL A . n 
A 1 126 ALA 126 155 155 ALA ALA A . n 
A 1 127 MET 127 156 156 MET MET A . n 
A 1 128 GLY 128 157 157 GLY GLY A . n 
A 1 129 LEU 129 158 158 LEU LEU A . n 
A 1 130 GLY 130 159 159 GLY GLY A . n 
A 1 131 GLY 131 160 160 GLY GLY A . n 
A 1 132 LEU 132 161 161 LEU LEU A . n 
A 1 133 ILE 133 162 162 ILE ILE A . n 
A 1 134 ILE 134 163 163 ILE ILE A . n 
A 1 135 ILE 135 164 164 ILE ILE A . n 
A 1 136 ASP 136 165 165 ASP ASP A . n 
A 1 137 ASP 137 166 166 ASP ASP A . n 
A 1 138 GLU 138 167 167 GLU GLU A . n 
A 1 139 GLU 139 168 168 GLU GLU A . n 
A 1 140 SER 140 169 169 SER SER A . n 
A 1 141 THR 141 170 170 THR THR A . n 
A 1 142 LYS 142 171 171 LYS LYS A . n 
A 1 143 LEU 143 172 172 LEU LEU A . n 
A 1 144 PRO 144 173 173 PRO PRO A . n 
A 1 145 LEU 145 174 174 LEU LEU A . n 
A 1 146 PRO 146 175 175 PRO PRO A . n 
A 1 147 LYS 147 176 176 LYS LYS A . n 
A 1 148 GLU 148 177 177 GLU GLU A . n 
A 1 149 TRP 149 178 178 TRP TRP A . n 
A 1 150 GLY 150 179 179 GLY GLY A . n 
A 1 151 VAL 151 180 180 VAL VAL A . n 
A 1 152 ASP 152 181 181 ASP ASP A . n 
A 1 153 ASP 153 182 182 ASP ASP A . n 
A 1 154 VAL 154 183 183 VAL VAL A . n 
A 1 155 PRO 155 184 184 PRO PRO A . n 
A 1 156 VAL 156 185 185 VAL VAL A . n 
A 1 157 ILE 157 186 186 ILE ILE A . n 
A 1 158 LEU 158 187 187 LEU LEU A . n 
A 1 159 GLN 159 188 188 GLN GLN A . n 
A 1 160 ASP 160 189 189 ASP ASP A . n 
A 1 161 LYS 161 190 190 LYS LYS A . n 
A 1 162 ARG 162 191 191 ARG ARG A . n 
A 1 163 LEU 163 192 192 LEU LEU A . n 
A 1 164 ASP 164 193 193 ASP ASP A . n 
A 1 165 ALA 165 194 194 ALA ALA A . n 
A 1 166 LYS 166 195 195 LYS LYS A . n 
A 1 167 GLY 167 196 196 GLY GLY A . n 
A 1 168 HIS 168 197 197 HIS HIS A . n 
A 1 169 ILE 169 198 198 ILE ILE A . n 
A 1 170 ASP 170 199 199 ASP ASP A . n 
A 1 171 TYR 171 200 200 TYR TYR A . n 
A 1 172 GLN 172 201 201 GLN GLN A . n 
A 1 173 LEU 173 202 202 LEU LEU A . n 
A 1 174 ASP 174 203 203 ASP ASP A . n 
A 1 175 ILE 175 204 204 ILE ILE A . n 
A 1 176 ILE 176 205 205 ILE ILE A . n 
A 1 177 THR 177 206 206 THR THR A . n 
A 1 178 ALA 178 207 207 ALA ALA A . n 
A 1 179 ALA 179 208 208 ALA ALA A . n 
A 1 180 VAL 180 209 209 VAL VAL A . n 
A 1 181 GLY 181 210 210 GLY GLY A . n 
A 1 182 TRP 182 211 211 TRP TRP A . n 
A 1 183 PHE 183 212 212 PHE PHE A . n 
A 1 184 GLY 184 213 213 GLY GLY A . n 
A 1 185 ASP 185 214 214 ASP ASP A . n 
A 1 186 MET 186 215 215 MET MET A . n 
A 1 187 MET 187 216 216 MET MET A . n 
A 1 188 LEU 188 217 217 LEU LEU A . n 
A 1 189 THR 189 218 218 THR THR A . n 
A 1 190 ASN 190 219 219 ASN ASN A . n 
A 1 191 GLY 191 220 220 GLY GLY A . n 
A 1 192 THR 192 221 221 THR THR A . n 
A 1 193 VAL 193 222 222 VAL VAL A . n 
A 1 194 TYR 194 223 223 TYR TYR A . n 
A 1 195 PRO 195 224 224 PRO PRO A . n 
A 1 196 GLN 196 225 225 GLN GLN A . n 
A 1 197 HIS 197 226 226 HIS HIS A . n 
A 1 198 LEU 198 227 227 LEU LEU A . n 
A 1 199 ALA 199 228 228 ALA ALA A . n 
A 1 200 PRO 200 229 229 PRO PRO A . n 
A 1 201 ARG 201 230 230 ARG ARG A . n 
A 1 202 GLY 202 231 231 GLY GLY A . n 
A 1 203 TRP 203 232 232 TRP TRP A . n 
A 1 204 LEU 204 233 233 LEU LEU A . n 
A 1 205 ARG 205 234 234 ARG ARG A . n 
A 1 206 LEU 206 235 235 LEU LEU A . n 
A 1 207 ARG 207 236 236 ARG ARG A . n 
A 1 208 PHE 208 237 237 PHE PHE A . n 
A 1 209 LEU 209 238 238 LEU LEU A . n 
A 1 210 ASN 210 239 239 ASN ASN A . n 
A 1 211 GLY 211 240 240 GLY GLY A . n 
A 1 212 CYS 212 241 241 CYS CYS A . n 
A 1 213 ASN 213 242 242 ASN ASN A . n 
A 1 214 ALA 214 243 243 ALA ALA A . n 
A 1 215 ARG 215 244 244 ARG ARG A . n 
A 1 216 SER 216 245 245 SER SER A . n 
A 1 217 LEU 217 246 246 LEU LEU A . n 
A 1 218 ASN 218 247 247 ASN ASN A . n 
A 1 219 LEU 219 248 248 LEU LEU A . n 
A 1 220 ALA 220 249 249 ALA ALA A . n 
A 1 221 THR 221 250 250 THR THR A . n 
A 1 222 SER 222 251 251 SER SER A . n 
A 1 223 ASP 223 252 252 ASP ASP A . n 
A 1 224 GLY 224 253 253 GLY GLY A . n 
A 1 225 ARG 225 254 254 ARG ARG A . n 
A 1 226 PRO 226 255 255 PRO PRO A . n 
A 1 227 LEU 227 256 256 LEU LEU A . n 
A 1 228 TYR 228 257 257 TYR TYR A . n 
A 1 229 VAL 229 258 258 VAL VAL A . n 
A 1 230 VAL 230 259 259 VAL VAL A . n 
A 1 231 GLY 231 260 260 GLY GLY A . n 
A 1 232 SER 232 261 261 SER SER A . n 
A 1 233 ASP 233 262 262 ASP ASP A . n 
A 1 234 GLY 234 263 263 GLY GLY A . n 
A 1 235 GLY 235 264 264 GLY GLY A . n 
A 1 236 LEU 236 265 265 LEU LEU A . n 
A 1 237 LEU 237 266 266 LEU LEU A . n 
A 1 238 GLY 238 267 267 GLY GLY A . n 
A 1 239 GLU 239 268 268 GLU GLU A . n 
A 1 240 PRO 240 269 269 PRO PRO A . n 
A 1 241 VAL 241 270 270 VAL VAL A . n 
A 1 242 LYS 242 271 271 LYS LYS A . n 
A 1 243 LEU 243 272 272 LEU LEU A . n 
A 1 244 THR 244 273 273 THR THR A . n 
A 1 245 GLU 245 274 274 GLU GLU A . n 
A 1 246 LEU 246 275 275 LEU LEU A . n 
A 1 247 PRO 247 276 276 PRO PRO A . n 
A 1 248 ILE 248 277 277 ILE ILE A . n 
A 1 249 LEU 249 278 278 LEU LEU A . n 
A 1 250 MET 250 279 279 MET MET A . n 
A 1 251 GLY 251 280 280 GLY GLY A . n 
A 1 252 GLU 252 281 281 GLU GLU A . n 
A 1 253 ARG 253 282 282 ARG ARG A . n 
A 1 254 PHE 254 283 283 PHE PHE A . n 
A 1 255 GLU 255 284 284 GLU GLU A . n 
A 1 256 VAL 256 285 285 VAL VAL A . n 
A 1 257 LEU 257 286 286 LEU LEU A . n 
A 1 258 VAL 258 287 287 VAL VAL A . n 
A 1 259 ASP 259 288 288 ASP ASP A . n 
A 1 260 THR 260 289 289 THR THR A . n 
A 1 261 ARG 261 290 290 ARG ARG A . n 
A 1 262 ASP 262 291 291 ASP ASP A . n 
A 1 263 GLY 263 292 292 GLY GLY A . n 
A 1 264 LYS 264 293 293 LYS LYS A . n 
A 1 265 ALA 265 294 294 ALA ALA A . n 
A 1 266 PHE 266 295 295 PHE PHE A . n 
A 1 267 ASP 267 296 296 ASP ASP A . n 
A 1 268 ILE 268 297 297 ILE ILE A . n 
A 1 269 ILE 269 298 298 ILE ILE A . n 
A 1 270 THR 270 299 299 THR THR A . n 
A 1 271 LEU 271 300 300 LEU LEU A . n 
A 1 272 PRO 272 301 301 PRO PRO A . n 
A 1 273 VAL 273 302 302 VAL VAL A . n 
A 1 274 LYS 274 303 303 LYS LYS A . n 
A 1 275 GLN 275 304 304 GLN GLN A . n 
A 1 276 MET 276 305 305 MET MET A . n 
A 1 277 GLY 277 306 306 GLY GLY A . n 
A 1 278 MET 278 307 307 MET MET A . n 
A 1 279 THR 279 308 308 THR THR A . n 
A 1 280 LEU 280 309 309 LEU LEU A . n 
A 1 281 PRO 281 310 310 PRO PRO A . n 
A 1 282 PRO 282 311 311 PRO PRO A . n 
A 1 283 PHE 283 312 312 PHE PHE A . n 
A 1 284 ASP 284 313 313 ASP ASP A . n 
A 1 285 ARG 285 314 314 ARG ARG A . n 
A 1 286 ALA 286 315 315 ALA ALA A . n 
A 1 287 LEU 287 316 316 LEU LEU A . n 
A 1 288 PRO 288 317 317 PRO PRO A . n 
A 1 289 VAL 289 318 318 VAL VAL A . n 
A 1 290 LEU 290 319 319 LEU LEU A . n 
A 1 291 HIS 291 320 320 HIS HIS A . n 
A 1 292 ILE 292 321 321 ILE ILE A . n 
A 1 293 GLN 293 322 322 GLN GLN A . n 
A 1 294 PRO 294 323 323 PRO PRO A . n 
A 1 295 THR 295 324 324 THR THR A . n 
A 1 296 LEU 296 325 325 LEU LEU A . n 
A 1 297 LYS 297 326 326 LYS LYS A . n 
A 1 298 SER 298 327 327 SER SER A . n 
A 1 299 ASN 299 328 328 ASN ASN A . n 
A 1 300 GLU 300 329 329 GLU GLU A . n 
A 1 301 ALA 301 330 330 ALA ALA A . n 
A 1 302 LYS 302 331 331 LYS LYS A . n 
A 1 303 LEU 303 332 332 LEU LEU A . n 
A 1 304 PRO 304 333 333 PRO PRO A . n 
A 1 305 ASP 305 334 334 ASP ASP A . n 
A 1 306 ALA 306 335 335 ALA ALA A . n 
A 1 307 LEU 307 336 336 LEU LEU A . n 
A 1 308 VAL 308 337 337 VAL VAL A . n 
A 1 309 ASN 309 338 338 ASN ASN A . n 
A 1 310 MET 310 339 339 MET MET A . n 
A 1 311 PRO 311 340 340 PRO PRO A . n 
A 1 312 ALA 312 341 341 ALA ALA A . n 
A 1 313 VAL 313 342 342 VAL VAL A . n 
A 1 314 PRO 314 343 343 PRO PRO A . n 
A 1 315 ALA 315 344 344 ALA ALA A . n 
A 1 316 ALA 316 345 345 ALA ALA A . n 
A 1 317 ASP 317 346 346 ASP ASP A . n 
A 1 318 ASN 318 347 347 ASN ASN A . n 
A 1 319 VAL 319 348 348 VAL VAL A . n 
A 1 320 LYS 320 349 349 LYS LYS A . n 
A 1 321 THR 321 350 350 THR THR A . n 
A 1 322 ARG 322 351 351 ARG ARG A . n 
A 1 323 TRP 323 352 352 TRP TRP A . n 
A 1 324 LEU 324 353 353 LEU LEU A . n 
A 1 325 GLN 325 354 354 GLN GLN A . n 
A 1 326 LEU 326 355 355 LEU LEU A . n 
A 1 327 MET 327 356 356 MET MET A . n 
A 1 328 MET 328 357 357 MET MET A . n 
A 1 329 ASP 329 358 358 ASP ASP A . n 
A 1 330 GLY 330 358 358 GLY GLY A A n 
A 1 331 GLY 331 358 358 GLY GLY A B n 
A 1 332 GLY 332 431 431 GLY GLY A . n 
A 1 333 ASN 333 432 432 ASN ASN A . n 
A 1 334 LYS 334 433 433 LYS LYS A . n 
A 1 335 ILE 335 434 434 ILE ILE A . n 
A 1 336 ASN 336 435 435 ASN ASN A . n 
A 1 337 GLY 337 436 436 GLY GLY A . n 
A 1 338 ILE 338 437 437 ILE ILE A . n 
A 1 339 ALA 339 438 438 ALA ALA A . n 
A 1 340 PHE 340 439 439 PHE PHE A . n 
A 1 341 ASP 341 440 440 ASP ASP A . n 
A 1 342 MET 342 441 441 MET MET A . n 
A 1 343 ALA 343 442 442 ALA ALA A . n 
A 1 344 LYS 344 443 443 LYS LYS A . n 
A 1 345 PRO 345 444 444 PRO PRO A . n 
A 1 346 MET 346 445 445 MET MET A . n 
A 1 347 PHE 347 446 446 PHE PHE A . n 
A 1 348 ASP 348 447 447 ASP ASP A . n 
A 1 349 VAL 349 448 448 VAL VAL A . n 
A 1 350 LYS 350 449 449 LYS LYS A . n 
A 1 351 ARG 351 450 450 ARG ARG A . n 
A 1 352 GLY 352 451 451 GLY GLY A . n 
A 1 353 THR 353 452 452 THR THR A . n 
A 1 354 TYR 354 453 453 TYR TYR A . n 
A 1 355 GLU 355 454 454 GLU GLU A . n 
A 1 356 LYS 356 455 455 LYS LYS A . n 
A 1 357 TRP 357 456 456 TRP TRP A . n 
A 1 358 THR 358 457 457 THR THR A . n 
A 1 359 ILE 359 458 458 ILE ILE A . n 
A 1 360 SER 360 459 459 SER SER A . n 
A 1 361 GLY 361 460 460 GLY GLY A . n 
A 1 362 GLU 362 461 461 GLU GLU A . n 
A 1 363 GLY 363 462 462 GLY GLY A . n 
A 1 364 ASP 364 463 463 ASP ASP A . n 
A 1 365 MET 365 464 464 MET MET A . n 
A 1 366 MET 366 465 465 MET MET A . n 
A 1 367 LEU 367 466 466 LEU LEU A . n 
A 1 368 HIS 368 467 467 HIS HIS A . n 
A 1 369 PRO 369 468 468 PRO PRO A . n 
A 1 370 PHE 370 469 469 PHE PHE A . n 
A 1 371 HIS 371 470 470 HIS HIS A . n 
A 1 372 ILE 372 471 471 ILE ILE A . n 
A 1 373 HIS 373 472 472 HIS HIS A . n 
A 1 374 GLY 374 473 473 GLY GLY A . n 
A 1 375 THR 375 474 474 THR THR A . n 
A 1 376 GLN 376 475 475 GLN GLN A . n 
A 1 377 PHE 377 476 476 PHE PHE A . n 
A 1 378 ARG 378 477 477 ARG ARG A . n 
A 1 379 ILE 379 478 478 ILE ILE A . n 
A 1 380 LEU 380 479 479 LEU LEU A . n 
A 1 381 SER 381 480 480 SER SER A . n 
A 1 382 GLU 382 481 481 GLU GLU A . n 
A 1 383 ASN 383 482 482 ASN ASN A . n 
A 1 384 GLY 384 483 483 GLY GLY A . n 
A 1 385 LYS 385 484 484 LYS LYS A . n 
A 1 386 PRO 386 485 485 PRO PRO A . n 
A 1 387 PRO 387 486 486 PRO PRO A . n 
A 1 388 ALA 388 487 487 ALA ALA A . n 
A 1 389 ALA 389 488 488 ALA ALA A . n 
A 1 390 HIS 390 489 489 HIS HIS A . n 
A 1 391 ARG 391 490 490 ARG ARG A . n 
A 1 392 SER 392 491 491 SER SER A . n 
A 1 393 GLY 393 492 492 GLY GLY A . n 
A 1 394 TRP 394 493 493 TRP TRP A . n 
A 1 395 LYS 395 494 494 LYS LYS A . n 
A 1 396 ASP 396 495 495 ASP ASP A . n 
A 1 397 THR 397 496 496 THR THR A . n 
A 1 398 VAL 398 497 497 VAL VAL A . n 
A 1 399 ARG 399 498 498 ARG ARG A . n 
A 1 400 VAL 400 499 499 VAL VAL A . n 
A 1 401 GLU 401 500 500 GLU GLU A . n 
A 1 402 GLY 402 501 501 GLY GLY A . n 
A 1 403 TRP 403 502 502 TRP TRP A . n 
A 1 404 ARG 404 503 503 ARG ARG A . n 
A 1 405 SER 405 504 504 SER SER A . n 
A 1 406 GLU 406 505 505 GLU GLU A . n 
A 1 407 VAL 407 506 506 VAL VAL A . n 
A 1 408 LEU 408 507 507 LEU LEU A . n 
A 1 409 VAL 409 508 508 VAL VAL A . n 
A 1 410 LYS 410 509 509 LYS LYS A . n 
A 1 411 PHE 411 510 510 PHE PHE A . n 
A 1 412 ASP 412 511 511 ASP ASP A . n 
A 1 413 HIS 413 512 512 HIS HIS A . n 
A 1 414 GLU 414 513 513 GLU GLU A . n 
A 1 415 ALA 415 514 514 ALA ALA A . n 
A 1 416 PRO 416 515 515 PRO PRO A . n 
A 1 417 LYS 417 516 516 LYS LYS A . n 
A 1 418 GLU 418 517 517 GLU GLU A . n 
A 1 419 ARG 419 518 518 ARG ARG A . n 
A 1 420 ALA 420 519 519 ALA ALA A . n 
A 1 421 TYR 421 520 520 TYR TYR A . n 
A 1 422 MET 422 521 521 MET MET A . n 
A 1 423 ALA 423 522 522 ALA ALA A . n 
A 1 424 HIS 424 523 523 HIS HIS A . n 
A 1 425 CYS 425 524 524 CYS CYS A . n 
A 1 426 HIS 426 525 525 HIS HIS A . n 
A 1 427 LEU 427 526 526 LEU LEU A . n 
A 1 428 LEU 428 527 527 LEU LEU A . n 
A 1 429 GLU 429 528 528 GLU GLU A . n 
A 1 430 HIS 430 529 529 HIS HIS A . n 
A 1 431 GLU 431 530 530 GLU GLU A . n 
A 1 432 ASP 432 531 531 ASP ASP A . n 
A 1 433 THR 433 532 532 THR THR A . n 
A 1 434 GLY 434 533 533 GLY GLY A . n 
A 1 435 MET 435 534 534 MET MET A . n 
A 1 436 MET 436 535 535 MET MET A . n 
A 1 437 MET 437 536 536 MET MET A . n 
A 1 438 SER 438 537 537 SER SER A . n 
A 1 439 PHE 439 538 538 PHE PHE A . n 
A 1 440 THR 440 539 539 THR THR A . n 
A 1 441 VAL 441 540 540 VAL VAL A . n 
A 1 442 SER 442 541 541 SER SER A . n 
A 1 443 SER 443 542 ?   ?   ?   A . n 
A 1 444 ALA 444 543 ?   ?   ?   A . n 
A 1 445 TRP 445 544 ?   ?   ?   A . n 
A 1 446 SER 446 545 ?   ?   ?   A . n 
A 1 447 HIS 447 546 ?   ?   ?   A . n 
A 1 448 PRO 448 547 ?   ?   ?   A . n 
A 1 449 GLN 449 548 ?   ?   ?   A . n 
A 1 450 PHE 450 549 ?   ?   ?   A . n 
A 1 451 GLU 451 550 ?   ?   ?   A . n 
A 1 452 LYS 452 551 ?   ?   ?   A . n 
B 1 1   ALA 1   30  30  ALA ALA B . n 
B 1 2   GLU 2   31  31  GLU GLU B . n 
B 1 3   HIS 3   32  32  HIS HIS B . n 
B 1 4   PRO 4   33  33  PRO PRO B . n 
B 1 5   THR 5   34  34  THR THR B . n 
B 1 6   LEU 6   35  35  LEU LEU B . n 
B 1 7   PRO 7   36  36  PRO PRO B . n 
B 1 8   ILE 8   37  37  ILE ILE B . n 
B 1 9   PRO 9   38  38  PRO PRO B . n 
B 1 10  ALA 10  39  39  ALA ALA B . n 
B 1 11  LEU 11  40  40  LEU LEU B . n 
B 1 12  LEU 12  41  41  LEU LEU B . n 
B 1 13  THR 13  42  42  THR THR B . n 
B 1 14  PRO 14  43  43  PRO PRO B . n 
B 1 15  ASP 15  44  44  ASP ASP B . n 
B 1 16  ALA 16  45  45  ALA ALA B . n 
B 1 17  ALA 17  46  46  ALA ALA B . n 
B 1 18  GLY 18  47  47  GLY GLY B . n 
B 1 19  LYS 19  48  48  LYS LYS B . n 
B 1 20  ILE 20  49  49  ILE ILE B . n 
B 1 21  ALA 21  50  50  ALA ALA B . n 
B 1 22  LEU 22  51  51  LEU LEU B . n 
B 1 23  ASN 23  52  52  ASN ASN B . n 
B 1 24  VAL 24  53  53  VAL VAL B . n 
B 1 25  GLN 25  54  54  GLN GLN B . n 
B 1 26  THR 26  55  55  THR THR B . n 
B 1 27  GLY 27  56  56  GLY GLY B . n 
B 1 28  SER 28  57  57  SER SER B . n 
B 1 29  MET 29  58  58  MET MET B . n 
B 1 30  LYS 30  59  59  LYS LYS B . n 
B 1 31  TRP 31  60  60  TRP TRP B . n 
B 1 32  LYS 32  61  61  LYS LYS B . n 
B 1 33  ALA 33  62  62  ALA ALA B . n 
B 1 34  GLY 34  63  63  GLY GLY B . n 
B 1 35  MET 35  64  64  MET MET B . n 
B 1 36  GLN 36  65  65  GLN GLN B . n 
B 1 37  THR 37  66  66  THR THR B . n 
B 1 38  PRO 38  67  67  PRO PRO B . n 
B 1 39  THR 39  68  68  THR THR B . n 
B 1 40  TRP 40  69  69  TRP TRP B . n 
B 1 41  GLY 41  70  70  GLY GLY B . n 
B 1 42  ILE 42  71  71  ILE ILE B . n 
B 1 43  ASN 43  72  72  ASN ASN B . n 
B 1 44  GLY 44  73  73  GLY GLY B . n 
B 1 45  PRO 45  74  74  PRO PRO B . n 
B 1 46  LEU 46  75  75  LEU LEU B . n 
B 1 47  LEU 47  76  76  LEU LEU B . n 
B 1 48  GLY 48  77  77  GLY GLY B . n 
B 1 49  PRO 49  78  78  PRO PRO B . n 
B 1 50  ALA 50  79  79  ALA ALA B . n 
B 1 51  MET 51  80  80  MET MET B . n 
B 1 52  ARG 52  81  81  ARG ARG B . n 
B 1 53  LEU 53  82  82  LEU LEU B . n 
B 1 54  GLN 54  83  83  GLN GLN B . n 
B 1 55  ARG 55  84  84  ARG ARG B . n 
B 1 56  GLY 56  85  85  GLY GLY B . n 
B 1 57  LYS 57  86  86  LYS LYS B . n 
B 1 58  ASP 58  87  87  ASP ASP B . n 
B 1 59  VAL 59  88  88  VAL VAL B . n 
B 1 60  ALA 60  89  89  ALA ALA B . n 
B 1 61  ILE 61  90  90  ILE ILE B . n 
B 1 62  ASN 62  91  91  ASN ASN B . n 
B 1 63  VAL 63  92  92  VAL VAL B . n 
B 1 64  THR 64  93  93  THR THR B . n 
B 1 65  ASN 65  94  94  ASN ASN B . n 
B 1 66  ALA 66  95  95  ALA ALA B . n 
B 1 67  LEU 67  96  96  LEU LEU B . n 
B 1 68  PRO 68  97  97  PRO PRO B . n 
B 1 69  GLU 69  98  98  GLU GLU B . n 
B 1 70  ALA 70  99  99  ALA ALA B . n 
B 1 71  THR 71  100 100 THR THR B . n 
B 1 72  THR 72  101 101 THR THR B . n 
B 1 73  MET 73  102 102 MET MET B . n 
B 1 74  HIS 74  103 103 HIS HIS B . n 
B 1 75  TRP 75  104 104 TRP TRP B . n 
B 1 76  HIS 76  105 105 HIS HIS B . n 
B 1 77  GLY 77  106 106 GLY GLY B . n 
B 1 78  MET 78  107 107 MET MET B . n 
B 1 79  GLU 79  108 108 GLU GLU B . n 
B 1 80  ILE 80  109 109 ILE ILE B . n 
B 1 81  PRO 81  110 110 PRO PRO B . n 
B 1 82  GLY 82  111 111 GLY GLY B . n 
B 1 83  THR 83  112 112 THR THR B . n 
B 1 84  SER 84  113 113 SER SER B . n 
B 1 85  ASP 85  114 114 ASP ASP B . n 
B 1 86  GLY 86  115 115 GLY GLY B . n 
B 1 87  GLY 87  116 116 GLY GLY B . n 
B 1 88  PRO 88  117 117 PRO PRO B . n 
B 1 89  GLN 89  118 118 GLN GLN B . n 
B 1 90  ALA 90  119 119 ALA ALA B . n 
B 1 91  VAL 91  120 120 VAL VAL B . n 
B 1 92  ILE 92  121 121 ILE ILE B . n 
B 1 93  GLU 93  122 122 GLU GLU B . n 
B 1 94  PRO 94  123 123 PRO PRO B . n 
B 1 95  GLY 95  124 124 GLY GLY B . n 
B 1 96  LYS 96  125 125 LYS LYS B . n 
B 1 97  MET 97  126 126 MET MET B . n 
B 1 98  TRP 98  127 127 TRP TRP B . n 
B 1 99  THR 99  128 128 THR THR B . n 
B 1 100 ALA 100 129 129 ALA ALA B . n 
B 1 101 GLU 101 130 130 GLU GLU B . n 
B 1 102 ILE 102 131 131 ILE ILE B . n 
B 1 103 LYS 103 132 132 LYS LYS B . n 
B 1 104 VAL 104 133 133 VAL VAL B . n 
B 1 105 ASP 105 134 134 ASP ASP B . n 
B 1 106 GLN 106 135 135 GLN GLN B . n 
B 1 107 PRO 107 136 136 PRO PRO B . n 
B 1 108 ALA 108 137 137 ALA ALA B . n 
B 1 109 THR 109 138 138 THR THR B . n 
B 1 110 THR 110 139 139 THR THR B . n 
B 1 111 ALA 111 140 140 ALA ALA B . n 
B 1 112 TRP 112 141 141 TRP TRP B . n 
B 1 113 PHE 113 142 142 PHE PHE B . n 
B 1 114 HIS 114 143 143 HIS HIS B . n 
B 1 115 PRO 115 144 144 PRO PRO B . n 
B 1 116 HIS 116 145 145 HIS HIS B . n 
B 1 117 THR 117 146 146 THR THR B . n 
B 1 118 HIS 118 147 147 HIS HIS B . n 
B 1 119 GLY 119 148 148 GLY GLY B . n 
B 1 120 LEU 120 149 149 LEU LEU B . n 
B 1 121 THR 121 150 150 THR THR B . n 
B 1 122 GLY 122 151 151 GLY GLY B . n 
B 1 123 ARG 123 152 152 ARG ARG B . n 
B 1 124 GLN 124 153 153 GLN GLN B . n 
B 1 125 VAL 125 154 154 VAL VAL B . n 
B 1 126 ALA 126 155 155 ALA ALA B . n 
B 1 127 MET 127 156 156 MET MET B . n 
B 1 128 GLY 128 157 157 GLY GLY B . n 
B 1 129 LEU 129 158 158 LEU LEU B . n 
B 1 130 GLY 130 159 159 GLY GLY B . n 
B 1 131 GLY 131 160 160 GLY GLY B . n 
B 1 132 LEU 132 161 161 LEU LEU B . n 
B 1 133 ILE 133 162 162 ILE ILE B . n 
B 1 134 ILE 134 163 163 ILE ILE B . n 
B 1 135 ILE 135 164 164 ILE ILE B . n 
B 1 136 ASP 136 165 165 ASP ASP B . n 
B 1 137 ASP 137 166 166 ASP ASP B . n 
B 1 138 GLU 138 167 167 GLU GLU B . n 
B 1 139 GLU 139 168 168 GLU GLU B . n 
B 1 140 SER 140 169 169 SER SER B . n 
B 1 141 THR 141 170 170 THR THR B . n 
B 1 142 LYS 142 171 171 LYS LYS B . n 
B 1 143 LEU 143 172 172 LEU LEU B . n 
B 1 144 PRO 144 173 173 PRO PRO B . n 
B 1 145 LEU 145 174 174 LEU LEU B . n 
B 1 146 PRO 146 175 175 PRO PRO B . n 
B 1 147 LYS 147 176 176 LYS LYS B . n 
B 1 148 GLU 148 177 177 GLU GLU B . n 
B 1 149 TRP 149 178 178 TRP TRP B . n 
B 1 150 GLY 150 179 179 GLY GLY B . n 
B 1 151 VAL 151 180 180 VAL VAL B . n 
B 1 152 ASP 152 181 181 ASP ASP B . n 
B 1 153 ASP 153 182 182 ASP ASP B . n 
B 1 154 VAL 154 183 183 VAL VAL B . n 
B 1 155 PRO 155 184 184 PRO PRO B . n 
B 1 156 VAL 156 185 185 VAL VAL B . n 
B 1 157 ILE 157 186 186 ILE ILE B . n 
B 1 158 LEU 158 187 187 LEU LEU B . n 
B 1 159 GLN 159 188 188 GLN GLN B . n 
B 1 160 ASP 160 189 189 ASP ASP B . n 
B 1 161 LYS 161 190 190 LYS LYS B . n 
B 1 162 ARG 162 191 191 ARG ARG B . n 
B 1 163 LEU 163 192 192 LEU LEU B . n 
B 1 164 ASP 164 193 193 ASP ASP B . n 
B 1 165 ALA 165 194 194 ALA ALA B . n 
B 1 166 LYS 166 195 195 LYS LYS B . n 
B 1 167 GLY 167 196 196 GLY GLY B . n 
B 1 168 HIS 168 197 197 HIS HIS B . n 
B 1 169 ILE 169 198 198 ILE ILE B . n 
B 1 170 ASP 170 199 199 ASP ASP B . n 
B 1 171 TYR 171 200 200 TYR TYR B . n 
B 1 172 GLN 172 201 201 GLN GLN B . n 
B 1 173 LEU 173 202 202 LEU LEU B . n 
B 1 174 ASP 174 203 203 ASP ASP B . n 
B 1 175 ILE 175 204 204 ILE ILE B . n 
B 1 176 ILE 176 205 205 ILE ILE B . n 
B 1 177 THR 177 206 206 THR THR B . n 
B 1 178 ALA 178 207 207 ALA ALA B . n 
B 1 179 ALA 179 208 208 ALA ALA B . n 
B 1 180 VAL 180 209 209 VAL VAL B . n 
B 1 181 GLY 181 210 210 GLY GLY B . n 
B 1 182 TRP 182 211 211 TRP TRP B . n 
B 1 183 PHE 183 212 212 PHE PHE B . n 
B 1 184 GLY 184 213 213 GLY GLY B . n 
B 1 185 ASP 185 214 214 ASP ASP B . n 
B 1 186 MET 186 215 215 MET MET B . n 
B 1 187 MET 187 216 216 MET MET B . n 
B 1 188 LEU 188 217 217 LEU LEU B . n 
B 1 189 THR 189 218 218 THR THR B . n 
B 1 190 ASN 190 219 219 ASN ASN B . n 
B 1 191 GLY 191 220 220 GLY GLY B . n 
B 1 192 THR 192 221 221 THR THR B . n 
B 1 193 VAL 193 222 222 VAL VAL B . n 
B 1 194 TYR 194 223 223 TYR TYR B . n 
B 1 195 PRO 195 224 224 PRO PRO B . n 
B 1 196 GLN 196 225 225 GLN GLN B . n 
B 1 197 HIS 197 226 226 HIS HIS B . n 
B 1 198 LEU 198 227 227 LEU LEU B . n 
B 1 199 ALA 199 228 228 ALA ALA B . n 
B 1 200 PRO 200 229 229 PRO PRO B . n 
B 1 201 ARG 201 230 230 ARG ARG B . n 
B 1 202 GLY 202 231 231 GLY GLY B . n 
B 1 203 TRP 203 232 232 TRP TRP B . n 
B 1 204 LEU 204 233 233 LEU LEU B . n 
B 1 205 ARG 205 234 234 ARG ARG B . n 
B 1 206 LEU 206 235 235 LEU LEU B . n 
B 1 207 ARG 207 236 236 ARG ARG B . n 
B 1 208 PHE 208 237 237 PHE PHE B . n 
B 1 209 LEU 209 238 238 LEU LEU B . n 
B 1 210 ASN 210 239 239 ASN ASN B . n 
B 1 211 GLY 211 240 240 GLY GLY B . n 
B 1 212 CYS 212 241 241 CYS CYS B . n 
B 1 213 ASN 213 242 242 ASN ASN B . n 
B 1 214 ALA 214 243 243 ALA ALA B . n 
B 1 215 ARG 215 244 244 ARG ARG B . n 
B 1 216 SER 216 245 245 SER SER B . n 
B 1 217 LEU 217 246 246 LEU LEU B . n 
B 1 218 ASN 218 247 247 ASN ASN B . n 
B 1 219 LEU 219 248 248 LEU LEU B . n 
B 1 220 ALA 220 249 249 ALA ALA B . n 
B 1 221 THR 221 250 250 THR THR B . n 
B 1 222 SER 222 251 251 SER SER B . n 
B 1 223 ASP 223 252 252 ASP ASP B . n 
B 1 224 GLY 224 253 253 GLY GLY B . n 
B 1 225 ARG 225 254 254 ARG ARG B . n 
B 1 226 PRO 226 255 255 PRO PRO B . n 
B 1 227 LEU 227 256 256 LEU LEU B . n 
B 1 228 TYR 228 257 257 TYR TYR B . n 
B 1 229 VAL 229 258 258 VAL VAL B . n 
B 1 230 VAL 230 259 259 VAL VAL B . n 
B 1 231 GLY 231 260 260 GLY GLY B . n 
B 1 232 SER 232 261 261 SER SER B . n 
B 1 233 ASP 233 262 262 ASP ASP B . n 
B 1 234 GLY 234 263 263 GLY GLY B . n 
B 1 235 GLY 235 264 264 GLY GLY B . n 
B 1 236 LEU 236 265 265 LEU LEU B . n 
B 1 237 LEU 237 266 266 LEU LEU B . n 
B 1 238 GLY 238 267 267 GLY GLY B . n 
B 1 239 GLU 239 268 268 GLU GLU B . n 
B 1 240 PRO 240 269 269 PRO PRO B . n 
B 1 241 VAL 241 270 270 VAL VAL B . n 
B 1 242 LYS 242 271 271 LYS LYS B . n 
B 1 243 LEU 243 272 272 LEU LEU B . n 
B 1 244 THR 244 273 273 THR THR B . n 
B 1 245 GLU 245 274 274 GLU GLU B . n 
B 1 246 LEU 246 275 275 LEU LEU B . n 
B 1 247 PRO 247 276 276 PRO PRO B . n 
B 1 248 ILE 248 277 277 ILE ILE B . n 
B 1 249 LEU 249 278 278 LEU LEU B . n 
B 1 250 MET 250 279 279 MET MET B . n 
B 1 251 GLY 251 280 280 GLY GLY B . n 
B 1 252 GLU 252 281 281 GLU GLU B . n 
B 1 253 ARG 253 282 282 ARG ARG B . n 
B 1 254 PHE 254 283 283 PHE PHE B . n 
B 1 255 GLU 255 284 284 GLU GLU B . n 
B 1 256 VAL 256 285 285 VAL VAL B . n 
B 1 257 LEU 257 286 286 LEU LEU B . n 
B 1 258 VAL 258 287 287 VAL VAL B . n 
B 1 259 ASP 259 288 288 ASP ASP B . n 
B 1 260 THR 260 289 289 THR THR B . n 
B 1 261 ARG 261 290 290 ARG ARG B . n 
B 1 262 ASP 262 291 291 ASP ASP B . n 
B 1 263 GLY 263 292 292 GLY GLY B . n 
B 1 264 LYS 264 293 293 LYS LYS B . n 
B 1 265 ALA 265 294 294 ALA ALA B . n 
B 1 266 PHE 266 295 295 PHE PHE B . n 
B 1 267 ASP 267 296 296 ASP ASP B . n 
B 1 268 ILE 268 297 297 ILE ILE B . n 
B 1 269 ILE 269 298 298 ILE ILE B . n 
B 1 270 THR 270 299 299 THR THR B . n 
B 1 271 LEU 271 300 300 LEU LEU B . n 
B 1 272 PRO 272 301 301 PRO PRO B . n 
B 1 273 VAL 273 302 302 VAL VAL B . n 
B 1 274 LYS 274 303 303 LYS LYS B . n 
B 1 275 GLN 275 304 304 GLN GLN B . n 
B 1 276 MET 276 305 305 MET MET B . n 
B 1 277 GLY 277 306 306 GLY GLY B . n 
B 1 278 MET 278 307 307 MET MET B . n 
B 1 279 THR 279 308 308 THR THR B . n 
B 1 280 LEU 280 309 309 LEU LEU B . n 
B 1 281 PRO 281 310 310 PRO PRO B . n 
B 1 282 PRO 282 311 311 PRO PRO B . n 
B 1 283 PHE 283 312 312 PHE PHE B . n 
B 1 284 ASP 284 313 313 ASP ASP B . n 
B 1 285 ARG 285 314 314 ARG ARG B . n 
B 1 286 ALA 286 315 315 ALA ALA B . n 
B 1 287 LEU 287 316 316 LEU LEU B . n 
B 1 288 PRO 288 317 317 PRO PRO B . n 
B 1 289 VAL 289 318 318 VAL VAL B . n 
B 1 290 LEU 290 319 319 LEU LEU B . n 
B 1 291 HIS 291 320 320 HIS HIS B . n 
B 1 292 ILE 292 321 321 ILE ILE B . n 
B 1 293 GLN 293 322 322 GLN GLN B . n 
B 1 294 PRO 294 323 323 PRO PRO B . n 
B 1 295 THR 295 324 324 THR THR B . n 
B 1 296 LEU 296 325 325 LEU LEU B . n 
B 1 297 LYS 297 326 326 LYS LYS B . n 
B 1 298 SER 298 327 327 SER SER B . n 
B 1 299 ASN 299 328 328 ASN ASN B . n 
B 1 300 GLU 300 329 329 GLU GLU B . n 
B 1 301 ALA 301 330 330 ALA ALA B . n 
B 1 302 LYS 302 331 331 LYS LYS B . n 
B 1 303 LEU 303 332 332 LEU LEU B . n 
B 1 304 PRO 304 333 333 PRO PRO B . n 
B 1 305 ASP 305 334 334 ASP ASP B . n 
B 1 306 ALA 306 335 335 ALA ALA B . n 
B 1 307 LEU 307 336 336 LEU LEU B . n 
B 1 308 VAL 308 337 337 VAL VAL B . n 
B 1 309 ASN 309 338 338 ASN ASN B . n 
B 1 310 MET 310 339 339 MET MET B . n 
B 1 311 PRO 311 340 340 PRO PRO B . n 
B 1 312 ALA 312 341 341 ALA ALA B . n 
B 1 313 VAL 313 342 342 VAL VAL B . n 
B 1 314 PRO 314 343 343 PRO PRO B . n 
B 1 315 ALA 315 344 344 ALA ALA B . n 
B 1 316 ALA 316 345 345 ALA ALA B . n 
B 1 317 ASP 317 346 346 ASP ASP B . n 
B 1 318 ASN 318 347 347 ASN ASN B . n 
B 1 319 VAL 319 348 348 VAL VAL B . n 
B 1 320 LYS 320 349 349 LYS LYS B . n 
B 1 321 THR 321 350 350 THR THR B . n 
B 1 322 ARG 322 351 351 ARG ARG B . n 
B 1 323 TRP 323 352 352 TRP TRP B . n 
B 1 324 LEU 324 353 353 LEU LEU B . n 
B 1 325 GLN 325 354 354 GLN GLN B . n 
B 1 326 LEU 326 355 355 LEU LEU B . n 
B 1 327 MET 327 356 356 MET MET B . n 
B 1 328 MET 328 357 357 MET MET B . n 
B 1 329 ASP 329 358 358 ASP ASP B . n 
B 1 330 GLY 330 358 358 GLY GLY B A n 
B 1 331 GLY 331 358 358 GLY GLY B B n 
B 1 332 GLY 332 431 431 GLY GLY B . n 
B 1 333 ASN 333 432 432 ASN ASN B . n 
B 1 334 LYS 334 433 433 LYS LYS B . n 
B 1 335 ILE 335 434 434 ILE ILE B . n 
B 1 336 ASN 336 435 435 ASN ASN B . n 
B 1 337 GLY 337 436 436 GLY GLY B . n 
B 1 338 ILE 338 437 437 ILE ILE B . n 
B 1 339 ALA 339 438 438 ALA ALA B . n 
B 1 340 PHE 340 439 439 PHE PHE B . n 
B 1 341 ASP 341 440 440 ASP ASP B . n 
B 1 342 MET 342 441 441 MET MET B . n 
B 1 343 ALA 343 442 442 ALA ALA B . n 
B 1 344 LYS 344 443 443 LYS LYS B . n 
B 1 345 PRO 345 444 444 PRO PRO B . n 
B 1 346 MET 346 445 445 MET MET B . n 
B 1 347 PHE 347 446 446 PHE PHE B . n 
B 1 348 ASP 348 447 447 ASP ASP B . n 
B 1 349 VAL 349 448 448 VAL VAL B . n 
B 1 350 LYS 350 449 449 LYS LYS B . n 
B 1 351 ARG 351 450 450 ARG ARG B . n 
B 1 352 GLY 352 451 451 GLY GLY B . n 
B 1 353 THR 353 452 452 THR THR B . n 
B 1 354 TYR 354 453 453 TYR TYR B . n 
B 1 355 GLU 355 454 454 GLU GLU B . n 
B 1 356 LYS 356 455 455 LYS LYS B . n 
B 1 357 TRP 357 456 456 TRP TRP B . n 
B 1 358 THR 358 457 457 THR THR B . n 
B 1 359 ILE 359 458 458 ILE ILE B . n 
B 1 360 SER 360 459 459 SER SER B . n 
B 1 361 GLY 361 460 460 GLY GLY B . n 
B 1 362 GLU 362 461 461 GLU GLU B . n 
B 1 363 GLY 363 462 462 GLY GLY B . n 
B 1 364 ASP 364 463 463 ASP ASP B . n 
B 1 365 MET 365 464 464 MET MET B . n 
B 1 366 MET 366 465 465 MET MET B . n 
B 1 367 LEU 367 466 466 LEU LEU B . n 
B 1 368 HIS 368 467 467 HIS HIS B . n 
B 1 369 PRO 369 468 468 PRO PRO B . n 
B 1 370 PHE 370 469 469 PHE PHE B . n 
B 1 371 HIS 371 470 470 HIS HIS B . n 
B 1 372 ILE 372 471 471 ILE ILE B . n 
B 1 373 HIS 373 472 472 HIS HIS B . n 
B 1 374 GLY 374 473 473 GLY GLY B . n 
B 1 375 THR 375 474 474 THR THR B . n 
B 1 376 GLN 376 475 475 GLN GLN B . n 
B 1 377 PHE 377 476 476 PHE PHE B . n 
B 1 378 ARG 378 477 477 ARG ARG B . n 
B 1 379 ILE 379 478 478 ILE ILE B . n 
B 1 380 LEU 380 479 479 LEU LEU B . n 
B 1 381 SER 381 480 480 SER SER B . n 
B 1 382 GLU 382 481 481 GLU GLU B . n 
B 1 383 ASN 383 482 482 ASN ASN B . n 
B 1 384 GLY 384 483 483 GLY GLY B . n 
B 1 385 LYS 385 484 484 LYS LYS B . n 
B 1 386 PRO 386 485 485 PRO PRO B . n 
B 1 387 PRO 387 486 486 PRO PRO B . n 
B 1 388 ALA 388 487 487 ALA ALA B . n 
B 1 389 ALA 389 488 488 ALA ALA B . n 
B 1 390 HIS 390 489 489 HIS HIS B . n 
B 1 391 ARG 391 490 490 ARG ARG B . n 
B 1 392 SER 392 491 491 SER SER B . n 
B 1 393 GLY 393 492 492 GLY GLY B . n 
B 1 394 TRP 394 493 493 TRP TRP B . n 
B 1 395 LYS 395 494 494 LYS LYS B . n 
B 1 396 ASP 396 495 495 ASP ASP B . n 
B 1 397 THR 397 496 496 THR THR B . n 
B 1 398 VAL 398 497 497 VAL VAL B . n 
B 1 399 ARG 399 498 498 ARG ARG B . n 
B 1 400 VAL 400 499 499 VAL VAL B . n 
B 1 401 GLU 401 500 500 GLU GLU B . n 
B 1 402 GLY 402 501 501 GLY GLY B . n 
B 1 403 TRP 403 502 502 TRP TRP B . n 
B 1 404 ARG 404 503 503 ARG ARG B . n 
B 1 405 SER 405 504 504 SER SER B . n 
B 1 406 GLU 406 505 505 GLU GLU B . n 
B 1 407 VAL 407 506 506 VAL VAL B . n 
B 1 408 LEU 408 507 507 LEU LEU B . n 
B 1 409 VAL 409 508 508 VAL VAL B . n 
B 1 410 LYS 410 509 509 LYS LYS B . n 
B 1 411 PHE 411 510 510 PHE PHE B . n 
B 1 412 ASP 412 511 511 ASP ASP B . n 
B 1 413 HIS 413 512 512 HIS HIS B . n 
B 1 414 GLU 414 513 513 GLU GLU B . n 
B 1 415 ALA 415 514 514 ALA ALA B . n 
B 1 416 PRO 416 515 515 PRO PRO B . n 
B 1 417 LYS 417 516 516 LYS LYS B . n 
B 1 418 GLU 418 517 517 GLU GLU B . n 
B 1 419 ARG 419 518 518 ARG ARG B . n 
B 1 420 ALA 420 519 519 ALA ALA B . n 
B 1 421 TYR 421 520 520 TYR TYR B . n 
B 1 422 MET 422 521 521 MET MET B . n 
B 1 423 ALA 423 522 522 ALA ALA B . n 
B 1 424 HIS 424 523 523 HIS HIS B . n 
B 1 425 CYS 425 524 524 CYS CYS B . n 
B 1 426 HIS 426 525 525 HIS HIS B . n 
B 1 427 LEU 427 526 526 LEU LEU B . n 
B 1 428 LEU 428 527 527 LEU LEU B . n 
B 1 429 GLU 429 528 528 GLU GLU B . n 
B 1 430 HIS 430 529 529 HIS HIS B . n 
B 1 431 GLU 431 530 530 GLU GLU B . n 
B 1 432 ASP 432 531 531 ASP ASP B . n 
B 1 433 THR 433 532 532 THR THR B . n 
B 1 434 GLY 434 533 533 GLY GLY B . n 
B 1 435 MET 435 534 534 MET MET B . n 
B 1 436 MET 436 535 535 MET MET B . n 
B 1 437 MET 437 536 536 MET MET B . n 
B 1 438 SER 438 537 537 SER SER B . n 
B 1 439 PHE 439 538 538 PHE PHE B . n 
B 1 440 THR 440 539 539 THR THR B . n 
B 1 441 VAL 441 540 540 VAL VAL B . n 
B 1 442 SER 442 541 541 SER SER B . n 
B 1 443 SER 443 542 ?   ?   ?   B . n 
B 1 444 ALA 444 543 ?   ?   ?   B . n 
B 1 445 TRP 445 544 ?   ?   ?   B . n 
B 1 446 SER 446 545 ?   ?   ?   B . n 
B 1 447 HIS 447 546 ?   ?   ?   B . n 
B 1 448 PRO 448 547 ?   ?   ?   B . n 
B 1 449 GLN 449 548 ?   ?   ?   B . n 
B 1 450 PHE 450 549 ?   ?   ?   B . n 
B 1 451 GLU 451 550 ?   ?   ?   B . n 
B 1 452 LYS 452 551 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        CU 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   CU 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 CU  1  601 601 CU  CU  A . 
D 2 CU  1  602 602 CU  CU  A . 
E 2 CU  1  603 603 CU  CU  A . 
F 2 CU  1  604 604 CU  CU  A . 
G 3 EDO 1  605 5   EDO EDO A . 
H 3 EDO 1  606 6   EDO EDO A . 
I 3 EDO 1  607 7   EDO EDO A . 
J 3 EDO 1  608 10  EDO EDO A . 
K 3 EDO 1  609 12  EDO EDO A . 
L 2 CU  1  601 601 CU  CU  B . 
M 2 CU  1  602 602 CU  CU  B . 
N 2 CU  1  603 603 CU  CU  B . 
O 2 CU  1  604 604 CU  CU  B . 
P 3 EDO 1  605 1   EDO EDO B . 
Q 3 EDO 1  606 2   EDO EDO B . 
R 3 EDO 1  607 3   EDO EDO B . 
S 3 EDO 1  608 4   EDO EDO B . 
T 3 EDO 1  609 8   EDO EDO B . 
U 3 EDO 1  610 9   EDO EDO B . 
V 3 EDO 1  611 11  EDO EDO B . 
W 4 HOH 1  701 32  HOH HOH A . 
W 4 HOH 2  702 7   HOH HOH A . 
W 4 HOH 3  703 17  HOH HOH A . 
W 4 HOH 4  704 36  HOH HOH A . 
W 4 HOH 5  705 19  HOH HOH A . 
W 4 HOH 6  706 140 HOH HOH A . 
W 4 HOH 7  707 120 HOH HOH A . 
W 4 HOH 8  708 139 HOH HOH A . 
W 4 HOH 9  709 52  HOH HOH A . 
W 4 HOH 10 710 47  HOH HOH A . 
W 4 HOH 11 711 25  HOH HOH A . 
W 4 HOH 12 712 96  HOH HOH A . 
W 4 HOH 13 713 143 HOH HOH A . 
W 4 HOH 14 714 38  HOH HOH A . 
W 4 HOH 15 715 20  HOH HOH A . 
W 4 HOH 16 716 12  HOH HOH A . 
W 4 HOH 17 717 50  HOH HOH A . 
W 4 HOH 18 718 70  HOH HOH A . 
W 4 HOH 19 719 113 HOH HOH A . 
W 4 HOH 20 720 128 HOH HOH A . 
W 4 HOH 21 721 66  HOH HOH A . 
W 4 HOH 22 722 127 HOH HOH A . 
W 4 HOH 23 723 4   HOH HOH A . 
W 4 HOH 24 724 94  HOH HOH A . 
W 4 HOH 25 725 83  HOH HOH A . 
W 4 HOH 26 726 107 HOH HOH A . 
W 4 HOH 27 727 10  HOH HOH A . 
W 4 HOH 28 728 40  HOH HOH A . 
W 4 HOH 29 729 79  HOH HOH A . 
W 4 HOH 30 730 45  HOH HOH A . 
W 4 HOH 31 731 68  HOH HOH A . 
W 4 HOH 32 732 28  HOH HOH A . 
W 4 HOH 33 733 105 HOH HOH A . 
W 4 HOH 34 734 133 HOH HOH A . 
W 4 HOH 35 735 137 HOH HOH A . 
W 4 HOH 36 736 118 HOH HOH A . 
W 4 HOH 37 737 103 HOH HOH A . 
W 4 HOH 38 738 24  HOH HOH A . 
W 4 HOH 39 739 3   HOH HOH A . 
W 4 HOH 40 740 15  HOH HOH A . 
W 4 HOH 41 741 112 HOH HOH A . 
W 4 HOH 42 742 55  HOH HOH A . 
W 4 HOH 43 743 11  HOH HOH A . 
W 4 HOH 44 744 119 HOH HOH A . 
W 4 HOH 45 745 73  HOH HOH A . 
W 4 HOH 46 746 86  HOH HOH A . 
W 4 HOH 47 747 90  HOH HOH A . 
W 4 HOH 48 748 93  HOH HOH A . 
W 4 HOH 49 749 126 HOH HOH A . 
W 4 HOH 50 750 88  HOH HOH A . 
W 4 HOH 51 751 95  HOH HOH A . 
W 4 HOH 52 752 44  HOH HOH A . 
W 4 HOH 53 753 121 HOH HOH A . 
W 4 HOH 54 754 37  HOH HOH A . 
W 4 HOH 55 755 115 HOH HOH A . 
W 4 HOH 56 756 21  HOH HOH A . 
W 4 HOH 57 757 18  HOH HOH A . 
W 4 HOH 58 758 61  HOH HOH A . 
W 4 HOH 59 759 77  HOH HOH A . 
W 4 HOH 60 760 58  HOH HOH A . 
W 4 HOH 61 761 9   HOH HOH A . 
W 4 HOH 62 762 142 HOH HOH A . 
W 4 HOH 63 763 62  HOH HOH A . 
W 4 HOH 64 764 30  HOH HOH A . 
W 4 HOH 65 765 57  HOH HOH A . 
W 4 HOH 66 766 72  HOH HOH A . 
W 4 HOH 67 767 91  HOH HOH A . 
W 4 HOH 68 768 26  HOH HOH A . 
W 4 HOH 69 769 27  HOH HOH A . 
W 4 HOH 70 770 125 HOH HOH A . 
W 4 HOH 71 771 116 HOH HOH A . 
W 4 HOH 72 772 75  HOH HOH A . 
W 4 HOH 73 773 13  HOH HOH A . 
W 4 HOH 74 774 84  HOH HOH A . 
W 4 HOH 75 775 124 HOH HOH A . 
X 4 HOH 1  701 85  HOH HOH B . 
X 4 HOH 2  702 135 HOH HOH B . 
X 4 HOH 3  703 141 HOH HOH B . 
X 4 HOH 4  704 31  HOH HOH B . 
X 4 HOH 5  705 114 HOH HOH B . 
X 4 HOH 6  706 60  HOH HOH B . 
X 4 HOH 7  707 136 HOH HOH B . 
X 4 HOH 8  708 123 HOH HOH B . 
X 4 HOH 9  709 48  HOH HOH B . 
X 4 HOH 10 710 5   HOH HOH B . 
X 4 HOH 11 711 97  HOH HOH B . 
X 4 HOH 12 712 34  HOH HOH B . 
X 4 HOH 13 713 16  HOH HOH B . 
X 4 HOH 14 714 122 HOH HOH B . 
X 4 HOH 15 715 59  HOH HOH B . 
X 4 HOH 16 716 98  HOH HOH B . 
X 4 HOH 17 717 81  HOH HOH B . 
X 4 HOH 18 718 117 HOH HOH B . 
X 4 HOH 19 719 80  HOH HOH B . 
X 4 HOH 20 720 6   HOH HOH B . 
X 4 HOH 21 721 14  HOH HOH B . 
X 4 HOH 22 722 1   HOH HOH B . 
X 4 HOH 23 723 110 HOH HOH B . 
X 4 HOH 24 724 39  HOH HOH B . 
X 4 HOH 25 725 138 HOH HOH B . 
X 4 HOH 26 726 8   HOH HOH B . 
X 4 HOH 27 727 42  HOH HOH B . 
X 4 HOH 28 728 53  HOH HOH B . 
X 4 HOH 29 729 87  HOH HOH B . 
X 4 HOH 30 730 56  HOH HOH B . 
X 4 HOH 31 731 63  HOH HOH B . 
X 4 HOH 32 732 132 HOH HOH B . 
X 4 HOH 33 733 109 HOH HOH B . 
X 4 HOH 34 734 41  HOH HOH B . 
X 4 HOH 35 735 74  HOH HOH B . 
X 4 HOH 36 736 46  HOH HOH B . 
X 4 HOH 37 737 69  HOH HOH B . 
X 4 HOH 38 738 106 HOH HOH B . 
X 4 HOH 39 739 29  HOH HOH B . 
X 4 HOH 40 740 54  HOH HOH B . 
X 4 HOH 41 741 92  HOH HOH B . 
X 4 HOH 42 742 33  HOH HOH B . 
X 4 HOH 43 743 104 HOH HOH B . 
X 4 HOH 44 744 71  HOH HOH B . 
X 4 HOH 45 745 101 HOH HOH B . 
X 4 HOH 46 746 108 HOH HOH B . 
X 4 HOH 47 747 100 HOH HOH B . 
X 4 HOH 48 748 2   HOH HOH B . 
X 4 HOH 49 749 129 HOH HOH B . 
X 4 HOH 50 750 76  HOH HOH B . 
X 4 HOH 51 751 65  HOH HOH B . 
X 4 HOH 52 752 67  HOH HOH B . 
X 4 HOH 53 753 99  HOH HOH B . 
X 4 HOH 54 754 130 HOH HOH B . 
X 4 HOH 55 755 89  HOH HOH B . 
X 4 HOH 56 756 131 HOH HOH B . 
X 4 HOH 57 757 43  HOH HOH B . 
X 4 HOH 58 758 82  HOH HOH B . 
X 4 HOH 59 759 134 HOH HOH B . 
X 4 HOH 60 760 49  HOH HOH B . 
X 4 HOH 61 761 51  HOH HOH B . 
X 4 HOH 62 762 102 HOH HOH B . 
X 4 HOH 63 763 23  HOH HOH B . 
X 4 HOH 64 764 111 HOH HOH B . 
X 4 HOH 65 765 35  HOH HOH B . 
X 4 HOH 66 766 78  HOH HOH B . 
X 4 HOH 67 767 64  HOH HOH B . 
X 4 HOH 68 768 22  HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER ? ? ? '2.10.4 (26-JUL-2023)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .                      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8R4H 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     169.273 
_cell.length_a_esd                 ? 
_cell.length_b                     169.273 
_cell.length_b_esd                 ? 
_cell.length_c                     90.387 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        18 
_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                         8R4H 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'H 3' 
_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                   8R4H 
_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             2.50 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.80 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              9.5 
_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    
;100 mM CHES/ Sodium hydroxide pH 9.5
200 mM Sodium chloride
1260 mM Ammonium sulfate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-06 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97856 
_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                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97856 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8R4H 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.937 
_reflns.d_resolution_low                               48.46 
_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                                     20565 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.94 
_reflns_shell.d_res_low                                     3.1 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3008 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.642 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -6.91590 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            -6.91590 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            13.83180 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               72.82 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.933 
_refine.correlation_coeff_Fo_to_Fc_free          0.899 
_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                                 8R4H 
_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                            2.937 
_refine.ls_d_res_low                             30.23 
_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                     20551 
_refine.ls_number_reflns_R_free                  1014 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.7 
_refine.ls_percent_reflns_R_free                 4.930 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2002 
_refine.ls_R_factor_R_free                       0.2451 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1979 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.404 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        8R4H 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.36 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.937 
_refine_hist.d_res_low                        30.23 
_refine_hist.number_atoms_solvent             143 
_refine_hist.number_atoms_total               7023 
_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        6824 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         56 
_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' ? 0.007 ? 7042 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 0.93  ? 9552 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2390 ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 1168 ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 7042 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 2.69  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 17.79 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 904  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 5749 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.94 
_refine_ls_shell.d_res_low                        2.96 
_refine_ls_shell.number_reflns_all                412 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             390 
_refine_ls_shell.percent_reflns_obs               87.79 
_refine_ls_shell.percent_reflns_R_free            5.34 
_refine_ls_shell.R_factor_all                     0.3099 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.3033 
_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   51 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.4451 
# 
_struct.entry_id                     8R4H 
_struct.title                        
'Crystal structure of the copper efflux oxidase (CueO) from Hafnia alvei deleted of the Met-rich domain' 
_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        8R4H 
_struct_keywords.text            'bacterial copper hemostasis, multi copper oxidase, METAL BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'METAL BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 2 ? 
M N N 2 ? 
N N N 2 ? 
O N N 2 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 3 ? 
S N N 3 ? 
T N N 3 ? 
U N N 3 ? 
V N N 3 ? 
W N N 4 ? 
X N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP A0A377PPH3_HAFAL A0A377PPH3 ? 1 
;AEHPTLPIPALLTPDAAGKIALNVQTGSMKWKAGMQTPTWGINGPLLGPAMRLQRGKDVAINVTNALPEATTMHWHGMEI
PGTSDGGPQAVIEPGKMWTAEIKVDQPATTAWFHPHTHGLTGRQVAMGLGGLIIIDDEESTKLPLPKEWGVDDVPVILQD
KRLDAKGHIDYQLDIITAAVGWFGDMMLTNGTVYPQHLAPRGWLRLRFLNGCNARSLNLATSDGRPLYVVGSDGGLLGEP
VKLTELPILMGERFEVLVDTRDGKAFDIITLPVKQMGMTLPPFDRALPVLHIQPTLKSNEAKLPDALVNMPAVPAADNVK
TRWLQLMMD
;
29  
2 UNP A0A097R5T5_HAFAL A0A097R5T5 ? 1 
;GNKINGIAFDMAKPMFDVKRGTYEKWTISGEGDMMLHPFHIHGIQFRILSENGKPPAAHRSGWKDTVRVEGWRSEVLVKF
DHEAPKERAYMAHCHLLEHEDTGMMMSFTVS
;
430 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8R4H A 1   ? 329 ? A0A377PPH3 29  ? 357 ? 30  358 
2 2 8R4H A 332 ? 442 ? A0A097R5T5 430 ? 540 ? 431 541 
3 1 8R4H B 1   ? 329 ? A0A377PPH3 29  ? 357 ? 30  358 
4 2 8R4H B 332 ? 442 ? A0A097R5T5 430 ? 540 ? 431 541 
# 
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 8R4H GLY A 330 A UNP A0A377PPH3 ?   ?   linker           358 1  
1 8R4H GLY A 331 B UNP A0A377PPH3 ?   ?   linker           358 2  
2 8R4H THR A 375 ? UNP A0A097R5T5 ILE 473 conflict         474 3  
2 8R4H SER A 443 ? UNP A0A097R5T5 ?   ?   'expression tag' 542 4  
2 8R4H ALA A 444 ? UNP A0A097R5T5 ?   ?   'expression tag' 543 5  
2 8R4H TRP A 445 ? UNP A0A097R5T5 ?   ?   'expression tag' 544 6  
2 8R4H SER A 446 ? UNP A0A097R5T5 ?   ?   'expression tag' 545 7  
2 8R4H HIS A 447 ? UNP A0A097R5T5 ?   ?   'expression tag' 546 8  
2 8R4H PRO A 448 ? UNP A0A097R5T5 ?   ?   'expression tag' 547 9  
2 8R4H GLN A 449 ? UNP A0A097R5T5 ?   ?   'expression tag' 548 10 
2 8R4H PHE A 450 ? UNP A0A097R5T5 ?   ?   'expression tag' 549 11 
2 8R4H GLU A 451 ? UNP A0A097R5T5 ?   ?   'expression tag' 550 12 
2 8R4H LYS A 452 ? UNP A0A097R5T5 ?   ?   'expression tag' 551 13 
3 8R4H GLY B 330 A UNP A0A377PPH3 ?   ?   linker           358 14 
3 8R4H GLY B 331 B UNP A0A377PPH3 ?   ?   linker           358 15 
4 8R4H THR B 375 ? UNP A0A097R5T5 ILE 473 conflict         474 16 
4 8R4H SER B 443 ? UNP A0A097R5T5 ?   ?   'expression tag' 542 17 
4 8R4H ALA B 444 ? UNP A0A097R5T5 ?   ?   'expression tag' 543 18 
4 8R4H TRP B 445 ? UNP A0A097R5T5 ?   ?   'expression tag' 544 19 
4 8R4H SER B 446 ? UNP A0A097R5T5 ?   ?   'expression tag' 545 20 
4 8R4H HIS B 447 ? UNP A0A097R5T5 ?   ?   'expression tag' 546 21 
4 8R4H PRO B 448 ? UNP A0A097R5T5 ?   ?   'expression tag' 547 22 
4 8R4H GLN B 449 ? UNP A0A097R5T5 ?   ?   'expression tag' 548 23 
4 8R4H PHE B 450 ? UNP A0A097R5T5 ?   ?   'expression tag' 549 24 
4 8R4H GLU B 451 ? UNP A0A097R5T5 ?   ?   'expression tag' 550 25 
4 8R4H LYS B 452 ? UNP A0A097R5T5 ?   ?   'expression tag' 551 26 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,J,K,W     
2 1 B,L,M,N,O,P,Q,R,S,T,U,V,X 
# 
_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 LEU A 120 ? GLY A 128 ? LEU A 149 GLY A 157 1 ? 9 
HELX_P HELX_P2 AA2 ASP A 137 ? LEU A 143 ? ASP A 166 LEU A 172 1 ? 7 
HELX_P HELX_P3 AA3 ASP A 174 ? VAL A 180 ? ASP A 203 VAL A 209 1 ? 7 
HELX_P HELX_P4 AA4 LEU A 427 ? THR A 433 ? LEU A 526 THR A 532 1 ? 7 
HELX_P HELX_P5 AA5 LEU B 120 ? GLY B 128 ? LEU B 149 GLY B 157 1 ? 9 
HELX_P HELX_P6 AA6 ASP B 137 ? LEU B 143 ? ASP B 166 LEU B 172 1 ? 7 
HELX_P HELX_P7 AA7 ASP B 174 ? VAL B 180 ? ASP B 203 VAL B 209 1 ? 7 
HELX_P HELX_P8 AA8 LEU B 427 ? THR B 433 ? LEU B 526 THR B 532 1 ? 7 
# 
_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 HIS 74  NE2 ? ? ? 1_555 E CU . CU ? ? A HIS 103 A CU 603 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc2  metalc ? ? A HIS 76  ND1 ? ? ? 1_555 C CU . CU ? ? A HIS 105 A CU 601 1_555 ? ? ? ? ? ? ? 1.852 ? ? 
metalc3  metalc ? ? A HIS 114 NE2 ? ? ? 1_555 C CU . CU ? ? A HIS 143 A CU 601 1_555 ? ? ? ? ? ? ? 1.903 ? ? 
metalc4  metalc ? ? A HIS 116 NE2 ? ? ? 1_555 D CU . CU ? ? A HIS 145 A CU 602 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc5  metalc ? ? A HIS 368 ND1 ? ? ? 1_555 F CU . CU ? ? A HIS 467 A CU 604 1_555 ? ? ? ? ? ? ? 1.832 ? ? 
metalc6  metalc ? ? A HIS 371 NE2 ? ? ? 1_555 E CU . CU ? ? A HIS 470 A CU 603 1_555 ? ? ? ? ? ? ? 1.736 ? ? 
metalc7  metalc ? ? A HIS 373 NE2 ? ? ? 1_555 D CU . CU ? ? A HIS 472 A CU 602 1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc8  metalc ? ? A HIS 424 NE2 ? ? ? 1_555 D CU . CU ? ? A HIS 523 A CU 602 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
metalc9  metalc ? ? A CYS 425 SG  ? ? ? 1_555 F CU . CU ? ? A CYS 524 A CU 604 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
metalc10 metalc ? ? A HIS 426 NE2 ? ? ? 1_555 C CU . CU ? ? A HIS 525 A CU 601 1_555 ? ? ? ? ? ? ? 2.267 ? ? 
metalc11 metalc ? ? A HIS 430 ND1 ? ? ? 1_555 F CU . CU ? ? A HIS 529 A CU 604 1_555 ? ? ? ? ? ? ? 1.865 ? ? 
metalc12 metalc ? ? B HIS 74  NE2 ? ? ? 1_555 N CU . CU ? ? B HIS 103 B CU 603 1_555 ? ? ? ? ? ? ? 1.944 ? ? 
metalc13 metalc ? ? B HIS 76  ND1 ? ? ? 1_555 L CU . CU ? ? B HIS 105 B CU 601 1_555 ? ? ? ? ? ? ? 1.823 ? ? 
metalc14 metalc ? ? B HIS 114 NE2 ? ? ? 1_555 L CU . CU ? ? B HIS 143 B CU 601 1_555 ? ? ? ? ? ? ? 1.894 ? ? 
metalc15 metalc ? ? B HIS 116 NE2 ? ? ? 1_555 M CU . CU ? ? B HIS 145 B CU 602 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
metalc16 metalc ? ? B HIS 368 ND1 ? ? ? 1_555 O CU . CU ? ? B HIS 467 B CU 604 1_555 ? ? ? ? ? ? ? 1.823 ? ? 
metalc17 metalc ? ? B HIS 371 NE2 ? ? ? 1_555 N CU . CU ? ? B HIS 470 B CU 603 1_555 ? ? ? ? ? ? ? 1.800 ? ? 
metalc18 metalc ? ? B HIS 373 NE2 ? ? ? 1_555 M CU . CU ? ? B HIS 472 B CU 602 1_555 ? ? ? ? ? ? ? 2.247 ? ? 
metalc19 metalc ? ? B HIS 424 NE2 ? ? ? 1_555 M CU . CU ? ? B HIS 523 B CU 602 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc20 metalc ? ? B CYS 425 SG  ? ? ? 1_555 O CU . CU ? ? B CYS 524 B CU 604 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
metalc21 metalc ? ? B HIS 426 NE2 ? ? ? 1_555 L CU . CU ? ? B HIS 525 B CU 601 1_555 ? ? ? ? ? ? ? 2.380 ? ? 
metalc22 metalc ? ? B HIS 430 ND1 ? ? ? 1_555 O CU . CU ? ? B HIS 529 B CU 604 1_555 ? ? ? ? ? ? ? 1.882 ? ? 
# 
_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  NE2 ? A HIS 74  ? A HIS 103 ? 1_555 CU ? E CU . ? A CU 603 ? 1_555 NE2 ? A HIS 371 ? A HIS 470 ? 1_555 138.1 ? 
2  ND1 ? A HIS 76  ? A HIS 105 ? 1_555 CU ? C CU . ? A CU 601 ? 1_555 NE2 ? A HIS 114 ? A HIS 143 ? 1_555 126.9 ? 
3  ND1 ? A HIS 76  ? A HIS 105 ? 1_555 CU ? C CU . ? A CU 601 ? 1_555 NE2 ? A HIS 426 ? A HIS 525 ? 1_555 104.0 ? 
4  NE2 ? A HIS 114 ? A HIS 143 ? 1_555 CU ? C CU . ? A CU 601 ? 1_555 NE2 ? A HIS 426 ? A HIS 525 ? 1_555 119.4 ? 
5  NE2 ? A HIS 116 ? A HIS 145 ? 1_555 CU ? D CU . ? A CU 602 ? 1_555 NE2 ? A HIS 373 ? A HIS 472 ? 1_555 86.2  ? 
6  NE2 ? A HIS 116 ? A HIS 145 ? 1_555 CU ? D CU . ? A CU 602 ? 1_555 NE2 ? A HIS 424 ? A HIS 523 ? 1_555 88.4  ? 
7  NE2 ? A HIS 373 ? A HIS 472 ? 1_555 CU ? D CU . ? A CU 602 ? 1_555 NE2 ? A HIS 424 ? A HIS 523 ? 1_555 84.2  ? 
8  ND1 ? A HIS 368 ? A HIS 467 ? 1_555 CU ? F CU . ? A CU 604 ? 1_555 SG  ? A CYS 425 ? A CYS 524 ? 1_555 108.6 ? 
9  ND1 ? A HIS 368 ? A HIS 467 ? 1_555 CU ? F CU . ? A CU 604 ? 1_555 ND1 ? A HIS 430 ? A HIS 529 ? 1_555 130.3 ? 
10 SG  ? A CYS 425 ? A CYS 524 ? 1_555 CU ? F CU . ? A CU 604 ? 1_555 ND1 ? A HIS 430 ? A HIS 529 ? 1_555 121.0 ? 
11 NE2 ? B HIS 74  ? B HIS 103 ? 1_555 CU ? N CU . ? B CU 603 ? 1_555 NE2 ? B HIS 371 ? B HIS 470 ? 1_555 138.5 ? 
12 ND1 ? B HIS 76  ? B HIS 105 ? 1_555 CU ? L CU . ? B CU 601 ? 1_555 NE2 ? B HIS 114 ? B HIS 143 ? 1_555 129.6 ? 
13 ND1 ? B HIS 76  ? B HIS 105 ? 1_555 CU ? L CU . ? B CU 601 ? 1_555 NE2 ? B HIS 426 ? B HIS 525 ? 1_555 100.3 ? 
14 NE2 ? B HIS 114 ? B HIS 143 ? 1_555 CU ? L CU . ? B CU 601 ? 1_555 NE2 ? B HIS 426 ? B HIS 525 ? 1_555 114.5 ? 
15 NE2 ? B HIS 116 ? B HIS 145 ? 1_555 CU ? M CU . ? B CU 602 ? 1_555 NE2 ? B HIS 373 ? B HIS 472 ? 1_555 86.1  ? 
16 NE2 ? B HIS 116 ? B HIS 145 ? 1_555 CU ? M CU . ? B CU 602 ? 1_555 NE2 ? B HIS 424 ? B HIS 523 ? 1_555 88.6  ? 
17 NE2 ? B HIS 373 ? B HIS 472 ? 1_555 CU ? M CU . ? B CU 602 ? 1_555 NE2 ? B HIS 424 ? B HIS 523 ? 1_555 84.6  ? 
18 ND1 ? B HIS 368 ? B HIS 467 ? 1_555 CU ? O CU . ? B CU 604 ? 1_555 SG  ? B CYS 425 ? B CYS 524 ? 1_555 109.2 ? 
19 ND1 ? B HIS 368 ? B HIS 467 ? 1_555 CU ? O CU . ? B CU 604 ? 1_555 ND1 ? B HIS 430 ? B HIS 529 ? 1_555 130.5 ? 
20 SG  ? B CYS 425 ? B CYS 524 ? 1_555 CU ? O CU . ? B CU 604 ? 1_555 ND1 ? B HIS 430 ? B HIS 529 ? 1_555 120.2 ? 
# 
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 PRO 281 A . ? PRO 310 A PRO 282 A ? PRO 311 A 1 -1.79 
2 PRO 281 B . ? PRO 310 B PRO 282 B ? PRO 311 B 1 2.89  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 6 ? 
AA4 ? 5 ? 
AA5 ? 5 ? 
AA6 ? 5 ? 
AA7 ? 5 ? 
AA8 ? 4 ? 
AA9 ? 6 ? 
AB1 ? 5 ? 
AB2 ? 5 ? 
AB3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? parallel      
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? parallel      
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? parallel      
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB3 1 2 ? parallel      
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? 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 11  ? LEU A 12  ? LEU A 40  LEU A 41  
AA1 2 ALA A 50  ? GLN A 54  ? ALA A 79  GLN A 83  
AA1 3 GLY A 131 ? ASP A 136 ? GLY A 160 ASP A 165 
AA1 4 THR A 110 ? HIS A 114 ? THR A 139 HIS A 143 
AA1 5 HIS A 74  ? HIS A 76  ? HIS A 103 HIS A 105 
AA2 1 GLN A 36  ? ILE A 42  ? GLN A 65  ILE A 71  
AA2 2 LYS A 19  ? LYS A 30  ? LYS A 48  LYS A 59  
AA2 3 ASP A 58  ? ASN A 65  ? ASP A 87  ASN A 94  
AA2 4 MET A 97  ? LYS A 103 ? MET A 126 LYS A 132 
AA3 1 MET A 186 ? THR A 189 ? MET A 215 THR A 218 
AA3 2 ASP A 153 ? LYS A 161 ? ASP A 182 LYS A 190 
AA3 3 TRP A 203 ? ASN A 210 ? TRP A 232 ASN A 239 
AA3 4 ARG A 253 ? ASP A 259 ? ARG A 282 ASP A 288 
AA3 5 LEU A 227 ? SER A 232 ? LEU A 256 SER A 261 
AA3 6 GLY A 235 ? LEU A 243 ? GLY A 264 LEU A 272 
AA4 1 GLN A 196 ? ARG A 201 ? GLN A 225 ARG A 230 
AA4 2 LEU A 287 ? SER A 298 ? LEU A 316 SER A 327 
AA4 3 PHE A 266 ? THR A 270 ? PHE A 295 THR A 299 
AA4 4 LEU A 217 ? THR A 221 ? LEU A 246 THR A 250 
AA4 5 LEU A 246 ? ILE A 248 ? LEU A 275 ILE A 277 
AA5 1 GLY A 332 ? ILE A 335 ? GLY A 431 ILE A 434 
AA5 2 LYS A 320 ? ASP A 329 ? LYS A 349 ASP A 358 
AA5 3 TYR A 354 ? SER A 360 ? TYR A 453 SER A 459 
AA5 4 ARG A 404 ? LYS A 410 ? ARG A 503 LYS A 509 
AA5 5 ARG A 378 ? SER A 381 ? ARG A 477 SER A 480 
AA6 1 ASP A 348 ? LYS A 350 ? ASP A 447 LYS A 449 
AA6 2 MET A 436 ? SER A 442 ? MET A 535 SER A 541 
AA6 3 TYR A 421 ? CYS A 425 ? TYR A 520 CYS A 524 
AA6 4 HIS A 368 ? ILE A 372 ? HIS A 467 ILE A 471 
AA6 5 THR A 397 ? VAL A 400 ? THR A 496 VAL A 499 
AA7 1 LEU B 11  ? LEU B 12  ? LEU B 40  LEU B 41  
AA7 2 ALA B 50  ? GLN B 54  ? ALA B 79  GLN B 83  
AA7 3 GLY B 131 ? ASP B 136 ? GLY B 160 ASP B 165 
AA7 4 THR B 110 ? HIS B 114 ? THR B 139 HIS B 143 
AA7 5 HIS B 74  ? HIS B 76  ? HIS B 103 HIS B 105 
AA8 1 GLN B 36  ? ILE B 42  ? GLN B 65  ILE B 71  
AA8 2 LYS B 19  ? LYS B 30  ? LYS B 48  LYS B 59  
AA8 3 ASP B 58  ? ASN B 65  ? ASP B 87  ASN B 94  
AA8 4 MET B 97  ? LYS B 103 ? MET B 126 LYS B 132 
AA9 1 MET B 186 ? THR B 189 ? MET B 215 THR B 218 
AA9 2 ASP B 153 ? LYS B 161 ? ASP B 182 LYS B 190 
AA9 3 TRP B 203 ? ASN B 210 ? TRP B 232 ASN B 239 
AA9 4 ARG B 253 ? ASP B 259 ? ARG B 282 ASP B 288 
AA9 5 LEU B 227 ? SER B 232 ? LEU B 256 SER B 261 
AA9 6 GLY B 235 ? LEU B 243 ? GLY B 264 LEU B 272 
AB1 1 GLN B 196 ? ARG B 201 ? GLN B 225 ARG B 230 
AB1 2 LEU B 287 ? SER B 298 ? LEU B 316 SER B 327 
AB1 3 PHE B 266 ? THR B 270 ? PHE B 295 THR B 299 
AB1 4 LEU B 217 ? THR B 221 ? LEU B 246 THR B 250 
AB1 5 LEU B 246 ? ILE B 248 ? LEU B 275 ILE B 277 
AB2 1 GLY B 332 ? ILE B 335 ? GLY B 431 ILE B 434 
AB2 2 LYS B 320 ? ASP B 329 ? LYS B 349 ASP B 358 
AB2 3 TYR B 354 ? SER B 360 ? TYR B 453 SER B 459 
AB2 4 ARG B 404 ? LYS B 410 ? ARG B 503 LYS B 509 
AB2 5 ARG B 378 ? SER B 381 ? ARG B 477 SER B 480 
AB3 1 ASP B 348 ? LYS B 350 ? ASP B 447 LYS B 449 
AB3 2 MET B 436 ? SER B 442 ? MET B 535 SER B 541 
AB3 3 TYR B 421 ? CYS B 425 ? TYR B 520 CYS B 524 
AB3 4 HIS B 368 ? ILE B 372 ? HIS B 467 ILE B 471 
AB3 5 THR B 397 ? VAL B 400 ? THR B 496 VAL B 499 
# 
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 LEU A 12  ? N LEU A 41  O ARG A 52  ? O ARG A 81  
AA1 2 3 N LEU A 53  ? N LEU A 82  O ILE A 134 ? O ILE A 163 
AA1 3 4 O ILE A 133 ? O ILE A 162 N ALA A 111 ? N ALA A 140 
AA1 4 5 O HIS A 114 ? O HIS A 143 N HIS A 74  ? N HIS A 103 
AA2 1 2 O GLY A 41  ? O GLY A 70  N GLN A 25  ? N GLN A 54  
AA2 2 3 N LEU A 22  ? N LEU A 51  O THR A 64  ? O THR A 93  
AA2 3 4 N VAL A 59  ? N VAL A 88  O ILE A 102 ? O ILE A 131 
AA3 1 2 O MET A 186 ? O MET A 215 N LYS A 161 ? N LYS A 190 
AA3 2 3 N VAL A 154 ? N VAL A 183 O ARG A 205 ? O ARG A 234 
AA3 3 4 N LEU A 206 ? N LEU A 235 O VAL A 256 ? O VAL A 285 
AA3 4 5 O GLU A 255 ? O GLU A 284 N VAL A 230 ? N VAL A 259 
AA3 5 6 N LEU A 227 ? N LEU A 256 O LEU A 243 ? O LEU A 272 
AA4 1 2 N HIS A 197 ? N HIS A 226 O HIS A 291 ? O HIS A 320 
AA4 2 3 O VAL A 289 ? O VAL A 318 N ILE A 268 ? N ILE A 297 
AA4 3 4 O ILE A 269 ? O ILE A 298 N ALA A 220 ? N ALA A 249 
AA4 4 5 N LEU A 219 ? N LEU A 248 O LEU A 246 ? O LEU A 275 
AA5 1 2 O LYS A 334 ? O LYS A 433 N MET A 327 ? N MET A 356 
AA5 2 3 N LEU A 324 ? N LEU A 353 O THR A 358 ? O THR A 457 
AA5 3 4 N ILE A 359 ? N ILE A 458 O SER A 405 ? O SER A 504 
AA5 4 5 O GLU A 406 ? O GLU A 505 N SER A 381 ? N SER A 480 
AA6 1 2 N VAL A 349 ? N VAL A 448 O THR A 440 ? O THR A 539 
AA6 2 3 O MET A 437 ? O MET A 536 N ALA A 423 ? N ALA A 522 
AA6 3 4 O HIS A 424 ? O HIS A 523 N HIS A 371 ? N HIS A 470 
AA6 4 5 N PHE A 370 ? N PHE A 469 O VAL A 398 ? O VAL A 497 
AA7 1 2 N LEU B 12  ? N LEU B 41  O ARG B 52  ? O ARG B 81  
AA7 2 3 N LEU B 53  ? N LEU B 82  O ILE B 134 ? O ILE B 163 
AA7 3 4 O ILE B 133 ? O ILE B 162 N ALA B 111 ? N ALA B 140 
AA7 4 5 O HIS B 114 ? O HIS B 143 N HIS B 74  ? N HIS B 103 
AA8 1 2 O GLY B 41  ? O GLY B 70  N GLN B 25  ? N GLN B 54  
AA8 2 3 N LEU B 22  ? N LEU B 51  O THR B 64  ? O THR B 93  
AA8 3 4 N VAL B 59  ? N VAL B 88  O ILE B 102 ? O ILE B 131 
AA9 1 2 O MET B 186 ? O MET B 215 N LYS B 161 ? N LYS B 190 
AA9 2 3 N VAL B 154 ? N VAL B 183 O ARG B 205 ? O ARG B 234 
AA9 3 4 N LEU B 206 ? N LEU B 235 O VAL B 256 ? O VAL B 285 
AA9 4 5 O GLU B 255 ? O GLU B 284 N VAL B 230 ? N VAL B 259 
AA9 5 6 N LEU B 227 ? N LEU B 256 O LEU B 243 ? O LEU B 272 
AB1 1 2 N HIS B 197 ? N HIS B 226 O HIS B 291 ? O HIS B 320 
AB1 2 3 O LEU B 290 ? O LEU B 319 N ILE B 268 ? N ILE B 297 
AB1 3 4 O ILE B 269 ? O ILE B 298 N ALA B 220 ? N ALA B 249 
AB1 4 5 N LEU B 219 ? N LEU B 248 O LEU B 246 ? O LEU B 275 
AB2 1 2 O LYS B 334 ? O LYS B 433 N MET B 327 ? N MET B 356 
AB2 2 3 N LEU B 326 ? N LEU B 355 O SER B 360 ? O SER B 459 
AB2 3 4 N ILE B 359 ? N ILE B 458 O SER B 405 ? O SER B 504 
AB2 4 5 O GLU B 406 ? O GLU B 505 N SER B 381 ? N SER B 480 
AB3 1 2 N VAL B 349 ? N VAL B 448 O THR B 440 ? O THR B 539 
AB3 2 3 O MET B 437 ? O MET B 536 N ALA B 423 ? N ALA B 522 
AB3 3 4 O HIS B 424 ? O HIS B 523 N HIS B 371 ? N HIS B 470 
AB3 4 5 N PHE B 370 ? N PHE B 469 O VAL B 398 ? O VAL B 497 
# 
_pdbx_entry_details.entry_id                   8R4H 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LEU A 76  ? ? 53.46   -144.48 
2  1 TRP A 104 ? ? -105.89 79.50   
3  1 ASP A 134 ? ? -146.65 53.27   
4  1 PRO A 173 ? ? -85.05  37.17   
5  1 ASP A 262 ? ? -36.90  -38.11  
6  1 LYS A 303 ? ? -86.70  32.47   
7  1 LEU A 332 ? ? 67.24   78.49   
8  1 LEU A 336 ? ? -93.61  -76.64  
9  1 ASP A 346 ? ? 56.12   -70.67  
10 1 MET A 357 ? ? -113.25 56.74   
11 1 PHE A 439 ? ? -34.23  104.85  
12 1 MET A 445 ? ? -27.00  -48.37  
13 1 ASP A 463 ? ? 173.24  119.49  
14 1 TRP A 502 ? ? -120.61 -157.51 
15 1 LEU B 76  ? ? 53.15   -144.18 
16 1 TRP B 104 ? ? -105.84 79.68   
17 1 ASP B 134 ? ? -146.36 52.86   
18 1 PRO B 173 ? ? -84.33  36.50   
19 1 LEU B 202 ? ? -90.20  55.61   
20 1 ASP B 262 ? ? -37.27  -38.08  
21 1 LEU B 336 ? ? -98.82  -96.45  
22 1 ASN B 347 ? ? -116.15 65.27   
23 1 ASP B 463 ? ? 173.20  119.40  
24 1 TRP B 502 ? ? -120.14 -157.80 
25 1 THR B 532 ? ? -95.18  30.26   
# 
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 SER 542 ? A SER 443 
2  1 Y 1 A ALA 543 ? A ALA 444 
3  1 Y 1 A TRP 544 ? A TRP 445 
4  1 Y 1 A SER 545 ? A SER 446 
5  1 Y 1 A HIS 546 ? A HIS 447 
6  1 Y 1 A PRO 547 ? A PRO 448 
7  1 Y 1 A GLN 548 ? A GLN 449 
8  1 Y 1 A PHE 549 ? A PHE 450 
9  1 Y 1 A GLU 550 ? A GLU 451 
10 1 Y 1 A LYS 551 ? A LYS 452 
11 1 Y 1 B SER 542 ? B SER 443 
12 1 Y 1 B ALA 543 ? B ALA 444 
13 1 Y 1 B TRP 544 ? B TRP 445 
14 1 Y 1 B SER 545 ? B SER 446 
15 1 Y 1 B HIS 546 ? B HIS 447 
16 1 Y 1 B PRO 547 ? B PRO 448 
17 1 Y 1 B GLN 548 ? B GLN 449 
18 1 Y 1 B PHE 549 ? B PHE 450 
19 1 Y 1 B GLU 550 ? B GLU 451 
20 1 Y 1 B LYS 551 ? B LYS 452 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CU  CU   CU N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
EDO C1   C  N N 89  
EDO O1   O  N N 90  
EDO C2   C  N N 91  
EDO O2   O  N N 92  
EDO H11  H  N N 93  
EDO H12  H  N N 94  
EDO HO1  H  N N 95  
EDO H21  H  N N 96  
EDO H22  H  N N 97  
EDO HO2  H  N N 98  
GLN N    N  N N 99  
GLN CA   C  N S 100 
GLN C    C  N N 101 
GLN O    O  N N 102 
GLN CB   C  N N 103 
GLN CG   C  N N 104 
GLN CD   C  N N 105 
GLN OE1  O  N N 106 
GLN NE2  N  N N 107 
GLN OXT  O  N N 108 
GLN H    H  N N 109 
GLN H2   H  N N 110 
GLN HA   H  N N 111 
GLN HB2  H  N N 112 
GLN HB3  H  N N 113 
GLN HG2  H  N N 114 
GLN HG3  H  N N 115 
GLN HE21 H  N N 116 
GLN HE22 H  N N 117 
GLN HXT  H  N N 118 
GLU N    N  N N 119 
GLU CA   C  N S 120 
GLU C    C  N N 121 
GLU O    O  N N 122 
GLU CB   C  N N 123 
GLU CG   C  N N 124 
GLU CD   C  N N 125 
GLU OE1  O  N N 126 
GLU OE2  O  N N 127 
GLU OXT  O  N N 128 
GLU H    H  N N 129 
GLU H2   H  N N 130 
GLU HA   H  N N 131 
GLU HB2  H  N N 132 
GLU HB3  H  N N 133 
GLU HG2  H  N N 134 
GLU HG3  H  N N 135 
GLU HE2  H  N N 136 
GLU HXT  H  N N 137 
GLY N    N  N N 138 
GLY CA   C  N N 139 
GLY C    C  N N 140 
GLY O    O  N N 141 
GLY OXT  O  N N 142 
GLY H    H  N N 143 
GLY H2   H  N N 144 
GLY HA2  H  N N 145 
GLY HA3  H  N N 146 
GLY HXT  H  N N 147 
HIS N    N  N N 148 
HIS CA   C  N S 149 
HIS C    C  N N 150 
HIS O    O  N N 151 
HIS CB   C  N N 152 
HIS CG   C  Y N 153 
HIS ND1  N  Y N 154 
HIS CD2  C  Y N 155 
HIS CE1  C  Y N 156 
HIS NE2  N  Y N 157 
HIS OXT  O  N N 158 
HIS H    H  N N 159 
HIS H2   H  N N 160 
HIS HA   H  N N 161 
HIS HB2  H  N N 162 
HIS HB3  H  N N 163 
HIS HD1  H  N N 164 
HIS HD2  H  N N 165 
HIS HE1  H  N N 166 
HIS HE2  H  N N 167 
HIS HXT  H  N N 168 
HOH O    O  N N 169 
HOH H1   H  N N 170 
HOH H2   H  N N 171 
ILE N    N  N N 172 
ILE CA   C  N S 173 
ILE C    C  N N 174 
ILE O    O  N N 175 
ILE CB   C  N S 176 
ILE CG1  C  N N 177 
ILE CG2  C  N N 178 
ILE CD1  C  N N 179 
ILE OXT  O  N N 180 
ILE H    H  N N 181 
ILE H2   H  N N 182 
ILE HA   H  N N 183 
ILE HB   H  N N 184 
ILE HG12 H  N N 185 
ILE HG13 H  N N 186 
ILE HG21 H  N N 187 
ILE HG22 H  N N 188 
ILE HG23 H  N N 189 
ILE HD11 H  N N 190 
ILE HD12 H  N N 191 
ILE HD13 H  N N 192 
ILE HXT  H  N N 193 
LEU N    N  N N 194 
LEU CA   C  N S 195 
LEU C    C  N N 196 
LEU O    O  N N 197 
LEU CB   C  N N 198 
LEU CG   C  N N 199 
LEU CD1  C  N N 200 
LEU CD2  C  N N 201 
LEU OXT  O  N N 202 
LEU H    H  N N 203 
LEU H2   H  N N 204 
LEU HA   H  N N 205 
LEU HB2  H  N N 206 
LEU HB3  H  N N 207 
LEU HG   H  N N 208 
LEU HD11 H  N N 209 
LEU HD12 H  N N 210 
LEU HD13 H  N N 211 
LEU HD21 H  N N 212 
LEU HD22 H  N N 213 
LEU HD23 H  N N 214 
LEU HXT  H  N N 215 
LYS N    N  N N 216 
LYS CA   C  N S 217 
LYS C    C  N N 218 
LYS O    O  N N 219 
LYS CB   C  N N 220 
LYS CG   C  N N 221 
LYS CD   C  N N 222 
LYS CE   C  N N 223 
LYS NZ   N  N N 224 
LYS OXT  O  N N 225 
LYS H    H  N N 226 
LYS H2   H  N N 227 
LYS HA   H  N N 228 
LYS HB2  H  N N 229 
LYS HB3  H  N N 230 
LYS HG2  H  N N 231 
LYS HG3  H  N N 232 
LYS HD2  H  N N 233 
LYS HD3  H  N N 234 
LYS HE2  H  N N 235 
LYS HE3  H  N N 236 
LYS HZ1  H  N N 237 
LYS HZ2  H  N N 238 
LYS HZ3  H  N N 239 
LYS HXT  H  N N 240 
MET N    N  N N 241 
MET CA   C  N S 242 
MET C    C  N N 243 
MET O    O  N N 244 
MET CB   C  N N 245 
MET CG   C  N N 246 
MET SD   S  N N 247 
MET CE   C  N N 248 
MET OXT  O  N N 249 
MET H    H  N N 250 
MET H2   H  N N 251 
MET HA   H  N N 252 
MET HB2  H  N N 253 
MET HB3  H  N N 254 
MET HG2  H  N N 255 
MET HG3  H  N N 256 
MET HE1  H  N N 257 
MET HE2  H  N N 258 
MET HE3  H  N N 259 
MET HXT  H  N N 260 
PHE N    N  N N 261 
PHE CA   C  N S 262 
PHE C    C  N N 263 
PHE O    O  N N 264 
PHE CB   C  N N 265 
PHE CG   C  Y N 266 
PHE CD1  C  Y N 267 
PHE CD2  C  Y N 268 
PHE CE1  C  Y N 269 
PHE CE2  C  Y N 270 
PHE CZ   C  Y N 271 
PHE OXT  O  N N 272 
PHE H    H  N N 273 
PHE H2   H  N N 274 
PHE HA   H  N N 275 
PHE HB2  H  N N 276 
PHE HB3  H  N N 277 
PHE HD1  H  N N 278 
PHE HD2  H  N N 279 
PHE HE1  H  N N 280 
PHE HE2  H  N N 281 
PHE HZ   H  N N 282 
PHE HXT  H  N N 283 
PRO N    N  N N 284 
PRO CA   C  N S 285 
PRO C    C  N N 286 
PRO O    O  N N 287 
PRO CB   C  N N 288 
PRO CG   C  N N 289 
PRO CD   C  N N 290 
PRO OXT  O  N N 291 
PRO H    H  N N 292 
PRO HA   H  N N 293 
PRO HB2  H  N N 294 
PRO HB3  H  N N 295 
PRO HG2  H  N N 296 
PRO HG3  H  N N 297 
PRO HD2  H  N N 298 
PRO HD3  H  N N 299 
PRO HXT  H  N N 300 
SER N    N  N N 301 
SER CA   C  N S 302 
SER C    C  N N 303 
SER O    O  N N 304 
SER CB   C  N N 305 
SER OG   O  N N 306 
SER OXT  O  N N 307 
SER H    H  N N 308 
SER H2   H  N N 309 
SER HA   H  N N 310 
SER HB2  H  N N 311 
SER HB3  H  N N 312 
SER HG   H  N N 313 
SER HXT  H  N N 314 
THR N    N  N N 315 
THR CA   C  N S 316 
THR C    C  N N 317 
THR O    O  N N 318 
THR CB   C  N R 319 
THR OG1  O  N N 320 
THR CG2  C  N N 321 
THR OXT  O  N N 322 
THR H    H  N N 323 
THR H2   H  N N 324 
THR HA   H  N N 325 
THR HB   H  N N 326 
THR HG1  H  N N 327 
THR HG21 H  N N 328 
THR HG22 H  N N 329 
THR HG23 H  N N 330 
THR HXT  H  N N 331 
TRP N    N  N N 332 
TRP CA   C  N S 333 
TRP C    C  N N 334 
TRP O    O  N N 335 
TRP CB   C  N N 336 
TRP CG   C  Y N 337 
TRP CD1  C  Y N 338 
TRP CD2  C  Y N 339 
TRP NE1  N  Y N 340 
TRP CE2  C  Y N 341 
TRP CE3  C  Y N 342 
TRP CZ2  C  Y N 343 
TRP CZ3  C  Y N 344 
TRP CH2  C  Y N 345 
TRP OXT  O  N N 346 
TRP H    H  N N 347 
TRP H2   H  N N 348 
TRP HA   H  N N 349 
TRP HB2  H  N N 350 
TRP HB3  H  N N 351 
TRP HD1  H  N N 352 
TRP HE1  H  N N 353 
TRP HE3  H  N N 354 
TRP HZ2  H  N N 355 
TRP HZ3  H  N N 356 
TRP HH2  H  N N 357 
TRP HXT  H  N N 358 
TYR N    N  N N 359 
TYR CA   C  N S 360 
TYR C    C  N N 361 
TYR O    O  N N 362 
TYR CB   C  N N 363 
TYR CG   C  Y N 364 
TYR CD1  C  Y N 365 
TYR CD2  C  Y N 366 
TYR CE1  C  Y N 367 
TYR CE2  C  Y N 368 
TYR CZ   C  Y N 369 
TYR OH   O  N N 370 
TYR OXT  O  N N 371 
TYR H    H  N N 372 
TYR H2   H  N N 373 
TYR HA   H  N N 374 
TYR HB2  H  N N 375 
TYR HB3  H  N N 376 
TYR HD1  H  N N 377 
TYR HD2  H  N N 378 
TYR HE1  H  N N 379 
TYR HE2  H  N N 380 
TYR HH   H  N N 381 
TYR HXT  H  N N 382 
VAL N    N  N N 383 
VAL CA   C  N S 384 
VAL C    C  N N 385 
VAL O    O  N N 386 
VAL CB   C  N N 387 
VAL CG1  C  N N 388 
VAL CG2  C  N N 389 
VAL OXT  O  N N 390 
VAL H    H  N N 391 
VAL H2   H  N N 392 
VAL HA   H  N N 393 
VAL HB   H  N N 394 
VAL HG11 H  N N 395 
VAL HG12 H  N N 396 
VAL HG13 H  N N 397 
VAL HG21 H  N N 398 
VAL HG22 H  N N 399 
VAL HG23 H  N N 400 
VAL HXT  H  N N 401 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
# 
_pdbx_audit_support.funding_organization   'Agence Nationale de la Recherche (ANR)' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8R4H 
_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]   0.005908 
_atom_sites.fract_transf_matrix[1][2]   0.003411 
_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]   0.006822 
_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]   0.011064 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CU 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? -10.872 9.983  29.897  1.00 79.85  ? 30  ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? -11.830 9.870  28.808  1.00 80.69  ? 30  ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? -12.629 11.184 28.499  1.00 81.06  ? 30  ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? -12.577 11.674 27.355  1.00 81.17  ? 30  ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? -12.775 8.694  29.066  1.00 81.04  ? 30  ALA A CB  1 
ATOM   6    N  N   . GLU A 1 2   ? -13.351 11.747 29.525  1.00 80.68  ? 31  GLU A N   1 
ATOM   7    C  CA  . GLU A 1 2   ? -14.210 12.945 29.452  1.00 80.52  ? 31  GLU A CA  1 
ATOM   8    C  C   . GLU A 1 2   ? -13.429 14.262 29.533  1.00 79.36  ? 31  GLU A C   1 
ATOM   9    O  O   . GLU A 1 2   ? -13.575 15.026 30.490  1.00 79.57  ? 31  GLU A O   1 
ATOM   10   C  CB  . GLU A 1 2   ? -15.281 12.886 30.549  1.00 83.63  ? 31  GLU A CB  1 
ATOM   11   C  CG  . GLU A 1 2   ? -16.234 11.720 30.403  1.00 90.15  ? 31  GLU A CG  1 
ATOM   12   C  CD  . GLU A 1 2   ? -17.619 12.035 30.926  1.00 99.26  ? 31  GLU A CD  1 
ATOM   13   O  OE1 . GLU A 1 2   ? -17.720 12.595 32.043  1.00 101.11 ? 31  GLU A OE1 1 
ATOM   14   O  OE2 . GLU A 1 2   ? -18.604 11.742 30.210  1.00 102.43 ? 31  GLU A OE2 1 
ATOM   15   N  N   . HIS A 1 3   ? -12.597 14.531 28.526  1.00 77.94  ? 32  HIS A N   1 
ATOM   16   C  CA  . HIS A 1 3   ? -11.712 15.688 28.549  1.00 76.80  ? 32  HIS A CA  1 
ATOM   17   C  C   . HIS A 1 3   ? -11.587 16.334 27.170  1.00 75.52  ? 32  HIS A C   1 
ATOM   18   O  O   . HIS A 1 3   ? -11.775 15.677 26.139  1.00 75.71  ? 32  HIS A O   1 
ATOM   19   C  CB  . HIS A 1 3   ? -10.334 15.250 29.089  1.00 77.18  ? 32  HIS A CB  1 
ATOM   20   C  CG  . HIS A 1 3   ? -10.407 14.709 30.484  1.00 78.60  ? 32  HIS A CG  1 
ATOM   21   N  ND1 . HIS A 1 3   ? -10.442 15.552 31.580  1.00 80.18  ? 32  HIS A ND1 1 
ATOM   22   C  CD2 . HIS A 1 3   ? -10.540 13.431 30.912  1.00 79.45  ? 32  HIS A CD2 1 
ATOM   23   C  CE1 . HIS A 1 3   ? -10.559 14.762 32.637  1.00 80.55  ? 32  HIS A CE1 1 
ATOM   24   N  NE2 . HIS A 1 3   ? -10.609 13.478 32.287  1.00 80.41  ? 32  HIS A NE2 1 
ATOM   25   N  N   . PRO A 1 4   ? -11.268 17.637 27.132  1.00 73.85  ? 33  PRO A N   1 
ATOM   26   C  CA  . PRO A 1 4   ? -11.169 18.322 25.834  1.00 72.71  ? 33  PRO A CA  1 
ATOM   27   C  C   . PRO A 1 4   ? -9.901  17.991 25.042  1.00 71.09  ? 33  PRO A C   1 
ATOM   28   O  O   . PRO A 1 4   ? -9.090  17.172 25.470  1.00 71.37  ? 33  PRO A O   1 
ATOM   29   C  CB  . PRO A 1 4   ? -11.245 19.815 26.218  1.00 73.62  ? 33  PRO A CB  1 
ATOM   30   C  CG  . PRO A 1 4   ? -11.492 19.859 27.712  1.00 74.16  ? 33  PRO A CG  1 
ATOM   31   C  CD  . PRO A 1 4   ? -11.031 18.565 28.254  1.00 72.89  ? 33  PRO A CD  1 
ATOM   32   N  N   . THR A 1 5   ? -9.734  18.614 23.876  1.00 69.20  ? 34  THR A N   1 
ATOM   33   C  CA  . THR A 1 5   ? -8.528  18.442 23.078  1.00 67.82  ? 34  THR A CA  1 
ATOM   34   C  C   . THR A 1 5   ? -7.679  19.698 23.259  1.00 66.55  ? 34  THR A C   1 
ATOM   35   O  O   . THR A 1 5   ? -8.218  20.803 23.220  1.00 66.96  ? 34  THR A O   1 
ATOM   36   C  CB  . THR A 1 5   ? -8.908  18.236 21.622  1.00 68.57  ? 34  THR A CB  1 
ATOM   37   O  OG1 . THR A 1 5   ? -9.548  16.965 21.497  1.00 69.89  ? 34  THR A OG1 1 
ATOM   38   C  CG2 . THR A 1 5   ? -7.719  18.355 20.686  1.00 68.35  ? 34  THR A CG2 1 
ATOM   39   N  N   . LEU A 1 6   ? -6.370  19.544 23.468  1.00 64.83  ? 35  LEU A N   1 
ATOM   40   C  CA  . LEU A 1 6   ? -5.465  20.675 23.645  1.00 63.64  ? 35  LEU A CA  1 
ATOM   41   C  C   . LEU A 1 6   ? -5.464  21.584 22.423  1.00 63.06  ? 35  LEU A C   1 
ATOM   42   O  O   . LEU A 1 6   ? -5.066  21.158 21.337  1.00 63.52  ? 35  LEU A O   1 
ATOM   43   C  CB  . LEU A 1 6   ? -4.033  20.174 23.903  1.00 63.33  ? 35  LEU A CB  1 
ATOM   44   C  CG  . LEU A 1 6   ? -2.959  21.261 24.005  1.00 63.83  ? 35  LEU A CG  1 
ATOM   45   C  CD1 . LEU A 1 6   ? -3.141  22.082 25.255  1.00 64.01  ? 35  LEU A CD1 1 
ATOM   46   C  CD2 . LEU A 1 6   ? -1.589  20.669 23.946  1.00 63.95  ? 35  LEU A CD2 1 
ATOM   47   N  N   . PRO A 1 7   ? -5.855  22.855 22.594  1.00 61.93  ? 36  PRO A N   1 
ATOM   48   C  CA  . PRO A 1 7   ? -5.838  23.783 21.460  1.00 61.50  ? 36  PRO A CA  1 
ATOM   49   C  C   . PRO A 1 7   ? -4.416  24.182 21.060  1.00 61.51  ? 36  PRO A C   1 
ATOM   50   O  O   . PRO A 1 7   ? -3.570  24.389 21.925  1.00 61.20  ? 36  PRO A O   1 
ATOM   51   C  CB  . PRO A 1 7   ? -6.608  25.000 21.990  1.00 61.77  ? 36  PRO A CB  1 
ATOM   52   C  CG  . PRO A 1 7   ? -7.248  24.556 23.251  1.00 62.13  ? 36  PRO A CG  1 
ATOM   53   C  CD  . PRO A 1 7   ? -6.354  23.512 23.808  1.00 60.99  ? 36  PRO A CD  1 
ATOM   54   N  N   . ILE A 1 8   ? -4.155  24.290 19.754  1.00 61.49  ? 37  ILE A N   1 
ATOM   55   C  CA  . ILE A 1 8   ? -2.851  24.723 19.282  1.00 61.85  ? 37  ILE A CA  1 
ATOM   56   C  C   . ILE A 1 8   ? -2.956  26.137 18.739  1.00 62.02  ? 37  ILE A C   1 
ATOM   57   O  O   . ILE A 1 8   ? -3.681  26.383 17.779  1.00 61.73  ? 37  ILE A O   1 
ATOM   58   C  CB  . ILE A 1 8   ? -2.235  23.769 18.237  1.00 62.29  ? 37  ILE A CB  1 
ATOM   59   C  CG1 . ILE A 1 8   ? -2.292  22.303 18.686  1.00 63.07  ? 37  ILE A CG1 1 
ATOM   60   C  CG2 . ILE A 1 8   ? -0.825  24.219 17.879  1.00 62.68  ? 37  ILE A CG2 1 
ATOM   61   C  CD1 . ILE A 1 8   ? -1.644  22.004 19.979  1.00 64.44  ? 37  ILE A CD1 1 
ATOM   62   N  N   . PRO A 1 9   ? -2.242  27.089 19.354  1.00 62.63  ? 38  PRO A N   1 
ATOM   63   C  CA  . PRO A 1 9   ? -2.271  28.466 18.848  1.00 63.17  ? 38  PRO A CA  1 
ATOM   64   C  C   . PRO A 1 9   ? -1.656  28.517 17.462  1.00 64.01  ? 38  PRO A C   1 
ATOM   65   O  O   . PRO A 1 9   ? -0.631  27.887 17.230  1.00 64.49  ? 38  PRO A O   1 
ATOM   66   C  CB  . PRO A 1 9   ? -1.395  29.225 19.847  1.00 63.79  ? 38  PRO A CB  1 
ATOM   67   C  CG  . PRO A 1 9   ? -1.322  28.345 21.070  1.00 64.06  ? 38  PRO A CG  1 
ATOM   68   C  CD  . PRO A 1 9   ? -1.346  26.960 20.516  1.00 62.40  ? 38  PRO A CD  1 
ATOM   69   N  N   . ALA A 1 10  ? -2.311  29.214 16.537  1.00 64.07  ? 39  ALA A N   1 
ATOM   70   C  CA  . ALA A 1 10  ? -1.876  29.336 15.153  1.00 64.38  ? 39  ALA A CA  1 
ATOM   71   C  C   . ALA A 1 10  ? -0.447  29.853 15.036  1.00 64.27  ? 39  ALA A C   1 
ATOM   72   O  O   . ALA A 1 10  ? -0.031  30.687 15.831  1.00 64.41  ? 39  ALA A O   1 
ATOM   73   C  CB  . ALA A 1 10  ? -2.824  30.258 14.407  1.00 64.78  ? 39  ALA A CB  1 
ATOM   74   N  N   . LEU A 1 11  ? 0.302   29.355 14.057  1.00 63.91  ? 40  LEU A N   1 
ATOM   75   C  CA  . LEU A 1 11  ? 1.684   29.762 13.867  1.00 64.22  ? 40  LEU A CA  1 
ATOM   76   C  C   . LEU A 1 11  ? 1.776   30.858 12.801  1.00 64.59  ? 40  LEU A C   1 
ATOM   77   O  O   . LEU A 1 11  ? 1.992   30.555 11.631  1.00 65.19  ? 40  LEU A O   1 
ATOM   78   C  CB  . LEU A 1 11  ? 2.490   28.531 13.459  1.00 64.40  ? 40  LEU A CB  1 
ATOM   79   C  CG  . LEU A 1 11  ? 4.005   28.594 13.572  1.00 65.73  ? 40  LEU A CG  1 
ATOM   80   C  CD1 . LEU A 1 11  ? 4.445   28.990 14.965  1.00 66.16  ? 40  LEU A CD1 1 
ATOM   81   C  CD2 . LEU A 1 11  ? 4.594   27.262 13.215  1.00 66.09  ? 40  LEU A CD2 1 
ATOM   82   N  N   . LEU A 1 12  ? 1.614   32.129 13.197  1.00 64.18  ? 41  LEU A N   1 
ATOM   83   C  CA  . LEU A 1 12  ? 1.647   33.238 12.241  1.00 64.43  ? 41  LEU A CA  1 
ATOM   84   C  C   . LEU A 1 12  ? 3.041   33.641 11.816  1.00 64.80  ? 41  LEU A C   1 
ATOM   85   O  O   . LEU A 1 12  ? 3.880   33.927 12.657  1.00 65.16  ? 41  LEU A O   1 
ATOM   86   C  CB  . LEU A 1 12  ? 0.947   34.500 12.779  1.00 64.52  ? 41  LEU A CB  1 
ATOM   87   C  CG  . LEU A 1 12  ? -0.388  34.390 13.495  1.00 65.84  ? 41  LEU A CG  1 
ATOM   88   C  CD1 . LEU A 1 12  ? -1.037  35.738 13.555  1.00 66.14  ? 41  LEU A CD1 1 
ATOM   89   C  CD2 . LEU A 1 12  ? -1.340  33.390 12.819  1.00 66.72  ? 41  LEU A CD2 1 
ATOM   90   N  N   . THR A 1 13  ? 3.261   33.760 10.514  1.00 64.69  ? 42  THR A N   1 
ATOM   91   C  CA  . THR A 1 13  ? 4.542   34.212 9.979   1.00 65.22  ? 42  THR A CA  1 
ATOM   92   C  C   . THR A 1 13  ? 4.369   35.600 9.366   1.00 65.18  ? 42  THR A C   1 
ATOM   93   O  O   . THR A 1 13  ? 3.277   35.938 8.900   1.00 65.20  ? 42  THR A O   1 
ATOM   94   C  CB  . THR A 1 13  ? 5.045   33.221 8.934   1.00 67.07  ? 42  THR A CB  1 
ATOM   95   O  OG1 . THR A 1 13  ? 4.037   33.070 7.936   1.00 68.56  ? 42  THR A OG1 1 
ATOM   96   C  CG2 . THR A 1 13  ? 5.383   31.869 9.536   1.00 67.72  ? 42  THR A CG2 1 
ATOM   97   N  N   . PRO A 1 14  ? 5.430   36.425 9.340   1.00 65.05  ? 43  PRO A N   1 
ATOM   98   C  CA  . PRO A 1 14  ? 5.300   37.766 8.742   1.00 65.28  ? 43  PRO A CA  1 
ATOM   99   C  C   . PRO A 1 14  ? 4.870   37.693 7.280   1.00 65.73  ? 43  PRO A C   1 
ATOM   100  O  O   . PRO A 1 14  ? 5.363   36.849 6.540   1.00 65.94  ? 43  PRO A O   1 
ATOM   101  C  CB  . PRO A 1 14  ? 6.699   38.368 8.904   1.00 65.85  ? 43  PRO A CB  1 
ATOM   102  C  CG  . PRO A 1 14  ? 7.330   37.577 10.020  1.00 66.23  ? 43  PRO A CG  1 
ATOM   103  C  CD  . PRO A 1 14  ? 6.790   36.193 9.858   1.00 64.64  ? 43  PRO A CD  1 
ATOM   104  N  N   . ASP A 1 15  ? 3.905   38.530 6.881   1.00 65.66  ? 44  ASP A N   1 
ATOM   105  C  CA  . ASP A 1 15  ? 3.360   38.502 5.530   1.00 65.78  ? 44  ASP A CA  1 
ATOM   106  C  C   . ASP A 1 15  ? 4.321   39.126 4.481   1.00 66.28  ? 44  ASP A C   1 
ATOM   107  O  O   . ASP A 1 15  ? 5.473   39.415 4.806   1.00 66.06  ? 44  ASP A O   1 
ATOM   108  C  CB  . ASP A 1 15  ? 1.935   39.113 5.504   1.00 66.62  ? 44  ASP A CB  1 
ATOM   109  C  CG  . ASP A 1 15  ? 1.810   40.599 5.773   1.00 69.87  ? 44  ASP A CG  1 
ATOM   110  O  OD1 . ASP A 1 15  ? 2.858   41.284 5.867   1.00 70.24  ? 44  ASP A OD1 1 
ATOM   111  O  OD2 . ASP A 1 15  ? 0.666   41.080 5.888   1.00 71.53  ? 44  ASP A OD2 1 
ATOM   112  N  N   . ALA A 1 16  ? 3.856   39.290 3.222   1.00 66.90  ? 45  ALA A N   1 
ATOM   113  C  CA  . ALA A 1 16  ? 4.602   39.860 2.099   1.00 67.88  ? 45  ALA A CA  1 
ATOM   114  C  C   . ALA A 1 16  ? 5.160   41.246 2.395   1.00 68.89  ? 45  ALA A C   1 
ATOM   115  O  O   . ALA A 1 16  ? 6.186   41.622 1.827   1.00 69.31  ? 45  ALA A O   1 
ATOM   116  C  CB  . ALA A 1 16  ? 3.717   39.917 0.868   1.00 67.98  ? 45  ALA A CB  1 
ATOM   117  N  N   . ALA A 1 17  ? 4.482   42.010 3.264   1.00 69.09  ? 46  ALA A N   1 
ATOM   118  C  CA  . ALA A 1 17  ? 4.926   43.332 3.686   1.00 69.76  ? 46  ALA A CA  1 
ATOM   119  C  C   . ALA A 1 17  ? 5.846   43.293 4.939   1.00 70.76  ? 46  ALA A C   1 
ATOM   120  O  O   . ALA A 1 17  ? 6.177   44.353 5.474   1.00 71.44  ? 46  ALA A O   1 
ATOM   121  C  CB  . ALA A 1 17  ? 3.719   44.200 3.974   1.00 69.70  ? 46  ALA A CB  1 
ATOM   122  N  N   . GLY A 1 18  ? 6.235   42.096 5.393   1.00 70.44  ? 47  GLY A N   1 
ATOM   123  C  CA  . GLY A 1 18  ? 7.038   41.901 6.594   1.00 70.55  ? 47  GLY A CA  1 
ATOM   124  C  C   . GLY A 1 18  ? 6.297   42.344 7.843   1.00 70.17  ? 47  GLY A C   1 
ATOM   125  O  O   . GLY A 1 18  ? 6.899   42.895 8.767   1.00 70.17  ? 47  GLY A O   1 
ATOM   126  N  N   . LYS A 1 19  ? 4.971   42.139 7.863   1.00 69.55  ? 48  LYS A N   1 
ATOM   127  C  CA  . LYS A 1 19  ? 4.138   42.567 8.978   1.00 69.29  ? 48  LYS A CA  1 
ATOM   128  C  C   . LYS A 1 19  ? 3.327   41.430 9.595   1.00 68.82  ? 48  LYS A C   1 
ATOM   129  O  O   . LYS A 1 19  ? 3.055   40.428 8.943   1.00 68.69  ? 48  LYS A O   1 
ATOM   130  C  CB  . LYS A 1 19  ? 3.193   43.705 8.537   1.00 70.83  ? 48  LYS A CB  1 
ATOM   131  C  CG  . LYS A 1 19  ? 3.902   45.025 8.235   1.00 73.95  ? 48  LYS A CG  1 
ATOM   132  C  CD  . LYS A 1 19  ? 3.093   45.898 7.285   1.00 77.16  ? 48  LYS A CD  1 
ATOM   133  C  CE  . LYS A 1 19  ? 3.569   47.325 7.252   1.00 80.23  ? 48  LYS A CE  1 
ATOM   134  N  NZ  . LYS A 1 19  ? 2.529   48.252 7.770   1.00 82.86  ? 48  LYS A NZ  1 
ATOM   135  N  N   . ILE A 1 20  ? 2.959   41.584 10.871  1.00 68.47  ? 49  ILE A N   1 
ATOM   136  C  CA  . ILE A 1 20  ? 2.113   40.631 11.583  1.00 68.58  ? 49  ILE A CA  1 
ATOM   137  C  C   . ILE A 1 20  ? 0.988   41.433 12.251  1.00 68.59  ? 49  ILE A C   1 
ATOM   138  O  O   . ILE A 1 20  ? 1.254   42.445 12.900  1.00 68.61  ? 49  ILE A O   1 
ATOM   139  C  CB  . ILE A 1 20  ? 2.874   39.703 12.571  1.00 68.92  ? 49  ILE A CB  1 
ATOM   140  C  CG1 . ILE A 1 20  ? 3.814   38.737 11.820  1.00 69.80  ? 49  ILE A CG1 1 
ATOM   141  C  CG2 . ILE A 1 20  ? 1.884   38.915 13.427  1.00 69.42  ? 49  ILE A CG2 1 
ATOM   142  C  CD1 . ILE A 1 20  ? 4.694   37.873 12.702  1.00 70.78  ? 49  ILE A CD1 1 
ATOM   143  N  N   . ALA A 1 21  ? -0.271  41.031 12.025  1.00 68.05  ? 50  ALA A N   1 
ATOM   144  C  CA  . ALA A 1 21  ? -1.405  41.744 12.591  1.00 67.49  ? 50  ALA A CA  1 
ATOM   145  C  C   . ALA A 1 21  ? -1.939  41.034 13.838  1.00 66.58  ? 50  ALA A C   1 
ATOM   146  O  O   . ALA A 1 21  ? -2.244  39.839 13.791  1.00 66.86  ? 50  ALA A O   1 
ATOM   147  C  CB  . ALA A 1 21  ? -2.506  41.878 11.551  1.00 67.54  ? 50  ALA A CB  1 
ATOM   148  N  N   . LEU A 1 22  ? -2.053  41.781 14.957  1.00 64.95  ? 51  LEU A N   1 
ATOM   149  C  CA  . LEU A 1 22  ? -2.587  41.264 16.212  1.00 63.35  ? 51  LEU A CA  1 
ATOM   150  C  C   . LEU A 1 22  ? -3.787  42.101 16.620  1.00 62.50  ? 51  LEU A C   1 
ATOM   151  O  O   . LEU A 1 22  ? -3.640  43.289 16.881  1.00 62.31  ? 51  LEU A O   1 
ATOM   152  C  CB  . LEU A 1 22  ? -1.535  41.335 17.322  1.00 62.79  ? 51  LEU A CB  1 
ATOM   153  C  CG  . LEU A 1 22  ? -0.293  40.482 17.177  1.00 63.11  ? 51  LEU A CG  1 
ATOM   154  C  CD1 . LEU A 1 22  ? 0.585   40.617 18.402  1.00 63.30  ? 51  LEU A CD1 1 
ATOM   155  C  CD2 . LEU A 1 22  ? -0.638  39.026 16.939  1.00 63.31  ? 51  LEU A CD2 1 
ATOM   156  N  N   . ASN A 1 23  ? -4.969  41.496 16.668  1.00 61.86  ? 52  ASN A N   1 
ATOM   157  C  CA  . ASN A 1 23  ? -6.175  42.191 17.072  1.00 61.72  ? 52  ASN A CA  1 
ATOM   158  C  C   . ASN A 1 23  ? -6.536  41.762 18.482  1.00 61.04  ? 52  ASN A C   1 
ATOM   159  O  O   . ASN A 1 23  ? -7.020  40.649 18.686  1.00 61.38  ? 52  ASN A O   1 
ATOM   160  C  CB  . ASN A 1 23  ? -7.327  41.894 16.121  1.00 63.16  ? 52  ASN A CB  1 
ATOM   161  C  CG  . ASN A 1 23  ? -8.455  42.890 16.257  1.00 67.29  ? 52  ASN A CG  1 
ATOM   162  O  OD1 . ASN A 1 23  ? -8.352  44.037 15.805  1.00 69.44  ? 52  ASN A OD1 1 
ATOM   163  N  ND2 . ASN A 1 23  ? -9.553  42.492 16.890  1.00 67.08  ? 52  ASN A ND2 1 
ATOM   164  N  N   . VAL A 1 24  ? -6.280  42.635 19.455  1.00 59.99  ? 53  VAL A N   1 
ATOM   165  C  CA  . VAL A 1 24  ? -6.589  42.386 20.859  1.00 59.75  ? 53  VAL A CA  1 
ATOM   166  C  C   . VAL A 1 24  ? -8.081  42.609 21.005  1.00 59.26  ? 53  VAL A C   1 
ATOM   167  O  O   . VAL A 1 24  ? -8.521  43.738 20.945  1.00 59.14  ? 53  VAL A O   1 
ATOM   168  C  CB  . VAL A 1 24  ? -5.784  43.354 21.760  1.00 60.35  ? 53  VAL A CB  1 
ATOM   169  C  CG1 . VAL A 1 24  ? -6.038  43.066 23.228  1.00 60.50  ? 53  VAL A CG1 1 
ATOM   170  C  CG2 . VAL A 1 24  ? -4.289  43.277 21.451  1.00 60.97  ? 53  VAL A CG2 1 
ATOM   171  N  N   . GLN A 1 25  ? -8.860  41.547 21.152  1.00 58.83  ? 54  GLN A N   1 
ATOM   172  C  CA  . GLN A 1 25  ? -10.311 41.643 21.194  1.00 58.90  ? 54  GLN A CA  1 
ATOM   173  C  C   . GLN A 1 25  ? -10.941 40.924 22.398  1.00 59.34  ? 54  GLN A C   1 
ATOM   174  O  O   . GLN A 1 25  ? -10.266 40.192 23.114  1.00 59.13  ? 54  GLN A O   1 
ATOM   175  C  CB  . GLN A 1 25  ? -10.861 41.037 19.892  1.00 59.78  ? 54  GLN A CB  1 
ATOM   176  C  CG  . GLN A 1 25  ? -10.640 39.527 19.810  1.00 61.47  ? 54  GLN A CG  1 
ATOM   177  C  CD  . GLN A 1 25  ? -10.374 39.071 18.408  1.00 64.48  ? 54  GLN A CD  1 
ATOM   178  O  OE1 . GLN A 1 25  ? -9.729  39.758 17.608  1.00 65.26  ? 54  GLN A OE1 1 
ATOM   179  N  NE2 . GLN A 1 25  ? -10.852 37.888 18.084  1.00 65.04  ? 54  GLN A NE2 1 
ATOM   180  N  N   . THR A 1 26  ? -12.255 41.109 22.588  1.00 59.62  ? 55  THR A N   1 
ATOM   181  C  CA  . THR A 1 26  ? -13.024 40.450 23.640  1.00 60.11  ? 55  THR A CA  1 
ATOM   182  C  C   . THR A 1 26  ? -13.551 39.073 23.140  1.00 59.90  ? 55  THR A C   1 
ATOM   183  O  O   . THR A 1 26  ? -13.472 38.763 21.955  1.00 60.10  ? 55  THR A O   1 
ATOM   184  C  CB  . THR A 1 26  ? -14.170 41.384 24.091  1.00 61.86  ? 55  THR A CB  1 
ATOM   185  O  OG1 . THR A 1 26  ? -15.149 41.476 23.044  1.00 63.09  ? 55  THR A OG1 1 
ATOM   186  C  CG2 . THR A 1 26  ? -13.676 42.770 24.479  1.00 62.31  ? 55  THR A CG2 1 
ATOM   187  N  N   . GLY A 1 27  ? -14.076 38.268 24.044  1.00 59.47  ? 56  GLY A N   1 
ATOM   188  C  CA  . GLY A 1 27  ? -14.619 36.963 23.711  1.00 59.85  ? 56  GLY A CA  1 
ATOM   189  C  C   . GLY A 1 27  ? -15.212 36.272 24.921  1.00 60.36  ? 56  GLY A C   1 
ATOM   190  O  O   . GLY A 1 27  ? -15.509 36.917 25.935  1.00 60.47  ? 56  GLY A O   1 
ATOM   191  N  N   . SER A 1 28  ? -15.394 34.960 24.826  1.00 60.54  ? 57  SER A N   1 
ATOM   192  C  CA  . SER A 1 28  ? -15.905 34.180 25.947  1.00 61.67  ? 57  SER A CA  1 
ATOM   193  C  C   . SER A 1 28  ? -15.406 32.730 25.921  1.00 62.41  ? 57  SER A C   1 
ATOM   194  O  O   . SER A 1 28  ? -15.003 32.225 24.873  1.00 62.89  ? 57  SER A O   1 
ATOM   195  C  CB  . SER A 1 28  ? -17.432 34.268 26.082  1.00 63.31  ? 57  SER A CB  1 
ATOM   196  O  OG  . SER A 1 28  ? -18.161 33.856 24.937  1.00 65.61  ? 57  SER A OG  1 
ATOM   197  N  N   . MET A 1 29  ? -15.366 32.086 27.087  1.00 62.17  ? 58  MET A N   1 
ATOM   198  C  CA  . MET A 1 29  ? -14.921 30.702 27.194  1.00 62.54  ? 58  MET A CA  1 
ATOM   199  C  C   . MET A 1 29  ? -15.892 29.966 28.088  1.00 62.98  ? 58  MET A C   1 
ATOM   200  O  O   . MET A 1 29  ? -16.281 30.506 29.117  1.00 62.93  ? 58  MET A O   1 
ATOM   201  C  CB  . MET A 1 29  ? -13.521 30.622 27.816  1.00 63.01  ? 58  MET A CB  1 
ATOM   202  C  CG  . MET A 1 29  ? -12.454 31.376 27.055  1.00 64.86  ? 58  MET A CG  1 
ATOM   203  S  SD  . MET A 1 29  ? -11.936 30.562 25.532  1.00 65.20  ? 58  MET A SD  1 
ATOM   204  C  CE  . MET A 1 29  ? -11.238 29.119 26.186  1.00 63.28  ? 58  MET A CE  1 
ATOM   205  N  N   . LYS A 1 30  ? -16.261 28.733 27.732  1.00 63.55  ? 59  LYS A N   1 
ATOM   206  C  CA  . LYS A 1 30  ? -17.198 27.971 28.548  1.00 65.02  ? 59  LYS A CA  1 
ATOM   207  C  C   . LYS A 1 30  ? -16.509 27.056 29.544  1.00 66.04  ? 59  LYS A C   1 
ATOM   208  O  O   . LYS A 1 30  ? -16.187 25.921 29.208  1.00 66.38  ? 59  LYS A O   1 
ATOM   209  C  CB  . LYS A 1 30  ? -18.204 27.211 27.673  1.00 67.75  ? 59  LYS A CB  1 
ATOM   210  C  CG  . LYS A 1 30  ? -19.221 28.140 27.013  1.00 72.59  ? 59  LYS A CG  1 
ATOM   211  C  CD  . LYS A 1 30  ? -19.901 27.533 25.777  1.00 77.49  ? 59  LYS A CD  1 
ATOM   212  C  CE  . LYS A 1 30  ? -19.092 27.702 24.507  1.00 81.09  ? 59  LYS A CE  1 
ATOM   213  N  NZ  . LYS A 1 30  ? -19.921 27.500 23.281  1.00 82.83  ? 59  LYS A NZ  1 
ATOM   214  N  N   . TRP A 1 31  ? -16.294 27.540 30.779  1.00 66.59  ? 60  TRP A N   1 
ATOM   215  C  CA  . TRP A 1 31  ? -15.662 26.745 31.837  1.00 67.49  ? 60  TRP A CA  1 
ATOM   216  C  C   . TRP A 1 31  ? -16.715 26.217 32.824  1.00 68.98  ? 60  TRP A C   1 
ATOM   217  O  O   . TRP A 1 31  ? -16.822 25.006 33.008  1.00 69.11  ? 60  TRP A O   1 
ATOM   218  C  CB  . TRP A 1 31  ? -14.545 27.534 32.552  1.00 66.85  ? 60  TRP A CB  1 
ATOM   219  C  CG  . TRP A 1 31  ? -13.358 27.823 31.680  1.00 66.88  ? 60  TRP A CG  1 
ATOM   220  C  CD1 . TRP A 1 31  ? -12.601 26.918 30.992  1.00 67.60  ? 60  TRP A CD1 1 
ATOM   221  C  CD2 . TRP A 1 31  ? -12.782 29.110 31.420  1.00 66.96  ? 60  TRP A CD2 1 
ATOM   222  N  NE1 . TRP A 1 31  ? -11.599 27.565 30.305  1.00 67.91  ? 60  TRP A NE1 1 
ATOM   223  C  CE2 . TRP A 1 31  ? -11.685 28.912 30.555  1.00 67.70  ? 60  TRP A CE2 1 
ATOM   224  C  CE3 . TRP A 1 31  ? -13.094 30.414 31.825  1.00 67.42  ? 60  TRP A CE3 1 
ATOM   225  C  CZ2 . TRP A 1 31  ? -10.889 29.970 30.107  1.00 68.16  ? 60  TRP A CZ2 1 
ATOM   226  C  CZ3 . TRP A 1 31  ? -12.306 31.456 31.381  1.00 68.12  ? 60  TRP A CZ3 1 
ATOM   227  C  CH2 . TRP A 1 31  ? -11.214 31.230 30.540  1.00 68.21  ? 60  TRP A CH2 1 
ATOM   228  N  N   . LYS A 1 32  ? -17.506 27.117 33.440  1.00 69.83  ? 61  LYS A N   1 
ATOM   229  C  CA  . LYS A 1 32  ? -18.584 26.717 34.348  1.00 70.87  ? 61  LYS A CA  1 
ATOM   230  C  C   . LYS A 1 32  ? -19.735 26.195 33.480  1.00 72.42  ? 61  LYS A C   1 
ATOM   231  O  O   . LYS A 1 32  ? -20.038 26.785 32.440  1.00 72.44  ? 61  LYS A O   1 
ATOM   232  C  CB  . LYS A 1 32  ? -19.057 27.907 35.205  1.00 71.85  ? 61  LYS A CB  1 
ATOM   233  C  CG  . LYS A 1 32  ? -18.642 27.845 36.677  1.00 75.02  ? 61  LYS A CG  1 
ATOM   234  C  CD  . LYS A 1 32  ? -19.192 29.044 37.476  1.00 78.44  ? 61  LYS A CD  1 
ATOM   235  C  CE  . LYS A 1 32  ? -19.061 28.918 38.982  1.00 81.06  ? 61  LYS A CE  1 
ATOM   236  N  NZ  . LYS A 1 32  ? -17.859 29.621 39.519  1.00 82.38  ? 61  LYS A NZ  1 
ATOM   237  N  N   . ALA A 1 33  ? -20.354 25.072 33.880  1.00 73.36  ? 62  ALA A N   1 
ATOM   238  C  CA  . ALA A 1 33  ? -21.435 24.465 33.098  1.00 74.34  ? 62  ALA A CA  1 
ATOM   239  C  C   . ALA A 1 33  ? -22.594 25.429 32.853  1.00 75.22  ? 62  ALA A C   1 
ATOM   240  O  O   . ALA A 1 33  ? -23.160 25.974 33.800  1.00 75.37  ? 62  ALA A O   1 
ATOM   241  C  CB  . ALA A 1 33  ? -21.926 23.190 33.767  1.00 74.43  ? 62  ALA A CB  1 
ATOM   242  N  N   . GLY A 1 34  ? -22.888 25.665 31.578  1.00 75.68  ? 63  GLY A N   1 
ATOM   243  C  CA  . GLY A 1 34  ? -23.944 26.575 31.147  1.00 76.41  ? 63  GLY A CA  1 
ATOM   244  C  C   . GLY A 1 34  ? -23.670 28.018 31.517  1.00 76.88  ? 63  GLY A C   1 
ATOM   245  O  O   . GLY A 1 34  ? -24.581 28.735 31.943  1.00 77.24  ? 63  GLY A O   1 
ATOM   246  N  N   . MET A 1 35  ? -22.406 28.448 31.381  1.00 76.60  ? 64  MET A N   1 
ATOM   247  C  CA  . MET A 1 35  ? -22.001 29.806 31.729  1.00 76.65  ? 64  MET A CA  1 
ATOM   248  C  C   . MET A 1 35  ? -20.843 30.262 30.857  1.00 76.32  ? 64  MET A C   1 
ATOM   249  O  O   . MET A 1 35  ? -19.725 29.787 31.030  1.00 76.64  ? 64  MET A O   1 
ATOM   250  C  CB  . MET A 1 35  ? -21.588 29.874 33.210  1.00 77.61  ? 64  MET A CB  1 
ATOM   251  C  CG  . MET A 1 35  ? -22.524 30.700 34.066  1.00 81.01  ? 64  MET A CG  1 
ATOM   252  S  SD  . MET A 1 35  ? -22.198 30.570 35.851  1.00 89.84  ? 64  MET A SD  1 
ATOM   253  C  CE  . MET A 1 35  ? -22.616 28.846 36.139  1.00 89.25  ? 64  MET A CE  1 
ATOM   254  N  N   . GLN A 1 36  ? -21.098 31.175 29.924  1.00 75.75  ? 65  GLN A N   1 
ATOM   255  C  CA  . GLN A 1 36  ? -20.042 31.716 29.074  1.00 75.60  ? 65  GLN A CA  1 
ATOM   256  C  C   . GLN A 1 36  ? -19.278 32.775 29.880  1.00 74.42  ? 65  GLN A C   1 
ATOM   257  O  O   . GLN A 1 36  ? -19.876 33.761 30.319  1.00 74.75  ? 65  GLN A O   1 
ATOM   258  C  CB  . GLN A 1 36  ? -20.642 32.355 27.808  1.00 77.99  ? 65  GLN A CB  1 
ATOM   259  C  CG  . GLN A 1 36  ? -21.204 31.353 26.810  1.00 82.96  ? 65  GLN A CG  1 
ATOM   260  C  CD  . GLN A 1 36  ? -20.290 31.152 25.617  1.00 89.08  ? 65  GLN A CD  1 
ATOM   261  O  OE1 . GLN A 1 36  ? -19.059 31.298 25.699  1.00 90.82  ? 65  GLN A OE1 1 
ATOM   262  N  NE2 . GLN A 1 36  ? -20.875 30.797 24.479  1.00 90.03  ? 65  GLN A NE2 1 
ATOM   263  N  N   . THR A 1 37  ? -17.981 32.565 30.103  1.00 72.83  ? 66  THR A N   1 
ATOM   264  C  CA  . THR A 1 37  ? -17.172 33.519 30.850  1.00 71.94  ? 66  THR A CA  1 
ATOM   265  C  C   . THR A 1 37  ? -16.603 34.559 29.920  1.00 71.10  ? 66  THR A C   1 
ATOM   266  O  O   . THR A 1 37  ? -15.867 34.209 29.016  1.00 71.41  ? 66  THR A O   1 
ATOM   267  C  CB  . THR A 1 37  ? -16.035 32.802 31.569  1.00 72.89  ? 66  THR A CB  1 
ATOM   268  O  OG1 . THR A 1 37  ? -16.603 31.967 32.572  1.00 74.47  ? 66  THR A OG1 1 
ATOM   269  C  CG2 . THR A 1 37  ? -15.039 33.762 32.204  1.00 72.71  ? 66  THR A CG2 1 
ATOM   270  N  N   . PRO A 1 38  ? -16.883 35.844 30.156  1.00 69.92  ? 67  PRO A N   1 
ATOM   271  C  CA  . PRO A 1 38  ? -16.288 36.889 29.318  1.00 69.10  ? 67  PRO A CA  1 
ATOM   272  C  C   . PRO A 1 38  ? -14.774 36.937 29.521  1.00 68.65  ? 67  PRO A C   1 
ATOM   273  O  O   . PRO A 1 38  ? -14.299 37.061 30.647  1.00 68.97  ? 67  PRO A O   1 
ATOM   274  C  CB  . PRO A 1 38  ? -16.945 38.172 29.832  1.00 69.88  ? 67  PRO A CB  1 
ATOM   275  C  CG  . PRO A 1 38  ? -18.110 37.731 30.644  1.00 70.66  ? 67  PRO A CG  1 
ATOM   276  C  CD  . PRO A 1 38  ? -17.740 36.412 31.208  1.00 69.39  ? 67  PRO A CD  1 
ATOM   277  N  N   . THR A 1 39  ? -14.020 36.787 28.430  1.00 67.67  ? 68  THR A N   1 
ATOM   278  C  CA  . THR A 1 39  ? -12.563 36.773 28.432  1.00 66.98  ? 68  THR A CA  1 
ATOM   279  C  C   . THR A 1 39  ? -11.994 37.726 27.362  1.00 66.16  ? 68  THR A C   1 
ATOM   280  O  O   . THR A 1 39  ? -12.739 38.269 26.563  1.00 66.20  ? 68  THR A O   1 
ATOM   281  C  CB  . THR A 1 39  ? -12.071 35.323 28.217  1.00 68.26  ? 68  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 39  ? -12.571 34.817 26.979  1.00 68.98  ? 68  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 39  ? -12.431 34.406 29.360  1.00 68.73  ? 68  THR A CG2 1 
ATOM   284  N  N   . TRP A 1 40  ? -10.681 37.943 27.366  1.00 65.40  ? 69  TRP A N   1 
ATOM   285  C  CA  . TRP A 1 40  ? -9.974  38.769 26.394  1.00 65.31  ? 69  TRP A CA  1 
ATOM   286  C  C   . TRP A 1 40  ? -8.973  37.874 25.640  1.00 65.48  ? 69  TRP A C   1 
ATOM   287  O  O   . TRP A 1 40  ? -8.580  36.836 26.159  1.00 65.99  ? 69  TRP A O   1 
ATOM   288  C  CB  . TRP A 1 40  ? -9.225  39.911 27.109  1.00 64.90  ? 69  TRP A CB  1 
ATOM   289  C  CG  . TRP A 1 40  ? -10.070 41.057 27.600  1.00 64.97  ? 69  TRP A CG  1 
ATOM   290  C  CD1 . TRP A 1 40  ? -11.417 41.224 27.455  1.00 65.43  ? 69  TRP A CD1 1 
ATOM   291  C  CD2 . TRP A 1 40  ? -9.599  42.210 28.309  1.00 65.09  ? 69  TRP A CD2 1 
ATOM   292  N  NE1 . TRP A 1 40  ? -11.812 42.410 28.025  1.00 65.56  ? 69  TRP A NE1 1 
ATOM   293  C  CE2 . TRP A 1 40  ? -10.714 43.036 28.557  1.00 65.59  ? 69  TRP A CE2 1 
ATOM   294  C  CE3 . TRP A 1 40  ? -8.337  42.630 28.754  1.00 65.40  ? 69  TRP A CE3 1 
ATOM   295  C  CZ2 . TRP A 1 40  ? -10.601 44.257 29.221  1.00 66.11  ? 69  TRP A CZ2 1 
ATOM   296  C  CZ3 . TRP A 1 40  ? -8.234  43.828 29.428  1.00 65.84  ? 69  TRP A CZ3 1 
ATOM   297  C  CH2 . TRP A 1 40  ? -9.354  44.627 29.654  1.00 65.99  ? 69  TRP A CH2 1 
ATOM   298  N  N   . GLY A 1 41  ? -8.584  38.261 24.427  1.00 64.74  ? 70  GLY A N   1 
ATOM   299  C  CA  . GLY A 1 41  ? -7.637  37.477 23.645  1.00 64.28  ? 70  GLY A CA  1 
ATOM   300  C  C   . GLY A 1 41  ? -7.117  38.153 22.395  1.00 63.74  ? 70  GLY A C   1 
ATOM   301  O  O   . GLY A 1 41  ? -7.749  39.055 21.849  1.00 64.12  ? 70  GLY A O   1 
ATOM   302  N  N   . ILE A 1 42  ? -5.965  37.716 21.926  1.00 62.85  ? 71  ILE A N   1 
ATOM   303  C  CA  . ILE A 1 42  ? -5.376  38.231 20.700  1.00 62.69  ? 71  ILE A CA  1 
ATOM   304  C  C   . ILE A 1 42  ? -5.759  37.290 19.553  1.00 61.93  ? 71  ILE A C   1 
ATOM   305  O  O   . ILE A 1 42  ? -5.371  36.120 19.553  1.00 62.13  ? 71  ILE A O   1 
ATOM   306  C  CB  . ILE A 1 42  ? -3.851  38.404 20.832  1.00 63.15  ? 71  ILE A CB  1 
ATOM   307  C  CG1 . ILE A 1 42  ? -3.520  39.377 21.964  1.00 64.30  ? 71  ILE A CG1 1 
ATOM   308  C  CG2 . ILE A 1 42  ? -3.269  38.886 19.521  1.00 63.52  ? 71  ILE A CG2 1 
ATOM   309  C  CD1 . ILE A 1 42  ? -2.924  38.750 23.133  1.00 65.56  ? 71  ILE A CD1 1 
ATOM   310  N  N   . ASN A 1 43  ? -6.573  37.791 18.616  1.00 60.60  ? 72  ASN A N   1 
ATOM   311  C  CA  . ASN A 1 43  ? -7.085  37.030 17.478  1.00 59.77  ? 72  ASN A CA  1 
ATOM   312  C  C   . ASN A 1 43  ? -8.026  35.877 17.874  1.00 59.33  ? 72  ASN A C   1 
ATOM   313  O  O   . ASN A 1 43  ? -8.257  34.979 17.070  1.00 59.87  ? 72  ASN A O   1 
ATOM   314  C  CB  . ASN A 1 43  ? -5.958  36.531 16.576  1.00 60.09  ? 72  ASN A CB  1 
ATOM   315  C  CG  . ASN A 1 43  ? -4.970  37.586 16.175  1.00 62.21  ? 72  ASN A CG  1 
ATOM   316  O  OD1 . ASN A 1 43  ? -5.145  38.765 16.464  1.00 63.45  ? 72  ASN A OD1 1 
ATOM   317  N  ND2 . ASN A 1 43  ? -3.898  37.182 15.500  1.00 61.96  ? 72  ASN A ND2 1 
ATOM   318  N  N   . GLY A 1 44  ? -8.581  35.921 19.080  1.00 58.23  ? 73  GLY A N   1 
ATOM   319  C  CA  . GLY A 1 44  ? -9.493  34.895 19.561  1.00 58.01  ? 73  GLY A CA  1 
ATOM   320  C  C   . GLY A 1 44  ? -10.142 35.263 20.876  1.00 57.83  ? 73  GLY A C   1 
ATOM   321  O  O   . GLY A 1 44  ? -10.010 36.392 21.352  1.00 58.20  ? 73  GLY A O   1 
ATOM   322  N  N   . PRO A 1 45  ? -10.859 34.316 21.495  1.00 57.30  ? 74  PRO A N   1 
ATOM   323  C  CA  . PRO A 1 45  ? -11.532 34.624 22.773  1.00 57.27  ? 74  PRO A CA  1 
ATOM   324  C  C   . PRO A 1 45  ? -10.616 34.649 24.003  1.00 57.11  ? 74  PRO A C   1 
ATOM   325  O  O   . PRO A 1 45  ? -10.986 35.205 25.039  1.00 57.38  ? 74  PRO A O   1 
ATOM   326  C  CB  . PRO A 1 45  ? -12.577 33.514 22.890  1.00 57.75  ? 74  PRO A CB  1 
ATOM   327  C  CG  . PRO A 1 45  ? -11.955 32.368 22.192  1.00 58.11  ? 74  PRO A CG  1 
ATOM   328  C  CD  . PRO A 1 45  ? -11.115 32.931 21.065  1.00 56.58  ? 74  PRO A CD  1 
ATOM   329  N  N   . LEU A 1 46  ? -9.439  34.026 23.889  1.00 56.37  ? 75  LEU A N   1 
ATOM   330  C  CA  . LEU A 1 46  ? -8.457  33.908 24.953  1.00 56.05  ? 75  LEU A CA  1 
ATOM   331  C  C   . LEU A 1 46  ? -7.096  33.592 24.347  1.00 56.41  ? 75  LEU A C   1 
ATOM   332  O  O   . LEU A 1 46  ? -7.009  33.045 23.235  1.00 56.86  ? 75  LEU A O   1 
ATOM   333  C  CB  . LEU A 1 46  ? -8.880  32.788 25.902  1.00 55.94  ? 75  LEU A CB  1 
ATOM   334  C  CG  . LEU A 1 46  ? -8.164  32.695 27.219  1.00 57.05  ? 75  LEU A CG  1 
ATOM   335  C  CD1 . LEU A 1 46  ? -8.971  33.337 28.313  1.00 57.57  ? 75  LEU A CD1 1 
ATOM   336  C  CD2 . LEU A 1 46  ? -7.947  31.264 27.568  1.00 57.73  ? 75  LEU A CD2 1 
ATOM   337  N  N   . LEU A 1 47  ? -6.030  33.944 25.085  1.00 55.83  ? 76  LEU A N   1 
ATOM   338  C  CA  . LEU A 1 47  ? -4.631  33.760 24.717  1.00 55.39  ? 76  LEU A CA  1 
ATOM   339  C  C   . LEU A 1 47  ? -4.346  34.380 23.327  1.00 55.75  ? 76  LEU A C   1 
ATOM   340  O  O   . LEU A 1 47  ? -4.882  35.443 23.067  1.00 55.61  ? 76  LEU A O   1 
ATOM   341  C  CB  . LEU A 1 47  ? -4.217  32.292 24.890  1.00 54.99  ? 76  LEU A CB  1 
ATOM   342  C  CG  . LEU A 1 47  ? -4.078  31.901 26.340  1.00 55.82  ? 76  LEU A CG  1 
ATOM   343  C  CD1 . LEU A 1 47  ? -3.982  30.423 26.493  1.00 56.04  ? 76  LEU A CD1 1 
ATOM   344  C  CD2 . LEU A 1 47  ? -2.884  32.589 26.967  1.00 56.84  ? 76  LEU A CD2 1 
ATOM   345  N  N   . GLY A 1 48  ? -3.482  33.802 22.497  1.00 56.34  ? 77  GLY A N   1 
ATOM   346  C  CA  . GLY A 1 48  ? -3.161  34.392 21.204  1.00 57.24  ? 77  GLY A CA  1 
ATOM   347  C  C   . GLY A 1 48  ? -2.392  33.476 20.292  1.00 58.21  ? 77  GLY A C   1 
ATOM   348  O  O   . GLY A 1 48  ? -2.227  32.292 20.577  1.00 58.59  ? 77  GLY A O   1 
ATOM   349  N  N   . PRO A 1 49  ? -1.879  34.025 19.192  1.00 58.55  ? 78  PRO A N   1 
ATOM   350  C  CA  . PRO A 1 49  ? -1.121  33.191 18.254  1.00 58.99  ? 78  PRO A CA  1 
ATOM   351  C  C   . PRO A 1 49  ? 0.353   33.010 18.639  1.00 59.44  ? 78  PRO A C   1 
ATOM   352  O  O   . PRO A 1 49  ? 0.856   33.652 19.559  1.00 59.50  ? 78  PRO A O   1 
ATOM   353  C  CB  . PRO A 1 49  ? -1.271  33.955 16.939  1.00 59.67  ? 78  PRO A CB  1 
ATOM   354  C  CG  . PRO A 1 49  ? -1.334  35.402 17.375  1.00 59.95  ? 78  PRO A CG  1 
ATOM   355  C  CD  . PRO A 1 49  ? -1.979  35.428 18.735  1.00 58.16  ? 78  PRO A CD  1 
ATOM   356  N  N   . ALA A 1 50  ? 1.039   32.131 17.927  1.00 59.43  ? 79  ALA A N   1 
ATOM   357  C  CA  . ALA A 1 50  ? 2.454   31.914 18.108  1.00 60.18  ? 79  ALA A CA  1 
ATOM   358  C  C   . ALA A 1 50  ? 3.122   32.575 16.899  1.00 61.15  ? 79  ALA A C   1 
ATOM   359  O  O   . ALA A 1 50  ? 2.982   32.079 15.787  1.00 61.53  ? 79  ALA A O   1 
ATOM   360  C  CB  . ALA A 1 50  ? 2.755   30.428 18.123  1.00 59.97  ? 79  ALA A CB  1 
ATOM   361  N  N   . MET A 1 51  ? 3.785   33.716 17.097  1.00 61.13  ? 80  MET A N   1 
ATOM   362  C  CA  . MET A 1 51  ? 4.452   34.404 16.004  1.00 61.69  ? 80  MET A CA  1 
ATOM   363  C  C   . MET A 1 51  ? 5.776   33.702 15.730  1.00 62.38  ? 80  MET A C   1 
ATOM   364  O  O   . MET A 1 51  ? 6.631   33.659 16.610  1.00 62.22  ? 80  MET A O   1 
ATOM   365  C  CB  . MET A 1 51  ? 4.685   35.885 16.353  1.00 62.32  ? 80  MET A CB  1 
ATOM   366  C  CG  . MET A 1 51  ? 3.431   36.588 16.837  1.00 64.20  ? 80  MET A CG  1 
ATOM   367  S  SD  . MET A 1 51  ? 3.577   38.398 16.933  1.00 66.38  ? 80  MET A SD  1 
ATOM   368  C  CE  . MET A 1 51  ? 4.813   38.566 18.174  1.00 63.89  ? 80  MET A CE  1 
ATOM   369  N  N   . ARG A 1 52  ? 5.932   33.108 14.533  1.00 62.85  ? 81  ARG A N   1 
ATOM   370  C  CA  . ARG A 1 52  ? 7.178   32.443 14.179  1.00 63.58  ? 81  ARG A CA  1 
ATOM   371  C  C   . ARG A 1 52  ? 8.051   33.464 13.473  1.00 64.88  ? 81  ARG A C   1 
ATOM   372  O  O   . ARG A 1 52  ? 7.683   33.994 12.420  1.00 65.09  ? 81  ARG A O   1 
ATOM   373  C  CB  . ARG A 1 52  ? 6.951   31.199 13.313  1.00 64.32  ? 81  ARG A CB  1 
ATOM   374  C  CG  . ARG A 1 52  ? 8.200   30.321 13.198  1.00 67.14  ? 81  ARG A CG  1 
ATOM   375  C  CD  . ARG A 1 52  ? 7.845   28.838 13.128  1.00 70.65  ? 81  ARG A CD  1 
ATOM   376  N  NE  . ARG A 1 52  ? 8.937   27.970 13.584  1.00 73.49  ? 81  ARG A NE  1 
ATOM   377  C  CZ  . ARG A 1 52  ? 8.787   26.712 13.992  1.00 74.85  ? 81  ARG A CZ  1 
ATOM   378  N  NH1 . ARG A 1 52  ? 7.582   26.156 14.026  1.00 74.44  ? 81  ARG A NH1 1 
ATOM   379  N  NH2 . ARG A 1 52  ? 9.839   26.005 14.387  1.00 74.16  ? 81  ARG A NH2 1 
ATOM   380  N  N   . LEU A 1 53  ? 9.184   33.793 14.097  1.00 65.41  ? 82  LEU A N   1 
ATOM   381  C  CA  . LEU A 1 53  ? 10.118  34.782 13.577  1.00 66.10  ? 82  LEU A CA  1 
ATOM   382  C  C   . LEU A 1 53  ? 11.485  34.160 13.364  1.00 67.39  ? 82  LEU A C   1 
ATOM   383  O  O   . LEU A 1 53  ? 11.901  33.296 14.126  1.00 67.26  ? 82  LEU A O   1 
ATOM   384  C  CB  . LEU A 1 53  ? 10.220  35.982 14.529  1.00 65.80  ? 82  LEU A CB  1 
ATOM   385  C  CG  . LEU A 1 53  ? 8.896   36.606 14.957  1.00 66.68  ? 82  LEU A CG  1 
ATOM   386  C  CD1 . LEU A 1 53  ? 9.113   37.655 16.006  1.00 67.13  ? 82  LEU A CD1 1 
ATOM   387  C  CD2 . LEU A 1 53  ? 8.145   37.161 13.775  1.00 67.25  ? 82  LEU A CD2 1 
ATOM   388  N  N   . GLN A 1 54  ? 12.174  34.585 12.312  1.00 68.67  ? 83  GLN A N   1 
ATOM   389  C  CA  . GLN A 1 54  ? 13.495  34.066 11.988  1.00 70.41  ? 83  GLN A CA  1 
ATOM   390  C  C   . GLN A 1 54  ? 14.556  35.043 12.492  1.00 71.05  ? 83  GLN A C   1 
ATOM   391  O  O   . GLN A 1 54  ? 14.365  36.257 12.395  1.00 71.08  ? 83  GLN A O   1 
ATOM   392  C  CB  . GLN A 1 54  ? 13.622  33.886 10.461  1.00 73.13  ? 83  GLN A CB  1 
ATOM   393  C  CG  . GLN A 1 54  ? 14.485  32.700 10.041  1.00 78.50  ? 83  GLN A CG  1 
ATOM   394  C  CD  . GLN A 1 54  ? 13.744  31.377 10.113  1.00 85.24  ? 83  GLN A CD  1 
ATOM   395  O  OE1 . GLN A 1 54  ? 12.499  31.318 10.163  1.00 87.02  ? 83  GLN A OE1 1 
ATOM   396  N  NE2 . GLN A 1 54  ? 14.501  30.277 10.109  1.00 86.23  ? 83  GLN A NE2 1 
ATOM   397  N  N   . ARG A 1 55  ? 15.668  34.523 13.035  1.00 71.36  ? 84  ARG A N   1 
ATOM   398  C  CA  . ARG A 1 55  ? 16.756  35.367 13.522  1.00 72.09  ? 84  ARG A CA  1 
ATOM   399  C  C   . ARG A 1 55  ? 17.383  36.094 12.347  1.00 72.58  ? 84  ARG A C   1 
ATOM   400  O  O   . ARG A 1 55  ? 17.679  35.480 11.321  1.00 72.84  ? 84  ARG A O   1 
ATOM   401  C  CB  . ARG A 1 55  ? 17.828  34.565 14.286  1.00 73.55  ? 84  ARG A CB  1 
ATOM   402  C  CG  . ARG A 1 55  ? 18.846  35.493 14.941  1.00 77.07  ? 84  ARG A CG  1 
ATOM   403  C  CD  . ARG A 1 55  ? 20.090  34.826 15.495  1.00 80.43  ? 84  ARG A CD  1 
ATOM   404  N  NE  . ARG A 1 55  ? 20.866  35.778 16.296  1.00 83.31  ? 84  ARG A NE  1 
ATOM   405  C  CZ  . ARG A 1 55  ? 21.801  35.437 17.179  1.00 84.99  ? 84  ARG A CZ  1 
ATOM   406  N  NH1 . ARG A 1 55  ? 22.096  34.157 17.385  1.00 84.43  ? 84  ARG A NH1 1 
ATOM   407  N  NH2 . ARG A 1 55  ? 22.438  36.372 17.876  1.00 84.40  ? 84  ARG A NH2 1 
ATOM   408  N  N   . GLY A 1 56  ? 17.519  37.400 12.481  1.00 72.37  ? 85  GLY A N   1 
ATOM   409  C  CA  . GLY A 1 56  ? 18.066  38.228 11.421  1.00 72.78  ? 85  GLY A CA  1 
ATOM   410  C  C   . GLY A 1 56  ? 16.973  38.957 10.675  1.00 72.94  ? 85  GLY A C   1 
ATOM   411  O  O   . GLY A 1 56  ? 17.134  40.125 10.321  1.00 73.34  ? 85  GLY A O   1 
ATOM   412  N  N   . LYS A 1 57  ? 15.842  38.284 10.452  1.00 72.71  ? 86  LYS A N   1 
ATOM   413  C  CA  . LYS A 1 57  ? 14.726  38.891 9.741   1.00 73.18  ? 86  LYS A CA  1 
ATOM   414  C  C   . LYS A 1 57  ? 13.970  39.923 10.586  1.00 73.15  ? 86  LYS A C   1 
ATOM   415  O  O   . LYS A 1 57  ? 13.970  39.866 11.819  1.00 73.33  ? 86  LYS A O   1 
ATOM   416  C  CB  . LYS A 1 57  ? 13.787  37.823 9.158   1.00 75.40  ? 86  LYS A CB  1 
ATOM   417  C  CG  . LYS A 1 57  ? 14.428  37.019 8.023   1.00 80.29  ? 86  LYS A CG  1 
ATOM   418  C  CD  . LYS A 1 57  ? 13.382  36.224 7.227   1.00 85.50  ? 86  LYS A CD  1 
ATOM   419  C  CE  . LYS A 1 57  ? 13.775  35.971 5.780   1.00 89.11  ? 86  LYS A CE  1 
ATOM   420  N  NZ  . LYS A 1 57  ? 12.653  35.399 4.980   1.00 90.58  ? 86  LYS A NZ  1 
ATOM   421  N  N   . ASP A 1 58  ? 13.378  40.903 9.908   1.00 72.60  ? 87  ASP A N   1 
ATOM   422  C  CA  . ASP A 1 58  ? 12.633  41.967 10.556  1.00 72.72  ? 87  ASP A CA  1 
ATOM   423  C  C   . ASP A 1 58  ? 11.132  41.714 10.506  1.00 71.74  ? 87  ASP A C   1 
ATOM   424  O  O   . ASP A 1 58  ? 10.656  40.928 9.687   1.00 72.16  ? 87  ASP A O   1 
ATOM   425  C  CB  . ASP A 1 58  ? 12.954  43.314 9.885   1.00 75.57  ? 87  ASP A CB  1 
ATOM   426  C  CG  . ASP A 1 58  ? 14.352  43.801 10.184  1.00 81.96  ? 87  ASP A CG  1 
ATOM   427  O  OD1 . ASP A 1 58  ? 15.308  43.006 10.012  1.00 82.15  ? 87  ASP A OD1 1 
ATOM   428  O  OD2 . ASP A 1 58  ? 14.495  44.980 10.587  1.00 85.33  ? 87  ASP A OD2 1 
ATOM   429  N  N   . VAL A 1 59  ? 10.377  42.403 11.371  1.00 70.22  ? 88  VAL A N   1 
ATOM   430  C  CA  . VAL A 1 59  ? 8.928   42.301 11.411  1.00 69.10  ? 88  VAL A CA  1 
ATOM   431  C  C   . VAL A 1 59  ? 8.341   43.569 12.018  1.00 67.81  ? 88  VAL A C   1 
ATOM   432  O  O   . VAL A 1 59  ? 8.953   44.197 12.876  1.00 67.87  ? 88  VAL A O   1 
ATOM   433  C  CB  . VAL A 1 59  ? 8.451   41.015 12.155  1.00 69.85  ? 88  VAL A CB  1 
ATOM   434  C  CG1 . VAL A 1 59  ? 8.756   41.084 13.648  1.00 70.58  ? 88  VAL A CG1 1 
ATOM   435  C  CG2 . VAL A 1 59  ? 6.970   40.739 11.913  1.00 70.16  ? 88  VAL A CG2 1 
ATOM   436  N  N   . ALA A 1 60  ? 7.175   43.971 11.541  1.00 66.82  ? 89  ALA A N   1 
ATOM   437  C  CA  . ALA A 1 60  ? 6.455   45.114 12.079  1.00 66.11  ? 89  ALA A CA  1 
ATOM   438  C  C   . ALA A 1 60  ? 5.183   44.523 12.635  1.00 65.31  ? 89  ALA A C   1 
ATOM   439  O  O   . ALA A 1 60  ? 4.457   43.863 11.898  1.00 65.25  ? 89  ALA A O   1 
ATOM   440  C  CB  . ALA A 1 60  ? 6.128   46.095 10.973  1.00 66.18  ? 89  ALA A CB  1 
ATOM   441  N  N   . ILE A 1 61  ? 4.933   44.688 13.938  1.00 64.55  ? 90  ILE A N   1 
ATOM   442  C  CA  . ILE A 1 61  ? 3.744   44.090 14.537  1.00 63.87  ? 90  ILE A CA  1 
ATOM   443  C  C   . ILE A 1 61  ? 2.661   45.133 14.786  1.00 63.72  ? 90  ILE A C   1 
ATOM   444  O  O   . ILE A 1 61  ? 2.774   45.983 15.657  1.00 63.08  ? 90  ILE A O   1 
ATOM   445  C  CB  . ILE A 1 61  ? 4.077   43.237 15.775  1.00 63.46  ? 90  ILE A CB  1 
ATOM   446  C  CG1 . ILE A 1 61  ? 5.200   42.243 15.447  1.00 63.52  ? 90  ILE A CG1 1 
ATOM   447  C  CG2 . ILE A 1 61  ? 2.831   42.509 16.254  1.00 63.69  ? 90  ILE A CG2 1 
ATOM   448  C  CD1 . ILE A 1 61  ? 5.930   41.796 16.580  1.00 64.34  ? 90  ILE A CD1 1 
ATOM   449  N  N   . ASN A 1 62  ? 1.613   45.060 13.980  1.00 64.31  ? 91  ASN A N   1 
ATOM   450  C  CA  . ASN A 1 62  ? 0.491   45.972 14.043  1.00 65.33  ? 91  ASN A CA  1 
ATOM   451  C  C   . ASN A 1 62  ? -0.518  45.515 15.076  1.00 66.04  ? 91  ASN A C   1 
ATOM   452  O  O   . ASN A 1 62  ? -1.421  44.727 14.775  1.00 66.21  ? 91  ASN A O   1 
ATOM   453  C  CB  . ASN A 1 62  ? -0.134  46.106 12.659  1.00 66.73  ? 91  ASN A CB  1 
ATOM   454  C  CG  . ASN A 1 62  ? 0.799   46.779 11.678  1.00 69.80  ? 91  ASN A CG  1 
ATOM   455  O  OD1 . ASN A 1 62  ? 1.523   47.716 12.020  1.00 70.43  ? 91  ASN A OD1 1 
ATOM   456  N  ND2 . ASN A 1 62  ? 0.809   46.320 10.438  1.00 71.09  ? 91  ASN A ND2 1 
ATOM   457  N  N   . VAL A 1 63  ? -0.349  46.003 16.312  1.00 66.35  ? 92  VAL A N   1 
ATOM   458  C  CA  . VAL A 1 63  ? -1.215  45.646 17.434  1.00 66.88  ? 92  VAL A CA  1 
ATOM   459  C  C   . VAL A 1 63  ? -2.399  46.601 17.498  1.00 67.46  ? 92  VAL A C   1 
ATOM   460  O  O   . VAL A 1 63  ? -2.228  47.773 17.815  1.00 67.65  ? 92  VAL A O   1 
ATOM   461  C  CB  . VAL A 1 63  ? -0.458  45.597 18.787  1.00 67.34  ? 92  VAL A CB  1 
ATOM   462  C  CG1 . VAL A 1 63  ? -1.329  44.980 19.870  1.00 67.87  ? 92  VAL A CG1 1 
ATOM   463  C  CG2 . VAL A 1 63  ? 0.853   44.837 18.664  1.00 67.84  ? 92  VAL A CG2 1 
ATOM   464  N  N   . THR A 1 64  ? -3.597  46.095 17.204  1.00 67.54  ? 93  THR A N   1 
ATOM   465  C  CA  . THR A 1 64  ? -4.830  46.872 17.212  1.00 68.03  ? 93  THR A CA  1 
ATOM   466  C  C   . THR A 1 64  ? -5.557  46.597 18.511  1.00 68.28  ? 93  THR A C   1 
ATOM   467  O  O   . THR A 1 64  ? -5.763  45.434 18.855  1.00 68.86  ? 93  THR A O   1 
ATOM   468  C  CB  . THR A 1 64  ? -5.755  46.420 16.068  1.00 69.46  ? 93  THR A CB  1 
ATOM   469  O  OG1 . THR A 1 64  ? -5.019  46.209 14.854  1.00 70.83  ? 93  THR A OG1 1 
ATOM   470  C  CG2 . THR A 1 64  ? -6.902  47.372 15.847  1.00 69.59  ? 93  THR A CG2 1 
ATOM   471  N  N   . ASN A 1 65  ? -5.962  47.648 19.228  1.00 67.69  ? 94  ASN A N   1 
ATOM   472  C  CA  . ASN A 1 65  ? -6.705  47.481 20.466  1.00 67.34  ? 94  ASN A CA  1 
ATOM   473  C  C   . ASN A 1 65  ? -8.175  47.549 20.133  1.00 66.83  ? 94  ASN A C   1 
ATOM   474  O  O   . ASN A 1 65  ? -8.643  48.582 19.692  1.00 67.00  ? 94  ASN A O   1 
ATOM   475  C  CB  . ASN A 1 65  ? -6.356  48.580 21.485  1.00 68.44  ? 94  ASN A CB  1 
ATOM   476  C  CG  . ASN A 1 65  ? -6.959  48.358 22.863  1.00 71.63  ? 94  ASN A CG  1 
ATOM   477  O  OD1 . ASN A 1 65  ? -7.661  47.372 23.119  1.00 72.66  ? 94  ASN A OD1 1 
ATOM   478  N  ND2 . ASN A 1 65  ? -6.695  49.263 23.796  1.00 71.85  ? 94  ASN A ND2 1 
ATOM   479  N  N   . ALA A 1 66  ? -8.892  46.450 20.305  1.00 66.22  ? 95  ALA A N   1 
ATOM   480  C  CA  . ALA A 1 66  ? -10.340 46.395 20.108  1.00 66.17  ? 95  ALA A CA  1 
ATOM   481  C  C   . ALA A 1 66  ? -11.083 46.172 21.435  1.00 66.54  ? 95  ALA A C   1 
ATOM   482  O  O   . ALA A 1 66  ? -12.233 45.742 21.429  1.00 66.94  ? 95  ALA A O   1 
ATOM   483  C  CB  . ALA A 1 66  ? -10.697 45.294 19.130  1.00 66.27  ? 95  ALA A CB  1 
ATOM   484  N  N   . LEU A 1 67  ? -10.425 46.433 22.570  1.00 66.40  ? 96  LEU A N   1 
ATOM   485  C  CA  . LEU A 1 67  ? -11.007 46.289 23.891  1.00 66.85  ? 96  LEU A CA  1 
ATOM   486  C  C   . LEU A 1 67  ? -11.663 47.612 24.296  1.00 67.59  ? 96  LEU A C   1 
ATOM   487  O  O   . LEU A 1 67  ? -11.300 48.668 23.770  1.00 68.20  ? 96  LEU A O   1 
ATOM   488  C  CB  . LEU A 1 67  ? -9.884  45.967 24.892  1.00 66.80  ? 96  LEU A CB  1 
ATOM   489  C  CG  . LEU A 1 67  ? -9.120  44.688 24.691  1.00 67.94  ? 96  LEU A CG  1 
ATOM   490  C  CD1 . LEU A 1 67  ? -8.031  44.555 25.743  1.00 68.38  ? 96  LEU A CD1 1 
ATOM   491  C  CD2 . LEU A 1 67  ? -10.040 43.498 24.747  1.00 68.55  ? 96  LEU A CD2 1 
ATOM   492  N  N   . PRO A 1 68  ? -12.590 47.596 25.269  1.00 67.37  ? 97  PRO A N   1 
ATOM   493  C  CA  . PRO A 1 68  ? -13.181 48.862 25.726  1.00 67.66  ? 97  PRO A CA  1 
ATOM   494  C  C   . PRO A 1 68  ? -12.204 49.766 26.499  1.00 68.25  ? 97  PRO A C   1 
ATOM   495  O  O   . PRO A 1 68  ? -12.511 50.941 26.721  1.00 69.01  ? 97  PRO A O   1 
ATOM   496  C  CB  . PRO A 1 68  ? -14.330 48.404 26.618  1.00 68.25  ? 97  PRO A CB  1 
ATOM   497  C  CG  . PRO A 1 68  ? -13.925 47.067 27.100  1.00 68.48  ? 97  PRO A CG  1 
ATOM   498  C  CD  . PRO A 1 68  ? -13.141 46.439 26.000  1.00 66.75  ? 97  PRO A CD  1 
ATOM   499  N  N   . GLU A 1 69  ? -11.032 49.241 26.912  1.00 67.59  ? 98  GLU A N   1 
ATOM   500  C  CA  . GLU A 1 69  ? -10.068 50.042 27.663  1.00 67.38  ? 98  GLU A CA  1 
ATOM   501  C  C   . GLU A 1 69  ? -8.642  49.914 27.137  1.00 66.08  ? 98  GLU A C   1 
ATOM   502  O  O   . GLU A 1 69  ? -8.341  48.987 26.384  1.00 66.17  ? 98  GLU A O   1 
ATOM   503  C  CB  . GLU A 1 69  ? -10.138 49.718 29.159  1.00 70.33  ? 98  GLU A CB  1 
ATOM   504  C  CG  . GLU A 1 69  ? -9.784  48.281 29.466  1.00 76.31  ? 98  GLU A CG  1 
ATOM   505  C  CD  . GLU A 1 69  ? -10.064 47.915 30.908  1.00 84.54  ? 98  GLU A CD  1 
ATOM   506  O  OE1 . GLU A 1 69  ? -9.094  47.683 31.672  1.00 85.70  ? 98  GLU A OE1 1 
ATOM   507  O  OE2 . GLU A 1 69  ? -11.262 47.873 31.275  1.00 87.04  ? 98  GLU A OE2 1 
ATOM   508  N  N   . ALA A 1 70  ? -7.776  50.885 27.498  1.00 64.44  ? 99  ALA A N   1 
ATOM   509  C  CA  . ALA A 1 70  ? -6.393  50.924 27.039  1.00 62.89  ? 99  ALA A CA  1 
ATOM   510  C  C   . ALA A 1 70  ? -5.590  49.753 27.543  1.00 61.22  ? 99  ALA A C   1 
ATOM   511  O  O   . ALA A 1 70  ? -5.839  49.229 28.626  1.00 60.81  ? 99  ALA A O   1 
ATOM   512  C  CB  . ALA A 1 70  ? -5.730  52.232 27.441  1.00 62.72  ? 99  ALA A CB  1 
ATOM   513  N  N   . THR A 1 71  ? -4.628  49.342 26.735  1.00 60.24  ? 100 THR A N   1 
ATOM   514  C  CA  . THR A 1 71  ? -3.732  48.229 27.010  1.00 60.07  ? 100 THR A CA  1 
ATOM   515  C  C   . THR A 1 71  ? -2.367  48.513 26.380  1.00 60.25  ? 100 THR A C   1 
ATOM   516  O  O   . THR A 1 71  ? -2.222  49.439 25.588  1.00 60.82  ? 100 THR A O   1 
ATOM   517  C  CB  . THR A 1 71  ? -4.336  46.932 26.394  1.00 60.93  ? 100 THR A CB  1 
ATOM   518  O  OG1 . THR A 1 71  ? -3.617  45.798 26.873  1.00 61.64  ? 100 THR A OG1 1 
ATOM   519  C  CG2 . THR A 1 71  ? -4.279  46.929 24.870  1.00 61.00  ? 100 THR A CG2 1 
ATOM   520  N  N   . THR A 1 72  ? -1.359  47.733 26.736  1.00 59.89  ? 101 THR A N   1 
ATOM   521  C  CA  . THR A 1 72  ? -0.053  47.794 26.082  1.00 60.13  ? 101 THR A CA  1 
ATOM   522  C  C   . THR A 1 72  ? 0.259   46.330 25.612  1.00 59.76  ? 101 THR A C   1 
ATOM   523  O  O   . THR A 1 72  ? -0.615  45.463 25.723  1.00 60.04  ? 101 THR A O   1 
ATOM   524  C  CB  . THR A 1 72  ? 1.018   48.481 26.972  1.00 61.61  ? 101 THR A CB  1 
ATOM   525  O  OG1 . THR A 1 72  ? 1.604   47.512 27.829  1.00 62.91  ? 101 THR A OG1 1 
ATOM   526  C  CG2 . THR A 1 72  ? 0.483   49.666 27.789  1.00 61.77  ? 101 THR A CG2 1 
ATOM   527  N  N   . MET A 1 73  ? 1.448   46.057 25.066  1.00 59.13  ? 102 MET A N   1 
ATOM   528  C  CA  . MET A 1 73  ? 1.800   44.699 24.650  1.00 59.22  ? 102 MET A CA  1 
ATOM   529  C  C   . MET A 1 73  ? 3.300   44.499 24.726  1.00 59.68  ? 102 MET A C   1 
ATOM   530  O  O   . MET A 1 73  ? 4.043   44.942 23.852  1.00 59.68  ? 102 MET A O   1 
ATOM   531  C  CB  . MET A 1 73  ? 1.237   44.348 23.262  1.00 59.42  ? 102 MET A CB  1 
ATOM   532  C  CG  . MET A 1 73  ? 1.231   42.849 22.968  1.00 61.33  ? 102 MET A CG  1 
ATOM   533  S  SD  . MET A 1 73  ? 0.247   41.845 24.128  1.00 64.17  ? 102 MET A SD  1 
ATOM   534  C  CE  . MET A 1 73  ? -1.379  42.556 23.874  1.00 60.66  ? 102 MET A CE  1 
ATOM   535  N  N   . HIS A 1 74  ? 3.748   43.887 25.811  1.00 59.95  ? 103 HIS A N   1 
ATOM   536  C  CA  . HIS A 1 74  ? 5.158   43.628 26.046  1.00 60.91  ? 103 HIS A CA  1 
ATOM   537  C  C   . HIS A 1 74  ? 5.593   42.351 25.336  1.00 61.01  ? 103 HIS A C   1 
ATOM   538  O  O   . HIS A 1 74  ? 4.834   41.389 25.309  1.00 61.66  ? 103 HIS A O   1 
ATOM   539  C  CB  . HIS A 1 74  ? 5.411   43.513 27.555  1.00 62.43  ? 103 HIS A CB  1 
ATOM   540  C  CG  . HIS A 1 74  ? 6.772   43.018 27.910  1.00 65.72  ? 103 HIS A CG  1 
ATOM   541  N  ND1 . HIS A 1 74  ? 7.908   43.550 27.322  1.00 67.58  ? 103 HIS A ND1 1 
ATOM   542  C  CD2 . HIS A 1 74  ? 7.136   42.034 28.766  1.00 67.29  ? 103 HIS A CD2 1 
ATOM   543  C  CE1 . HIS A 1 74  ? 8.925   42.887 27.849  1.00 68.40  ? 103 HIS A CE1 1 
ATOM   544  N  NE2 . HIS A 1 74  ? 8.512   41.964 28.723  1.00 68.58  ? 103 HIS A NE2 1 
ATOM   545  N  N   . TRP A 1 75  ? 6.817   42.326 24.789  1.00 60.13  ? 104 TRP A N   1 
ATOM   546  C  CA  . TRP A 1 75  ? 7.336   41.126 24.129  1.00 59.50  ? 104 TRP A CA  1 
ATOM   547  C  C   . TRP A 1 75  ? 8.375   40.502 25.059  1.00 58.87  ? 104 TRP A C   1 
ATOM   548  O  O   . TRP A 1 75  ? 9.578   40.719 24.872  1.00 59.11  ? 104 TRP A O   1 
ATOM   549  C  CB  . TRP A 1 75  ? 7.967   41.453 22.755  1.00 59.25  ? 104 TRP A CB  1 
ATOM   550  C  CG  . TRP A 1 75  ? 7.226   42.484 21.960  1.00 59.19  ? 104 TRP A CG  1 
ATOM   551  C  CD1 . TRP A 1 75  ? 7.626   43.759 21.704  1.00 59.85  ? 104 TRP A CD1 1 
ATOM   552  C  CD2 . TRP A 1 75  ? 5.914   42.351 21.387  1.00 59.11  ? 104 TRP A CD2 1 
ATOM   553  N  NE1 . TRP A 1 75  ? 6.666   44.418 20.971  1.00 60.17  ? 104 TRP A NE1 1 
ATOM   554  C  CE2 . TRP A 1 75  ? 5.603   43.573 20.762  1.00 59.79  ? 104 TRP A CE2 1 
ATOM   555  C  CE3 . TRP A 1 75  ? 4.999   41.298 21.291  1.00 59.37  ? 104 TRP A CE3 1 
ATOM   556  C  CZ2 . TRP A 1 75  ? 4.400   43.780 20.086  1.00 59.99  ? 104 TRP A CZ2 1 
ATOM   557  C  CZ3 . TRP A 1 75  ? 3.804   41.513 20.641  1.00 59.89  ? 104 TRP A CZ3 1 
ATOM   558  C  CH2 . TRP A 1 75  ? 3.513   42.742 20.050  1.00 59.92  ? 104 TRP A CH2 1 
ATOM   559  N  N   . HIS A 1 76  ? 7.893   39.766 26.086  1.00 57.71  ? 105 HIS A N   1 
ATOM   560  C  CA  . HIS A 1 76  ? 8.682   39.106 27.136  1.00 57.25  ? 105 HIS A CA  1 
ATOM   561  C  C   . HIS A 1 76  ? 9.778   38.192 26.591  1.00 57.31  ? 105 HIS A C   1 
ATOM   562  O  O   . HIS A 1 76  ? 9.492   37.175 25.965  1.00 57.19  ? 105 HIS A O   1 
ATOM   563  C  CB  . HIS A 1 76  ? 7.747   38.330 28.078  1.00 57.03  ? 105 HIS A CB  1 
ATOM   564  C  CG  . HIS A 1 76  ? 8.364   37.862 29.367  1.00 57.07  ? 105 HIS A CG  1 
ATOM   565  N  ND1 . HIS A 1 76  ? 7.887   38.296 30.590  1.00 57.79  ? 105 HIS A ND1 1 
ATOM   566  C  CD2 . HIS A 1 76  ? 9.352   36.962 29.583  1.00 57.68  ? 105 HIS A CD2 1 
ATOM   567  C  CE1 . HIS A 1 76  ? 8.617   37.681 31.499  1.00 58.09  ? 105 HIS A CE1 1 
ATOM   568  N  NE2 . HIS A 1 76  ? 9.507   36.866 30.943  1.00 58.33  ? 105 HIS A NE2 1 
ATOM   569  N  N   . GLY A 1 77  ? 11.025  38.564 26.847  1.00 57.12  ? 106 GLY A N   1 
ATOM   570  C  CA  . GLY A 1 77  ? 12.167  37.781 26.399  1.00 57.33  ? 106 GLY A CA  1 
ATOM   571  C  C   . GLY A 1 77  ? 12.880  38.330 25.183  1.00 57.78  ? 106 GLY A C   1 
ATOM   572  O  O   . GLY A 1 77  ? 13.974  37.866 24.856  1.00 58.08  ? 106 GLY A O   1 
ATOM   573  N  N   . MET A 1 78  ? 12.289  39.323 24.497  1.00 57.79  ? 107 MET A N   1 
ATOM   574  C  CA  . MET A 1 78  ? 12.914  39.891 23.298  1.00 58.36  ? 107 MET A CA  1 
ATOM   575  C  C   . MET A 1 78  ? 14.030  40.898 23.581  1.00 58.79  ? 107 MET A C   1 
ATOM   576  O  O   . MET A 1 78  ? 13.891  41.790 24.418  1.00 58.67  ? 107 MET A O   1 
ATOM   577  C  CB  . MET A 1 78  ? 11.865  40.500 22.356  1.00 59.04  ? 107 MET A CB  1 
ATOM   578  C  CG  . MET A 1 78  ? 10.824  39.500 21.894  1.00 61.17  ? 107 MET A CG  1 
ATOM   579  S  SD  . MET A 1 78  ? 11.500  38.041 21.046  1.00 63.60  ? 107 MET A SD  1 
ATOM   580  C  CE  . MET A 1 78  ? 11.967  38.748 19.520  1.00 61.39  ? 107 MET A CE  1 
ATOM   581  N  N   . GLU A 1 79  ? 15.141  40.749 22.861  1.00 59.40  ? 108 GLU A N   1 
ATOM   582  C  CA  . GLU A 1 79  ? 16.292  41.640 22.970  1.00 60.55  ? 108 GLU A CA  1 
ATOM   583  C  C   . GLU A 1 79  ? 16.099  42.696 21.886  1.00 61.34  ? 108 GLU A C   1 
ATOM   584  O  O   . GLU A 1 79  ? 16.619  42.594 20.780  1.00 61.27  ? 108 GLU A O   1 
ATOM   585  C  CB  . GLU A 1 79  ? 17.607  40.872 22.782  1.00 63.01  ? 108 GLU A CB  1 
ATOM   586  C  CG  . GLU A 1 79  ? 17.636  39.540 23.505  1.00 68.74  ? 108 GLU A CG  1 
ATOM   587  C  CD  . GLU A 1 79  ? 19.001  39.102 23.987  1.00 77.37  ? 108 GLU A CD  1 
ATOM   588  O  OE1 . GLU A 1 79  ? 19.390  37.946 23.700  1.00 78.56  ? 108 GLU A OE1 1 
ATOM   589  O  OE2 . GLU A 1 79  ? 19.680  39.913 24.659  1.00 81.01  ? 108 GLU A OE2 1 
ATOM   590  N  N   . ILE A 1 80  ? 15.239  43.653 22.185  1.00 61.96  ? 109 ILE A N   1 
ATOM   591  C  CA  . ILE A 1 80  ? 14.851  44.723 21.282  1.00 62.95  ? 109 ILE A CA  1 
ATOM   592  C  C   . ILE A 1 80  ? 15.017  46.079 21.985  1.00 64.21  ? 109 ILE A C   1 
ATOM   593  O  O   . ILE A 1 80  ? 15.054  46.141 23.218  1.00 64.23  ? 109 ILE A O   1 
ATOM   594  C  CB  . ILE A 1 80  ? 13.367  44.484 20.888  1.00 63.29  ? 109 ILE A CB  1 
ATOM   595  C  CG1 . ILE A 1 80  ? 12.457  44.463 22.142  1.00 63.84  ? 109 ILE A CG1 1 
ATOM   596  C  CG2 . ILE A 1 80  ? 13.217  43.207 20.056  1.00 63.74  ? 109 ILE A CG2 1 
ATOM   597  C  CD1 . ILE A 1 80  ? 11.011  44.363 21.849  1.00 64.94  ? 109 ILE A CD1 1 
ATOM   598  N  N   . PRO A 1 81  ? 15.085  47.187 21.223  1.00 64.97  ? 110 PRO A N   1 
ATOM   599  C  CA  . PRO A 1 81  ? 15.178  48.506 21.863  1.00 65.48  ? 110 PRO A CA  1 
ATOM   600  C  C   . PRO A 1 81  ? 13.910  48.852 22.644  1.00 66.29  ? 110 PRO A C   1 
ATOM   601  O  O   . PRO A 1 81  ? 12.820  48.403 22.295  1.00 66.01  ? 110 PRO A O   1 
ATOM   602  C  CB  . PRO A 1 81  ? 15.358  49.467 20.681  1.00 66.18  ? 110 PRO A CB  1 
ATOM   603  C  CG  . PRO A 1 81  ? 15.709  48.618 19.516  1.00 66.49  ? 110 PRO A CG  1 
ATOM   604  C  CD  . PRO A 1 81  ? 15.049  47.304 19.754  1.00 64.79  ? 110 PRO A CD  1 
ATOM   605  N  N   . GLY A 1 82  ? 14.068  49.655 23.692  1.00 67.15  ? 111 GLY A N   1 
ATOM   606  C  CA  . GLY A 1 82  ? 12.970  50.084 24.554  1.00 68.31  ? 111 GLY A CA  1 
ATOM   607  C  C   . GLY A 1 82  ? 11.814  50.738 23.822  1.00 69.18  ? 111 GLY A C   1 
ATOM   608  O  O   . GLY A 1 82  ? 10.673  50.715 24.289  1.00 69.20  ? 111 GLY A O   1 
ATOM   609  N  N   . THR A 1 83  ? 12.104  51.311 22.656  1.00 69.71  ? 112 THR A N   1 
ATOM   610  C  CA  . THR A 1 83  ? 11.114  51.957 21.801  1.00 70.56  ? 112 THR A CA  1 
ATOM   611  C  C   . THR A 1 83  ? 10.111  50.951 21.196  1.00 71.60  ? 112 THR A C   1 
ATOM   612  O  O   . THR A 1 83  ? 9.027   51.342 20.781  1.00 71.73  ? 112 THR A O   1 
ATOM   613  C  CB  . THR A 1 83  ? 11.844  52.773 20.732  1.00 71.38  ? 112 THR A CB  1 
ATOM   614  O  OG1 . THR A 1 83  ? 12.694  51.902 19.975  1.00 72.06  ? 112 THR A OG1 1 
ATOM   615  C  CG2 . THR A 1 83  ? 12.677  53.886 21.340  1.00 71.70  ? 112 THR A CG2 1 
ATOM   616  N  N   . SER A 1 84  ? 10.470  49.660 21.155  1.00 72.12  ? 113 SER A N   1 
ATOM   617  C  CA  . SER A 1 84  ? 9.633   48.592 20.613  1.00 72.81  ? 113 SER A CA  1 
ATOM   618  C  C   . SER A 1 84  ? 9.150   47.595 21.684  1.00 73.42  ? 113 SER A C   1 
ATOM   619  O  O   . SER A 1 84  ? 8.384   46.703 21.348  1.00 73.41  ? 113 SER A O   1 
ATOM   620  C  CB  . SER A 1 84  ? 10.412  47.811 19.559  1.00 74.02  ? 113 SER A CB  1 
ATOM   621  O  OG  . SER A 1 84  ? 11.138  48.645 18.669  1.00 76.17  ? 113 SER A OG  1 
ATOM   622  N  N   . ASP A 1 85  ? 9.617   47.716 22.942  1.00 73.88  ? 114 ASP A N   1 
ATOM   623  C  CA  . ASP A 1 85  ? 9.311   46.793 24.041  1.00 75.02  ? 114 ASP A CA  1 
ATOM   624  C  C   . ASP A 1 85  ? 7.836   46.658 24.382  1.00 75.72  ? 114 ASP A C   1 
ATOM   625  O  O   . ASP A 1 85  ? 7.390   45.567 24.735  1.00 75.56  ? 114 ASP A O   1 
ATOM   626  C  CB  . ASP A 1 85  ? 10.106  47.166 25.303  1.00 77.02  ? 114 ASP A CB  1 
ATOM   627  C  CG  . ASP A 1 85  ? 10.453  45.988 26.195  1.00 81.67  ? 114 ASP A CG  1 
ATOM   628  O  OD1 . ASP A 1 85  ? 10.405  44.835 25.704  1.00 82.83  ? 114 ASP A OD1 1 
ATOM   629  O  OD2 . ASP A 1 85  ? 10.790  46.218 27.374  1.00 83.58  ? 114 ASP A OD2 1 
ATOM   630  N  N   . GLY A 1 86  ? 7.102   47.761 24.295  1.00 76.13  ? 115 GLY A N   1 
ATOM   631  C  CA  . GLY A 1 86  ? 5.679   47.773 24.607  1.00 76.76  ? 115 GLY A CA  1 
ATOM   632  C  C   . GLY A 1 86  ? 5.372   47.752 26.090  1.00 77.10  ? 115 GLY A C   1 
ATOM   633  O  O   . GLY A 1 86  ? 4.426   47.095 26.524  1.00 77.24  ? 115 GLY A O   1 
ATOM   634  N  N   . GLY A 1 87  ? 6.153   48.490 26.869  1.00 77.04  ? 116 GLY A N   1 
ATOM   635  C  CA  . GLY A 1 87  ? 5.958   48.588 28.309  1.00 77.27  ? 116 GLY A CA  1 
ATOM   636  C  C   . GLY A 1 87  ? 4.783   49.471 28.688  1.00 77.38  ? 116 GLY A C   1 
ATOM   637  O  O   . GLY A 1 87  ? 3.926   49.773 27.852  1.00 77.84  ? 116 GLY A O   1 
ATOM   638  N  N   . PRO A 1 88  ? 4.723   49.929 29.951  1.00 76.71  ? 117 PRO A N   1 
ATOM   639  C  CA  . PRO A 1 88  ? 3.584   50.764 30.370  1.00 76.28  ? 117 PRO A CA  1 
ATOM   640  C  C   . PRO A 1 88  ? 3.535   52.154 29.750  1.00 76.15  ? 117 PRO A C   1 
ATOM   641  O  O   . PRO A 1 88  ? 2.548   52.853 29.947  1.00 76.64  ? 117 PRO A O   1 
ATOM   642  C  CB  . PRO A 1 88  ? 3.729   50.830 31.887  1.00 76.99  ? 117 PRO A CB  1 
ATOM   643  C  CG  . PRO A 1 88  ? 5.169   50.579 32.144  1.00 77.49  ? 117 PRO A CG  1 
ATOM   644  C  CD  . PRO A 1 88  ? 5.648   49.658 31.066  1.00 76.06  ? 117 PRO A CD  1 
ATOM   645  N  N   . GLN A 1 89  ? 4.576   52.565 29.012  1.00 75.45  ? 118 GLN A N   1 
ATOM   646  C  CA  . GLN A 1 89  ? 4.587   53.865 28.348  1.00 75.36  ? 118 GLN A CA  1 
ATOM   647  C  C   . GLN A 1 89  ? 3.975   53.777 26.944  1.00 75.30  ? 118 GLN A C   1 
ATOM   648  O  O   . GLN A 1 89  ? 3.374   54.746 26.482  1.00 75.77  ? 118 GLN A O   1 
ATOM   649  C  CB  . GLN A 1 89  ? 6.005   54.425 28.269  1.00 76.84  ? 118 GLN A CB  1 
ATOM   650  C  CG  . GLN A 1 89  ? 6.689   54.499 29.624  1.00 80.64  ? 118 GLN A CG  1 
ATOM   651  C  CD  . GLN A 1 89  ? 8.039   53.821 29.600  1.00 85.21  ? 118 GLN A CD  1 
ATOM   652  O  OE1 . GLN A 1 89  ? 9.080   54.453 29.851  1.00 86.76  ? 118 GLN A OE1 1 
ATOM   653  N  NE2 . GLN A 1 89  ? 8.051   52.525 29.276  1.00 85.15  ? 118 GLN A NE2 1 
ATOM   654  N  N   . ALA A 1 90  ? 4.123   52.626 26.259  1.00 74.52  ? 119 ALA A N   1 
ATOM   655  C  CA  . ALA A 1 90  ? 3.562   52.431 24.924  1.00 74.05  ? 119 ALA A CA  1 
ATOM   656  C  C   . ALA A 1 90  ? 2.078   52.068 25.046  1.00 73.18  ? 119 ALA A C   1 
ATOM   657  O  O   . ALA A 1 90  ? 1.695   50.917 24.840  1.00 73.10  ? 119 ALA A O   1 
ATOM   658  C  CB  . ALA A 1 90  ? 4.324   51.334 24.193  1.00 74.28  ? 119 ALA A CB  1 
ATOM   659  N  N   . VAL A 1 91  ? 1.246   53.055 25.387  1.00 72.40  ? 120 VAL A N   1 
ATOM   660  C  CA  . VAL A 1 91  ? -0.174  52.821 25.583  1.00 72.25  ? 120 VAL A CA  1 
ATOM   661  C  C   . VAL A 1 91  ? -0.967  52.842 24.297  1.00 72.42  ? 120 VAL A C   1 
ATOM   662  O  O   . VAL A 1 91  ? -0.965  53.838 23.573  1.00 72.50  ? 120 VAL A O   1 
ATOM   663  C  CB  . VAL A 1 91  ? -0.776  53.782 26.620  1.00 72.66  ? 120 VAL A CB  1 
ATOM   664  C  CG1 . VAL A 1 91  ? -2.245  53.454 26.876  1.00 73.21  ? 120 VAL A CG1 1 
ATOM   665  C  CG2 . VAL A 1 91  ? 0.018   53.742 27.913  1.00 73.00  ? 120 VAL A CG2 1 
ATOM   666  N  N   . ILE A 1 92  ? -1.669  51.738 24.027  1.00 72.20  ? 121 ILE A N   1 
ATOM   667  C  CA  . ILE A 1 92  ? -2.526  51.583 22.862  1.00 72.23  ? 121 ILE A CA  1 
ATOM   668  C  C   . ILE A 1 92  ? -3.928  51.883 23.338  1.00 72.60  ? 121 ILE A C   1 
ATOM   669  O  O   . ILE A 1 92  ? -4.503  51.073 24.058  1.00 72.84  ? 121 ILE A O   1 
ATOM   670  C  CB  . ILE A 1 92  ? -2.469  50.143 22.289  1.00 72.55  ? 121 ILE A CB  1 
ATOM   671  C  CG1 . ILE A 1 92  ? -1.041  49.563 22.253  1.00 73.30  ? 121 ILE A CG1 1 
ATOM   672  C  CG2 . ILE A 1 92  ? -3.131  50.088 20.920  1.00 73.05  ? 121 ILE A CG2 1 
ATOM   673  C  CD1 . ILE A 1 92  ? -0.967  48.107 21.882  1.00 74.18  ? 121 ILE A CD1 1 
ATOM   674  N  N   . GLU A 1 93  ? -4.475  53.046 22.979  1.00 72.60  ? 122 GLU A N   1 
ATOM   675  C  CA  . GLU A 1 93  ? -5.833  53.411 23.387  1.00 72.87  ? 122 GLU A CA  1 
ATOM   676  C  C   . GLU A 1 93  ? -6.889  52.582 22.635  1.00 72.80  ? 122 GLU A C   1 
ATOM   677  O  O   . GLU A 1 93  ? -6.602  52.079 21.547  1.00 72.90  ? 122 GLU A O   1 
ATOM   678  C  CB  . GLU A 1 93  ? -6.058  54.912 23.173  1.00 74.93  ? 122 GLU A CB  1 
ATOM   679  C  CG  . GLU A 1 93  ? -5.167  55.777 24.046  1.00 80.02  ? 122 GLU A CG  1 
ATOM   680  C  CD  . GLU A 1 93  ? -5.481  55.769 25.530  1.00 85.77  ? 122 GLU A CD  1 
ATOM   681  O  OE1 . GLU A 1 93  ? -4.558  56.053 26.328  1.00 87.25  ? 122 GLU A OE1 1 
ATOM   682  O  OE2 . GLU A 1 93  ? -6.646  55.489 25.897  1.00 86.95  ? 122 GLU A OE2 1 
ATOM   683  N  N   . PRO A 1 94  ? -8.104  52.383 23.196  1.00 72.51  ? 123 PRO A N   1 
ATOM   684  C  CA  . PRO A 1 94  ? -9.119  51.582 22.481  1.00 72.56  ? 123 PRO A CA  1 
ATOM   685  C  C   . PRO A 1 94  ? -9.416  52.129 21.088  1.00 72.80  ? 123 PRO A C   1 
ATOM   686  O  O   . PRO A 1 94  ? -9.488  53.345 20.900  1.00 73.31  ? 123 PRO A O   1 
ATOM   687  C  CB  . PRO A 1 94  ? -10.354 51.678 23.378  1.00 73.07  ? 123 PRO A CB  1 
ATOM   688  C  CG  . PRO A 1 94  ? -9.840  52.028 24.705  1.00 73.47  ? 123 PRO A CG  1 
ATOM   689  C  CD  . PRO A 1 94  ? -8.614  52.864 24.492  1.00 71.95  ? 123 PRO A CD  1 
ATOM   690  N  N   . GLY A 1 95  ? -9.513  51.232 20.120  1.00 72.06  ? 124 GLY A N   1 
ATOM   691  C  CA  . GLY A 1 95  ? -9.749  51.596 18.731  1.00 71.78  ? 124 GLY A CA  1 
ATOM   692  C  C   . GLY A 1 95  ? -8.512  52.027 17.967  1.00 71.37  ? 124 GLY A C   1 
ATOM   693  O  O   . GLY A 1 95  ? -8.591  52.284 16.762  1.00 71.28  ? 124 GLY A O   1 
ATOM   694  N  N   . LYS A 1 96  ? -7.358  52.112 18.645  1.00 71.04  ? 125 LYS A N   1 
ATOM   695  C  CA  . LYS A 1 96  ? -6.114  52.547 18.011  1.00 71.25  ? 125 LYS A CA  1 
ATOM   696  C  C   . LYS A 1 96  ? -5.156  51.392 17.717  1.00 71.00  ? 125 LYS A C   1 
ATOM   697  O  O   . LYS A 1 96  ? -5.357  50.287 18.203  1.00 71.25  ? 125 LYS A O   1 
ATOM   698  C  CB  . LYS A 1 96  ? -5.441  53.639 18.858  1.00 73.25  ? 125 LYS A CB  1 
ATOM   699  C  CG  . LYS A 1 96  ? -6.346  54.842 19.095  1.00 78.15  ? 125 LYS A CG  1 
ATOM   700  C  CD  . LYS A 1 96  ? -6.388  55.739 17.868  1.00 83.26  ? 125 LYS A CD  1 
ATOM   701  C  CE  . LYS A 1 96  ? -7.217  56.982 18.059  1.00 87.21  ? 125 LYS A CE  1 
ATOM   702  N  NZ  . LYS A 1 96  ? -7.183  57.835 16.839  1.00 89.81  ? 125 LYS A NZ  1 
ATOM   703  N  N   . MET A 1 97  ? -4.133  51.639 16.902  1.00 70.61  ? 126 MET A N   1 
ATOM   704  C  CA  . MET A 1 97  ? -3.168  50.616 16.547  1.00 70.81  ? 126 MET A CA  1 
ATOM   705  C  C   . MET A 1 97  ? -1.734  51.108 16.723  1.00 71.20  ? 126 MET A C   1 
ATOM   706  O  O   . MET A 1 97  ? -1.356  52.156 16.186  1.00 71.81  ? 126 MET A O   1 
ATOM   707  C  CB  . MET A 1 97  ? -3.410  50.127 15.109  1.00 71.32  ? 126 MET A CB  1 
ATOM   708  C  CG  . MET A 1 97  ? -2.539  48.958 14.703  1.00 73.02  ? 126 MET A CG  1 
ATOM   709  S  SD  . MET A 1 97  ? -1.055  49.458 13.809  1.00 74.54  ? 126 MET A SD  1 
ATOM   710  C  CE  . MET A 1 97  ? -1.728  49.766 12.245  1.00 73.54  ? 126 MET A CE  1 
ATOM   711  N  N   . TRP A 1 98  ? -0.930  50.339 17.463  1.00 70.53  ? 127 TRP A N   1 
ATOM   712  C  CA  . TRP A 1 98  ? 0.475   50.646 17.692  1.00 70.34  ? 127 TRP A CA  1 
ATOM   713  C  C   . TRP A 1 98  ? 1.309   49.637 16.931  1.00 69.58  ? 127 TRP A C   1 
ATOM   714  O  O   . TRP A 1 98  ? 1.002   48.447 16.937  1.00 69.68  ? 127 TRP A O   1 
ATOM   715  C  CB  . TRP A 1 98  ? 0.801   50.593 19.202  1.00 70.70  ? 127 TRP A CB  1 
ATOM   716  C  CG  . TRP A 1 98  ? 2.265   50.497 19.555  1.00 71.86  ? 127 TRP A CG  1 
ATOM   717  C  CD1 . TRP A 1 98  ? 3.207   51.477 19.432  1.00 72.94  ? 127 TRP A CD1 1 
ATOM   718  C  CD2 . TRP A 1 98  ? 2.937   49.367 20.138  1.00 72.25  ? 127 TRP A CD2 1 
ATOM   719  N  NE1 . TRP A 1 98  ? 4.428   51.019 19.874  1.00 73.36  ? 127 TRP A NE1 1 
ATOM   720  C  CE2 . TRP A 1 98  ? 4.290   49.726 20.316  1.00 73.06  ? 127 TRP A CE2 1 
ATOM   721  C  CE3 . TRP A 1 98  ? 2.525   48.087 20.532  1.00 72.80  ? 127 TRP A CE3 1 
ATOM   722  C  CZ2 . TRP A 1 98  ? 5.231   48.849 20.862  1.00 73.46  ? 127 TRP A CZ2 1 
ATOM   723  C  CZ3 . TRP A 1 98  ? 3.457   47.226 21.082  1.00 73.48  ? 127 TRP A CZ3 1 
ATOM   724  C  CH2 . TRP A 1 98  ? 4.792   47.607 21.238  1.00 73.51  ? 127 TRP A CH2 1 
ATOM   725  N  N   . THR A 1 99  ? 2.378   50.103 16.300  1.00 68.75  ? 128 THR A N   1 
ATOM   726  C  CA  . THR A 1 99  ? 3.274   49.227 15.568  1.00 68.51  ? 128 THR A CA  1 
ATOM   727  C  C   . THR A 1 99  ? 4.594   49.065 16.308  1.00 68.78  ? 128 THR A C   1 
ATOM   728  O  O   . THR A 1 99  ? 5.146   50.047 16.805  1.00 68.91  ? 128 THR A O   1 
ATOM   729  C  CB  . THR A 1 99  ? 3.486   49.772 14.178  1.00 69.04  ? 128 THR A CB  1 
ATOM   730  O  OG1 . THR A 1 99  ? 2.216   49.834 13.532  1.00 69.76  ? 128 THR A OG1 1 
ATOM   731  C  CG2 . THR A 1 99  ? 4.469   48.945 13.375  1.00 69.18  ? 128 THR A CG2 1 
ATOM   732  N  N   . ALA A 1 100 ? 5.098   47.827 16.392  1.00 68.71  ? 129 ALA A N   1 
ATOM   733  C  CA  . ALA A 1 100 ? 6.367   47.545 17.043  1.00 69.12  ? 129 ALA A CA  1 
ATOM   734  C  C   . ALA A 1 100 ? 7.332   46.992 16.021  1.00 69.88  ? 129 ALA A C   1 
ATOM   735  O  O   . ALA A 1 100 ? 7.118   45.885 15.523  1.00 69.54  ? 129 ALA A O   1 
ATOM   736  C  CB  . ALA A 1 100 ? 6.173   46.533 18.155  1.00 69.10  ? 129 ALA A CB  1 
ATOM   737  N  N   . GLU A 1 101 ? 8.381   47.758 15.681  1.00 70.88  ? 130 GLU A N   1 
ATOM   738  C  CA  . GLU A 1 101 ? 9.374   47.272 14.728  1.00 72.38  ? 130 GLU A CA  1 
ATOM   739  C  C   . GLU A 1 101 ? 10.387  46.422 15.486  1.00 72.67  ? 130 GLU A C   1 
ATOM   740  O  O   . GLU A 1 101 ? 10.993  46.879 16.455  1.00 72.56  ? 130 GLU A O   1 
ATOM   741  C  CB  . GLU A 1 101 ? 10.054  48.419 13.967  1.00 76.31  ? 130 GLU A CB  1 
ATOM   742  C  CG  . GLU A 1 101 ? 9.882   48.342 12.453  1.00 83.86  ? 130 GLU A CG  1 
ATOM   743  C  CD  . GLU A 1 101 ? 10.611  47.211 11.744  1.00 94.00  ? 130 GLU A CD  1 
ATOM   744  O  OE1 . GLU A 1 101 ? 10.114  46.767 10.682  1.00 96.63  ? 130 GLU A OE1 1 
ATOM   745  O  OE2 . GLU A 1 101 ? 11.674  46.768 12.241  1.00 97.00  ? 130 GLU A OE2 1 
ATOM   746  N  N   . ILE A 1 102 ? 10.524  45.162 15.081  1.00 72.68  ? 131 ILE A N   1 
ATOM   747  C  CA  . ILE A 1 102 ? 11.408  44.222 15.750  1.00 72.92  ? 131 ILE A CA  1 
ATOM   748  C  C   . ILE A 1 102 ? 12.373  43.568 14.773  1.00 72.86  ? 131 ILE A C   1 
ATOM   749  O  O   . ILE A 1 102 ? 11.951  43.001 13.764  1.00 72.61  ? 131 ILE A O   1 
ATOM   750  C  CB  . ILE A 1 102 ? 10.554  43.152 16.485  1.00 73.40  ? 131 ILE A CB  1 
ATOM   751  C  CG1 . ILE A 1 102 ? 9.711   43.793 17.595  1.00 74.02  ? 131 ILE A CG1 1 
ATOM   752  C  CG2 . ILE A 1 102 ? 11.422  41.994 17.012  1.00 74.02  ? 131 ILE A CG2 1 
ATOM   753  C  CD1 . ILE A 1 102 ? 8.825   42.874 18.314  1.00 75.23  ? 131 ILE A CD1 1 
ATOM   754  N  N   . LYS A 1 103 ? 13.670  43.626 15.088  1.00 72.75  ? 132 LYS A N   1 
ATOM   755  C  CA  . LYS A 1 103 ? 14.677  42.954 14.284  1.00 73.05  ? 132 LYS A CA  1 
ATOM   756  C  C   . LYS A 1 103 ? 15.224  41.859 15.168  1.00 71.82  ? 132 LYS A C   1 
ATOM   757  O  O   . LYS A 1 103 ? 15.901  42.157 16.149  1.00 71.61  ? 132 LYS A O   1 
ATOM   758  C  CB  . LYS A 1 103 ? 15.796  43.914 13.863  1.00 76.46  ? 132 LYS A CB  1 
ATOM   759  C  CG  . LYS A 1 103 ? 16.884  43.215 13.045  1.00 83.00  ? 132 LYS A CG  1 
ATOM   760  C  CD  . LYS A 1 103 ? 17.727  44.194 12.223  1.00 88.88  ? 132 LYS A CD  1 
ATOM   761  C  CE  . LYS A 1 103 ? 18.694  43.493 11.294  1.00 92.69  ? 132 LYS A CE  1 
ATOM   762  N  NZ  . LYS A 1 103 ? 18.007  42.904 10.115  1.00 94.61  ? 132 LYS A NZ  1 
ATOM   763  N  N   . VAL A 1 104 ? 14.871  40.604 14.875  1.00 71.01  ? 133 VAL A N   1 
ATOM   764  C  CA  . VAL A 1 104 ? 15.289  39.459 15.687  1.00 70.75  ? 133 VAL A CA  1 
ATOM   765  C  C   . VAL A 1 104 ? 16.813  39.343 15.722  1.00 70.50  ? 133 VAL A C   1 
ATOM   766  O  O   . VAL A 1 104 ? 17.435  39.284 14.671  1.00 70.83  ? 133 VAL A O   1 
ATOM   767  C  CB  . VAL A 1 104 ? 14.621  38.137 15.231  1.00 71.00  ? 133 VAL A CB  1 
ATOM   768  C  CG1 . VAL A 1 104 ? 14.873  37.028 16.249  1.00 71.39  ? 133 VAL A CG1 1 
ATOM   769  C  CG2 . VAL A 1 104 ? 13.123  38.324 14.992  1.00 71.03  ? 133 VAL A CG2 1 
ATOM   770  N  N   . ASP A 1 105 ? 17.417  39.366 16.915  1.00 69.85  ? 134 ASP A N   1 
ATOM   771  C  CA  . ASP A 1 105 ? 18.872  39.309 17.038  1.00 69.94  ? 134 ASP A CA  1 
ATOM   772  C  C   . ASP A 1 105 ? 19.252  38.552 18.311  1.00 69.00  ? 134 ASP A C   1 
ATOM   773  O  O   . ASP A 1 105 ? 20.003  39.053 19.154  1.00 69.27  ? 134 ASP A O   1 
ATOM   774  C  CB  . ASP A 1 105 ? 19.444  40.741 17.054  1.00 72.46  ? 134 ASP A CB  1 
ATOM   775  C  CG  . ASP A 1 105 ? 20.947  40.832 16.900  1.00 77.94  ? 134 ASP A CG  1 
ATOM   776  O  OD1 . ASP A 1 105 ? 21.563  39.827 16.471  1.00 79.55  ? 134 ASP A OD1 1 
ATOM   777  O  OD2 . ASP A 1 105 ? 21.509  41.903 17.213  1.00 79.87  ? 134 ASP A OD2 1 
ATOM   778  N  N   . GLN A 1 106 ? 18.711  37.342 18.451  1.00 67.56  ? 135 GLN A N   1 
ATOM   779  C  CA  . GLN A 1 106 ? 18.927  36.495 19.626  1.00 66.33  ? 135 GLN A CA  1 
ATOM   780  C  C   . GLN A 1 106 ? 18.724  35.018 19.264  1.00 65.95  ? 135 GLN A C   1 
ATOM   781  O  O   . GLN A 1 106 ? 18.100  34.719 18.237  1.00 66.11  ? 135 GLN A O   1 
ATOM   782  C  CB  . GLN A 1 106 ? 17.961  36.917 20.747  1.00 66.23  ? 135 GLN A CB  1 
ATOM   783  C  CG  . GLN A 1 106 ? 16.507  36.693 20.410  1.00 66.14  ? 135 GLN A CG  1 
ATOM   784  C  CD  . GLN A 1 106 ? 15.635  37.328 21.447  1.00 67.12  ? 135 GLN A CD  1 
ATOM   785  O  OE1 . GLN A 1 106 ? 15.048  38.391 21.223  1.00 67.85  ? 135 GLN A OE1 1 
ATOM   786  N  NE2 . GLN A 1 106 ? 15.548  36.702 22.614  1.00 66.13  ? 135 GLN A NE2 1 
ATOM   787  N  N   . PRO A 1 107 ? 19.234  34.065 20.074  1.00 65.31  ? 136 PRO A N   1 
ATOM   788  C  CA  . PRO A 1 107 ? 19.062  32.645 19.724  1.00 65.16  ? 136 PRO A CA  1 
ATOM   789  C  C   . PRO A 1 107 ? 17.603  32.178 19.675  1.00 65.19  ? 136 PRO A C   1 
ATOM   790  O  O   . PRO A 1 107 ? 16.699  32.884 20.129  1.00 65.59  ? 136 PRO A O   1 
ATOM   791  C  CB  . PRO A 1 107 ? 19.871  31.914 20.800  1.00 65.60  ? 136 PRO A CB  1 
ATOM   792  C  CG  . PRO A 1 107 ? 20.782  32.942 21.369  1.00 65.93  ? 136 PRO A CG  1 
ATOM   793  C  CD  . PRO A 1 107 ? 20.022  34.216 21.311  1.00 64.48  ? 136 PRO A CD  1 
ATOM   794  N  N   . ALA A 1 108 ? 17.382  30.995 19.088  1.00 64.61  ? 137 ALA A N   1 
ATOM   795  C  CA  . ALA A 1 108 ? 16.066  30.388 18.926  1.00 64.69  ? 137 ALA A CA  1 
ATOM   796  C  C   . ALA A 1 108 ? 15.494  30.046 20.279  1.00 64.23  ? 137 ALA A C   1 
ATOM   797  O  O   . ALA A 1 108 ? 16.190  29.454 21.102  1.00 64.58  ? 137 ALA A O   1 
ATOM   798  C  CB  . ALA A 1 108 ? 16.180  29.130 18.082  1.00 65.12  ? 137 ALA A CB  1 
ATOM   799  N  N   . THR A 1 109 ? 14.241  30.458 20.537  1.00 63.40  ? 138 THR A N   1 
ATOM   800  C  CA  . THR A 1 109 ? 13.604  30.253 21.836  1.00 63.14  ? 138 THR A CA  1 
ATOM   801  C  C   . THR A 1 109 ? 12.054  30.257 21.748  1.00 62.34  ? 138 THR A C   1 
ATOM   802  O  O   . THR A 1 109 ? 11.490  30.453 20.665  1.00 62.49  ? 138 THR A O   1 
ATOM   803  C  CB  . THR A 1 109 ? 14.003  31.430 22.749  1.00 65.13  ? 138 THR A CB  1 
ATOM   804  O  OG1 . THR A 1 109 ? 15.404  31.625 22.730  1.00 67.31  ? 138 THR A OG1 1 
ATOM   805  C  CG2 . THR A 1 109 ? 13.533  31.225 24.140  1.00 65.31  ? 138 THR A CG2 1 
ATOM   806  N  N   . THR A 1 110 ? 11.374  30.008 22.894  1.00 61.21  ? 139 THR A N   1 
ATOM   807  C  CA  . THR A 1 110 ? 9.963   30.180 23.074  1.00 60.64  ? 139 THR A CA  1 
ATOM   808  C  C   . THR A 1 110 ? 9.880   31.415 23.964  1.00 59.93  ? 139 THR A C   1 
ATOM   809  O  O   . THR A 1 110 ? 9.998   31.303 25.183  1.00 61.01  ? 139 THR A O   1 
ATOM   810  C  CB  . THR A 1 110 ? 9.308   29.007 23.816  1.00 61.36  ? 139 THR A CB  1 
ATOM   811  O  OG1 . THR A 1 110 ? 9.827   27.773 23.347  1.00 62.18  ? 139 THR A OG1 1 
ATOM   812  C  CG2 . THR A 1 110 ? 7.797   29.029 23.688  1.00 61.46  ? 139 THR A CG2 1 
ATOM   813  N  N   . ALA A 1 111 ? 9.780   32.590 23.369  1.00 57.99  ? 140 ALA A N   1 
ATOM   814  C  CA  . ALA A 1 111 ? 9.568   33.821 24.120  1.00 56.73  ? 140 ALA A CA  1 
ATOM   815  C  C   . ALA A 1 111 ? 8.017   34.012 24.166  1.00 55.24  ? 140 ALA A C   1 
ATOM   816  O  O   . ALA A 1 111 ? 7.291   33.192 23.584  1.00 55.40  ? 140 ALA A O   1 
ATOM   817  C  CB  . ALA A 1 111 ? 10.259  34.982 23.401  1.00 56.94  ? 140 ALA A CB  1 
ATOM   818  N  N   . TRP A 1 112 ? 7.495   35.036 24.863  1.00 53.81  ? 141 TRP A N   1 
ATOM   819  C  CA  . TRP A 1 112 ? 6.045   35.242 24.890  1.00 52.88  ? 141 TRP A CA  1 
ATOM   820  C  C   . TRP A 1 112 ? 5.653   36.706 24.918  1.00 53.28  ? 141 TRP A C   1 
ATOM   821  O  O   . TRP A 1 112 ? 6.515   37.575 24.991  1.00 53.64  ? 141 TRP A O   1 
ATOM   822  C  CB  . TRP A 1 112 ? 5.396   34.441 26.026  1.00 51.83  ? 141 TRP A CB  1 
ATOM   823  C  CG  . TRP A 1 112 ? 5.621   34.938 27.418  1.00 50.51  ? 141 TRP A CG  1 
ATOM   824  C  CD1 . TRP A 1 112 ? 6.805   34.988 28.088  1.00 50.56  ? 141 TRP A CD1 1 
ATOM   825  C  CD2 . TRP A 1 112 ? 4.604   35.204 28.386  1.00 49.82  ? 141 TRP A CD2 1 
ATOM   826  N  NE1 . TRP A 1 112 ? 6.592   35.356 29.392  1.00 50.57  ? 141 TRP A NE1 1 
ATOM   827  C  CE2 . TRP A 1 112 ? 5.247   35.489 29.603  1.00 50.21  ? 141 TRP A CE2 1 
ATOM   828  C  CE3 . TRP A 1 112 ? 3.207   35.262 28.332  1.00 50.00  ? 141 TRP A CE3 1 
ATOM   829  C  CZ2 . TRP A 1 112 ? 4.545   35.859 30.745  1.00 50.57  ? 141 TRP A CZ2 1 
ATOM   830  C  CZ3 . TRP A 1 112 ? 2.514   35.622 29.467  1.00 50.37  ? 141 TRP A CZ3 1 
ATOM   831  C  CH2 . TRP A 1 112 ? 3.181   35.926 30.652  1.00 50.36  ? 141 TRP A CH2 1 
ATOM   832  N  N   . PHE A 1 113 ? 4.367   36.987 24.772  1.00 53.43  ? 142 PHE A N   1 
ATOM   833  C  CA  . PHE A 1 113 ? 3.888   38.355 24.801  1.00 54.08  ? 142 PHE A CA  1 
ATOM   834  C  C   . PHE A 1 113 ? 2.645   38.484 25.630  1.00 54.47  ? 142 PHE A C   1 
ATOM   835  O  O   . PHE A 1 113 ? 1.819   37.576 25.666  1.00 54.96  ? 142 PHE A O   1 
ATOM   836  C  CB  . PHE A 1 113 ? 3.728   38.943 23.396  1.00 54.20  ? 142 PHE A CB  1 
ATOM   837  C  CG  . PHE A 1 113 ? 2.682   38.333 22.497  1.00 55.19  ? 142 PHE A CG  1 
ATOM   838  C  CD1 . PHE A 1 113 ? 1.383   38.816 22.492  1.00 56.28  ? 142 PHE A CD1 1 
ATOM   839  C  CD2 . PHE A 1 113 ? 3.018   37.348 21.586  1.00 55.99  ? 142 PHE A CD2 1 
ATOM   840  C  CE1 . PHE A 1 113 ? 0.426   38.282 21.638  1.00 57.04  ? 142 PHE A CE1 1 
ATOM   841  C  CE2 . PHE A 1 113 ? 2.066   36.831 20.720  1.00 56.92  ? 142 PHE A CE2 1 
ATOM   842  C  CZ  . PHE A 1 113 ? 0.776   37.301 20.749  1.00 56.89  ? 142 PHE A CZ  1 
ATOM   843  N  N   . HIS A 1 114 ? 2.526   39.594 26.322  1.00 54.16  ? 143 HIS A N   1 
ATOM   844  C  CA  . HIS A 1 114 ? 1.387   39.866 27.188  1.00 54.81  ? 143 HIS A CA  1 
ATOM   845  C  C   . HIS A 1 114 ? 1.352   41.365 27.475  1.00 56.26  ? 143 HIS A C   1 
ATOM   846  O  O   . HIS A 1 114 ? 2.393   42.035 27.394  1.00 56.84  ? 143 HIS A O   1 
ATOM   847  C  CB  . HIS A 1 114 ? 1.523   39.079 28.503  1.00 54.66  ? 143 HIS A CB  1 
ATOM   848  C  CG  . HIS A 1 114 ? 2.768   39.394 29.274  1.00 56.13  ? 143 HIS A CG  1 
ATOM   849  N  ND1 . HIS A 1 114 ? 2.751   40.263 30.353  1.00 57.84  ? 143 HIS A ND1 1 
ATOM   850  C  CD2 . HIS A 1 114 ? 4.029   38.936 29.108  1.00 56.97  ? 143 HIS A CD2 1 
ATOM   851  C  CE1 . HIS A 1 114 ? 3.992   40.296 30.809  1.00 58.14  ? 143 HIS A CE1 1 
ATOM   852  N  NE2 . HIS A 1 114 ? 4.795   39.513 30.093  1.00 58.01  ? 143 HIS A NE2 1 
ATOM   853  N  N   . PRO A 1 115 ? 0.183   41.923 27.845  1.00 56.06  ? 144 PRO A N   1 
ATOM   854  C  CA  . PRO A 1 115 ? 0.141   43.356 28.177  1.00 56.03  ? 144 PRO A CA  1 
ATOM   855  C  C   . PRO A 1 115 ? 1.050   43.715 29.356  1.00 56.43  ? 144 PRO A C   1 
ATOM   856  O  O   . PRO A 1 115 ? 1.414   42.860 30.172  1.00 55.93  ? 144 PRO A O   1 
ATOM   857  C  CB  . PRO A 1 115 ? -1.333  43.599 28.517  1.00 56.33  ? 144 PRO A CB  1 
ATOM   858  C  CG  . PRO A 1 115 ? -1.877  42.263 28.863  1.00 56.47  ? 144 PRO A CG  1 
ATOM   859  C  CD  . PRO A 1 115 ? -1.137  41.290 28.004  1.00 55.10  ? 144 PRO A CD  1 
ATOM   860  N  N   . HIS A 1 116 ? 1.450   44.986 29.416  1.00 56.91  ? 145 HIS A N   1 
ATOM   861  C  CA  . HIS A 1 116 ? 2.282   45.524 30.502  1.00 57.14  ? 145 HIS A CA  1 
ATOM   862  C  C   . HIS A 1 116 ? 1.701   46.851 31.028  1.00 57.02  ? 145 HIS A C   1 
ATOM   863  O  O   . HIS A 1 116 ? 2.448   47.703 31.494  1.00 57.31  ? 145 HIS A O   1 
ATOM   864  C  CB  . HIS A 1 116 ? 3.713   45.746 30.013  1.00 57.76  ? 145 HIS A CB  1 
ATOM   865  C  CG  . HIS A 1 116 ? 4.729   45.487 31.066  1.00 60.48  ? 145 HIS A CG  1 
ATOM   866  N  ND1 . HIS A 1 116 ? 4.714   46.176 32.259  1.00 62.40  ? 145 HIS A ND1 1 
ATOM   867  C  CD2 . HIS A 1 116 ? 5.760   44.613 31.076  1.00 62.04  ? 145 HIS A CD2 1 
ATOM   868  C  CE1 . HIS A 1 116 ? 5.737   45.710 32.955  1.00 63.10  ? 145 HIS A CE1 1 
ATOM   869  N  NE2 . HIS A 1 116 ? 6.391   44.761 32.288  1.00 63.20  ? 145 HIS A NE2 1 
ATOM   870  N  N   . THR A 1 117 ? 0.377   47.012 30.937  1.00 56.71  ? 146 THR A N   1 
ATOM   871  C  CA  . THR A 1 117 ? -0.392  48.188 31.325  1.00 57.44  ? 146 THR A CA  1 
ATOM   872  C  C   . THR A 1 117 ? -0.066  48.617 32.746  1.00 58.07  ? 146 THR A C   1 
ATOM   873  O  O   . THR A 1 117 ? -0.046  47.779 33.646  1.00 58.48  ? 146 THR A O   1 
ATOM   874  C  CB  . THR A 1 117 ? -1.896  47.897 31.189  1.00 58.56  ? 146 THR A CB  1 
ATOM   875  O  OG1 . THR A 1 117 ? -2.138  47.151 29.994  1.00 59.79  ? 146 THR A OG1 1 
ATOM   876  C  CG2 . THR A 1 117 ? -2.750  49.162 31.203  1.00 58.37  ? 146 THR A CG2 1 
ATOM   877  N  N   . HIS A 1 118 ? 0.192   49.920 32.943  1.00 57.84  ? 147 HIS A N   1 
ATOM   878  C  CA  . HIS A 1 118 ? 0.534   50.486 34.241  1.00 58.20  ? 147 HIS A CA  1 
ATOM   879  C  C   . HIS A 1 118 ? -0.484  50.146 35.321  1.00 57.36  ? 147 HIS A C   1 
ATOM   880  O  O   . HIS A 1 118 ? -1.656  50.505 35.192  1.00 57.51  ? 147 HIS A O   1 
ATOM   881  C  CB  . HIS A 1 118 ? 0.700   52.006 34.134  1.00 60.04  ? 147 HIS A CB  1 
ATOM   882  C  CG  . HIS A 1 118 ? 1.176   52.620 35.408  1.00 63.57  ? 147 HIS A CG  1 
ATOM   883  N  ND1 . HIS A 1 118 ? 2.517   52.649 35.730  1.00 65.64  ? 147 HIS A ND1 1 
ATOM   884  C  CD2 . HIS A 1 118 ? 0.464   53.149 36.431  1.00 65.18  ? 147 HIS A CD2 1 
ATOM   885  C  CE1 . HIS A 1 118 ? 2.585   53.213 36.924  1.00 66.48  ? 147 HIS A CE1 1 
ATOM   886  N  NE2 . HIS A 1 118 ? 1.373   53.523 37.389  1.00 66.55  ? 147 HIS A NE2 1 
ATOM   887  N  N   . GLY A 1 119 ? -0.030  49.436 36.353  1.00 56.36  ? 148 GLY A N   1 
ATOM   888  C  CA  . GLY A 1 119 ? -0.865  49.010 37.466  1.00 56.38  ? 148 GLY A CA  1 
ATOM   889  C  C   . GLY A 1 119 ? -2.055  48.141 37.091  1.00 56.64  ? 148 GLY A C   1 
ATOM   890  O  O   . GLY A 1 119 ? -2.973  47.964 37.894  1.00 56.98  ? 148 GLY A O   1 
ATOM   891  N  N   . LEU A 1 120 ? -2.073  47.605 35.867  1.00 56.41  ? 149 LEU A N   1 
ATOM   892  C  CA  . LEU A 1 120 ? -3.184  46.779 35.420  1.00 56.64  ? 149 LEU A CA  1 
ATOM   893  C  C   . LEU A 1 120 ? -2.781  45.479 34.737  1.00 57.19  ? 149 LEU A C   1 
ATOM   894  O  O   . LEU A 1 120 ? -3.670  44.710 34.378  1.00 57.32  ? 149 LEU A O   1 
ATOM   895  C  CB  . LEU A 1 120 ? -4.126  47.595 34.531  1.00 56.49  ? 149 LEU A CB  1 
ATOM   896  C  CG  . LEU A 1 120 ? -5.020  48.580 35.280  1.00 57.20  ? 149 LEU A CG  1 
ATOM   897  C  CD1 . LEU A 1 120 ? -5.838  49.387 34.332  1.00 57.63  ? 149 LEU A CD1 1 
ATOM   898  C  CD2 . LEU A 1 120 ? -5.934  47.861 36.258  1.00 57.79  ? 149 LEU A CD2 1 
ATOM   899  N  N   . THR A 1 121 ? -1.463  45.215 34.595  1.00 57.42  ? 150 THR A N   1 
ATOM   900  C  CA  . THR A 1 121 ? -0.874  44.011 33.990  1.00 58.12  ? 150 THR A CA  1 
ATOM   901  C  C   . THR A 1 121 ? -1.536  42.712 34.433  1.00 57.93  ? 150 THR A C   1 
ATOM   902  O  O   . THR A 1 121 ? -1.946  41.940 33.578  1.00 57.95  ? 150 THR A O   1 
ATOM   903  C  CB  . THR A 1 121 ? 0.639   43.958 34.253  1.00 60.28  ? 150 THR A CB  1 
ATOM   904  O  OG1 . THR A 1 121 ? 1.247   45.179 33.834  1.00 62.08  ? 150 THR A OG1 1 
ATOM   905  C  CG2 . THR A 1 121 ? 1.302   42.755 33.606  1.00 60.70  ? 150 THR A CG2 1 
ATOM   906  N  N   . GLY A 1 122 ? -1.656  42.498 35.748  1.00 57.77  ? 151 GLY A N   1 
ATOM   907  C  CA  . GLY A 1 122 ? -2.270  41.307 36.320  1.00 57.61  ? 151 GLY A CA  1 
ATOM   908  C  C   . GLY A 1 122 ? -3.704  41.112 35.880  1.00 56.91  ? 151 GLY A C   1 
ATOM   909  O  O   . GLY A 1 122 ? -4.073  40.026 35.444  1.00 56.82  ? 151 GLY A O   1 
ATOM   910  N  N   . ARG A 1 123 ? -4.506  42.166 35.951  1.00 56.28  ? 152 ARG A N   1 
ATOM   911  C  CA  . ARG A 1 123 ? -5.904  42.106 35.556  1.00 56.66  ? 152 ARG A CA  1 
ATOM   912  C  C   . ARG A 1 123 ? -6.077  41.668 34.090  1.00 56.49  ? 152 ARG A C   1 
ATOM   913  O  O   . ARG A 1 123 ? -6.838  40.748 33.816  1.00 56.68  ? 152 ARG A O   1 
ATOM   914  C  CB  . ARG A 1 123 ? -6.545  43.474 35.774  1.00 58.36  ? 152 ARG A CB  1 
ATOM   915  C  CG  . ARG A 1 123 ? -8.056  43.508 35.604  1.00 62.03  ? 152 ARG A CG  1 
ATOM   916  C  CD  . ARG A 1 123 ? -8.557  44.918 35.858  1.00 66.75  ? 152 ARG A CD  1 
ATOM   917  N  NE  . ARG A 1 123 ? -7.961  45.460 37.088  1.00 71.01  ? 152 ARG A NE  1 
ATOM   918  C  CZ  . ARG A 1 123 ? -8.458  45.283 38.306  1.00 73.91  ? 152 ARG A CZ  1 
ATOM   919  N  NH1 . ARG A 1 123 ? -9.602  44.633 38.474  1.00 73.59  ? 152 ARG A NH1 1 
ATOM   920  N  NH2 . ARG A 1 123 ? -7.824  45.771 39.365  1.00 74.01  ? 152 ARG A NH2 1 
ATOM   921  N  N   . GLN A 1 124 ? -5.357  42.316 33.165  1.00 55.82  ? 153 GLN A N   1 
ATOM   922  C  CA  . GLN A 1 124 ? -5.420  42.048 31.734  1.00 55.95  ? 153 GLN A CA  1 
ATOM   923  C  C   . GLN A 1 124 ? -4.868  40.671 31.354  1.00 56.53  ? 153 GLN A C   1 
ATOM   924  O  O   . GLN A 1 124 ? -5.455  40.004 30.501  1.00 56.93  ? 153 GLN A O   1 
ATOM   925  C  CB  . GLN A 1 124 ? -4.734  43.170 30.956  1.00 56.75  ? 153 GLN A CB  1 
ATOM   926  C  CG  . GLN A 1 124 ? -5.215  44.529 31.420  1.00 59.27  ? 153 GLN A CG  1 
ATOM   927  C  CD  . GLN A 1 124 ? -4.925  45.624 30.436  1.00 61.92  ? 153 GLN A CD  1 
ATOM   928  O  OE1 . GLN A 1 124 ? -3.964  45.556 29.664  1.00 61.66  ? 153 GLN A OE1 1 
ATOM   929  N  NE2 . GLN A 1 124 ? -5.749  46.673 30.466  1.00 62.31  ? 153 GLN A NE2 1 
ATOM   930  N  N   . VAL A 1 125 ? -3.784  40.218 32.011  1.00 56.14  ? 154 VAL A N   1 
ATOM   931  C  CA  . VAL A 1 125 ? -3.238  38.883 31.766  1.00 56.10  ? 154 VAL A CA  1 
ATOM   932  C  C   . VAL A 1 125 ? -4.263  37.841 32.256  1.00 56.67  ? 154 VAL A C   1 
ATOM   933  O  O   . VAL A 1 125 ? -4.544  36.873 31.536  1.00 57.02  ? 154 VAL A O   1 
ATOM   934  C  CB  . VAL A 1 125 ? -1.837  38.695 32.400  1.00 55.93  ? 154 VAL A CB  1 
ATOM   935  C  CG1 . VAL A 1 125 ? -1.464  37.223 32.521  1.00 56.31  ? 154 VAL A CG1 1 
ATOM   936  C  CG2 . VAL A 1 125 ? -0.778  39.448 31.614  1.00 55.90  ? 154 VAL A CG2 1 
ATOM   937  N  N   . ALA A 1 126 ? -4.867  38.082 33.440  1.00 56.36  ? 155 ALA A N   1 
ATOM   938  C  CA  . ALA A 1 126 ? -5.918  37.218 33.988  1.00 56.69  ? 155 ALA A CA  1 
ATOM   939  C  C   . ALA A 1 126 ? -7.146  37.224 33.076  1.00 57.02  ? 155 ALA A C   1 
ATOM   940  O  O   . ALA A 1 126 ? -7.824  36.205 32.978  1.00 57.58  ? 155 ALA A O   1 
ATOM   941  C  CB  . ALA A 1 126 ? -6.320  37.672 35.384  1.00 56.70  ? 155 ALA A CB  1 
ATOM   942  N  N   . MET A 1 127 ? -7.441  38.361 32.416  1.00 56.27  ? 156 MET A N   1 
ATOM   943  C  CA  . MET A 1 127 ? -8.566  38.456 31.490  1.00 55.87  ? 156 MET A CA  1 
ATOM   944  C  C   . MET A 1 127 ? -8.443  37.510 30.323  1.00 56.10  ? 156 MET A C   1 
ATOM   945  O  O   . MET A 1 127 ? -9.453  37.073 29.792  1.00 56.34  ? 156 MET A O   1 
ATOM   946  C  CB  . MET A 1 127 ? -8.783  39.890 30.982  1.00 55.49  ? 156 MET A CB  1 
ATOM   947  C  CG  . MET A 1 127 ? -9.531  40.773 31.954  1.00 55.89  ? 156 MET A CG  1 
ATOM   948  S  SD  . MET A 1 127 ? -11.117 40.080 32.494  1.00 56.01  ? 156 MET A SD  1 
ATOM   949  C  CE  . MET A 1 127 ? -11.998 40.060 30.956  1.00 52.00  ? 156 MET A CE  1 
ATOM   950  N  N   . GLY A 1 128 ? -7.220  37.195 29.923  1.00 55.87  ? 157 GLY A N   1 
ATOM   951  C  CA  . GLY A 1 128 ? -6.994  36.267 28.832  1.00 55.83  ? 157 GLY A CA  1 
ATOM   952  C  C   . GLY A 1 128 ? -5.912  36.665 27.864  1.00 55.50  ? 157 GLY A C   1 
ATOM   953  O  O   . GLY A 1 128 ? -5.563  35.869 27.003  1.00 55.80  ? 157 GLY A O   1 
ATOM   954  N  N   . LEU A 1 129 ? -5.383  37.881 27.974  1.00 55.05  ? 158 LEU A N   1 
ATOM   955  C  CA  . LEU A 1 129 ? -4.328  38.326 27.080  1.00 55.32  ? 158 LEU A CA  1 
ATOM   956  C  C   . LEU A 1 129 ? -3.019  37.589 27.344  1.00 55.21  ? 158 LEU A C   1 
ATOM   957  O  O   . LEU A 1 129 ? -2.603  37.417 28.490  1.00 55.05  ? 158 LEU A O   1 
ATOM   958  C  CB  . LEU A 1 129 ? -4.148  39.843 27.144  1.00 55.73  ? 158 LEU A CB  1 
ATOM   959  C  CG  . LEU A 1 129 ? -5.365  40.682 26.813  1.00 57.25  ? 158 LEU A CG  1 
ATOM   960  C  CD1 . LEU A 1 129 ? -5.036  42.131 26.891  1.00 57.74  ? 158 LEU A CD1 1 
ATOM   961  C  CD2 . LEU A 1 129 ? -5.880  40.371 25.437  1.00 58.25  ? 158 LEU A CD2 1 
ATOM   962  N  N   . GLY A 1 130 ? -2.433  37.108 26.262  1.00 55.29  ? 159 GLY A N   1 
ATOM   963  C  CA  . GLY A 1 130 ? -1.196  36.348 26.249  1.00 56.29  ? 159 GLY A CA  1 
ATOM   964  C  C   . GLY A 1 130 ? -0.956  35.715 24.889  1.00 57.41  ? 159 GLY A C   1 
ATOM   965  O  O   . GLY A 1 130 ? -1.891  35.504 24.121  1.00 57.96  ? 159 GLY A O   1 
ATOM   966  N  N   . GLY A 1 131 ? 0.294   35.432 24.573  1.00 57.30  ? 160 GLY A N   1 
ATOM   967  C  CA  . GLY A 1 131 ? 0.652   34.815 23.305  1.00 57.25  ? 160 GLY A CA  1 
ATOM   968  C  C   . GLY A 1 131 ? 2.082   34.322 23.290  1.00 57.39  ? 160 GLY A C   1 
ATOM   969  O  O   . GLY A 1 131 ? 2.828   34.524 24.252  1.00 57.42  ? 160 GLY A O   1 
ATOM   970  N  N   . LEU A 1 132 ? 2.486   33.686 22.192  1.00 57.25  ? 161 LEU A N   1 
ATOM   971  C  CA  . LEU A 1 132 ? 3.835   33.137 22.074  1.00 57.51  ? 161 LEU A CA  1 
ATOM   972  C  C   . LEU A 1 132 ? 4.658   33.780 20.965  1.00 58.30  ? 161 LEU A C   1 
ATOM   973  O  O   . LEU A 1 132 ? 4.112   34.394 20.055  1.00 58.60  ? 161 LEU A O   1 
ATOM   974  C  CB  . LEU A 1 132 ? 3.748   31.629 21.815  1.00 57.08  ? 161 LEU A CB  1 
ATOM   975  C  CG  . LEU A 1 132 ? 3.229   30.823 22.959  1.00 57.53  ? 161 LEU A CG  1 
ATOM   976  C  CD1 . LEU A 1 132 ? 2.512   29.618 22.462  1.00 57.41  ? 161 LEU A CD1 1 
ATOM   977  C  CD2 . LEU A 1 132 ? 4.343   30.458 23.901  1.00 58.40  ? 161 LEU A CD2 1 
ATOM   978  N  N   . ILE A 1 133 ? 5.983   33.638 21.055  1.00 58.40  ? 162 ILE A N   1 
ATOM   979  C  CA  . ILE A 1 133 ? 6.938   34.090 20.054  1.00 59.04  ? 162 ILE A CA  1 
ATOM   980  C  C   . ILE A 1 133 ? 7.925   32.921 19.856  1.00 60.56  ? 162 ILE A C   1 
ATOM   981  O  O   . ILE A 1 133 ? 8.691   32.598 20.763  1.00 60.54  ? 162 ILE A O   1 
ATOM   982  C  CB  . ILE A 1 133 ? 7.679   35.409 20.433  1.00 58.68  ? 162 ILE A CB  1 
ATOM   983  C  CG1 . ILE A 1 133 ? 6.707   36.588 20.633  1.00 58.97  ? 162 ILE A CG1 1 
ATOM   984  C  CG2 . ILE A 1 133 ? 8.739   35.742 19.384  1.00 59.02  ? 162 ILE A CG2 1 
ATOM   985  C  CD1 . ILE A 1 133 ? 7.365   37.965 21.000  1.00 59.72  ? 162 ILE A CD1 1 
ATOM   986  N  N   . ILE A 1 134 ? 7.870   32.258 18.698  1.00 61.23  ? 163 ILE A N   1 
ATOM   987  C  CA  . ILE A 1 134 ? 8.782   31.165 18.398  1.00 62.19  ? 163 ILE A CA  1 
ATOM   988  C  C   . ILE A 1 134 ? 9.895   31.715 17.538  1.00 64.33  ? 163 ILE A C   1 
ATOM   989  O  O   . ILE A 1 134 ? 9.653   32.107 16.399  1.00 64.84  ? 163 ILE A O   1 
ATOM   990  C  CB  . ILE A 1 134 ? 8.052   30.002 17.694  1.00 61.86  ? 163 ILE A CB  1 
ATOM   991  C  CG1 . ILE A 1 134 ? 6.866   29.483 18.538  1.00 62.72  ? 163 ILE A CG1 1 
ATOM   992  C  CG2 . ILE A 1 134 ? 9.022   28.894 17.312  1.00 61.64  ? 163 ILE A CG2 1 
ATOM   993  C  CD1 . ILE A 1 134 ? 7.191   29.130 19.986  1.00 64.03  ? 163 ILE A CD1 1 
ATOM   994  N  N   . ILE A 1 135 ? 11.106  31.788 18.085  1.00 65.40  ? 164 ILE A N   1 
ATOM   995  C  CA  . ILE A 1 135 ? 12.254  32.288 17.334  1.00 66.82  ? 164 ILE A CA  1 
ATOM   996  C  C   . ILE A 1 135 ? 12.999  31.100 16.723  1.00 68.17  ? 164 ILE A C   1 
ATOM   997  O  O   . ILE A 1 135 ? 13.146  30.065 17.369  1.00 68.30  ? 164 ILE A O   1 
ATOM   998  C  CB  . ILE A 1 135 ? 13.155  33.180 18.228  1.00 67.36  ? 164 ILE A CB  1 
ATOM   999  C  CG1 . ILE A 1 135 ? 12.380  34.413 18.698  1.00 68.38  ? 164 ILE A CG1 1 
ATOM   1000 C  CG2 . ILE A 1 135 ? 14.440  33.591 17.508  1.00 67.80  ? 164 ILE A CG2 1 
ATOM   1001 C  CD1 . ILE A 1 135 ? 13.083  35.174 19.736  1.00 69.83  ? 164 ILE A CD1 1 
ATOM   1002 N  N   . ASP A 1 136 ? 13.411  31.235 15.456  1.00 68.99  ? 165 ASP A N   1 
ATOM   1003 C  CA  . ASP A 1 136 ? 14.122  30.207 14.704  1.00 70.03  ? 165 ASP A CA  1 
ATOM   1004 C  C   . ASP A 1 136 ? 15.486  30.699 14.266  1.00 71.50  ? 165 ASP A C   1 
ATOM   1005 O  O   . ASP A 1 136 ? 15.612  31.845 13.851  1.00 71.50  ? 165 ASP A O   1 
ATOM   1006 C  CB  . ASP A 1 136 ? 13.357  29.902 13.415  1.00 70.47  ? 165 ASP A CB  1 
ATOM   1007 C  CG  . ASP A 1 136 ? 12.210  28.947 13.559  1.00 73.18  ? 165 ASP A CG  1 
ATOM   1008 O  OD1 . ASP A 1 136 ? 12.189  28.189 14.559  1.00 73.55  ? 165 ASP A OD1 1 
ATOM   1009 O  OD2 . ASP A 1 136 ? 11.347  28.931 12.661  1.00 74.84  ? 165 ASP A OD2 1 
ATOM   1010 N  N   . ASP A 1 137 ? 16.485  29.819 14.274  1.00 72.35  ? 166 ASP A N   1 
ATOM   1011 C  CA  . ASP A 1 137 ? 17.800  30.149 13.737  1.00 73.65  ? 166 ASP A CA  1 
ATOM   1012 C  C   . ASP A 1 137 ? 18.397  28.934 12.997  1.00 75.60  ? 166 ASP A C   1 
ATOM   1013 O  O   . ASP A 1 137 ? 17.859  27.830 13.100  1.00 76.26  ? 166 ASP A O   1 
ATOM   1014 C  CB  . ASP A 1 137 ? 18.740  30.780 14.781  1.00 74.23  ? 166 ASP A CB  1 
ATOM   1015 C  CG  . ASP A 1 137 ? 19.150  29.925 15.958  1.00 76.88  ? 166 ASP A CG  1 
ATOM   1016 O  OD1 . ASP A 1 137 ? 19.366  28.722 15.769  1.00 76.63  ? 166 ASP A OD1 1 
ATOM   1017 O  OD2 . ASP A 1 137 ? 19.311  30.477 17.061  1.00 79.00  ? 166 ASP A OD2 1 
ATOM   1018 N  N   . GLU A 1 138 ? 19.454  29.138 12.207  1.00 76.65  ? 167 GLU A N   1 
ATOM   1019 C  CA  . GLU A 1 138 ? 20.063  28.050 11.449  1.00 78.20  ? 167 GLU A CA  1 
ATOM   1020 C  C   . GLU A 1 138 ? 20.631  26.982 12.383  1.00 78.71  ? 167 GLU A C   1 
ATOM   1021 O  O   . GLU A 1 138 ? 20.426  25.792 12.147  1.00 78.94  ? 167 GLU A O   1 
ATOM   1022 C  CB  . GLU A 1 138 ? 21.153  28.592 10.506  1.00 82.14  ? 167 GLU A CB  1 
ATOM   1023 C  CG  . GLU A 1 138 ? 21.763  27.533 9.597   1.00 90.06  ? 167 GLU A CG  1 
ATOM   1024 C  CD  . GLU A 1 138 ? 23.210  27.778 9.208   1.00 99.20  ? 167 GLU A CD  1 
ATOM   1025 O  OE1 . GLU A 1 138 ? 24.069  27.820 10.120  1.00 101.34 ? 167 GLU A OE1 1 
ATOM   1026 O  OE2 . GLU A 1 138 ? 23.488  27.910 7.993   1.00 101.81 ? 167 GLU A OE2 1 
ATOM   1027 N  N   . GLU A 1 139 ? 21.312  27.409 13.457  1.00 78.70  ? 168 GLU A N   1 
ATOM   1028 C  CA  . GLU A 1 139 ? 21.925  26.502 14.427  1.00 79.22  ? 168 GLU A CA  1 
ATOM   1029 C  C   . GLU A 1 139 ? 20.939  25.487 15.030  1.00 78.73  ? 168 GLU A C   1 
ATOM   1030 O  O   . GLU A 1 139 ? 21.222  24.289 15.034  1.00 78.89  ? 168 GLU A O   1 
ATOM   1031 C  CB  . GLU A 1 139 ? 22.643  27.296 15.530  1.00 82.60  ? 168 GLU A CB  1 
ATOM   1032 C  CG  . GLU A 1 139 ? 23.378  26.417 16.524  1.00 90.26  ? 168 GLU A CG  1 
ATOM   1033 C  CD  . GLU A 1 139 ? 24.250  27.166 17.516  1.00 101.36 ? 168 GLU A CD  1 
ATOM   1034 O  OE1 . GLU A 1 139 ? 25.178  26.537 18.078  1.00 103.99 ? 168 GLU A OE1 1 
ATOM   1035 O  OE2 . GLU A 1 139 ? 24.012  28.380 17.728  1.00 104.38 ? 168 GLU A OE2 1 
ATOM   1036 N  N   . SER A 1 140 ? 19.774  25.965 15.494  1.00 77.85  ? 169 SER A N   1 
ATOM   1037 C  CA  . SER A 1 140 ? 18.733  25.144 16.102  1.00 77.40  ? 169 SER A CA  1 
ATOM   1038 C  C   . SER A 1 140 ? 18.060  24.228 15.090  1.00 77.41  ? 169 SER A C   1 
ATOM   1039 O  O   . SER A 1 140 ? 17.681  23.107 15.435  1.00 78.02  ? 169 SER A O   1 
ATOM   1040 C  CB  . SER A 1 140 ? 17.674  26.029 16.756  1.00 77.96  ? 169 SER A CB  1 
ATOM   1041 O  OG  . SER A 1 140 ? 16.812  26.655 15.815  1.00 79.29  ? 169 SER A OG  1 
ATOM   1042 N  N   . THR A 1 141 ? 17.878  24.718 13.855  1.00 76.57  ? 170 THR A N   1 
ATOM   1043 C  CA  . THR A 1 141 ? 17.197  23.990 12.791  1.00 76.44  ? 170 THR A CA  1 
ATOM   1044 C  C   . THR A 1 141 ? 17.950  22.726 12.371  1.00 76.49  ? 170 THR A C   1 
ATOM   1045 O  O   . THR A 1 141 ? 17.322  21.726 12.031  1.00 76.66  ? 170 THR A O   1 
ATOM   1046 C  CB  . THR A 1 141 ? 16.904  24.942 11.637  1.00 77.44  ? 170 THR A CB  1 
ATOM   1047 O  OG1 . THR A 1 141 ? 15.994  25.946 12.106  1.00 78.48  ? 170 THR A OG1 1 
ATOM   1048 C  CG2 . THR A 1 141 ? 16.318  24.239 10.431  1.00 77.59  ? 170 THR A CG2 1 
ATOM   1049 N  N   . LYS A 1 142 ? 19.286  22.743 12.460  1.00 76.20  ? 171 LYS A N   1 
ATOM   1050 C  CA  . LYS A 1 142 ? 20.118  21.588 12.126  1.00 76.37  ? 171 LYS A CA  1 
ATOM   1051 C  C   . LYS A 1 142 ? 19.855  20.407 13.080  1.00 75.52  ? 171 LYS A C   1 
ATOM   1052 O  O   . LYS A 1 142 ? 19.915  19.251 12.660  1.00 75.88  ? 171 LYS A O   1 
ATOM   1053 C  CB  . LYS A 1 142 ? 21.599  21.975 12.191  1.00 79.28  ? 171 LYS A CB  1 
ATOM   1054 C  CG  . LYS A 1 142 ? 22.009  22.988 11.138  1.00 84.98  ? 171 LYS A CG  1 
ATOM   1055 C  CD  . LYS A 1 142 ? 23.445  23.463 11.345  1.00 90.63  ? 171 LYS A CD  1 
ATOM   1056 C  CE  . LYS A 1 142 ? 23.890  24.362 10.216  1.00 95.14  ? 171 LYS A CE  1 
ATOM   1057 N  NZ  . LYS A 1 142 ? 25.216  24.980 10.484  1.00 97.64  ? 171 LYS A NZ  1 
ATOM   1058 N  N   . LEU A 1 143 ? 19.580  20.705 14.358  1.00 74.07  ? 172 LEU A N   1 
ATOM   1059 C  CA  . LEU A 1 143 ? 19.310  19.707 15.389  1.00 73.23  ? 172 LEU A CA  1 
ATOM   1060 C  C   . LEU A 1 143 ? 18.070  18.890 15.047  1.00 72.08  ? 172 LEU A C   1 
ATOM   1061 O  O   . LEU A 1 143 ? 17.106  19.437 14.512  1.00 72.25  ? 172 LEU A O   1 
ATOM   1062 C  CB  . LEU A 1 143 ? 19.119  20.404 16.743  1.00 73.47  ? 172 LEU A CB  1 
ATOM   1063 C  CG  . LEU A 1 143 ? 20.363  21.045 17.325  1.00 74.72  ? 172 LEU A CG  1 
ATOM   1064 C  CD1 . LEU A 1 143 ? 20.024  21.852 18.543  1.00 75.14  ? 172 LEU A CD1 1 
ATOM   1065 C  CD2 . LEU A 1 143 ? 21.382  19.997 17.683  1.00 75.26  ? 172 LEU A CD2 1 
ATOM   1066 N  N   . PRO A 1 144 ? 18.057  17.582 15.368  1.00 70.75  ? 173 PRO A N   1 
ATOM   1067 C  CA  . PRO A 1 144 ? 16.890  16.755 15.015  1.00 69.98  ? 173 PRO A CA  1 
ATOM   1068 C  C   . PRO A 1 144 ? 15.743  16.790 16.023  1.00 69.34  ? 173 PRO A C   1 
ATOM   1069 O  O   . PRO A 1 144 ? 15.126  15.763 16.270  1.00 69.00  ? 173 PRO A O   1 
ATOM   1070 C  CB  . PRO A 1 144 ? 17.482  15.354 14.910  1.00 70.66  ? 173 PRO A CB  1 
ATOM   1071 C  CG  . PRO A 1 144 ? 18.597  15.360 15.900  1.00 71.34  ? 173 PRO A CG  1 
ATOM   1072 C  CD  . PRO A 1 144 ? 19.124  16.775 15.996  1.00 70.02  ? 173 PRO A CD  1 
ATOM   1073 N  N   . LEU A 1 145 ? 15.483  17.952 16.625  1.00 69.02  ? 174 LEU A N   1 
ATOM   1074 C  CA  . LEU A 1 145 ? 14.404  18.121 17.590  1.00 69.10  ? 174 LEU A CA  1 
ATOM   1075 C  C   . LEU A 1 145 ? 13.066  18.094 16.866  1.00 69.24  ? 174 LEU A C   1 
ATOM   1076 O  O   . LEU A 1 145 ? 12.997  18.521 15.710  1.00 69.67  ? 174 LEU A O   1 
ATOM   1077 C  CB  . LEU A 1 145 ? 14.544  19.483 18.282  1.00 69.37  ? 174 LEU A CB  1 
ATOM   1078 C  CG  . LEU A 1 145 ? 15.793  19.730 19.109  1.00 71.22  ? 174 LEU A CG  1 
ATOM   1079 C  CD1 . LEU A 1 145 ? 15.736  21.090 19.760  1.00 71.86  ? 174 LEU A CD1 1 
ATOM   1080 C  CD2 . LEU A 1 145 ? 15.961  18.681 20.179  1.00 72.09  ? 174 LEU A CD2 1 
ATOM   1081 N  N   . PRO A 1 146 ? 11.970  17.654 17.528  1.00 68.58  ? 175 PRO A N   1 
ATOM   1082 C  CA  . PRO A 1 146 ? 10.657  17.672 16.860  1.00 68.37  ? 175 PRO A CA  1 
ATOM   1083 C  C   . PRO A 1 146 ? 10.287  19.081 16.380  1.00 68.17  ? 175 PRO A C   1 
ATOM   1084 O  O   . PRO A 1 146 ? 10.454  20.043 17.126  1.00 68.26  ? 175 PRO A O   1 
ATOM   1085 C  CB  . PRO A 1 146 ? 9.703   17.165 17.948  1.00 68.88  ? 175 PRO A CB  1 
ATOM   1086 C  CG  . PRO A 1 146 ? 10.551  16.419 18.895  1.00 69.13  ? 175 PRO A CG  1 
ATOM   1087 C  CD  . PRO A 1 146 ? 11.870  17.121 18.897  1.00 67.69  ? 175 PRO A CD  1 
ATOM   1088 N  N   . LYS A 1 147 ? 9.884   19.209 15.108  1.00 67.64  ? 176 LYS A N   1 
ATOM   1089 C  CA  . LYS A 1 147 ? 9.578   20.505 14.502  1.00 67.62  ? 176 LYS A CA  1 
ATOM   1090 C  C   . LYS A 1 147 ? 8.148   20.652 13.999  1.00 66.50  ? 176 LYS A C   1 
ATOM   1091 O  O   . LYS A 1 147 ? 7.782   21.748 13.565  1.00 66.96  ? 176 LYS A O   1 
ATOM   1092 C  CB  . LYS A 1 147 ? 10.528  20.770 13.329  1.00 70.43  ? 176 LYS A CB  1 
ATOM   1093 C  CG  . LYS A 1 147 ? 11.979  20.939 13.740  1.00 76.21  ? 176 LYS A CG  1 
ATOM   1094 C  CD  . LYS A 1 147 ? 12.933  20.287 12.748  1.00 81.68  ? 176 LYS A CD  1 
ATOM   1095 C  CE  . LYS A 1 147 ? 14.368  20.517 13.153  1.00 86.43  ? 176 LYS A CE  1 
ATOM   1096 N  NZ  . LYS A 1 147 ? 15.332  19.814 12.257  1.00 89.37  ? 176 LYS A NZ  1 
ATOM   1097 N  N   . GLU A 1 148 ? 7.357   19.570 13.999  1.00 64.76  ? 177 GLU A N   1 
ATOM   1098 C  CA  . GLU A 1 148 ? 5.988   19.646 13.502  1.00 63.91  ? 177 GLU A CA  1 
ATOM   1099 C  C   . GLU A 1 148 ? 5.074   20.333 14.489  1.00 62.63  ? 177 GLU A C   1 
ATOM   1100 O  O   . GLU A 1 148 ? 4.569   19.698 15.415  1.00 62.60  ? 177 GLU A O   1 
ATOM   1101 C  CB  . GLU A 1 148 ? 5.440   18.266 13.133  1.00 65.82  ? 177 GLU A CB  1 
ATOM   1102 C  CG  . GLU A 1 148 ? 4.152   18.351 12.337  1.00 69.44  ? 177 GLU A CG  1 
ATOM   1103 C  CD  . GLU A 1 148 ? 3.721   17.056 11.690  1.00 75.31  ? 177 GLU A CD  1 
ATOM   1104 O  OE1 . GLU A 1 148 ? 2.831   17.109 10.810  1.00 77.23  ? 177 GLU A OE1 1 
ATOM   1105 O  OE2 . GLU A 1 148 ? 4.260   15.989 12.064  1.00 77.17  ? 177 GLU A OE2 1 
ATOM   1106 N  N   . TRP A 1 149 ? 4.855   21.639 14.280  1.00 61.36  ? 178 TRP A N   1 
ATOM   1107 C  CA  . TRP A 1 149 ? 4.009   22.471 15.127  1.00 60.86  ? 178 TRP A CA  1 
ATOM   1108 C  C   . TRP A 1 149 ? 2.632   21.868 15.364  1.00 60.66  ? 178 TRP A C   1 
ATOM   1109 O  O   . TRP A 1 149 ? 1.991   21.393 14.429  1.00 61.25  ? 178 TRP A O   1 
ATOM   1110 C  CB  . TRP A 1 149 ? 3.853   23.858 14.511  1.00 60.46  ? 178 TRP A CB  1 
ATOM   1111 C  CG  . TRP A 1 149 ? 3.083   24.803 15.375  1.00 60.65  ? 178 TRP A CG  1 
ATOM   1112 C  CD1 . TRP A 1 149 ? 1.798   25.218 15.200  1.00 61.31  ? 178 TRP A CD1 1 
ATOM   1113 C  CD2 . TRP A 1 149 ? 3.537   25.399 16.595  1.00 60.81  ? 178 TRP A CD2 1 
ATOM   1114 N  NE1 . TRP A 1 149 ? 1.433   26.065 16.219  1.00 61.52  ? 178 TRP A NE1 1 
ATOM   1115 C  CE2 . TRP A 1 149 ? 2.486   26.198 17.086  1.00 61.43  ? 178 TRP A CE2 1 
ATOM   1116 C  CE3 . TRP A 1 149 ? 4.750   25.363 17.305  1.00 61.43  ? 178 TRP A CE3 1 
ATOM   1117 C  CZ2 . TRP A 1 149 ? 2.603   26.943 18.255  1.00 62.32  ? 178 TRP A CZ2 1 
ATOM   1118 C  CZ3 . TRP A 1 149 ? 4.866   26.105 18.461  1.00 62.36  ? 178 TRP A CZ3 1 
ATOM   1119 C  CH2 . TRP A 1 149 ? 3.808   26.896 18.918  1.00 62.58  ? 178 TRP A CH2 1 
ATOM   1120 N  N   . GLY A 1 150 ? 2.213   21.845 16.615  1.00 59.68  ? 179 GLY A N   1 
ATOM   1121 C  CA  . GLY A 1 150 ? 0.918   21.304 16.976  1.00 59.80  ? 179 GLY A CA  1 
ATOM   1122 C  C   . GLY A 1 150 ? 0.815   19.800 16.917  1.00 60.51  ? 179 GLY A C   1 
ATOM   1123 O  O   . GLY A 1 150 ? -0.230  19.256 17.263  1.00 61.02  ? 179 GLY A O   1 
ATOM   1124 N  N   . VAL A 1 151 ? 1.875   19.109 16.466  1.00 60.32  ? 180 VAL A N   1 
ATOM   1125 C  CA  . VAL A 1 151 ? 1.883   17.653 16.393  1.00 60.27  ? 180 VAL A CA  1 
ATOM   1126 C  C   . VAL A 1 151 ? 2.931   17.101 17.363  1.00 60.07  ? 180 VAL A C   1 
ATOM   1127 O  O   . VAL A 1 151 ? 2.565   16.442 18.336  1.00 60.08  ? 180 VAL A O   1 
ATOM   1128 C  CB  . VAL A 1 151 ? 2.042   17.140 14.938  1.00 60.87  ? 180 VAL A CB  1 
ATOM   1129 C  CG1 . VAL A 1 151 ? 2.350   15.648 14.912  1.00 61.49  ? 180 VAL A CG1 1 
ATOM   1130 C  CG2 . VAL A 1 151 ? 0.802   17.456 14.113  1.00 61.23  ? 180 VAL A CG2 1 
ATOM   1131 N  N   . ASP A 1 152 ? 4.222   17.407 17.129  1.00 59.79  ? 181 ASP A N   1 
ATOM   1132 C  CA  . ASP A 1 152 ? 5.307   16.988 18.010  1.00 59.99  ? 181 ASP A CA  1 
ATOM   1133 C  C   . ASP A 1 152 ? 6.086   18.167 18.607  1.00 60.04  ? 181 ASP A C   1 
ATOM   1134 O  O   . ASP A 1 152 ? 6.961   17.952 19.428  1.00 60.41  ? 181 ASP A O   1 
ATOM   1135 C  CB  . ASP A 1 152 ? 6.248   15.956 17.358  1.00 61.75  ? 181 ASP A CB  1 
ATOM   1136 C  CG  . ASP A 1 152 ? 6.796   16.289 15.981  1.00 66.46  ? 181 ASP A CG  1 
ATOM   1137 O  OD1 . ASP A 1 152 ? 7.103   17.462 15.739  1.00 68.17  ? 181 ASP A OD1 1 
ATOM   1138 O  OD2 . ASP A 1 152 ? 6.970   15.355 15.165  1.00 67.50  ? 181 ASP A OD2 1 
ATOM   1139 N  N   . ASP A 1 153 ? 5.768   19.402 18.213  1.00 59.72  ? 182 ASP A N   1 
ATOM   1140 C  CA  . ASP A 1 153 ? 6.366   20.617 18.748  1.00 59.85  ? 182 ASP A CA  1 
ATOM   1141 C  C   . ASP A 1 153 ? 5.148   21.334 19.290  1.00 59.82  ? 182 ASP A C   1 
ATOM   1142 O  O   . ASP A 1 153 ? 4.387   21.926 18.521  1.00 59.92  ? 182 ASP A O   1 
ATOM   1143 C  CB  . ASP A 1 153 ? 7.016   21.433 17.616  1.00 61.27  ? 182 ASP A CB  1 
ATOM   1144 C  CG  . ASP A 1 153 ? 7.783   22.658 18.077  1.00 65.44  ? 182 ASP A CG  1 
ATOM   1145 O  OD1 . ASP A 1 153 ? 7.829   22.904 19.306  1.00 65.68  ? 182 ASP A OD1 1 
ATOM   1146 O  OD2 . ASP A 1 153 ? 8.342   23.369 17.209  1.00 67.75  ? 182 ASP A OD2 1 
ATOM   1147 N  N   . VAL A 1 154 ? 4.886   21.181 20.592  1.00 59.09  ? 183 VAL A N   1 
ATOM   1148 C  CA  . VAL A 1 154 ? 3.649   21.670 21.182  1.00 58.44  ? 183 VAL A CA  1 
ATOM   1149 C  C   . VAL A 1 154 ? 3.818   22.709 22.271  1.00 57.28  ? 183 VAL A C   1 
ATOM   1150 O  O   . VAL A 1 154 ? 4.456   22.450 23.292  1.00 57.56  ? 183 VAL A O   1 
ATOM   1151 C  CB  . VAL A 1 154 ? 2.827   20.462 21.713  1.00 59.42  ? 183 VAL A CB  1 
ATOM   1152 C  CG1 . VAL A 1 154 ? 1.505   20.914 22.302  1.00 59.99  ? 183 VAL A CG1 1 
ATOM   1153 C  CG2 . VAL A 1 154 ? 2.590   19.427 20.618  1.00 60.18  ? 183 VAL A CG2 1 
ATOM   1154 N  N   . PRO A 1 155 ? 3.125   23.851 22.137  1.00 55.76  ? 184 PRO A N   1 
ATOM   1155 C  CA  . PRO A 1 155 ? 3.150   24.848 23.214  1.00 54.61  ? 184 PRO A CA  1 
ATOM   1156 C  C   . PRO A 1 155 ? 2.216   24.473 24.369  1.00 53.75  ? 184 PRO A C   1 
ATOM   1157 O  O   . PRO A 1 155 ? 1.075   24.071 24.143  1.00 53.74  ? 184 PRO A O   1 
ATOM   1158 C  CB  . PRO A 1 155 ? 2.641   26.101 22.521  1.00 55.12  ? 184 PRO A CB  1 
ATOM   1159 C  CG  . PRO A 1 155 ? 1.724   25.600 21.501  1.00 55.84  ? 184 PRO A CG  1 
ATOM   1160 C  CD  . PRO A 1 155 ? 2.286   24.293 21.008  1.00 54.78  ? 184 PRO A CD  1 
ATOM   1161 N  N   . VAL A 1 156 ? 2.693   24.605 25.611  1.00 52.79  ? 185 VAL A N   1 
ATOM   1162 C  CA  . VAL A 1 156 ? 1.878   24.315 26.785  1.00 52.14  ? 185 VAL A CA  1 
ATOM   1163 C  C   . VAL A 1 156 ? 1.877   25.525 27.724  1.00 51.26  ? 185 VAL A C   1 
ATOM   1164 O  O   . VAL A 1 156 ? 2.819   25.725 28.484  1.00 50.91  ? 185 VAL A O   1 
ATOM   1165 C  CB  . VAL A 1 156 ? 2.323   23.022 27.506  1.00 52.81  ? 185 VAL A CB  1 
ATOM   1166 C  CG1 . VAL A 1 156 ? 1.384   22.691 28.656  1.00 53.39  ? 185 VAL A CG1 1 
ATOM   1167 C  CG2 . VAL A 1 156 ? 2.434   21.852 26.540  1.00 52.99  ? 185 VAL A CG2 1 
ATOM   1168 N  N   . ILE A 1 157 ? 0.828   26.345 27.640  1.00 50.83  ? 186 ILE A N   1 
ATOM   1169 C  CA  . ILE A 1 157 ? 0.644   27.536 28.461  1.00 50.93  ? 186 ILE A CA  1 
ATOM   1170 C  C   . ILE A 1 157 ? -0.197  27.174 29.655  1.00 50.66  ? 186 ILE A C   1 
ATOM   1171 O  O   . ILE A 1 157 ? -1.378  26.888 29.516  1.00 50.22  ? 186 ILE A O   1 
ATOM   1172 C  CB  . ILE A 1 157 ? -0.046  28.645 27.653  1.00 51.79  ? 186 ILE A CB  1 
ATOM   1173 C  CG1 . ILE A 1 157 ? 0.752   28.992 26.382  1.00 52.57  ? 186 ILE A CG1 1 
ATOM   1174 C  CG2 . ILE A 1 157 ? -0.303  29.874 28.527  1.00 52.38  ? 186 ILE A CG2 1 
ATOM   1175 C  CD1 . ILE A 1 157 ? -0.026  29.815 25.433  1.00 53.67  ? 186 ILE A CD1 1 
ATOM   1176 N  N   . LEU A 1 158 ? 0.410   27.202 30.833  1.00 51.07  ? 187 LEU A N   1 
ATOM   1177 C  CA  . LEU A 1 158 ? -0.225  26.835 32.086  1.00 51.80  ? 187 LEU A CA  1 
ATOM   1178 C  C   . LEU A 1 158 ? -0.563  28.052 32.922  1.00 52.91  ? 187 LEU A C   1 
ATOM   1179 O  O   . LEU A 1 158 ? 0.323   28.711 33.442  1.00 53.35  ? 187 LEU A O   1 
ATOM   1180 C  CB  . LEU A 1 158 ? 0.719   25.916 32.864  1.00 51.80  ? 187 LEU A CB  1 
ATOM   1181 C  CG  . LEU A 1 158 ? 1.111   24.639 32.150  1.00 52.85  ? 187 LEU A CG  1 
ATOM   1182 C  CD1 . LEU A 1 158 ? 2.169   23.904 32.912  1.00 52.84  ? 187 LEU A CD1 1 
ATOM   1183 C  CD2 . LEU A 1 158 ? -0.097  23.765 31.910  1.00 53.52  ? 187 LEU A CD2 1 
ATOM   1184 N  N   . GLN A 1 159 ? -1.848  28.354 33.049  1.00 53.22  ? 188 GLN A N   1 
ATOM   1185 C  CA  . GLN A 1 159 ? -2.330  29.484 33.825  1.00 53.64  ? 188 GLN A CA  1 
ATOM   1186 C  C   . GLN A 1 159 ? -3.455  29.012 34.717  1.00 54.84  ? 188 GLN A C   1 
ATOM   1187 O  O   . GLN A 1 159 ? -4.304  28.249 34.268  1.00 55.26  ? 188 GLN A O   1 
ATOM   1188 C  CB  . GLN A 1 159 ? -2.931  30.556 32.901  1.00 54.69  ? 188 GLN A CB  1 
ATOM   1189 C  CG  . GLN A 1 159 ? -2.105  30.947 31.696  1.00 57.80  ? 188 GLN A CG  1 
ATOM   1190 C  CD  . GLN A 1 159 ? -2.875  31.906 30.826  1.00 62.97  ? 188 GLN A CD  1 
ATOM   1191 O  OE1 . GLN A 1 159 ? -3.907  31.559 30.227  1.00 64.48  ? 188 GLN A OE1 1 
ATOM   1192 N  NE2 . GLN A 1 159 ? -2.400  33.144 30.751  1.00 64.15  ? 188 GLN A NE2 1 
ATOM   1193 N  N   . ASP A 1 160 ? -3.521  29.512 35.945  1.00 55.50  ? 189 ASP A N   1 
ATOM   1194 C  CA  . ASP A 1 160 ? -4.654  29.215 36.823  1.00 56.44  ? 189 ASP A CA  1 
ATOM   1195 C  C   . ASP A 1 160 ? -5.602  30.425 36.825  1.00 56.76  ? 189 ASP A C   1 
ATOM   1196 O  O   . ASP A 1 160 ? -5.161  31.554 36.603  1.00 56.84  ? 189 ASP A O   1 
ATOM   1197 C  CB  . ASP A 1 160 ? -4.206  28.836 38.240  1.00 58.50  ? 189 ASP A CB  1 
ATOM   1198 C  CG  . ASP A 1 160 ? -3.626  29.980 39.049  1.00 63.41  ? 189 ASP A CG  1 
ATOM   1199 O  OD1 . ASP A 1 160 ? -2.979  30.864 38.449  1.00 64.72  ? 189 ASP A OD1 1 
ATOM   1200 O  OD2 . ASP A 1 160 ? -3.813  29.988 40.282  1.00 64.90  ? 189 ASP A OD2 1 
ATOM   1201 N  N   . LYS A 1 161 ? -6.899  30.195 37.024  1.00 56.87  ? 190 LYS A N   1 
ATOM   1202 C  CA  . LYS A 1 161 ? -7.878  31.284 37.034  1.00 57.20  ? 190 LYS A CA  1 
ATOM   1203 C  C   . LYS A 1 161 ? -8.918  31.095 38.134  1.00 59.30  ? 190 LYS A C   1 
ATOM   1204 O  O   . LYS A 1 161 ? -9.210  29.968 38.536  1.00 59.12  ? 190 LYS A O   1 
ATOM   1205 C  CB  . LYS A 1 161 ? -8.576  31.431 35.665  1.00 56.36  ? 190 LYS A CB  1 
ATOM   1206 C  CG  . LYS A 1 161 ? -7.691  31.968 34.540  1.00 55.94  ? 190 LYS A CG  1 
ATOM   1207 C  CD  . LYS A 1 161 ? -8.509  32.532 33.391  1.00 55.84  ? 190 LYS A CD  1 
ATOM   1208 C  CE  . LYS A 1 161 ? -7.668  32.951 32.214  1.00 56.34  ? 190 LYS A CE  1 
ATOM   1209 N  NZ  . LYS A 1 161 ? -6.524  33.786 32.636  1.00 56.50  ? 190 LYS A NZ  1 
ATOM   1210 N  N   . ARG A 1 162 ? -9.494  32.200 38.609  1.00 61.09  ? 191 ARG A N   1 
ATOM   1211 C  CA  . ARG A 1 162 ? -10.524 32.160 39.640  1.00 63.06  ? 191 ARG A CA  1 
ATOM   1212 C  C   . ARG A 1 162 ? -11.803 32.728 39.076  1.00 64.63  ? 191 ARG A C   1 
ATOM   1213 O  O   . ARG A 1 162 ? -11.777 33.805 38.494  1.00 64.68  ? 191 ARG A O   1 
ATOM   1214 C  CB  . ARG A 1 162 ? -10.100 32.966 40.872  1.00 64.97  ? 191 ARG A CB  1 
ATOM   1215 C  CG  . ARG A 1 162 ? -11.062 32.815 42.033  1.00 70.04  ? 191 ARG A CG  1 
ATOM   1216 C  CD  . ARG A 1 162 ? -10.364 32.974 43.363  1.00 75.66  ? 191 ARG A CD  1 
ATOM   1217 N  NE  . ARG A 1 162 ? -9.843  34.331 43.543  1.00 81.36  ? 191 ARG A NE  1 
ATOM   1218 C  CZ  . ARG A 1 162 ? -8.793  34.636 44.305  1.00 85.23  ? 191 ARG A CZ  1 
ATOM   1219 N  NH1 . ARG A 1 162 ? -8.126  33.679 44.946  1.00 85.03  ? 191 ARG A NH1 1 
ATOM   1220 N  NH2 . ARG A 1 162 ? -8.384  35.898 44.409  1.00 85.41  ? 191 ARG A NH2 1 
ATOM   1221 N  N   . LEU A 1 163 ? -12.924 32.013 39.231  1.00 65.88  ? 192 LEU A N   1 
ATOM   1222 C  CA  . LEU A 1 163 ? -14.213 32.505 38.752  1.00 67.42  ? 192 LEU A CA  1 
ATOM   1223 C  C   . LEU A 1 163 ? -15.208 32.734 39.894  1.00 68.92  ? 192 LEU A C   1 
ATOM   1224 O  O   . LEU A 1 163 ? -15.233 31.971 40.859  1.00 69.19  ? 192 LEU A O   1 
ATOM   1225 C  CB  . LEU A 1 163 ? -14.825 31.531 37.742  1.00 67.77  ? 192 LEU A CB  1 
ATOM   1226 C  CG  . LEU A 1 163 ? -13.953 31.133 36.560  1.00 69.66  ? 192 LEU A CG  1 
ATOM   1227 C  CD1 . LEU A 1 163 ? -14.691 30.170 35.659  1.00 69.96  ? 192 LEU A CD1 1 
ATOM   1228 C  CD2 . LEU A 1 163 ? -13.505 32.357 35.756  1.00 70.71  ? 192 LEU A CD2 1 
ATOM   1229 N  N   . ASP A 1 164 ? -16.049 33.763 39.773  1.00 69.75  ? 193 ASP A N   1 
ATOM   1230 C  CA  . ASP A 1 164 ? -17.093 34.020 40.765  1.00 71.08  ? 193 ASP A CA  1 
ATOM   1231 C  C   . ASP A 1 164 ? -18.321 33.095 40.508  1.00 72.36  ? 193 ASP A C   1 
ATOM   1232 O  O   . ASP A 1 164 ? -18.358 32.393 39.488  1.00 72.67  ? 193 ASP A O   1 
ATOM   1233 C  CB  . ASP A 1 164 ? -17.475 35.518 40.787  1.00 72.80  ? 193 ASP A CB  1 
ATOM   1234 C  CG  . ASP A 1 164 ? -18.202 36.035 39.558  1.00 78.13  ? 193 ASP A CG  1 
ATOM   1235 O  OD1 . ASP A 1 164 ? -18.576 35.211 38.697  1.00 78.69  ? 193 ASP A OD1 1 
ATOM   1236 O  OD2 . ASP A 1 164 ? -18.404 37.268 39.459  1.00 80.96  ? 193 ASP A OD2 1 
ATOM   1237 N  N   . ALA A 1 165 ? -19.328 33.109 41.404  1.00 72.70  ? 194 ALA A N   1 
ATOM   1238 C  CA  . ALA A 1 165 ? -20.538 32.293 41.257  1.00 73.46  ? 194 ALA A CA  1 
ATOM   1239 C  C   . ALA A 1 165 ? -21.251 32.492 39.913  1.00 74.30  ? 194 ALA A C   1 
ATOM   1240 O  O   . ALA A 1 165 ? -21.785 31.528 39.363  1.00 74.90  ? 194 ALA A O   1 
ATOM   1241 C  CB  . ALA A 1 165 ? -21.497 32.568 42.396  1.00 73.55  ? 194 ALA A CB  1 
ATOM   1242 N  N   . LYS A 1 166 ? -21.237 33.721 39.364  1.00 74.30  ? 195 LYS A N   1 
ATOM   1243 C  CA  . LYS A 1 166 ? -21.870 33.991 38.064  1.00 74.70  ? 195 LYS A CA  1 
ATOM   1244 C  C   . LYS A 1 166 ? -21.012 33.568 36.844  1.00 74.39  ? 195 LYS A C   1 
ATOM   1245 O  O   . LYS A 1 166 ? -21.378 33.873 35.705  1.00 74.55  ? 195 LYS A O   1 
ATOM   1246 C  CB  . LYS A 1 166 ? -22.245 35.475 37.920  1.00 77.29  ? 195 LYS A CB  1 
ATOM   1247 C  CG  . LYS A 1 166 ? -22.906 36.105 39.135  1.00 82.62  ? 195 LYS A CG  1 
ATOM   1248 C  CD  . LYS A 1 166 ? -23.301 37.556 38.826  1.00 88.35  ? 195 LYS A CD  1 
ATOM   1249 C  CE  . LYS A 1 166 ? -23.507 38.401 40.064  1.00 92.66  ? 195 LYS A CE  1 
ATOM   1250 N  NZ  . LYS A 1 166 ? -23.725 39.831 39.722  1.00 95.04  ? 195 LYS A NZ  1 
ATOM   1251 N  N   . GLY A 1 167 ? -19.871 32.923 37.090  1.00 73.67  ? 196 GLY A N   1 
ATOM   1252 C  CA  . GLY A 1 167 ? -18.971 32.463 36.042  1.00 73.42  ? 196 GLY A CA  1 
ATOM   1253 C  C   . GLY A 1 167 ? -17.902 33.455 35.627  1.00 72.63  ? 196 GLY A C   1 
ATOM   1254 O  O   . GLY A 1 167 ? -16.897 33.062 35.032  1.00 72.58  ? 196 GLY A O   1 
ATOM   1255 N  N   . HIS A 1 168 ? -18.100 34.745 35.939  1.00 71.67  ? 197 HIS A N   1 
ATOM   1256 C  CA  . HIS A 1 168 ? -17.161 35.810 35.581  1.00 71.30  ? 197 HIS A CA  1 
ATOM   1257 C  C   . HIS A 1 168 ? -15.782 35.644 36.216  1.00 70.24  ? 197 HIS A C   1 
ATOM   1258 O  O   . HIS A 1 168 ? -15.658 34.977 37.237  1.00 70.40  ? 197 HIS A O   1 
ATOM   1259 C  CB  . HIS A 1 168 ? -17.747 37.177 35.944  1.00 72.53  ? 197 HIS A CB  1 
ATOM   1260 C  CG  . HIS A 1 168 ? -19.133 37.382 35.418  1.00 75.89  ? 197 HIS A CG  1 
ATOM   1261 N  ND1 . HIS A 1 168 ? -20.138 37.909 36.215  1.00 77.95  ? 197 HIS A ND1 1 
ATOM   1262 C  CD2 . HIS A 1 168 ? -19.649 37.076 34.203  1.00 77.29  ? 197 HIS A CD2 1 
ATOM   1263 C  CE1 . HIS A 1 168 ? -21.218 37.939 35.451  1.00 78.67  ? 197 HIS A CE1 1 
ATOM   1264 N  NE2 . HIS A 1 168 ? -20.972 37.445 34.232  1.00 78.59  ? 197 HIS A NE2 1 
ATOM   1265 N  N   . ILE A 1 169 ? -14.739 36.223 35.599  1.00 68.95  ? 198 ILE A N   1 
ATOM   1266 C  CA  . ILE A 1 169 ? -13.393 36.139 36.163  1.00 68.10  ? 198 ILE A CA  1 
ATOM   1267 C  C   . ILE A 1 169 ? -13.337 37.005 37.411  1.00 67.18  ? 198 ILE A C   1 
ATOM   1268 O  O   . ILE A 1 169 ? -13.588 38.208 37.347  1.00 66.98  ? 198 ILE A O   1 
ATOM   1269 C  CB  . ILE A 1 169 ? -12.297 36.514 35.136  1.00 68.54  ? 198 ILE A CB  1 
ATOM   1270 C  CG1 . ILE A 1 169 ? -12.260 35.501 33.970  1.00 69.30  ? 198 ILE A CG1 1 
ATOM   1271 C  CG2 . ILE A 1 169 ? -10.931 36.627 35.818  1.00 68.90  ? 198 ILE A CG2 1 
ATOM   1272 C  CD1 . ILE A 1 169 ? -11.305 35.840 32.842  1.00 70.07  ? 198 ILE A CD1 1 
ATOM   1273 N  N   . ASP A 1 170 ? -13.069 36.381 38.553  1.00 66.66  ? 199 ASP A N   1 
ATOM   1274 C  CA  . ASP A 1 170 ? -13.021 37.064 39.836  1.00 66.69  ? 199 ASP A CA  1 
ATOM   1275 C  C   . ASP A 1 170 ? -11.653 37.646 40.129  1.00 66.02  ? 199 ASP A C   1 
ATOM   1276 O  O   . ASP A 1 170 ? -10.803 36.984 40.717  1.00 65.86  ? 199 ASP A O   1 
ATOM   1277 C  CB  . ASP A 1 170 ? -13.441 36.107 40.952  1.00 69.34  ? 199 ASP A CB  1 
ATOM   1278 C  CG  . ASP A 1 170 ? -13.589 36.746 42.315  1.00 75.98  ? 199 ASP A CG  1 
ATOM   1279 O  OD1 . ASP A 1 170 ? -13.632 37.999 42.388  1.00 76.87  ? 199 ASP A OD1 1 
ATOM   1280 O  OD2 . ASP A 1 170 ? -13.679 35.995 43.310  1.00 79.38  ? 199 ASP A OD2 1 
ATOM   1281 N  N   . TYR A 1 171 ? -11.448 38.899 39.741  1.00 65.68  ? 200 TYR A N   1 
ATOM   1282 C  CA  . TYR A 1 171 ? -10.196 39.589 39.997  1.00 65.63  ? 200 TYR A CA  1 
ATOM   1283 C  C   . TYR A 1 171 ? -10.435 40.921 40.706  1.00 66.98  ? 200 TYR A C   1 
ATOM   1284 O  O   . TYR A 1 171 ? -11.005 41.855 40.129  1.00 67.00  ? 200 TYR A O   1 
ATOM   1285 C  CB  . TYR A 1 171 ? -9.405  39.801 38.706  1.00 64.53  ? 200 TYR A CB  1 
ATOM   1286 C  CG  . TYR A 1 171 ? -8.030  40.395 38.924  1.00 64.17  ? 200 TYR A CG  1 
ATOM   1287 C  CD1 . TYR A 1 171 ? -7.858  41.763 39.086  1.00 64.57  ? 200 TYR A CD1 1 
ATOM   1288 C  CD2 . TYR A 1 171 ? -6.895  39.603 38.877  1.00 64.48  ? 200 TYR A CD2 1 
ATOM   1289 C  CE1 . TYR A 1 171 ? -6.600  42.316 39.266  1.00 65.23  ? 200 TYR A CE1 1 
ATOM   1290 C  CE2 . TYR A 1 171 ? -5.631  40.145 39.038  1.00 65.10  ? 200 TYR A CE2 1 
ATOM   1291 C  CZ  . TYR A 1 171 ? -5.486  41.504 39.240  1.00 66.02  ? 200 TYR A CZ  1 
ATOM   1292 O  OH  . TYR A 1 171 ? -4.238  42.057 39.404  1.00 67.52  ? 200 TYR A OH  1 
ATOM   1293 N  N   . GLN A 1 172 ? -9.984  40.996 41.966  1.00 67.81  ? 201 GLN A N   1 
ATOM   1294 C  CA  . GLN A 1 172 ? -10.037 42.196 42.792  1.00 69.08  ? 201 GLN A CA  1 
ATOM   1295 C  C   . GLN A 1 172 ? -8.618  42.465 43.274  1.00 68.41  ? 201 GLN A C   1 
ATOM   1296 O  O   . GLN A 1 172 ? -7.966  41.542 43.752  1.00 68.50  ? 201 GLN A O   1 
ATOM   1297 C  CB  . GLN A 1 172 ? -10.949 41.994 44.015  1.00 72.86  ? 201 GLN A CB  1 
ATOM   1298 C  CG  . GLN A 1 172 ? -12.308 41.365 43.713  1.00 81.15  ? 201 GLN A CG  1 
ATOM   1299 C  CD  . GLN A 1 172 ? -13.348 42.347 43.193  1.00 90.19  ? 201 GLN A CD  1 
ATOM   1300 O  OE1 . GLN A 1 172 ? -13.040 43.444 42.677  1.00 93.10  ? 201 GLN A OE1 1 
ATOM   1301 N  NE2 . GLN A 1 172 ? -14.617 41.959 43.314  1.00 91.29  ? 201 GLN A NE2 1 
ATOM   1302 N  N   . LEU A 1 173 ? -8.130  43.706 43.149  1.00 67.58  ? 202 LEU A N   1 
ATOM   1303 C  CA  . LEU A 1 173 ? -6.801  44.047 43.634  1.00 67.33  ? 202 LEU A CA  1 
ATOM   1304 C  C   . LEU A 1 173 ? -6.853  44.519 45.103  1.00 67.99  ? 202 LEU A C   1 
ATOM   1305 O  O   . LEU A 1 173 ? -6.395  45.615 45.445  1.00 68.21  ? 202 LEU A O   1 
ATOM   1306 C  CB  . LEU A 1 173 ? -6.096  45.064 42.726  1.00 66.81  ? 202 LEU A CB  1 
ATOM   1307 C  CG  . LEU A 1 173 ? -4.589  45.242 42.965  1.00 67.39  ? 202 LEU A CG  1 
ATOM   1308 C  CD1 . LEU A 1 173 ? -3.839  43.929 42.850  1.00 67.61  ? 202 LEU A CD1 1 
ATOM   1309 C  CD2 . LEU A 1 173 ? -4.010  46.281 42.038  1.00 67.76  ? 202 LEU A CD2 1 
ATOM   1310 N  N   . ASP A 1 174 ? -7.420  43.677 45.976  1.00 68.03  ? 203 ASP A N   1 
ATOM   1311 C  CA  . ASP A 1 174 ? -7.483  43.975 47.398  1.00 68.74  ? 203 ASP A CA  1 
ATOM   1312 C  C   . ASP A 1 174 ? -6.099  43.735 48.074  1.00 69.78  ? 203 ASP A C   1 
ATOM   1313 O  O   . ASP A 1 174 ? -5.158  43.324 47.389  1.00 69.95  ? 203 ASP A O   1 
ATOM   1314 C  CB  . ASP A 1 174 ? -8.630  43.184 48.054  1.00 69.94  ? 203 ASP A CB  1 
ATOM   1315 C  CG  . ASP A 1 174 ? -8.602  41.690 47.824  1.00 73.36  ? 203 ASP A CG  1 
ATOM   1316 O  OD1 . ASP A 1 174 ? -7.586  41.190 47.320  1.00 73.47  ? 203 ASP A OD1 1 
ATOM   1317 O  OD2 . ASP A 1 174 ? -9.601  41.019 48.162  1.00 75.39  ? 203 ASP A OD2 1 
ATOM   1318 N  N   . ILE A 1 175 ? -5.952  44.014 49.388  1.00 70.17  ? 204 ILE A N   1 
ATOM   1319 C  CA  . ILE A 1 175 ? -4.652  43.838 50.053  1.00 70.91  ? 204 ILE A CA  1 
ATOM   1320 C  C   . ILE A 1 175 ? -4.153  42.384 50.048  1.00 70.67  ? 204 ILE A C   1 
ATOM   1321 O  O   . ILE A 1 175 ? -2.939  42.180 50.017  1.00 70.84  ? 204 ILE A O   1 
ATOM   1322 C  CB  . ILE A 1 175 ? -4.588  44.435 51.473  1.00 72.01  ? 204 ILE A CB  1 
ATOM   1323 C  CG1 . ILE A 1 175 ? -5.854  44.117 52.274  1.00 73.52  ? 204 ILE A CG1 1 
ATOM   1324 C  CG2 . ILE A 1 175 ? -4.301  45.927 51.425  1.00 72.56  ? 204 ILE A CG2 1 
ATOM   1325 C  CD1 . ILE A 1 175 ? -5.700  44.321 53.715  1.00 75.17  ? 204 ILE A CD1 1 
ATOM   1326 N  N   . ILE A 1 176 ? -5.061  41.384 50.063  1.00 69.95  ? 205 ILE A N   1 
ATOM   1327 C  CA  . ILE A 1 176 ? -4.637  39.981 50.042  1.00 69.85  ? 205 ILE A CA  1 
ATOM   1328 C  C   . ILE A 1 176 ? -4.044  39.617 48.690  1.00 69.78  ? 205 ILE A C   1 
ATOM   1329 O  O   . ILE A 1 176 ? -2.913  39.144 48.641  1.00 70.04  ? 205 ILE A O   1 
ATOM   1330 C  CB  . ILE A 1 176 ? -5.733  38.967 50.454  1.00 70.52  ? 205 ILE A CB  1 
ATOM   1331 C  CG1 . ILE A 1 176 ? -6.637  39.493 51.577  1.00 72.16  ? 205 ILE A CG1 1 
ATOM   1332 C  CG2 . ILE A 1 176 ? -5.127  37.617 50.803  1.00 70.80  ? 205 ILE A CG2 1 
ATOM   1333 C  CD1 . ILE A 1 176 ? -8.000  40.025 51.072  1.00 73.91  ? 205 ILE A CD1 1 
ATOM   1334 N  N   . THR A 1 177 ? -4.778  39.866 47.589  1.00 69.36  ? 206 THR A N   1 
ATOM   1335 C  CA  . THR A 1 177 ? -4.259  39.559 46.259  1.00 69.27  ? 206 THR A CA  1 
ATOM   1336 C  C   . THR A 1 177 ? -3.050  40.426 45.914  1.00 68.80  ? 206 THR A C   1 
ATOM   1337 O  O   . THR A 1 177 ? -2.201  39.971 45.169  1.00 68.95  ? 206 THR A O   1 
ATOM   1338 C  CB  . THR A 1 177 ? -5.350  39.596 45.188  1.00 70.57  ? 206 THR A CB  1 
ATOM   1339 O  OG1 . THR A 1 177 ? -5.704  40.947 44.943  1.00 71.84  ? 206 THR A OG1 1 
ATOM   1340 C  CG2 . THR A 1 177 ? -6.580  38.785 45.566  1.00 70.76  ? 206 THR A CG2 1 
ATOM   1341 N  N   . ALA A 1 178 ? -2.934  41.638 46.477  1.00 68.42  ? 207 ALA A N   1 
ATOM   1342 C  CA  . ALA A 1 178 ? -1.757  42.478 46.232  1.00 68.87  ? 207 ALA A CA  1 
ATOM   1343 C  C   . ALA A 1 178 ? -0.506  41.948 46.953  1.00 69.61  ? 207 ALA A C   1 
ATOM   1344 O  O   . ALA A 1 178 ? 0.611   42.237 46.532  1.00 69.75  ? 207 ALA A O   1 
ATOM   1345 C  CB  . ALA A 1 178 ? -2.029  43.911 46.651  1.00 68.79  ? 207 ALA A CB  1 
ATOM   1346 N  N   . ALA A 1 179 ? -0.689  41.189 48.045  1.00 69.84  ? 208 ALA A N   1 
ATOM   1347 C  CA  . ALA A 1 179 ? 0.418   40.656 48.819  1.00 70.22  ? 208 ALA A CA  1 
ATOM   1348 C  C   . ALA A 1 179 ? 0.777   39.212 48.465  1.00 70.24  ? 208 ALA A C   1 
ATOM   1349 O  O   . ALA A 1 179 ? 1.952   38.951 48.224  1.00 70.59  ? 208 ALA A O   1 
ATOM   1350 C  CB  . ALA A 1 179 ? 0.139   40.799 50.306  1.00 70.51  ? 208 ALA A CB  1 
ATOM   1351 N  N   . VAL A 1 180 ? -0.188  38.272 48.454  1.00 69.78  ? 209 VAL A N   1 
ATOM   1352 C  CA  . VAL A 1 180 ? 0.133   36.882 48.102  1.00 70.13  ? 209 VAL A CA  1 
ATOM   1353 C  C   . VAL A 1 180 ? 0.079   36.661 46.583  1.00 70.26  ? 209 VAL A C   1 
ATOM   1354 O  O   . VAL A 1 180 ? 0.883   35.904 46.030  1.00 70.51  ? 209 VAL A O   1 
ATOM   1355 C  CB  . VAL A 1 180 ? -0.665  35.801 48.879  1.00 70.75  ? 209 VAL A CB  1 
ATOM   1356 C  CG1 . VAL A 1 180 ? -0.409  35.904 50.375  1.00 71.48  ? 209 VAL A CG1 1 
ATOM   1357 C  CG2 . VAL A 1 180 ? -2.153  35.872 48.582  1.00 71.09  ? 209 VAL A CG2 1 
ATOM   1358 N  N   . GLY A 1 181 ? -0.843  37.348 45.926  1.00 69.61  ? 210 GLY A N   1 
ATOM   1359 C  CA  . GLY A 1 181 ? -1.016  37.243 44.489  1.00 69.43  ? 210 GLY A CA  1 
ATOM   1360 C  C   . GLY A 1 181 ? -2.403  36.784 44.105  1.00 68.87  ? 210 GLY A C   1 
ATOM   1361 O  O   . GLY A 1 181 ? -3.243  36.504 44.970  1.00 68.99  ? 210 GLY A O   1 
ATOM   1362 N  N   . TRP A 1 182 ? -2.656  36.728 42.794  1.00 67.82  ? 211 TRP A N   1 
ATOM   1363 C  CA  . TRP A 1 182 ? -3.926  36.267 42.276  1.00 66.97  ? 211 TRP A CA  1 
ATOM   1364 C  C   . TRP A 1 182 ? -3.751  34.834 41.871  1.00 67.22  ? 211 TRP A C   1 
ATOM   1365 O  O   . TRP A 1 182 ? -2.888  34.507 41.060  1.00 67.61  ? 211 TRP A O   1 
ATOM   1366 C  CB  . TRP A 1 182 ? -4.386  37.087 41.071  1.00 66.00  ? 211 TRP A CB  1 
ATOM   1367 C  CG  . TRP A 1 182 ? -5.797  36.793 40.660  1.00 65.76  ? 211 TRP A CG  1 
ATOM   1368 C  CD1 . TRP A 1 182 ? -6.937  37.171 41.308  1.00 66.49  ? 211 TRP A CD1 1 
ATOM   1369 C  CD2 . TRP A 1 182 ? -6.217  36.079 39.491  1.00 65.66  ? 211 TRP A CD2 1 
ATOM   1370 N  NE1 . TRP A 1 182 ? -8.042  36.751 40.605  1.00 66.63  ? 211 TRP A NE1 1 
ATOM   1371 C  CE2 . TRP A 1 182 ? -7.628  36.074 39.487  1.00 66.27  ? 211 TRP A CE2 1 
ATOM   1372 C  CE3 . TRP A 1 182 ? -5.536  35.444 38.440  1.00 66.05  ? 211 TRP A CE3 1 
ATOM   1373 C  CZ2 . TRP A 1 182 ? -8.366  35.449 38.485  1.00 66.60  ? 211 TRP A CZ2 1 
ATOM   1374 C  CZ3 . TRP A 1 182 ? -6.270  34.810 37.459  1.00 66.50  ? 211 TRP A CZ3 1 
ATOM   1375 C  CH2 . TRP A 1 182 ? -7.666  34.838 37.474  1.00 66.63  ? 211 TRP A CH2 1 
ATOM   1376 N  N   . PHE A 1 183 ? -4.551  33.974 42.466  1.00 66.86  ? 212 PHE A N   1 
ATOM   1377 C  CA  . PHE A 1 183 ? -4.563  32.556 42.159  1.00 66.75  ? 212 PHE A CA  1 
ATOM   1378 C  C   . PHE A 1 183 ? -6.026  32.059 42.054  1.00 66.49  ? 212 PHE A C   1 
ATOM   1379 O  O   . PHE A 1 183 ? -6.962  32.798 42.386  1.00 66.78  ? 212 PHE A O   1 
ATOM   1380 C  CB  . PHE A 1 183 ? -3.742  31.777 43.184  1.00 66.60  ? 212 PHE A CB  1 
ATOM   1381 C  CG  . PHE A 1 183 ? -4.155  32.016 44.610  1.00 67.46  ? 212 PHE A CG  1 
ATOM   1382 C  CD1 . PHE A 1 183 ? -5.174  31.278 45.186  1.00 68.34  ? 212 PHE A CD1 1 
ATOM   1383 C  CD2 . PHE A 1 183 ? -3.513  32.961 45.384  1.00 68.33  ? 212 PHE A CD2 1 
ATOM   1384 C  CE1 . PHE A 1 183 ? -5.554  31.498 46.499  1.00 68.86  ? 212 PHE A CE1 1 
ATOM   1385 C  CE2 . PHE A 1 183 ? -3.888  33.169 46.703  1.00 68.95  ? 212 PHE A CE2 1 
ATOM   1386 C  CZ  . PHE A 1 183 ? -4.910  32.443 47.247  1.00 68.67  ? 212 PHE A CZ  1 
ATOM   1387 N  N   . GLY A 1 184 ? -6.216  30.841 41.564  1.00 65.65  ? 213 GLY A N   1 
ATOM   1388 C  CA  . GLY A 1 184 ? -7.552  30.298 41.392  1.00 65.32  ? 213 GLY A CA  1 
ATOM   1389 C  C   . GLY A 1 184 ? -7.666  28.826 41.675  1.00 64.92  ? 213 GLY A C   1 
ATOM   1390 O  O   . GLY A 1 184 ? -6.663  28.133 41.867  1.00 64.89  ? 213 GLY A O   1 
ATOM   1391 N  N   . ASP A 1 185 ? -8.908  28.354 41.718  1.00 64.51  ? 214 ASP A N   1 
ATOM   1392 C  CA  . ASP A 1 185 ? -9.240  26.945 41.937  1.00 64.66  ? 214 ASP A CA  1 
ATOM   1393 C  C   . ASP A 1 185 ? -9.415  26.178 40.604  1.00 63.52  ? 214 ASP A C   1 
ATOM   1394 O  O   . ASP A 1 185 ? -9.962  25.075 40.607  1.00 64.00  ? 214 ASP A O   1 
ATOM   1395 C  CB  . ASP A 1 185 ? -10.538 26.845 42.761  1.00 67.66  ? 214 ASP A CB  1 
ATOM   1396 C  CG  . ASP A 1 185 ? -11.769 27.401 42.051  1.00 74.86  ? 214 ASP A CG  1 
ATOM   1397 O  OD1 . ASP A 1 185 ? -11.684 28.536 41.496  1.00 75.99  ? 214 ASP A OD1 1 
ATOM   1398 O  OD2 . ASP A 1 185 ? -12.820 26.706 42.046  1.00 77.82  ? 214 ASP A OD2 1 
ATOM   1399 N  N   . MET A 1 186 ? -8.983  26.767 39.471  1.00 61.81  ? 215 MET A N   1 
ATOM   1400 C  CA  . MET A 1 186 ? -9.123  26.175 38.152  1.00 60.64  ? 215 MET A CA  1 
ATOM   1401 C  C   . MET A 1 186 ? -7.808  26.232 37.387  1.00 59.94  ? 215 MET A C   1 
ATOM   1402 O  O   . MET A 1 186 ? -7.276  27.317 37.170  1.00 60.00  ? 215 MET A O   1 
ATOM   1403 C  CB  . MET A 1 186 ? -10.207 26.918 37.373  1.00 60.58  ? 215 MET A CB  1 
ATOM   1404 C  CG  . MET A 1 186 ? -10.322 26.481 35.946  1.00 61.75  ? 215 MET A CG  1 
ATOM   1405 S  SD  . MET A 1 186 ? -11.545 27.441 35.081  1.00 63.73  ? 215 MET A SD  1 
ATOM   1406 C  CE  . MET A 1 186 ? -13.002 26.808 35.851  1.00 65.42  ? 215 MET A CE  1 
ATOM   1407 N  N   . MET A 1 187 ? -7.312  25.072 36.931  1.00 58.98  ? 216 MET A N   1 
ATOM   1408 C  CA  . MET A 1 187 ? -6.084  25.027 36.162  1.00 58.53  ? 216 MET A CA  1 
ATOM   1409 C  C   . MET A 1 187 ? -6.364  24.972 34.668  1.00 58.57  ? 216 MET A C   1 
ATOM   1410 O  O   . MET A 1 187 ? -7.179  24.167 34.204  1.00 58.84  ? 216 MET A O   1 
ATOM   1411 C  CB  . MET A 1 187 ? -5.218  23.843 36.580  1.00 58.91  ? 216 MET A CB  1 
ATOM   1412 C  CG  . MET A 1 187 ? -3.831  23.890 35.991  1.00 60.83  ? 216 MET A CG  1 
ATOM   1413 S  SD  . MET A 1 187 ? -2.901  25.351 36.511  1.00 63.14  ? 216 MET A SD  1 
ATOM   1414 C  CE  . MET A 1 187 ? -1.529  25.179 35.534  1.00 60.38  ? 216 MET A CE  1 
ATOM   1415 N  N   . LEU A 1 188 ? -5.689  25.837 33.907  1.00 58.03  ? 217 LEU A N   1 
ATOM   1416 C  CA  . LEU A 1 188 ? -5.860  25.878 32.468  1.00 57.91  ? 217 LEU A CA  1 
ATOM   1417 C  C   . LEU A 1 188 ? -4.571  25.534 31.741  1.00 58.14  ? 217 LEU A C   1 
ATOM   1418 O  O   . LEU A 1 188 ? -3.477  25.878 32.202  1.00 58.48  ? 217 LEU A O   1 
ATOM   1419 C  CB  . LEU A 1 188 ? -6.369  27.240 32.023  1.00 57.66  ? 217 LEU A CB  1 
ATOM   1420 C  CG  . LEU A 1 188 ? -7.738  27.620 32.535  1.00 58.64  ? 217 LEU A CG  1 
ATOM   1421 C  CD1 . LEU A 1 188 ? -8.056  29.043 32.173  1.00 58.98  ? 217 LEU A CD1 1 
ATOM   1422 C  CD2 . LEU A 1 188 ? -8.813  26.687 31.994  1.00 59.09  ? 217 LEU A CD2 1 
ATOM   1423 N  N   . THR A 1 189 ? -4.714  24.818 30.617  1.00 57.39  ? 218 THR A N   1 
ATOM   1424 C  CA  . THR A 1 189 ? -3.635  24.397 29.734  1.00 57.01  ? 218 THR A CA  1 
ATOM   1425 C  C   . THR A 1 189 ? -4.116  24.857 28.381  1.00 57.44  ? 218 THR A C   1 
ATOM   1426 O  O   . THR A 1 189 ? -5.055  24.269 27.844  1.00 58.22  ? 218 THR A O   1 
ATOM   1427 C  CB  . THR A 1 189 ? -3.484  22.886 29.773  1.00 57.44  ? 218 THR A CB  1 
ATOM   1428 O  OG1 . THR A 1 189 ? -3.357  22.459 31.126  1.00 58.32  ? 218 THR A OG1 1 
ATOM   1429 C  CG2 . THR A 1 189 ? -2.311  22.406 28.955  1.00 57.63  ? 218 THR A CG2 1 
ATOM   1430 N  N   . ASN A 1 190 ? -3.575  25.979 27.891  1.00 56.78  ? 219 ASN A N   1 
ATOM   1431 C  CA  . ASN A 1 190 ? -4.020  26.618 26.661  1.00 56.64  ? 219 ASN A CA  1 
ATOM   1432 C  C   . ASN A 1 190 ? -5.511  27.034 26.753  1.00 57.20  ? 219 ASN A C   1 
ATOM   1433 O  O   . ASN A 1 190 ? -6.221  27.011 25.752  1.00 57.19  ? 219 ASN A O   1 
ATOM   1434 C  CB  . ASN A 1 190 ? -3.690  25.772 25.424  1.00 56.92  ? 219 ASN A CB  1 
ATOM   1435 C  CG  . ASN A 1 190 ? -2.193  25.661 25.154  1.00 59.48  ? 219 ASN A CG  1 
ATOM   1436 O  OD1 . ASN A 1 190 ? -1.365  26.126 25.936  1.00 60.69  ? 219 ASN A OD1 1 
ATOM   1437 N  ND2 . ASN A 1 190 ? -1.791  25.052 24.040  1.00 59.25  ? 219 ASN A ND2 1 
ATOM   1438 N  N   . GLY A 1 191 ? -5.941  27.447 27.954  1.00 57.40  ? 220 GLY A N   1 
ATOM   1439 C  CA  . GLY A 1 191 ? -7.309  27.857 28.254  1.00 58.27  ? 220 GLY A CA  1 
ATOM   1440 C  C   . GLY A 1 191 ? -8.288  26.697 28.344  1.00 59.40  ? 220 GLY A C   1 
ATOM   1441 O  O   . GLY A 1 191 ? -9.483  26.857 28.095  1.00 59.08  ? 220 GLY A O   1 
ATOM   1442 N  N   . THR A 1 192 ? -7.788  25.510 28.692  1.00 60.46  ? 221 THR A N   1 
ATOM   1443 C  CA  . THR A 1 192 ? -8.602  24.307 28.717  1.00 61.71  ? 221 THR A CA  1 
ATOM   1444 C  C   . THR A 1 192 ? -8.360  23.531 29.971  1.00 62.58  ? 221 THR A C   1 
ATOM   1445 O  O   . THR A 1 192 ? -7.209  23.371 30.373  1.00 63.17  ? 221 THR A O   1 
ATOM   1446 C  CB  . THR A 1 192 ? -8.218  23.439 27.528  1.00 63.50  ? 221 THR A CB  1 
ATOM   1447 O  OG1 . THR A 1 192 ? -8.453  24.169 26.334  1.00 64.87  ? 221 THR A OG1 1 
ATOM   1448 C  CG2 . THR A 1 192 ? -9.010  22.192 27.466  1.00 64.26  ? 221 THR A CG2 1 
ATOM   1449 N  N   . VAL A 1 193 ? -9.426  23.019 30.581  1.00 62.76  ? 222 VAL A N   1 
ATOM   1450 C  CA  . VAL A 1 193 ? -9.272  22.241 31.798  1.00 63.76  ? 222 VAL A CA  1 
ATOM   1451 C  C   . VAL A 1 193 ? -8.846  20.812 31.502  1.00 64.51  ? 222 VAL A C   1 
ATOM   1452 O  O   . VAL A 1 193 ? -9.653  20.019 31.015  1.00 64.78  ? 222 VAL A O   1 
ATOM   1453 C  CB  . VAL A 1 193 ? -10.513 22.314 32.696  1.00 64.46  ? 222 VAL A CB  1 
ATOM   1454 C  CG1 . VAL A 1 193 ? -10.315 21.459 33.941  1.00 64.94  ? 222 VAL A CG1 1 
ATOM   1455 C  CG2 . VAL A 1 193 ? -10.820 23.762 33.067  1.00 64.95  ? 222 VAL A CG2 1 
ATOM   1456 N  N   . TYR A 1 194 ? -7.562  20.503 31.774  1.00 64.64  ? 223 TYR A N   1 
ATOM   1457 C  CA  . TYR A 1 194 ? -6.955  19.179 31.587  1.00 65.04  ? 223 TYR A CA  1 
ATOM   1458 C  C   . TYR A 1 194 ? -7.234  18.585 30.202  1.00 64.37  ? 223 TYR A C   1 
ATOM   1459 O  O   . TYR A 1 194 ? -7.982  17.614 30.072  1.00 64.38  ? 223 TYR A O   1 
ATOM   1460 C  CB  . TYR A 1 194 ? -7.418  18.256 32.728  1.00 65.70  ? 223 TYR A CB  1 
ATOM   1461 C  CG  . TYR A 1 194 ? -6.834  16.857 32.790  1.00 67.31  ? 223 TYR A CG  1 
ATOM   1462 C  CD1 . TYR A 1 194 ? -5.629  16.550 32.167  1.00 68.54  ? 223 TYR A CD1 1 
ATOM   1463 C  CD2 . TYR A 1 194 ? -7.446  15.863 33.541  1.00 68.32  ? 223 TYR A CD2 1 
ATOM   1464 C  CE1 . TYR A 1 194 ? -5.095  15.269 32.225  1.00 69.55  ? 223 TYR A CE1 1 
ATOM   1465 C  CE2 . TYR A 1 194 ? -6.913  14.587 33.622  1.00 69.30  ? 223 TYR A CE2 1 
ATOM   1466 C  CZ  . TYR A 1 194 ? -5.740  14.291 32.962  1.00 70.58  ? 223 TYR A CZ  1 
ATOM   1467 O  OH  . TYR A 1 194 ? -5.229  13.021 33.067  1.00 72.63  ? 223 TYR A OH  1 
ATOM   1468 N  N   . PRO A 1 195 ? -6.638  19.161 29.151  1.00 63.74  ? 224 PRO A N   1 
ATOM   1469 C  CA  . PRO A 1 195 ? -6.879  18.632 27.801  1.00 63.67  ? 224 PRO A CA  1 
ATOM   1470 C  C   . PRO A 1 195 ? -6.014  17.415 27.440  1.00 63.88  ? 224 PRO A C   1 
ATOM   1471 O  O   . PRO A 1 195 ? -5.134  17.024 28.206  1.00 64.14  ? 224 PRO A O   1 
ATOM   1472 C  CB  . PRO A 1 195 ? -6.561  19.830 26.907  1.00 64.28  ? 224 PRO A CB  1 
ATOM   1473 C  CG  . PRO A 1 195 ? -5.559  20.619 27.662  1.00 64.69  ? 224 PRO A CG  1 
ATOM   1474 C  CD  . PRO A 1 195 ? -5.735  20.330 29.130  1.00 63.11  ? 224 PRO A CD  1 
ATOM   1475 N  N   . GLN A 1 196 ? -6.245  16.829 26.260  1.00 63.59  ? 225 GLN A N   1 
ATOM   1476 C  CA  . GLN A 1 196 ? -5.435  15.722 25.790  1.00 63.84  ? 225 GLN A CA  1 
ATOM   1477 C  C   . GLN A 1 196 ? -4.770  16.094 24.469  1.00 63.51  ? 225 GLN A C   1 
ATOM   1478 O  O   . GLN A 1 196 ? -5.307  16.885 23.695  1.00 63.36  ? 225 GLN A O   1 
ATOM   1479 C  CB  . GLN A 1 196 ? -6.277  14.460 25.618  1.00 66.50  ? 225 GLN A CB  1 
ATOM   1480 C  CG  . GLN A 1 196 ? -5.425  13.195 25.590  1.00 72.06  ? 225 GLN A CG  1 
ATOM   1481 C  CD  . GLN A 1 196 ? -6.140  11.979 25.054  1.00 77.69  ? 225 GLN A CD  1 
ATOM   1482 O  OE1 . GLN A 1 196 ? -6.651  11.981 23.931  1.00 79.49  ? 225 GLN A OE1 1 
ATOM   1483 N  NE2 . GLN A 1 196 ? -6.167  10.905 25.841  1.00 78.43  ? 225 GLN A NE2 1 
ATOM   1484 N  N   . HIS A 1 197 ? -3.594  15.528 24.213  1.00 63.16  ? 226 HIS A N   1 
ATOM   1485 C  CA  . HIS A 1 197 ? -2.900  15.748 22.958  1.00 63.21  ? 226 HIS A CA  1 
ATOM   1486 C  C   . HIS A 1 197 ? -2.383  14.419 22.415  1.00 62.91  ? 226 HIS A C   1 
ATOM   1487 O  O   . HIS A 1 197 ? -1.852  13.609 23.166  1.00 62.80  ? 226 HIS A O   1 
ATOM   1488 C  CB  . HIS A 1 197 ? -1.773  16.790 23.089  1.00 63.78  ? 226 HIS A CB  1 
ATOM   1489 C  CG  . HIS A 1 197 ? -0.987  16.962 21.820  1.00 65.07  ? 226 HIS A CG  1 
ATOM   1490 N  ND1 . HIS A 1 197 ? -1.561  17.519 20.687  1.00 66.57  ? 226 HIS A ND1 1 
ATOM   1491 C  CD2 . HIS A 1 197 ? 0.277   16.581 21.525  1.00 65.93  ? 226 HIS A CD2 1 
ATOM   1492 C  CE1 . HIS A 1 197 ? -0.630  17.470 19.751  1.00 67.04  ? 226 HIS A CE1 1 
ATOM   1493 N  NE2 . HIS A 1 197 ? 0.493   16.910 20.204  1.00 67.13  ? 226 HIS A NE2 1 
ATOM   1494 N  N   . LEU A 1 198 ? -2.569  14.189 21.117  1.00 62.52  ? 227 LEU A N   1 
ATOM   1495 C  CA  . LEU A 1 198 ? -2.113  12.978 20.457  1.00 62.79  ? 227 LEU A CA  1 
ATOM   1496 C  C   . LEU A 1 198 ? -0.769  13.275 19.831  1.00 64.23  ? 227 LEU A C   1 
ATOM   1497 O  O   . LEU A 1 198 ? -0.668  14.176 18.996  1.00 64.89  ? 227 LEU A O   1 
ATOM   1498 C  CB  . LEU A 1 198 ? -3.112  12.573 19.363  1.00 62.11  ? 227 LEU A CB  1 
ATOM   1499 C  CG  . LEU A 1 198 ? -4.509  12.210 19.818  1.00 62.00  ? 227 LEU A CG  1 
ATOM   1500 C  CD1 . LEU A 1 198 ? -5.386  11.939 18.644  1.00 61.90  ? 227 LEU A CD1 1 
ATOM   1501 C  CD2 . LEU A 1 198 ? -4.490  11.025 20.726  1.00 62.31  ? 227 LEU A CD2 1 
ATOM   1502 N  N   . ALA A 1 199 ? 0.265   12.560 20.248  1.00 64.70  ? 228 ALA A N   1 
ATOM   1503 C  CA  . ALA A 1 199 ? 1.616   12.805 19.755  1.00 65.75  ? 228 ALA A CA  1 
ATOM   1504 C  C   . ALA A 1 199 ? 2.219   11.595 19.038  1.00 66.60  ? 228 ALA A C   1 
ATOM   1505 O  O   . ALA A 1 199 ? 1.951   10.453 19.412  1.00 67.06  ? 228 ALA A O   1 
ATOM   1506 C  CB  . ALA A 1 199 ? 2.506   13.198 20.924  1.00 66.00  ? 228 ALA A CB  1 
ATOM   1507 N  N   . PRO A 1 200 ? 3.092   11.815 18.040  1.00 66.51  ? 229 PRO A N   1 
ATOM   1508 C  CA  . PRO A 1 200 ? 3.734   10.663 17.380  1.00 66.01  ? 229 PRO A CA  1 
ATOM   1509 C  C   . PRO A 1 200 ? 4.699   9.928  18.315  1.00 65.61  ? 229 PRO A C   1 
ATOM   1510 O  O   . PRO A 1 200 ? 5.217   10.508 19.273  1.00 65.53  ? 229 PRO A O   1 
ATOM   1511 C  CB  . PRO A 1 200 ? 4.484   11.295 16.203  1.00 66.57  ? 229 PRO A CB  1 
ATOM   1512 C  CG  . PRO A 1 200 ? 4.703   12.703 16.602  1.00 67.23  ? 229 PRO A CG  1 
ATOM   1513 C  CD  . PRO A 1 200 ? 3.547   13.103 17.472  1.00 65.93  ? 229 PRO A CD  1 
ATOM   1514 N  N   . ARG A 1 201 ? 4.939   8.645  18.030  1.00 65.11  ? 230 ARG A N   1 
ATOM   1515 C  CA  . ARG A 1 201 ? 5.893   7.845  18.780  1.00 64.93  ? 230 ARG A CA  1 
ATOM   1516 C  C   . ARG A 1 201 ? 7.301   8.308  18.400  1.00 64.13  ? 230 ARG A C   1 
ATOM   1517 O  O   . ARG A 1 201 ? 7.591   8.526  17.231  1.00 63.88  ? 230 ARG A O   1 
ATOM   1518 C  CB  . ARG A 1 201 ? 5.730   6.368  18.438  1.00 66.61  ? 230 ARG A CB  1 
ATOM   1519 C  CG  . ARG A 1 201 ? 4.534   5.726  19.091  1.00 70.18  ? 230 ARG A CG  1 
ATOM   1520 C  CD  . ARG A 1 201 ? 4.179   4.446  18.369  1.00 74.37  ? 230 ARG A CD  1 
ATOM   1521 N  NE  . ARG A 1 201 ? 3.015   3.816  18.987  1.00 78.93  ? 230 ARG A NE  1 
ATOM   1522 C  CZ  . ARG A 1 201 ? 3.069   2.735  19.762  1.00 82.02  ? 230 ARG A CZ  1 
ATOM   1523 N  NH1 . ARG A 1 201 ? 4.231   2.127  19.990  1.00 82.41  ? 230 ARG A NH1 1 
ATOM   1524 N  NH2 . ARG A 1 201 ? 1.957   2.231  20.288  1.00 81.38  ? 230 ARG A NH2 1 
ATOM   1525 N  N   . GLY A 1 202 ? 8.155   8.461  19.392  1.00 63.47  ? 231 GLY A N   1 
ATOM   1526 C  CA  . GLY A 1 202 ? 9.514   8.937  19.200  1.00 63.22  ? 231 GLY A CA  1 
ATOM   1527 C  C   . GLY A 1 202 ? 9.809   9.939  20.287  1.00 62.71  ? 231 GLY A C   1 
ATOM   1528 O  O   . GLY A 1 202 ? 9.842   9.582  21.470  1.00 62.49  ? 231 GLY A O   1 
ATOM   1529 N  N   . TRP A 1 203 ? 9.952   11.215 19.903  1.00 62.11  ? 232 TRP A N   1 
ATOM   1530 C  CA  . TRP A 1 203 ? 10.144  12.275 20.886  1.00 61.88  ? 232 TRP A CA  1 
ATOM   1531 C  C   . TRP A 1 203 ? 9.030   13.315 20.783  1.00 61.19  ? 232 TRP A C   1 
ATOM   1532 O  O   . TRP A 1 203 ? 8.399   13.466 19.730  1.00 61.60  ? 232 TRP A O   1 
ATOM   1533 C  CB  . TRP A 1 203 ? 11.540  12.906 20.781  1.00 61.81  ? 232 TRP A CB  1 
ATOM   1534 C  CG  . TRP A 1 203 ? 12.628  11.979 21.222  1.00 62.41  ? 232 TRP A CG  1 
ATOM   1535 C  CD1 . TRP A 1 203 ? 13.322  11.097 20.443  1.00 63.55  ? 232 TRP A CD1 1 
ATOM   1536 C  CD2 . TRP A 1 203 ? 13.088  11.780 22.562  1.00 62.47  ? 232 TRP A CD2 1 
ATOM   1537 N  NE1 . TRP A 1 203 ? 14.199  10.372 21.215  1.00 63.78  ? 232 TRP A NE1 1 
ATOM   1538 C  CE2 . TRP A 1 203 ? 14.087  10.784 22.520  1.00 63.25  ? 232 TRP A CE2 1 
ATOM   1539 C  CE3 . TRP A 1 203 ? 12.767  12.360 23.796  1.00 63.08  ? 232 TRP A CE3 1 
ATOM   1540 C  CZ2 . TRP A 1 203 ? 14.764  10.361 23.662  1.00 63.55  ? 232 TRP A CZ2 1 
ATOM   1541 C  CZ3 . TRP A 1 203 ? 13.434  11.931 24.928  1.00 63.70  ? 232 TRP A CZ3 1 
ATOM   1542 C  CH2 . TRP A 1 203 ? 14.422  10.947 24.852  1.00 63.69  ? 232 TRP A CH2 1 
ATOM   1543 N  N   . LEU A 1 204 ? 8.757   14.000 21.888  1.00 59.84  ? 233 LEU A N   1 
ATOM   1544 C  CA  . LEU A 1 204 ? 7.731   15.030 21.905  1.00 59.18  ? 233 LEU A CA  1 
ATOM   1545 C  C   . LEU A 1 204 ? 8.308   16.264 22.594  1.00 58.48  ? 233 LEU A C   1 
ATOM   1546 O  O   . LEU A 1 204 ? 8.775   16.175 23.721  1.00 58.79  ? 233 LEU A O   1 
ATOM   1547 C  CB  . LEU A 1 204 ? 6.448   14.519 22.597  1.00 58.93  ? 233 LEU A CB  1 
ATOM   1548 C  CG  . LEU A 1 204 ? 5.389   15.572 22.930  1.00 59.25  ? 233 LEU A CG  1 
ATOM   1549 C  CD1 . LEU A 1 204 ? 4.864   16.241 21.674  1.00 59.53  ? 233 LEU A CD1 1 
ATOM   1550 C  CD2 . LEU A 1 204 ? 4.268   14.972 23.725  1.00 58.98  ? 233 LEU A CD2 1 
ATOM   1551 N  N   . ARG A 1 205 ? 8.318   17.393 21.905  1.00 57.44  ? 234 ARG A N   1 
ATOM   1552 C  CA  . ARG A 1 205 ? 8.862   18.630 22.438  1.00 57.42  ? 234 ARG A CA  1 
ATOM   1553 C  C   . ARG A 1 205 ? 7.733   19.514 22.960  1.00 57.57  ? 234 ARG A C   1 
ATOM   1554 O  O   . ARG A 1 205 ? 6.844   19.894 22.196  1.00 57.96  ? 234 ARG A O   1 
ATOM   1555 C  CB  . ARG A 1 205 ? 9.650   19.335 21.334  1.00 58.45  ? 234 ARG A CB  1 
ATOM   1556 C  CG  . ARG A 1 205 ? 10.117  20.750 21.619  1.00 60.72  ? 234 ARG A CG  1 
ATOM   1557 C  CD  . ARG A 1 205 ? 10.566  21.327 20.298  1.00 63.31  ? 234 ARG A CD  1 
ATOM   1558 N  NE  . ARG A 1 205 ? 11.595  22.360 20.411  1.00 65.60  ? 234 ARG A NE  1 
ATOM   1559 C  CZ  . ARG A 1 205 ? 12.239  22.889 19.372  1.00 67.26  ? 234 ARG A CZ  1 
ATOM   1560 N  NH1 . ARG A 1 205 ? 11.978  22.473 18.137  1.00 66.56  ? 234 ARG A NH1 1 
ATOM   1561 N  NH2 . ARG A 1 205 ? 13.148  23.834 19.560  1.00 67.36  ? 234 ARG A NH2 1 
ATOM   1562 N  N   . LEU A 1 206 ? 7.750   19.809 24.271  1.00 56.79  ? 235 LEU A N   1 
ATOM   1563 C  CA  . LEU A 1 206 ? 6.747   20.644 24.917  1.00 56.56  ? 235 LEU A CA  1 
ATOM   1564 C  C   . LEU A 1 206 ? 7.377   21.974 25.293  1.00 56.69  ? 235 LEU A C   1 
ATOM   1565 O  O   . LEU A 1 206 ? 8.372   22.014 26.024  1.00 56.90  ? 235 LEU A O   1 
ATOM   1566 C  CB  . LEU A 1 206 ? 6.204   19.965 26.183  1.00 56.42  ? 235 LEU A CB  1 
ATOM   1567 C  CG  . LEU A 1 206 ? 5.644   18.576 25.998  1.00 57.65  ? 235 LEU A CG  1 
ATOM   1568 C  CD1 . LEU A 1 206 ? 5.505   17.873 27.321  1.00 58.26  ? 235 LEU A CD1 1 
ATOM   1569 C  CD2 . LEU A 1 206 ? 4.324   18.617 25.287  1.00 58.24  ? 235 LEU A CD2 1 
ATOM   1570 N  N   . ARG A 1 207 ? 6.803   23.063 24.800  1.00 56.37  ? 236 ARG A N   1 
ATOM   1571 C  CA  . ARG A 1 207 ? 7.300   24.391 25.119  1.00 56.79  ? 236 ARG A CA  1 
ATOM   1572 C  C   . ARG A 1 207 ? 6.460   24.906 26.286  1.00 57.17  ? 236 ARG A C   1 
ATOM   1573 O  O   . ARG A 1 207 ? 5.378   25.451 26.078  1.00 57.76  ? 236 ARG A O   1 
ATOM   1574 C  CB  . ARG A 1 207 ? 7.199   25.314 23.890  1.00 57.66  ? 236 ARG A CB  1 
ATOM   1575 C  CG  . ARG A 1 207 ? 7.992   24.835 22.680  1.00 60.12  ? 236 ARG A CG  1 
ATOM   1576 C  CD  . ARG A 1 207 ? 7.715   25.775 21.534  1.00 64.46  ? 236 ARG A CD  1 
ATOM   1577 N  NE  . ARG A 1 207 ? 8.391   25.405 20.289  1.00 67.81  ? 236 ARG A NE  1 
ATOM   1578 C  CZ  . ARG A 1 207 ? 9.478   26.004 19.813  1.00 68.96  ? 236 ARG A CZ  1 
ATOM   1579 N  NH1 . ARG A 1 207 ? 10.050  26.992 20.489  1.00 68.19  ? 236 ARG A NH1 1 
ATOM   1580 N  NH2 . ARG A 1 207 ? 10.012  25.608 18.666  1.00 68.64  ? 236 ARG A NH2 1 
ATOM   1581 N  N   . PHE A 1 208 ? 6.923   24.685 27.511  1.00 56.71  ? 237 PHE A N   1 
ATOM   1582 C  CA  . PHE A 1 208 ? 6.180   25.074 28.701  1.00 57.08  ? 237 PHE A CA  1 
ATOM   1583 C  C   . PHE A 1 208 ? 6.299   26.550 29.054  1.00 56.94  ? 237 PHE A C   1 
ATOM   1584 O  O   . PHE A 1 208 ? 7.404   27.068 29.158  1.00 56.86  ? 237 PHE A O   1 
ATOM   1585 C  CB  . PHE A 1 208 ? 6.661   24.252 29.896  1.00 57.39  ? 237 PHE A CB  1 
ATOM   1586 C  CG  . PHE A 1 208 ? 6.207   22.819 29.899  1.00 58.22  ? 237 PHE A CG  1 
ATOM   1587 C  CD1 . PHE A 1 208 ? 4.866   22.503 29.997  1.00 59.21  ? 237 PHE A CD1 1 
ATOM   1588 C  CD2 . PHE A 1 208 ? 7.124   21.788 29.884  1.00 59.14  ? 237 PHE A CD2 1 
ATOM   1589 C  CE1 . PHE A 1 208 ? 4.447   21.181 30.030  1.00 59.94  ? 237 PHE A CE1 1 
ATOM   1590 C  CE2 . PHE A 1 208 ? 6.702   20.468 29.916  1.00 60.04  ? 237 PHE A CE2 1 
ATOM   1591 C  CZ  . PHE A 1 208 ? 5.368   20.172 30.006  1.00 59.79  ? 237 PHE A CZ  1 
ATOM   1592 N  N   . LEU A 1 209 ? 5.162   27.210 29.297  1.00 56.62  ? 238 LEU A N   1 
ATOM   1593 C  CA  . LEU A 1 209 ? 5.122   28.599 29.732  1.00 56.61  ? 238 LEU A CA  1 
ATOM   1594 C  C   . LEU A 1 209 ? 4.229   28.645 30.955  1.00 56.92  ? 238 LEU A C   1 
ATOM   1595 O  O   . LEU A 1 209 ? 3.072   28.252 30.861  1.00 57.40  ? 238 LEU A O   1 
ATOM   1596 C  CB  . LEU A 1 209 ? 4.553   29.526 28.641  1.00 56.57  ? 238 LEU A CB  1 
ATOM   1597 C  CG  . LEU A 1 209 ? 4.025   30.919 29.088  1.00 58.07  ? 238 LEU A CG  1 
ATOM   1598 C  CD1 . LEU A 1 209 ? 5.135   31.805 29.608  1.00 58.27  ? 238 LEU A CD1 1 
ATOM   1599 C  CD2 . LEU A 1 209 ? 3.260   31.617 27.970  1.00 58.83  ? 238 LEU A CD2 1 
ATOM   1600 N  N   . ASN A 1 210 ? 4.739   29.152 32.085  1.00 56.29  ? 239 ASN A N   1 
ATOM   1601 C  CA  . ASN A 1 210 ? 3.912   29.337 33.268  1.00 55.97  ? 239 ASN A CA  1 
ATOM   1602 C  C   . ASN A 1 210 ? 3.310   30.733 33.098  1.00 56.44  ? 239 ASN A C   1 
ATOM   1603 O  O   . ASN A 1 210 ? 3.989   31.733 33.333  1.00 56.62  ? 239 ASN A O   1 
ATOM   1604 C  CB  . ASN A 1 210 ? 4.760   29.264 34.533  1.00 56.15  ? 239 ASN A CB  1 
ATOM   1605 C  CG  . ASN A 1 210 ? 4.042   29.619 35.810  1.00 58.15  ? 239 ASN A CG  1 
ATOM   1606 O  OD1 . ASN A 1 210 ? 2.918   30.130 35.812  1.00 58.78  ? 239 ASN A OD1 1 
ATOM   1607 N  ND2 . ASN A 1 210 ? 4.688   29.364 36.938  1.00 58.44  ? 239 ASN A ND2 1 
ATOM   1608 N  N   . GLY A 1 211 ? 2.065   30.788 32.645  1.00 56.22  ? 240 GLY A N   1 
ATOM   1609 C  CA  . GLY A 1 211 ? 1.360   32.044 32.434  1.00 56.45  ? 240 GLY A CA  1 
ATOM   1610 C  C   . GLY A 1 211 ? 0.515   32.497 33.612  1.00 56.45  ? 240 GLY A C   1 
ATOM   1611 O  O   . GLY A 1 211 ? -0.363  33.349 33.444  1.00 56.76  ? 240 GLY A O   1 
ATOM   1612 N  N   . CYS A 1 212 ? 0.755   31.926 34.814  1.00 55.96  ? 241 CYS A N   1 
ATOM   1613 C  CA  . CYS A 1 212 ? 0.018   32.299 36.029  1.00 55.82  ? 241 CYS A CA  1 
ATOM   1614 C  C   . CYS A 1 212 ? 0.453   33.664 36.489  1.00 55.93  ? 241 CYS A C   1 
ATOM   1615 O  O   . CYS A 1 212 ? 1.629   33.996 36.372  1.00 56.39  ? 241 CYS A O   1 
ATOM   1616 C  CB  . CYS A 1 212 ? 0.221   31.279 37.145  1.00 56.08  ? 241 CYS A CB  1 
ATOM   1617 S  SG  . CYS A 1 212 ? -0.186  29.574 36.703  1.00 58.22  ? 241 CYS A SG  1 
ATOM   1618 N  N   . ASN A 1 213 ? -0.463  34.438 37.077  1.00 55.51  ? 242 ASN A N   1 
ATOM   1619 C  CA  . ASN A 1 213 ? -0.122  35.761 37.593  1.00 55.35  ? 242 ASN A CA  1 
ATOM   1620 C  C   . ASN A 1 213 ? 0.787   35.642 38.809  1.00 55.82  ? 242 ASN A C   1 
ATOM   1621 O  O   . ASN A 1 213 ? 1.747   36.406 38.938  1.00 56.36  ? 242 ASN A O   1 
ATOM   1622 C  CB  . ASN A 1 213 ? -1.367  36.530 37.996  1.00 55.46  ? 242 ASN A CB  1 
ATOM   1623 C  CG  . ASN A 1 213 ? -2.296  36.807 36.875  1.00 57.06  ? 242 ASN A CG  1 
ATOM   1624 O  OD1 . ASN A 1 213 ? -2.322  36.093 35.873  1.00 58.99  ? 242 ASN A OD1 1 
ATOM   1625 N  ND2 . ASN A 1 213 ? -3.090  37.842 37.032  1.00 56.71  ? 242 ASN A ND2 1 
ATOM   1626 N  N   . ALA A 1 214 ? 0.493   34.682 39.696  1.00 55.31  ? 243 ALA A N   1 
ATOM   1627 C  CA  . ALA A 1 214 ? 1.261   34.523 40.914  1.00 55.47  ? 243 ALA A CA  1 
ATOM   1628 C  C   . ALA A 1 214 ? 1.675   33.084 41.214  1.00 55.88  ? 243 ALA A C   1 
ATOM   1629 O  O   . ALA A 1 214 ? 2.605   32.875 41.993  1.00 56.34  ? 243 ALA A O   1 
ATOM   1630 C  CB  . ALA A 1 214 ? 0.453   35.059 42.071  1.00 55.15  ? 243 ALA A CB  1 
ATOM   1631 N  N   . ARG A 1 215 ? 0.965   32.098 40.663  1.00 55.23  ? 244 ARG A N   1 
ATOM   1632 C  CA  . ARG A 1 215 ? 1.236   30.699 40.974  1.00 55.03  ? 244 ARG A CA  1 
ATOM   1633 C  C   . ARG A 1 215 ? 2.496   30.119 40.357  1.00 55.11  ? 244 ARG A C   1 
ATOM   1634 O  O   . ARG A 1 215 ? 2.626   30.094 39.141  1.00 55.27  ? 244 ARG A O   1 
ATOM   1635 C  CB  . ARG A 1 215 ? 0.027   29.837 40.589  1.00 55.85  ? 244 ARG A CB  1 
ATOM   1636 C  CG  . ARG A 1 215 ? 0.211   28.334 40.807  1.00 57.28  ? 244 ARG A CG  1 
ATOM   1637 C  CD  . ARG A 1 215 ? -1.072  27.590 40.578  1.00 58.99  ? 244 ARG A CD  1 
ATOM   1638 N  NE  . ARG A 1 215 ? -2.153  28.109 41.419  1.00 61.54  ? 244 ARG A NE  1 
ATOM   1639 C  CZ  . ARG A 1 215 ? -2.393  27.711 42.662  1.00 64.72  ? 244 ARG A CZ  1 
ATOM   1640 N  NH1 . ARG A 1 215 ? -1.647  26.763 43.217  1.00 65.43  ? 244 ARG A NH1 1 
ATOM   1641 N  NH2 . ARG A 1 215 ? -3.403  28.231 43.350  1.00 64.83  ? 244 ARG A NH2 1 
ATOM   1642 N  N   . SER A 1 216 ? 3.383   29.570 41.188  1.00 55.17  ? 245 SER A N   1 
ATOM   1643 C  CA  . SER A 1 216 ? 4.552   28.849 40.680  1.00 55.88  ? 245 SER A CA  1 
ATOM   1644 C  C   . SER A 1 216 ? 4.152   27.368 40.502  1.00 56.33  ? 245 SER A C   1 
ATOM   1645 O  O   . SER A 1 216 ? 3.238   26.888 41.185  1.00 56.91  ? 245 SER A O   1 
ATOM   1646 C  CB  . SER A 1 216 ? 5.745   28.985 41.621  1.00 56.89  ? 245 SER A CB  1 
ATOM   1647 O  OG  . SER A 1 216 ? 5.532   28.306 42.844  1.00 58.59  ? 245 SER A OG  1 
ATOM   1648 N  N   . LEU A 1 217 ? 4.785   26.659 39.560  1.00 55.84  ? 246 LEU A N   1 
ATOM   1649 C  CA  . LEU A 1 217 ? 4.415   25.267 39.289  1.00 56.21  ? 246 LEU A CA  1 
ATOM   1650 C  C   . LEU A 1 217 ? 5.599   24.302 39.380  1.00 57.08  ? 246 LEU A C   1 
ATOM   1651 O  O   . LEU A 1 217 ? 6.742   24.744 39.327  1.00 57.45  ? 246 LEU A O   1 
ATOM   1652 C  CB  . LEU A 1 217 ? 3.753   25.190 37.900  1.00 55.94  ? 246 LEU A CB  1 
ATOM   1653 C  CG  . LEU A 1 217 ? 2.522   26.083 37.711  1.00 55.93  ? 246 LEU A CG  1 
ATOM   1654 C  CD1 . LEU A 1 217 ? 2.215   26.323 36.250  1.00 55.65  ? 246 LEU A CD1 1 
ATOM   1655 C  CD2 . LEU A 1 217 ? 1.343   25.531 38.454  1.00 56.36  ? 246 LEU A CD2 1 
ATOM   1656 N  N   . ASN A 1 218 ? 5.340   22.990 39.534  1.00 57.29  ? 247 ASN A N   1 
ATOM   1657 C  CA  . ASN A 1 218 ? 6.430   22.003 39.593  1.00 58.17  ? 247 ASN A CA  1 
ATOM   1658 C  C   . ASN A 1 218 ? 6.082   20.821 38.716  1.00 58.71  ? 247 ASN A C   1 
ATOM   1659 O  O   . ASN A 1 218 ? 5.438   19.878 39.159  1.00 58.68  ? 247 ASN A O   1 
ATOM   1660 C  CB  . ASN A 1 218 ? 6.719   21.534 41.019  1.00 59.26  ? 247 ASN A CB  1 
ATOM   1661 C  CG  . ASN A 1 218 ? 8.058   20.839 41.143  1.00 62.48  ? 247 ASN A CG  1 
ATOM   1662 O  OD1 . ASN A 1 218 ? 8.921   20.917 40.257  1.00 63.98  ? 247 ASN A OD1 1 
ATOM   1663 N  ND2 . ASN A 1 218 ? 8.267   20.151 42.248  1.00 62.86  ? 247 ASN A ND2 1 
ATOM   1664 N  N   . LEU A 1 219 ? 6.502   20.874 37.468  1.00 58.95  ? 248 LEU A N   1 
ATOM   1665 C  CA  . LEU A 1 219 ? 6.135   19.869 36.478  1.00 59.30  ? 248 LEU A CA  1 
ATOM   1666 C  C   . LEU A 1 219 ? 6.865   18.555 36.621  1.00 60.19  ? 248 LEU A C   1 
ATOM   1667 O  O   . LEU A 1 219 ? 8.024   18.510 36.990  1.00 60.81  ? 248 LEU A O   1 
ATOM   1668 C  CB  . LEU A 1 219 ? 6.286   20.420 35.054  1.00 59.03  ? 248 LEU A CB  1 
ATOM   1669 C  CG  . LEU A 1 219 ? 5.740   21.833 34.851  1.00 60.37  ? 248 LEU A CG  1 
ATOM   1670 C  CD1 . LEU A 1 219 ? 6.052   22.332 33.474  1.00 61.35  ? 248 LEU A CD1 1 
ATOM   1671 C  CD2 . LEU A 1 219 ? 4.253   21.914 35.155  1.00 60.56  ? 248 LEU A CD2 1 
ATOM   1672 N  N   . ALA A 1 220 ? 6.167   17.476 36.341  1.00 60.14  ? 249 ALA A N   1 
ATOM   1673 C  CA  . ALA A 1 220 ? 6.690   16.117 36.419  1.00 60.58  ? 249 ALA A CA  1 
ATOM   1674 C  C   . ALA A 1 220 ? 5.767   15.210 35.561  1.00 61.37  ? 249 ALA A C   1 
ATOM   1675 O  O   . ALA A 1 220 ? 4.747   15.677 35.055  1.00 61.46  ? 249 ALA A O   1 
ATOM   1676 C  CB  . ALA A 1 220 ? 6.701   15.657 37.886  1.00 60.44  ? 249 ALA A CB  1 
ATOM   1677 N  N   . THR A 1 221 ? 6.142   13.945 35.342  1.00 61.67  ? 250 THR A N   1 
ATOM   1678 C  CA  . THR A 1 221 ? 5.283   13.004 34.638  1.00 61.99  ? 250 THR A CA  1 
ATOM   1679 C  C   . THR A 1 221 ? 4.558   12.122 35.681  1.00 61.43  ? 250 THR A C   1 
ATOM   1680 O  O   . THR A 1 221 ? 5.055   11.908 36.791  1.00 60.78  ? 250 THR A O   1 
ATOM   1681 C  CB  . THR A 1 221 ? 6.087   12.194 33.628  1.00 63.91  ? 250 THR A CB  1 
ATOM   1682 O  OG1 . THR A 1 221 ? 7.170   11.599 34.325  1.00 65.35  ? 250 THR A OG1 1 
ATOM   1683 C  CG2 . THR A 1 221 ? 6.622   13.049 32.498  1.00 64.32  ? 250 THR A CG2 1 
ATOM   1684 N  N   . SER A 1 222 ? 3.377   11.636 35.324  1.00 61.36  ? 251 SER A N   1 
ATOM   1685 C  CA  . SER A 1 222 ? 2.582   10.799 36.208  1.00 62.07  ? 251 SER A CA  1 
ATOM   1686 C  C   . SER A 1 222 ? 3.248   9.445  36.457  1.00 62.63  ? 251 SER A C   1 
ATOM   1687 O  O   . SER A 1 222 ? 3.198   8.939  37.578  1.00 62.82  ? 251 SER A O   1 
ATOM   1688 C  CB  . SER A 1 222 ? 1.189   10.599 35.624  1.00 63.26  ? 251 SER A CB  1 
ATOM   1689 O  OG  . SER A 1 222 ? 1.290   10.121 34.294  1.00 65.44  ? 251 SER A OG  1 
ATOM   1690 N  N   . ASP A 1 223 ? 3.894   8.869  35.427  1.00 62.66  ? 252 ASP A N   1 
ATOM   1691 C  CA  . ASP A 1 223 ? 4.552   7.574  35.567  1.00 62.99  ? 252 ASP A CA  1 
ATOM   1692 C  C   . ASP A 1 223 ? 6.061   7.648  35.780  1.00 63.62  ? 252 ASP A C   1 
ATOM   1693 O  O   . ASP A 1 223 ? 6.777   6.714  35.413  1.00 63.78  ? 252 ASP A O   1 
ATOM   1694 C  CB  . ASP A 1 223 ? 4.219   6.644  34.399  1.00 64.49  ? 252 ASP A CB  1 
ATOM   1695 C  CG  . ASP A 1 223 ? 4.677   7.101  33.029  1.00 69.24  ? 252 ASP A CG  1 
ATOM   1696 O  OD1 . ASP A 1 223 ? 5.671   7.864  32.955  1.00 70.18  ? 252 ASP A OD1 1 
ATOM   1697 O  OD2 . ASP A 1 223 ? 4.051   6.681  32.026  1.00 71.04  ? 252 ASP A OD2 1 
ATOM   1698 N  N   . GLY A 1 224 ? 6.528   8.757  36.346  1.00 63.80  ? 253 GLY A N   1 
ATOM   1699 C  CA  . GLY A 1 224 ? 7.933   8.968  36.682  1.00 64.08  ? 253 GLY A CA  1 
ATOM   1700 C  C   . GLY A 1 224 ? 8.934   9.102  35.555  1.00 64.01  ? 253 GLY A C   1 
ATOM   1701 O  O   . GLY A 1 224 ? 10.116  9.329  35.826  1.00 63.82  ? 253 GLY A O   1 
ATOM   1702 N  N   . ARG A 1 225 ? 8.489   9.001  34.287  1.00 64.18  ? 254 ARG A N   1 
ATOM   1703 C  CA  . ARG A 1 225 ? 9.406   9.137  33.153  1.00 64.92  ? 254 ARG A CA  1 
ATOM   1704 C  C   . ARG A 1 225 ? 10.122  10.491 33.145  1.00 66.36  ? 254 ARG A C   1 
ATOM   1705 O  O   . ARG A 1 225 ? 9.625   11.478 33.706  1.00 66.83  ? 254 ARG A O   1 
ATOM   1706 C  CB  . ARG A 1 225 ? 8.716   8.830  31.819  1.00 65.36  ? 254 ARG A CB  1 
ATOM   1707 C  CG  . ARG A 1 225 ? 7.916   9.950  31.216  1.00 67.09  ? 254 ARG A CG  1 
ATOM   1708 C  CD  . ARG A 1 225 ? 7.343   9.500  29.892  1.00 69.37  ? 254 ARG A CD  1 
ATOM   1709 N  NE  . ARG A 1 225 ? 6.350   8.438  30.065  1.00 72.41  ? 254 ARG A NE  1 
ATOM   1710 C  CZ  . ARG A 1 225 ? 6.054   7.530  29.139  1.00 75.98  ? 254 ARG A CZ  1 
ATOM   1711 N  NH1 . ARG A 1 225 ? 6.677   7.540  27.964  1.00 76.10  ? 254 ARG A NH1 1 
ATOM   1712 N  NH2 . ARG A 1 225 ? 5.124   6.611  29.375  1.00 76.33  ? 254 ARG A NH2 1 
ATOM   1713 N  N   . PRO A 1 226 ? 11.344  10.536 32.606  1.00 66.86  ? 255 PRO A N   1 
ATOM   1714 C  CA  . PRO A 1 226 ? 12.107  11.790 32.655  1.00 66.89  ? 255 PRO A CA  1 
ATOM   1715 C  C   . PRO A 1 226 ? 11.597  12.895 31.741  1.00 66.41  ? 255 PRO A C   1 
ATOM   1716 O  O   . PRO A 1 226 ? 10.979  12.645 30.717  1.00 66.60  ? 255 PRO A O   1 
ATOM   1717 C  CB  . PRO A 1 226 ? 13.532  11.364 32.256  1.00 67.87  ? 255 PRO A CB  1 
ATOM   1718 C  CG  . PRO A 1 226 ? 13.521  9.864  32.213  1.00 68.29  ? 255 PRO A CG  1 
ATOM   1719 C  CD  . PRO A 1 226 ? 12.112  9.459  31.955  1.00 66.59  ? 255 PRO A CD  1 
ATOM   1720 N  N   . LEU A 1 227 ? 11.873  14.123 32.136  1.00 65.70  ? 256 LEU A N   1 
ATOM   1721 C  CA  . LEU A 1 227 ? 11.618  15.324 31.363  1.00 65.48  ? 256 LEU A CA  1 
ATOM   1722 C  C   . LEU A 1 227 ? 13.029  15.807 31.029  1.00 66.19  ? 256 LEU A C   1 
ATOM   1723 O  O   . LEU A 1 227 ? 13.817  16.057 31.950  1.00 67.12  ? 256 LEU A O   1 
ATOM   1724 C  CB  . LEU A 1 227 ? 10.883  16.386 32.207  1.00 64.81  ? 256 LEU A CB  1 
ATOM   1725 C  CG  . LEU A 1 227 ? 9.397   16.165 32.475  1.00 64.83  ? 256 LEU A CG  1 
ATOM   1726 C  CD1 . LEU A 1 227 ? 8.812   17.335 33.186  1.00 65.16  ? 256 LEU A CD1 1 
ATOM   1727 C  CD2 . LEU A 1 227 ? 8.623   15.949 31.199  1.00 64.96  ? 256 LEU A CD2 1 
ATOM   1728 N  N   . TYR A 1 228 ? 13.393  15.833 29.744  1.00 65.46  ? 257 TYR A N   1 
ATOM   1729 C  CA  . TYR A 1 228 ? 14.746  16.235 29.366  1.00 65.34  ? 257 TYR A CA  1 
ATOM   1730 C  C   . TYR A 1 228 ? 14.722  17.679 28.948  1.00 64.53  ? 257 TYR A C   1 
ATOM   1731 O  O   . TYR A 1 228 ? 14.321  17.982 27.819  1.00 64.31  ? 257 TYR A O   1 
ATOM   1732 C  CB  . TYR A 1 228 ? 15.296  15.363 28.226  1.00 65.74  ? 257 TYR A CB  1 
ATOM   1733 C  CG  . TYR A 1 228 ? 15.363  13.885 28.532  1.00 66.99  ? 257 TYR A CG  1 
ATOM   1734 C  CD1 . TYR A 1 228 ? 14.238  13.081 28.419  1.00 68.39  ? 257 TYR A CD1 1 
ATOM   1735 C  CD2 . TYR A 1 228 ? 16.563  13.277 28.864  1.00 67.98  ? 257 TYR A CD2 1 
ATOM   1736 C  CE1 . TYR A 1 228 ? 14.293  11.720 28.680  1.00 69.49  ? 257 TYR A CE1 1 
ATOM   1737 C  CE2 . TYR A 1 228 ? 16.634  11.913 29.115  1.00 69.23  ? 257 TYR A CE2 1 
ATOM   1738 C  CZ  . TYR A 1 228 ? 15.496  11.134 29.014  1.00 70.48  ? 257 TYR A CZ  1 
ATOM   1739 O  OH  . TYR A 1 228 ? 15.542  9.782  29.251  1.00 72.43  ? 257 TYR A OH  1 
ATOM   1740 N  N   . VAL A 1 229 ? 15.132  18.577 29.850  1.00 63.92  ? 258 VAL A N   1 
ATOM   1741 C  CA  . VAL A 1 229 ? 15.139  20.000 29.523  1.00 63.94  ? 258 VAL A CA  1 
ATOM   1742 C  C   . VAL A 1 229 ? 16.152  20.295 28.418  1.00 64.15  ? 258 VAL A C   1 
ATOM   1743 O  O   . VAL A 1 229 ? 17.316  19.930 28.547  1.00 64.26  ? 258 VAL A O   1 
ATOM   1744 C  CB  . VAL A 1 229 ? 15.351  20.900 30.756  1.00 63.94  ? 258 VAL A CB  1 
ATOM   1745 C  CG1 . VAL A 1 229 ? 15.297  22.368 30.363  1.00 64.15  ? 258 VAL A CG1 1 
ATOM   1746 C  CG2 . VAL A 1 229 ? 14.315  20.596 31.824  1.00 64.37  ? 258 VAL A CG2 1 
ATOM   1747 N  N   . VAL A 1 230 ? 15.693  20.897 27.311  1.00 63.85  ? 259 VAL A N   1 
ATOM   1748 C  CA  . VAL A 1 230 ? 16.565  21.272 26.194  1.00 64.00  ? 259 VAL A CA  1 
ATOM   1749 C  C   . VAL A 1 230 ? 16.693  22.778 25.990  1.00 63.72  ? 259 VAL A C   1 
ATOM   1750 O  O   . VAL A 1 230 ? 17.570  23.205 25.255  1.00 63.91  ? 259 VAL A O   1 
ATOM   1751 C  CB  . VAL A 1 230 ? 16.191  20.593 24.861  1.00 64.89  ? 259 VAL A CB  1 
ATOM   1752 C  CG1 . VAL A 1 230 ? 16.386  19.084 24.934  1.00 65.70  ? 259 VAL A CG1 1 
ATOM   1753 C  CG2 . VAL A 1 230 ? 14.775  20.951 24.439  1.00 65.31  ? 259 VAL A CG2 1 
ATOM   1754 N  N   . GLY A 1 231 ? 15.801  23.562 26.582  1.00 62.96  ? 260 GLY A N   1 
ATOM   1755 C  CA  . GLY A 1 231 ? 15.833  25.004 26.429  1.00 62.37  ? 260 GLY A CA  1 
ATOM   1756 C  C   . GLY A 1 231 ? 15.268  25.734 27.624  1.00 61.28  ? 260 GLY A C   1 
ATOM   1757 O  O   . GLY A 1 231 ? 14.505  25.170 28.409  1.00 61.25  ? 260 GLY A O   1 
ATOM   1758 N  N   . SER A 1 232 ? 15.651  26.992 27.767  1.00 60.28  ? 261 SER A N   1 
ATOM   1759 C  CA  . SER A 1 232 ? 15.158  27.846 28.834  1.00 59.98  ? 261 SER A CA  1 
ATOM   1760 C  C   . SER A 1 232 ? 14.613  29.154 28.215  1.00 59.76  ? 261 SER A C   1 
ATOM   1761 O  O   . SER A 1 232 ? 14.498  29.243 26.984  1.00 59.86  ? 261 SER A O   1 
ATOM   1762 C  CB  . SER A 1 232 ? 16.261  28.104 29.860  1.00 60.92  ? 261 SER A CB  1 
ATOM   1763 O  OG  . SER A 1 232 ? 17.468  28.533 29.254  1.00 62.30  ? 261 SER A OG  1 
ATOM   1764 N  N   . ASP A 1 233 ? 14.253  30.159 29.059  1.00 59.07  ? 262 ASP A N   1 
ATOM   1765 C  CA  . ASP A 1 233 ? 13.708  31.456 28.653  1.00 58.42  ? 262 ASP A CA  1 
ATOM   1766 C  C   . ASP A 1 233 ? 14.282  32.041 27.392  1.00 59.12  ? 262 ASP A C   1 
ATOM   1767 O  O   . ASP A 1 233 ? 13.548  32.690 26.660  1.00 58.92  ? 262 ASP A O   1 
ATOM   1768 C  CB  . ASP A 1 233 ? 13.906  32.497 29.743  1.00 58.08  ? 262 ASP A CB  1 
ATOM   1769 C  CG  . ASP A 1 233 ? 13.326  32.163 31.080  1.00 60.40  ? 262 ASP A CG  1 
ATOM   1770 O  OD1 . ASP A 1 233 ? 12.530  31.209 31.161  1.00 60.37  ? 262 ASP A OD1 1 
ATOM   1771 O  OD2 . ASP A 1 233 ? 13.664  32.852 32.048  1.00 62.89  ? 262 ASP A OD2 1 
ATOM   1772 N  N   . GLY A 1 234 ? 15.587  31.880 27.175  1.00 59.91  ? 263 GLY A N   1 
ATOM   1773 C  CA  . GLY A 1 234 ? 16.236  32.497 26.030  1.00 61.12  ? 263 GLY A CA  1 
ATOM   1774 C  C   . GLY A 1 234 ? 17.172  31.692 25.164  1.00 62.09  ? 263 GLY A C   1 
ATOM   1775 O  O   . GLY A 1 234 ? 18.099  32.254 24.575  1.00 61.83  ? 263 GLY A O   1 
ATOM   1776 N  N   . GLY A 1 235 ? 16.867  30.417 24.987  1.00 63.08  ? 264 GLY A N   1 
ATOM   1777 C  CA  . GLY A 1 235 ? 17.652  29.578 24.098  1.00 64.33  ? 264 GLY A CA  1 
ATOM   1778 C  C   . GLY A 1 235 ? 17.857  28.181 24.611  1.00 65.71  ? 264 GLY A C   1 
ATOM   1779 O  O   . GLY A 1 235 ? 17.574  27.884 25.777  1.00 66.01  ? 264 GLY A O   1 
ATOM   1780 N  N   . LEU A 1 236 ? 18.369  27.323 23.741  1.00 66.28  ? 265 LEU A N   1 
ATOM   1781 C  CA  . LEU A 1 236 ? 18.647  25.949 24.110  1.00 67.14  ? 265 LEU A CA  1 
ATOM   1782 C  C   . LEU A 1 236 ? 19.864  25.893 25.027  1.00 68.23  ? 265 LEU A C   1 
ATOM   1783 O  O   . LEU A 1 236 ? 20.747  26.756 24.959  1.00 68.41  ? 265 LEU A O   1 
ATOM   1784 C  CB  . LEU A 1 236 ? 18.900  25.101 22.857  1.00 67.41  ? 265 LEU A CB  1 
ATOM   1785 C  CG  . LEU A 1 236 ? 17.845  25.185 21.755  1.00 69.35  ? 265 LEU A CG  1 
ATOM   1786 C  CD1 . LEU A 1 236 ? 18.251  24.365 20.550  1.00 69.76  ? 265 LEU A CD1 1 
ATOM   1787 C  CD2 . LEU A 1 236 ? 16.476  24.740 22.254  1.00 70.46  ? 265 LEU A CD2 1 
ATOM   1788 N  N   . LEU A 1 237 ? 19.911  24.881 25.897  1.00 68.63  ? 266 LEU A N   1 
ATOM   1789 C  CA  . LEU A 1 237 ? 21.055  24.697 26.787  1.00 69.29  ? 266 LEU A CA  1 
ATOM   1790 C  C   . LEU A 1 237 ? 22.229  24.119 25.951  1.00 69.61  ? 266 LEU A C   1 
ATOM   1791 O  O   . LEU A 1 237 ? 22.057  23.824 24.764  1.00 69.45  ? 266 LEU A O   1 
ATOM   1792 C  CB  . LEU A 1 237 ? 20.676  23.730 27.930  1.00 69.70  ? 266 LEU A CB  1 
ATOM   1793 C  CG  . LEU A 1 237 ? 19.382  24.012 28.664  1.00 71.47  ? 266 LEU A CG  1 
ATOM   1794 C  CD1 . LEU A 1 237 ? 19.039  22.887 29.599  1.00 72.48  ? 266 LEU A CD1 1 
ATOM   1795 C  CD2 . LEU A 1 237 ? 19.465  25.301 29.420  1.00 72.05  ? 266 LEU A CD2 1 
ATOM   1796 N  N   . GLY A 1 238 ? 23.405  23.975 26.562  1.00 69.75  ? 267 GLY A N   1 
ATOM   1797 C  CA  . GLY A 1 238 ? 24.550  23.390 25.878  1.00 70.60  ? 267 GLY A CA  1 
ATOM   1798 C  C   . GLY A 1 238 ? 24.291  21.938 25.515  1.00 71.31  ? 267 GLY A C   1 
ATOM   1799 O  O   . GLY A 1 238 ? 24.638  21.493 24.417  1.00 71.30  ? 267 GLY A O   1 
ATOM   1800 N  N   . GLU A 1 239 ? 23.628  21.210 26.434  1.00 71.54  ? 268 GLU A N   1 
ATOM   1801 C  CA  . GLU A 1 239 ? 23.237  19.807 26.295  1.00 72.25  ? 268 GLU A CA  1 
ATOM   1802 C  C   . GLU A 1 239 ? 22.002  19.539 27.176  1.00 72.34  ? 268 GLU A C   1 
ATOM   1803 O  O   . GLU A 1 239 ? 21.808  20.230 28.190  1.00 72.67  ? 268 GLU A O   1 
ATOM   1804 C  CB  . GLU A 1 239 ? 24.404  18.886 26.699  1.00 75.24  ? 268 GLU A CB  1 
ATOM   1805 C  CG  . GLU A 1 239 ? 25.002  19.201 28.059  1.00 81.42  ? 268 GLU A CG  1 
ATOM   1806 C  CD  . GLU A 1 239 ? 25.788  18.056 28.670  1.00 88.83  ? 268 GLU A CD  1 
ATOM   1807 O  OE1 . GLU A 1 239 ? 25.799  17.943 29.917  1.00 90.76  ? 268 GLU A OE1 1 
ATOM   1808 O  OE2 . GLU A 1 239 ? 26.378  17.263 27.902  1.00 90.73  ? 268 GLU A OE2 1 
ATOM   1809 N  N   . PRO A 1 240 ? 21.139  18.562 26.810  1.00 71.65  ? 269 PRO A N   1 
ATOM   1810 C  CA  . PRO A 1 240 ? 19.942  18.297 27.627  1.00 71.34  ? 269 PRO A CA  1 
ATOM   1811 C  C   . PRO A 1 240 ? 20.205  17.932 29.085  1.00 71.60  ? 269 PRO A C   1 
ATOM   1812 O  O   . PRO A 1 240 ? 21.196  17.286 29.401  1.00 71.81  ? 269 PRO A O   1 
ATOM   1813 C  CB  . PRO A 1 240 ? 19.246  17.160 26.882  1.00 71.60  ? 269 PRO A CB  1 
ATOM   1814 C  CG  . PRO A 1 240 ? 19.764  17.243 25.500  1.00 72.09  ? 269 PRO A CG  1 
ATOM   1815 C  CD  . PRO A 1 240 ? 21.181  17.681 25.631  1.00 70.85  ? 269 PRO A CD  1 
ATOM   1816 N  N   . VAL A 1 241 ? 19.319  18.378 29.976  1.00 71.59  ? 270 VAL A N   1 
ATOM   1817 C  CA  . VAL A 1 241 ? 19.404  18.117 31.411  1.00 72.19  ? 270 VAL A CA  1 
ATOM   1818 C  C   . VAL A 1 241 ? 18.230  17.217 31.824  1.00 72.91  ? 270 VAL A C   1 
ATOM   1819 O  O   . VAL A 1 241 ? 17.075  17.650 31.781  1.00 73.37  ? 270 VAL A O   1 
ATOM   1820 C  CB  . VAL A 1 241 ? 19.405  19.443 32.201  1.00 72.79  ? 270 VAL A CB  1 
ATOM   1821 C  CG1 . VAL A 1 241 ? 19.383  19.197 33.704  1.00 73.25  ? 270 VAL A CG1 1 
ATOM   1822 C  CG2 . VAL A 1 241 ? 20.597  20.299 31.808  1.00 73.36  ? 270 VAL A CG2 1 
ATOM   1823 N  N   . LYS A 1 242 ? 18.522  15.954 32.176  1.00 72.56  ? 271 LYS A N   1 
ATOM   1824 C  CA  . LYS A 1 242 ? 17.503  14.983 32.569  1.00 72.80  ? 271 LYS A CA  1 
ATOM   1825 C  C   . LYS A 1 242 ? 16.977  15.324 33.967  1.00 72.58  ? 271 LYS A C   1 
ATOM   1826 O  O   . LYS A 1 242 ? 17.754  15.338 34.925  1.00 72.43  ? 271 LYS A O   1 
ATOM   1827 C  CB  . LYS A 1 242 ? 18.097  13.560 32.539  1.00 74.55  ? 271 LYS A CB  1 
ATOM   1828 C  CG  . LYS A 1 242 ? 17.092  12.437 32.746  1.00 77.51  ? 271 LYS A CG  1 
ATOM   1829 C  CD  . LYS A 1 242 ? 17.706  11.285 33.527  1.00 81.05  ? 271 LYS A CD  1 
ATOM   1830 C  CE  . LYS A 1 242 ? 16.882  10.023 33.407  1.00 85.10  ? 271 LYS A CE  1 
ATOM   1831 N  NZ  . LYS A 1 242 ? 16.248  9.595  34.689  1.00 87.09  ? 271 LYS A NZ  1 
ATOM   1832 N  N   . LEU A 1 243 ? 15.668  15.630 34.072  1.00 72.28  ? 272 LEU A N   1 
ATOM   1833 C  CA  . LEU A 1 243 ? 15.016  15.999 35.336  1.00 72.56  ? 272 LEU A CA  1 
ATOM   1834 C  C   . LEU A 1 243 ? 13.750  15.178 35.563  1.00 72.45  ? 272 LEU A C   1 
ATOM   1835 O  O   . LEU A 1 243 ? 13.114  14.771 34.591  1.00 72.62  ? 272 LEU A O   1 
ATOM   1836 C  CB  . LEU A 1 243 ? 14.570  17.478 35.297  1.00 72.93  ? 272 LEU A CB  1 
ATOM   1837 C  CG  . LEU A 1 243 ? 15.626  18.571 35.306  1.00 74.79  ? 272 LEU A CG  1 
ATOM   1838 C  CD1 . LEU A 1 243 ? 14.973  19.920 35.430  1.00 75.30  ? 272 LEU A CD1 1 
ATOM   1839 C  CD2 . LEU A 1 243 ? 16.585  18.405 36.467  1.00 75.69  ? 272 LEU A CD2 1 
ATOM   1840 N  N   . THR A 1 244 ? 13.338  14.991 36.834  1.00 71.64  ? 273 THR A N   1 
ATOM   1841 C  CA  . THR A 1 244 ? 12.041  14.369 37.109  1.00 71.46  ? 273 THR A CA  1 
ATOM   1842 C  C   . THR A 1 244 ? 11.067  15.490 37.459  1.00 70.77  ? 273 THR A C   1 
ATOM   1843 O  O   . THR A 1 244 ? 9.962   15.522 36.923  1.00 71.23  ? 273 THR A O   1 
ATOM   1844 C  CB  . THR A 1 244 ? 12.090  13.209 38.114  1.00 73.12  ? 273 THR A CB  1 
ATOM   1845 O  OG1 . THR A 1 244 ? 12.774  13.617 39.296  1.00 74.86  ? 273 THR A OG1 1 
ATOM   1846 C  CG2 . THR A 1 244 ? 12.735  11.960 37.535  1.00 73.26  ? 273 THR A CG2 1 
ATOM   1847 N  N   . GLU A 1 245 ? 11.501  16.455 38.294  1.00 69.62  ? 274 GLU A N   1 
ATOM   1848 C  CA  . GLU A 1 245 ? 10.694  17.621 38.636  1.00 69.07  ? 274 GLU A CA  1 
ATOM   1849 C  C   . GLU A 1 245 ? 11.302  18.884 38.010  1.00 68.36  ? 274 GLU A C   1 
ATOM   1850 O  O   . GLU A 1 245 ? 12.512  19.106 38.091  1.00 68.57  ? 274 GLU A O   1 
ATOM   1851 C  CB  . GLU A 1 245 ? 10.608  17.807 40.148  1.00 70.95  ? 274 GLU A CB  1 
ATOM   1852 C  CG  . GLU A 1 245 ? 10.223  16.557 40.904  1.00 75.28  ? 274 GLU A CG  1 
ATOM   1853 C  CD  . GLU A 1 245 ? 9.914   16.770 42.373  1.00 80.52  ? 274 GLU A CD  1 
ATOM   1854 O  OE1 . GLU A 1 245 ? 9.499   15.791 43.035  1.00 82.21  ? 274 GLU A OE1 1 
ATOM   1855 O  OE2 . GLU A 1 245 ? 10.072  17.912 42.860  1.00 81.89  ? 274 GLU A OE2 1 
ATOM   1856 N  N   . LEU A 1 246 ? 10.457  19.714 37.392  1.00 67.14  ? 275 LEU A N   1 
ATOM   1857 C  CA  . LEU A 1 246 ? 10.863  20.962 36.756  1.00 66.17  ? 275 LEU A CA  1 
ATOM   1858 C  C   . LEU A 1 246 ? 10.063  22.118 37.310  1.00 65.18  ? 275 LEU A C   1 
ATOM   1859 O  O   . LEU A 1 246 ? 8.945   22.385 36.864  1.00 65.18  ? 275 LEU A O   1 
ATOM   1860 C  CB  . LEU A 1 246 ? 10.700  20.901 35.231  1.00 66.12  ? 275 LEU A CB  1 
ATOM   1861 C  CG  . LEU A 1 246 ? 11.066  22.166 34.450  1.00 67.00  ? 275 LEU A CG  1 
ATOM   1862 C  CD1 . LEU A 1 246 ? 12.503  22.572 34.678  1.00 67.72  ? 275 LEU A CD1 1 
ATOM   1863 C  CD2 . LEU A 1 246 ? 10.844  21.962 32.995  1.00 67.06  ? 275 LEU A CD2 1 
ATOM   1864 N  N   . PRO A 1 247 ? 10.599  22.789 38.334  1.00 64.24  ? 276 PRO A N   1 
ATOM   1865 C  CA  . PRO A 1 247 ? 9.893   23.958 38.877  1.00 63.51  ? 276 PRO A CA  1 
ATOM   1866 C  C   . PRO A 1 247 ? 9.953   25.105 37.865  1.00 63.01  ? 276 PRO A C   1 
ATOM   1867 O  O   . PRO A 1 247 ? 11.023  25.434 37.340  1.00 62.57  ? 276 PRO A O   1 
ATOM   1868 C  CB  . PRO A 1 247 ? 10.662  24.285 40.158  1.00 64.11  ? 276 PRO A CB  1 
ATOM   1869 C  CG  . PRO A 1 247 ? 11.662  23.159 40.341  1.00 64.72  ? 276 PRO A CG  1 
ATOM   1870 C  CD  . PRO A 1 247 ? 11.896  22.574 38.999  1.00 63.41  ? 276 PRO A CD  1 
ATOM   1871 N  N   . ILE A 1 248 ? 8.788   25.651 37.526  1.00 62.67  ? 277 ILE A N   1 
ATOM   1872 C  CA  . ILE A 1 248 ? 8.709   26.733 36.565  1.00 62.59  ? 277 ILE A CA  1 
ATOM   1873 C  C   . ILE A 1 248 ? 8.043   27.939 37.211  1.00 62.57  ? 277 ILE A C   1 
ATOM   1874 O  O   . ILE A 1 248 ? 6.967   27.813 37.790  1.00 62.48  ? 277 ILE A O   1 
ATOM   1875 C  CB  . ILE A 1 248 ? 8.057   26.260 35.245  1.00 62.72  ? 277 ILE A CB  1 
ATOM   1876 C  CG1 . ILE A 1 248 ? 8.064   27.371 34.179  1.00 63.61  ? 277 ILE A CG1 1 
ATOM   1877 C  CG2 . ILE A 1 248 ? 6.670   25.671 35.475  1.00 62.92  ? 277 ILE A CG2 1 
ATOM   1878 C  CD1 . ILE A 1 248 ? 7.729   26.896 32.821  1.00 64.90  ? 277 ILE A CD1 1 
ATOM   1879 N  N   . LEU A 1 249 ? 8.731   29.092 37.194  1.00 62.45  ? 278 LEU A N   1 
ATOM   1880 C  CA  . LEU A 1 249 ? 8.220   30.318 37.803  1.00 62.66  ? 278 LEU A CA  1 
ATOM   1881 C  C   . LEU A 1 249 ? 7.360   31.132 36.841  1.00 62.65  ? 278 LEU A C   1 
ATOM   1882 O  O   . LEU A 1 249 ? 7.475   30.971 35.632  1.00 62.85  ? 278 LEU A O   1 
ATOM   1883 C  CB  . LEU A 1 249 ? 9.382   31.185 38.300  1.00 62.81  ? 278 LEU A CB  1 
ATOM   1884 C  CG  . LEU A 1 249 ? 10.291  30.578 39.365  1.00 64.24  ? 278 LEU A CG  1 
ATOM   1885 C  CD1 . LEU A 1 249 ? 11.395  31.556 39.751  1.00 64.68  ? 278 LEU A CD1 1 
ATOM   1886 C  CD2 . LEU A 1 249 ? 9.499   30.124 40.589  1.00 64.53  ? 278 LEU A CD2 1 
ATOM   1887 N  N   . MET A 1 250 ? 6.509   32.023 37.380  1.00 62.26  ? 279 MET A N   1 
ATOM   1888 C  CA  . MET A 1 250 ? 5.638   32.895 36.584  1.00 62.27  ? 279 MET A CA  1 
ATOM   1889 C  C   . MET A 1 250 ? 6.432   33.698 35.546  1.00 62.02  ? 279 MET A C   1 
ATOM   1890 O  O   . MET A 1 250 ? 7.347   34.444 35.902  1.00 62.29  ? 279 MET A O   1 
ATOM   1891 C  CB  . MET A 1 250 ? 4.835   33.847 37.485  1.00 63.01  ? 279 MET A CB  1 
ATOM   1892 C  CG  . MET A 1 250 ? 4.040   33.147 38.565  1.00 65.92  ? 279 MET A CG  1 
ATOM   1893 S  SD  . MET A 1 250 ? 5.031   32.785 40.033  1.00 73.11  ? 279 MET A SD  1 
ATOM   1894 C  CE  . MET A 1 250 ? 5.197   34.404 40.689  1.00 74.60  ? 279 MET A CE  1 
ATOM   1895 N  N   . GLY A 1 251 ? 6.096   33.499 34.276  1.00 61.33  ? 280 GLY A N   1 
ATOM   1896 C  CA  . GLY A 1 251 ? 6.758   34.167 33.164  1.00 61.21  ? 280 GLY A CA  1 
ATOM   1897 C  C   . GLY A 1 251 ? 7.848   33.345 32.498  1.00 60.98  ? 280 GLY A C   1 
ATOM   1898 O  O   . GLY A 1 251 ? 8.274   33.670 31.386  1.00 61.48  ? 280 GLY A O   1 
ATOM   1899 N  N   . GLU A 1 252 ? 8.303   32.265 33.155  1.00 60.02  ? 281 GLU A N   1 
ATOM   1900 C  CA  . GLU A 1 252 ? 9.366   31.416 32.614  1.00 59.76  ? 281 GLU A CA  1 
ATOM   1901 C  C   . GLU A 1 252 ? 8.950   30.444 31.506  1.00 59.07  ? 281 GLU A C   1 
ATOM   1902 O  O   . GLU A 1 252 ? 7.816   29.971 31.466  1.00 59.17  ? 281 GLU A O   1 
ATOM   1903 C  CB  . GLU A 1 252 ? 10.053  30.634 33.737  1.00 61.96  ? 281 GLU A CB  1 
ATOM   1904 C  CG  . GLU A 1 252 ? 11.143  31.427 34.416  1.00 66.91  ? 281 GLU A CG  1 
ATOM   1905 C  CD  . GLU A 1 252 ? 11.811  30.731 35.583  1.00 72.82  ? 281 GLU A CD  1 
ATOM   1906 O  OE1 . GLU A 1 252 ? 12.842  31.265 36.054  1.00 73.65  ? 281 GLU A OE1 1 
ATOM   1907 O  OE2 . GLU A 1 252 ? 11.315  29.666 36.027  1.00 73.54  ? 281 GLU A OE2 1 
ATOM   1908 N  N   . ARG A 1 253 ? 9.900   30.108 30.632  1.00 58.11  ? 282 ARG A N   1 
ATOM   1909 C  CA  . ARG A 1 253 ? 9.652   29.155 29.564  1.00 57.69  ? 282 ARG A CA  1 
ATOM   1910 C  C   . ARG A 1 253 ? 10.716  28.089 29.581  1.00 58.21  ? 282 ARG A C   1 
ATOM   1911 O  O   . ARG A 1 253 ? 11.900  28.396 29.730  1.00 58.28  ? 282 ARG A O   1 
ATOM   1912 C  CB  . ARG A 1 253 ? 9.619   29.821 28.184  1.00 57.84  ? 282 ARG A CB  1 
ATOM   1913 C  CG  . ARG A 1 253 ? 8.348   30.584 27.908  1.00 59.23  ? 282 ARG A CG  1 
ATOM   1914 C  CD  . ARG A 1 253 ? 8.483   32.008 28.376  1.00 61.18  ? 282 ARG A CD  1 
ATOM   1915 N  NE  . ARG A 1 253 ? 9.514   32.732 27.639  1.00 62.45  ? 282 ARG A NE  1 
ATOM   1916 C  CZ  . ARG A 1 253 ? 10.429  33.515 28.196  1.00 63.28  ? 282 ARG A CZ  1 
ATOM   1917 N  NH1 . ARG A 1 253 ? 11.312  34.145 27.442  1.00 62.81  ? 282 ARG A NH1 1 
ATOM   1918 N  NH2 . ARG A 1 253 ? 10.460  33.681 29.515  1.00 62.59  ? 282 ARG A NH2 1 
ATOM   1919 N  N   . PHE A 1 254 ? 10.303  26.833 29.408  1.00 58.33  ? 283 PHE A N   1 
ATOM   1920 C  CA  . PHE A 1 254 ? 11.236  25.716 29.384  1.00 58.70  ? 283 PHE A CA  1 
ATOM   1921 C  C   . PHE A 1 254 ? 10.835  24.801 28.283  1.00 59.39  ? 283 PHE A C   1 
ATOM   1922 O  O   . PHE A 1 254 ? 9.690   24.359 28.268  1.00 60.23  ? 283 PHE A O   1 
ATOM   1923 C  CB  . PHE A 1 254 ? 11.172  24.928 30.693  1.00 58.32  ? 283 PHE A CB  1 
ATOM   1924 C  CG  . PHE A 1 254 ? 12.083  25.459 31.762  1.00 58.90  ? 283 PHE A CG  1 
ATOM   1925 C  CD1 . PHE A 1 254 ? 13.457  25.348 31.640  1.00 59.71  ? 283 PHE A CD1 1 
ATOM   1926 C  CD2 . PHE A 1 254 ? 11.569  26.078 32.887  1.00 59.71  ? 283 PHE A CD2 1 
ATOM   1927 C  CE1 . PHE A 1 254 ? 14.302  25.855 32.622  1.00 60.38  ? 283 PHE A CE1 1 
ATOM   1928 C  CE2 . PHE A 1 254 ? 12.417  26.583 33.869  1.00 60.56  ? 283 PHE A CE2 1 
ATOM   1929 C  CZ  . PHE A 1 254 ? 13.776  26.468 33.730  1.00 60.28  ? 283 PHE A CZ  1 
ATOM   1930 N  N   . GLU A 1 255 ? 11.750  24.488 27.376  1.00 58.99  ? 284 GLU A N   1 
ATOM   1931 C  CA  . GLU A 1 255 ? 11.455  23.534 26.318  1.00 59.36  ? 284 GLU A CA  1 
ATOM   1932 C  C   . GLU A 1 255 ? 11.917  22.174 26.818  1.00 60.53  ? 284 GLU A C   1 
ATOM   1933 O  O   . GLU A 1 255 ? 13.063  22.045 27.247  1.00 60.50  ? 284 GLU A O   1 
ATOM   1934 C  CB  . GLU A 1 255 ? 12.169  23.912 25.021  1.00 60.03  ? 284 GLU A CB  1 
ATOM   1935 C  CG  . GLU A 1 255 ? 11.737  25.255 24.476  1.00 62.17  ? 284 GLU A CG  1 
ATOM   1936 C  CD  . GLU A 1 255 ? 12.278  25.571 23.099  1.00 66.22  ? 284 GLU A CD  1 
ATOM   1937 O  OE1 . GLU A 1 255 ? 12.682  26.733 22.868  1.00 67.17  ? 284 GLU A OE1 1 
ATOM   1938 O  OE2 . GLU A 1 255 ? 12.298  24.654 22.249  1.00 68.03  ? 284 GLU A OE2 1 
ATOM   1939 N  N   . VAL A 1 256 ? 11.011  21.184 26.860  1.00 61.41  ? 285 VAL A N   1 
ATOM   1940 C  CA  . VAL A 1 256 ? 11.386  19.852 27.347  1.00 62.59  ? 285 VAL A CA  1 
ATOM   1941 C  C   . VAL A 1 256 ? 11.067  18.775 26.312  1.00 63.81  ? 285 VAL A C   1 
ATOM   1942 O  O   . VAL A 1 256 ? 10.085  18.877 25.581  1.00 63.96  ? 285 VAL A O   1 
ATOM   1943 C  CB  . VAL A 1 256 ? 10.862  19.468 28.773  1.00 62.84  ? 285 VAL A CB  1 
ATOM   1944 C  CG1 . VAL A 1 256 ? 10.700  20.690 29.666  1.00 63.55  ? 285 VAL A CG1 1 
ATOM   1945 C  CG2 . VAL A 1 256 ? 9.577   18.648 28.730  1.00 62.63  ? 285 VAL A CG2 1 
ATOM   1946 N  N   . LEU A 1 257 ? 11.891  17.733 26.281  1.00 64.15  ? 286 LEU A N   1 
ATOM   1947 C  CA  . LEU A 1 257 ? 11.675  16.616 25.390  1.00 64.97  ? 286 LEU A CA  1 
ATOM   1948 C  C   . LEU A 1 257 ? 11.220  15.406 26.187  1.00 65.05  ? 286 LEU A C   1 
ATOM   1949 O  O   . LEU A 1 257 ? 11.799  15.097 27.226  1.00 65.25  ? 286 LEU A O   1 
ATOM   1950 C  CB  . LEU A 1 257 ? 12.955  16.294 24.625  1.00 65.81  ? 286 LEU A CB  1 
ATOM   1951 C  CG  . LEU A 1 257 ? 13.037  16.850 23.219  1.00 68.33  ? 286 LEU A CG  1 
ATOM   1952 C  CD1 . LEU A 1 257 ? 14.322  16.443 22.571  1.00 69.31  ? 286 LEU A CD1 1 
ATOM   1953 C  CD2 . LEU A 1 257 ? 11.933  16.301 22.369  1.00 69.47  ? 286 LEU A CD2 1 
ATOM   1954 N  N   . VAL A 1 258 ? 10.163  14.739 25.724  1.00 64.90  ? 287 VAL A N   1 
ATOM   1955 C  CA  . VAL A 1 258 ? 9.631   13.562 26.403  1.00 65.13  ? 287 VAL A CA  1 
ATOM   1956 C  C   . VAL A 1 258 ? 9.671   12.363 25.480  1.00 64.96  ? 287 VAL A C   1 
ATOM   1957 O  O   . VAL A 1 258 ? 9.346   12.475 24.302  1.00 64.93  ? 287 VAL A O   1 
ATOM   1958 C  CB  . VAL A 1 258 ? 8.217   13.751 26.997  1.00 66.14  ? 287 VAL A CB  1 
ATOM   1959 C  CG1 . VAL A 1 258 ? 7.957   12.698 28.063  1.00 66.97  ? 287 VAL A CG1 1 
ATOM   1960 C  CG2 . VAL A 1 258 ? 8.032   15.142 27.591  1.00 66.66  ? 287 VAL A CG2 1 
ATOM   1961 N  N   . ASP A 1 259 ? 10.085  11.213 26.012  1.00 64.83  ? 288 ASP A N   1 
ATOM   1962 C  CA  . ASP A 1 259 ? 10.170  9.981  25.243  1.00 64.94  ? 288 ASP A CA  1 
ATOM   1963 C  C   . ASP A 1 259 ? 8.792   9.304  25.105  1.00 64.75  ? 288 ASP A C   1 
ATOM   1964 O  O   . ASP A 1 259 ? 8.197   8.867  26.096  1.00 64.63  ? 288 ASP A O   1 
ATOM   1965 C  CB  . ASP A 1 259 ? 11.177  9.035  25.908  1.00 66.44  ? 288 ASP A CB  1 
ATOM   1966 C  CG  . ASP A 1 259 ? 11.827  8.050  24.965  1.00 70.85  ? 288 ASP A CG  1 
ATOM   1967 O  OD1 . ASP A 1 259 ? 11.252  7.789  23.892  1.00 70.68  ? 288 ASP A OD1 1 
ATOM   1968 O  OD2 . ASP A 1 259 ? 12.902  7.524  25.311  1.00 74.09  ? 288 ASP A OD2 1 
ATOM   1969 N  N   . THR A 1 260 ? 8.281   9.233  23.874  1.00 64.45  ? 289 THR A N   1 
ATOM   1970 C  CA  . THR A 1 260 ? 7.000   8.567  23.617  1.00 64.54  ? 289 THR A CA  1 
ATOM   1971 C  C   . THR A 1 260 ? 7.161   7.251  22.847  1.00 65.64  ? 289 THR A C   1 
ATOM   1972 O  O   . THR A 1 260 ? 6.155   6.706  22.398  1.00 66.04  ? 289 THR A O   1 
ATOM   1973 C  CB  . THR A 1 260 ? 6.075   9.476  22.835  1.00 64.16  ? 289 THR A CB  1 
ATOM   1974 O  OG1 . THR A 1 260 ? 6.706   9.809  21.600  1.00 64.10  ? 289 THR A OG1 1 
ATOM   1975 C  CG2 . THR A 1 260 ? 5.698   10.721 23.610  1.00 64.22  ? 289 THR A CG2 1 
ATOM   1976 N  N   . ARG A 1 261 ? 8.412   6.747  22.681  1.00 65.76  ? 290 ARG A N   1 
ATOM   1977 C  CA  . ARG A 1 261 ? 8.713   5.528  21.943  1.00 66.17  ? 290 ARG A CA  1 
ATOM   1978 C  C   . ARG A 1 261 ? 8.011   4.309  22.502  1.00 67.26  ? 290 ARG A C   1 
ATOM   1979 O  O   . ARG A 1 261 ? 7.634   3.428  21.727  1.00 67.66  ? 290 ARG A O   1 
ATOM   1980 C  CB  . ARG A 1 261 ? 10.226  5.313  21.839  1.00 66.71  ? 290 ARG A CB  1 
ATOM   1981 C  CG  . ARG A 1 261 ? 10.863  6.291  20.858  1.00 67.95  ? 290 ARG A CG  1 
ATOM   1982 C  CD  . ARG A 1 261 ? 12.369  6.201  20.773  1.00 68.87  ? 290 ARG A CD  1 
ATOM   1983 N  NE  . ARG A 1 261 ? 13.021  6.433  22.065  1.00 69.86  ? 290 ARG A NE  1 
ATOM   1984 C  CZ  . ARG A 1 261 ? 14.337  6.542  22.227  1.00 70.69  ? 290 ARG A CZ  1 
ATOM   1985 N  NH1 . ARG A 1 261 ? 15.153  6.476  21.179  1.00 69.81  ? 290 ARG A NH1 1 
ATOM   1986 N  NH2 . ARG A 1 261 ? 14.848  6.738  23.434  1.00 70.07  ? 290 ARG A NH2 1 
ATOM   1987 N  N   . ASP A 1 262 ? 7.772   4.274  23.828  1.00 67.42  ? 291 ASP A N   1 
ATOM   1988 C  CA  . ASP A 1 262 ? 7.065   3.153  24.444  1.00 68.32  ? 291 ASP A CA  1 
ATOM   1989 C  C   . ASP A 1 262 ? 5.569   3.076  24.097  1.00 68.11  ? 291 ASP A C   1 
ATOM   1990 O  O   . ASP A 1 262 ? 4.928   2.072  24.403  1.00 68.72  ? 291 ASP A O   1 
ATOM   1991 C  CB  . ASP A 1 262 ? 7.262   3.125  25.966  1.00 71.95  ? 291 ASP A CB  1 
ATOM   1992 C  CG  . ASP A 1 262 ? 6.585   4.262  26.705  1.00 80.34  ? 291 ASP A CG  1 
ATOM   1993 O  OD1 . ASP A 1 262 ? 6.448   5.363  26.111  1.00 82.92  ? 291 ASP A OD1 1 
ATOM   1994 O  OD2 . ASP A 1 262 ? 6.196   4.060  27.879  1.00 82.76  ? 291 ASP A OD2 1 
ATOM   1995 N  N   . GLY A 1 263 ? 5.020   4.124  23.495  1.00 67.20  ? 292 GLY A N   1 
ATOM   1996 C  CA  . GLY A 1 263 ? 3.625   4.148  23.086  1.00 66.96  ? 292 GLY A CA  1 
ATOM   1997 C  C   . GLY A 1 263 ? 2.606   4.251  24.199  1.00 66.91  ? 292 GLY A C   1 
ATOM   1998 O  O   . GLY A 1 263 ? 1.410   4.286  23.913  1.00 66.81  ? 292 GLY A O   1 
ATOM   1999 N  N   . LYS A 1 264 ? 3.047   4.314  25.470  1.00 67.13  ? 293 LYS A N   1 
ATOM   2000 C  CA  . LYS A 1 264 ? 2.128   4.398  26.613  1.00 68.21  ? 293 LYS A CA  1 
ATOM   2001 C  C   . LYS A 1 264 ? 1.690   5.821  26.926  1.00 68.58  ? 293 LYS A C   1 
ATOM   2002 O  O   . LYS A 1 264 ? 2.498   6.749  26.881  1.00 69.09  ? 293 LYS A O   1 
ATOM   2003 C  CB  . LYS A 1 264 ? 2.706   3.722  27.879  1.00 70.45  ? 293 LYS A CB  1 
ATOM   2004 C  CG  . LYS A 1 264 ? 2.514   2.199  27.912  1.00 75.40  ? 293 LYS A CG  1 
ATOM   2005 C  CD  . LYS A 1 264 ? 3.857   1.449  28.077  1.00 80.50  ? 293 LYS A CD  1 
ATOM   2006 C  CE  . LYS A 1 264 ? 3.942   0.148  27.292  1.00 83.18  ? 293 LYS A CE  1 
ATOM   2007 N  NZ  . LYS A 1 264 ? 3.141   -0.947 27.903  1.00 84.30  ? 293 LYS A NZ  1 
ATOM   2008 N  N   . ALA A 1 265 ? 0.406   5.988  27.238  1.00 68.11  ? 294 ALA A N   1 
ATOM   2009 C  CA  . ALA A 1 265 ? -0.128  7.289  27.598  1.00 68.14  ? 294 ALA A CA  1 
ATOM   2010 C  C   . ALA A 1 265 ? 0.324   7.661  29.006  1.00 68.33  ? 294 ALA A C   1 
ATOM   2011 O  O   . ALA A 1 265 ? 0.615   6.787  29.832  1.00 68.41  ? 294 ALA A O   1 
ATOM   2012 C  CB  . ALA A 1 265 ? -1.641  7.280  27.521  1.00 68.12  ? 294 ALA A CB  1 
ATOM   2013 N  N   . PHE A 1 266 ? 0.396   8.966  29.271  1.00 68.15  ? 295 PHE A N   1 
ATOM   2014 C  CA  . PHE A 1 266 ? 0.838   9.499  30.558  1.00 68.26  ? 295 PHE A CA  1 
ATOM   2015 C  C   . PHE A 1 266 ? 0.400   10.958 30.711  1.00 68.36  ? 295 PHE A C   1 
ATOM   2016 O  O   . PHE A 1 266 ? 0.014   11.593 29.731  1.00 68.50  ? 295 PHE A O   1 
ATOM   2017 C  CB  . PHE A 1 266 ? 2.374   9.369  30.696  1.00 68.04  ? 295 PHE A CB  1 
ATOM   2018 C  CG  . PHE A 1 266 ? 3.169   10.127 29.658  1.00 68.62  ? 295 PHE A CG  1 
ATOM   2019 C  CD1 . PHE A 1 266 ? 3.371   9.600  28.394  1.00 69.17  ? 295 PHE A CD1 1 
ATOM   2020 C  CD2 . PHE A 1 266 ? 3.729   11.360 29.953  1.00 69.47  ? 295 PHE A CD2 1 
ATOM   2021 C  CE1 . PHE A 1 266 ? 4.103   10.296 27.443  1.00 69.81  ? 295 PHE A CE1 1 
ATOM   2022 C  CE2 . PHE A 1 266 ? 4.453   12.058 28.995  1.00 70.03  ? 295 PHE A CE2 1 
ATOM   2023 C  CZ  . PHE A 1 266 ? 4.632   11.523 27.747  1.00 69.63  ? 295 PHE A CZ  1 
ATOM   2024 N  N   . ASP A 1 267 ? 0.495   11.503 31.926  1.00 68.10  ? 296 ASP A N   1 
ATOM   2025 C  CA  . ASP A 1 267 ? 0.146   12.891 32.182  1.00 68.23  ? 296 ASP A CA  1 
ATOM   2026 C  C   . ASP A 1 267 ? 1.348   13.755 32.515  1.00 67.98  ? 296 ASP A C   1 
ATOM   2027 O  O   . ASP A 1 267 ? 2.344   13.292 33.068  1.00 67.95  ? 296 ASP A O   1 
ATOM   2028 C  CB  . ASP A 1 267 ? -0.809  12.973 33.375  1.00 70.45  ? 296 ASP A CB  1 
ATOM   2029 C  CG  . ASP A 1 267 ? -2.163  12.403 33.080  1.00 76.81  ? 296 ASP A CG  1 
ATOM   2030 O  OD1 . ASP A 1 267 ? -2.657  12.609 31.953  1.00 77.98  ? 296 ASP A OD1 1 
ATOM   2031 O  OD2 . ASP A 1 267 ? -2.743  11.760 33.979  1.00 79.58  ? 296 ASP A OD2 1 
ATOM   2032 N  N   . ILE A 1 268 ? 1.226   15.034 32.213  1.00 67.60  ? 297 ILE A N   1 
ATOM   2033 C  CA  . ILE A 1 268 ? 2.157   16.054 32.643  1.00 67.38  ? 297 ILE A CA  1 
ATOM   2034 C  C   . ILE A 1 268 ? 1.438   16.553 33.881  1.00 67.45  ? 297 ILE A C   1 
ATOM   2035 O  O   . ILE A 1 268 ? 0.275   16.942 33.786  1.00 67.87  ? 297 ILE A O   1 
ATOM   2036 C  CB  . ILE A 1 268 ? 2.322   17.183 31.604  1.00 67.51  ? 297 ILE A CB  1 
ATOM   2037 C  CG1 . ILE A 1 268 ? 3.097   16.691 30.372  1.00 68.15  ? 297 ILE A CG1 1 
ATOM   2038 C  CG2 . ILE A 1 268 ? 3.009   18.389 32.243  1.00 68.09  ? 297 ILE A CG2 1 
ATOM   2039 C  CD1 . ILE A 1 268 ? 4.505   16.206 30.655  1.00 69.17  ? 297 ILE A CD1 1 
ATOM   2040 N  N   . ILE A 1 269 ? 2.056   16.430 35.052  1.00 66.92  ? 298 ILE A N   1 
ATOM   2041 C  CA  . ILE A 1 269 ? 1.423   16.834 36.304  1.00 67.05  ? 298 ILE A CA  1 
ATOM   2042 C  C   . ILE A 1 269 ? 2.195   17.945 36.991  1.00 67.45  ? 298 ILE A C   1 
ATOM   2043 O  O   . ILE A 1 269 ? 3.399   18.083 36.790  1.00 67.40  ? 298 ILE A O   1 
ATOM   2044 C  CB  . ILE A 1 269 ? 1.253   15.621 37.254  1.00 67.13  ? 298 ILE A CB  1 
ATOM   2045 C  CG1 . ILE A 1 269 ? 2.614   14.964 37.534  1.00 68.26  ? 298 ILE A CG1 1 
ATOM   2046 C  CG2 . ILE A 1 269 ? 0.270   14.615 36.692  1.00 67.26  ? 298 ILE A CG2 1 
ATOM   2047 C  CD1 . ILE A 1 269 ? 2.605   13.865 38.544  1.00 69.86  ? 298 ILE A CD1 1 
ATOM   2048 N  N   . THR A 1 270 ? 1.502   18.738 37.815  1.00 67.60  ? 299 THR A N   1 
ATOM   2049 C  CA  . THR A 1 270 ? 2.158   19.769 38.606  1.00 68.20  ? 299 THR A CA  1 
ATOM   2050 C  C   . THR A 1 270 ? 2.017   19.383 40.078  1.00 68.51  ? 299 THR A C   1 
ATOM   2051 O  O   . THR A 1 270 ? 0.962   18.925 40.525  1.00 68.33  ? 299 THR A O   1 
ATOM   2052 C  CB  . THR A 1 270 ? 1.742   21.206 38.232  1.00 69.58  ? 299 THR A CB  1 
ATOM   2053 O  OG1 . THR A 1 270 ? 2.553   22.126 38.974  1.00 70.53  ? 299 THR A OG1 1 
ATOM   2054 C  CG2 . THR A 1 270 ? 0.267   21.484 38.475  1.00 70.07  ? 299 THR A CG2 1 
ATOM   2055 N  N   . LEU A 1 271 ? 3.123   19.481 40.798  1.00 68.77  ? 300 LEU A N   1 
ATOM   2056 C  CA  . LEU A 1 271 ? 3.223   19.093 42.198  1.00 69.35  ? 300 LEU A CA  1 
ATOM   2057 C  C   . LEU A 1 271 ? 2.925   20.249 43.136  1.00 70.01  ? 300 LEU A C   1 
ATOM   2058 O  O   . LEU A 1 271 ? 3.123   21.407 42.767  1.00 70.32  ? 300 LEU A O   1 
ATOM   2059 C  CB  . LEU A 1 271 ? 4.635   18.546 42.448  1.00 69.29  ? 300 LEU A CB  1 
ATOM   2060 C  CG  . LEU A 1 271 ? 4.991   17.339 41.599  1.00 70.16  ? 300 LEU A CG  1 
ATOM   2061 C  CD1 . LEU A 1 271 ? 6.450   17.015 41.695  1.00 70.30  ? 300 LEU A CD1 1 
ATOM   2062 C  CD2 . LEU A 1 271 ? 4.141   16.161 41.973  1.00 70.95  ? 300 LEU A CD2 1 
ATOM   2063 N  N   . PRO A 1 272 ? 2.423   19.970 44.351  1.00 70.17  ? 301 PRO A N   1 
ATOM   2064 C  CA  . PRO A 1 272 ? 2.118   21.067 45.279  1.00 70.30  ? 301 PRO A CA  1 
ATOM   2065 C  C   . PRO A 1 272 ? 3.378   21.849 45.648  1.00 70.59  ? 301 PRO A C   1 
ATOM   2066 O  O   . PRO A 1 272 ? 4.448   21.258 45.839  1.00 70.38  ? 301 PRO A O   1 
ATOM   2067 C  CB  . PRO A 1 272 ? 1.510   20.350 46.489  1.00 70.89  ? 301 PRO A CB  1 
ATOM   2068 C  CG  . PRO A 1 272 ? 1.066   19.027 45.968  1.00 71.33  ? 301 PRO A CG  1 
ATOM   2069 C  CD  . PRO A 1 272 ? 2.093   18.663 44.946  1.00 69.73  ? 301 PRO A CD  1 
ATOM   2070 N  N   . VAL A 1 273 ? 3.269   23.181 45.681  1.00 70.75  ? 302 VAL A N   1 
ATOM   2071 C  CA  . VAL A 1 273 ? 4.416   24.020 46.012  1.00 71.40  ? 302 VAL A CA  1 
ATOM   2072 C  C   . VAL A 1 273 ? 4.285   24.609 47.423  1.00 72.65  ? 302 VAL A C   1 
ATOM   2073 O  O   . VAL A 1 273 ? 3.174   24.778 47.935  1.00 72.81  ? 302 VAL A O   1 
ATOM   2074 C  CB  . VAL A 1 273 ? 4.686   25.108 44.944  1.00 71.52  ? 302 VAL A CB  1 
ATOM   2075 C  CG1 . VAL A 1 273 ? 4.920   24.486 43.576  1.00 71.65  ? 302 VAL A CG1 1 
ATOM   2076 C  CG2 . VAL A 1 273 ? 3.547   26.125 44.888  1.00 72.05  ? 302 VAL A CG2 1 
ATOM   2077 N  N   . LYS A 1 274 ? 5.425   24.923 48.056  1.00 73.21  ? 303 LYS A N   1 
ATOM   2078 C  CA  . LYS A 1 274 ? 5.401   25.515 49.389  1.00 74.25  ? 303 LYS A CA  1 
ATOM   2079 C  C   . LYS A 1 274 ? 5.273   27.038 49.328  1.00 74.83  ? 303 LYS A C   1 
ATOM   2080 O  O   . LYS A 1 274 ? 5.796   27.735 50.194  1.00 75.59  ? 303 LYS A O   1 
ATOM   2081 C  CB  . LYS A 1 274 ? 6.622   25.074 50.232  1.00 76.59  ? 303 LYS A CB  1 
ATOM   2082 C  CG  . LYS A 1 274 ? 6.939   23.574 50.134  1.00 81.25  ? 303 LYS A CG  1 
ATOM   2083 C  CD  . LYS A 1 274 ? 6.908   22.809 51.474  1.00 85.60  ? 303 LYS A CD  1 
ATOM   2084 C  CE  . LYS A 1 274 ? 6.874   21.312 51.251  1.00 88.85  ? 303 LYS A CE  1 
ATOM   2085 N  NZ  . LYS A 1 274 ? 6.972   20.568 52.532  1.00 90.77  ? 303 LYS A NZ  1 
ATOM   2086 N  N   . GLN A 1 275 ? 4.573   27.557 48.318  1.00 74.36  ? 304 GLN A N   1 
ATOM   2087 C  CA  . GLN A 1 275 ? 4.351   28.989 48.159  1.00 74.49  ? 304 GLN A CA  1 
ATOM   2088 C  C   . GLN A 1 275 ? 3.044   29.352 48.856  1.00 74.01  ? 304 GLN A C   1 
ATOM   2089 O  O   . GLN A 1 275 ? 2.125   28.531 48.905  1.00 74.02  ? 304 GLN A O   1 
ATOM   2090 C  CB  . GLN A 1 275 ? 4.286   29.341 46.671  1.00 76.47  ? 304 GLN A CB  1 
ATOM   2091 C  CG  . GLN A 1 275 ? 4.578   30.800 46.346  1.00 80.49  ? 304 GLN A CG  1 
ATOM   2092 C  CD  . GLN A 1 275 ? 4.094   31.160 44.959  1.00 85.11  ? 304 GLN A CD  1 
ATOM   2093 O  OE1 . GLN A 1 275 ? 4.023   30.318 44.059  1.00 86.29  ? 304 GLN A OE1 1 
ATOM   2094 N  NE2 . GLN A 1 275 ? 3.731   32.419 44.757  1.00 85.92  ? 304 GLN A NE2 1 
ATOM   2095 N  N   . MET A 1 276 ? 2.960   30.562 49.412  1.00 73.53  ? 305 MET A N   1 
ATOM   2096 C  CA  . MET A 1 276 ? 1.773   30.972 50.151  1.00 73.60  ? 305 MET A CA  1 
ATOM   2097 C  C   . MET A 1 276 ? 0.533   31.095 49.302  1.00 73.59  ? 305 MET A C   1 
ATOM   2098 O  O   . MET A 1 276 ? 0.565   31.762 48.272  1.00 73.97  ? 305 MET A O   1 
ATOM   2099 C  CB  . MET A 1 276 ? 2.016   32.269 50.915  1.00 74.32  ? 305 MET A CB  1 
ATOM   2100 C  CG  . MET A 1 276 ? 0.992   32.491 52.002  1.00 76.61  ? 305 MET A CG  1 
ATOM   2101 S  SD  . MET A 1 276 ? 1.341   33.923 53.033  1.00 80.16  ? 305 MET A SD  1 
ATOM   2102 C  CE  . MET A 1 276 ? 2.994   33.547 53.593  1.00 74.78  ? 305 MET A CE  1 
ATOM   2103 N  N   . GLY A 1 277 ? -0.554  30.466 49.747  1.00 73.13  ? 306 GLY A N   1 
ATOM   2104 C  CA  . GLY A 1 277 ? -1.835  30.504 49.047  1.00 73.29  ? 306 GLY A CA  1 
ATOM   2105 C  C   . GLY A 1 277 ? -1.952  29.520 47.902  1.00 73.32  ? 306 GLY A C   1 
ATOM   2106 O  O   . GLY A 1 277 ? -3.060  29.191 47.472  1.00 73.41  ? 306 GLY A O   1 
ATOM   2107 N  N   . MET A 1 278 ? -0.811  29.026 47.406  1.00 73.20  ? 307 MET A N   1 
ATOM   2108 C  CA  . MET A 1 278 ? -0.763  28.089 46.287  1.00 73.82  ? 307 MET A CA  1 
ATOM   2109 C  C   . MET A 1 278 ? -0.869  26.609 46.699  1.00 74.70  ? 307 MET A C   1 
ATOM   2110 O  O   . MET A 1 278 ? -0.612  25.719 45.881  1.00 74.81  ? 307 MET A O   1 
ATOM   2111 C  CB  . MET A 1 278 ? 0.522   28.312 45.462  1.00 74.06  ? 307 MET A CB  1 
ATOM   2112 C  CG  . MET A 1 278 ? 0.861   29.777 45.204  1.00 74.59  ? 307 MET A CG  1 
ATOM   2113 S  SD  . MET A 1 278 ? -0.456  30.733 44.423  1.00 72.72  ? 307 MET A SD  1 
ATOM   2114 C  CE  . MET A 1 278 ? 0.166   32.337 44.634  1.00 71.11  ? 307 MET A CE  1 
ATOM   2115 N  N   . THR A 1 279 ? -1.266  26.354 47.953  1.00 75.11  ? 308 THR A N   1 
ATOM   2116 C  CA  . THR A 1 279 ? -1.372  25.029 48.554  1.00 75.75  ? 308 THR A CA  1 
ATOM   2117 C  C   . THR A 1 279 ? -2.803  24.474 48.564  1.00 75.93  ? 308 THR A C   1 
ATOM   2118 O  O   . THR A 1 279 ? -2.984  23.258 48.615  1.00 76.13  ? 308 THR A O   1 
ATOM   2119 C  CB  . THR A 1 279 ? -0.839  25.125 49.988  1.00 77.38  ? 308 THR A CB  1 
ATOM   2120 O  OG1 . THR A 1 279 ? -1.654  26.057 50.707  1.00 78.75  ? 308 THR A OG1 1 
ATOM   2121 C  CG2 . THR A 1 279 ? 0.612   25.595 50.039  1.00 77.70  ? 308 THR A CG2 1 
ATOM   2122 N  N   . LEU A 1 280 ? -3.808  25.358 48.532  1.00 75.91  ? 309 LEU A N   1 
ATOM   2123 C  CA  . LEU A 1 280 ? -5.231  25.009 48.598  1.00 76.59  ? 309 LEU A CA  1 
ATOM   2124 C  C   . LEU A 1 280 ? -5.700  24.161 47.408  1.00 77.29  ? 309 LEU A C   1 
ATOM   2125 O  O   . LEU A 1 280 ? -5.166  24.301 46.304  1.00 77.69  ? 309 LEU A O   1 
ATOM   2126 C  CB  . LEU A 1 280 ? -6.095  26.284 48.723  1.00 76.84  ? 309 LEU A CB  1 
ATOM   2127 C  CG  . LEU A 1 280 ? -5.582  27.374 49.669  1.00 78.74  ? 309 LEU A CG  1 
ATOM   2128 C  CD1 . LEU A 1 280 ? -6.428  28.620 49.578  1.00 79.21  ? 309 LEU A CD1 1 
ATOM   2129 C  CD2 . LEU A 1 280 ? -5.482  26.875 51.105  1.00 79.70  ? 309 LEU A CD2 1 
ATOM   2130 N  N   . PRO A 1 281 ? -6.718  23.292 47.623  1.00 77.07  ? 310 PRO A N   1 
ATOM   2131 C  CA  . PRO A 1 281 ? -7.234  22.451 46.518  1.00 76.95  ? 310 PRO A CA  1 
ATOM   2132 C  C   . PRO A 1 281 ? -7.607  23.216 45.246  1.00 77.02  ? 310 PRO A C   1 
ATOM   2133 O  O   . PRO A 1 281 ? -7.998  24.384 45.336  1.00 77.24  ? 310 PRO A O   1 
ATOM   2134 C  CB  . PRO A 1 281 ? -8.487  21.802 47.120  1.00 77.36  ? 310 PRO A CB  1 
ATOM   2135 C  CG  . PRO A 1 281 ? -8.320  21.887 48.570  1.00 77.66  ? 310 PRO A CG  1 
ATOM   2136 C  CD  . PRO A 1 281 ? -7.433  23.036 48.889  1.00 76.22  ? 310 PRO A CD  1 
ATOM   2137 N  N   . PRO A 1 282 ? -7.521  22.593 44.046  1.00 76.83  ? 311 PRO A N   1 
ATOM   2138 C  CA  . PRO A 1 282 ? -7.063  21.215 43.750  1.00 76.81  ? 311 PRO A CA  1 
ATOM   2139 C  C   . PRO A 1 282 ? -5.544  21.002 43.800  1.00 76.90  ? 311 PRO A C   1 
ATOM   2140 O  O   . PRO A 1 282 ? -5.059  19.885 43.606  1.00 76.91  ? 311 PRO A O   1 
ATOM   2141 C  CB  . PRO A 1 282 ? -7.566  20.998 42.316  1.00 77.34  ? 311 PRO A CB  1 
ATOM   2142 C  CG  . PRO A 1 282 ? -7.486  22.360 41.700  1.00 77.68  ? 311 PRO A CG  1 
ATOM   2143 C  CD  . PRO A 1 282 ? -7.885  23.314 42.806  1.00 76.28  ? 311 PRO A CD  1 
ATOM   2144 N  N   . PHE A 1 283 ? -4.796  22.072 44.072  1.00 76.71  ? 312 PHE A N   1 
ATOM   2145 C  CA  . PHE A 1 283 ? -3.344  22.045 44.118  1.00 76.83  ? 312 PHE A CA  1 
ATOM   2146 C  C   . PHE A 1 283 ? -2.768  21.411 45.396  1.00 77.05  ? 312 PHE A C   1 
ATOM   2147 O  O   . PHE A 1 283 ? -1.546  21.373 45.554  1.00 77.07  ? 312 PHE A O   1 
ATOM   2148 C  CB  . PHE A 1 283 ? -2.783  23.452 43.878  1.00 76.51  ? 312 PHE A CB  1 
ATOM   2149 C  CG  . PHE A 1 283 ? -3.234  24.070 42.569  1.00 76.65  ? 312 PHE A CG  1 
ATOM   2150 C  CD1 . PHE A 1 283 ? -2.505  23.884 41.409  1.00 77.29  ? 312 PHE A CD1 1 
ATOM   2151 C  CD2 . PHE A 1 283 ? -4.373  24.854 42.508  1.00 77.08  ? 312 PHE A CD2 1 
ATOM   2152 C  CE1 . PHE A 1 283 ? -2.914  24.462 40.214  1.00 77.82  ? 312 PHE A CE1 1 
ATOM   2153 C  CE2 . PHE A 1 283 ? -4.773  25.436 41.313  1.00 77.62  ? 312 PHE A CE2 1 
ATOM   2154 C  CZ  . PHE A 1 283 ? -4.048  25.228 40.172  1.00 77.47  ? 312 PHE A CZ  1 
ATOM   2155 N  N   . ASP A 1 284 ? -3.637  20.874 46.276  1.00 77.03  ? 313 ASP A N   1 
ATOM   2156 C  CA  . ASP A 1 284 ? -3.244  20.155 47.493  1.00 77.32  ? 313 ASP A CA  1 
ATOM   2157 C  C   . ASP A 1 284 ? -2.530  18.824 47.154  1.00 77.05  ? 313 ASP A C   1 
ATOM   2158 O  O   . ASP A 1 284 ? -1.694  18.366 47.924  1.00 77.16  ? 313 ASP A O   1 
ATOM   2159 C  CB  . ASP A 1 284 ? -4.472  19.902 48.399  1.00 78.86  ? 313 ASP A CB  1 
ATOM   2160 C  CG  . ASP A 1 284 ? -5.612  19.110 47.764  1.00 83.03  ? 313 ASP A CG  1 
ATOM   2161 O  OD1 . ASP A 1 284 ? -5.604  18.937 46.526  1.00 83.69  ? 313 ASP A OD1 1 
ATOM   2162 O  OD2 . ASP A 1 284 ? -6.517  18.671 48.508  1.00 85.12  ? 313 ASP A OD2 1 
ATOM   2163 N  N   . ARG A 1 285 ? -2.871  18.216 46.005  1.00 76.57  ? 314 ARG A N   1 
ATOM   2164 C  CA  . ARG A 1 285 ? -2.306  16.959 45.508  1.00 76.86  ? 314 ARG A CA  1 
ATOM   2165 C  C   . ARG A 1 285 ? -1.689  17.167 44.109  1.00 75.39  ? 314 ARG A C   1 
ATOM   2166 O  O   . ARG A 1 285 ? -1.797  18.254 43.552  1.00 75.80  ? 314 ARG A O   1 
ATOM   2167 C  CB  . ARG A 1 285 ? -3.414  15.862 45.422  1.00 80.08  ? 314 ARG A CB  1 
ATOM   2168 C  CG  . ARG A 1 285 ? -4.150  15.527 46.710  1.00 86.29  ? 314 ARG A CG  1 
ATOM   2169 C  CD  . ARG A 1 285 ? -3.579  14.326 47.478  1.00 91.94  ? 314 ARG A CD  1 
ATOM   2170 N  NE  . ARG A 1 285 ? -4.471  13.893 48.551  1.00 96.57  ? 314 ARG A NE  1 
ATOM   2171 C  CZ  . ARG A 1 285 ? -4.280  14.145 49.842  1.00 100.13 ? 314 ARG A CZ  1 
ATOM   2172 N  NH1 . ARG A 1 285 ? -3.208  14.821 50.246  1.00 100.13 ? 314 ARG A NH1 1 
ATOM   2173 N  NH2 . ARG A 1 285 ? -5.145  13.706 50.743  1.00 100.86 ? 314 ARG A NH2 1 
ATOM   2174 N  N   . ALA A 1 286 ? -1.064  16.126 43.529  1.00 73.73  ? 315 ALA A N   1 
ATOM   2175 C  CA  . ALA A 1 286 ? -0.514  16.209 42.177  1.00 72.62  ? 315 ALA A CA  1 
ATOM   2176 C  C   . ALA A 1 286 ? -1.680  16.402 41.190  1.00 70.72  ? 315 ALA A C   1 
ATOM   2177 O  O   . ALA A 1 286 ? -2.686  15.696 41.264  1.00 70.36  ? 315 ALA A O   1 
ATOM   2178 C  CB  . ALA A 1 286 ? 0.273   14.951 41.838  1.00 72.77  ? 315 ALA A CB  1 
ATOM   2179 N  N   . LEU A 1 287 ? -1.564  17.409 40.325  1.00 69.10  ? 316 LEU A N   1 
ATOM   2180 C  CA  . LEU A 1 287 ? -2.627  17.760 39.412  1.00 68.16  ? 316 LEU A CA  1 
ATOM   2181 C  C   . LEU A 1 287 ? -2.239  17.583 37.947  1.00 67.27  ? 316 LEU A C   1 
ATOM   2182 O  O   . LEU A 1 287 ? -1.344  18.262 37.444  1.00 67.43  ? 316 LEU A O   1 
ATOM   2183 C  CB  . LEU A 1 287 ? -3.030  19.214 39.693  1.00 68.20  ? 316 LEU A CB  1 
ATOM   2184 C  CG  . LEU A 1 287 ? -4.083  19.830 38.795  1.00 69.34  ? 316 LEU A CG  1 
ATOM   2185 C  CD1 . LEU A 1 287 ? -5.373  19.061 38.870  1.00 69.90  ? 316 LEU A CD1 1 
ATOM   2186 C  CD2 . LEU A 1 287 ? -4.324  21.271 39.168  1.00 69.83  ? 316 LEU A CD2 1 
ATOM   2187 N  N   . PRO A 1 288 ? -2.941  16.690 37.230  1.00 65.91  ? 317 PRO A N   1 
ATOM   2188 C  CA  . PRO A 1 288 ? -2.637  16.509 35.808  1.00 64.85  ? 317 PRO A CA  1 
ATOM   2189 C  C   . PRO A 1 288 ? -3.072  17.729 34.994  1.00 63.25  ? 317 PRO A C   1 
ATOM   2190 O  O   . PRO A 1 288 ? -4.226  18.154 35.071  1.00 63.36  ? 317 PRO A O   1 
ATOM   2191 C  CB  . PRO A 1 288 ? -3.408  15.232 35.439  1.00 65.68  ? 317 PRO A CB  1 
ATOM   2192 C  CG  . PRO A 1 288 ? -3.897  14.651 36.744  1.00 66.11  ? 317 PRO A CG  1 
ATOM   2193 C  CD  . PRO A 1 288 ? -4.035  15.803 37.669  1.00 64.92  ? 317 PRO A CD  1 
ATOM   2194 N  N   . VAL A 1 289 ? -2.136  18.327 34.261  1.00 61.49  ? 318 VAL A N   1 
ATOM   2195 C  CA  . VAL A 1 289 ? -2.434  19.505 33.462  1.00 60.37  ? 318 VAL A CA  1 
ATOM   2196 C  C   . VAL A 1 289 ? -2.595  19.166 31.976  1.00 60.32  ? 318 VAL A C   1 
ATOM   2197 O  O   . VAL A 1 289 ? -3.332  19.858 31.271  1.00 60.38  ? 318 VAL A O   1 
ATOM   2198 C  CB  . VAL A 1 289 ? -1.421  20.653 33.703  1.00 59.86  ? 318 VAL A CB  1 
ATOM   2199 C  CG1 . VAL A 1 289 ? -1.509  21.167 35.130  1.00 60.13  ? 318 VAL A CG1 1 
ATOM   2200 C  CG2 . VAL A 1 289 ? 0.005   20.226 33.377  1.00 59.73  ? 318 VAL A CG2 1 
ATOM   2201 N  N   . LEU A 1 290 ? -1.924  18.106 31.496  1.00 59.86  ? 319 LEU A N   1 
ATOM   2202 C  CA  . LEU A 1 290 ? -1.995  17.743 30.085  1.00 59.87  ? 319 LEU A CA  1 
ATOM   2203 C  C   . LEU A 1 290 ? -1.841  16.237 29.929  1.00 60.52  ? 319 LEU A C   1 
ATOM   2204 O  O   . LEU A 1 290 ? -0.980  15.646 30.567  1.00 60.73  ? 319 LEU A O   1 
ATOM   2205 C  CB  . LEU A 1 290 ? -0.900  18.493 29.294  1.00 59.39  ? 319 LEU A CB  1 
ATOM   2206 C  CG  . LEU A 1 290 ? -0.663  18.068 27.841  1.00 59.78  ? 319 LEU A CG  1 
ATOM   2207 C  CD1 . LEU A 1 290 ? -1.864  18.374 26.976  1.00 60.20  ? 319 LEU A CD1 1 
ATOM   2208 C  CD2 . LEU A 1 290 ? 0.562   18.743 27.274  1.00 59.92  ? 319 LEU A CD2 1 
ATOM   2209 N  N   . HIS A 1 291 ? -2.684  15.613 29.100  1.00 60.64  ? 320 HIS A N   1 
ATOM   2210 C  CA  . HIS A 1 291 ? -2.612  14.176 28.886  1.00 61.03  ? 320 HIS A CA  1 
ATOM   2211 C  C   . HIS A 1 291 ? -1.994  13.862 27.547  1.00 60.91  ? 320 HIS A C   1 
ATOM   2212 O  O   . HIS A 1 291 ? -2.545  14.215 26.514  1.00 60.93  ? 320 HIS A O   1 
ATOM   2213 C  CB  . HIS A 1 291 ? -3.991  13.522 28.994  1.00 62.13  ? 320 HIS A CB  1 
ATOM   2214 C  CG  . HIS A 1 291 ? -3.937  12.027 29.024  1.00 64.90  ? 320 HIS A CG  1 
ATOM   2215 N  ND1 . HIS A 1 291 ? -3.741  11.336 30.207  1.00 66.77  ? 320 HIS A ND1 1 
ATOM   2216 C  CD2 . HIS A 1 291 ? -4.058  11.135 28.015  1.00 66.37  ? 320 HIS A CD2 1 
ATOM   2217 C  CE1 . HIS A 1 291 ? -3.757  10.052 29.884  1.00 67.40  ? 320 HIS A CE1 1 
ATOM   2218 N  NE2 . HIS A 1 291 ? -3.946  9.882  28.578  1.00 67.68  ? 320 HIS A NE2 1 
ATOM   2219 N  N   . ILE A 1 292 ? -0.850  13.189 27.564  1.00 60.74  ? 321 ILE A N   1 
ATOM   2220 C  CA  . ILE A 1 292 ? -0.172  12.793 26.349  1.00 61.03  ? 321 ILE A CA  1 
ATOM   2221 C  C   . ILE A 1 292 ? -0.610  11.380 25.982  1.00 61.63  ? 321 ILE A C   1 
ATOM   2222 O  O   . ILE A 1 292 ? -0.535  10.477 26.816  1.00 62.08  ? 321 ILE A O   1 
ATOM   2223 C  CB  . ILE A 1 292 ? 1.351   12.884 26.535  1.00 61.31  ? 321 ILE A CB  1 
ATOM   2224 C  CG1 . ILE A 1 292 ? 1.777   14.283 26.991  1.00 61.80  ? 321 ILE A CG1 1 
ATOM   2225 C  CG2 . ILE A 1 292 ? 2.073   12.441 25.264  1.00 61.84  ? 321 ILE A CG2 1 
ATOM   2226 C  CD1 . ILE A 1 292 ? 1.425   15.356 26.039  1.00 63.05  ? 321 ILE A CD1 1 
ATOM   2227 N  N   . GLN A 1 293 ? -1.131  11.212 24.758  1.00 61.06  ? 322 GLN A N   1 
ATOM   2228 C  CA  . GLN A 1 293 ? -1.568  9.931  24.238  1.00 61.04  ? 322 GLN A CA  1 
ATOM   2229 C  C   . GLN A 1 293 ? -0.807  9.666  22.964  1.00 61.11  ? 322 GLN A C   1 
ATOM   2230 O  O   . GLN A 1 293 ? -1.143  10.231 21.929  1.00 60.75  ? 322 GLN A O   1 
ATOM   2231 C  CB  . GLN A 1 293 ? -3.081  9.933  23.953  1.00 62.25  ? 322 GLN A CB  1 
ATOM   2232 C  CG  . GLN A 1 293 ? -3.594  8.658  23.259  1.00 64.89  ? 322 GLN A CG  1 
ATOM   2233 C  CD  . GLN A 1 293 ? -3.393  7.422  24.096  1.00 68.15  ? 322 GLN A CD  1 
ATOM   2234 O  OE1 . GLN A 1 293 ? -4.092  7.218  25.091  1.00 71.05  ? 322 GLN A OE1 1 
ATOM   2235 N  NE2 . GLN A 1 293 ? -2.443  6.571  23.721  1.00 66.67  ? 322 GLN A NE2 1 
ATOM   2236 N  N   . PRO A 1 294 ? 0.227   8.811  23.012  1.00 61.92  ? 323 PRO A N   1 
ATOM   2237 C  CA  . PRO A 1 294 ? 0.970   8.510  21.784  1.00 62.71  ? 323 PRO A CA  1 
ATOM   2238 C  C   . PRO A 1 294 ? 0.122   7.721  20.779  1.00 64.85  ? 323 PRO A C   1 
ATOM   2239 O  O   . PRO A 1 294 ? -0.572  6.764  21.139  1.00 65.03  ? 323 PRO A O   1 
ATOM   2240 C  CB  . PRO A 1 294 ? 2.193   7.721  22.273  1.00 62.80  ? 323 PRO A CB  1 
ATOM   2241 C  CG  . PRO A 1 294 ? 2.184   7.816  23.761  1.00 63.03  ? 323 PRO A CG  1 
ATOM   2242 C  CD  . PRO A 1 294 ? 0.767   8.071  24.170  1.00 61.49  ? 323 PRO A CD  1 
ATOM   2243 N  N   . THR A 1 295 ? 0.159   8.157  19.515  1.00 66.17  ? 324 THR A N   1 
ATOM   2244 C  CA  . THR A 1 295 ? -0.577  7.550  18.400  1.00 67.98  ? 324 THR A CA  1 
ATOM   2245 C  C   . THR A 1 295 ? 0.213   6.340  17.808  1.00 69.12  ? 324 THR A C   1 
ATOM   2246 O  O   . THR A 1 295 ? 1.263   5.982  18.340  1.00 69.48  ? 324 THR A O   1 
ATOM   2247 C  CB  . THR A 1 295 ? -0.855  8.655  17.340  1.00 69.93  ? 324 THR A CB  1 
ATOM   2248 O  OG1 . THR A 1 295 ? 0.367   9.003  16.676  1.00 71.24  ? 324 THR A OG1 1 
ATOM   2249 C  CG2 . THR A 1 295 ? -1.500  9.888  17.935  1.00 70.34  ? 324 THR A CG2 1 
ATOM   2250 N  N   . LEU A 1 296 ? -0.287  5.699  16.734  1.00 69.50  ? 325 LEU A N   1 
ATOM   2251 C  CA  . LEU A 1 296 ? 0.445   4.610  16.094  1.00 70.31  ? 325 LEU A CA  1 
ATOM   2252 C  C   . LEU A 1 296 ? 1.570   5.157  15.187  1.00 71.20  ? 325 LEU A C   1 
ATOM   2253 O  O   . LEU A 1 296 ? 2.610   4.510  15.049  1.00 71.17  ? 325 LEU A O   1 
ATOM   2254 C  CB  . LEU A 1 296 ? -0.512  3.688  15.324  1.00 70.23  ? 325 LEU A CB  1 
ATOM   2255 C  CG  . LEU A 1 296 ? -1.473  2.904  16.200  1.00 71.04  ? 325 LEU A CG  1 
ATOM   2256 C  CD1 . LEU A 1 296 ? -2.438  2.131  15.371  1.00 71.57  ? 325 LEU A CD1 1 
ATOM   2257 C  CD2 . LEU A 1 296 ? -0.733  1.982  17.130  1.00 71.37  ? 325 LEU A CD2 1 
ATOM   2258 N  N   . LYS A 1 297 ? 1.375   6.376  14.617  1.00 71.70  ? 326 LYS A N   1 
ATOM   2259 C  CA  . LYS A 1 297 ? 2.334   7.087  13.752  1.00 72.52  ? 326 LYS A CA  1 
ATOM   2260 C  C   . LYS A 1 297 ? 3.629   7.443  14.508  1.00 72.64  ? 326 LYS A C   1 
ATOM   2261 O  O   . LYS A 1 297 ? 3.652   7.382  15.739  1.00 72.75  ? 326 LYS A O   1 
ATOM   2262 C  CB  . LYS A 1 297 ? 1.685   8.348  13.163  1.00 75.26  ? 326 LYS A CB  1 
ATOM   2263 C  CG  . LYS A 1 297 ? 0.876   8.094  11.904  1.00 81.31  ? 326 LYS A CG  1 
ATOM   2264 C  CD  . LYS A 1 297 ? 0.293   9.395  11.349  1.00 88.10  ? 326 LYS A CD  1 
ATOM   2265 C  CE  . LYS A 1 297 ? -0.076  9.246  9.888   1.00 93.08  ? 326 LYS A CE  1 
ATOM   2266 N  NZ  . LYS A 1 297 ? -0.366  10.557 9.228   1.00 95.43  ? 326 LYS A NZ  1 
ATOM   2267 N  N   . SER A 1 298 ? 4.714   7.782  13.792  1.00 72.73  ? 327 SER A N   1 
ATOM   2268 C  CA  . SER A 1 298 ? 5.986   8.066  14.464  1.00 73.47  ? 327 SER A CA  1 
ATOM   2269 C  C   . SER A 1 298 ? 6.818   9.180  13.830  1.00 73.97  ? 327 SER A C   1 
ATOM   2270 O  O   . SER A 1 298 ? 6.610   9.529  12.672  1.00 74.45  ? 327 SER A O   1 
ATOM   2271 C  CB  . SER A 1 298 ? 6.812   6.786  14.579  1.00 74.92  ? 327 SER A CB  1 
ATOM   2272 O  OG  . SER A 1 298 ? 7.053   6.208  13.306  1.00 77.18  ? 327 SER A OG  1 
ATOM   2273 N  N   . ASN A 1 299 ? 7.767   9.733  14.590  1.00 73.91  ? 328 ASN A N   1 
ATOM   2274 C  CA  . ASN A 1 299 ? 8.666   10.764 14.083  1.00 74.61  ? 328 ASN A CA  1 
ATOM   2275 C  C   . ASN A 1 299 ? 10.152  10.323 14.142  1.00 75.25  ? 328 ASN A C   1 
ATOM   2276 O  O   . ASN A 1 299 ? 10.486  9.339  14.810  1.00 75.09  ? 328 ASN A O   1 
ATOM   2277 C  CB  . ASN A 1 299 ? 8.415   12.130 14.767  1.00 75.49  ? 328 ASN A CB  1 
ATOM   2278 C  CG  . ASN A 1 299 ? 8.732   12.253 16.244  1.00 77.87  ? 328 ASN A CG  1 
ATOM   2279 O  OD1 . ASN A 1 299 ? 9.428   11.440 16.857  1.00 79.21  ? 328 ASN A OD1 1 
ATOM   2280 N  ND2 . ASN A 1 299 ? 8.243   13.311 16.846  1.00 78.08  ? 328 ASN A ND2 1 
ATOM   2281 N  N   . GLU A 1 300 ? 11.037  11.037 13.432  1.00 75.79  ? 329 GLU A N   1 
ATOM   2282 C  CA  . GLU A 1 300 ? 12.457  10.688 13.414  1.00 76.80  ? 329 GLU A CA  1 
ATOM   2283 C  C   . GLU A 1 300 ? 13.318  11.551 14.351  1.00 76.89  ? 329 GLU A C   1 
ATOM   2284 O  O   . GLU A 1 300 ? 14.524  11.658 14.129  1.00 77.09  ? 329 GLU A O   1 
ATOM   2285 C  CB  . GLU A 1 300 ? 13.016  10.719 11.982  1.00 79.96  ? 329 GLU A CB  1 
ATOM   2286 C  CG  . GLU A 1 300 ? 12.316  9.767  11.028  1.00 87.72  ? 329 GLU A CG  1 
ATOM   2287 C  CD  . GLU A 1 300 ? 11.262  10.423 10.152  1.00 98.59  ? 329 GLU A CD  1 
ATOM   2288 O  OE1 . GLU A 1 300 ? 10.599  11.375 10.627  1.00 101.52 ? 329 GLU A OE1 1 
ATOM   2289 O  OE2 . GLU A 1 300 ? 11.098  9.986  8.987   1.00 101.36 ? 329 GLU A OE2 1 
ATOM   2290 N  N   . ALA A 1 301 ? 12.711  12.166 15.387  1.00 76.46  ? 330 ALA A N   1 
ATOM   2291 C  CA  . ALA A 1 301 ? 13.442  13.001 16.345  1.00 76.56  ? 330 ALA A CA  1 
ATOM   2292 C  C   . ALA A 1 301 ? 14.476  12.185 17.124  1.00 77.03  ? 330 ALA A C   1 
ATOM   2293 O  O   . ALA A 1 301 ? 14.319  10.963 17.236  1.00 77.40  ? 330 ALA A O   1 
ATOM   2294 C  CB  . ALA A 1 301 ? 12.476  13.673 17.297  1.00 76.48  ? 330 ALA A CB  1 
ATOM   2295 N  N   . LYS A 1 302 ? 15.533  12.837 17.661  1.00 76.92  ? 331 LYS A N   1 
ATOM   2296 C  CA  . LYS A 1 302 ? 16.581  12.072 18.341  1.00 77.36  ? 331 LYS A CA  1 
ATOM   2297 C  C   . LYS A 1 302 ? 16.950  12.450 19.788  1.00 77.47  ? 331 LYS A C   1 
ATOM   2298 O  O   . LYS A 1 302 ? 17.480  11.588 20.491  1.00 77.84  ? 331 LYS A O   1 
ATOM   2299 C  CB  . LYS A 1 302 ? 17.871  12.096 17.508  1.00 79.05  ? 331 LYS A CB  1 
ATOM   2300 C  CG  . LYS A 1 302 ? 18.119  10.829 16.709  1.00 82.75  ? 331 LYS A CG  1 
ATOM   2301 C  CD  . LYS A 1 302 ? 17.606  10.965 15.291  1.00 87.52  ? 331 LYS A CD  1 
ATOM   2302 C  CE  . LYS A 1 302 ? 17.289  9.625  14.666  1.00 91.82  ? 331 LYS A CE  1 
ATOM   2303 N  NZ  . LYS A 1 302 ? 16.113  8.951  15.305  1.00 93.86  ? 331 LYS A NZ  1 
ATOM   2304 N  N   . LEU A 1 303 ? 16.764  13.705 20.214  1.00 77.00  ? 332 LEU A N   1 
ATOM   2305 C  CA  . LEU A 1 303 ? 17.247  14.181 21.519  1.00 77.33  ? 332 LEU A CA  1 
ATOM   2306 C  C   . LEU A 1 303 ? 18.783  14.173 21.444  1.00 78.35  ? 332 LEU A C   1 
ATOM   2307 O  O   . LEU A 1 303 ? 19.423  13.196 21.836  1.00 78.56  ? 332 LEU A O   1 
ATOM   2308 C  CB  . LEU A 1 303 ? 16.752  13.349 22.719  1.00 76.99  ? 332 LEU A CB  1 
ATOM   2309 C  CG  . LEU A 1 303 ? 17.326  13.776 24.079  1.00 77.73  ? 332 LEU A CG  1 
ATOM   2310 C  CD1 . LEU A 1 303 ? 16.345  14.600 24.865  1.00 77.97  ? 332 LEU A CD1 1 
ATOM   2311 C  CD2 . LEU A 1 303 ? 17.767  12.594 24.879  1.00 78.12  ? 332 LEU A CD2 1 
ATOM   2312 N  N   . PRO A 1 304 ? 19.374  15.189 20.794  1.00 78.79  ? 333 PRO A N   1 
ATOM   2313 C  CA  . PRO A 1 304 ? 20.829  15.176 20.581  1.00 79.26  ? 333 PRO A CA  1 
ATOM   2314 C  C   . PRO A 1 304 ? 21.691  15.220 21.836  1.00 79.88  ? 333 PRO A C   1 
ATOM   2315 O  O   . PRO A 1 304 ? 21.272  15.725 22.866  1.00 79.97  ? 333 PRO A O   1 
ATOM   2316 C  CB  . PRO A 1 304 ? 21.074  16.392 19.684  1.00 80.04  ? 333 PRO A CB  1 
ATOM   2317 C  CG  . PRO A 1 304 ? 19.893  17.259 19.859  1.00 80.34  ? 333 PRO A CG  1 
ATOM   2318 C  CD  . PRO A 1 304 ? 18.740  16.372 20.185  1.00 78.46  ? 333 PRO A CD  1 
ATOM   2319 N  N   . ASP A 1 305 ? 22.902  14.675 21.735  1.00 80.32  ? 334 ASP A N   1 
ATOM   2320 C  CA  . ASP A 1 305 ? 23.860  14.630 22.834  1.00 81.36  ? 334 ASP A CA  1 
ATOM   2321 C  C   . ASP A 1 305 ? 24.281  16.049 23.243  1.00 81.83  ? 334 ASP A C   1 
ATOM   2322 O  O   . ASP A 1 305 ? 24.393  16.355 24.429  1.00 81.76  ? 334 ASP A O   1 
ATOM   2323 C  CB  . ASP A 1 305 ? 25.077  13.789 22.418  1.00 83.50  ? 334 ASP A CB  1 
ATOM   2324 C  CG  . ASP A 1 305 ? 24.730  12.329 22.207  1.00 89.16  ? 334 ASP A CG  1 
ATOM   2325 O  OD1 . ASP A 1 305 ? 23.949  11.783 23.017  1.00 90.23  ? 334 ASP A OD1 1 
ATOM   2326 O  OD2 . ASP A 1 305 ? 25.235  11.729 21.224  1.00 91.57  ? 334 ASP A OD2 1 
ATOM   2327 N  N   . ALA A 1 306 ? 24.499  16.910 22.248  1.00 81.97  ? 335 ALA A N   1 
ATOM   2328 C  CA  . ALA A 1 306 ? 24.855  18.310 22.439  1.00 82.32  ? 335 ALA A CA  1 
ATOM   2329 C  C   . ALA A 1 306 ? 23.865  19.153 21.627  1.00 82.77  ? 335 ALA A C   1 
ATOM   2330 O  O   . ALA A 1 306 ? 23.539  18.794 20.492  1.00 82.60  ? 335 ALA A O   1 
ATOM   2331 C  CB  . ALA A 1 306 ? 26.275  18.561 21.960  1.00 82.27  ? 335 ALA A CB  1 
ATOM   2332 N  N   . LEU A 1 307 ? 23.371  20.250 22.203  1.00 83.16  ? 336 LEU A N   1 
ATOM   2333 C  CA  . LEU A 1 307 ? 22.405  21.104 21.520  1.00 84.27  ? 336 LEU A CA  1 
ATOM   2334 C  C   . LEU A 1 307 ? 23.081  22.281 20.761  1.00 85.38  ? 336 LEU A C   1 
ATOM   2335 O  O   . LEU A 1 307 ? 23.222  22.221 19.544  1.00 85.55  ? 336 LEU A O   1 
ATOM   2336 C  CB  . LEU A 1 307 ? 21.304  21.573 22.499  1.00 84.42  ? 336 LEU A CB  1 
ATOM   2337 C  CG  . LEU A 1 307 ? 20.672  20.482 23.361  1.00 85.61  ? 336 LEU A CG  1 
ATOM   2338 C  CD1 . LEU A 1 307 ? 20.040  21.059 24.601  1.00 85.88  ? 336 LEU A CD1 1 
ATOM   2339 C  CD2 . LEU A 1 307 ? 19.686  19.672 22.566  1.00 86.25  ? 336 LEU A CD2 1 
ATOM   2340 N  N   . VAL A 1 308 ? 23.517  23.328 21.463  1.00 85.97  ? 337 VAL A N   1 
ATOM   2341 C  CA  . VAL A 1 308 ? 24.177  24.482 20.850  1.00 86.90  ? 337 VAL A CA  1 
ATOM   2342 C  C   . VAL A 1 308 ? 25.467  24.813 21.633  1.00 88.29  ? 337 VAL A C   1 
ATOM   2343 O  O   . VAL A 1 308 ? 25.664  24.301 22.747  1.00 88.45  ? 337 VAL A O   1 
ATOM   2344 C  CB  . VAL A 1 308 ? 23.222  25.708 20.816  1.00 87.19  ? 337 VAL A CB  1 
ATOM   2345 C  CG1 . VAL A 1 308 ? 22.025  25.472 19.900  1.00 87.62  ? 337 VAL A CG1 1 
ATOM   2346 C  CG2 . VAL A 1 308 ? 22.769  26.086 22.220  1.00 87.43  ? 337 VAL A CG2 1 
ATOM   2347 N  N   . ASN A 1 309 ? 26.347  25.669 21.064  1.00 89.10  ? 338 ASN A N   1 
ATOM   2348 C  CA  . ASN A 1 309 ? 27.553  26.060 21.789  1.00 90.24  ? 338 ASN A CA  1 
ATOM   2349 C  C   . ASN A 1 309 ? 27.177  27.092 22.845  1.00 90.38  ? 338 ASN A C   1 
ATOM   2350 O  O   . ASN A 1 309 ? 27.082  28.283 22.538  1.00 90.54  ? 338 ASN A O   1 
ATOM   2351 C  CB  . ASN A 1 309 ? 28.659  26.592 20.876  1.00 92.33  ? 338 ASN A CB  1 
ATOM   2352 C  CG  . ASN A 1 309 ? 29.849  27.141 21.654  1.00 97.32  ? 338 ASN A CG  1 
ATOM   2353 O  OD1 . ASN A 1 309 ? 30.336  26.529 22.626  1.00 98.45  ? 338 ASN A OD1 1 
ATOM   2354 N  ND2 . ASN A 1 309 ? 30.301  28.338 21.273  1.00 98.72  ? 338 ASN A ND2 1 
ATOM   2355 N  N   . MET A 1 310 ? 26.953  26.627 24.082  1.00 90.02  ? 339 MET A N   1 
ATOM   2356 C  CA  . MET A 1 310 ? 26.650  27.515 25.187  1.00 89.76  ? 339 MET A CA  1 
ATOM   2357 C  C   . MET A 1 310 ? 27.958  28.153 25.599  1.00 89.92  ? 339 MET A C   1 
ATOM   2358 O  O   . MET A 1 310 ? 28.895  27.453 25.985  1.00 90.15  ? 339 MET A O   1 
ATOM   2359 C  CB  . MET A 1 310 ? 26.055  26.748 26.369  1.00 89.83  ? 339 MET A CB  1 
ATOM   2360 C  CG  . MET A 1 310 ? 25.752  27.635 27.551  1.00 91.25  ? 339 MET A CG  1 
ATOM   2361 S  SD  . MET A 1 310 ? 24.559  28.936 27.165  1.00 93.04  ? 339 MET A SD  1 
ATOM   2362 C  CE  . MET A 1 310 ? 23.147  27.979 26.892  1.00 91.17  ? 339 MET A CE  1 
ATOM   2363 N  N   . PRO A 1 311 ? 28.062  29.480 25.477  1.00 89.59  ? 340 PRO A N   1 
ATOM   2364 C  CA  . PRO A 1 311 ? 29.319  30.142 25.834  1.00 89.37  ? 340 PRO A CA  1 
ATOM   2365 C  C   . PRO A 1 311 ? 29.630  30.067 27.318  1.00 89.27  ? 340 PRO A C   1 
ATOM   2366 O  O   . PRO A 1 311 ? 28.728  29.882 28.139  1.00 89.44  ? 340 PRO A O   1 
ATOM   2367 C  CB  . PRO A 1 311 ? 29.091  31.594 25.398  1.00 90.17  ? 340 PRO A CB  1 
ATOM   2368 C  CG  . PRO A 1 311 ? 27.887  31.567 24.511  1.00 90.66  ? 340 PRO A CG  1 
ATOM   2369 C  CD  . PRO A 1 311 ? 27.052  30.450 25.020  1.00 89.02  ? 340 PRO A CD  1 
ATOM   2370 N  N   . ALA A 1 312 ? 30.908  30.214 27.665  1.00 88.99  ? 341 ALA A N   1 
ATOM   2371 C  CA  . ALA A 1 312 ? 31.306  30.227 29.069  1.00 89.34  ? 341 ALA A CA  1 
ATOM   2372 C  C   . ALA A 1 312 ? 30.847  31.539 29.706  1.00 89.42  ? 341 ALA A C   1 
ATOM   2373 O  O   . ALA A 1 312 ? 30.670  32.537 29.002  1.00 89.51  ? 341 ALA A O   1 
ATOM   2374 C  CB  . ALA A 1 312 ? 32.811  30.101 29.176  1.00 89.59  ? 341 ALA A CB  1 
ATOM   2375 N  N   . VAL A 1 313 ? 30.631  31.543 31.020  1.00 89.36  ? 342 VAL A N   1 
ATOM   2376 C  CA  . VAL A 1 313 ? 30.207  32.764 31.701  1.00 89.95  ? 342 VAL A CA  1 
ATOM   2377 C  C   . VAL A 1 313 ? 31.432  33.638 31.930  1.00 91.21  ? 342 VAL A C   1 
ATOM   2378 O  O   . VAL A 1 313 ? 32.381  33.213 32.592  1.00 91.42  ? 342 VAL A O   1 
ATOM   2379 C  CB  . VAL A 1 313 ? 29.440  32.510 33.013  1.00 90.03  ? 342 VAL A CB  1 
ATOM   2380 C  CG1 . VAL A 1 313 ? 28.762  33.790 33.493  1.00 90.37  ? 342 VAL A CG1 1 
ATOM   2381 C  CG2 . VAL A 1 313 ? 28.420  31.390 32.846  1.00 90.37  ? 342 VAL A CG2 1 
ATOM   2382 N  N   . PRO A 1 314 ? 31.454  34.850 31.348  1.00 91.76  ? 343 PRO A N   1 
ATOM   2383 C  CA  . PRO A 1 314 ? 32.616  35.722 31.534  1.00 92.14  ? 343 PRO A CA  1 
ATOM   2384 C  C   . PRO A 1 314 ? 32.745  36.171 32.976  1.00 93.19  ? 343 PRO A C   1 
ATOM   2385 O  O   . PRO A 1 314 ? 31.741  36.513 33.609  1.00 93.18  ? 343 PRO A O   1 
ATOM   2386 C  CB  . PRO A 1 314 ? 32.330  36.920 30.620  1.00 92.59  ? 343 PRO A CB  1 
ATOM   2387 C  CG  . PRO A 1 314 ? 31.177  36.540 29.782  1.00 93.00  ? 343 PRO A CG  1 
ATOM   2388 C  CD  . PRO A 1 314 ? 30.415  35.493 30.525  1.00 91.47  ? 343 PRO A CD  1 
ATOM   2389 N  N   . ALA A 1 315 ? 33.979  36.146 33.500  1.00 93.94  ? 344 ALA A N   1 
ATOM   2390 C  CA  . ALA A 1 315 ? 34.251  36.602 34.856  1.00 95.04  ? 344 ALA A CA  1 
ATOM   2391 C  C   . ALA A 1 315 ? 34.265  38.124 34.776  1.00 95.77  ? 344 ALA A C   1 
ATOM   2392 O  O   . ALA A 1 315 ? 35.227  38.701 34.285  1.00 96.13  ? 344 ALA A O   1 
ATOM   2393 C  CB  . ALA A 1 315 ? 35.596  36.072 35.321  1.00 95.26  ? 344 ALA A CB  1 
ATOM   2394 N  N   . ALA A 1 316 ? 33.172  38.764 35.197  1.00 95.92  ? 345 ALA A N   1 
ATOM   2395 C  CA  . ALA A 1 316 ? 32.973  40.208 35.117  1.00 96.59  ? 345 ALA A CA  1 
ATOM   2396 C  C   . ALA A 1 316 ? 34.186  41.044 35.551  1.00 96.88  ? 345 ALA A C   1 
ATOM   2397 O  O   . ALA A 1 316 ? 34.647  41.897 34.792  1.00 97.21  ? 345 ALA A O   1 
ATOM   2398 C  CB  . ALA A 1 316 ? 31.726  40.600 35.908  1.00 96.94  ? 345 ALA A CB  1 
ATOM   2399 N  N   . ASP A 1 317 ? 34.746  40.708 36.720  1.00 96.56  ? 346 ASP A N   1 
ATOM   2400 C  CA  . ASP A 1 317 ? 35.856  41.308 37.445  1.00 96.50  ? 346 ASP A CA  1 
ATOM   2401 C  C   . ASP A 1 317 ? 35.634  42.790 37.728  1.00 95.77  ? 346 ASP A C   1 
ATOM   2402 O  O   . ASP A 1 317 ? 35.408  43.116 38.884  1.00 95.98  ? 346 ASP A O   1 
ATOM   2403 C  CB  . ASP A 1 317 ? 37.241  41.022 36.827  1.00 98.14  ? 346 ASP A CB  1 
ATOM   2404 C  CG  . ASP A 1 317 ? 37.844  39.692 37.277  1.00 101.78 ? 346 ASP A CG  1 
ATOM   2405 O  OD1 . ASP A 1 317 ? 37.128  38.900 37.944  1.00 102.13 ? 346 ASP A OD1 1 
ATOM   2406 O  OD2 . ASP A 1 317 ? 39.023  39.439 36.958  1.00 103.57 ? 346 ASP A OD2 1 
ATOM   2407 N  N   . ASN A 1 318 ? 35.680  43.680 36.719  1.00 94.79  ? 347 ASN A N   1 
ATOM   2408 C  CA  . ASN A 1 318 ? 35.487  45.105 36.961  1.00 94.41  ? 347 ASN A CA  1 
ATOM   2409 C  C   . ASN A 1 318 ? 34.292  45.673 36.193  1.00 92.99  ? 347 ASN A C   1 
ATOM   2410 O  O   . ASN A 1 318 ? 34.469  46.444 35.243  1.00 93.02  ? 347 ASN A O   1 
ATOM   2411 C  CB  . ASN A 1 318 ? 36.761  45.902 36.642  1.00 96.36  ? 347 ASN A CB  1 
ATOM   2412 C  CG  . ASN A 1 318 ? 38.035  45.299 37.174  1.00 100.62 ? 347 ASN A CG  1 
ATOM   2413 O  OD1 . ASN A 1 318 ? 38.372  45.426 38.363  1.00 101.69 ? 347 ASN A OD1 1 
ATOM   2414 N  ND2 . ASN A 1 318 ? 38.769  44.629 36.289  1.00 101.75 ? 347 ASN A ND2 1 
ATOM   2415 N  N   . VAL A 1 319 ? 33.069  45.303 36.594  1.00 91.46  ? 348 VAL A N   1 
ATOM   2416 C  CA  . VAL A 1 319 ? 31.863  45.837 35.953  1.00 90.29  ? 348 VAL A CA  1 
ATOM   2417 C  C   . VAL A 1 319 ? 31.029  46.623 36.973  1.00 88.90  ? 348 VAL A C   1 
ATOM   2418 O  O   . VAL A 1 319 ? 31.230  46.475 38.184  1.00 88.97  ? 348 VAL A O   1 
ATOM   2419 C  CB  . VAL A 1 319 ? 31.026  44.742 35.260  1.00 90.85  ? 348 VAL A CB  1 
ATOM   2420 C  CG1 . VAL A 1 319 ? 31.847  43.988 34.224  1.00 91.30  ? 348 VAL A CG1 1 
ATOM   2421 C  CG2 . VAL A 1 319 ? 30.430  43.793 36.288  1.00 91.35  ? 348 VAL A CG2 1 
ATOM   2422 N  N   . LYS A 1 320 ? 30.109  47.471 36.493  1.00 87.53  ? 349 LYS A N   1 
ATOM   2423 C  CA  . LYS A 1 320 ? 29.269  48.240 37.401  1.00 86.80  ? 349 LYS A CA  1 
ATOM   2424 C  C   . LYS A 1 320 ? 28.258  47.311 38.060  1.00 86.22  ? 349 LYS A C   1 
ATOM   2425 O  O   . LYS A 1 320 ? 27.517  46.620 37.370  1.00 86.37  ? 349 LYS A O   1 
ATOM   2426 C  CB  . LYS A 1 320 ? 28.585  49.416 36.677  1.00 87.81  ? 349 LYS A CB  1 
ATOM   2427 C  CG  . LYS A 1 320 ? 27.660  50.258 37.561  1.00 91.02  ? 349 LYS A CG  1 
ATOM   2428 C  CD  . LYS A 1 320 ? 28.354  50.854 38.792  1.00 94.67  ? 349 LYS A CD  1 
ATOM   2429 C  CE  . LYS A 1 320 ? 27.387  51.567 39.708  1.00 97.59  ? 349 LYS A CE  1 
ATOM   2430 N  NZ  . LYS A 1 320 ? 26.877  52.823 39.093  1.00 99.67  ? 349 LYS A NZ  1 
ATOM   2431 N  N   . THR A 1 321 ? 28.279  47.235 39.389  1.00 85.56  ? 350 THR A N   1 
ATOM   2432 C  CA  . THR A 1 321 ? 27.328  46.396 40.115  1.00 85.47  ? 350 THR A CA  1 
ATOM   2433 C  C   . THR A 1 321 ? 26.011  47.151 40.368  1.00 85.30  ? 350 THR A C   1 
ATOM   2434 O  O   . THR A 1 321 ? 25.978  48.381 40.292  1.00 85.58  ? 350 THR A O   1 
ATOM   2435 C  CB  . THR A 1 321 ? 27.937  45.858 41.415  1.00 86.33  ? 350 THR A CB  1 
ATOM   2436 O  OG1 . THR A 1 321 ? 27.975  46.901 42.392  1.00 87.02  ? 350 THR A OG1 1 
ATOM   2437 C  CG2 . THR A 1 321 ? 29.317  45.248 41.206  1.00 86.64  ? 350 THR A CG2 1 
ATOM   2438 N  N   . ARG A 1 322 ? 24.925  46.420 40.657  1.00 84.51  ? 351 ARG A N   1 
ATOM   2439 C  CA  . ARG A 1 322 ? 23.644  47.053 40.966  1.00 84.15  ? 351 ARG A CA  1 
ATOM   2440 C  C   . ARG A 1 322 ? 23.015  46.384 42.163  1.00 84.21  ? 351 ARG A C   1 
ATOM   2441 O  O   . ARG A 1 322 ? 23.177  45.178 42.355  1.00 84.52  ? 351 ARG A O   1 
ATOM   2442 C  CB  . ARG A 1 322 ? 22.658  46.963 39.796  1.00 84.58  ? 351 ARG A CB  1 
ATOM   2443 C  CG  . ARG A 1 322 ? 23.117  47.623 38.519  1.00 86.54  ? 351 ARG A CG  1 
ATOM   2444 C  CD  . ARG A 1 322 ? 23.207  49.131 38.590  1.00 88.36  ? 351 ARG A CD  1 
ATOM   2445 N  NE  . ARG A 1 322 ? 23.774  49.650 37.345  1.00 89.70  ? 351 ARG A NE  1 
ATOM   2446 C  CZ  . ARG A 1 322 ? 24.037  50.929 37.109  1.00 90.74  ? 351 ARG A CZ  1 
ATOM   2447 N  NH1 . ARG A 1 322 ? 23.788  51.848 38.036  1.00 90.04  ? 351 ARG A NH1 1 
ATOM   2448 N  NH2 . ARG A 1 322 ? 24.551  51.302 35.946  1.00 90.22  ? 351 ARG A NH2 1 
ATOM   2449 N  N   . TRP A 1 323 ? 22.275  47.154 42.959  1.00 83.88  ? 352 TRP A N   1 
ATOM   2450 C  CA  . TRP A 1 323 ? 21.557  46.582 44.083  1.00 84.14  ? 352 TRP A CA  1 
ATOM   2451 C  C   . TRP A 1 323 ? 20.101  46.962 44.009  1.00 84.06  ? 352 TRP A C   1 
ATOM   2452 O  O   . TRP A 1 323 ? 19.748  48.140 44.075  1.00 83.87  ? 352 TRP A O   1 
ATOM   2453 C  CB  . TRP A 1 323 ? 22.158  46.949 45.441  1.00 84.17  ? 352 TRP A CB  1 
ATOM   2454 C  CG  . TRP A 1 323 ? 21.552  46.163 46.566  1.00 84.63  ? 352 TRP A CG  1 
ATOM   2455 C  CD1 . TRP A 1 323 ? 20.361  46.399 47.188  1.00 85.55  ? 352 TRP A CD1 1 
ATOM   2456 C  CD2 . TRP A 1 323 ? 22.098  44.989 47.174  1.00 84.80  ? 352 TRP A CD2 1 
ATOM   2457 N  NE1 . TRP A 1 323 ? 20.128  45.437 48.144  1.00 85.88  ? 352 TRP A NE1 1 
ATOM   2458 C  CE2 . TRP A 1 323 ? 21.193  44.575 48.174  1.00 85.57  ? 352 TRP A CE2 1 
ATOM   2459 C  CE3 . TRP A 1 323 ? 23.272  44.256 46.983  1.00 85.46  ? 352 TRP A CE3 1 
ATOM   2460 C  CZ2 . TRP A 1 323 ? 21.430  43.465 48.979  1.00 86.19  ? 352 TRP A CZ2 1 
ATOM   2461 C  CZ3 . TRP A 1 323 ? 23.511  43.162 47.792  1.00 86.36  ? 352 TRP A CZ3 1 
ATOM   2462 C  CH2 . TRP A 1 323 ? 22.586  42.764 48.760  1.00 86.42  ? 352 TRP A CH2 1 
ATOM   2463 N  N   . LEU A 1 324 ? 19.253  45.951 43.858  1.00 83.95  ? 353 LEU A N   1 
ATOM   2464 C  CA  . LEU A 1 324 ? 17.823  46.141 43.800  1.00 84.21  ? 353 LEU A CA  1 
ATOM   2465 C  C   . LEU A 1 324 ? 17.231  45.395 44.982  1.00 84.50  ? 353 LEU A C   1 
ATOM   2466 O  O   . LEU A 1 324 ? 17.164  44.181 44.969  1.00 84.35  ? 353 LEU A O   1 
ATOM   2467 C  CB  . LEU A 1 324 ? 17.254  45.612 42.472  1.00 84.27  ? 353 LEU A CB  1 
ATOM   2468 C  CG  . LEU A 1 324 ? 17.966  46.061 41.188  1.00 85.38  ? 353 LEU A CG  1 
ATOM   2469 C  CD1 . LEU A 1 324 ? 17.315  45.456 39.975  1.00 85.85  ? 353 LEU A CD1 1 
ATOM   2470 C  CD2 . LEU A 1 324 ? 17.995  47.571 41.057  1.00 85.88  ? 353 LEU A CD2 1 
ATOM   2471 N  N   . GLN A 1 325 ? 16.863  46.118 46.024  1.00 84.88  ? 354 GLN A N   1 
ATOM   2472 C  CA  . GLN A 1 325 ? 16.286  45.540 47.220  1.00 85.98  ? 354 GLN A CA  1 
ATOM   2473 C  C   . GLN A 1 325 ? 14.764  45.617 47.120  1.00 86.49  ? 354 GLN A C   1 
ATOM   2474 O  O   . GLN A 1 325 ? 14.189  46.706 47.118  1.00 86.77  ? 354 GLN A O   1 
ATOM   2475 C  CB  . GLN A 1 325 ? 16.845  46.249 48.482  1.00 87.99  ? 354 GLN A CB  1 
ATOM   2476 C  CG  . GLN A 1 325 ? 15.966  46.239 49.746  1.00 92.23  ? 354 GLN A CG  1 
ATOM   2477 C  CD  . GLN A 1 325 ? 15.922  44.921 50.494  1.00 97.69  ? 354 GLN A CD  1 
ATOM   2478 O  OE1 . GLN A 1 325 ? 16.685  43.988 50.220  1.00 99.51  ? 354 GLN A OE1 1 
ATOM   2479 N  NE2 . GLN A 1 325 ? 15.031  44.825 51.479  1.00 98.37  ? 354 GLN A NE2 1 
ATOM   2480 N  N   . LEU A 1 326 ? 14.123  44.458 46.992  1.00 86.38  ? 355 LEU A N   1 
ATOM   2481 C  CA  . LEU A 1 326 ? 12.670  44.374 46.919  1.00 86.98  ? 355 LEU A CA  1 
ATOM   2482 C  C   . LEU A 1 326 ? 12.146  44.438 48.340  1.00 88.41  ? 355 LEU A C   1 
ATOM   2483 O  O   . LEU A 1 326 ? 12.709  43.798 49.233  1.00 88.71  ? 355 LEU A O   1 
ATOM   2484 C  CB  . LEU A 1 326 ? 12.229  43.048 46.293  1.00 86.75  ? 355 LEU A CB  1 
ATOM   2485 C  CG  . LEU A 1 326 ? 12.977  42.593 45.059  1.00 87.81  ? 355 LEU A CG  1 
ATOM   2486 C  CD1 . LEU A 1 326 ? 12.543  41.216 44.656  1.00 88.17  ? 355 LEU A CD1 1 
ATOM   2487 C  CD2 . LEU A 1 326 ? 12.829  43.588 43.926  1.00 88.38  ? 355 LEU A CD2 1 
ATOM   2488 N  N   . MET A 1 327 ? 11.082  45.210 48.573  1.00 89.15  ? 356 MET A N   1 
ATOM   2489 C  CA  . MET A 1 327 ? 10.524  45.344 49.915  1.00 90.25  ? 356 MET A CA  1 
ATOM   2490 C  C   . MET A 1 327 ? 9.012   45.358 49.942  1.00 91.19  ? 356 MET A C   1 
ATOM   2491 O  O   . MET A 1 327 ? 8.373   46.185 49.292  1.00 90.97  ? 356 MET A O   1 
ATOM   2492 C  CB  . MET A 1 327 ? 10.992  46.636 50.609  1.00 90.91  ? 356 MET A CB  1 
ATOM   2493 C  CG  . MET A 1 327 ? 12.424  47.034 50.361  1.00 92.53  ? 356 MET A CG  1 
ATOM   2494 S  SD  . MET A 1 327 ? 12.559  48.822 50.137  1.00 94.51  ? 356 MET A SD  1 
ATOM   2495 C  CE  . MET A 1 327 ? 11.906  49.402 51.714  1.00 91.83  ? 356 MET A CE  1 
ATOM   2496 N  N   . MET A 1 328 ? 8.447   44.508 50.784  1.00 92.02  ? 357 MET A N   1 
ATOM   2497 C  CA  . MET A 1 328 ? 7.018   44.495 51.041  1.00 93.30  ? 357 MET A CA  1 
ATOM   2498 C  C   . MET A 1 328 ? 6.914   44.945 52.514  1.00 95.28  ? 357 MET A C   1 
ATOM   2499 O  O   . MET A 1 328 ? 6.402   44.212 53.361  1.00 95.63  ? 357 MET A O   1 
ATOM   2500 C  CB  . MET A 1 328 ? 6.458   43.076 50.878  1.00 93.18  ? 357 MET A CB  1 
ATOM   2501 C  CG  . MET A 1 328 ? 6.810   42.417 49.591  1.00 93.84  ? 357 MET A CG  1 
ATOM   2502 S  SD  . MET A 1 328 ? 6.059   40.786 49.516  1.00 92.93  ? 357 MET A SD  1 
ATOM   2503 C  CE  . MET A 1 328 ? 4.336   41.214 49.421  1.00 90.13  ? 357 MET A CE  1 
ATOM   2504 N  N   . ASP A 1 329 ? 7.465   46.130 52.832  1.00 96.16  ? 358 ASP A N   1 
ATOM   2505 C  CA  . ASP A 1 329 ? 7.501   46.611 54.211  1.00 97.23  ? 358 ASP A CA  1 
ATOM   2506 C  C   . ASP A 1 329 ? 6.596   47.821 54.433  1.00 97.21  ? 358 ASP A C   1 
ATOM   2507 O  O   . ASP A 1 329 ? 6.508   48.702 53.571  1.00 97.51  ? 358 ASP A O   1 
ATOM   2508 C  CB  . ASP A 1 329 ? 8.962   46.936 54.608  1.00 100.16 ? 358 ASP A CB  1 
ATOM   2509 C  CG  . ASP A 1 329 ? 9.247   47.053 56.104  1.00 106.72 ? 358 ASP A CG  1 
ATOM   2510 O  OD1 . ASP A 1 329 ? 8.858   46.125 56.868  1.00 107.58 ? 358 ASP A OD1 1 
ATOM   2511 O  OD2 . ASP A 1 329 ? 9.884   48.057 56.512  1.00 109.54 ? 358 ASP A OD2 1 
ATOM   2512 N  N   . GLY A 1 330 A 5.936   47.834 55.589  1.00 96.68  ? 358 GLY A N   1 
ATOM   2513 C  CA  . GLY A 1 330 A 5.071   48.916 56.035  1.00 96.81  ? 358 GLY A CA  1 
ATOM   2514 C  C   . GLY A 1 330 A 3.948   49.319 55.103  1.00 96.63  ? 358 GLY A C   1 
ATOM   2515 O  O   . GLY A 1 330 A 2.865   48.729 55.141  1.00 96.77  ? 358 GLY A O   1 
ATOM   2516 N  N   . GLY A 1 331 B 4.207   50.351 54.298  1.00 95.93  ? 358 GLY A N   1 
ATOM   2517 C  CA  . GLY A 1 331 B 3.241   50.914 53.365  1.00 95.56  ? 358 GLY A CA  1 
ATOM   2518 C  C   . GLY A 1 331 B 2.824   49.980 52.252  1.00 94.83  ? 358 GLY A C   1 
ATOM   2519 O  O   . GLY A 1 331 B 1.628   49.847 51.969  1.00 94.85  ? 358 GLY A O   1 
ATOM   2520 N  N   . GLY A 1 332 ? 3.803   49.337 51.622  1.00 93.90  ? 431 GLY A N   1 
ATOM   2521 C  CA  . GLY A 1 332 ? 3.501   48.421 50.531  1.00 93.58  ? 431 GLY A CA  1 
ATOM   2522 C  C   . GLY A 1 332 ? 4.680   47.830 49.787  1.00 92.92  ? 431 GLY A C   1 
ATOM   2523 O  O   . GLY A 1 332 ? 5.706   47.487 50.386  1.00 93.32  ? 431 GLY A O   1 
ATOM   2524 N  N   . ASN A 1 333 ? 4.509   47.653 48.459  1.00 91.51  ? 432 ASN A N   1 
ATOM   2525 C  CA  . ASN A 1 333 ? 5.522   47.068 47.585  1.00 90.47  ? 432 ASN A CA  1 
ATOM   2526 C  C   . ASN A 1 333 ? 6.400   48.151 46.960  1.00 89.34  ? 432 ASN A C   1 
ATOM   2527 O  O   . ASN A 1 333 ? 5.886   49.115 46.392  1.00 89.48  ? 432 ASN A O   1 
ATOM   2528 C  CB  . ASN A 1 333 ? 4.867   46.192 46.518  1.00 91.23  ? 432 ASN A CB  1 
ATOM   2529 C  CG  . ASN A 1 333 ? 4.238   44.940 47.080  1.00 94.03  ? 432 ASN A CG  1 
ATOM   2530 O  OD1 . ASN A 1 333 ? 4.919   44.090 47.638  1.00 95.11  ? 432 ASN A OD1 1 
ATOM   2531 N  ND2 . ASN A 1 333 ? 2.925   44.790 46.948  1.00 94.45  ? 432 ASN A ND2 1 
ATOM   2532 N  N   . LYS A 1 334 ? 7.726   48.015 47.102  1.00 88.09  ? 433 LYS A N   1 
ATOM   2533 C  CA  . LYS A 1 334 ? 8.682   48.995 46.581  1.00 87.42  ? 433 LYS A CA  1 
ATOM   2534 C  C   . LYS A 1 334 ? 10.070  48.386 46.302  1.00 86.60  ? 433 LYS A C   1 
ATOM   2535 O  O   . LYS A 1 334 ? 10.384  47.315 46.806  1.00 86.74  ? 433 LYS A O   1 
ATOM   2536 C  CB  . LYS A 1 334 ? 8.794   50.224 47.525  1.00 88.88  ? 433 LYS A CB  1 
ATOM   2537 C  CG  . LYS A 1 334 ? 8.592   49.954 49.028  1.00 92.15  ? 433 LYS A CG  1 
ATOM   2538 C  CD  . LYS A 1 334 ? 8.163   51.224 49.802  1.00 95.32  ? 433 LYS A CD  1 
ATOM   2539 C  CE  . LYS A 1 334 ? 7.508   50.955 51.149  1.00 98.08  ? 433 LYS A CE  1 
ATOM   2540 N  NZ  . LYS A 1 334 ? 8.422   50.287 52.123  1.00 99.46  ? 433 LYS A NZ  1 
ATOM   2541 N  N   . ILE A 1 335 ? 10.882  49.040 45.466  1.00 85.59  ? 434 ILE A N   1 
ATOM   2542 C  CA  . ILE A 1 335 ? 12.247  48.597 45.202  1.00 85.32  ? 434 ILE A CA  1 
ATOM   2543 C  C   . ILE A 1 335 ? 13.171  49.759 45.562  1.00 84.80  ? 434 ILE A C   1 
ATOM   2544 O  O   . ILE A 1 335 ? 12.989  50.862 45.031  1.00 84.90  ? 434 ILE A O   1 
ATOM   2545 C  CB  . ILE A 1 335 ? 12.502  48.135 43.751  1.00 86.02  ? 434 ILE A CB  1 
ATOM   2546 C  CG1 . ILE A 1 335 ? 11.490  47.069 43.288  1.00 87.10  ? 434 ILE A CG1 1 
ATOM   2547 C  CG2 . ILE A 1 335 ? 13.953  47.641 43.612  1.00 86.40  ? 434 ILE A CG2 1 
ATOM   2548 C  CD1 . ILE A 1 335 ? 11.740  46.524 41.827  1.00 88.38  ? 434 ILE A CD1 1 
ATOM   2549 N  N   . ASN A 1 336 ? 14.149  49.518 46.466  1.00 83.76  ? 435 ASN A N   1 
ATOM   2550 C  CA  . ASN A 1 336 ? 15.081  50.538 46.953  1.00 83.05  ? 435 ASN A CA  1 
ATOM   2551 C  C   . ASN A 1 336 ? 14.338  51.705 47.579  1.00 83.24  ? 435 ASN A C   1 
ATOM   2552 O  O   . ASN A 1 336 ? 14.646  52.866 47.312  1.00 83.04  ? 435 ASN A O   1 
ATOM   2553 C  CB  . ASN A 1 336 ? 16.043  51.005 45.860  1.00 82.80  ? 435 ASN A CB  1 
ATOM   2554 C  CG  . ASN A 1 336 ? 17.100  49.998 45.506  1.00 83.77  ? 435 ASN A CG  1 
ATOM   2555 O  OD1 . ASN A 1 336 ? 17.141  48.890 46.032  1.00 83.56  ? 435 ASN A OD1 1 
ATOM   2556 N  ND2 . ASN A 1 336 ? 17.986  50.369 44.601  1.00 84.35  ? 435 ASN A ND2 1 
ATOM   2557 N  N   . GLY A 1 337 ? 13.327  51.378 48.375  1.00 83.57  ? 436 GLY A N   1 
ATOM   2558 C  CA  . GLY A 1 337 ? 12.492  52.362 49.047  1.00 84.56  ? 436 GLY A CA  1 
ATOM   2559 C  C   . GLY A 1 337 ? 11.470  53.015 48.144  1.00 85.34  ? 436 GLY A C   1 
ATOM   2560 O  O   . GLY A 1 337 ? 10.401  53.421 48.600  1.00 85.65  ? 436 GLY A O   1 
ATOM   2561 N  N   . ILE A 1 338 ? 11.789  53.120 46.857  1.00 85.53  ? 437 ILE A N   1 
ATOM   2562 C  CA  . ILE A 1 338 ? 10.912  53.753 45.883  1.00 86.11  ? 437 ILE A CA  1 
ATOM   2563 C  C   . ILE A 1 338 ? 9.893   52.761 45.329  1.00 86.36  ? 437 ILE A C   1 
ATOM   2564 O  O   . ILE A 1 338 ? 10.280  51.725 44.793  1.00 86.63  ? 437 ILE A O   1 
ATOM   2565 C  CB  . ILE A 1 338 ? 11.722  54.369 44.701  1.00 86.53  ? 437 ILE A CB  1 
ATOM   2566 C  CG1 . ILE A 1 338 ? 13.050  55.027 45.141  1.00 87.07  ? 437 ILE A CG1 1 
ATOM   2567 C  CG2 . ILE A 1 338 ? 10.857  55.342 43.900  1.00 87.10  ? 437 ILE A CG2 1 
ATOM   2568 C  CD1 . ILE A 1 338 ? 14.029  55.179 44.023  1.00 87.88  ? 437 ILE A CD1 1 
ATOM   2569 N  N   . ALA A 1 339 ? 8.603   53.071 45.451  1.00 86.16  ? 438 ALA A N   1 
ATOM   2570 C  CA  . ALA A 1 339 ? 7.567   52.260 44.815  1.00 86.40  ? 438 ALA A CA  1 
ATOM   2571 C  C   . ALA A 1 339 ? 7.571   52.755 43.339  1.00 86.91  ? 438 ALA A C   1 
ATOM   2572 O  O   . ALA A 1 339 ? 7.756   53.952 43.105  1.00 87.32  ? 438 ALA A O   1 
ATOM   2573 C  CB  . ALA A 1 339 ? 6.220   52.526 45.469  1.00 86.30  ? 438 ALA A CB  1 
ATOM   2574 N  N   . PHE A 1 340 ? 7.417   51.855 42.351  1.00 86.67  ? 439 PHE A N   1 
ATOM   2575 C  CA  . PHE A 1 340 ? 7.506   52.195 40.921  1.00 87.02  ? 439 PHE A CA  1 
ATOM   2576 C  C   . PHE A 1 340 ? 6.993   53.581 40.495  1.00 87.43  ? 439 PHE A C   1 
ATOM   2577 O  O   . PHE A 1 340 ? 5.794   53.800 40.332  1.00 87.44  ? 439 PHE A O   1 
ATOM   2578 C  CB  . PHE A 1 340 ? 6.853   51.141 40.017  1.00 86.88  ? 439 PHE A CB  1 
ATOM   2579 C  CG  . PHE A 1 340 ? 7.032   51.443 38.541  1.00 87.23  ? 439 PHE A CG  1 
ATOM   2580 C  CD1 . PHE A 1 340 ? 8.297   51.549 37.987  1.00 87.83  ? 439 PHE A CD1 1 
ATOM   2581 C  CD2 . PHE A 1 340 ? 5.937   51.677 37.727  1.00 87.78  ? 439 PHE A CD2 1 
ATOM   2582 C  CE1 . PHE A 1 340 ? 8.459   51.837 36.639  1.00 88.41  ? 439 PHE A CE1 1 
ATOM   2583 C  CE2 . PHE A 1 340 ? 6.103   51.968 36.381  1.00 88.32  ? 439 PHE A CE2 1 
ATOM   2584 C  CZ  . PHE A 1 340 ? 7.362   52.039 35.844  1.00 88.11  ? 439 PHE A CZ  1 
ATOM   2585 N  N   . ASP A 1 341 ? 7.945   54.468 40.219  1.00 87.67  ? 440 ASP A N   1 
ATOM   2586 C  CA  . ASP A 1 341 ? 7.695   55.798 39.702  1.00 88.41  ? 440 ASP A CA  1 
ATOM   2587 C  C   . ASP A 1 341 ? 8.132   55.738 38.254  1.00 88.20  ? 440 ASP A C   1 
ATOM   2588 O  O   . ASP A 1 341 ? 9.317   55.554 37.966  1.00 87.90  ? 440 ASP A O   1 
ATOM   2589 C  CB  . ASP A 1 341 ? 8.529   56.835 40.462  1.00 91.13  ? 440 ASP A CB  1 
ATOM   2590 C  CG  . ASP A 1 341 ? 8.409   58.244 39.910  1.00 96.92  ? 440 ASP A CG  1 
ATOM   2591 O  OD1 . ASP A 1 341 ? 7.327   58.579 39.358  1.00 97.91  ? 440 ASP A OD1 1 
ATOM   2592 O  OD2 . ASP A 1 341 ? 9.390   59.011 40.031  1.00 99.10  ? 440 ASP A OD2 1 
ATOM   2593 N  N   . MET A 1 342 ? 7.171   55.858 37.347  1.00 88.23  ? 441 MET A N   1 
ATOM   2594 C  CA  . MET A 1 342 ? 7.433   55.780 35.914  1.00 88.71  ? 441 MET A CA  1 
ATOM   2595 C  C   . MET A 1 342 ? 8.285   56.958 35.411  1.00 88.38  ? 441 MET A C   1 
ATOM   2596 O  O   . MET A 1 342 ? 9.109   56.782 34.518  1.00 88.55  ? 441 MET A O   1 
ATOM   2597 C  CB  . MET A 1 342 ? 6.096   55.668 35.143  1.00 89.77  ? 441 MET A CB  1 
ATOM   2598 C  CG  . MET A 1 342 ? 6.248   55.193 33.709  1.00 92.91  ? 441 MET A CG  1 
ATOM   2599 S  SD  . MET A 1 342 ? 4.781   54.371 33.005  1.00 100.59 ? 441 MET A SD  1 
ATOM   2600 C  CE  . MET A 1 342 ? 3.526   55.636 33.264  1.00 99.05  ? 441 MET A CE  1 
ATOM   2601 N  N   . ALA A 1 343 ? 8.131   58.138 36.020  1.00 87.68  ? 442 ALA A N   1 
ATOM   2602 C  CA  . ALA A 1 343 ? 8.848   59.336 35.591  1.00 87.40  ? 442 ALA A CA  1 
ATOM   2603 C  C   . ALA A 1 343 ? 10.336  59.345 35.895  1.00 87.11  ? 442 ALA A C   1 
ATOM   2604 O  O   . ALA A 1 343 ? 11.051  60.175 35.334  1.00 87.27  ? 442 ALA A O   1 
ATOM   2605 C  CB  . ALA A 1 343 ? 8.193   60.574 36.177  1.00 87.40  ? 442 ALA A CB  1 
ATOM   2606 N  N   . LYS A 1 344 ? 10.811  58.448 36.775  1.00 86.53  ? 443 LYS A N   1 
ATOM   2607 C  CA  . LYS A 1 344 ? 12.222  58.444 37.135  1.00 86.26  ? 443 LYS A CA  1 
ATOM   2608 C  C   . LYS A 1 344 ? 12.925  57.089 36.984  1.00 85.21  ? 443 LYS A C   1 
ATOM   2609 O  O   . LYS A 1 344 ? 12.926  56.268 37.896  1.00 84.91  ? 443 LYS A O   1 
ATOM   2610 C  CB  . LYS A 1 344 ? 12.418  59.012 38.545  1.00 88.55  ? 443 LYS A CB  1 
ATOM   2611 C  CG  . LYS A 1 344 ? 12.754  60.497 38.539  1.00 93.23  ? 443 LYS A CG  1 
ATOM   2612 C  CD  . LYS A 1 344 ? 12.692  61.087 39.940  1.00 97.92  ? 443 LYS A CD  1 
ATOM   2613 C  CE  . LYS A 1 344 ? 11.312  61.616 40.251  1.00 101.80 ? 443 LYS A CE  1 
ATOM   2614 N  NZ  . LYS A 1 344 ? 11.111  61.863 41.702  1.00 103.91 ? 443 LYS A NZ  1 
ATOM   2615 N  N   . PRO A 1 345 ? 13.591  56.887 35.841  1.00 84.50  ? 444 PRO A N   1 
ATOM   2616 C  CA  . PRO A 1 345 ? 14.351  55.648 35.648  1.00 84.28  ? 444 PRO A CA  1 
ATOM   2617 C  C   . PRO A 1 345 ? 15.600  55.614 36.521  1.00 84.09  ? 444 PRO A C   1 
ATOM   2618 O  O   . PRO A 1 345 ? 16.533  56.375 36.286  1.00 84.34  ? 444 PRO A O   1 
ATOM   2619 C  CB  . PRO A 1 345 ? 14.740  55.691 34.160  1.00 84.94  ? 444 PRO A CB  1 
ATOM   2620 C  CG  . PRO A 1 345 ? 13.923  56.789 33.557  1.00 85.41  ? 444 PRO A CG  1 
ATOM   2621 C  CD  . PRO A 1 345 ? 13.681  57.761 34.661  1.00 83.91  ? 444 PRO A CD  1 
ATOM   2622 N  N   . MET A 1 346 ? 15.613  54.706 37.503  1.00 83.55  ? 445 MET A N   1 
ATOM   2623 C  CA  . MET A 1 346 ? 16.683  54.443 38.467  1.00 83.55  ? 445 MET A CA  1 
ATOM   2624 C  C   . MET A 1 346 ? 18.115  54.778 38.028  1.00 83.34  ? 445 MET A C   1 
ATOM   2625 O  O   . MET A 1 346 ? 18.846  55.397 38.803  1.00 83.74  ? 445 MET A O   1 
ATOM   2626 C  CB  . MET A 1 346 ? 16.639  52.974 38.894  1.00 84.37  ? 445 MET A CB  1 
ATOM   2627 C  CG  . MET A 1 346 ? 15.497  52.629 39.806  1.00 86.89  ? 445 MET A CG  1 
ATOM   2628 S  SD  . MET A 1 346 ? 16.012  52.348 41.519  1.00 90.91  ? 445 MET A SD  1 
ATOM   2629 C  CE  . MET A 1 346 ? 17.449  51.289 41.285  1.00 88.79  ? 445 MET A CE  1 
ATOM   2630 N  N   . PHE A 1 347 ? 18.530  54.343 36.820  1.00 82.45  ? 446 PHE A N   1 
ATOM   2631 C  CA  . PHE A 1 347 ? 19.896  54.556 36.348  1.00 82.29  ? 446 PHE A CA  1 
ATOM   2632 C  C   . PHE A 1 347 ? 20.049  54.354 34.840  1.00 82.32  ? 446 PHE A C   1 
ATOM   2633 O  O   . PHE A 1 347 ? 19.167  53.793 34.195  1.00 82.45  ? 446 PHE A O   1 
ATOM   2634 C  CB  . PHE A 1 347 ? 20.884  53.637 37.109  1.00 82.10  ? 446 PHE A CB  1 
ATOM   2635 C  CG  . PHE A 1 347 ? 20.452  52.196 37.219  1.00 82.68  ? 446 PHE A CG  1 
ATOM   2636 C  CD1 . PHE A 1 347 ? 20.603  51.327 36.154  1.00 83.57  ? 446 PHE A CD1 1 
ATOM   2637 C  CD2 . PHE A 1 347 ? 19.904  51.709 38.390  1.00 83.44  ? 446 PHE A CD2 1 
ATOM   2638 C  CE1 . PHE A 1 347 ? 20.185  50.009 36.248  1.00 84.19  ? 446 PHE A CE1 1 
ATOM   2639 C  CE2 . PHE A 1 347 ? 19.482  50.391 38.478  1.00 84.25  ? 446 PHE A CE2 1 
ATOM   2640 C  CZ  . PHE A 1 347 ? 19.626  49.550 37.407  1.00 84.04  ? 446 PHE A CZ  1 
ATOM   2641 N  N   . ASP A 1 348 ? 21.184  54.803 34.280  1.00 82.06  ? 447 ASP A N   1 
ATOM   2642 C  CA  . ASP A 1 348 ? 21.501  54.638 32.865  1.00 82.18  ? 447 ASP A CA  1 
ATOM   2643 C  C   . ASP A 1 348 ? 22.598  53.585 32.733  1.00 82.75  ? 447 ASP A C   1 
ATOM   2644 O  O   . ASP A 1 348 ? 23.509  53.508 33.560  1.00 83.17  ? 447 ASP A O   1 
ATOM   2645 C  CB  . ASP A 1 348 ? 21.924  55.973 32.224  1.00 83.00  ? 447 ASP A CB  1 
ATOM   2646 C  CG  . ASP A 1 348 ? 22.224  55.907 30.736  1.00 86.15  ? 447 ASP A CG  1 
ATOM   2647 O  OD1 . ASP A 1 348 ? 21.269  55.796 29.937  1.00 85.81  ? 447 ASP A OD1 1 
ATOM   2648 O  OD2 . ASP A 1 348 ? 23.411  55.998 30.366  1.00 88.74  ? 447 ASP A OD2 1 
ATOM   2649 N  N   . VAL A 1 349 ? 22.478  52.745 31.715  1.00 82.59  ? 448 VAL A N   1 
ATOM   2650 C  CA  . VAL A 1 349 ? 23.391  51.656 31.445  1.00 83.16  ? 448 VAL A CA  1 
ATOM   2651 C  C   . VAL A 1 349 ? 24.050  51.906 30.101  1.00 83.62  ? 448 VAL A C   1 
ATOM   2652 O  O   . VAL A 1 349 ? 23.374  52.288 29.147  1.00 83.66  ? 448 VAL A O   1 
ATOM   2653 C  CB  . VAL A 1 349 ? 22.625  50.303 31.456  1.00 83.92  ? 448 VAL A CB  1 
ATOM   2654 C  CG1 . VAL A 1 349 ? 23.550  49.136 31.124  1.00 84.36  ? 448 VAL A CG1 1 
ATOM   2655 C  CG2 . VAL A 1 349 ? 21.918  50.077 32.793  1.00 84.37  ? 448 VAL A CG2 1 
ATOM   2656 N  N   . LYS A 1 350 ? 25.373  51.724 30.025  1.00 83.86  ? 449 LYS A N   1 
ATOM   2657 C  CA  . LYS A 1 350 ? 26.088  51.894 28.769  1.00 84.52  ? 449 LYS A CA  1 
ATOM   2658 C  C   . LYS A 1 350 ? 25.762  50.673 27.899  1.00 84.29  ? 449 LYS A C   1 
ATOM   2659 O  O   . LYS A 1 350 ? 26.008  49.547 28.330  1.00 84.53  ? 449 LYS A O   1 
ATOM   2660 C  CB  . LYS A 1 350 ? 27.605  51.990 29.028  1.00 87.04  ? 449 LYS A CB  1 
ATOM   2661 C  CG  . LYS A 1 350 ? 28.426  52.162 27.760  1.00 91.81  ? 449 LYS A CG  1 
ATOM   2662 C  CD  . LYS A 1 350 ? 29.875  52.514 28.070  1.00 96.60  ? 449 LYS A CD  1 
ATOM   2663 C  CE  . LYS A 1 350 ? 30.670  52.623 26.799  1.00 100.86 ? 449 LYS A CE  1 
ATOM   2664 N  NZ  . LYS A 1 350 ? 31.154  51.299 26.321  1.00 103.29 ? 449 LYS A NZ  1 
ATOM   2665 N  N   . ARG A 1 351 ? 25.206  50.886 26.688  1.00 83.61  ? 450 ARG A N   1 
ATOM   2666 C  CA  . ARG A 1 351 ? 24.879  49.793 25.769  1.00 83.57  ? 450 ARG A CA  1 
ATOM   2667 C  C   . ARG A 1 351 ? 26.114  48.933 25.450  1.00 83.15  ? 450 ARG A C   1 
ATOM   2668 O  O   . ARG A 1 351 ? 27.240  49.438 25.443  1.00 83.52  ? 450 ARG A O   1 
ATOM   2669 C  CB  . ARG A 1 351 ? 24.242  50.341 24.477  1.00 85.14  ? 450 ARG A CB  1 
ATOM   2670 C  CG  . ARG A 1 351 ? 23.912  49.279 23.427  1.00 89.07  ? 450 ARG A CG  1 
ATOM   2671 C  CD  . ARG A 1 351 ? 23.337  49.869 22.148  1.00 93.89  ? 450 ARG A CD  1 
ATOM   2672 N  NE  . ARG A 1 351 ? 24.366  50.285 21.188  1.00 98.74  ? 450 ARG A NE  1 
ATOM   2673 C  CZ  . ARG A 1 351 ? 24.738  51.550 20.980  1.00 102.42 ? 450 ARG A CZ  1 
ATOM   2674 N  NH1 . ARG A 1 351 ? 24.182  52.539 21.677  1.00 102.42 ? 450 ARG A NH1 1 
ATOM   2675 N  NH2 . ARG A 1 351 ? 25.665  51.836 20.078  1.00 102.70 ? 450 ARG A NH2 1 
ATOM   2676 N  N   . GLY A 1 352 ? 25.888  47.635 25.269  1.00 82.09  ? 451 GLY A N   1 
ATOM   2677 C  CA  . GLY A 1 352 ? 26.911  46.653 24.938  1.00 81.48  ? 451 GLY A CA  1 
ATOM   2678 C  C   . GLY A 1 352 ? 27.846  46.273 26.068  1.00 80.44  ? 451 GLY A C   1 
ATOM   2679 O  O   . GLY A 1 352 ? 28.804  45.532 25.842  1.00 80.54  ? 451 GLY A O   1 
ATOM   2680 N  N   . THR A 1 353 ? 27.587  46.762 27.288  1.00 79.37  ? 452 THR A N   1 
ATOM   2681 C  CA  . THR A 1 353 ? 28.472  46.477 28.412  1.00 79.03  ? 452 THR A CA  1 
ATOM   2682 C  C   . THR A 1 353 ? 27.860  45.565 29.492  1.00 78.06  ? 452 THR A C   1 
ATOM   2683 O  O   . THR A 1 353 ? 26.686  45.679 29.858  1.00 78.05  ? 452 THR A O   1 
ATOM   2684 C  CB  . THR A 1 353 ? 29.024  47.774 29.020  1.00 80.57  ? 452 THR A CB  1 
ATOM   2685 O  OG1 . THR A 1 353 ? 28.007  48.439 29.775  1.00 81.90  ? 452 THR A OG1 1 
ATOM   2686 C  CG2 . THR A 1 353 ? 29.618  48.700 27.970  1.00 80.86  ? 452 THR A CG2 1 
ATOM   2687 N  N   . TYR A 1 354 ? 28.699  44.662 30.002  1.00 76.93  ? 453 TYR A N   1 
ATOM   2688 C  CA  . TYR A 1 354 ? 28.331  43.733 31.050  1.00 76.21  ? 453 TYR A CA  1 
ATOM   2689 C  C   . TYR A 1 354 ? 28.183  44.447 32.368  1.00 75.37  ? 453 TYR A C   1 
ATOM   2690 O  O   . TYR A 1 354 ? 28.852  45.439 32.639  1.00 75.66  ? 453 TYR A O   1 
ATOM   2691 C  CB  . TYR A 1 354 ? 29.391  42.642 31.193  1.00 76.21  ? 453 TYR A CB  1 
ATOM   2692 C  CG  . TYR A 1 354 ? 29.245  41.517 30.197  1.00 77.18  ? 453 TYR A CG  1 
ATOM   2693 C  CD1 . TYR A 1 354 ? 28.324  40.501 30.399  1.00 78.05  ? 453 TYR A CD1 1 
ATOM   2694 C  CD2 . TYR A 1 354 ? 30.039  41.459 29.063  1.00 78.39  ? 453 TYR A CD2 1 
ATOM   2695 C  CE1 . TYR A 1 354 ? 28.211  39.443 29.508  1.00 79.13  ? 453 TYR A CE1 1 
ATOM   2696 C  CE2 . TYR A 1 354 ? 29.930  40.411 28.157  1.00 79.46  ? 453 TYR A CE2 1 
ATOM   2697 C  CZ  . TYR A 1 354 ? 29.013  39.403 28.384  1.00 80.29  ? 453 TYR A CZ  1 
ATOM   2698 O  OH  . TYR A 1 354 ? 28.911  38.359 27.496  1.00 81.78  ? 453 TYR A OH  1 
ATOM   2699 N  N   . GLU A 1 355 ? 27.306  43.928 33.192  1.00 74.25  ? 454 GLU A N   1 
ATOM   2700 C  CA  . GLU A 1 355 ? 27.039  44.445 34.514  1.00 73.78  ? 454 GLU A CA  1 
ATOM   2701 C  C   . GLU A 1 355 ? 26.694  43.263 35.432  1.00 74.15  ? 454 GLU A C   1 
ATOM   2702 O  O   . GLU A 1 355 ? 26.298  42.194 34.960  1.00 74.04  ? 454 GLU A O   1 
ATOM   2703 C  CB  . GLU A 1 355 ? 25.885  45.453 34.474  1.00 74.38  ? 454 GLU A CB  1 
ATOM   2704 C  CG  . GLU A 1 355 ? 26.300  46.882 34.179  1.00 76.04  ? 454 GLU A CG  1 
ATOM   2705 C  CD  . GLU A 1 355 ? 25.333  47.924 34.706  1.00 79.45  ? 454 GLU A CD  1 
ATOM   2706 O  OE1 . GLU A 1 355 ? 25.343  49.064 34.186  1.00 79.68  ? 454 GLU A OE1 1 
ATOM   2707 O  OE2 . GLU A 1 355 ? 24.563  47.603 35.640  1.00 80.56  ? 454 GLU A OE2 1 
ATOM   2708 N  N   . LYS A 1 356 ? 26.845  43.455 36.743  1.00 74.26  ? 455 LYS A N   1 
ATOM   2709 C  CA  . LYS A 1 356 ? 26.569  42.406 37.707  1.00 74.73  ? 455 LYS A CA  1 
ATOM   2710 C  C   . LYS A 1 356 ? 25.443  42.885 38.598  1.00 74.49  ? 455 LYS A C   1 
ATOM   2711 O  O   . LYS A 1 356 ? 25.661  43.712 39.477  1.00 74.46  ? 455 LYS A O   1 
ATOM   2712 C  CB  . LYS A 1 356 ? 27.839  42.093 38.510  1.00 77.43  ? 455 LYS A CB  1 
ATOM   2713 C  CG  . LYS A 1 356 ? 27.821  40.713 39.159  1.00 83.19  ? 455 LYS A CG  1 
ATOM   2714 C  CD  . LYS A 1 356 ? 28.967  40.522 40.174  1.00 89.02  ? 455 LYS A CD  1 
ATOM   2715 C  CE  . LYS A 1 356 ? 28.863  41.415 41.397  1.00 93.07  ? 455 LYS A CE  1 
ATOM   2716 N  NZ  . LYS A 1 356 ? 29.873  41.056 42.429  1.00 94.88  ? 455 LYS A NZ  1 
ATOM   2717 N  N   . TRP A 1 357 ? 24.225  42.406 38.341  1.00 74.25  ? 456 TRP A N   1 
ATOM   2718 C  CA  . TRP A 1 357 ? 23.057  42.859 39.089  1.00 74.78  ? 456 TRP A CA  1 
ATOM   2719 C  C   . TRP A 1 357 ? 22.726  41.981 40.274  1.00 74.82  ? 456 TRP A C   1 
ATOM   2720 O  O   . TRP A 1 357 ? 22.755  40.768 40.151  1.00 74.94  ? 456 TRP A O   1 
ATOM   2721 C  CB  . TRP A 1 357 ? 21.840  42.935 38.169  1.00 75.08  ? 456 TRP A CB  1 
ATOM   2722 C  CG  . TRP A 1 357 ? 21.833  44.093 37.221  1.00 75.98  ? 456 TRP A CG  1 
ATOM   2723 C  CD1 . TRP A 1 357 ? 22.902  44.638 36.570  1.00 76.97  ? 456 TRP A CD1 1 
ATOM   2724 C  CD2 . TRP A 1 357 ? 20.677  44.792 36.749  1.00 76.19  ? 456 TRP A CD2 1 
ATOM   2725 N  NE1 . TRP A 1 357 ? 22.486  45.664 35.755  1.00 77.32  ? 456 TRP A NE1 1 
ATOM   2726 C  CE2 . TRP A 1 357 ? 21.121  45.774 35.841  1.00 77.16  ? 456 TRP A CE2 1 
ATOM   2727 C  CE3 . TRP A 1 357 ? 19.308  44.693 37.019  1.00 76.61  ? 456 TRP A CE3 1 
ATOM   2728 C  CZ2 . TRP A 1 357 ? 20.243  46.639 35.195  1.00 77.94  ? 456 TRP A CZ2 1 
ATOM   2729 C  CZ3 . TRP A 1 357 ? 18.442  45.560 36.392  1.00 77.56  ? 456 TRP A CZ3 1 
ATOM   2730 C  CH2 . TRP A 1 357 ? 18.908  46.517 35.490  1.00 77.97  ? 456 TRP A CH2 1 
ATOM   2731 N  N   . THR A 1 358 ? 22.349  42.584 41.406  1.00 74.66  ? 457 THR A N   1 
ATOM   2732 C  CA  . THR A 1 358 ? 21.996  41.827 42.598  1.00 75.14  ? 457 THR A CA  1 
ATOM   2733 C  C   . THR A 1 358 ? 20.623  42.220 43.145  1.00 75.45  ? 457 THR A C   1 
ATOM   2734 O  O   . THR A 1 358 ? 20.403  43.360 43.532  1.00 75.39  ? 457 THR A O   1 
ATOM   2735 C  CB  . THR A 1 358 ? 23.101  41.917 43.640  1.00 76.59  ? 457 THR A CB  1 
ATOM   2736 O  OG1 . THR A 1 358 ? 24.316  41.419 43.069  1.00 77.83  ? 457 THR A OG1 1 
ATOM   2737 C  CG2 . THR A 1 358 ? 22.766  41.142 44.897  1.00 76.92  ? 457 THR A CG2 1 
ATOM   2738 N  N   . ILE A 1 359 ? 19.699  41.270 43.162  1.00 75.65  ? 458 ILE A N   1 
ATOM   2739 C  CA  . ILE A 1 359 ? 18.329  41.485 43.617  1.00 76.31  ? 458 ILE A CA  1 
ATOM   2740 C  C   . ILE A 1 359 ? 18.167  40.831 44.973  1.00 77.56  ? 458 ILE A C   1 
ATOM   2741 O  O   . ILE A 1 359 ? 18.615  39.701 45.149  1.00 77.77  ? 458 ILE A O   1 
ATOM   2742 C  CB  . ILE A 1 359 ? 17.311  40.922 42.593  1.00 76.20  ? 458 ILE A CB  1 
ATOM   2743 C  CG1 . ILE A 1 359 ? 17.619  41.398 41.167  1.00 76.45  ? 458 ILE A CG1 1 
ATOM   2744 C  CG2 . ILE A 1 359 ? 15.884  41.261 42.995  1.00 76.55  ? 458 ILE A CG2 1 
ATOM   2745 C  CD1 . ILE A 1 359 ? 18.277  40.376 40.315  1.00 77.26  ? 458 ILE A CD1 1 
ATOM   2746 N  N   . SER A 1 360 ? 17.528  41.524 45.931  1.00 78.18  ? 459 SER A N   1 
ATOM   2747 C  CA  . SER A 1 360 ? 17.393  41.023 47.290  1.00 79.46  ? 459 SER A CA  1 
ATOM   2748 C  C   . SER A 1 360 ? 15.966  40.916 47.784  1.00 80.73  ? 459 SER A C   1 
ATOM   2749 O  O   . SER A 1 360 ? 15.217  41.886 47.719  1.00 81.00  ? 459 SER A O   1 
ATOM   2750 C  CB  . SER A 1 360 ? 18.199  41.899 48.240  1.00 81.11  ? 459 SER A CB  1 
ATOM   2751 O  OG  . SER A 1 360 ? 17.909  41.649 49.606  1.00 84.12  ? 459 SER A OG  1 
ATOM   2752 N  N   . GLY A 1 361 ? 15.643  39.763 48.360  1.00 81.37  ? 460 GLY A N   1 
ATOM   2753 C  CA  . GLY A 1 361 ? 14.336  39.493 48.943  1.00 82.54  ? 460 GLY A CA  1 
ATOM   2754 C  C   . GLY A 1 361 ? 14.404  39.170 50.426  1.00 83.81  ? 460 GLY A C   1 
ATOM   2755 O  O   . GLY A 1 361 ? 13.485  38.553 50.975  1.00 83.94  ? 460 GLY A O   1 
ATOM   2756 N  N   . GLU A 1 362 ? 15.509  39.572 51.087  1.00 84.44  ? 461 GLU A N   1 
ATOM   2757 C  CA  . GLU A 1 362 ? 15.711  39.374 52.518  1.00 85.30  ? 461 GLU A CA  1 
ATOM   2758 C  C   . GLU A 1 362 ? 14.705  40.232 53.271  1.00 86.38  ? 461 GLU A C   1 
ATOM   2759 O  O   . GLU A 1 362 ? 14.378  41.337 52.837  1.00 86.62  ? 461 GLU A O   1 
ATOM   2760 C  CB  . GLU A 1 362 ? 17.135  39.768 52.921  1.00 87.01  ? 461 GLU A CB  1 
ATOM   2761 C  CG  . GLU A 1 362 ? 18.214  39.176 52.036  1.00 91.36  ? 461 GLU A CG  1 
ATOM   2762 C  CD  . GLU A 1 362 ? 19.496  39.982 52.039  1.00 97.62  ? 461 GLU A CD  1 
ATOM   2763 O  OE1 . GLU A 1 362 ? 20.134  40.085 53.111  1.00 99.38  ? 461 GLU A OE1 1 
ATOM   2764 O  OE2 . GLU A 1 362 ? 19.858  40.528 50.973  1.00 99.37  ? 461 GLU A OE2 1 
ATOM   2765 N  N   . GLY A 1 363 ? 14.215  39.719 54.388  1.00 86.98  ? 462 GLY A N   1 
ATOM   2766 C  CA  . GLY A 1 363 ? 13.208  40.423 55.172  1.00 87.94  ? 462 GLY A CA  1 
ATOM   2767 C  C   . GLY A 1 363 ? 11.899  40.435 54.414  1.00 88.45  ? 462 GLY A C   1 
ATOM   2768 O  O   . GLY A 1 363 ? 11.264  41.483 54.247  1.00 88.68  ? 462 GLY A O   1 
ATOM   2769 N  N   . ASP A 1 364 ? 11.528  39.249 53.924  1.00 88.23  ? 463 ASP A N   1 
ATOM   2770 C  CA  . ASP A 1 364 ? 10.369  38.995 53.091  1.00 88.42  ? 463 ASP A CA  1 
ATOM   2771 C  C   . ASP A 1 364 ? 10.497  37.540 52.672  1.00 87.62  ? 463 ASP A C   1 
ATOM   2772 O  O   . ASP A 1 364 ? 11.502  37.185 52.040  1.00 87.67  ? 463 ASP A O   1 
ATOM   2773 C  CB  . ASP A 1 364 ? 10.463  39.875 51.832  1.00 90.70  ? 463 ASP A CB  1 
ATOM   2774 C  CG  . ASP A 1 364 ? 9.313   39.744 50.879  1.00 96.00  ? 463 ASP A CG  1 
ATOM   2775 O  OD1 . ASP A 1 364 ? 8.234   39.305 51.316  1.00 97.20  ? 463 ASP A OD1 1 
ATOM   2776 O  OD2 . ASP A 1 364 ? 9.487   40.094 49.695  1.00 98.21  ? 463 ASP A OD2 1 
ATOM   2777 N  N   . MET A 1 365 ? 9.516   36.694 53.029  1.00 86.66  ? 464 MET A N   1 
ATOM   2778 C  CA  . MET A 1 365 ? 9.587   35.290 52.620  1.00 86.36  ? 464 MET A CA  1 
ATOM   2779 C  C   . MET A 1 365 ? 8.755   34.963 51.377  1.00 84.33  ? 464 MET A C   1 
ATOM   2780 O  O   . MET A 1 365 ? 8.500   33.792 51.102  1.00 84.56  ? 464 MET A O   1 
ATOM   2781 C  CB  . MET A 1 365 ? 9.265   34.327 53.768  1.00 88.40  ? 464 MET A CB  1 
ATOM   2782 C  CG  . MET A 1 365 ? 10.521  33.755 54.443  1.00 93.41  ? 464 MET A CG  1 
ATOM   2783 S  SD  . MET A 1 365 ? 11.849  33.153 53.327  1.00 105.55 ? 464 MET A SD  1 
ATOM   2784 C  CE  . MET A 1 365 ? 11.013  31.763 52.517  1.00 104.78 ? 464 MET A CE  1 
ATOM   2785 N  N   . MET A 1 366 ? 8.386   35.982 50.600  1.00 82.20  ? 465 MET A N   1 
ATOM   2786 C  CA  . MET A 1 366 ? 7.608   35.794 49.393  1.00 80.80  ? 465 MET A CA  1 
ATOM   2787 C  C   . MET A 1 366 ? 8.481   35.417 48.194  1.00 79.65  ? 465 MET A C   1 
ATOM   2788 O  O   . MET A 1 366 ? 9.707   35.581 48.240  1.00 80.49  ? 465 MET A O   1 
ATOM   2789 C  CB  . MET A 1 366 ? 6.773   37.044 49.114  1.00 80.92  ? 465 MET A CB  1 
ATOM   2790 C  CG  . MET A 1 366 ? 5.833   37.385 50.246  1.00 82.45  ? 465 MET A CG  1 
ATOM   2791 S  SD  . MET A 1 366 ? 4.606   36.119 50.589  1.00 84.60  ? 465 MET A SD  1 
ATOM   2792 C  CE  . MET A 1 366 ? 3.765   36.064 49.031  1.00 82.69  ? 465 MET A CE  1 
ATOM   2793 N  N   . LEU A 1 367 ? 7.851   34.881 47.127  1.00 77.38  ? 466 LEU A N   1 
ATOM   2794 C  CA  . LEU A 1 367 ? 8.557   34.464 45.922  1.00 75.55  ? 466 LEU A CA  1 
ATOM   2795 C  C   . LEU A 1 367 ? 8.599   35.596 44.906  1.00 73.65  ? 466 LEU A C   1 
ATOM   2796 O  O   . LEU A 1 367 ? 7.560   36.168 44.578  1.00 73.77  ? 466 LEU A O   1 
ATOM   2797 C  CB  . LEU A 1 367 ? 7.880   33.224 45.318  1.00 75.49  ? 466 LEU A CB  1 
ATOM   2798 C  CG  . LEU A 1 367 ? 8.445   32.736 43.986  1.00 76.37  ? 466 LEU A CG  1 
ATOM   2799 C  CD1 . LEU A 1 367 ? 9.863   32.255 44.137  1.00 76.56  ? 466 LEU A CD1 1 
ATOM   2800 C  CD2 . LEU A 1 367 ? 7.584   31.653 43.409  1.00 77.11  ? 466 LEU A CD2 1 
ATOM   2801 N  N   . HIS A 1 368 ? 9.792   35.917 44.402  1.00 71.82  ? 467 HIS A N   1 
ATOM   2802 C  CA  . HIS A 1 368 ? 9.934   36.983 43.425  1.00 70.72  ? 467 HIS A CA  1 
ATOM   2803 C  C   . HIS A 1 368 ? 10.710  36.557 42.202  1.00 69.93  ? 467 HIS A C   1 
ATOM   2804 O  O   . HIS A 1 368 ? 11.939  36.623 42.208  1.00 70.34  ? 467 HIS A O   1 
ATOM   2805 C  CB  . HIS A 1 368 ? 10.611  38.208 44.038  1.00 70.82  ? 467 HIS A CB  1 
ATOM   2806 C  CG  . HIS A 1 368 ? 9.946   38.694 45.277  1.00 72.47  ? 467 HIS A CG  1 
ATOM   2807 N  ND1 . HIS A 1 368 ? 8.813   39.478 45.221  1.00 74.23  ? 467 HIS A ND1 1 
ATOM   2808 C  CD2 . HIS A 1 368 ? 10.264  38.474 46.573  1.00 73.52  ? 467 HIS A CD2 1 
ATOM   2809 C  CE1 . HIS A 1 368 ? 8.478   39.715 46.478  1.00 74.71  ? 467 HIS A CE1 1 
ATOM   2810 N  NE2 . HIS A 1 368 ? 9.319   39.125 47.328  1.00 74.69  ? 467 HIS A NE2 1 
ATOM   2811 N  N   . PRO A 1 369 ? 10.022  36.180 41.114  1.00 68.60  ? 468 PRO A N   1 
ATOM   2812 C  CA  . PRO A 1 369 ? 10.745  35.836 39.890  1.00 67.72  ? 468 PRO A CA  1 
ATOM   2813 C  C   . PRO A 1 369 ? 11.189  37.146 39.230  1.00 66.97  ? 468 PRO A C   1 
ATOM   2814 O  O   . PRO A 1 369 ? 10.392  37.802 38.556  1.00 67.11  ? 468 PRO A O   1 
ATOM   2815 C  CB  . PRO A 1 369 ? 9.699   35.081 39.060  1.00 68.39  ? 468 PRO A CB  1 
ATOM   2816 C  CG  . PRO A 1 369 ? 8.491   34.946 39.930  1.00 68.95  ? 468 PRO A CG  1 
ATOM   2817 C  CD  . PRO A 1 369 ? 8.568   36.042 40.932  1.00 67.85  ? 468 PRO A CD  1 
ATOM   2818 N  N   . PHE A 1 370 ? 12.426  37.581 39.517  1.00 65.52  ? 469 PHE A N   1 
ATOM   2819 C  CA  . PHE A 1 370 ? 12.917  38.839 38.980  1.00 64.22  ? 469 PHE A CA  1 
ATOM   2820 C  C   . PHE A 1 370 ? 13.135  38.808 37.476  1.00 63.18  ? 469 PHE A C   1 
ATOM   2821 O  O   . PHE A 1 370 ? 14.034  38.125 36.989  1.00 63.34  ? 469 PHE A O   1 
ATOM   2822 C  CB  . PHE A 1 370 ? 14.165  39.330 39.708  1.00 63.46  ? 469 PHE A CB  1 
ATOM   2823 C  CG  . PHE A 1 370 ? 14.240  40.827 39.580  1.00 63.03  ? 469 PHE A CG  1 
ATOM   2824 C  CD1 . PHE A 1 370 ? 13.336  41.637 40.241  1.00 63.21  ? 469 PHE A CD1 1 
ATOM   2825 C  CD2 . PHE A 1 370 ? 15.132  41.417 38.706  1.00 63.44  ? 469 PHE A CD2 1 
ATOM   2826 C  CE1 . PHE A 1 370 ? 13.372  43.009 40.089  1.00 63.81  ? 469 PHE A CE1 1 
ATOM   2827 C  CE2 . PHE A 1 370 ? 15.167  42.794 38.555  1.00 64.06  ? 469 PHE A CE2 1 
ATOM   2828 C  CZ  . PHE A 1 370 ? 14.284  43.581 39.244  1.00 63.73  ? 469 PHE A CZ  1 
ATOM   2829 N  N   . HIS A 1 371 ? 12.317  39.573 36.747  1.00 61.92  ? 470 HIS A N   1 
ATOM   2830 C  CA  . HIS A 1 371 ? 12.377  39.672 35.293  1.00 61.32  ? 470 HIS A CA  1 
ATOM   2831 C  C   . HIS A 1 371 ? 13.011  40.996 34.839  1.00 61.25  ? 470 HIS A C   1 
ATOM   2832 O  O   . HIS A 1 371 ? 12.659  42.054 35.354  1.00 61.32  ? 470 HIS A O   1 
ATOM   2833 C  CB  . HIS A 1 371 ? 10.965  39.499 34.700  1.00 61.10  ? 470 HIS A CB  1 
ATOM   2834 C  CG  . HIS A 1 371 ? 10.889  39.698 33.217  1.00 61.31  ? 470 HIS A CG  1 
ATOM   2835 N  ND1 . HIS A 1 371 ? 11.705  38.994 32.352  1.00 62.57  ? 470 HIS A ND1 1 
ATOM   2836 C  CD2 . HIS A 1 371 ? 10.078  40.502 32.494  1.00 61.67  ? 470 HIS A CD2 1 
ATOM   2837 C  CE1 . HIS A 1 371 ? 11.372  39.400 31.139  1.00 62.58  ? 470 HIS A CE1 1 
ATOM   2838 N  NE2 . HIS A 1 371 ? 10.390  40.298 31.179  1.00 62.31  ? 470 HIS A NE2 1 
ATOM   2839 N  N   . ILE A 1 372 ? 13.948  40.932 33.885  1.00 61.00  ? 471 ILE A N   1 
ATOM   2840 C  CA  . ILE A 1 372 ? 14.613  42.113 33.340  1.00 61.67  ? 471 ILE A CA  1 
ATOM   2841 C  C   . ILE A 1 372 ? 14.296  42.263 31.837  1.00 62.84  ? 471 ILE A C   1 
ATOM   2842 O  O   . ILE A 1 372 ? 14.490  41.323 31.061  1.00 63.32  ? 471 ILE A O   1 
ATOM   2843 C  CB  . ILE A 1 372 ? 16.139  42.070 33.610  1.00 61.61  ? 471 ILE A CB  1 
ATOM   2844 C  CG1 . ILE A 1 372 ? 16.427  41.964 35.122  1.00 62.08  ? 471 ILE A CG1 1 
ATOM   2845 C  CG2 . ILE A 1 372 ? 16.838  43.281 32.990  1.00 61.69  ? 471 ILE A CG2 1 
ATOM   2846 C  CD1 . ILE A 1 372 ? 17.819  41.630 35.439  1.00 62.93  ? 471 ILE A CD1 1 
ATOM   2847 N  N   . HIS A 1 373 ? 13.803  43.437 31.429  1.00 62.99  ? 472 HIS A N   1 
ATOM   2848 C  CA  . HIS A 1 373 ? 13.440  43.685 30.039  1.00 63.66  ? 472 HIS A CA  1 
ATOM   2849 C  C   . HIS A 1 373 ? 14.650  43.872 29.109  1.00 64.92  ? 472 HIS A C   1 
ATOM   2850 O  O   . HIS A 1 373 ? 15.747  44.195 29.557  1.00 65.10  ? 472 HIS A O   1 
ATOM   2851 C  CB  . HIS A 1 373 ? 12.522  44.906 29.940  1.00 63.79  ? 472 HIS A CB  1 
ATOM   2852 C  CG  . HIS A 1 373 ? 11.150  44.703 30.492  1.00 65.17  ? 472 HIS A CG  1 
ATOM   2853 N  ND1 . HIS A 1 373 ? 10.056  45.315 29.920  1.00 66.88  ? 472 HIS A ND1 1 
ATOM   2854 C  CD2 . HIS A 1 373 ? 10.738  43.980 31.558  1.00 66.30  ? 472 HIS A CD2 1 
ATOM   2855 C  CE1 . HIS A 1 373 ? 9.014   44.942 30.646  1.00 67.39  ? 472 HIS A CE1 1 
ATOM   2856 N  NE2 . HIS A 1 373 ? 9.379   44.150 31.653  1.00 67.35  ? 472 HIS A NE2 1 
ATOM   2857 N  N   . GLY A 1 374 ? 14.425  43.655 27.818  1.00 65.65  ? 473 GLY A N   1 
ATOM   2858 C  CA  . GLY A 1 374 ? 15.417  43.830 26.768  1.00 66.81  ? 473 GLY A CA  1 
ATOM   2859 C  C   . GLY A 1 374 ? 16.686  43.011 26.849  1.00 67.85  ? 473 GLY A C   1 
ATOM   2860 O  O   . GLY A 1 374 ? 17.669  43.354 26.188  1.00 68.43  ? 473 GLY A O   1 
ATOM   2861 N  N   . THR A 1 375 ? 16.694  41.930 27.642  1.00 68.12  ? 474 THR A N   1 
ATOM   2862 C  CA  . THR A 1 375 ? 17.896  41.106 27.761  1.00 68.85  ? 474 THR A CA  1 
ATOM   2863 C  C   . THR A 1 375 ? 17.598  39.611 28.027  1.00 69.39  ? 474 THR A C   1 
ATOM   2864 O  O   . THR A 1 375 ? 16.462  39.216 28.319  1.00 69.25  ? 474 THR A O   1 
ATOM   2865 C  CB  . THR A 1 375 ? 18.848  41.711 28.823  1.00 69.91  ? 474 THR A CB  1 
ATOM   2866 O  OG1 . THR A 1 375 ? 20.170  41.216 28.601  1.00 70.73  ? 474 THR A OG1 1 
ATOM   2867 C  CG2 . THR A 1 375 ? 18.409  41.389 30.231  1.00 70.41  ? 474 THR A CG2 1 
ATOM   2868 N  N   . GLN A 1 376 ? 18.649  38.798 27.864  1.00 69.56  ? 475 GLN A N   1 
ATOM   2869 C  CA  . GLN A 1 376 ? 18.747  37.387 28.149  1.00 70.13  ? 475 GLN A CA  1 
ATOM   2870 C  C   . GLN A 1 376 ? 20.100  37.296 28.843  1.00 70.83  ? 475 GLN A C   1 
ATOM   2871 O  O   . GLN A 1 376 ? 21.117  37.612 28.230  1.00 70.92  ? 475 GLN A O   1 
ATOM   2872 C  CB  . GLN A 1 376 ? 18.743  36.593 26.849  1.00 71.19  ? 475 GLN A CB  1 
ATOM   2873 C  CG  . GLN A 1 376 ? 17.908  35.333 26.933  1.00 73.20  ? 475 GLN A CG  1 
ATOM   2874 C  CD  . GLN A 1 376 ? 16.473  35.581 27.321  1.00 75.62  ? 475 GLN A CD  1 
ATOM   2875 O  OE1 . GLN A 1 376 ? 15.746  36.331 26.678  1.00 78.04  ? 475 GLN A OE1 1 
ATOM   2876 N  NE2 . GLN A 1 376 ? 16.033  34.937 28.370  1.00 74.54  ? 475 GLN A NE2 1 
ATOM   2877 N  N   . PHE A 1 377 ? 20.103  36.988 30.145  1.00 71.05  ? 476 PHE A N   1 
ATOM   2878 C  CA  . PHE A 1 377 ? 21.316  36.967 30.951  1.00 71.86  ? 476 PHE A CA  1 
ATOM   2879 C  C   . PHE A 1 377 ? 21.761  35.551 31.416  1.00 72.27  ? 476 PHE A C   1 
ATOM   2880 O  O   . PHE A 1 377 ? 21.204  34.557 30.970  1.00 72.48  ? 476 PHE A O   1 
ATOM   2881 C  CB  . PHE A 1 377 ? 21.131  37.926 32.145  1.00 72.16  ? 476 PHE A CB  1 
ATOM   2882 C  CG  . PHE A 1 377 ? 19.906  37.671 32.989  1.00 73.42  ? 476 PHE A CG  1 
ATOM   2883 C  CD1 . PHE A 1 377 ? 19.821  36.548 33.799  1.00 74.32  ? 476 PHE A CD1 1 
ATOM   2884 C  CD2 . PHE A 1 377 ? 18.841  38.556 32.979  1.00 74.51  ? 476 PHE A CD2 1 
ATOM   2885 C  CE1 . PHE A 1 377 ? 18.685  36.304 34.559  1.00 75.10  ? 476 PHE A CE1 1 
ATOM   2886 C  CE2 . PHE A 1 377 ? 17.716  38.324 33.765  1.00 75.25  ? 476 PHE A CE2 1 
ATOM   2887 C  CZ  . PHE A 1 377 ? 17.649  37.202 34.553  1.00 75.07  ? 476 PHE A CZ  1 
ATOM   2888 N  N   . ARG A 1 378 ? 22.783  35.468 32.296  1.00 72.16  ? 477 ARG A N   1 
ATOM   2889 C  CA  . ARG A 1 378 ? 23.277  34.225 32.874  1.00 72.22  ? 477 ARG A CA  1 
ATOM   2890 C  C   . ARG A 1 378 ? 23.230  34.387 34.382  1.00 72.81  ? 477 ARG A C   1 
ATOM   2891 O  O   . ARG A 1 378 ? 23.824  35.326 34.914  1.00 72.84  ? 477 ARG A O   1 
ATOM   2892 C  CB  . ARG A 1 378 ? 24.720  33.963 32.441  1.00 72.77  ? 477 ARG A CB  1 
ATOM   2893 C  CG  . ARG A 1 378 ? 24.901  33.935 30.944  1.00 75.34  ? 477 ARG A CG  1 
ATOM   2894 C  CD  . ARG A 1 378 ? 24.213  32.739 30.306  1.00 78.00  ? 477 ARG A CD  1 
ATOM   2895 N  NE  . ARG A 1 378 ? 24.872  31.465 30.619  1.00 80.11  ? 477 ARG A NE  1 
ATOM   2896 C  CZ  . ARG A 1 378 ? 25.952  31.005 29.989  1.00 82.13  ? 477 ARG A CZ  1 
ATOM   2897 N  NH1 . ARG A 1 378 ? 26.533  31.728 29.038  1.00 81.74  ? 477 ARG A NH1 1 
ATOM   2898 N  NH2 . ARG A 1 378 ? 26.469  29.832 30.316  1.00 82.29  ? 477 ARG A NH2 1 
ATOM   2899 N  N   . ILE A 1 379 ? 22.502  33.504 35.077  1.00 73.09  ? 478 ILE A N   1 
ATOM   2900 C  CA  . ILE A 1 379 ? 22.410  33.585 36.535  1.00 73.68  ? 478 ILE A CA  1 
ATOM   2901 C  C   . ILE A 1 379 ? 23.747  33.170 37.164  1.00 74.49  ? 478 ILE A C   1 
ATOM   2902 O  O   . ILE A 1 379 ? 24.269  32.098 36.849  1.00 74.78  ? 478 ILE A O   1 
ATOM   2903 C  CB  . ILE A 1 379 ? 21.238  32.723 37.073  1.00 73.67  ? 478 ILE A CB  1 
ATOM   2904 C  CG1 . ILE A 1 379 ? 19.888  33.151 36.463  1.00 74.40  ? 478 ILE A CG1 1 
ATOM   2905 C  CG2 . ILE A 1 379 ? 21.204  32.734 38.600  1.00 73.91  ? 478 ILE A CG2 1 
ATOM   2906 C  CD1 . ILE A 1 379 ? 18.710  32.252 36.825  1.00 75.52  ? 478 ILE A CD1 1 
ATOM   2907 N  N   . LEU A 1 380 ? 24.334  34.039 37.997  1.00 74.59  ? 479 LEU A N   1 
ATOM   2908 C  CA  . LEU A 1 380 ? 25.592  33.723 38.678  1.00 74.97  ? 479 LEU A CA  1 
ATOM   2909 C  C   . LEU A 1 380 ? 25.250  33.004 39.984  1.00 75.86  ? 479 LEU A C   1 
ATOM   2910 O  O   . LEU A 1 380 ? 25.799  31.943 40.275  1.00 76.06  ? 479 LEU A O   1 
ATOM   2911 C  CB  . LEU A 1 380 ? 26.423  34.991 38.947  1.00 74.61  ? 479 LEU A CB  1 
ATOM   2912 C  CG  . LEU A 1 380 ? 26.750  35.843 37.725  1.00 75.37  ? 479 LEU A CG  1 
ATOM   2913 C  CD1 . LEU A 1 380 ? 27.499  37.092 38.118  1.00 75.86  ? 479 LEU A CD1 1 
ATOM   2914 C  CD2 . LEU A 1 380 ? 27.550  35.072 36.710  1.00 75.62  ? 479 LEU A CD2 1 
ATOM   2915 N  N   . SER A 1 381 ? 24.296  33.555 40.738  1.00 76.23  ? 480 SER A N   1 
ATOM   2916 C  CA  . SER A 1 381 ? 23.844  32.958 41.980  1.00 77.17  ? 480 SER A CA  1 
ATOM   2917 C  C   . SER A 1 381 ? 22.317  33.072 42.082  1.00 78.15  ? 480 SER A C   1 
ATOM   2918 O  O   . SER A 1 381 ? 21.761  34.159 41.941  1.00 78.18  ? 480 SER A O   1 
ATOM   2919 C  CB  . SER A 1 381 ? 24.523  33.633 43.168  1.00 78.07  ? 480 SER A CB  1 
ATOM   2920 O  OG  . SER A 1 381 ? 23.884  33.358 44.405  1.00 80.04  ? 480 SER A OG  1 
ATOM   2921 N  N   . GLU A 1 382 ? 21.646  31.945 42.312  1.00 78.56  ? 481 GLU A N   1 
ATOM   2922 C  CA  . GLU A 1 382 ? 20.203  31.941 42.471  1.00 79.44  ? 481 GLU A CA  1 
ATOM   2923 C  C   . GLU A 1 382 ? 19.848  31.624 43.927  1.00 80.00  ? 481 GLU A C   1 
ATOM   2924 O  O   . GLU A 1 382 ? 20.008  30.482 44.361  1.00 80.04  ? 481 GLU A O   1 
ATOM   2925 C  CB  . GLU A 1 382 ? 19.567  30.925 41.526  1.00 81.89  ? 481 GLU A CB  1 
ATOM   2926 C  CG  . GLU A 1 382 ? 18.058  31.042 41.463  1.00 86.05  ? 481 GLU A CG  1 
ATOM   2927 C  CD  . GLU A 1 382 ? 17.490  30.486 40.176  1.00 91.48  ? 481 GLU A CD  1 
ATOM   2928 O  OE1 . GLU A 1 382 ? 18.007  29.455 39.687  1.00 91.37  ? 481 GLU A OE1 1 
ATOM   2929 O  OE2 . GLU A 1 382 ? 16.535  31.095 39.644  1.00 94.36  ? 481 GLU A OE2 1 
ATOM   2930 N  N   . ASN A 1 383 ? 19.416  32.650 44.683  1.00 80.19  ? 482 ASN A N   1 
ATOM   2931 C  CA  . ASN A 1 383 ? 19.031  32.554 46.089  1.00 80.74  ? 482 ASN A CA  1 
ATOM   2932 C  C   . ASN A 1 383 ? 20.169  31.998 46.955  1.00 81.84  ? 482 ASN A C   1 
ATOM   2933 O  O   . ASN A 1 383 ? 19.937  31.186 47.854  1.00 81.87  ? 482 ASN A O   1 
ATOM   2934 C  CB  . ASN A 1 383 ? 17.768  31.724 46.235  1.00 81.13  ? 482 ASN A CB  1 
ATOM   2935 C  CG  . ASN A 1 383 ? 16.702  32.372 47.073  1.00 83.68  ? 482 ASN A CG  1 
ATOM   2936 O  OD1 . ASN A 1 383 ? 16.765  33.555 47.416  1.00 84.40  ? 482 ASN A OD1 1 
ATOM   2937 N  ND2 . ASN A 1 383 ? 15.684  31.603 47.418  1.00 84.37  ? 482 ASN A ND2 1 
ATOM   2938 N  N   . GLY A 1 384 ? 21.392  32.429 46.661  1.00 82.32  ? 483 GLY A N   1 
ATOM   2939 C  CA  . GLY A 1 384 ? 22.568  31.971 47.385  1.00 83.14  ? 483 GLY A CA  1 
ATOM   2940 C  C   . GLY A 1 384 ? 23.290  30.842 46.676  1.00 83.63  ? 483 GLY A C   1 
ATOM   2941 O  O   . GLY A 1 384 ? 24.462  30.982 46.311  1.00 84.10  ? 483 GLY A O   1 
ATOM   2942 N  N   . LYS A 1 385 ? 22.594  29.720 46.457  1.00 83.24  ? 484 LYS A N   1 
ATOM   2943 C  CA  . LYS A 1 385 ? 23.178  28.563 45.770  1.00 83.59  ? 484 LYS A CA  1 
ATOM   2944 C  C   . LYS A 1 385 ? 23.412  28.844 44.270  1.00 83.10  ? 484 LYS A C   1 
ATOM   2945 O  O   . LYS A 1 385 ? 22.690  29.652 43.684  1.00 83.08  ? 484 LYS A O   1 
ATOM   2946 C  CB  . LYS A 1 385 ? 22.256  27.325 45.929  1.00 85.70  ? 484 LYS A CB  1 
ATOM   2947 C  CG  . LYS A 1 385 ? 21.765  27.089 47.353  1.00 89.74  ? 484 LYS A CG  1 
ATOM   2948 C  CD  . LYS A 1 385 ? 21.136  25.732 47.535  1.00 94.26  ? 484 LYS A CD  1 
ATOM   2949 C  CE  . LYS A 1 385 ? 20.620  25.558 48.941  1.00 98.62  ? 484 LYS A CE  1 
ATOM   2950 N  NZ  . LYS A 1 385 ? 20.329  24.128 49.241  1.00 101.44 ? 484 LYS A NZ  1 
ATOM   2951 N  N   . PRO A 1 386 ? 24.385  28.174 43.613  1.00 82.39  ? 485 PRO A N   1 
ATOM   2952 C  CA  . PRO A 1 386 ? 24.558  28.375 42.163  1.00 82.09  ? 485 PRO A CA  1 
ATOM   2953 C  C   . PRO A 1 386 ? 23.323  27.885 41.383  1.00 82.04  ? 485 PRO A C   1 
ATOM   2954 O  O   . PRO A 1 386 ? 22.531  27.094 41.916  1.00 82.52  ? 485 PRO A O   1 
ATOM   2955 C  CB  . PRO A 1 386 ? 25.804  27.538 41.835  1.00 82.60  ? 485 PRO A CB  1 
ATOM   2956 C  CG  . PRO A 1 386 ? 26.446  27.249 43.135  1.00 83.15  ? 485 PRO A CG  1 
ATOM   2957 C  CD  . PRO A 1 386 ? 25.329  27.166 44.121  1.00 81.73  ? 485 PRO A CD  1 
ATOM   2958 N  N   . PRO A 1 387 ? 23.098  28.361 40.137  1.00 81.13  ? 486 PRO A N   1 
ATOM   2959 C  CA  . PRO A 1 387 ? 21.899  27.927 39.404  1.00 80.30  ? 486 PRO A CA  1 
ATOM   2960 C  C   . PRO A 1 387 ? 21.960  26.466 38.989  1.00 79.61  ? 486 PRO A C   1 
ATOM   2961 O  O   . PRO A 1 387 ? 23.045  25.959 38.705  1.00 80.39  ? 486 PRO A O   1 
ATOM   2962 C  CB  . PRO A 1 387 ? 21.892  28.846 38.181  1.00 81.02  ? 486 PRO A CB  1 
ATOM   2963 C  CG  . PRO A 1 387 ? 23.319  29.168 37.957  1.00 81.61  ? 486 PRO A CG  1 
ATOM   2964 C  CD  . PRO A 1 387 ? 23.903  29.305 39.334  1.00 80.49  ? 486 PRO A CD  1 
ATOM   2965 N  N   . ALA A 1 388 ? 20.804  25.793 38.935  1.00 77.98  ? 487 ALA A N   1 
ATOM   2966 C  CA  . ALA A 1 388 ? 20.728  24.398 38.505  1.00 77.12  ? 487 ALA A CA  1 
ATOM   2967 C  C   . ALA A 1 388 ? 21.257  24.232 37.062  1.00 75.87  ? 487 ALA A C   1 
ATOM   2968 O  O   . ALA A 1 388 ? 21.422  25.230 36.356  1.00 75.85  ? 487 ALA A O   1 
ATOM   2969 C  CB  . ALA A 1 388 ? 19.284  23.918 38.602  1.00 77.50  ? 487 ALA A CB  1 
ATOM   2970 N  N   . ALA A 1 389 ? 21.524  22.991 36.609  1.00 74.81  ? 488 ALA A N   1 
ATOM   2971 C  CA  . ALA A 1 389 ? 22.021  22.764 35.253  1.00 74.29  ? 488 ALA A CA  1 
ATOM   2972 C  C   . ALA A 1 389 ? 21.100  23.370 34.181  1.00 73.77  ? 488 ALA A C   1 
ATOM   2973 O  O   . ALA A 1 389 ? 21.571  24.091 33.306  1.00 73.47  ? 488 ALA A O   1 
ATOM   2974 C  CB  . ALA A 1 389 ? 22.223  21.277 35.010  1.00 74.38  ? 488 ALA A CB  1 
ATOM   2975 N  N   . HIS A 1 390 ? 19.782  23.154 34.305  1.00 73.43  ? 489 HIS A N   1 
ATOM   2976 C  CA  . HIS A 1 390 ? 18.817  23.705 33.353  1.00 73.05  ? 489 HIS A CA  1 
ATOM   2977 C  C   . HIS A 1 390 ? 18.574  25.221 33.536  1.00 72.85  ? 489 HIS A C   1 
ATOM   2978 O  O   . HIS A 1 390 ? 18.097  25.879 32.611  1.00 73.14  ? 489 HIS A O   1 
ATOM   2979 C  CB  . HIS A 1 390 ? 17.504  22.918 33.405  1.00 72.86  ? 489 HIS A CB  1 
ATOM   2980 C  CG  . HIS A 1 390 ? 16.835  22.994 34.734  1.00 73.90  ? 489 HIS A CG  1 
ATOM   2981 N  ND1 . HIS A 1 390 ? 17.444  22.508 35.871  1.00 75.66  ? 489 HIS A ND1 1 
ATOM   2982 C  CD2 . HIS A 1 390 ? 15.629  23.502 35.068  1.00 74.79  ? 489 HIS A CD2 1 
ATOM   2983 C  CE1 . HIS A 1 390 ? 16.595  22.738 36.859  1.00 76.02  ? 489 HIS A CE1 1 
ATOM   2984 N  NE2 . HIS A 1 390 ? 15.490  23.335 36.423  1.00 75.73  ? 489 HIS A NE2 1 
ATOM   2985 N  N   . ARG A 1 391 ? 18.922  25.777 34.698  1.00 72.14  ? 490 ARG A N   1 
ATOM   2986 C  CA  . ARG A 1 391 ? 18.748  27.207 34.951  1.00 72.20  ? 490 ARG A CA  1 
ATOM   2987 C  C   . ARG A 1 391 ? 20.036  28.038 34.766  1.00 72.80  ? 490 ARG A C   1 
ATOM   2988 O  O   . ARG A 1 391 ? 20.064  29.215 35.123  1.00 72.74  ? 490 ARG A O   1 
ATOM   2989 C  CB  . ARG A 1 391 ? 18.176  27.418 36.351  1.00 72.67  ? 490 ARG A CB  1 
ATOM   2990 C  CG  . ARG A 1 391 ? 16.873  26.676 36.543  1.00 74.21  ? 490 ARG A CG  1 
ATOM   2991 C  CD  . ARG A 1 391 ? 16.254  26.953 37.886  1.00 75.90  ? 490 ARG A CD  1 
ATOM   2992 N  NE  . ARG A 1 391 ? 15.880  28.354 38.055  1.00 77.54  ? 490 ARG A NE  1 
ATOM   2993 C  CZ  . ARG A 1 391 ? 14.752  28.891 37.606  1.00 79.23  ? 490 ARG A CZ  1 
ATOM   2994 N  NH1 . ARG A 1 391 ? 13.892  28.160 36.905  1.00 79.24  ? 490 ARG A NH1 1 
ATOM   2995 N  NH2 . ARG A 1 391 ? 14.485  30.171 37.830  1.00 78.61  ? 490 ARG A NH2 1 
ATOM   2996 N  N   . SER A 1 392 ? 21.091  27.439 34.196  1.00 72.98  ? 491 SER A N   1 
ATOM   2997 C  CA  . SER A 1 392 ? 22.375  28.110 34.011  1.00 73.45  ? 491 SER A CA  1 
ATOM   2998 C  C   . SER A 1 392 ? 22.633  28.653 32.593  1.00 73.18  ? 491 SER A C   1 
ATOM   2999 O  O   . SER A 1 392 ? 23.727  29.168 32.327  1.00 73.62  ? 491 SER A O   1 
ATOM   3000 C  CB  . SER A 1 392 ? 23.503  27.168 34.403  1.00 75.27  ? 491 SER A CB  1 
ATOM   3001 O  OG  . SER A 1 392 ? 23.466  26.038 33.548  1.00 78.60  ? 491 SER A OG  1 
ATOM   3002 N  N   . GLY A 1 393 ? 21.648  28.544 31.705  1.00 72.14  ? 492 GLY A N   1 
ATOM   3003 C  CA  . GLY A 1 393 ? 21.787  29.029 30.338  1.00 71.47  ? 492 GLY A CA  1 
ATOM   3004 C  C   . GLY A 1 393 ? 21.237  30.427 30.196  1.00 70.56  ? 492 GLY A C   1 
ATOM   3005 O  O   . GLY A 1 393 ? 21.447  31.263 31.073  1.00 70.61  ? 492 GLY A O   1 
ATOM   3006 N  N   . TRP A 1 394 ? 20.499  30.684 29.114  1.00 69.52  ? 493 TRP A N   1 
ATOM   3007 C  CA  . TRP A 1 394 ? 19.897  31.990 28.897  1.00 69.10  ? 493 TRP A CA  1 
ATOM   3008 C  C   . TRP A 1 394 ? 18.557  32.152 29.600  1.00 67.37  ? 493 TRP A C   1 
ATOM   3009 O  O   . TRP A 1 394 ? 17.572  31.498 29.259  1.00 66.85  ? 493 TRP A O   1 
ATOM   3010 C  CB  . TRP A 1 394 ? 19.800  32.316 27.410  1.00 69.77  ? 493 TRP A CB  1 
ATOM   3011 C  CG  . TRP A 1 394 ? 21.131  32.363 26.743  1.00 71.12  ? 493 TRP A CG  1 
ATOM   3012 C  CD1 . TRP A 1 394 ? 21.649  31.439 25.891  1.00 72.37  ? 493 TRP A CD1 1 
ATOM   3013 C  CD2 . TRP A 1 394 ? 22.153  33.342 26.946  1.00 71.77  ? 493 TRP A CD2 1 
ATOM   3014 N  NE1 . TRP A 1 394 ? 22.927  31.790 25.536  1.00 72.98  ? 493 TRP A NE1 1 
ATOM   3015 C  CE2 . TRP A 1 394 ? 23.265  32.952 26.178  1.00 72.68  ? 493 TRP A CE2 1 
ATOM   3016 C  CE3 . TRP A 1 394 ? 22.245  34.502 27.720  1.00 72.57  ? 493 TRP A CE3 1 
ATOM   3017 C  CZ2 . TRP A 1 394 ? 24.439  33.696 26.138  1.00 73.20  ? 493 TRP A CZ2 1 
ATOM   3018 C  CZ3 . TRP A 1 394 ? 23.414  35.231 27.685  1.00 73.34  ? 493 TRP A CZ3 1 
ATOM   3019 C  CH2 . TRP A 1 394 ? 24.488  34.833 26.893  1.00 73.30  ? 493 TRP A CH2 1 
ATOM   3020 N  N   . LYS A 1 395 ? 18.534  33.023 30.603  1.00 66.25  ? 494 LYS A N   1 
ATOM   3021 C  CA  . LYS A 1 395 ? 17.343  33.278 31.395  1.00 65.71  ? 494 LYS A CA  1 
ATOM   3022 C  C   . LYS A 1 395 ? 16.995  34.763 31.424  1.00 65.22  ? 494 LYS A C   1 
ATOM   3023 O  O   . LYS A 1 395 ? 17.881  35.593 31.373  1.00 65.26  ? 494 LYS A O   1 
ATOM   3024 C  CB  . LYS A 1 395 ? 17.586  32.806 32.842  1.00 66.58  ? 494 LYS A CB  1 
ATOM   3025 C  CG  . LYS A 1 395 ? 17.865  31.323 32.985  1.00 68.66  ? 494 LYS A CG  1 
ATOM   3026 C  CD  . LYS A 1 395 ? 16.604  30.491 32.871  1.00 71.58  ? 494 LYS A CD  1 
ATOM   3027 C  CE  . LYS A 1 395 ? 15.865  30.400 34.181  1.00 74.25  ? 494 LYS A CE  1 
ATOM   3028 N  NZ  . LYS A 1 395 ? 14.969  31.558 34.404  1.00 75.81  ? 494 LYS A NZ  1 
ATOM   3029 N  N   . ASP A 1 396 ? 15.716  35.097 31.461  1.00 64.81  ? 495 ASP A N   1 
ATOM   3030 C  CA  . ASP A 1 396 ? 15.273  36.485 31.648  1.00 65.47  ? 495 ASP A CA  1 
ATOM   3031 C  C   . ASP A 1 396 ? 14.563  36.689 33.000  1.00 66.67  ? 495 ASP A C   1 
ATOM   3032 O  O   . ASP A 1 396 ? 14.073  37.778 33.286  1.00 66.89  ? 495 ASP A O   1 
ATOM   3033 C  CB  . ASP A 1 396 ? 14.408  37.019 30.488  1.00 65.99  ? 495 ASP A CB  1 
ATOM   3034 C  CG  . ASP A 1 396 ? 13.177  36.216 30.127  1.00 66.74  ? 495 ASP A CG  1 
ATOM   3035 O  OD1 . ASP A 1 396 ? 12.260  36.120 30.970  1.00 66.45  ? 495 ASP A OD1 1 
ATOM   3036 O  OD2 . ASP A 1 396 ? 13.111  35.726 28.989  1.00 67.88  ? 495 ASP A OD2 1 
ATOM   3037 N  N   . THR A 1 397 ? 14.521  35.630 33.817  1.00 67.07  ? 496 THR A N   1 
ATOM   3038 C  CA  . THR A 1 397 ? 13.906  35.538 35.116  1.00 67.96  ? 496 THR A CA  1 
ATOM   3039 C  C   . THR A 1 397 ? 14.916  34.840 36.045  1.00 69.62  ? 496 THR A C   1 
ATOM   3040 O  O   . THR A 1 397 ? 15.672  33.970 35.610  1.00 69.73  ? 496 THR A O   1 
ATOM   3041 C  CB  . THR A 1 397 ? 12.587  34.745 34.979  1.00 68.44  ? 496 THR A CB  1 
ATOM   3042 O  OG1 . THR A 1 397 ? 11.781  35.318 33.940  1.00 69.14  ? 496 THR A OG1 1 
ATOM   3043 C  CG2 . THR A 1 397 ? 11.798  34.693 36.266  1.00 68.45  ? 496 THR A CG2 1 
ATOM   3044 N  N   . VAL A 1 398 ? 14.955  35.252 37.313  1.00 70.71  ? 497 VAL A N   1 
ATOM   3045 C  CA  . VAL A 1 398 ? 15.825  34.654 38.319  1.00 72.30  ? 497 VAL A CA  1 
ATOM   3046 C  C   . VAL A 1 398 ? 15.041  34.589 39.631  1.00 73.90  ? 497 VAL A C   1 
ATOM   3047 O  O   . VAL A 1 398 ? 14.337  35.539 39.964  1.00 74.05  ? 497 VAL A O   1 
ATOM   3048 C  CB  . VAL A 1 398 ? 17.176  35.409 38.447  1.00 73.41  ? 497 VAL A CB  1 
ATOM   3049 C  CG1 . VAL A 1 398 ? 16.973  36.895 38.747  1.00 74.04  ? 497 VAL A CG1 1 
ATOM   3050 C  CG2 . VAL A 1 398 ? 18.080  34.760 39.489  1.00 74.07  ? 497 VAL A CG2 1 
ATOM   3051 N  N   . ARG A 1 399 ? 15.099  33.456 40.348  1.00 75.09  ? 498 ARG A N   1 
ATOM   3052 C  CA  . ARG A 1 399 ? 14.351  33.306 41.603  1.00 76.74  ? 498 ARG A CA  1 
ATOM   3053 C  C   . ARG A 1 399 ? 14.890  34.174 42.747  1.00 77.74  ? 498 ARG A C   1 
ATOM   3054 O  O   . ARG A 1 399 ? 16.074  34.109 43.062  1.00 78.16  ? 498 ARG A O   1 
ATOM   3055 C  CB  . ARG A 1 399 ? 14.316  31.838 42.050  1.00 78.49  ? 498 ARG A CB  1 
ATOM   3056 C  CG  . ARG A 1 399 ? 13.368  31.612 43.209  1.00 82.07  ? 498 ARG A CG  1 
ATOM   3057 C  CD  . ARG A 1 399 ? 13.655  30.329 43.938  1.00 86.51  ? 498 ARG A CD  1 
ATOM   3058 N  NE  . ARG A 1 399 ? 12.417  29.755 44.463  1.00 91.41  ? 498 ARG A NE  1 
ATOM   3059 C  CZ  . ARG A 1 399 ? 11.710  28.807 43.848  1.00 95.13  ? 498 ARG A CZ  1 
ATOM   3060 N  NH1 . ARG A 1 399 ? 12.137  28.285 42.700  1.00 95.21  ? 498 ARG A NH1 1 
ATOM   3061 N  NH2 . ARG A 1 399 ? 10.584  28.352 44.390  1.00 95.26  ? 498 ARG A NH2 1 
ATOM   3062 N  N   . VAL A 1 400 ? 14.031  34.990 43.364  1.00 77.99  ? 499 VAL A N   1 
ATOM   3063 C  CA  . VAL A 1 400 ? 14.431  35.811 44.503  1.00 79.14  ? 499 VAL A CA  1 
ATOM   3064 C  C   . VAL A 1 400 ? 13.419  35.550 45.622  1.00 80.33  ? 499 VAL A C   1 
ATOM   3065 O  O   . VAL A 1 400 ? 12.386  36.202 45.673  1.00 80.60  ? 499 VAL A O   1 
ATOM   3066 C  CB  . VAL A 1 400 ? 14.536  37.317 44.162  1.00 80.06  ? 499 VAL A CB  1 
ATOM   3067 C  CG1 . VAL A 1 400 ? 15.082  38.097 45.346  1.00 80.61  ? 499 VAL A CG1 1 
ATOM   3068 C  CG2 . VAL A 1 400 ? 15.403  37.555 42.929  1.00 80.64  ? 499 VAL A CG2 1 
ATOM   3069 N  N   . GLU A 1 401 ? 13.689  34.572 46.491  1.00 80.86  ? 500 GLU A N   1 
ATOM   3070 C  CA  . GLU A 1 401 ? 12.751  34.191 47.540  1.00 81.89  ? 500 GLU A CA  1 
ATOM   3071 C  C   . GLU A 1 401 ? 13.442  34.069 48.899  1.00 83.30  ? 500 GLU A C   1 
ATOM   3072 O  O   . GLU A 1 401 ? 13.978  33.013 49.226  1.00 83.54  ? 500 GLU A O   1 
ATOM   3073 C  CB  . GLU A 1 401 ? 12.105  32.856 47.143  1.00 83.26  ? 500 GLU A CB  1 
ATOM   3074 C  CG  . GLU A 1 401 ? 10.977  32.362 48.026  1.00 86.62  ? 500 GLU A CG  1 
ATOM   3075 C  CD  . GLU A 1 401 ? 10.570  30.933 47.711  1.00 91.71  ? 500 GLU A CD  1 
ATOM   3076 O  OE1 . GLU A 1 401 ? 9.384   30.587 47.921  1.00 92.31  ? 500 GLU A OE1 1 
ATOM   3077 O  OE2 . GLU A 1 401 ? 11.440  30.158 47.249  1.00 93.25  ? 500 GLU A OE2 1 
ATOM   3078 N  N   . GLY A 1 402 ? 13.431  35.144 49.679  1.00 83.96  ? 501 GLY A N   1 
ATOM   3079 C  CA  . GLY A 1 402 ? 14.024  35.132 51.013  1.00 85.00  ? 501 GLY A CA  1 
ATOM   3080 C  C   . GLY A 1 402 ? 15.477  35.565 51.119  1.00 85.95  ? 501 GLY A C   1 
ATOM   3081 O  O   . GLY A 1 402 ? 15.870  36.154 52.128  1.00 86.02  ? 501 GLY A O   1 
ATOM   3082 N  N   . TRP A 1 403 ? 16.299  35.241 50.118  1.00 86.52  ? 502 TRP A N   1 
ATOM   3083 C  CA  . TRP A 1 403 ? 17.709  35.637 50.135  1.00 87.73  ? 502 TRP A CA  1 
ATOM   3084 C  C   . TRP A 1 403 ? 18.017  36.526 48.880  1.00 87.38  ? 502 TRP A C   1 
ATOM   3085 O  O   . TRP A 1 403 ? 17.101  37.161 48.356  1.00 87.65  ? 502 TRP A O   1 
ATOM   3086 C  CB  . TRP A 1 403 ? 18.639  34.399 50.341  1.00 88.81  ? 502 TRP A CB  1 
ATOM   3087 C  CG  . TRP A 1 403 ? 20.109  34.707 50.552  1.00 90.76  ? 502 TRP A CG  1 
ATOM   3088 C  CD1 . TRP A 1 403 ? 21.153  34.284 49.777  1.00 92.08  ? 502 TRP A CD1 1 
ATOM   3089 C  CD2 . TRP A 1 403 ? 20.686  35.539 51.576  1.00 91.39  ? 502 TRP A CD2 1 
ATOM   3090 N  NE1 . TRP A 1 403 ? 22.340  34.793 50.258  1.00 92.52  ? 502 TRP A NE1 1 
ATOM   3091 C  CE2 . TRP A 1 403 ? 22.081  35.567 51.359  1.00 92.29  ? 502 TRP A CE2 1 
ATOM   3092 C  CE3 . TRP A 1 403 ? 20.162  36.250 52.663  1.00 92.15  ? 502 TRP A CE3 1 
ATOM   3093 C  CZ2 . TRP A 1 403 ? 22.950  36.287 52.180  1.00 93.13  ? 502 TRP A CZ2 1 
ATOM   3094 C  CZ3 . TRP A 1 403 ? 21.025  36.962 53.473  1.00 93.18  ? 502 TRP A CZ3 1 
ATOM   3095 C  CH2 . TRP A 1 403 ? 22.400  36.982 53.225  1.00 93.30  ? 502 TRP A CH2 1 
ATOM   3096 N  N   . ARG A 1 404 ? 19.274  36.626 48.440  1.00 86.42  ? 503 ARG A N   1 
ATOM   3097 C  CA  . ARG A 1 404 ? 19.639  37.452 47.307  1.00 86.39  ? 503 ARG A CA  1 
ATOM   3098 C  C   . ARG A 1 404 ? 20.152  36.635 46.132  1.00 85.82  ? 503 ARG A C   1 
ATOM   3099 O  O   . ARG A 1 404 ? 20.795  35.599 46.308  1.00 86.02  ? 503 ARG A O   1 
ATOM   3100 C  CB  . ARG A 1 404 ? 20.650  38.546 47.716  1.00 87.98  ? 503 ARG A CB  1 
ATOM   3101 C  CG  . ARG A 1 404 ? 21.785  38.046 48.612  1.00 91.13  ? 503 ARG A CG  1 
ATOM   3102 C  CD  . ARG A 1 404 ? 22.834  39.106 48.901  1.00 93.97  ? 503 ARG A CD  1 
ATOM   3103 N  NE  . ARG A 1 404 ? 23.459  38.882 50.203  1.00 96.88  ? 503 ARG A NE  1 
ATOM   3104 C  CZ  . ARG A 1 404 ? 23.349  39.706 51.240  1.00 99.80  ? 503 ARG A CZ  1 
ATOM   3105 N  NH1 . ARG A 1 404 ? 22.683  40.848 51.122  1.00 99.99  ? 503 ARG A NH1 1 
ATOM   3106 N  NH2 . ARG A 1 404 ? 23.925  39.406 52.397  1.00 100.00 ? 503 ARG A NH2 1 
ATOM   3107 N  N   . SER A 1 405 ? 19.858  37.124 44.926  1.00 85.02  ? 504 SER A N   1 
ATOM   3108 C  CA  . SER A 1 405 ? 20.271  36.536 43.662  1.00 84.38  ? 504 SER A CA  1 
ATOM   3109 C  C   . SER A 1 405 ? 21.162  37.518 42.923  1.00 83.57  ? 504 SER A C   1 
ATOM   3110 O  O   . SER A 1 405 ? 21.030  38.726 43.095  1.00 83.59  ? 504 SER A O   1 
ATOM   3111 C  CB  . SER A 1 405 ? 19.058  36.210 42.801  1.00 85.73  ? 504 SER A CB  1 
ATOM   3112 O  OG  . SER A 1 405 ? 18.532  34.931 43.102  1.00 87.79  ? 504 SER A OG  1 
ATOM   3113 N  N   . GLU A 1 406 ? 22.057  37.004 42.085  1.00 82.65  ? 505 GLU A N   1 
ATOM   3114 C  CA  . GLU A 1 406 ? 22.971  37.842 41.326  1.00 82.17  ? 505 GLU A CA  1 
ATOM   3115 C  C   . GLU A 1 406 ? 23.120  37.292 39.909  1.00 80.90  ? 505 GLU A C   1 
ATOM   3116 O  O   . GLU A 1 406 ? 23.334  36.099 39.735  1.00 80.83  ? 505 GLU A O   1 
ATOM   3117 C  CB  . GLU A 1 406 ? 24.319  37.931 42.056  1.00 85.07  ? 505 GLU A CB  1 
ATOM   3118 C  CG  . GLU A 1 406 ? 25.450  38.584 41.285  1.00 90.93  ? 505 GLU A CG  1 
ATOM   3119 C  CD  . GLU A 1 406 ? 26.773  38.440 42.007  1.00 97.80  ? 505 GLU A CD  1 
ATOM   3120 O  OE1 . GLU A 1 406 ? 26.988  39.178 42.997  1.00 99.18  ? 505 GLU A OE1 1 
ATOM   3121 O  OE2 . GLU A 1 406 ? 27.583  37.574 41.601  1.00 99.66  ? 505 GLU A OE2 1 
ATOM   3122 N  N   . VAL A 1 407 ? 22.958  38.157 38.897  1.00 79.78  ? 506 VAL A N   1 
ATOM   3123 C  CA  . VAL A 1 407 ? 23.031  37.776 37.484  1.00 79.07  ? 506 VAL A CA  1 
ATOM   3124 C  C   . VAL A 1 407 ? 24.017  38.650 36.693  1.00 77.92  ? 506 VAL A C   1 
ATOM   3125 O  O   . VAL A 1 407 ? 24.345  39.761 37.105  1.00 77.83  ? 506 VAL A O   1 
ATOM   3126 C  CB  . VAL A 1 407 ? 21.618  37.799 36.823  1.00 79.82  ? 506 VAL A CB  1 
ATOM   3127 C  CG1 . VAL A 1 407 ? 20.674  36.814 37.497  1.00 80.42  ? 506 VAL A CG1 1 
ATOM   3128 C  CG2 . VAL A 1 407 ? 21.026  39.204 36.831  1.00 80.13  ? 506 VAL A CG2 1 
ATOM   3129 N  N   . LEU A 1 408 ? 24.451  38.157 35.537  1.00 76.99  ? 507 LEU A N   1 
ATOM   3130 C  CA  . LEU A 1 408 ? 25.352  38.898 34.677  1.00 76.85  ? 507 LEU A CA  1 
ATOM   3131 C  C   . LEU A 1 408 ? 24.571  39.373 33.443  1.00 76.91  ? 507 LEU A C   1 
ATOM   3132 O  O   . LEU A 1 408 ? 24.412  38.629 32.460  1.00 77.03  ? 507 LEU A O   1 
ATOM   3133 C  CB  . LEU A 1 408 ? 26.561  38.033 34.294  1.00 76.85  ? 507 LEU A CB  1 
ATOM   3134 C  CG  . LEU A 1 408 ? 27.535  38.670 33.326  1.00 78.24  ? 507 LEU A CG  1 
ATOM   3135 C  CD1 . LEU A 1 408 ? 28.359  39.724 33.996  1.00 78.93  ? 507 LEU A CD1 1 
ATOM   3136 C  CD2 . LEU A 1 408 ? 28.419  37.643 32.698  1.00 78.97  ? 507 LEU A CD2 1 
ATOM   3137 N  N   . VAL A 1 409 ? 24.058  40.617 33.520  1.00 76.33  ? 508 VAL A N   1 
ATOM   3138 C  CA  . VAL A 1 409 ? 23.278  41.246 32.456  1.00 76.38  ? 508 VAL A CA  1 
ATOM   3139 C  C   . VAL A 1 409 ? 24.142  42.048 31.485  1.00 76.75  ? 508 VAL A C   1 
ATOM   3140 O  O   . VAL A 1 409 ? 25.228  42.496 31.832  1.00 77.27  ? 508 VAL A O   1 
ATOM   3141 C  CB  . VAL A 1 409 ? 22.162  42.141 33.030  1.00 76.81  ? 508 VAL A CB  1 
ATOM   3142 C  CG1 . VAL A 1 409 ? 21.040  41.311 33.618  1.00 77.46  ? 508 VAL A CG1 1 
ATOM   3143 C  CG2 . VAL A 1 409 ? 22.721  43.118 34.052  1.00 77.07  ? 508 VAL A CG2 1 
ATOM   3144 N  N   . LYS A 1 410 ? 23.635  42.256 30.275  1.00 76.27  ? 509 LYS A N   1 
ATOM   3145 C  CA  . LYS A 1 410 ? 24.281  43.042 29.235  1.00 76.15  ? 509 LYS A CA  1 
ATOM   3146 C  C   . LYS A 1 410 ? 23.171  43.436 28.272  1.00 76.02  ? 509 LYS A C   1 
ATOM   3147 O  O   . LYS A 1 410 ? 22.373  42.585 27.856  1.00 76.02  ? 509 LYS A O   1 
ATOM   3148 C  CB  . LYS A 1 410 ? 25.380  42.235 28.528  1.00 77.56  ? 509 LYS A CB  1 
ATOM   3149 C  CG  . LYS A 1 410 ? 25.998  42.956 27.340  1.00 80.62  ? 509 LYS A CG  1 
ATOM   3150 C  CD  . LYS A 1 410 ? 27.164  42.165 26.807  1.00 84.66  ? 509 LYS A CD  1 
ATOM   3151 C  CE  . LYS A 1 410 ? 27.559  42.567 25.412  1.00 88.63  ? 509 LYS A CE  1 
ATOM   3152 N  NZ  . LYS A 1 410 ? 26.534  42.172 24.413  1.00 90.62  ? 509 LYS A NZ  1 
ATOM   3153 N  N   . PHE A 1 411 ? 23.080  44.728 27.960  1.00 75.65  ? 510 PHE A N   1 
ATOM   3154 C  CA  . PHE A 1 411 ? 22.010  45.224 27.109  1.00 75.63  ? 510 PHE A CA  1 
ATOM   3155 C  C   . PHE A 1 411 ? 22.554  45.673 25.784  1.00 76.88  ? 510 PHE A C   1 
ATOM   3156 O  O   . PHE A 1 411 ? 23.264  46.666 25.734  1.00 77.44  ? 510 PHE A O   1 
ATOM   3157 C  CB  . PHE A 1 411 ? 21.254  46.363 27.812  1.00 74.64  ? 510 PHE A CB  1 
ATOM   3158 C  CG  . PHE A 1 411 ? 20.723  45.946 29.161  1.00 74.34  ? 510 PHE A CG  1 
ATOM   3159 C  CD1 . PHE A 1 411 ? 19.485  45.346 29.277  1.00 74.84  ? 510 PHE A CD1 1 
ATOM   3160 C  CD2 . PHE A 1 411 ? 21.496  46.076 30.298  1.00 74.68  ? 510 PHE A CD2 1 
ATOM   3161 C  CE1 . PHE A 1 411 ? 19.022  44.909 30.504  1.00 75.22  ? 510 PHE A CE1 1 
ATOM   3162 C  CE2 . PHE A 1 411 ? 21.028  45.640 31.526  1.00 75.25  ? 510 PHE A CE2 1 
ATOM   3163 C  CZ  . PHE A 1 411 ? 19.799  45.049 31.620  1.00 74.98  ? 510 PHE A CZ  1 
ATOM   3164 N  N   . ASP A 1 412 ? 22.236  44.951 24.705  1.00 77.24  ? 511 ASP A N   1 
ATOM   3165 C  CA  . ASP A 1 412 ? 22.716  45.305 23.367  1.00 78.16  ? 511 ASP A CA  1 
ATOM   3166 C  C   . ASP A 1 412 ? 21.852  46.331 22.632  1.00 78.13  ? 511 ASP A C   1 
ATOM   3167 O  O   . ASP A 1 412 ? 22.170  46.672 21.492  1.00 78.28  ? 511 ASP A O   1 
ATOM   3168 C  CB  . ASP A 1 412 ? 22.892  44.050 22.497  1.00 80.79  ? 511 ASP A CB  1 
ATOM   3169 C  CG  . ASP A 1 412 ? 24.211  43.351 22.728  1.00 86.88  ? 511 ASP A CG  1 
ATOM   3170 O  OD1 . ASP A 1 412 ? 25.223  44.058 22.970  1.00 88.01  ? 511 ASP A OD1 1 
ATOM   3171 O  OD2 . ASP A 1 412 ? 24.236  42.094 22.673  1.00 89.28  ? 511 ASP A OD2 1 
ATOM   3172 N  N   . HIS A 1 413 ? 20.763  46.807 23.253  1.00 77.82  ? 512 HIS A N   1 
ATOM   3173 C  CA  . HIS A 1 413 ? 19.881  47.757 22.593  1.00 78.42  ? 512 HIS A CA  1 
ATOM   3174 C  C   . HIS A 1 413 ? 19.578  48.963 23.460  1.00 79.56  ? 512 HIS A C   1 
ATOM   3175 O  O   . HIS A 1 413 ? 19.556  48.860 24.678  1.00 79.63  ? 512 HIS A O   1 
ATOM   3176 C  CB  . HIS A 1 413 ? 18.595  47.069 22.114  1.00 78.50  ? 512 HIS A CB  1 
ATOM   3177 C  CG  . HIS A 1 413 ? 18.863  45.881 21.250  1.00 79.47  ? 512 HIS A CG  1 
ATOM   3178 N  ND1 . HIS A 1 413 ? 18.975  45.998 19.879  1.00 80.90  ? 512 HIS A ND1 1 
ATOM   3179 C  CD2 . HIS A 1 413 ? 19.108  44.598 21.602  1.00 80.34  ? 512 HIS A CD2 1 
ATOM   3180 C  CE1 . HIS A 1 413 ? 19.245  44.781 19.439  1.00 81.30  ? 512 HIS A CE1 1 
ATOM   3181 N  NE2 . HIS A 1 413 ? 19.342  43.908 20.442  1.00 81.24  ? 512 HIS A NE2 1 
ATOM   3182 N  N   . GLU A 1 414 ? 19.347  50.110 22.829  1.00 80.26  ? 513 GLU A N   1 
ATOM   3183 C  CA  . GLU A 1 414 ? 19.062  51.342 23.542  1.00 81.40  ? 513 GLU A CA  1 
ATOM   3184 C  C   . GLU A 1 414 ? 17.657  51.348 24.143  1.00 82.20  ? 513 GLU A C   1 
ATOM   3185 O  O   . GLU A 1 414 ? 16.805  50.550 23.763  1.00 82.06  ? 513 GLU A O   1 
ATOM   3186 C  CB  . GLU A 1 414 ? 19.249  52.542 22.602  1.00 84.07  ? 513 GLU A CB  1 
ATOM   3187 C  CG  . GLU A 1 414 ? 20.694  52.855 22.268  1.00 88.92  ? 513 GLU A CG  1 
ATOM   3188 C  CD  . GLU A 1 414 ? 20.833  53.661 20.994  1.00 94.61  ? 513 GLU A CD  1 
ATOM   3189 O  OE1 . GLU A 1 414 ? 20.034  54.605 20.797  1.00 95.60  ? 513 GLU A OE1 1 
ATOM   3190 O  OE2 . GLU A 1 414 ? 21.733  53.341 20.185  1.00 96.64  ? 513 GLU A OE2 1 
ATOM   3191 N  N   . ALA A 1 415 ? 17.430  52.257 25.091  1.00 82.79  ? 514 ALA A N   1 
ATOM   3192 C  CA  . ALA A 1 415 ? 16.167  52.448 25.780  1.00 83.98  ? 514 ALA A CA  1 
ATOM   3193 C  C   . ALA A 1 415 ? 16.183  53.873 26.307  1.00 85.32  ? 514 ALA A C   1 
ATOM   3194 O  O   . ALA A 1 415 ? 16.831  54.143 27.319  1.00 85.69  ? 514 ALA A O   1 
ATOM   3195 C  CB  . ALA A 1 415 ? 16.057  51.478 26.943  1.00 84.03  ? 514 ALA A CB  1 
ATOM   3196 N  N   . PRO A 1 416 ? 15.505  54.816 25.622  1.00 85.60  ? 515 PRO A N   1 
ATOM   3197 C  CA  . PRO A 1 416 ? 15.500  56.211 26.107  1.00 85.56  ? 515 PRO A CA  1 
ATOM   3198 C  C   . PRO A 1 416 ? 14.664  56.417 27.379  1.00 85.58  ? 515 PRO A C   1 
ATOM   3199 O  O   . PRO A 1 416 ? 14.030  55.476 27.846  1.00 85.83  ? 515 PRO A O   1 
ATOM   3200 C  CB  . PRO A 1 416 ? 14.912  56.974 24.919  1.00 86.33  ? 515 PRO A CB  1 
ATOM   3201 C  CG  . PRO A 1 416 ? 14.002  55.984 24.262  1.00 86.72  ? 515 PRO A CG  1 
ATOM   3202 C  CD  . PRO A 1 416 ? 14.695  54.659 24.395  1.00 85.15  ? 515 PRO A CD  1 
ATOM   3203 N  N   . LYS A 1 417 ? 14.653  57.638 27.946  1.00 85.17  ? 516 LYS A N   1 
ATOM   3204 C  CA  . LYS A 1 417 ? 13.865  57.911 29.150  1.00 85.29  ? 516 LYS A CA  1 
ATOM   3205 C  C   . LYS A 1 417 ? 12.374  57.702 28.895  1.00 84.82  ? 516 LYS A C   1 
ATOM   3206 O  O   . LYS A 1 417 ? 11.671  57.116 29.716  1.00 84.87  ? 516 LYS A O   1 
ATOM   3207 C  CB  . LYS A 1 417 ? 14.115  59.337 29.658  1.00 87.61  ? 516 LYS A CB  1 
ATOM   3208 C  CG  . LYS A 1 417 ? 13.378  59.642 30.964  1.00 92.46  ? 516 LYS A CG  1 
ATOM   3209 C  CD  . LYS A 1 417 ? 13.406  61.118 31.308  1.00 97.57  ? 516 LYS A CD  1 
ATOM   3210 C  CE  . LYS A 1 417 ? 12.800  61.389 32.666  1.00 101.23 ? 516 LYS A CE  1 
ATOM   3211 N  NZ  . LYS A 1 417 ? 13.331  62.647 33.269  1.00 103.07 ? 516 LYS A NZ  1 
ATOM   3212 N  N   . GLU A 1 418 ? 11.913  58.142 27.729  1.00 84.42  ? 517 GLU A N   1 
ATOM   3213 C  CA  . GLU A 1 418 ? 10.520  58.062 27.302  1.00 84.79  ? 517 GLU A CA  1 
ATOM   3214 C  C   . GLU A 1 418 ? 10.050  56.617 27.145  1.00 84.17  ? 517 GLU A C   1 
ATOM   3215 O  O   . GLU A 1 418 ? 8.901   56.302 27.456  1.00 84.15  ? 517 GLU A O   1 
ATOM   3216 C  CB  . GLU A 1 418 ? 10.316  58.833 25.980  1.00 87.85  ? 517 GLU A CB  1 
ATOM   3217 C  CG  . GLU A 1 418 ? 11.159  60.095 25.839  1.00 93.52  ? 517 GLU A CG  1 
ATOM   3218 C  CD  . GLU A 1 418 ? 12.443  59.880 25.060  1.00 101.17 ? 517 GLU A CD  1 
ATOM   3219 O  OE1 . GLU A 1 418 ? 13.488  60.440 25.466  1.00 103.11 ? 517 GLU A OE1 1 
ATOM   3220 O  OE2 . GLU A 1 418 ? 12.405  59.142 24.047  1.00 103.19 ? 517 GLU A OE2 1 
ATOM   3221 N  N   . ARG A 1 419 ? 10.938  55.748 26.643  1.00 83.35  ? 518 ARG A N   1 
ATOM   3222 C  CA  . ARG A 1 419 ? 10.655  54.332 26.439  1.00 82.89  ? 518 ARG A CA  1 
ATOM   3223 C  C   . ARG A 1 419 ? 11.760  53.513 27.100  1.00 81.99  ? 518 ARG A C   1 
ATOM   3224 O  O   . ARG A 1 419 ? 12.602  52.919 26.426  1.00 81.97  ? 518 ARG A O   1 
ATOM   3225 C  CB  . ARG A 1 419 ? 10.560  54.023 24.947  1.00 84.61  ? 518 ARG A CB  1 
ATOM   3226 C  CG  . ARG A 1 419 ? 9.401   54.743 24.281  1.00 88.85  ? 518 ARG A CG  1 
ATOM   3227 C  CD  . ARG A 1 419 ? 8.098   54.028 24.533  1.00 93.40  ? 518 ARG A CD  1 
ATOM   3228 N  NE  . ARG A 1 419 ? 7.806   53.076 23.458  1.00 98.12  ? 518 ARG A NE  1 
ATOM   3229 C  CZ  . ARG A 1 419 ? 6.818   53.212 22.578  1.00 101.39 ? 518 ARG A CZ  1 
ATOM   3230 N  NH1 . ARG A 1 419 ? 5.974   54.235 22.669  1.00 102.08 ? 518 ARG A NH1 1 
ATOM   3231 N  NH2 . ARG A 1 419 ? 6.633   52.298 21.634  1.00 100.87 ? 518 ARG A NH2 1 
ATOM   3232 N  N   . ALA A 1 420 ? 11.799  53.559 28.438  1.00 80.89  ? 519 ALA A N   1 
ATOM   3233 C  CA  . ALA A 1 420 ? 12.803  52.859 29.226  1.00 80.16  ? 519 ALA A CA  1 
ATOM   3234 C  C   . ALA A 1 420 ? 12.420  51.422 29.518  1.00 79.03  ? 519 ALA A C   1 
ATOM   3235 O  O   . ALA A 1 420 ? 11.238  51.097 29.614  1.00 79.04  ? 519 ALA A O   1 
ATOM   3236 C  CB  . ALA A 1 420 ? 13.039  53.596 30.529  1.00 80.37  ? 519 ALA A CB  1 
ATOM   3237 N  N   . TYR A 1 421 ? 13.432  50.565 29.689  1.00 77.88  ? 520 TYR A N   1 
ATOM   3238 C  CA  . TYR A 1 421 ? 13.244  49.160 30.031  1.00 77.11  ? 520 TYR A CA  1 
ATOM   3239 C  C   . TYR A 1 421 ? 12.680  49.035 31.447  1.00 76.40  ? 520 TYR A C   1 
ATOM   3240 O  O   . TYR A 1 421 ? 12.760  49.973 32.236  1.00 76.90  ? 520 TYR A O   1 
ATOM   3241 C  CB  . TYR A 1 421 ? 14.587  48.433 30.002  1.00 76.96  ? 520 TYR A CB  1 
ATOM   3242 C  CG  . TYR A 1 421 ? 15.140  48.166 28.629  1.00 77.70  ? 520 TYR A CG  1 
ATOM   3243 C  CD1 . TYR A 1 421 ? 14.308  47.791 27.586  1.00 78.70  ? 520 TYR A CD1 1 
ATOM   3244 C  CD2 . TYR A 1 421 ? 16.507  48.181 28.397  1.00 78.57  ? 520 TYR A CD2 1 
ATOM   3245 C  CE1 . TYR A 1 421 ? 14.817  47.494 26.329  1.00 79.65  ? 520 TYR A CE1 1 
ATOM   3246 C  CE2 . TYR A 1 421 ? 17.030  47.894 27.143  1.00 79.52  ? 520 TYR A CE2 1 
ATOM   3247 C  CZ  . TYR A 1 421 ? 16.180  47.556 26.109  1.00 80.60  ? 520 TYR A CZ  1 
ATOM   3248 O  OH  . TYR A 1 421 ? 16.683  47.256 24.868  1.00 82.31  ? 520 TYR A OH  1 
ATOM   3249 N  N   . MET A 1 422 ? 12.120  47.875 31.781  1.00 75.17  ? 521 MET A N   1 
ATOM   3250 C  CA  . MET A 1 422 ? 11.586  47.626 33.119  1.00 74.09  ? 521 MET A CA  1 
ATOM   3251 C  C   . MET A 1 422 ? 12.302  46.433 33.751  1.00 72.41  ? 521 MET A C   1 
ATOM   3252 O  O   . MET A 1 422 ? 12.865  45.586 33.067  1.00 72.54  ? 521 MET A O   1 
ATOM   3253 C  CB  . MET A 1 422 ? 10.069  47.349 33.079  1.00 74.97  ? 521 MET A CB  1 
ATOM   3254 C  CG  . MET A 1 422 ? 9.276   48.336 32.256  1.00 77.35  ? 521 MET A CG  1 
ATOM   3255 S  SD  . MET A 1 422 ? 8.620   49.645 33.287  1.00 81.90  ? 521 MET A SD  1 
ATOM   3256 C  CE  . MET A 1 422 ? 8.930   51.032 32.264  1.00 80.38  ? 521 MET A CE  1 
ATOM   3257 N  N   . ALA A 1 423 ? 12.300  46.387 35.057  1.00 70.83  ? 522 ALA A N   1 
ATOM   3258 C  CA  . ALA A 1 423 ? 12.872  45.289 35.813  1.00 70.05  ? 522 ALA A CA  1 
ATOM   3259 C  C   . ALA A 1 423 ? 11.898  45.122 36.943  1.00 68.82  ? 522 ALA A C   1 
ATOM   3260 O  O   . ALA A 1 423 ? 11.597  46.110 37.613  1.00 69.07  ? 522 ALA A O   1 
ATOM   3261 C  CB  . ALA A 1 423 ? 14.244  45.662 36.335  1.00 70.28  ? 522 ALA A CB  1 
ATOM   3262 N  N   . HIS A 1 424 ? 11.336  43.919 37.118  1.00 67.56  ? 523 HIS A N   1 
ATOM   3263 C  CA  . HIS A 1 424 ? 10.316  43.746 38.146  1.00 67.41  ? 523 HIS A CA  1 
ATOM   3264 C  C   . HIS A 1 424 ? 10.099  42.312 38.594  1.00 66.37  ? 523 HIS A C   1 
ATOM   3265 O  O   . HIS A 1 424 ? 10.618  41.373 38.007  1.00 66.18  ? 523 HIS A O   1 
ATOM   3266 C  CB  . HIS A 1 424 ? 8.987   44.343 37.633  1.00 68.74  ? 523 HIS A CB  1 
ATOM   3267 C  CG  . HIS A 1 424 ? 8.566   43.790 36.306  1.00 71.28  ? 523 HIS A CG  1 
ATOM   3268 N  ND1 . HIS A 1 424 ? 7.749   42.677 36.219  1.00 73.01  ? 523 HIS A ND1 1 
ATOM   3269 C  CD2 . HIS A 1 424 ? 8.910   44.186 35.055  1.00 72.25  ? 523 HIS A CD2 1 
ATOM   3270 C  CE1 . HIS A 1 424 ? 7.607   42.446 34.924  1.00 73.61  ? 523 HIS A CE1 1 
ATOM   3271 N  NE2 . HIS A 1 424 ? 8.290   43.330 34.185  1.00 73.29  ? 523 HIS A NE2 1 
ATOM   3272 N  N   . CYS A 1 425 ? 9.321   42.157 39.651  1.00 65.57  ? 524 CYS A N   1 
ATOM   3273 C  CA  . CYS A 1 425 ? 8.924   40.872 40.173  1.00 65.46  ? 524 CYS A CA  1 
ATOM   3274 C  C   . CYS A 1 425 ? 7.802   40.406 39.236  1.00 65.37  ? 524 CYS A C   1 
ATOM   3275 O  O   . CYS A 1 425 ? 6.807   41.133 39.050  1.00 65.72  ? 524 CYS A O   1 
ATOM   3276 C  CB  . CYS A 1 425 ? 8.423   41.052 41.602  1.00 65.64  ? 524 CYS A CB  1 
ATOM   3277 S  SG  . CYS A 1 425 ? 7.608   39.602 42.300  1.00 67.42  ? 524 CYS A SG  1 
ATOM   3278 N  N   . HIS A 1 426 ? 7.965   39.217 38.614  1.00 64.17  ? 525 HIS A N   1 
ATOM   3279 C  CA  . HIS A 1 426 ? 6.945   38.738 37.685  1.00 63.06  ? 525 HIS A CA  1 
ATOM   3280 C  C   . HIS A 1 426 ? 5.711   38.166 38.376  1.00 62.48  ? 525 HIS A C   1 
ATOM   3281 O  O   . HIS A 1 426 ? 4.836   37.635 37.701  1.00 63.21  ? 525 HIS A O   1 
ATOM   3282 C  CB  . HIS A 1 426 ? 7.482   37.783 36.619  1.00 62.87  ? 525 HIS A CB  1 
ATOM   3283 C  CG  . HIS A 1 426 ? 6.790   37.965 35.303  1.00 63.09  ? 525 HIS A CG  1 
ATOM   3284 N  ND1 . HIS A 1 426 ? 5.613   37.295 35.008  1.00 64.24  ? 525 HIS A ND1 1 
ATOM   3285 C  CD2 . HIS A 1 426 ? 7.098   38.784 34.271  1.00 63.82  ? 525 HIS A CD2 1 
ATOM   3286 C  CE1 . HIS A 1 426 ? 5.269   37.689 33.796  1.00 64.63  ? 525 HIS A CE1 1 
ATOM   3287 N  NE2 . HIS A 1 426 ? 6.127   38.593 33.314  1.00 64.81  ? 525 HIS A NE2 1 
ATOM   3288 N  N   . LEU A 1 427 ? 5.561   38.369 39.696  1.00 61.40  ? 526 LEU A N   1 
ATOM   3289 C  CA  . LEU A 1 427 ? 4.316   38.053 40.386  1.00 61.19  ? 526 LEU A CA  1 
ATOM   3290 C  C   . LEU A 1 427 ? 3.554   39.341 40.074  1.00 61.31  ? 526 LEU A C   1 
ATOM   3291 O  O   . LEU A 1 427 ? 3.860   40.388 40.641  1.00 61.71  ? 526 LEU A O   1 
ATOM   3292 C  CB  . LEU A 1 427 ? 4.535   37.902 41.893  1.00 60.63  ? 526 LEU A CB  1 
ATOM   3293 C  CG  . LEU A 1 427 ? 3.441   37.201 42.655  1.00 60.69  ? 526 LEU A CG  1 
ATOM   3294 C  CD1 . LEU A 1 427 ? 3.994   36.548 43.863  1.00 60.95  ? 526 LEU A CD1 1 
ATOM   3295 C  CD2 . LEU A 1 427 ? 2.331   38.148 43.018  1.00 60.91  ? 526 LEU A CD2 1 
ATOM   3296 N  N   . LEU A 1 428 ? 2.731   39.289 39.025  1.00 60.61  ? 527 LEU A N   1 
ATOM   3297 C  CA  . LEU A 1 428 ? 2.058   40.438 38.453  1.00 60.68  ? 527 LEU A CA  1 
ATOM   3298 C  C   . LEU A 1 428 ? 1.460   41.429 39.449  1.00 60.83  ? 527 LEU A C   1 
ATOM   3299 O  O   . LEU A 1 428 ? 1.618   42.628 39.248  1.00 60.81  ? 527 LEU A O   1 
ATOM   3300 C  CB  . LEU A 1 428 ? 1.004   39.989 37.448  1.00 60.76  ? 527 LEU A CB  1 
ATOM   3301 C  CG  . LEU A 1 428 ? 1.512   39.131 36.285  1.00 61.85  ? 527 LEU A CG  1 
ATOM   3302 C  CD1 . LEU A 1 428 ? 0.402   38.843 35.329  1.00 62.40  ? 527 LEU A CD1 1 
ATOM   3303 C  CD2 . LEU A 1 428 ? 2.681   39.782 35.542  1.00 61.98  ? 527 LEU A CD2 1 
ATOM   3304 N  N   . GLU A 1 429 ? 0.823   40.957 40.522  1.00 60.86  ? 528 GLU A N   1 
ATOM   3305 C  CA  . GLU A 1 429 ? 0.236   41.862 41.513  1.00 61.09  ? 528 GLU A CA  1 
ATOM   3306 C  C   . GLU A 1 429 ? 1.308   42.648 42.276  1.00 61.37  ? 528 GLU A C   1 
ATOM   3307 O  O   . GLU A 1 429 ? 1.093   43.821 42.556  1.00 61.87  ? 528 GLU A O   1 
ATOM   3308 C  CB  . GLU A 1 429 ? -0.742  41.137 42.444  1.00 62.56  ? 528 GLU A CB  1 
ATOM   3309 C  CG  . GLU A 1 429 ? -2.026  40.727 41.737  1.00 65.61  ? 528 GLU A CG  1 
ATOM   3310 C  CD  . GLU A 1 429 ? -1.883  39.565 40.773  1.00 69.69  ? 528 GLU A CD  1 
ATOM   3311 O  OE1 . GLU A 1 429 ? -2.483  39.607 39.676  1.00 68.71  ? 528 GLU A OE1 1 
ATOM   3312 O  OE2 . GLU A 1 429 ? -1.162  38.604 41.123  1.00 72.51  ? 528 GLU A OE2 1 
ATOM   3313 N  N   . HIS A 1 430 ? 2.489   42.051 42.538  1.00 60.81  ? 529 HIS A N   1 
ATOM   3314 C  CA  . HIS A 1 430 ? 3.587   42.779 43.182  1.00 60.74  ? 529 HIS A CA  1 
ATOM   3315 C  C   . HIS A 1 430 ? 4.052   43.894 42.261  1.00 61.13  ? 529 HIS A C   1 
ATOM   3316 O  O   . HIS A 1 430 ? 4.197   45.031 42.701  1.00 61.11  ? 529 HIS A O   1 
ATOM   3317 C  CB  . HIS A 1 430 ? 4.781   41.857 43.502  1.00 60.65  ? 529 HIS A CB  1 
ATOM   3318 C  CG  . HIS A 1 430 ? 4.569   40.932 44.651  1.00 61.45  ? 529 HIS A CG  1 
ATOM   3319 N  ND1 . HIS A 1 430 ? 5.504   39.968 44.966  1.00 63.16  ? 529 HIS A ND1 1 
ATOM   3320 C  CD2 . HIS A 1 430 ? 3.542   40.848 45.528  1.00 62.23  ? 529 HIS A CD2 1 
ATOM   3321 C  CE1 . HIS A 1 430 ? 5.016   39.322 46.012  1.00 63.52  ? 529 HIS A CE1 1 
ATOM   3322 N  NE2 . HIS A 1 430 ? 3.841   39.821 46.389  1.00 63.30  ? 529 HIS A NE2 1 
ATOM   3323 N  N   . GLU A 1 431 ? 4.229   43.564 40.972  1.00 61.38  ? 530 GLU A N   1 
ATOM   3324 C  CA  . GLU A 1 431 ? 4.626   44.501 39.937  1.00 62.24  ? 530 GLU A CA  1 
ATOM   3325 C  C   . GLU A 1 431 ? 3.623   45.669 39.843  1.00 62.90  ? 530 GLU A C   1 
ATOM   3326 O  O   . GLU A 1 431 ? 4.020   46.832 39.835  1.00 63.07  ? 530 GLU A O   1 
ATOM   3327 C  CB  . GLU A 1 431 ? 4.729   43.756 38.597  1.00 63.88  ? 530 GLU A CB  1 
ATOM   3328 C  CG  . GLU A 1 431 ? 4.949   44.659 37.403  1.00 66.71  ? 530 GLU A CG  1 
ATOM   3329 C  CD  . GLU A 1 431 ? 4.665   44.004 36.072  1.00 71.58  ? 530 GLU A CD  1 
ATOM   3330 O  OE1 . GLU A 1 431 ? 4.383   44.743 35.103  1.00 72.55  ? 530 GLU A OE1 1 
ATOM   3331 O  OE2 . GLU A 1 431 ? 4.711   42.756 35.995  1.00 73.61  ? 530 GLU A OE2 1 
ATOM   3332 N  N   . ASP A 1 432 ? 2.339   45.357 39.805  1.00 63.22  ? 531 ASP A N   1 
ATOM   3333 C  CA  . ASP A 1 432 ? 1.291   46.360 39.696  1.00 64.58  ? 531 ASP A CA  1 
ATOM   3334 C  C   . ASP A 1 432 ? 1.205   47.277 40.896  1.00 65.44  ? 531 ASP A C   1 
ATOM   3335 O  O   . ASP A 1 432 ? 0.852   48.449 40.762  1.00 65.89  ? 531 ASP A O   1 
ATOM   3336 C  CB  . ASP A 1 432 ? -0.065  45.688 39.464  1.00 66.87  ? 531 ASP A CB  1 
ATOM   3337 C  CG  . ASP A 1 432 ? -0.283  45.216 38.039  1.00 72.90  ? 531 ASP A CG  1 
ATOM   3338 O  OD1 . ASP A 1 432 ? 0.472   45.677 37.125  1.00 73.39  ? 531 ASP A OD1 1 
ATOM   3339 O  OD2 . ASP A 1 432 ? -1.221  44.409 37.820  1.00 75.56  ? 531 ASP A OD2 1 
ATOM   3340 N  N   . THR A 1 433 ? 1.511   46.749 42.069  1.00 65.47  ? 532 THR A N   1 
ATOM   3341 C  CA  . THR A 1 433 ? 1.446   47.519 43.292  1.00 65.70  ? 532 THR A CA  1 
ATOM   3342 C  C   . THR A 1 433 ? 2.801   48.125 43.686  1.00 65.95  ? 532 THR A C   1 
ATOM   3343 O  O   . THR A 1 433 ? 3.029   48.356 44.864  1.00 66.27  ? 532 THR A O   1 
ATOM   3344 C  CB  . THR A 1 433 ? 0.824   46.666 44.397  1.00 66.76  ? 532 THR A CB  1 
ATOM   3345 O  OG1 . THR A 1 433 ? 1.580   45.462 44.535  1.00 67.64  ? 532 THR A OG1 1 
ATOM   3346 C  CG2 . THR A 1 433 ? -0.631  46.331 44.114  1.00 66.98  ? 532 THR A CG2 1 
ATOM   3347 N  N   . GLY A 1 434 ? 3.679   48.372 42.721  1.00 65.83  ? 533 GLY A N   1 
ATOM   3348 C  CA  . GLY A 1 434 ? 4.949   49.027 43.002  1.00 66.53  ? 533 GLY A CA  1 
ATOM   3349 C  C   . GLY A 1 434 ? 6.257   48.285 42.821  1.00 67.19  ? 533 GLY A C   1 
ATOM   3350 O  O   . GLY A 1 434 ? 7.275   48.946 42.614  1.00 67.30  ? 533 GLY A O   1 
ATOM   3351 N  N   . MET A 1 435 ? 6.287   46.941 42.954  1.00 67.44  ? 534 MET A N   1 
ATOM   3352 C  CA  . MET A 1 435 ? 7.541   46.187 42.818  1.00 68.21  ? 534 MET A CA  1 
ATOM   3353 C  C   . MET A 1 435 ? 8.007   46.052 41.369  1.00 69.56  ? 534 MET A C   1 
ATOM   3354 O  O   . MET A 1 435 ? 8.012   44.960 40.792  1.00 69.86  ? 534 MET A O   1 
ATOM   3355 C  CB  . MET A 1 435 ? 7.468   44.822 43.501  1.00 68.59  ? 534 MET A CB  1 
ATOM   3356 C  CG  . MET A 1 435 ? 8.837   44.283 43.871  1.00 70.44  ? 534 MET A CG  1 
ATOM   3357 S  SD  . MET A 1 435 ? 8.811   42.685 44.725  1.00 73.01  ? 534 MET A SD  1 
ATOM   3358 C  CE  . MET A 1 435 ? 7.841   43.097 46.148  1.00 68.00  ? 534 MET A CE  1 
ATOM   3359 N  N   . MET A 1 436 ? 8.388   47.191 40.787  1.00 70.05  ? 535 MET A N   1 
ATOM   3360 C  CA  . MET A 1 436 ? 8.874   47.384 39.425  1.00 70.61  ? 535 MET A CA  1 
ATOM   3361 C  C   . MET A 1 436 ? 9.784   48.635 39.412  1.00 71.90  ? 535 MET A C   1 
ATOM   3362 O  O   . MET A 1 436 ? 9.698   49.494 40.299  1.00 72.16  ? 535 MET A O   1 
ATOM   3363 C  CB  . MET A 1 436 ? 7.691   47.562 38.444  1.00 70.07  ? 535 MET A CB  1 
ATOM   3364 C  CG  . MET A 1 436 ? 8.137   47.854 37.024  1.00 70.44  ? 535 MET A CG  1 
ATOM   3365 S  SD  . MET A 1 436 ? 6.988   47.395 35.715  1.00 69.77  ? 535 MET A SD  1 
ATOM   3366 C  CE  . MET A 1 436 ? 5.541   48.339 36.219  1.00 66.97  ? 535 MET A CE  1 
ATOM   3367 N  N   . MET A 1 437 ? 10.666  48.725 38.417  1.00 72.37  ? 536 MET A N   1 
ATOM   3368 C  CA  . MET A 1 437 ? 11.560  49.861 38.269  1.00 73.27  ? 536 MET A CA  1 
ATOM   3369 C  C   . MET A 1 437 ? 11.969  50.032 36.815  1.00 73.50  ? 536 MET A C   1 
ATOM   3370 O  O   . MET A 1 437 ? 11.895  49.088 36.035  1.00 73.67  ? 536 MET A O   1 
ATOM   3371 C  CB  . MET A 1 437 ? 12.796  49.691 39.152  1.00 74.38  ? 536 MET A CB  1 
ATOM   3372 C  CG  . MET A 1 437 ? 13.561  48.452 38.840  1.00 77.52  ? 536 MET A CG  1 
ATOM   3373 S  SD  . MET A 1 437 ? 15.295  48.816 38.575  1.00 84.92  ? 536 MET A SD  1 
ATOM   3374 C  CE  . MET A 1 437 ? 15.307  49.047 36.947  1.00 83.72  ? 536 MET A CE  1 
ATOM   3375 N  N   . SER A 1 438 ? 12.391  51.241 36.445  1.00 73.40  ? 537 SER A N   1 
ATOM   3376 C  CA  . SER A 1 438 ? 12.845  51.505 35.085  1.00 73.53  ? 537 SER A CA  1 
ATOM   3377 C  C   . SER A 1 438 ? 14.306  51.899 35.054  1.00 73.70  ? 537 SER A C   1 
ATOM   3378 O  O   . SER A 1 438 ? 14.860  52.340 36.059  1.00 73.76  ? 537 SER A O   1 
ATOM   3379 C  CB  . SER A 1 438 ? 11.962  52.525 34.357  1.00 74.52  ? 537 SER A CB  1 
ATOM   3380 O  OG  . SER A 1 438 ? 11.377  53.516 35.186  1.00 76.73  ? 537 SER A OG  1 
ATOM   3381 N  N   . PHE A 1 439 ? 14.948  51.667 33.917  1.00 73.68  ? 538 PHE A N   1 
ATOM   3382 C  CA  . PHE A 1 439 ? 16.350  51.985 33.690  1.00 73.97  ? 538 PHE A CA  1 
ATOM   3383 C  C   . PHE A 1 439 ? 16.563  52.232 32.196  1.00 74.08  ? 538 PHE A C   1 
ATOM   3384 O  O   . PHE A 1 439 ? 15.896  51.628 31.350  1.00 73.76  ? 538 PHE A O   1 
ATOM   3385 C  CB  . PHE A 1 439 ? 17.271  50.878 34.217  1.00 73.99  ? 538 PHE A CB  1 
ATOM   3386 C  CG  . PHE A 1 439 ? 17.150  49.566 33.483  1.00 75.01  ? 538 PHE A CG  1 
ATOM   3387 C  CD1 . PHE A 1 439 ? 16.147  48.669 33.795  1.00 75.87  ? 538 PHE A CD1 1 
ATOM   3388 C  CD2 . PHE A 1 439 ? 18.049  49.223 32.491  1.00 76.01  ? 538 PHE A CD2 1 
ATOM   3389 C  CE1 . PHE A 1 439 ? 16.051  47.456 33.141  1.00 76.70  ? 538 PHE A CE1 1 
ATOM   3390 C  CE2 . PHE A 1 439 ? 17.924  48.030 31.809  1.00 76.70  ? 538 PHE A CE2 1 
ATOM   3391 C  CZ  . PHE A 1 439 ? 16.939  47.145 32.152  1.00 76.58  ? 538 PHE A CZ  1 
ATOM   3392 N  N   . THR A 1 440 ? 17.472  53.151 31.874  1.00 74.30  ? 539 THR A N   1 
ATOM   3393 C  CA  . THR A 1 440 ? 17.745  53.526 30.489  1.00 74.70  ? 539 THR A CA  1 
ATOM   3394 C  C   . THR A 1 440 ? 19.033  52.911 29.954  1.00 75.29  ? 539 THR A C   1 
ATOM   3395 O  O   . THR A 1 440 ? 19.920  52.599 30.725  1.00 75.46  ? 539 THR A O   1 
ATOM   3396 C  CB  . THR A 1 440 ? 17.725  55.049 30.370  1.00 75.52  ? 539 THR A CB  1 
ATOM   3397 O  OG1 . THR A 1 440 ? 18.629  55.601 31.328  1.00 76.20  ? 539 THR A OG1 1 
ATOM   3398 C  CG2 . THR A 1 440 ? 16.343  55.619 30.619  1.00 75.87  ? 539 THR A CG2 1 
ATOM   3399 N  N   . VAL A 1 441 ? 19.117  52.679 28.649  1.00 75.66  ? 540 VAL A N   1 
ATOM   3400 C  CA  . VAL A 1 441 ? 20.319  52.130 28.022  1.00 76.73  ? 540 VAL A CA  1 
ATOM   3401 C  C   . VAL A 1 441 ? 20.682  53.071 26.868  1.00 78.28  ? 540 VAL A C   1 
ATOM   3402 O  O   . VAL A 1 441 ? 19.798  53.481 26.112  1.00 78.34  ? 540 VAL A O   1 
ATOM   3403 C  CB  . VAL A 1 441 ? 20.154  50.655 27.562  1.00 77.19  ? 540 VAL A CB  1 
ATOM   3404 C  CG1 . VAL A 1 441 ? 21.419  50.146 26.887  1.00 77.46  ? 540 VAL A CG1 1 
ATOM   3405 C  CG2 . VAL A 1 441 ? 19.789  49.751 28.734  1.00 77.72  ? 540 VAL A CG2 1 
ATOM   3406 N  N   . SER A 1 442 ? 21.963  53.452 26.748  1.00 79.24  ? 541 SER A N   1 
ATOM   3407 C  CA  . SER A 1 442 ? 22.372  54.413 25.719  1.00 80.47  ? 541 SER A CA  1 
ATOM   3408 C  C   . SER A 1 442 ? 23.810  54.196 25.220  1.00 81.40  ? 541 SER A C   1 
ATOM   3409 O  O   . SER A 1 442 ? 24.684  53.890 26.065  1.00 81.69  ? 541 SER A O   1 
ATOM   3410 C  CB  . SER A 1 442 ? 22.197  55.836 26.245  1.00 81.63  ? 541 SER A CB  1 
ATOM   3411 O  OG  . SER A 1 442 ? 22.670  55.948 27.578  1.00 83.54  ? 541 SER A OG  1 
ATOM   3412 N  N   . ALA B 1 1   ? 13.563  11.220 77.973  1.00 74.56  ? 30  ALA B N   1 
ATOM   3413 C  CA  . ALA B 1 1   ? 13.988  12.547 78.404  1.00 75.15  ? 30  ALA B CA  1 
ATOM   3414 C  C   . ALA B 1 1   ? 14.151  13.549 77.258  1.00 75.42  ? 30  ALA B C   1 
ATOM   3415 O  O   . ALA B 1 1   ? 14.718  14.617 77.472  1.00 75.76  ? 30  ALA B O   1 
ATOM   3416 C  CB  . ALA B 1 1   ? 15.289  12.439 79.183  1.00 75.58  ? 30  ALA B CB  1 
ATOM   3417 N  N   . GLU B 1 2   ? 13.658  13.232 76.051  1.00 75.16  ? 31  GLU B N   1 
ATOM   3418 C  CA  . GLU B 1 2   ? 13.817  14.114 74.894  1.00 75.03  ? 31  GLU B CA  1 
ATOM   3419 C  C   . GLU B 1 2   ? 12.749  15.195 74.746  1.00 74.83  ? 31  GLU B C   1 
ATOM   3420 O  O   . GLU B 1 2   ? 12.770  15.929 73.760  1.00 74.96  ? 31  GLU B O   1 
ATOM   3421 C  CB  . GLU B 1 2   ? 13.931  13.297 73.610  1.00 76.87  ? 31  GLU B CB  1 
ATOM   3422 C  CG  . GLU B 1 2   ? 15.056  12.284 73.679  1.00 81.95  ? 31  GLU B CG  1 
ATOM   3423 C  CD  . GLU B 1 2   ? 16.437  12.862 73.933  1.00 89.87  ? 31  GLU B CD  1 
ATOM   3424 O  OE1 . GLU B 1 2   ? 16.920  13.645 73.085  1.00 92.04  ? 31  GLU B OE1 1 
ATOM   3425 O  OE2 . GLU B 1 2   ? 17.042  12.527 74.977  1.00 92.27  ? 31  GLU B OE2 1 
ATOM   3426 N  N   . HIS B 1 3   ? 11.816  15.297 75.705  1.00 74.41  ? 32  HIS B N   1 
ATOM   3427 C  CA  . HIS B 1 3   ? 10.780  16.338 75.706  1.00 74.27  ? 32  HIS B CA  1 
ATOM   3428 C  C   . HIS B 1 3   ? 10.655  16.975 77.089  1.00 73.35  ? 32  HIS B C   1 
ATOM   3429 O  O   . HIS B 1 3   ? 10.890  16.324 78.111  1.00 73.65  ? 32  HIS B O   1 
ATOM   3430 C  CB  . HIS B 1 3   ? 9.416   15.807 75.209  1.00 75.40  ? 32  HIS B CB  1 
ATOM   3431 C  CG  . HIS B 1 3   ? 9.481   15.269 73.821  1.00 78.44  ? 32  HIS B CG  1 
ATOM   3432 N  ND1 . HIS B 1 3   ? 9.469   16.107 72.721  1.00 80.45  ? 32  HIS B ND1 1 
ATOM   3433 C  CD2 . HIS B 1 3   ? 9.655   13.996 73.400  1.00 79.89  ? 32  HIS B CD2 1 
ATOM   3434 C  CE1 . HIS B 1 3   ? 9.606   15.317 71.669  1.00 81.11  ? 32  HIS B CE1 1 
ATOM   3435 N  NE2 . HIS B 1 3   ? 9.716   14.038 72.028  1.00 81.16  ? 32  HIS B NE2 1 
ATOM   3436 N  N   . PRO B 1 4   ? 10.279  18.258 77.141  1.00 72.08  ? 33  PRO B N   1 
ATOM   3437 C  CA  . PRO B 1 4   ? 10.157  18.927 78.446  1.00 71.18  ? 33  PRO B CA  1 
ATOM   3438 C  C   . PRO B 1 4   ? 8.909   18.524 79.245  1.00 69.92  ? 33  PRO B C   1 
ATOM   3439 O  O   . PRO B 1 4   ? 8.134   17.668 78.810  1.00 70.30  ? 33  PRO B O   1 
ATOM   3440 C  CB  . PRO B 1 4   ? 10.153  20.423 78.072  1.00 72.06  ? 33  PRO B CB  1 
ATOM   3441 C  CG  . PRO B 1 4   ? 10.372  20.489 76.576  1.00 72.73  ? 33  PRO B CG  1 
ATOM   3442 C  CD  . PRO B 1 4   ? 9.976   19.176 76.027  1.00 71.40  ? 33  PRO B CD  1 
ATOM   3443 N  N   . THR B 1 5   ? 8.721   19.124 80.422  1.00 68.26  ? 34  THR B N   1 
ATOM   3444 C  CA  . THR B 1 5   ? 7.526   18.885 81.217  1.00 67.47  ? 34  THR B CA  1 
ATOM   3445 C  C   . THR B 1 5   ? 6.631   20.104 81.064  1.00 66.80  ? 34  THR B C   1 
ATOM   3446 O  O   . THR B 1 5   ? 7.128   21.230 81.116  1.00 67.36  ? 34  THR B O   1 
ATOM   3447 C  CB  . THR B 1 5   ? 7.904   18.620 82.663  1.00 68.38  ? 34  THR B CB  1 
ATOM   3448 O  OG1 . THR B 1 5   ? 8.466   17.314 82.735  1.00 69.84  ? 34  THR B OG1 1 
ATOM   3449 C  CG2 . THR B 1 5   ? 6.730   18.728 83.611  1.00 68.12  ? 34  THR B CG2 1 
ATOM   3450 N  N   . LEU B 1 6   ? 5.323   19.893 80.862  1.00 65.37  ? 35  LEU B N   1 
ATOM   3451 C  CA  . LEU B 1 6   ? 4.367   20.985 80.707  1.00 64.22  ? 35  LEU B CA  1 
ATOM   3452 C  C   . LEU B 1 6   ? 4.345   21.889 81.935  1.00 62.58  ? 35  LEU B C   1 
ATOM   3453 O  O   . LEU B 1 6   ? 3.998   21.444 83.024  1.00 62.33  ? 35  LEU B O   1 
ATOM   3454 C  CB  . LEU B 1 6   ? 2.959   20.420 80.455  1.00 64.42  ? 35  LEU B CB  1 
ATOM   3455 C  CG  . LEU B 1 6   ? 1.838   21.452 80.376  1.00 65.42  ? 35  LEU B CG  1 
ATOM   3456 C  CD1 . LEU B 1 6   ? 1.958   22.284 79.137  1.00 65.45  ? 35  LEU B CD1 1 
ATOM   3457 C  CD2 . LEU B 1 6   ? 0.506   20.789 80.443  1.00 66.19  ? 35  LEU B CD2 1 
ATOM   3458 N  N   . PRO B 1 7   ? 4.664   23.176 81.761  1.00 61.67  ? 36  PRO B N   1 
ATOM   3459 C  CA  . PRO B 1 7   ? 4.620   24.102 82.897  1.00 61.50  ? 36  PRO B CA  1 
ATOM   3460 C  C   . PRO B 1 7   ? 3.188   24.432 83.322  1.00 61.93  ? 36  PRO B C   1 
ATOM   3461 O  O   . PRO B 1 7   ? 2.317   24.600 82.468  1.00 62.16  ? 36  PRO B O   1 
ATOM   3462 C  CB  . PRO B 1 7   ? 5.316   25.359 82.355  1.00 61.64  ? 36  PRO B CB  1 
ATOM   3463 C  CG  . PRO B 1 7   ? 5.967   24.945 81.089  1.00 61.93  ? 36  PRO B CG  1 
ATOM   3464 C  CD  . PRO B 1 7   ? 5.109   23.862 80.540  1.00 60.73  ? 36  PRO B CD  1 
ATOM   3465 N  N   . ILE B 1 8   ? 2.941   24.520 84.636  1.00 61.61  ? 37  ILE B N   1 
ATOM   3466 C  CA  . ILE B 1 8   ? 1.618   24.883 85.124  1.00 61.46  ? 37  ILE B CA  1 
ATOM   3467 C  C   . ILE B 1 8   ? 1.654   26.297 85.670  1.00 61.73  ? 37  ILE B C   1 
ATOM   3468 O  O   . ILE B 1 8   ? 2.372   26.575 86.621  1.00 61.35  ? 37  ILE B O   1 
ATOM   3469 C  CB  . ILE B 1 8   ? 1.059   23.899 86.169  1.00 61.27  ? 37  ILE B CB  1 
ATOM   3470 C  CG1 . ILE B 1 8   ? 1.186   22.433 85.717  1.00 61.85  ? 37  ILE B CG1 1 
ATOM   3471 C  CG2 . ILE B 1 8   ? -0.367  24.281 86.535  1.00 61.50  ? 37  ILE B CG2 1 
ATOM   3472 C  CD1 . ILE B 1 8   ? 0.543   22.103 84.431  1.00 63.53  ? 37  ILE B CD1 1 
ATOM   3473 N  N   . PRO B 1 9   ? 0.896   27.218 85.061  1.00 62.49  ? 38  PRO B N   1 
ATOM   3474 C  CA  . PRO B 1 9   ? 0.873   28.600 85.565  1.00 62.80  ? 38  PRO B CA  1 
ATOM   3475 C  C   . PRO B 1 9   ? 0.268   28.621 86.952  1.00 63.15  ? 38  PRO B C   1 
ATOM   3476 O  O   . PRO B 1 9   ? -0.729  27.943 87.188  1.00 63.33  ? 38  PRO B O   1 
ATOM   3477 C  CB  . PRO B 1 9   ? -0.037  29.330 84.572  1.00 63.52  ? 38  PRO B CB  1 
ATOM   3478 C  CG  . PRO B 1 9   ? -0.086  28.440 83.350  1.00 64.01  ? 38  PRO B CG  1 
ATOM   3479 C  CD  . PRO B 1 9   ? -0.001  27.050 83.904  1.00 62.28  ? 38  PRO B CD  1 
ATOM   3480 N  N   . ALA B 1 10  ? 0.904   29.349 87.872  1.00 63.05  ? 39  ALA B N   1 
ATOM   3481 C  CA  . ALA B 1 10  ? 0.475   29.450 89.258  1.00 63.65  ? 39  ALA B CA  1 
ATOM   3482 C  C   . ALA B 1 10  ? -0.977  29.900 89.387  1.00 64.31  ? 39  ALA B C   1 
ATOM   3483 O  O   . ALA B 1 10  ? -1.443  30.710 88.597  1.00 64.22  ? 39  ALA B O   1 
ATOM   3484 C  CB  . ALA B 1 10  ? 1.379   30.404 90.005  1.00 63.80  ? 39  ALA B CB  1 
ATOM   3485 N  N   . LEU B 1 11  ? -1.694  29.363 90.372  1.00 64.49  ? 40  LEU B N   1 
ATOM   3486 C  CA  . LEU B 1 11  ? -3.090  29.698 90.580  1.00 64.96  ? 40  LEU B CA  1 
ATOM   3487 C  C   . LEU B 1 11  ? -3.214  30.784 91.644  1.00 66.38  ? 40  LEU B C   1 
ATOM   3488 O  O   . LEU B 1 11  ? -3.394  30.462 92.815  1.00 67.06  ? 40  LEU B O   1 
ATOM   3489 C  CB  . LEU B 1 11  ? -3.828  28.429 91.004  1.00 64.48  ? 40  LEU B CB  1 
ATOM   3490 C  CG  . LEU B 1 11  ? -5.340  28.420 90.907  1.00 65.03  ? 40  LEU B CG  1 
ATOM   3491 C  CD1 . LEU B 1 11  ? -5.817  28.799 89.515  1.00 65.43  ? 40  LEU B CD1 1 
ATOM   3492 C  CD2 . LEU B 1 11  ? -5.858  27.059 91.264  1.00 65.28  ? 40  LEU B CD2 1 
ATOM   3493 N  N   . LEU B 1 12  ? -3.119  32.070 91.247  1.00 66.73  ? 41  LEU B N   1 
ATOM   3494 C  CA  . LEU B 1 12  ? -3.192  33.176 92.206  1.00 67.69  ? 41  LEU B CA  1 
ATOM   3495 C  C   . LEU B 1 12  ? -4.598  33.505 92.651  1.00 68.61  ? 41  LEU B C   1 
ATOM   3496 O  O   . LEU B 1 12  ? -5.466  33.744 91.821  1.00 68.74  ? 41  LEU B O   1 
ATOM   3497 C  CB  . LEU B 1 12  ? -2.560  34.468 91.671  1.00 67.84  ? 41  LEU B CB  1 
ATOM   3498 C  CG  . LEU B 1 12  ? -1.234  34.424 90.940  1.00 69.49  ? 41  LEU B CG  1 
ATOM   3499 C  CD1 . LEU B 1 12  ? -0.653  35.808 90.889  1.00 69.84  ? 41  LEU B CD1 1 
ATOM   3500 C  CD2 . LEU B 1 12  ? -0.221  33.462 91.595  1.00 70.50  ? 41  LEU B CD2 1 
ATOM   3501 N  N   . THR B 1 13  ? -4.806  33.606 93.959  1.00 69.03  ? 42  THR B N   1 
ATOM   3502 C  CA  . THR B 1 13  ? -6.107  33.983 94.506  1.00 69.96  ? 42  THR B CA  1 
ATOM   3503 C  C   . THR B 1 13  ? -6.009  35.372 95.115  1.00 70.44  ? 42  THR B C   1 
ATOM   3504 O  O   . THR B 1 13  ? -4.928  35.767 95.566  1.00 70.69  ? 42  THR B O   1 
ATOM   3505 C  CB  . THR B 1 13  ? -6.550  32.963 95.548  1.00 71.61  ? 42  THR B CB  1 
ATOM   3506 O  OG1 . THR B 1 13  ? -5.526  32.855 96.530  1.00 72.86  ? 42  THR B OG1 1 
ATOM   3507 C  CG2 . THR B 1 13  ? -6.836  31.599 94.943  1.00 72.08  ? 42  THR B CG2 1 
ATOM   3508 N  N   . PRO B 1 14  ? -7.112  36.141 95.150  1.00 70.51  ? 43  PRO B N   1 
ATOM   3509 C  CA  . PRO B 1 14  ? -7.044  37.486 95.752  1.00 70.86  ? 43  PRO B CA  1 
ATOM   3510 C  C   . PRO B 1 14  ? -6.610  37.429 97.219  1.00 71.16  ? 43  PRO B C   1 
ATOM   3511 O  O   . PRO B 1 14  ? -7.055  36.554 97.964  1.00 71.49  ? 43  PRO B O   1 
ATOM   3512 C  CB  . PRO B 1 14  ? -8.475  38.016 95.601  1.00 71.50  ? 43  PRO B CB  1 
ATOM   3513 C  CG  . PRO B 1 14  ? -9.077  37.199 94.502  1.00 71.59  ? 43  PRO B CG  1 
ATOM   3514 C  CD  . PRO B 1 14  ? -8.469  35.840 94.661  1.00 69.91  ? 43  PRO B CD  1 
ATOM   3515 N  N   . ASP B 1 15  ? -5.690  38.313 97.617  1.00 70.86  ? 44  ASP B N   1 
ATOM   3516 C  CA  . ASP B 1 15  ? -5.145  38.303 98.970  1.00 70.95  ? 44  ASP B CA  1 
ATOM   3517 C  C   . ASP B 1 15  ? -6.138  38.876 100.020 1.00 71.42  ? 44  ASP B C   1 
ATOM   3518 O  O   . ASP B 1 15  ? -7.304  39.106 99.690  1.00 71.72  ? 44  ASP B O   1 
ATOM   3519 C  CB  . ASP B 1 15  ? -3.755  38.981 99.004  1.00 71.82  ? 44  ASP B CB  1 
ATOM   3520 C  CG  . ASP B 1 15  ? -3.701  40.472 98.736  1.00 75.44  ? 44  ASP B CG  1 
ATOM   3521 O  OD1 . ASP B 1 15  ? -4.778  41.103 98.642  1.00 75.10  ? 44  ASP B OD1 1 
ATOM   3522 O  OD2 . ASP B 1 15  ? -2.579  41.009 98.615  1.00 78.12  ? 44  ASP B OD2 1 
ATOM   3523 N  N   . ALA B 1 16  ? -5.692  39.062 101.282 1.00 71.21  ? 45  ALA B N   1 
ATOM   3524 C  CA  . ALA B 1 16  ? -6.498  39.580 102.386 1.00 71.46  ? 45  ALA B CA  1 
ATOM   3525 C  C   . ALA B 1 16  ? -7.115  40.943 102.089 1.00 71.75  ? 45  ALA B C   1 
ATOM   3526 O  O   . ALA B 1 16  ? -8.165  41.275 102.643 1.00 72.19  ? 45  ALA B O   1 
ATOM   3527 C  CB  . ALA B 1 16  ? -5.646  39.673 103.632 1.00 71.74  ? 45  ALA B CB  1 
ATOM   3528 N  N   . ALA B 1 17  ? -6.454  41.743 101.240 1.00 71.39  ? 46  ALA B N   1 
ATOM   3529 C  CA  . ALA B 1 17  ? -6.948  43.048 100.819 1.00 71.83  ? 46  ALA B CA  1 
ATOM   3530 C  C   . ALA B 1 17  ? -7.850  42.975 99.559  1.00 72.84  ? 46  ALA B C   1 
ATOM   3531 O  O   . ALA B 1 17  ? -8.220  44.016 99.015  1.00 73.25  ? 46  ALA B O   1 
ATOM   3532 C  CB  . ALA B 1 17  ? -5.773  43.965 100.540 1.00 71.81  ? 46  ALA B CB  1 
ATOM   3533 N  N   . GLY B 1 18  ? -8.181  41.765 99.103  1.00 72.83  ? 47  GLY B N   1 
ATOM   3534 C  CA  . GLY B 1 18  ? -8.968  41.529 97.904  1.00 73.06  ? 47  GLY B CA  1 
ATOM   3535 C  C   . GLY B 1 18  ? -8.241  42.005 96.665  1.00 72.76  ? 47  GLY B C   1 
ATOM   3536 O  O   . GLY B 1 18  ? -8.867  42.523 95.743  1.00 73.19  ? 47  GLY B O   1 
ATOM   3537 N  N   . LYS B 1 19  ? -6.912  41.864 96.643  1.00 72.19  ? 48  LYS B N   1 
ATOM   3538 C  CA  . LYS B 1 19  ? -6.105  42.334 95.527  1.00 72.01  ? 48  LYS B CA  1 
ATOM   3539 C  C   . LYS B 1 19  ? -5.249  41.241 94.903  1.00 71.94  ? 48  LYS B C   1 
ATOM   3540 O  O   . LYS B 1 19  ? -4.927  40.248 95.552  1.00 72.08  ? 48  LYS B O   1 
ATOM   3541 C  CB  . LYS B 1 19  ? -5.211  43.512 95.965  1.00 73.72  ? 48  LYS B CB  1 
ATOM   3542 C  CG  . LYS B 1 19  ? -5.977  44.797 96.276  1.00 77.61  ? 48  LYS B CG  1 
ATOM   3543 C  CD  . LYS B 1 19  ? -5.205  45.698 97.227  1.00 82.07  ? 48  LYS B CD  1 
ATOM   3544 C  CE  . LYS B 1 19  ? -5.729  47.112 97.259  1.00 86.08  ? 48  LYS B CE  1 
ATOM   3545 N  NZ  . LYS B 1 19  ? -4.712  48.078 96.742  1.00 88.97  ? 48  LYS B NZ  1 
ATOM   3546 N  N   . ILE B 1 20  ? -4.899  41.417 93.622  1.00 71.34  ? 49  ILE B N   1 
ATOM   3547 C  CA  . ILE B 1 20  ? -4.009  40.508 92.901  1.00 71.14  ? 49  ILE B CA  1 
ATOM   3548 C  C   . ILE B 1 20  ? -2.934  41.364 92.224  1.00 71.14  ? 49  ILE B C   1 
ATOM   3549 O  O   . ILE B 1 20  ? -3.260  42.363 91.581  1.00 71.83  ? 49  ILE B O   1 
ATOM   3550 C  CB  . ILE B 1 20  ? -4.736  39.552 91.917  1.00 71.16  ? 49  ILE B CB  1 
ATOM   3551 C  CG1 . ILE B 1 20  ? -5.635  38.544 92.674  1.00 71.94  ? 49  ILE B CG1 1 
ATOM   3552 C  CG2 . ILE B 1 20  ? -3.721  38.817 91.049  1.00 71.29  ? 49  ILE B CG2 1 
ATOM   3553 C  CD1 . ILE B 1 20  ? -6.480  37.647 91.803  1.00 72.88  ? 49  ILE B CD1 1 
ATOM   3554 N  N   . ALA B 1 21  ? -1.658  41.031 92.437  1.00 70.08  ? 50  ALA B N   1 
ATOM   3555 C  CA  . ALA B 1 21  ? -0.564  41.800 91.863  1.00 69.53  ? 50  ALA B CA  1 
ATOM   3556 C  C   . ALA B 1 21  ? 0.000   41.123 90.612  1.00 69.20  ? 50  ALA B C   1 
ATOM   3557 O  O   . ALA B 1 21  ? 0.359   39.940 90.649  1.00 69.33  ? 50  ALA B O   1 
ATOM   3558 C  CB  . ALA B 1 21  ? 0.532   41.999 92.897  1.00 69.49  ? 50  ALA B CB  1 
ATOM   3559 N  N   . LEU B 1 22  ? 0.071   41.882 89.497  1.00 68.31  ? 51  LEU B N   1 
ATOM   3560 C  CA  . LEU B 1 22  ? 0.620   41.395 88.236  1.00 67.69  ? 51  LEU B CA  1 
ATOM   3561 C  C   . LEU B 1 22  ? 1.780   42.287 87.818  1.00 67.62  ? 51  LEU B C   1 
ATOM   3562 O  O   . LEU B 1 22  ? 1.574   43.465 87.562  1.00 67.88  ? 51  LEU B O   1 
ATOM   3563 C  CB  . LEU B 1 22  ? -0.446  41.417 87.135  1.00 67.40  ? 51  LEU B CB  1 
ATOM   3564 C  CG  . LEU B 1 22  ? -1.648  40.507 87.284  1.00 68.24  ? 51  LEU B CG  1 
ATOM   3565 C  CD1 . LEU B 1 22  ? -2.541  40.608 86.064  1.00 68.52  ? 51  LEU B CD1 1 
ATOM   3566 C  CD2 . LEU B 1 22  ? -1.232  39.069 87.512  1.00 68.78  ? 51  LEU B CD2 1 
ATOM   3567 N  N   . ASN B 1 23  ? 2.991   41.742 87.756  1.00 67.18  ? 52  ASN B N   1 
ATOM   3568 C  CA  . ASN B 1 23  ? 4.156   42.496 87.337  1.00 67.56  ? 52  ASN B CA  1 
ATOM   3569 C  C   . ASN B 1 23  ? 4.525   42.083 85.927  1.00 68.34  ? 52  ASN B C   1 
ATOM   3570 O  O   . ASN B 1 23  ? 5.060   40.994 85.719  1.00 68.51  ? 52  ASN B O   1 
ATOM   3571 C  CB  . ASN B 1 23  ? 5.333   42.255 88.261  1.00 68.56  ? 52  ASN B CB  1 
ATOM   3572 C  CG  . ASN B 1 23  ? 6.413   43.303 88.123  1.00 71.42  ? 52  ASN B CG  1 
ATOM   3573 O  OD1 . ASN B 1 23  ? 6.265   44.438 88.584  1.00 72.84  ? 52  ASN B OD1 1 
ATOM   3574 N  ND2 . ASN B 1 23  ? 7.525   42.954 87.485  1.00 71.38  ? 52  ASN B ND2 1 
ATOM   3575 N  N   . VAL B 1 24  ? 4.216   42.948 84.952  1.00 68.41  ? 53  VAL B N   1 
ATOM   3576 C  CA  . VAL B 1 24  ? 4.517   42.719 83.542  1.00 68.28  ? 53  VAL B CA  1 
ATOM   3577 C  C   . VAL B 1 24  ? 5.997   43.014 83.382  1.00 67.77  ? 53  VAL B C   1 
ATOM   3578 O  O   . VAL B 1 24  ? 6.386   44.164 83.444  1.00 67.72  ? 53  VAL B O   1 
ATOM   3579 C  CB  . VAL B 1 24  ? 3.655   43.653 82.657  1.00 68.98  ? 53  VAL B CB  1 
ATOM   3580 C  CG1 . VAL B 1 24  ? 3.901   43.382 81.186  1.00 69.47  ? 53  VAL B CG1 1 
ATOM   3581 C  CG2 . VAL B 1 24  ? 2.172   43.507 82.982  1.00 69.48  ? 53  VAL B CG2 1 
ATOM   3582 N  N   . GLN B 1 25  ? 6.823   41.990 83.224  1.00 67.35  ? 54  GLN B N   1 
ATOM   3583 C  CA  . GLN B 1 25  ? 8.268   42.151 83.163  1.00 67.51  ? 54  GLN B CA  1 
ATOM   3584 C  C   . GLN B 1 25  ? 8.914   41.471 81.950  1.00 68.04  ? 54  GLN B C   1 
ATOM   3585 O  O   . GLN B 1 25  ? 8.260   40.713 81.239  1.00 67.95  ? 54  GLN B O   1 
ATOM   3586 C  CB  . GLN B 1 25  ? 8.861   41.563 84.452  1.00 68.41  ? 54  GLN B CB  1 
ATOM   3587 C  CG  . GLN B 1 25  ? 8.706   40.049 84.531  1.00 70.74  ? 54  GLN B CG  1 
ATOM   3588 C  CD  . GLN B 1 25  ? 8.474   39.572 85.935  1.00 74.93  ? 54  GLN B CD  1 
ATOM   3589 O  OE1 . GLN B 1 25  ? 7.800   40.224 86.745  1.00 76.22  ? 54  GLN B OE1 1 
ATOM   3590 N  NE2 . GLN B 1 25  ? 9.012   38.404 86.247  1.00 75.41  ? 54  GLN B NE2 1 
ATOM   3591 N  N   . THR B 1 26  ? 10.214  41.720 81.741  1.00 68.56  ? 55  THR B N   1 
ATOM   3592 C  CA  . THR B 1 26  ? 11.001  41.103 80.673  1.00 69.62  ? 55  THR B CA  1 
ATOM   3593 C  C   . THR B 1 26  ? 11.594  39.754 81.155  1.00 70.49  ? 55  THR B C   1 
ATOM   3594 O  O   . THR B 1 26  ? 11.537  39.434 82.342  1.00 71.24  ? 55  THR B O   1 
ATOM   3595 C  CB  . THR B 1 26  ? 12.091  42.091 80.201  1.00 71.33  ? 55  THR B CB  1 
ATOM   3596 O  OG1 . THR B 1 26  ? 13.088  42.225 81.219  1.00 72.73  ? 55  THR B OG1 1 
ATOM   3597 C  CG2 . THR B 1 26  ? 11.527  43.456 79.835  1.00 71.60  ? 55  THR B CG2 1 
ATOM   3598 N  N   . GLY B 1 27  ? 12.145  38.974 80.241  1.00 70.38  ? 56  GLY B N   1 
ATOM   3599 C  CA  . GLY B 1 27  ? 12.749  37.692 80.572  1.00 71.22  ? 56  GLY B CA  1 
ATOM   3600 C  C   . GLY B 1 27  ? 13.363  37.022 79.367  1.00 71.90  ? 56  GLY B C   1 
ATOM   3601 O  O   . GLY B 1 27  ? 13.620  37.673 78.352  1.00 71.88  ? 56  GLY B O   1 
ATOM   3602 N  N   . SER B 1 28  ? 13.604  35.718 79.466  1.00 72.41  ? 57  SER B N   1 
ATOM   3603 C  CA  . SER B 1 28  ? 14.134  34.950 78.342  1.00 73.35  ? 57  SER B CA  1 
ATOM   3604 C  C   . SER B 1 28  ? 13.692  33.480 78.373  1.00 73.81  ? 57  SER B C   1 
ATOM   3605 O  O   . SER B 1 28  ? 13.325  32.962 79.423  1.00 74.11  ? 57  SER B O   1 
ATOM   3606 C  CB  . SER B 1 28  ? 15.652  35.092 78.196  1.00 74.84  ? 57  SER B CB  1 
ATOM   3607 O  OG  . SER B 1 28  ? 16.399  34.699 79.336  1.00 77.34  ? 57  SER B OG  1 
ATOM   3608 N  N   . MET B 1 29  ? 13.654  32.833 77.208  1.00 73.68  ? 58  MET B N   1 
ATOM   3609 C  CA  . MET B 1 29  ? 13.262  31.428 77.101  1.00 73.97  ? 58  MET B CA  1 
ATOM   3610 C  C   . MET B 1 29  ? 14.253  30.728 76.199  1.00 75.08  ? 58  MET B C   1 
ATOM   3611 O  O   . MET B 1 29  ? 14.619  31.285 75.165  1.00 75.50  ? 58  MET B O   1 
ATOM   3612 C  CB  . MET B 1 29  ? 11.866  31.297 76.488  1.00 73.83  ? 58  MET B CB  1 
ATOM   3613 C  CG  . MET B 1 29  ? 10.782  32.017 77.253  1.00 74.71  ? 58  MET B CG  1 
ATOM   3614 S  SD  . MET B 1 29  ? 10.306  31.181 78.778  1.00 72.81  ? 58  MET B SD  1 
ATOM   3615 C  CE  . MET B 1 29  ? 9.664   29.702 78.129  1.00 67.89  ? 58  MET B CE  1 
ATOM   3616 N  N   . LYS B 1 30  ? 14.665  29.508 76.550  1.00 75.63  ? 59  LYS B N   1 
ATOM   3617 C  CA  . LYS B 1 30  ? 15.621  28.778 75.719  1.00 76.85  ? 59  LYS B CA  1 
ATOM   3618 C  C   . LYS B 1 30  ? 14.953  27.839 74.726  1.00 77.29  ? 59  LYS B C   1 
ATOM   3619 O  O   . LYS B 1 30  ? 14.678  26.695 75.068  1.00 77.72  ? 59  LYS B O   1 
ATOM   3620 C  CB  . LYS B 1 30  ? 16.656  28.045 76.582  1.00 79.47  ? 59  LYS B CB  1 
ATOM   3621 C  CG  . LYS B 1 30  ? 17.650  29.006 77.233  1.00 84.80  ? 59  LYS B CG  1 
ATOM   3622 C  CD  . LYS B 1 30  ? 18.368  28.425 78.459  1.00 89.85  ? 59  LYS B CD  1 
ATOM   3623 C  CE  . LYS B 1 30  ? 17.551  28.553 79.731  1.00 93.94  ? 59  LYS B CE  1 
ATOM   3624 N  NZ  . LYS B 1 30  ? 18.383  28.377 80.956  1.00 96.05  ? 59  LYS B NZ  1 
ATOM   3625 N  N   . TRP B 1 31  ? 14.699  28.312 73.496  1.00 77.13  ? 60  TRP B N   1 
ATOM   3626 C  CA  . TRP B 1 31  ? 14.086  27.503 72.440  1.00 77.77  ? 60  TRP B CA  1 
ATOM   3627 C  C   . TRP B 1 31  ? 15.147  27.009 71.437  1.00 79.35  ? 60  TRP B C   1 
ATOM   3628 O  O   . TRP B 1 31  ? 15.300  25.797 71.255  1.00 79.45  ? 60  TRP B O   1 
ATOM   3629 C  CB  . TRP B 1 31  ? 12.959  28.270 71.736  1.00 77.07  ? 60  TRP B CB  1 
ATOM   3630 C  CG  . TRP B 1 31  ? 11.775  28.514 72.609  1.00 76.89  ? 60  TRP B CG  1 
ATOM   3631 C  CD1 . TRP B 1 31  ? 11.055  27.582 73.291  1.00 77.57  ? 60  TRP B CD1 1 
ATOM   3632 C  CD2 . TRP B 1 31  ? 11.155  29.775 72.876  1.00 76.62  ? 60  TRP B CD2 1 
ATOM   3633 N  NE1 . TRP B 1 31  ? 10.034  28.186 73.982  1.00 77.68  ? 60  TRP B NE1 1 
ATOM   3634 C  CE2 . TRP B 1 31  ? 10.070  29.533 73.742  1.00 77.32  ? 60  TRP B CE2 1 
ATOM   3635 C  CE3 . TRP B 1 31  ? 11.416  31.089 72.475  1.00 76.83  ? 60  TRP B CE3 1 
ATOM   3636 C  CZ2 . TRP B 1 31  ? 9.247   30.552 74.206  1.00 77.84  ? 60  TRP B CZ2 1 
ATOM   3637 C  CZ3 . TRP B 1 31  ? 10.591  32.095 72.929  1.00 77.61  ? 60  TRP B CZ3 1 
ATOM   3638 C  CH2 . TRP B 1 31  ? 9.517   31.823 73.777  1.00 77.81  ? 60  TRP B CH2 1 
ATOM   3639 N  N   . LYS B 1 32  ? 15.889  27.942 70.802  1.00 80.17  ? 61  LYS B N   1 
ATOM   3640 C  CA  . LYS B 1 32  ? 16.961  27.587 69.877  1.00 81.23  ? 61  LYS B CA  1 
ATOM   3641 C  C   . LYS B 1 32  ? 18.137  27.107 70.728  1.00 82.53  ? 61  LYS B C   1 
ATOM   3642 O  O   . LYS B 1 32  ? 18.434  27.708 71.764  1.00 82.44  ? 61  LYS B O   1 
ATOM   3643 C  CB  . LYS B 1 32  ? 17.375  28.802 69.016  1.00 82.71  ? 61  LYS B CB  1 
ATOM   3644 C  CG  . LYS B 1 32  ? 16.948  28.729 67.540  1.00 85.77  ? 61  LYS B CG  1 
ATOM   3645 C  CD  . LYS B 1 32  ? 17.443  29.956 66.736  1.00 89.15  ? 61  LYS B CD  1 
ATOM   3646 C  CE  . LYS B 1 32  ? 17.300  29.835 65.231  1.00 92.03  ? 61  LYS B CE  1 
ATOM   3647 N  NZ  . LYS B 1 32  ? 16.074  30.503 64.709  1.00 93.71  ? 61  LYS B NZ  1 
ATOM   3648 N  N   . ALA B 1 33  ? 18.785  26.010 70.315  1.00 83.67  ? 62  ALA B N   1 
ATOM   3649 C  CA  . ALA B 1 33  ? 19.914  25.440 71.054  1.00 85.08  ? 62  ALA B CA  1 
ATOM   3650 C  C   . ALA B 1 33  ? 21.032  26.452 71.299  1.00 86.02  ? 62  ALA B C   1 
ATOM   3651 O  O   . ALA B 1 33  ? 21.566  27.026 70.348  1.00 86.14  ? 62  ALA B O   1 
ATOM   3652 C  CB  . ALA B 1 33  ? 20.452  24.217 70.329  1.00 85.48  ? 62  ALA B CB  1 
ATOM   3653 N  N   . GLY B 1 34  ? 21.331  26.689 72.574  1.00 86.47  ? 63  GLY B N   1 
ATOM   3654 C  CA  . GLY B 1 34  ? 22.361  27.635 72.987  1.00 87.51  ? 63  GLY B CA  1 
ATOM   3655 C  C   . GLY B 1 34  ? 22.025  29.072 72.636  1.00 88.28  ? 63  GLY B C   1 
ATOM   3656 O  O   . GLY B 1 34  ? 22.897  29.837 72.212  1.00 88.68  ? 63  GLY B O   1 
ATOM   3657 N  N   . MET B 1 35  ? 20.750  29.448 72.792  1.00 88.14  ? 64  MET B N   1 
ATOM   3658 C  CA  . MET B 1 35  ? 20.296  30.796 72.463  1.00 88.21  ? 64  MET B CA  1 
ATOM   3659 C  C   . MET B 1 35  ? 19.142  31.203 73.368  1.00 87.24  ? 64  MET B C   1 
ATOM   3660 O  O   . MET B 1 35  ? 18.041  30.678 73.221  1.00 87.74  ? 64  MET B O   1 
ATOM   3661 C  CB  . MET B 1 35  ? 19.850  30.858 70.990  1.00 89.61  ? 64  MET B CB  1 
ATOM   3662 C  CG  . MET B 1 35  ? 20.742  31.721 70.121  1.00 93.84  ? 64  MET B CG  1 
ATOM   3663 S  SD  . MET B 1 35  ? 20.382  31.595 68.342  1.00 103.38 ? 64  MET B SD  1 
ATOM   3664 C  CE  . MET B 1 35  ? 20.882  29.881 68.037  1.00 102.54 ? 64  MET B CE  1 
ATOM   3665 N  N   . GLN B 1 36  ? 19.381  32.130 74.300  1.00 85.72  ? 65  GLN B N   1 
ATOM   3666 C  CA  . GLN B 1 36  ? 18.319  32.626 75.171  1.00 84.69  ? 65  GLN B CA  1 
ATOM   3667 C  C   . GLN B 1 36  ? 17.510  33.661 74.383  1.00 82.70  ? 65  GLN B C   1 
ATOM   3668 O  O   . GLN B 1 36  ? 18.069  34.668 73.944  1.00 82.97  ? 65  GLN B O   1 
ATOM   3669 C  CB  . GLN B 1 36  ? 18.908  33.278 76.431  1.00 86.95  ? 65  GLN B CB  1 
ATOM   3670 C  CG  . GLN B 1 36  ? 19.513  32.289 77.420  1.00 91.71  ? 65  GLN B CG  1 
ATOM   3671 C  CD  . GLN B 1 36  ? 18.624  32.056 78.621  1.00 97.46  ? 65  GLN B CD  1 
ATOM   3672 O  OE1 . GLN B 1 36  ? 17.391  32.165 78.555  1.00 99.53  ? 65  GLN B OE1 1 
ATOM   3673 N  NE2 . GLN B 1 36  ? 19.229  31.715 79.748  1.00 98.31  ? 65  GLN B NE2 1 
ATOM   3674 N  N   . THR B 1 37  ? 16.216  33.406 74.168  1.00 80.45  ? 66  THR B N   1 
ATOM   3675 C  CA  . THR B 1 37  ? 15.371  34.334 73.431  1.00 78.77  ? 66  THR B CA  1 
ATOM   3676 C  C   . THR B 1 37  ? 14.775  35.352 74.365  1.00 76.52  ? 66  THR B C   1 
ATOM   3677 O  O   . THR B 1 37  ? 14.056  34.975 75.268  1.00 76.49  ? 66  THR B O   1 
ATOM   3678 C  CB  . THR B 1 37  ? 14.253  33.578 72.714  1.00 80.19  ? 66  THR B CB  1 
ATOM   3679 O  OG1 . THR B 1 37  ? 14.840  32.771 71.699  1.00 81.37  ? 66  THR B OG1 1 
ATOM   3680 C  CG2 . THR B 1 37  ? 13.211  34.510 72.087  1.00 80.51  ? 66  THR B CG2 1 
ATOM   3681 N  N   . PRO B 1 38  ? 15.008  36.646 74.132  1.00 74.76  ? 67  PRO B N   1 
ATOM   3682 C  CA  . PRO B 1 38  ? 14.370  37.671 74.966  1.00 73.99  ? 67  PRO B CA  1 
ATOM   3683 C  C   . PRO B 1 38  ? 12.852  37.667 74.776  1.00 73.38  ? 67  PRO B C   1 
ATOM   3684 O  O   . PRO B 1 38  ? 12.361  37.784 73.651  1.00 73.45  ? 67  PRO B O   1 
ATOM   3685 C  CB  . PRO B 1 38  ? 14.971  38.974 74.443  1.00 74.57  ? 67  PRO B CB  1 
ATOM   3686 C  CG  . PRO B 1 38  ? 16.154  38.572 73.635  1.00 75.00  ? 67  PRO B CG  1 
ATOM   3687 C  CD  . PRO B 1 38  ? 15.826  37.247 73.072  1.00 73.79  ? 67  PRO B CD  1 
ATOM   3688 N  N   . THR B 1 39  ? 12.114  37.481 75.874  1.00 72.47  ? 68  THR B N   1 
ATOM   3689 C  CA  . THR B 1 39  ? 10.656  37.411 75.883  1.00 72.13  ? 68  THR B CA  1 
ATOM   3690 C  C   . THR B 1 39  ? 10.053  38.337 76.958  1.00 71.92  ? 68  THR B C   1 
ATOM   3691 O  O   . THR B 1 39  ? 10.780  38.912 77.749  1.00 72.28  ? 68  THR B O   1 
ATOM   3692 C  CB  . THR B 1 39  ? 10.229  35.946 76.099  1.00 73.06  ? 68  THR B CB  1 
ATOM   3693 O  OG1 . THR B 1 39  ? 10.764  35.461 77.333  1.00 73.80  ? 68  THR B OG1 1 
ATOM   3694 C  CG2 . THR B 1 39  ? 10.618  35.047 74.950  1.00 73.32  ? 68  THR B CG2 1 
ATOM   3695 N  N   . TRP B 1 40  ? 8.733   38.500 76.970  1.00 71.47  ? 69  TRP B N   1 
ATOM   3696 C  CA  . TRP B 1 40  ? 7.998   39.291 77.953  1.00 71.61  ? 69  TRP B CA  1 
ATOM   3697 C  C   . TRP B 1 40  ? 7.045   38.351 78.716  1.00 71.23  ? 69  TRP B C   1 
ATOM   3698 O  O   . TRP B 1 40  ? 6.688   37.297 78.195  1.00 71.36  ? 69  TRP B O   1 
ATOM   3699 C  CB  . TRP B 1 40  ? 7.188   40.402 77.251  1.00 71.70  ? 69  TRP B CB  1 
ATOM   3700 C  CG  . TRP B 1 40  ? 7.972   41.585 76.753  1.00 72.45  ? 69  TRP B CG  1 
ATOM   3701 C  CD1 . TRP B 1 40  ? 9.311   41.811 76.880  1.00 73.42  ? 69  TRP B CD1 1 
ATOM   3702 C  CD2 . TRP B 1 40  ? 7.438   42.721 76.058  1.00 72.91  ? 69  TRP B CD2 1 
ATOM   3703 N  NE1 . TRP B 1 40  ? 9.643   43.021 76.312  1.00 73.84  ? 69  TRP B NE1 1 
ATOM   3704 C  CE2 . TRP B 1 40  ? 8.510   43.600 75.801  1.00 73.56  ? 69  TRP B CE2 1 
ATOM   3705 C  CE3 . TRP B 1 40  ? 6.152   43.082 75.628  1.00 73.48  ? 69  TRP B CE3 1 
ATOM   3706 C  CZ2 . TRP B 1 40  ? 8.333   44.814 75.141  1.00 73.89  ? 69  TRP B CZ2 1 
ATOM   3707 C  CZ3 . TRP B 1 40  ? 5.987   44.278 74.958  1.00 73.95  ? 69  TRP B CZ3 1 
ATOM   3708 C  CH2 . TRP B 1 40  ? 7.068   45.126 74.722  1.00 73.93  ? 69  TRP B CH2 1 
ATOM   3709 N  N   . GLY B 1 41  ? 6.651   38.721 79.932  1.00 70.57  ? 70  GLY B N   1 
ATOM   3710 C  CA  . GLY B 1 41  ? 5.748   37.888 80.721  1.00 70.37  ? 70  GLY B CA  1 
ATOM   3711 C  C   . GLY B 1 41  ? 5.213   38.529 81.982  1.00 69.69  ? 70  GLY B C   1 
ATOM   3712 O  O   . GLY B 1 41  ? 5.811   39.456 82.523  1.00 70.16  ? 70  GLY B O   1 
ATOM   3713 N  N   . ILE B 1 42  ? 4.088   38.036 82.463  1.00 68.56  ? 71  ILE B N   1 
ATOM   3714 C  CA  . ILE B 1 42  ? 3.492   38.521 83.697  1.00 68.27  ? 71  ILE B CA  1 
ATOM   3715 C  C   . ILE B 1 42  ? 3.929   37.592 84.829  1.00 67.70  ? 71  ILE B C   1 
ATOM   3716 O  O   . ILE B 1 42  ? 3.590   36.403 84.823  1.00 67.80  ? 71  ILE B O   1 
ATOM   3717 C  CB  . ILE B 1 42  ? 1.958   38.627 83.585  1.00 68.52  ? 71  ILE B CB  1 
ATOM   3718 C  CG1 . ILE B 1 42  ? 1.568   39.588 82.460  1.00 69.39  ? 71  ILE B CG1 1 
ATOM   3719 C  CG2 . ILE B 1 42  ? 1.368   39.073 84.903  1.00 68.70  ? 71  ILE B CG2 1 
ATOM   3720 C  CD1 . ILE B 1 42  ? 0.993   38.938 81.291  1.00 70.55  ? 71  ILE B CD1 1 
ATOM   3721 N  N   . ASN B 1 43  ? 4.734   38.125 85.761  1.00 66.57  ? 72  ASN B N   1 
ATOM   3722 C  CA  . ASN B 1 43  ? 5.289   37.379 86.889  1.00 65.98  ? 72  ASN B CA  1 
ATOM   3723 C  C   . ASN B 1 43  ? 6.264   36.269 86.478  1.00 65.79  ? 72  ASN B C   1 
ATOM   3724 O  O   . ASN B 1 43  ? 6.535   35.376 87.276  1.00 66.26  ? 72  ASN B O   1 
ATOM   3725 C  CB  . ASN B 1 43  ? 4.196   36.828 87.809  1.00 65.94  ? 72  ASN B CB  1 
ATOM   3726 C  CG  . ASN B 1 43  ? 3.166   37.840 88.226  1.00 66.71  ? 72  ASN B CG  1 
ATOM   3727 O  OD1 . ASN B 1 43  ? 3.286   39.024 87.945  1.00 66.59  ? 72  ASN B OD1 1 
ATOM   3728 N  ND2 . ASN B 1 43  ? 2.117   37.386 88.899  1.00 66.96  ? 72  ASN B ND2 1 
ATOM   3729 N  N   . GLY B 1 44  ? 6.807   36.350 85.271  1.00 64.95  ? 73  GLY B N   1 
ATOM   3730 C  CA  . GLY B 1 44  ? 7.756   35.365 84.773  1.00 64.79  ? 73  GLY B CA  1 
ATOM   3731 C  C   . GLY B 1 44  ? 8.372   35.770 83.452  1.00 64.44  ? 73  GLY B C   1 
ATOM   3732 O  O   . GLY B 1 44  ? 8.191   36.898 82.983  1.00 64.73  ? 73  GLY B O   1 
ATOM   3733 N  N   . PRO B 1 45  ? 9.120   34.861 82.823  1.00 63.60  ? 74  PRO B N   1 
ATOM   3734 C  CA  . PRO B 1 45  ? 9.771   35.210 81.546  1.00 63.42  ? 74  PRO B CA  1 
ATOM   3735 C  C   . PRO B 1 45  ? 8.843   35.198 80.326  1.00 63.10  ? 74  PRO B C   1 
ATOM   3736 O  O   . PRO B 1 45  ? 9.179   35.769 79.288  1.00 63.59  ? 74  PRO B O   1 
ATOM   3737 C  CB  . PRO B 1 45  ? 10.868  34.155 81.424  1.00 63.91  ? 74  PRO B CB  1 
ATOM   3738 C  CG  . PRO B 1 45  ? 10.306  32.976 82.125  1.00 64.28  ? 74  PRO B CG  1 
ATOM   3739 C  CD  . PRO B 1 45  ? 9.448   33.491 83.251  1.00 62.76  ? 74  PRO B CD  1 
ATOM   3740 N  N   . LEU B 1 46  ? 7.697   34.525 80.450  1.00 62.06  ? 75  LEU B N   1 
ATOM   3741 C  CA  . LEU B 1 46  ? 6.713   34.363 79.394  1.00 61.77  ? 75  LEU B CA  1 
ATOM   3742 C  C   . LEU B 1 46  ? 5.374   33.975 80.010  1.00 62.07  ? 75  LEU B C   1 
ATOM   3743 O  O   . LEU B 1 46  ? 5.322   33.419 81.116  1.00 62.10  ? 75  LEU B O   1 
ATOM   3744 C  CB  . LEU B 1 46  ? 7.179   33.271 78.432  1.00 61.52  ? 75  LEU B CB  1 
ATOM   3745 C  CG  . LEU B 1 46  ? 6.448   33.145 77.119  1.00 62.18  ? 75  LEU B CG  1 
ATOM   3746 C  CD1 . LEU B 1 46  ? 7.209   33.831 76.017  1.00 62.40  ? 75  LEU B CD1 1 
ATOM   3747 C  CD2 . LEU B 1 46  ? 6.283   31.700 76.771  1.00 62.58  ? 75  LEU B CD2 1 
ATOM   3748 N  N   . LEU B 1 47  ? 4.290   34.275 79.281  1.00 61.96  ? 76  LEU B N   1 
ATOM   3749 C  CA  . LEU B 1 47  ? 2.900   34.028 79.660  1.00 62.01  ? 76  LEU B CA  1 
ATOM   3750 C  C   . LEU B 1 47  ? 2.595   34.635 81.063  1.00 62.63  ? 76  LEU B C   1 
ATOM   3751 O  O   . LEU B 1 47  ? 3.096   35.721 81.329  1.00 63.22  ? 76  LEU B O   1 
ATOM   3752 C  CB  . LEU B 1 47  ? 2.554   32.546 79.490  1.00 61.50  ? 76  LEU B CB  1 
ATOM   3753 C  CG  . LEU B 1 47  ? 2.414   32.153 78.046  1.00 62.04  ? 76  LEU B CG  1 
ATOM   3754 C  CD1 . LEU B 1 47  ? 2.381   30.666 77.894  1.00 62.45  ? 76  LEU B CD1 1 
ATOM   3755 C  CD2 . LEU B 1 47  ? 1.185   32.789 77.437  1.00 62.56  ? 76  LEU B CD2 1 
ATOM   3756 N  N   . GLY B 1 48  ? 1.768   34.013 81.898  1.00 62.25  ? 77  GLY B N   1 
ATOM   3757 C  CA  . GLY B 1 48  ? 1.437   34.585 83.195  1.00 62.63  ? 77  GLY B CA  1 
ATOM   3758 C  C   . GLY B 1 48  ? 0.720   33.626 84.109  1.00 63.04  ? 77  GLY B C   1 
ATOM   3759 O  O   . GLY B 1 48  ? 0.602   32.433 83.820  1.00 63.68  ? 77  GLY B O   1 
ATOM   3760 N  N   . PRO B 1 49  ? 0.204   34.146 85.220  1.00 62.45  ? 78  PRO B N   1 
ATOM   3761 C  CA  . PRO B 1 49  ? -0.498  33.275 86.168  1.00 62.23  ? 78  PRO B CA  1 
ATOM   3762 C  C   . PRO B 1 49  ? -1.966  33.032 85.809  1.00 61.79  ? 78  PRO B C   1 
ATOM   3763 O  O   . PRO B 1 49  ? -2.507  33.657 84.903  1.00 61.83  ? 78  PRO B O   1 
ATOM   3764 C  CB  . PRO B 1 49  ? -0.358  34.036 87.484  1.00 63.14  ? 78  PRO B CB  1 
ATOM   3765 C  CG  . PRO B 1 49  ? -0.368  35.483 87.053  1.00 63.73  ? 78  PRO B CG  1 
ATOM   3766 C  CD  . PRO B 1 49  ? 0.256   35.546 85.684  1.00 61.99  ? 78  PRO B CD  1 
ATOM   3767 N  N   . ALA B 1 50  ? -2.599  32.117 86.517  1.00 61.49  ? 79  ALA B N   1 
ATOM   3768 C  CA  . ALA B 1 50  ? -4.004  31.831 86.355  1.00 62.11  ? 79  ALA B CA  1 
ATOM   3769 C  C   . ALA B 1 50  ? -4.689  32.452 87.572  1.00 62.72  ? 79  ALA B C   1 
ATOM   3770 O  O   . ALA B 1 50  ? -4.521  31.956 88.679  1.00 62.90  ? 79  ALA B O   1 
ATOM   3771 C  CB  . ALA B 1 50  ? -4.231  30.329 86.335  1.00 62.21  ? 79  ALA B CB  1 
ATOM   3772 N  N   . MET B 1 51  ? -5.401  33.564 87.386  1.00 62.91  ? 80  MET B N   1 
ATOM   3773 C  CA  . MET B 1 51  ? -6.091  34.218 88.485  1.00 63.69  ? 80  MET B CA  1 
ATOM   3774 C  C   . MET B 1 51  ? -7.376  33.451 88.775  1.00 64.81  ? 80  MET B C   1 
ATOM   3775 O  O   . MET B 1 51  ? -8.237  33.373 87.908  1.00 64.80  ? 80  MET B O   1 
ATOM   3776 C  CB  . MET B 1 51  ? -6.398  35.684 88.142  1.00 64.03  ? 80  MET B CB  1 
ATOM   3777 C  CG  . MET B 1 51  ? -5.182  36.444 87.647  1.00 66.45  ? 80  MET B CG  1 
ATOM   3778 S  SD  . MET B 1 51  ? -5.386  38.246 87.552  1.00 71.79  ? 80  MET B SD  1 
ATOM   3779 C  CE  . MET B 1 51  ? -6.663  38.367 86.331  1.00 69.92  ? 80  MET B CE  1 
ATOM   3780 N  N   . ARG B 1 52  ? -7.488  32.840 89.970  1.00 65.31  ? 81  ARG B N   1 
ATOM   3781 C  CA  . ARG B 1 52  ? -8.696  32.116 90.333  1.00 66.10  ? 81  ARG B CA  1 
ATOM   3782 C  C   . ARG B 1 52  ? -9.614  33.095 91.053  1.00 67.02  ? 81  ARG B C   1 
ATOM   3783 O  O   . ARG B 1 52  ? -9.268  33.629 92.108  1.00 66.95  ? 81  ARG B O   1 
ATOM   3784 C  CB  . ARG B 1 52  ? -8.401  30.875 91.191  1.00 67.14  ? 81  ARG B CB  1 
ATOM   3785 C  CG  . ARG B 1 52  ? -9.606  29.939 91.321  1.00 70.54  ? 81  ARG B CG  1 
ATOM   3786 C  CD  . ARG B 1 52  ? -9.181  28.479 91.368  1.00 75.43  ? 81  ARG B CD  1 
ATOM   3787 N  NE  . ARG B 1 52  ? -10.231 27.560 90.918  1.00 79.09  ? 81  ARG B NE  1 
ATOM   3788 C  CZ  . ARG B 1 52  ? -10.021 26.306 90.516  1.00 80.78  ? 81  ARG B CZ  1 
ATOM   3789 N  NH1 . ARG B 1 52  ? -8.794  25.811 90.475  1.00 79.19  ? 81  ARG B NH1 1 
ATOM   3790 N  NH2 . ARG B 1 52  ? -11.041 25.547 90.133  1.00 81.01  ? 81  ARG B NH2 1 
ATOM   3791 N  N   . LEU B 1 53  ? -10.765 33.373 90.442  1.00 67.52  ? 82  LEU B N   1 
ATOM   3792 C  CA  . LEU B 1 53  ? -11.736 34.306 90.986  1.00 68.52  ? 82  LEU B CA  1 
ATOM   3793 C  C   . LEU B 1 53  ? -13.069 33.610 91.216  1.00 70.04  ? 82  LEU B C   1 
ATOM   3794 O  O   . LEU B 1 53  ? -13.445 32.722 90.461  1.00 69.98  ? 82  LEU B O   1 
ATOM   3795 C  CB  . LEU B 1 53  ? -11.911 35.505 90.048  1.00 68.49  ? 82  LEU B CB  1 
ATOM   3796 C  CG  . LEU B 1 53  ? -10.628 36.187 89.592  1.00 69.65  ? 82  LEU B CG  1 
ATOM   3797 C  CD1 . LEU B 1 53  ? -10.908 37.232 88.555  1.00 70.12  ? 82  LEU B CD1 1 
ATOM   3798 C  CD2 . LEU B 1 53  ? -9.895  36.782 90.752  1.00 70.47  ? 82  LEU B CD2 1 
ATOM   3799 N  N   . GLN B 1 54  ? -13.774 34.000 92.276  1.00 71.15  ? 83  GLN B N   1 
ATOM   3800 C  CA  . GLN B 1 54  ? -15.066 33.414 92.615  1.00 72.21  ? 83  GLN B CA  1 
ATOM   3801 C  C   . GLN B 1 54  ? -16.171 34.341 92.128  1.00 72.49  ? 83  GLN B C   1 
ATOM   3802 O  O   . GLN B 1 54  ? -16.035 35.563 92.221  1.00 72.51  ? 83  GLN B O   1 
ATOM   3803 C  CB  . GLN B 1 54  ? -15.167 33.223 94.139  1.00 74.59  ? 83  GLN B CB  1 
ATOM   3804 C  CG  . GLN B 1 54  ? -15.961 31.992 94.563  1.00 79.33  ? 83  GLN B CG  1 
ATOM   3805 C  CD  . GLN B 1 54  ? -15.156 30.706 94.478  1.00 85.18  ? 83  GLN B CD  1 
ATOM   3806 O  OE1 . GLN B 1 54  ? -13.913 30.711 94.416  1.00 87.30  ? 83  GLN B OE1 1 
ATOM   3807 N  NE2 . GLN B 1 54  ? -15.855 29.566 94.483  1.00 85.45  ? 83  GLN B NE2 1 
ATOM   3808 N  N   . ARG B 1 55  ? -17.260 33.773 91.596  1.00 72.72  ? 84  ARG B N   1 
ATOM   3809 C  CA  . ARG B 1 55  ? -18.391 34.572 91.128  1.00 73.47  ? 84  ARG B CA  1 
ATOM   3810 C  C   . ARG B 1 55  ? -19.041 35.269 92.314  1.00 73.84  ? 84  ARG B C   1 
ATOM   3811 O  O   . ARG B 1 55  ? -19.299 34.641 93.337  1.00 74.20  ? 84  ARG B O   1 
ATOM   3812 C  CB  . ARG B 1 55  ? -19.435 33.724 90.380  1.00 74.83  ? 84  ARG B CB  1 
ATOM   3813 C  CG  . ARG B 1 55  ? -20.509 34.606 89.751  1.00 77.30  ? 84  ARG B CG  1 
ATOM   3814 C  CD  . ARG B 1 55  ? -21.712 33.876 89.201  1.00 80.26  ? 84  ARG B CD  1 
ATOM   3815 N  NE  . ARG B 1 55  ? -22.540 34.793 88.415  1.00 83.27  ? 84  ARG B NE  1 
ATOM   3816 C  CZ  . ARG B 1 55  ? -23.470 34.413 87.546  1.00 86.01  ? 84  ARG B CZ  1 
ATOM   3817 N  NH1 . ARG B 1 55  ? -23.707 33.121 87.336  1.00 85.83  ? 84  ARG B NH1 1 
ATOM   3818 N  NH2 . ARG B 1 55  ? -24.160 35.319 86.866  1.00 86.13  ? 84  ARG B NH2 1 
ATOM   3819 N  N   . GLY B 1 56  ? -19.235 36.567 92.189  1.00 73.64  ? 85  GLY B N   1 
ATOM   3820 C  CA  . GLY B 1 56  ? -19.808 37.361 93.259  1.00 74.38  ? 85  GLY B CA  1 
ATOM   3821 C  C   . GLY B 1 56  ? -18.743 38.139 93.994  1.00 75.24  ? 85  GLY B C   1 
ATOM   3822 O  O   . GLY B 1 56  ? -18.956 39.298 94.361  1.00 75.56  ? 85  GLY B O   1 
ATOM   3823 N  N   . LYS B 1 57  ? -17.575 37.519 94.194  1.00 75.59  ? 86  LYS B N   1 
ATOM   3824 C  CA  . LYS B 1 57  ? -16.481 38.175 94.891  1.00 76.45  ? 86  LYS B CA  1 
ATOM   3825 C  C   . LYS B 1 57  ? -15.790 39.243 94.041  1.00 76.89  ? 86  LYS B C   1 
ATOM   3826 O  O   . LYS B 1 57  ? -15.802 39.189 92.812  1.00 76.84  ? 86  LYS B O   1 
ATOM   3827 C  CB  . LYS B 1 57  ? -15.486 37.150 95.457  1.00 78.79  ? 86  LYS B CB  1 
ATOM   3828 C  CG  . LYS B 1 57  ? -16.079 36.316 96.600  1.00 83.70  ? 86  LYS B CG  1 
ATOM   3829 C  CD  . LYS B 1 57  ? -14.999 35.546 97.374  1.00 89.11  ? 86  LYS B CD  1 
ATOM   3830 C  CE  . LYS B 1 57  ? -15.340 35.287 98.828  1.00 92.58  ? 86  LYS B CE  1 
ATOM   3831 N  NZ  . LYS B 1 57  ? -14.206 34.645 99.551  1.00 94.15  ? 86  LYS B NZ  1 
ATOM   3832 N  N   . ASP B 1 58  ? -15.243 40.251 94.711  1.00 77.20  ? 87  ASP B N   1 
ATOM   3833 C  CA  . ASP B 1 58  ? -14.557 41.362 94.059  1.00 77.81  ? 87  ASP B CA  1 
ATOM   3834 C  C   . ASP B 1 58  ? -13.048 41.180 94.087  1.00 77.74  ? 87  ASP B C   1 
ATOM   3835 O  O   . ASP B 1 58  ? -12.528 40.401 94.888  1.00 78.10  ? 87  ASP B O   1 
ATOM   3836 C  CB  . ASP B 1 58  ? -14.928 42.690 94.735  1.00 79.97  ? 87  ASP B CB  1 
ATOM   3837 C  CG  . ASP B 1 58  ? -16.352 43.107 94.467  1.00 86.16  ? 87  ASP B CG  1 
ATOM   3838 O  OD1 . ASP B 1 58  ? -17.261 42.262 94.642  1.00 87.10  ? 87  ASP B OD1 1 
ATOM   3839 O  OD2 . ASP B 1 58  ? -16.563 44.280 94.081  1.00 89.16  ? 87  ASP B OD2 1 
ATOM   3840 N  N   . VAL B 1 59  ? -12.343 41.899 93.205  1.00 76.96  ? 88  VAL B N   1 
ATOM   3841 C  CA  . VAL B 1 59  ? -10.892 41.861 93.136  1.00 76.74  ? 88  VAL B CA  1 
ATOM   3842 C  C   . VAL B 1 59  ? -10.367 43.161 92.530  1.00 76.38  ? 88  VAL B C   1 
ATOM   3843 O  O   . VAL B 1 59  ? -11.022 43.771 91.692  1.00 76.49  ? 88  VAL B O   1 
ATOM   3844 C  CB  . VAL B 1 59  ? -10.369 40.605 92.387  1.00 77.47  ? 88  VAL B CB  1 
ATOM   3845 C  CG1 . VAL B 1 59  ? -10.692 40.669 90.904  1.00 78.04  ? 88  VAL B CG1 1 
ATOM   3846 C  CG2 . VAL B 1 59  ? -8.875  40.395 92.611  1.00 78.02  ? 88  VAL B CG2 1 
ATOM   3847 N  N   . ALA B 1 60  ? -9.217  43.616 92.995  1.00 75.75  ? 89  ALA B N   1 
ATOM   3848 C  CA  . ALA B 1 60  ? -8.564  44.792 92.460  1.00 75.90  ? 89  ALA B CA  1 
ATOM   3849 C  C   . ALA B 1 60  ? -7.272  44.262 91.886  1.00 76.60  ? 89  ALA B C   1 
ATOM   3850 O  O   . ALA B 1 60  ? -6.506  43.630 92.613  1.00 77.14  ? 89  ALA B O   1 
ATOM   3851 C  CB  . ALA B 1 60  ? -8.273  45.781 93.568  1.00 75.81  ? 89  ALA B CB  1 
ATOM   3852 N  N   . ILE B 1 61  ? -7.042  44.447 90.583  1.00 76.49  ? 90  ILE B N   1 
ATOM   3853 C  CA  . ILE B 1 61  ? -5.833  43.906 89.969  1.00 76.72  ? 90  ILE B CA  1 
ATOM   3854 C  C   . ILE B 1 61  ? -4.807  44.996 89.715  1.00 76.73  ? 90  ILE B C   1 
ATOM   3855 O  O   . ILE B 1 61  ? -4.972  45.844 88.839  1.00 76.61  ? 90  ILE B O   1 
ATOM   3856 C  CB  . ILE B 1 61  ? -6.135  43.048 88.729  1.00 77.16  ? 90  ILE B CB  1 
ATOM   3857 C  CG1 . ILE B 1 61  ? -7.209  41.996 89.065  1.00 78.09  ? 90  ILE B CG1 1 
ATOM   3858 C  CG2 . ILE B 1 61  ? -4.863  42.380 88.239  1.00 77.43  ? 90  ILE B CG2 1 
ATOM   3859 C  CD1 . ILE B 1 61  ? -7.931  41.521 87.938  1.00 79.29  ? 90  ILE B CD1 1 
ATOM   3860 N  N   . ASN B 1 62  ? -3.746  44.969 90.517  1.00 76.53  ? 91  ASN B N   1 
ATOM   3861 C  CA  . ASN B 1 62  ? -2.670  45.930 90.442  1.00 77.00  ? 91  ASN B CA  1 
ATOM   3862 C  C   . ASN B 1 62  ? -1.652  45.522 89.387  1.00 76.96  ? 91  ASN B C   1 
ATOM   3863 O  O   . ASN B 1 62  ? -0.713  44.772 89.671  1.00 77.12  ? 91  ASN B O   1 
ATOM   3864 C  CB  . ASN B 1 62  ? -2.039  46.087 91.811  1.00 78.83  ? 91  ASN B CB  1 
ATOM   3865 C  CG  . ASN B 1 62  ? -2.989  46.705 92.806  1.00 83.27  ? 91  ASN B CG  1 
ATOM   3866 O  OD1 . ASN B 1 62  ? -3.753  47.612 92.476  1.00 85.05  ? 91  ASN B OD1 1 
ATOM   3867 N  ND2 . ASN B 1 62  ? -2.966  46.240 94.050  1.00 84.24  ? 91  ASN B ND2 1 
ATOM   3868 N  N   . VAL B 1 63  ? -1.855  46.006 88.153  1.00 76.45  ? 92  VAL B N   1 
ATOM   3869 C  CA  . VAL B 1 63  ? -0.979  45.701 87.024  1.00 76.27  ? 92  VAL B CA  1 
ATOM   3870 C  C   . VAL B 1 63  ? 0.159   46.712 86.951  1.00 76.25  ? 92  VAL B C   1 
ATOM   3871 O  O   . VAL B 1 63  ? -0.072  47.873 86.640  1.00 76.39  ? 92  VAL B O   1 
ATOM   3872 C  CB  . VAL B 1 63  ? -1.744  45.623 85.681  1.00 76.60  ? 92  VAL B CB  1 
ATOM   3873 C  CG1 . VAL B 1 63  ? -0.854  45.052 84.588  1.00 77.03  ? 92  VAL B CG1 1 
ATOM   3874 C  CG2 . VAL B 1 63  ? -3.016  44.799 85.814  1.00 77.02  ? 92  VAL B CG2 1 
ATOM   3875 N  N   . THR B 1 64  ? 1.385   46.268 87.236  1.00 75.95  ? 93  THR B N   1 
ATOM   3876 C  CA  . THR B 1 64  ? 2.579   47.102 87.222  1.00 76.07  ? 93  THR B CA  1 
ATOM   3877 C  C   . THR B 1 64  ? 3.310   46.867 85.918  1.00 76.08  ? 93  THR B C   1 
ATOM   3878 O  O   . THR B 1 64  ? 3.580   45.717 85.571  1.00 76.28  ? 93  THR B O   1 
ATOM   3879 C  CB  . THR B 1 64  ? 3.532   46.692 88.350  1.00 77.59  ? 93  THR B CB  1 
ATOM   3880 O  OG1 . THR B 1 64  ? 2.822   46.439 89.569  1.00 79.01  ? 93  THR B OG1 1 
ATOM   3881 C  CG2 . THR B 1 64  ? 4.637   47.704 88.568  1.00 77.91  ? 93  THR B CG2 1 
ATOM   3882 N  N   . ASN B 1 65  ? 3.652   47.944 85.198  1.00 75.49  ? 94  ASN B N   1 
ATOM   3883 C  CA  . ASN B 1 65  ? 4.394   47.815 83.952  1.00 74.91  ? 94  ASN B CA  1 
ATOM   3884 C  C   . ASN B 1 65  ? 5.862   47.951 84.269  1.00 73.95  ? 94  ASN B C   1 
ATOM   3885 O  O   . ASN B 1 65  ? 6.286   49.006 84.705  1.00 74.04  ? 94  ASN B O   1 
ATOM   3886 C  CB  . ASN B 1 65  ? 3.978   48.895 82.941  1.00 75.99  ? 94  ASN B CB  1 
ATOM   3887 C  CG  . ASN B 1 65  ? 4.572   48.707 81.556  1.00 79.18  ? 94  ASN B CG  1 
ATOM   3888 O  OD1 . ASN B 1 65  ? 5.314   47.759 81.291  1.00 80.23  ? 94  ASN B OD1 1 
ATOM   3889 N  ND2 . ASN B 1 65  ? 4.258   49.602 80.629  1.00 79.90  ? 94  ASN B ND2 1 
ATOM   3890 N  N   . ALA B 1 66  ? 6.626   46.884 84.086  1.00 73.09  ? 95  ALA B N   1 
ATOM   3891 C  CA  . ALA B 1 66  ? 8.079   46.896 84.267  1.00 73.00  ? 95  ALA B CA  1 
ATOM   3892 C  C   . ALA B 1 66  ? 8.820   46.715 82.932  1.00 73.28  ? 95  ALA B C   1 
ATOM   3893 O  O   . ALA B 1 66  ? 9.993   46.343 82.928  1.00 73.32  ? 95  ALA B O   1 
ATOM   3894 C  CB  . ALA B 1 66  ? 8.501   45.813 85.236  1.00 72.98  ? 95  ALA B CB  1 
ATOM   3895 N  N   . LEU B 1 67  ? 8.133   46.948 81.803  1.00 73.31  ? 96  LEU B N   1 
ATOM   3896 C  CA  . LEU B 1 67  ? 8.700   46.844 80.470  1.00 73.82  ? 96  LEU B CA  1 
ATOM   3897 C  C   . LEU B 1 67  ? 9.281   48.195 80.064  1.00 74.30  ? 96  LEU B C   1 
ATOM   3898 O  O   . LEU B 1 67  ? 8.873   49.227 80.598  1.00 74.50  ? 96  LEU B O   1 
ATOM   3899 C  CB  . LEU B 1 67  ? 7.581   46.475 79.483  1.00 74.01  ? 96  LEU B CB  1 
ATOM   3900 C  CG  . LEU B 1 67  ? 6.882   45.152 79.692  1.00 75.25  ? 96  LEU B CG  1 
ATOM   3901 C  CD1 . LEU B 1 67  ? 5.793   44.967 78.655  1.00 75.61  ? 96  LEU B CD1 1 
ATOM   3902 C  CD2 . LEU B 1 67  ? 7.861   44.005 79.618  1.00 75.86  ? 96  LEU B CD2 1 
ATOM   3903 N  N   . PRO B 1 68  ? 10.199  48.230 79.083  1.00 74.30  ? 97  PRO B N   1 
ATOM   3904 C  CA  . PRO B 1 68  ? 10.727  49.526 78.631  1.00 74.51  ? 97  PRO B CA  1 
ATOM   3905 C  C   . PRO B 1 68  ? 9.704   50.390 77.875  1.00 75.12  ? 97  PRO B C   1 
ATOM   3906 O  O   . PRO B 1 68  ? 9.951   51.578 77.669  1.00 75.26  ? 97  PRO B O   1 
ATOM   3907 C  CB  . PRO B 1 68  ? 11.897  49.129 77.737  1.00 75.08  ? 97  PRO B CB  1 
ATOM   3908 C  CG  . PRO B 1 68  ? 11.548  47.777 77.243  1.00 75.40  ? 97  PRO B CG  1 
ATOM   3909 C  CD  . PRO B 1 68  ? 10.800  47.105 78.343  1.00 73.76  ? 97  PRO B CD  1 
ATOM   3910 N  N   . GLU B 1 69  ? 8.557   49.817 77.465  1.00 75.26  ? 98  GLU B N   1 
ATOM   3911 C  CA  . GLU B 1 69  ? 7.547   50.575 76.727  1.00 75.69  ? 98  GLU B CA  1 
ATOM   3912 C  C   . GLU B 1 69  ? 6.131   50.371 77.263  1.00 75.24  ? 98  GLU B C   1 
ATOM   3913 O  O   . GLU B 1 69  ? 5.879   49.422 78.010  1.00 75.37  ? 98  GLU B O   1 
ATOM   3914 C  CB  . GLU B 1 69  ? 7.622   50.256 75.231  1.00 78.77  ? 98  GLU B CB  1 
ATOM   3915 C  CG  . GLU B 1 69  ? 7.332   48.805 74.924  1.00 85.18  ? 98  GLU B CG  1 
ATOM   3916 C  CD  . GLU B 1 69  ? 7.615   48.450 73.480  1.00 93.30  ? 98  GLU B CD  1 
ATOM   3917 O  OE1 . GLU B 1 69  ? 6.647   48.184 72.726  1.00 94.30  ? 98  GLU B OE1 1 
ATOM   3918 O  OE2 . GLU B 1 69  ? 8.811   48.442 73.104  1.00 95.74  ? 98  GLU B OE2 1 
ATOM   3919 N  N   . ALA B 1 70  ? 5.219   51.299 76.917  1.00 74.55  ? 99  ALA B N   1 
ATOM   3920 C  CA  . ALA B 1 70  ? 3.840   51.267 77.393  1.00 74.22  ? 99  ALA B CA  1 
ATOM   3921 C  C   . ALA B 1 70  ? 3.085   50.062 76.891  1.00 73.55  ? 99  ALA B C   1 
ATOM   3922 O  O   . ALA B 1 70  ? 3.351   49.553 75.801  1.00 73.77  ? 99  ALA B O   1 
ATOM   3923 C  CB  . ALA B 1 70  ? 3.111   52.544 77.011  1.00 74.28  ? 99  ALA B CB  1 
ATOM   3924 N  N   . THR B 1 71  ? 2.149   49.606 77.705  1.00 72.48  ? 100 THR B N   1 
ATOM   3925 C  CA  . THR B 1 71  ? 1.308   48.450 77.435  1.00 72.10  ? 100 THR B CA  1 
ATOM   3926 C  C   . THR B 1 71  ? -0.063  48.663 78.091  1.00 71.46  ? 100 THR B C   1 
ATOM   3927 O  O   . THR B 1 71  ? -0.241  49.581 78.886  1.00 71.59  ? 100 THR B O   1 
ATOM   3928 C  CB  . THR B 1 71  ? 1.983   47.179 78.033  1.00 73.38  ? 100 THR B CB  1 
ATOM   3929 O  OG1 . THR B 1 71  ? 1.302   46.019 77.558  1.00 74.16  ? 100 THR B OG1 1 
ATOM   3930 C  CG2 . THR B 1 71  ? 1.947   47.162 79.565  1.00 73.85  ? 100 THR B CG2 1 
ATOM   3931 N  N   . THR B 1 72  ? -1.040  47.840 77.742  1.00 70.71  ? 101 THR B N   1 
ATOM   3932 C  CA  . THR B 1 72  ? -2.338  47.842 78.410  1.00 70.82  ? 101 THR B CA  1 
ATOM   3933 C  C   . THR B 1 72  ? -2.577  46.364 78.875  1.00 70.25  ? 101 THR B C   1 
ATOM   3934 O  O   . THR B 1 72  ? -1.665  45.538 78.742  1.00 70.79  ? 101 THR B O   1 
ATOM   3935 C  CB  . THR B 1 72  ? -3.452  48.483 77.537  1.00 72.67  ? 101 THR B CB  1 
ATOM   3936 O  OG1 . THR B 1 72  ? -4.003  47.496 76.677  1.00 74.45  ? 101 THR B OG1 1 
ATOM   3937 C  CG2 . THR B 1 72  ? -2.988  49.688 76.727  1.00 72.95  ? 101 THR B CG2 1 
ATOM   3938 N  N   . MET B 1 73  ? -3.750  46.032 79.439  1.00 68.88  ? 102 MET B N   1 
ATOM   3939 C  CA  . MET B 1 73  ? -4.030  44.657 79.842  1.00 68.14  ? 102 MET B CA  1 
ATOM   3940 C  C   . MET B 1 73  ? -5.523  44.386 79.782  1.00 67.58  ? 102 MET B C   1 
ATOM   3941 O  O   . MET B 1 73  ? -6.278  44.786 80.664  1.00 67.98  ? 102 MET B O   1 
ATOM   3942 C  CB  . MET B 1 73  ? -3.430  44.326 81.217  1.00 68.51  ? 102 MET B CB  1 
ATOM   3943 C  CG  . MET B 1 73  ? -3.344  42.829 81.504  1.00 70.45  ? 102 MET B CG  1 
ATOM   3944 S  SD  . MET B 1 73  ? -2.311  41.883 80.339  1.00 72.13  ? 102 MET B SD  1 
ATOM   3945 C  CE  . MET B 1 73  ? -0.741  42.664 80.579  1.00 67.44  ? 102 MET B CE  1 
ATOM   3946 N  N   . HIS B 1 74  ? -5.956  43.763 78.706  1.00 66.54  ? 103 HIS B N   1 
ATOM   3947 C  CA  . HIS B 1 74  ? -7.353  43.438 78.492  1.00 66.34  ? 103 HIS B CA  1 
ATOM   3948 C  C   . HIS B 1 74  ? -7.718  42.136 79.201  1.00 66.08  ? 103 HIS B C   1 
ATOM   3949 O  O   . HIS B 1 74  ? -6.917  41.206 79.214  1.00 66.63  ? 103 HIS B O   1 
ATOM   3950 C  CB  . HIS B 1 74  ? -7.619  43.318 76.986  1.00 67.32  ? 103 HIS B CB  1 
ATOM   3951 C  CG  . HIS B 1 74  ? -8.960  42.758 76.645  1.00 70.27  ? 103 HIS B CG  1 
ATOM   3952 N  ND1 . HIS B 1 74  ? -10.112 43.234 77.246  1.00 72.35  ? 103 HIS B ND1 1 
ATOM   3953 C  CD2 . HIS B 1 74  ? -9.289  41.762 75.790  1.00 71.68  ? 103 HIS B CD2 1 
ATOM   3954 C  CE1 . HIS B 1 74  ? -11.104 42.524 76.733  1.00 73.01  ? 103 HIS B CE1 1 
ATOM   3955 N  NE2 . HIS B 1 74  ? -10.659 41.627 75.849  1.00 72.99  ? 103 HIS B NE2 1 
ATOM   3956 N  N   . TRP B 1 75  ? -8.929  42.051 79.762  1.00 65.16  ? 104 TRP B N   1 
ATOM   3957 C  CA  . TRP B 1 75  ? -9.386  40.827 80.422  1.00 64.84  ? 104 TRP B CA  1 
ATOM   3958 C  C   . TRP B 1 75  ? -10.407 40.159 79.502  1.00 64.12  ? 104 TRP B C   1 
ATOM   3959 O  O   . TRP B 1 75  ? -11.616 40.315 79.705  1.00 64.32  ? 104 TRP B O   1 
ATOM   3960 C  CB  . TRP B 1 75  ? -10.015 41.114 81.810  1.00 64.91  ? 104 TRP B CB  1 
ATOM   3961 C  CG  . TRP B 1 75  ? -9.312  42.174 82.603  1.00 65.64  ? 104 TRP B CG  1 
ATOM   3962 C  CD1 . TRP B 1 75  ? -9.766  43.431 82.867  1.00 66.53  ? 104 TRP B CD1 1 
ATOM   3963 C  CD2 . TRP B 1 75  ? -7.987  42.101 83.154  1.00 65.72  ? 104 TRP B CD2 1 
ATOM   3964 N  NE1 . TRP B 1 75  ? -8.822  44.134 83.582  1.00 66.76  ? 104 TRP B NE1 1 
ATOM   3965 C  CE2 . TRP B 1 75  ? -7.721  43.338 83.771  1.00 66.41  ? 104 TRP B CE2 1 
ATOM   3966 C  CE3 . TRP B 1 75  ? -7.019  41.093 83.229  1.00 66.13  ? 104 TRP B CE3 1 
ATOM   3967 C  CZ2 . TRP B 1 75  ? -6.519  43.598 84.423  1.00 66.94  ? 104 TRP B CZ2 1 
ATOM   3968 C  CZ3 . TRP B 1 75  ? -5.820  41.365 83.852  1.00 66.73  ? 104 TRP B CZ3 1 
ATOM   3969 C  CH2 . TRP B 1 75  ? -5.583  42.600 84.445  1.00 66.80  ? 104 TRP B CH2 1 
ATOM   3970 N  N   . HIS B 1 76  ? -9.906  39.449 78.474  1.00 63.04  ? 105 HIS B N   1 
ATOM   3971 C  CA  . HIS B 1 76  ? -10.678 38.756 77.437  1.00 62.80  ? 105 HIS B CA  1 
ATOM   3972 C  C   . HIS B 1 76  ? -11.715 37.792 77.992  1.00 62.57  ? 105 HIS B C   1 
ATOM   3973 O  O   . HIS B 1 76  ? -11.371 36.784 78.603  1.00 62.78  ? 105 HIS B O   1 
ATOM   3974 C  CB  . HIS B 1 76  ? -9.718  38.022 76.478  1.00 63.58  ? 105 HIS B CB  1 
ATOM   3975 C  CG  . HIS B 1 76  ? -10.330 37.531 75.199  1.00 65.34  ? 105 HIS B CG  1 
ATOM   3976 N  ND1 . HIS B 1 76  ? -9.894  37.997 73.971  1.00 66.86  ? 105 HIS B ND1 1 
ATOM   3977 C  CD2 . HIS B 1 76  ? -11.279 36.586 74.993  1.00 66.28  ? 105 HIS B CD2 1 
ATOM   3978 C  CE1 . HIS B 1 76  ? -10.609 37.351 73.067  1.00 67.16  ? 105 HIS B CE1 1 
ATOM   3979 N  NE2 . HIS B 1 76  ? -11.455 36.489 73.633  1.00 67.11  ? 105 HIS B NE2 1 
ATOM   3980 N  N   . GLY B 1 77  ? -12.979 38.100 77.755  1.00 62.22  ? 106 GLY B N   1 
ATOM   3981 C  CA  . GLY B 1 77  ? -14.080 37.265 78.213  1.00 62.46  ? 106 GLY B CA  1 
ATOM   3982 C  C   . GLY B 1 77  ? -14.804 37.770 79.442  1.00 62.44  ? 106 GLY B C   1 
ATOM   3983 O  O   . GLY B 1 77  ? -15.864 37.246 79.784  1.00 62.04  ? 106 GLY B O   1 
ATOM   3984 N  N   . MET B 1 78  ? -14.252 38.785 80.121  1.00 62.94  ? 107 MET B N   1 
ATOM   3985 C  CA  . MET B 1 78  ? -14.885 39.313 81.330  1.00 64.13  ? 107 MET B CA  1 
ATOM   3986 C  C   . MET B 1 78  ? -16.056 40.263 81.061  1.00 65.57  ? 107 MET B C   1 
ATOM   3987 O  O   . MET B 1 78  ? -15.971 41.170 80.222  1.00 65.68  ? 107 MET B O   1 
ATOM   3988 C  CB  . MET B 1 78  ? -13.854 39.967 82.263  1.00 64.32  ? 107 MET B CB  1 
ATOM   3989 C  CG  . MET B 1 78  ? -12.760 39.022 82.701  1.00 65.75  ? 107 MET B CG  1 
ATOM   3990 S  SD  . MET B 1 78  ? -13.351 37.534 83.541  1.00 67.54  ? 107 MET B SD  1 
ATOM   3991 C  CE  . MET B 1 78  ? -13.834 38.204 85.088  1.00 67.33  ? 107 MET B CE  1 
ATOM   3992 N  N   . GLU B 1 79  ? -17.148 40.057 81.799  1.00 66.37  ? 108 GLU B N   1 
ATOM   3993 C  CA  . GLU B 1 79  ? -18.340 40.893 81.715  1.00 67.64  ? 108 GLU B CA  1 
ATOM   3994 C  C   . GLU B 1 79  ? -18.184 41.958 82.794  1.00 69.07  ? 108 GLU B C   1 
ATOM   3995 O  O   . GLU B 1 79  ? -18.678 41.827 83.915  1.00 68.98  ? 108 GLU B O   1 
ATOM   3996 C  CB  . GLU B 1 79  ? -19.611 40.062 81.924  1.00 69.10  ? 108 GLU B CB  1 
ATOM   3997 C  CG  . GLU B 1 79  ? -19.581 38.736 81.199  1.00 72.92  ? 108 GLU B CG  1 
ATOM   3998 C  CD  . GLU B 1 79  ? -20.931 38.239 80.741  1.00 80.40  ? 108 GLU B CD  1 
ATOM   3999 O  OE1 . GLU B 1 79  ? -21.259 37.062 81.021  1.00 80.51  ? 108 GLU B OE1 1 
ATOM   4000 O  OE2 . GLU B 1 79  ? -21.653 39.026 80.086  1.00 84.78  ? 108 GLU B OE2 1 
ATOM   4001 N  N   . ILE B 1 80  ? -17.380 42.957 82.473  1.00 70.15  ? 109 ILE B N   1 
ATOM   4002 C  CA  . ILE B 1 80  ? -17.025 44.040 83.375  1.00 71.67  ? 109 ILE B CA  1 
ATOM   4003 C  C   . ILE B 1 80  ? -17.262 45.389 82.686  1.00 73.26  ? 109 ILE B C   1 
ATOM   4004 O  O   . ILE B 1 80  ? -17.316 45.453 81.458  1.00 73.50  ? 109 ILE B O   1 
ATOM   4005 C  CB  . ILE B 1 80  ? -15.525 43.869 83.750  1.00 71.83  ? 109 ILE B CB  1 
ATOM   4006 C  CG1 . ILE B 1 80  ? -14.636 43.892 82.491  1.00 72.73  ? 109 ILE B CG1 1 
ATOM   4007 C  CG2 . ILE B 1 80  ? -15.307 42.598 84.574  1.00 72.03  ? 109 ILE B CG2 1 
ATOM   4008 C  CD1 . ILE B 1 80  ? -13.178 43.866 82.761  1.00 74.27  ? 109 ILE B CD1 1 
ATOM   4009 N  N   . PRO B 1 81  ? -17.371 46.487 83.452  1.00 74.03  ? 110 PRO B N   1 
ATOM   4010 C  CA  . PRO B 1 81  ? -17.541 47.801 82.816  1.00 74.92  ? 110 PRO B CA  1 
ATOM   4011 C  C   . PRO B 1 81  ? -16.304 48.204 82.009  1.00 76.39  ? 110 PRO B C   1 
ATOM   4012 O  O   . PRO B 1 81  ? -15.189 47.802 82.346  1.00 76.20  ? 110 PRO B O   1 
ATOM   4013 C  CB  . PRO B 1 81  ? -17.754 48.748 84.003  1.00 75.28  ? 110 PRO B CB  1 
ATOM   4014 C  CG  . PRO B 1 81  ? -18.053 47.871 85.167  1.00 75.42  ? 110 PRO B CG  1 
ATOM   4015 C  CD  . PRO B 1 81  ? -17.327 46.601 84.919  1.00 73.64  ? 110 PRO B CD  1 
ATOM   4016 N  N   . GLY B 1 82  ? -16.517 49.007 80.963  1.00 77.46  ? 111 GLY B N   1 
ATOM   4017 C  CA  . GLY B 1 82  ? -15.456 49.497 80.086  1.00 78.73  ? 111 GLY B CA  1 
ATOM   4018 C  C   . GLY B 1 82  ? -14.327 50.204 80.811  1.00 80.08  ? 111 GLY B C   1 
ATOM   4019 O  O   . GLY B 1 82  ? -13.192 50.240 80.328  1.00 80.39  ? 111 GLY B O   1 
ATOM   4020 N  N   . THR B 1 83  ? -14.630 50.758 81.988  1.00 80.77  ? 112 THR B N   1 
ATOM   4021 C  CA  . THR B 1 83  ? -13.659 51.442 82.834  1.00 81.93  ? 112 THR B CA  1 
ATOM   4022 C  C   . THR B 1 83  ? -12.600 50.490 83.419  1.00 82.63  ? 112 THR B C   1 
ATOM   4023 O  O   . THR B 1 83  ? -11.535 50.940 83.824  1.00 82.85  ? 112 THR B O   1 
ATOM   4024 C  CB  . THR B 1 83  ? -14.410 52.211 83.921  1.00 83.61  ? 112 THR B CB  1 
ATOM   4025 O  OG1 . THR B 1 83  ? -15.197 51.291 84.685  1.00 84.94  ? 112 THR B OG1 1 
ATOM   4026 C  CG2 . THR B 1 83  ? -15.315 53.285 83.342  1.00 83.93  ? 112 THR B CG2 1 
ATOM   4027 N  N   . SER B 1 84  ? -12.892 49.184 83.459  1.00 82.93  ? 113 SER B N   1 
ATOM   4028 C  CA  . SER B 1 84  ? -11.997 48.156 83.986  1.00 83.60  ? 113 SER B CA  1 
ATOM   4029 C  C   . SER B 1 84  ? -11.476 47.192 82.909  1.00 84.14  ? 113 SER B C   1 
ATOM   4030 O  O   . SER B 1 84  ? -10.666 46.336 83.232  1.00 84.38  ? 113 SER B O   1 
ATOM   4031 C  CB  . SER B 1 84  ? -12.724 47.331 85.046  1.00 84.85  ? 113 SER B CB  1 
ATOM   4032 O  OG  . SER B 1 84  ? -13.474 48.129 85.949  1.00 87.42  ? 113 SER B OG  1 
ATOM   4033 N  N   . ASP B 1 85  ? -11.962 47.294 81.659  1.00 84.27  ? 114 ASP B N   1 
ATOM   4034 C  CA  . ASP B 1 85  ? -11.624 46.389 80.559  1.00 84.84  ? 114 ASP B CA  1 
ATOM   4035 C  C   . ASP B 1 85  ? -10.150 46.330 80.200  1.00 85.09  ? 114 ASP B C   1 
ATOM   4036 O  O   . ASP B 1 85  ? -9.657  45.264 79.841  1.00 85.01  ? 114 ASP B O   1 
ATOM   4037 C  CB  . ASP B 1 85  ? -12.457 46.723 79.312  1.00 86.61  ? 114 ASP B CB  1 
ATOM   4038 C  CG  . ASP B 1 85  ? -12.758 45.534 78.423  1.00 90.61  ? 114 ASP B CG  1 
ATOM   4039 O  OD1 . ASP B 1 85  ? -12.650 44.387 78.908  1.00 91.31  ? 114 ASP B OD1 1 
ATOM   4040 O  OD2 . ASP B 1 85  ? -13.118 45.751 77.250  1.00 92.45  ? 114 ASP B OD2 1 
ATOM   4041 N  N   . GLY B 1 86  ? -9.470  47.465 80.281  1.00 85.34  ? 115 GLY B N   1 
ATOM   4042 C  CA  . GLY B 1 86  ? -8.053  47.547 79.955  1.00 86.31  ? 115 GLY B CA  1 
ATOM   4043 C  C   . GLY B 1 86  ? -7.760  47.552 78.471  1.00 87.15  ? 115 GLY B C   1 
ATOM   4044 O  O   . GLY B 1 86  ? -6.789  46.943 78.021  1.00 87.42  ? 115 GLY B O   1 
ATOM   4045 N  N   . GLY B 1 87  ? -8.583  48.260 77.711  1.00 87.36  ? 116 GLY B N   1 
ATOM   4046 C  CA  . GLY B 1 87  ? -8.411  48.371 76.268  1.00 87.99  ? 116 GLY B CA  1 
ATOM   4047 C  C   . GLY B 1 87  ? -7.282  49.306 75.878  1.00 88.27  ? 116 GLY B C   1 
ATOM   4048 O  O   . GLY B 1 87  ? -6.430  49.639 76.703  1.00 88.61  ? 116 GLY B O   1 
ATOM   4049 N  N   . PRO B 1 88  ? -7.261  49.775 74.621  1.00 87.93  ? 117 PRO B N   1 
ATOM   4050 C  CA  . PRO B 1 88  ? -6.167  50.662 74.190  1.00 87.71  ? 117 PRO B CA  1 
ATOM   4051 C  C   . PRO B 1 88  ? -6.173  52.048 74.817  1.00 87.66  ? 117 PRO B C   1 
ATOM   4052 O  O   . PRO B 1 88  ? -5.218  52.787 74.613  1.00 87.88  ? 117 PRO B O   1 
ATOM   4053 C  CB  . PRO B 1 88  ? -6.334  50.731 72.675  1.00 88.57  ? 117 PRO B CB  1 
ATOM   4054 C  CG  . PRO B 1 88  ? -7.769  50.423 72.440  1.00 89.16  ? 117 PRO B CG  1 
ATOM   4055 C  CD  . PRO B 1 88  ? -8.191  49.471 73.520  1.00 87.54  ? 117 PRO B CD  1 
ATOM   4056 N  N   . GLN B 1 89  ? -7.225  52.407 75.574  1.00 87.22  ? 118 GLN B N   1 
ATOM   4057 C  CA  . GLN B 1 89  ? -7.288  53.702 76.245  1.00 87.39  ? 118 GLN B CA  1 
ATOM   4058 C  C   . GLN B 1 89  ? -6.649  53.635 77.640  1.00 86.78  ? 118 GLN B C   1 
ATOM   4059 O  O   . GLN B 1 89  ? -6.083  54.628 78.101  1.00 87.57  ? 118 GLN B O   1 
ATOM   4060 C  CB  . GLN B 1 89  ? -8.735  54.190 76.351  1.00 89.63  ? 118 GLN B CB  1 
ATOM   4061 C  CG  . GLN B 1 89  ? -9.435  54.252 75.011  1.00 94.43  ? 118 GLN B CG  1 
ATOM   4062 C  CD  . GLN B 1 89  ? -10.751 53.523 75.048  1.00 100.24 ? 118 GLN B CD  1 
ATOM   4063 O  OE1 . GLN B 1 89  ? -11.819 54.115 74.817  1.00 101.87 ? 118 GLN B OE1 1 
ATOM   4064 N  NE2 . GLN B 1 89  ? -10.702 52.221 75.354  1.00 101.27 ? 118 GLN B NE2 1 
ATOM   4065 N  N   . ALA B 1 90  ? -6.739  52.479 78.318  1.00 85.08  ? 119 ALA B N   1 
ATOM   4066 C  CA  . ALA B 1 90  ? -6.153  52.308 79.645  1.00 83.76  ? 119 ALA B CA  1 
ATOM   4067 C  C   . ALA B 1 90  ? -4.658  52.008 79.500  1.00 82.14  ? 119 ALA B C   1 
ATOM   4068 O  O   . ALA B 1 90  ? -4.222  50.874 79.690  1.00 82.52  ? 119 ALA B O   1 
ATOM   4069 C  CB  . ALA B 1 90  ? -6.856  51.171 80.375  1.00 83.96  ? 119 ALA B CB  1 
ATOM   4070 N  N   . VAL B 1 91  ? -3.875  53.023 79.147  1.00 80.46  ? 120 VAL B N   1 
ATOM   4071 C  CA  . VAL B 1 91  ? -2.445  52.854 78.932  1.00 79.53  ? 120 VAL B CA  1 
ATOM   4072 C  C   . VAL B 1 91  ? -1.641  52.902 80.213  1.00 79.16  ? 120 VAL B C   1 
ATOM   4073 O  O   . VAL B 1 91  ? -1.687  53.887 80.952  1.00 79.50  ? 120 VAL B O   1 
ATOM   4074 C  CB  . VAL B 1 91  ? -1.900  53.847 77.894  1.00 79.65  ? 120 VAL B CB  1 
ATOM   4075 C  CG1 . VAL B 1 91  ? -0.427  53.595 77.618  1.00 79.92  ? 120 VAL B CG1 1 
ATOM   4076 C  CG2 . VAL B 1 91  ? -2.703  53.774 76.613  1.00 80.14  ? 120 VAL B CG2 1 
ATOM   4077 N  N   . ILE B 1 92  ? -0.891  51.831 80.467  1.00 78.38  ? 121 ILE B N   1 
ATOM   4078 C  CA  . ILE B 1 92  ? -0.010  51.709 81.619  1.00 78.23  ? 121 ILE B CA  1 
ATOM   4079 C  C   . ILE B 1 92  ? 1.371   52.083 81.132  1.00 78.23  ? 121 ILE B C   1 
ATOM   4080 O  O   . ILE B 1 92  ? 1.975   51.308 80.398  1.00 78.51  ? 121 ILE B O   1 
ATOM   4081 C  CB  . ILE B 1 92  ? 0.009   50.266 82.185  1.00 78.62  ? 121 ILE B CB  1 
ATOM   4082 C  CG1 . ILE B 1 92  ? -1.396  49.626 82.237  1.00 79.39  ? 121 ILE B CG1 1 
ATOM   4083 C  CG2 . ILE B 1 92  ? 0.688   50.237 83.545  1.00 78.99  ? 121 ILE B CG2 1 
ATOM   4084 C  CD1 . ILE B 1 92  ? -1.399  48.169 82.596  1.00 80.49  ? 121 ILE B CD1 1 
ATOM   4085 N  N   . GLU B 1 93  ? 1.862   53.270 81.489  1.00 77.90  ? 122 GLU B N   1 
ATOM   4086 C  CA  . GLU B 1 93  ? 3.192   53.703 81.062  1.00 78.13  ? 122 GLU B CA  1 
ATOM   4087 C  C   . GLU B 1 93  ? 4.295   52.924 81.799  1.00 78.11  ? 122 GLU B C   1 
ATOM   4088 O  O   . GLU B 1 93  ? 4.045   52.415 82.889  1.00 78.16  ? 122 GLU B O   1 
ATOM   4089 C  CB  . GLU B 1 93  ? 3.340   55.217 81.283  1.00 80.17  ? 122 GLU B CB  1 
ATOM   4090 C  CG  . GLU B 1 93  ? 2.396   56.043 80.434  1.00 84.06  ? 122 GLU B CG  1 
ATOM   4091 C  CD  . GLU B 1 93  ? 2.704   56.060 78.949  1.00 90.07  ? 122 GLU B CD  1 
ATOM   4092 O  OE1 . GLU B 1 93  ? 1.770   56.310 78.155  1.00 91.26  ? 122 GLU B OE1 1 
ATOM   4093 O  OE2 . GLU B 1 93  ? 3.877   55.834 78.574  1.00 92.26  ? 122 GLU B OE2 1 
ATOM   4094 N  N   . PRO B 1 94  ? 5.509   52.782 81.225  1.00 78.06  ? 123 PRO B N   1 
ATOM   4095 C  CA  . PRO B 1 94  ? 6.570   52.031 81.925  1.00 78.39  ? 123 PRO B CA  1 
ATOM   4096 C  C   . PRO B 1 94  ? 6.857   52.586 83.313  1.00 79.25  ? 123 PRO B C   1 
ATOM   4097 O  O   . PRO B 1 94  ? 6.871   53.804 83.502  1.00 80.04  ? 123 PRO B O   1 
ATOM   4098 C  CB  . PRO B 1 94  ? 7.789   52.196 81.016  1.00 78.94  ? 123 PRO B CB  1 
ATOM   4099 C  CG  . PRO B 1 94  ? 7.248   52.527 79.693  1.00 79.24  ? 123 PRO B CG  1 
ATOM   4100 C  CD  . PRO B 1 94  ? 5.980   53.295 79.927  1.00 77.61  ? 123 PRO B CD  1 
ATOM   4101 N  N   . GLY B 1 95  ? 7.015   51.692 84.279  1.00 78.82  ? 124 GLY B N   1 
ATOM   4102 C  CA  . GLY B 1 95  ? 7.245   52.063 85.669  1.00 78.77  ? 124 GLY B CA  1 
ATOM   4103 C  C   . GLY B 1 95  ? 5.995   52.439 86.445  1.00 78.41  ? 124 GLY B C   1 
ATOM   4104 O  O   . GLY B 1 95  ? 6.072   52.702 87.646  1.00 78.66  ? 124 GLY B O   1 
ATOM   4105 N  N   . LYS B 1 96  ? 4.834   52.469 85.787  1.00 77.97  ? 125 LYS B N   1 
ATOM   4106 C  CA  . LYS B 1 96  ? 3.582   52.843 86.442  1.00 78.04  ? 125 LYS B CA  1 
ATOM   4107 C  C   . LYS B 1 96  ? 2.684   51.634 86.734  1.00 77.28  ? 125 LYS B C   1 
ATOM   4108 O  O   . LYS B 1 96  ? 2.932   50.539 86.235  1.00 77.09  ? 125 LYS B O   1 
ATOM   4109 C  CB  . LYS B 1 96  ? 2.842   53.895 85.600  1.00 80.65  ? 125 LYS B CB  1 
ATOM   4110 C  CG  . LYS B 1 96  ? 3.675   55.140 85.344  1.00 86.03  ? 125 LYS B CG  1 
ATOM   4111 C  CD  . LYS B 1 96  ? 3.683   56.053 86.553  1.00 91.13  ? 125 LYS B CD  1 
ATOM   4112 C  CE  . LYS B 1 96  ? 4.424   57.336 86.277  1.00 94.93  ? 125 LYS B CE  1 
ATOM   4113 N  NZ  . LYS B 1 96  ? 4.131   58.357 87.319  1.00 97.48  ? 125 LYS B NZ  1 
ATOM   4114 N  N   . MET B 1 97  ? 1.648   51.830 87.553  1.00 76.79  ? 126 MET B N   1 
ATOM   4115 C  CA  . MET B 1 97  ? 0.735   50.758 87.909  1.00 76.84  ? 126 MET B CA  1 
ATOM   4116 C  C   . MET B 1 97  ? -0.716  51.180 87.748  1.00 76.51  ? 126 MET B C   1 
ATOM   4117 O  O   . MET B 1 97  ? -1.137  52.196 88.291  1.00 76.47  ? 126 MET B O   1 
ATOM   4118 C  CB  . MET B 1 97  ? 1.012   50.270 89.346  1.00 77.68  ? 126 MET B CB  1 
ATOM   4119 C  CG  . MET B 1 97  ? 0.209   49.055 89.748  1.00 79.54  ? 126 MET B CG  1 
ATOM   4120 S  SD  . MET B 1 97  ? -1.288  49.477 90.660  1.00 84.48  ? 126 MET B SD  1 
ATOM   4121 C  CE  . MET B 1 97  ? -0.604  49.820 92.231  1.00 82.26  ? 126 MET B CE  1 
ATOM   4122 N  N   . TRP B 1 98  ? -1.486  50.378 87.024  1.00 76.40  ? 127 TRP B N   1 
ATOM   4123 C  CA  . TRP B 1 98  ? -2.909  50.614 86.812  1.00 76.75  ? 127 TRP B CA  1 
ATOM   4124 C  C   . TRP B 1 98  ? -3.690  49.562 87.572  1.00 76.00  ? 127 TRP B C   1 
ATOM   4125 O  O   . TRP B 1 98  ? -3.329  48.388 87.554  1.00 75.72  ? 127 TRP B O   1 
ATOM   4126 C  CB  . TRP B 1 98  ? -3.253  50.567 85.305  1.00 77.23  ? 127 TRP B CB  1 
ATOM   4127 C  CG  . TRP B 1 98  ? -4.713  50.405 84.970  1.00 78.19  ? 127 TRP B CG  1 
ATOM   4128 C  CD1 . TRP B 1 98  ? -5.698  51.339 85.110  1.00 79.16  ? 127 TRP B CD1 1 
ATOM   4129 C  CD2 . TRP B 1 98  ? -5.335  49.248 84.385  1.00 78.42  ? 127 TRP B CD2 1 
ATOM   4130 N  NE1 . TRP B 1 98  ? -6.902  50.827 84.675  1.00 79.46  ? 127 TRP B NE1 1 
ATOM   4131 C  CE2 . TRP B 1 98  ? -6.706  49.545 84.223  1.00 79.26  ? 127 TRP B CE2 1 
ATOM   4132 C  CE3 . TRP B 1 98  ? -4.866  47.989 83.983  1.00 78.82  ? 127 TRP B CE3 1 
ATOM   4133 C  CZ2 . TRP B 1 98  ? -7.608  48.627 83.686  1.00 79.85  ? 127 TRP B CZ2 1 
ATOM   4134 C  CZ3 . TRP B 1 98  ? -5.761  47.086 83.444  1.00 79.60  ? 127 TRP B CZ3 1 
ATOM   4135 C  CH2 . TRP B 1 98  ? -7.113  47.405 83.306  1.00 79.82  ? 127 TRP B CH2 1 
ATOM   4136 N  N   . THR B 1 99  ? -4.769  49.977 88.217  1.00 75.56  ? 128 THR B N   1 
ATOM   4137 C  CA  . THR B 1 99  ? -5.614  49.060 88.958  1.00 75.76  ? 128 THR B CA  1 
ATOM   4138 C  C   . THR B 1 99  ? -6.931  48.843 88.236  1.00 75.83  ? 128 THR B C   1 
ATOM   4139 O  O   . THR B 1 99  ? -7.533  49.801 87.756  1.00 76.14  ? 128 THR B O   1 
ATOM   4140 C  CB  . THR B 1 99  ? -5.833  49.592 90.357  1.00 77.01  ? 128 THR B CB  1 
ATOM   4141 O  OG1 . THR B 1 99  ? -4.559  49.707 90.991  1.00 78.20  ? 128 THR B OG1 1 
ATOM   4142 C  CG2 . THR B 1 99  ? -6.773  48.716 91.170  1.00 77.25  ? 128 THR B CG2 1 
ATOM   4143 N  N   . ALA B 1 100 ? -7.378  47.588 88.150  1.00 75.36  ? 129 ALA B N   1 
ATOM   4144 C  CA  . ALA B 1 100 ? -8.642  47.258 87.512  1.00 75.35  ? 129 ALA B CA  1 
ATOM   4145 C  C   . ALA B 1 100 ? -9.570  46.653 88.548  1.00 75.52  ? 129 ALA B C   1 
ATOM   4146 O  O   . ALA B 1 100 ? -9.302  45.553 89.034  1.00 75.66  ? 129 ALA B O   1 
ATOM   4147 C  CB  . ALA B 1 100 ? -8.413  46.260 86.391  1.00 75.32  ? 129 ALA B CB  1 
ATOM   4148 N  N   . GLU B 1 101 ? -10.651 47.363 88.905  1.00 75.35  ? 130 GLU B N   1 
ATOM   4149 C  CA  . GLU B 1 101 ? -11.611 46.825 89.865  1.00 75.53  ? 130 GLU B CA  1 
ATOM   4150 C  C   . GLU B 1 101 ? -12.587 45.935 89.114  1.00 75.21  ? 130 GLU B C   1 
ATOM   4151 O  O   . GLU B 1 101 ? -13.222 46.369 88.158  1.00 75.17  ? 130 GLU B O   1 
ATOM   4152 C  CB  . GLU B 1 101 ? -12.339 47.936 90.638  1.00 78.21  ? 130 GLU B CB  1 
ATOM   4153 C  CG  . GLU B 1 101 ? -12.141 47.860 92.147  1.00 84.01  ? 130 GLU B CG  1 
ATOM   4154 C  CD  . GLU B 1 101 ? -12.802 46.691 92.863  1.00 91.08  ? 130 GLU B CD  1 
ATOM   4155 O  OE1 . GLU B 1 101 ? -12.268 46.268 93.915  1.00 91.98  ? 130 GLU B OE1 1 
ATOM   4156 O  OE2 . GLU B 1 101 ? -13.851 46.202 92.381  1.00 93.32  ? 130 GLU B OE2 1 
ATOM   4157 N  N   . ILE B 1 102 ? -12.661 44.669 89.509  1.00 74.88  ? 131 ILE B N   1 
ATOM   4158 C  CA  . ILE B 1 102 ? -13.514 43.692 88.851  1.00 74.98  ? 131 ILE B CA  1 
ATOM   4159 C  C   . ILE B 1 102 ? -14.434 42.986 89.839  1.00 75.00  ? 131 ILE B C   1 
ATOM   4160 O  O   . ILE B 1 102 ? -13.971 42.433 90.839  1.00 75.21  ? 131 ILE B O   1 
ATOM   4161 C  CB  . ILE B 1 102 ? -12.617 42.668 88.106  1.00 75.55  ? 131 ILE B CB  1 
ATOM   4162 C  CG1 . ILE B 1 102 ? -11.804 43.350 86.994  1.00 76.29  ? 131 ILE B CG1 1 
ATOM   4163 C  CG2 . ILE B 1 102 ? -13.432 41.460 87.591  1.00 76.21  ? 131 ILE B CG2 1 
ATOM   4164 C  CD1 . ILE B 1 102 ? -10.886 42.478 86.262  1.00 77.69  ? 131 ILE B CD1 1 
ATOM   4165 N  N   . LYS B 1 103 ? -15.731 42.981 89.548  1.00 74.73  ? 132 LYS B N   1 
ATOM   4166 C  CA  . LYS B 1 103 ? -16.688 42.257 90.367  1.00 75.16  ? 132 LYS B CA  1 
ATOM   4167 C  C   . LYS B 1 103 ? -17.190 41.135 89.490  1.00 74.75  ? 132 LYS B C   1 
ATOM   4168 O  O   . LYS B 1 103 ? -17.900 41.402 88.527  1.00 75.11  ? 132 LYS B O   1 
ATOM   4169 C  CB  . LYS B 1 103 ? -17.848 43.160 90.809  1.00 77.93  ? 132 LYS B CB  1 
ATOM   4170 C  CG  . LYS B 1 103 ? -18.890 42.407 91.637  1.00 83.54  ? 132 LYS B CG  1 
ATOM   4171 C  CD  . LYS B 1 103 ? -19.766 43.342 92.466  1.00 89.31  ? 132 LYS B CD  1 
ATOM   4172 C  CE  . LYS B 1 103 ? -20.690 42.592 93.401  1.00 93.79  ? 132 LYS B CE  1 
ATOM   4173 N  NZ  . LYS B 1 103 ? -19.964 42.022 94.568  1.00 96.16  ? 132 LYS B NZ  1 
ATOM   4174 N  N   . VAL B 1 104 ? -16.772 39.898 89.766  1.00 74.03  ? 133 VAL B N   1 
ATOM   4175 C  CA  . VAL B 1 104 ? -17.148 38.735 88.956  1.00 73.84  ? 133 VAL B CA  1 
ATOM   4176 C  C   . VAL B 1 104 ? -18.664 38.551 88.952  1.00 73.82  ? 133 VAL B C   1 
ATOM   4177 O  O   . VAL B 1 104 ? -19.267 38.467 90.014  1.00 73.98  ? 133 VAL B O   1 
ATOM   4178 C  CB  . VAL B 1 104 ? -16.418 37.445 89.405  1.00 74.33  ? 133 VAL B CB  1 
ATOM   4179 C  CG1 . VAL B 1 104 ? -16.624 36.337 88.393  1.00 74.91  ? 133 VAL B CG1 1 
ATOM   4180 C  CG2 . VAL B 1 104 ? -14.930 37.694 89.625  1.00 74.67  ? 133 VAL B CG2 1 
ATOM   4181 N  N   . ASP B 1 105 ? -19.289 38.549 87.771  1.00 73.57  ? 134 ASP B N   1 
ATOM   4182 C  CA  . ASP B 1 105 ? -20.742 38.423 87.666  1.00 73.65  ? 134 ASP B CA  1 
ATOM   4183 C  C   . ASP B 1 105 ? -21.093 37.647 86.397  1.00 72.80  ? 134 ASP B C   1 
ATOM   4184 O  O   . ASP B 1 105 ? -21.874 38.110 85.565  1.00 73.39  ? 134 ASP B O   1 
ATOM   4185 C  CB  . ASP B 1 105 ? -21.377 39.824 87.648  1.00 76.40  ? 134 ASP B CB  1 
ATOM   4186 C  CG  . ASP B 1 105 ? -22.884 39.838 87.814  1.00 82.89  ? 134 ASP B CG  1 
ATOM   4187 O  OD1 . ASP B 1 105 ? -23.444 38.806 88.260  1.00 84.25  ? 134 ASP B OD1 1 
ATOM   4188 O  OD2 . ASP B 1 105 ? -23.507 40.877 87.487  1.00 85.43  ? 134 ASP B OD2 1 
ATOM   4189 N  N   . GLN B 1 106 ? -20.490 36.467 86.242  1.00 71.27  ? 135 GLN B N   1 
ATOM   4190 C  CA  . GLN B 1 106 ? -20.678 35.614 85.072  1.00 70.11  ? 135 GLN B CA  1 
ATOM   4191 C  C   . GLN B 1 106 ? -20.402 34.145 85.425  1.00 69.82  ? 135 GLN B C   1 
ATOM   4192 O  O   . GLN B 1 106 ? -19.753 33.874 86.437  1.00 70.00  ? 135 GLN B O   1 
ATOM   4193 C  CB  . GLN B 1 106 ? -19.752 36.088 83.945  1.00 70.15  ? 135 GLN B CB  1 
ATOM   4194 C  CG  . GLN B 1 106 ? -18.287 35.943 84.264  1.00 71.19  ? 135 GLN B CG  1 
ATOM   4195 C  CD  . GLN B 1 106 ? -17.454 36.618 83.217  1.00 72.70  ? 135 GLN B CD  1 
ATOM   4196 O  OE1 . GLN B 1 106 ? -16.913 37.709 83.436  1.00 73.85  ? 135 GLN B OE1 1 
ATOM   4197 N  NE2 . GLN B 1 106 ? -17.348 35.996 82.051  1.00 71.53  ? 135 GLN B NE2 1 
ATOM   4198 N  N   . PRO B 1 107 ? -20.874 33.169 84.617  1.00 69.28  ? 136 PRO B N   1 
ATOM   4199 C  CA  . PRO B 1 107 ? -20.627 31.760 84.957  1.00 68.65  ? 136 PRO B CA  1 
ATOM   4200 C  C   . PRO B 1 107 ? -19.148 31.368 84.980  1.00 67.92  ? 136 PRO B C   1 
ATOM   4201 O  O   . PRO B 1 107 ? -18.286 32.122 84.523  1.00 67.73  ? 136 PRO B O   1 
ATOM   4202 C  CB  . PRO B 1 107 ? -21.420 30.989 83.894  1.00 69.37  ? 136 PRO B CB  1 
ATOM   4203 C  CG  . PRO B 1 107 ? -22.392 31.966 83.351  1.00 70.07  ? 136 PRO B CG  1 
ATOM   4204 C  CD  . PRO B 1 107 ? -21.689 33.282 83.394  1.00 68.82  ? 136 PRO B CD  1 
ATOM   4205 N  N   . ALA B 1 108 ? -18.863 30.191 85.555  1.00 67.12  ? 137 ALA B N   1 
ATOM   4206 C  CA  . ALA B 1 108 ? -17.515 29.645 85.700  1.00 66.67  ? 137 ALA B CA  1 
ATOM   4207 C  C   . ALA B 1 108 ? -16.947 29.337 84.343  1.00 65.72  ? 137 ALA B C   1 
ATOM   4208 O  O   . ALA B 1 108 ? -17.624 28.714 83.532  1.00 65.28  ? 137 ALA B O   1 
ATOM   4209 C  CB  . ALA B 1 108 ? -17.556 28.380 86.539  1.00 66.89  ? 137 ALA B CB  1 
ATOM   4210 N  N   . THR B 1 109 ? -15.721 29.815 84.068  1.00 65.23  ? 138 THR B N   1 
ATOM   4211 C  CA  . THR B 1 109 ? -15.091 29.650 82.762  1.00 65.10  ? 138 THR B CA  1 
ATOM   4212 C  C   . THR B 1 109 ? -13.542 29.727 82.827  1.00 64.70  ? 138 THR B C   1 
ATOM   4213 O  O   . THR B 1 109 ? -12.973 29.952 83.900  1.00 64.84  ? 138 THR B O   1 
ATOM   4214 C  CB  . THR B 1 109 ? -15.553 30.812 81.865  1.00 66.68  ? 138 THR B CB  1 
ATOM   4215 O  OG1 . THR B 1 109 ? -16.957 30.936 81.901  1.00 68.89  ? 138 THR B OG1 1 
ATOM   4216 C  CG2 . THR B 1 109 ? -15.099 30.631 80.469  1.00 66.90  ? 138 THR B CG2 1 
ATOM   4217 N  N   . THR B 1 110 ? -12.865 29.505 81.669  1.00 63.68  ? 139 THR B N   1 
ATOM   4218 C  CA  . THR B 1 110 ? -11.468 29.748 81.475  1.00 63.10  ? 139 THR B CA  1 
ATOM   4219 C  C   . THR B 1 110 ? -11.458 30.998 80.588  1.00 62.73  ? 139 THR B C   1 
ATOM   4220 O  O   . THR B 1 110 ? -11.585 30.887 79.373  1.00 63.52  ? 139 THR B O   1 
ATOM   4221 C  CB  . THR B 1 110 ? -10.771 28.613 80.723  1.00 63.48  ? 139 THR B CB  1 
ATOM   4222 O  OG1 . THR B 1 110 ? -11.227 27.352 81.186  1.00 64.22  ? 139 THR B OG1 1 
ATOM   4223 C  CG2 . THR B 1 110 ? -9.262  28.705 80.831  1.00 63.39  ? 139 THR B CG2 1 
ATOM   4224 N  N   . ALA B 1 111 ? -11.412 32.177 81.187  1.00 61.33  ? 140 ALA B N   1 
ATOM   4225 C  CA  . ALA B 1 111 ? -11.269 33.420 80.441  1.00 60.85  ? 140 ALA B CA  1 
ATOM   4226 C  C   . ALA B 1 111 ? -9.732  33.687 80.377  1.00 60.65  ? 140 ALA B C   1 
ATOM   4227 O  O   . ALA B 1 111 ? -8.960  32.900 80.943  1.00 60.59  ? 140 ALA B O   1 
ATOM   4228 C  CB  . ALA B 1 111 ? -12.002 34.542 81.173  1.00 60.89  ? 140 ALA B CB  1 
ATOM   4229 N  N   . TRP B 1 112 ? -9.268  34.739 79.678  1.00 60.57  ? 141 TRP B N   1 
ATOM   4230 C  CA  . TRP B 1 112 ? -7.829  35.010 79.631  1.00 60.97  ? 141 TRP B CA  1 
ATOM   4231 C  C   . TRP B 1 112 ? -7.505  36.492 79.601  1.00 61.01  ? 141 TRP B C   1 
ATOM   4232 O  O   . TRP B 1 112 ? -8.406  37.320 79.544  1.00 60.73  ? 141 TRP B O   1 
ATOM   4233 C  CB  . TRP B 1 112 ? -7.159  34.237 78.486  1.00 61.08  ? 141 TRP B CB  1 
ATOM   4234 C  CG  . TRP B 1 112 ? -7.424  34.732 77.099  1.00 61.51  ? 141 TRP B CG  1 
ATOM   4235 C  CD1 . TRP B 1 112 ? -8.618  34.734 76.447  1.00 62.39  ? 141 TRP B CD1 1 
ATOM   4236 C  CD2 . TRP B 1 112 ? -6.431  35.054 76.117  1.00 61.59  ? 141 TRP B CD2 1 
ATOM   4237 N  NE1 . TRP B 1 112 ? -8.441  35.117 75.139  1.00 62.69  ? 141 TRP B NE1 1 
ATOM   4238 C  CE2 . TRP B 1 112 ? -7.105  35.316 74.911  1.00 62.31  ? 141 TRP B CE2 1 
ATOM   4239 C  CE3 . TRP B 1 112 ? -5.038  35.178 76.150  1.00 62.06  ? 141 TRP B CE3 1 
ATOM   4240 C  CZ2 . TRP B 1 112 ? -6.436  35.719 73.762  1.00 62.69  ? 141 TRP B CZ2 1 
ATOM   4241 C  CZ3 . TRP B 1 112 ? -4.379  35.575 75.006  1.00 62.52  ? 141 TRP B CZ3 1 
ATOM   4242 C  CH2 . TRP B 1 112 ? -5.076  35.850 73.835  1.00 62.53  ? 141 TRP B CH2 1 
ATOM   4243 N  N   . PHE B 1 113 ? -6.229  36.830 79.728  1.00 61.41  ? 142 PHE B N   1 
ATOM   4244 C  CA  . PHE B 1 113 ? -5.815  38.218 79.695  1.00 62.39  ? 142 PHE B CA  1 
ATOM   4245 C  C   . PHE B 1 113 ? -4.590  38.407 78.850  1.00 62.68  ? 142 PHE B C   1 
ATOM   4246 O  O   . PHE B 1 113 ? -3.727  37.536 78.791  1.00 62.60  ? 142 PHE B O   1 
ATOM   4247 C  CB  . PHE B 1 113 ? -5.662  38.811 81.100  1.00 62.80  ? 142 PHE B CB  1 
ATOM   4248 C  CG  . PHE B 1 113 ? -4.577  38.248 81.983  1.00 63.96  ? 142 PHE B CG  1 
ATOM   4249 C  CD1 . PHE B 1 113 ? -3.301  38.790 81.973  1.00 65.11  ? 142 PHE B CD1 1 
ATOM   4250 C  CD2 . PHE B 1 113 ? -4.853  37.242 82.890  1.00 65.00  ? 142 PHE B CD2 1 
ATOM   4251 C  CE1 . PHE B 1 113 ? -2.311  38.298 82.812  1.00 65.93  ? 142 PHE B CE1 1 
ATOM   4252 C  CE2 . PHE B 1 113 ? -3.868  36.768 83.743  1.00 65.98  ? 142 PHE B CE2 1 
ATOM   4253 C  CZ  . PHE B 1 113 ? -2.603  37.298 83.698  1.00 65.91  ? 142 PHE B CZ  1 
ATOM   4254 N  N   . HIS B 1 114 ? -4.529  39.534 78.171  1.00 62.84  ? 143 HIS B N   1 
ATOM   4255 C  CA  . HIS B 1 114 ? -3.421  39.866 77.283  1.00 63.42  ? 143 HIS B CA  1 
ATOM   4256 C  C   . HIS B 1 114 ? -3.462  41.364 77.000  1.00 63.55  ? 143 HIS B C   1 
ATOM   4257 O  O   . HIS B 1 114 ? -4.525  41.977 77.100  1.00 63.36  ? 143 HIS B O   1 
ATOM   4258 C  CB  . HIS B 1 114 ? -3.537  39.077 75.968  1.00 64.12  ? 143 HIS B CB  1 
ATOM   4259 C  CG  . HIS B 1 114 ? -4.808  39.336 75.217  1.00 66.83  ? 143 HIS B CG  1 
ATOM   4260 N  ND1 . HIS B 1 114 ? -4.844  40.206 74.145  1.00 68.74  ? 143 HIS B ND1 1 
ATOM   4261 C  CD2 . HIS B 1 114 ? -6.046  38.814 75.402  1.00 68.10  ? 143 HIS B CD2 1 
ATOM   4262 C  CE1 . HIS B 1 114 ? -6.094  40.180 73.708  1.00 69.46  ? 143 HIS B CE1 1 
ATOM   4263 N  NE2 . HIS B 1 114 ? -6.853  39.357 74.436  1.00 69.28  ? 143 HIS B NE2 1 
ATOM   4264 N  N   . PRO B 1 115 ? -2.325  41.979 76.619  1.00 63.63  ? 144 PRO B N   1 
ATOM   4265 C  CA  . PRO B 1 115 ? -2.353  43.414 76.295  1.00 63.78  ? 144 PRO B CA  1 
ATOM   4266 C  C   . PRO B 1 115 ? -3.292  43.738 75.131  1.00 64.56  ? 144 PRO B C   1 
ATOM   4267 O  O   . PRO B 1 115 ? -3.623  42.872 74.317  1.00 64.63  ? 144 PRO B O   1 
ATOM   4268 C  CB  . PRO B 1 115 ? -0.894  43.727 75.942  1.00 64.16  ? 144 PRO B CB  1 
ATOM   4269 C  CG  . PRO B 1 115 ? -0.289  42.420 75.594  1.00 64.54  ? 144 PRO B CG  1 
ATOM   4270 C  CD  . PRO B 1 115 ? -0.975  41.409 76.446  1.00 62.92  ? 144 PRO B CD  1 
ATOM   4271 N  N   . HIS B 1 116 ? -3.759  44.985 75.084  1.00 64.95  ? 145 HIS B N   1 
ATOM   4272 C  CA  . HIS B 1 116 ? -4.630  45.482 74.010  1.00 65.82  ? 145 HIS B CA  1 
ATOM   4273 C  C   . HIS B 1 116 ? -4.121  46.845 73.479  1.00 66.41  ? 145 HIS B C   1 
ATOM   4274 O  O   . HIS B 1 116 ? -4.914  47.665 73.017  1.00 66.27  ? 145 HIS B O   1 
ATOM   4275 C  CB  . HIS B 1 116 ? -6.061  45.638 74.519  1.00 66.97  ? 145 HIS B CB  1 
ATOM   4276 C  CG  . HIS B 1 116 ? -7.081  45.341 73.480  1.00 70.09  ? 145 HIS B CG  1 
ATOM   4277 N  ND1 . HIS B 1 116 ? -7.117  46.042 72.289  1.00 72.35  ? 145 HIS B ND1 1 
ATOM   4278 C  CD2 . HIS B 1 116 ? -8.066  44.416 73.478  1.00 71.68  ? 145 HIS B CD2 1 
ATOM   4279 C  CE1 . HIS B 1 116 ? -8.121  45.525 71.600  1.00 73.13  ? 145 HIS B CE1 1 
ATOM   4280 N  NE2 . HIS B 1 116 ? -8.725  44.543 72.276  1.00 73.11  ? 145 HIS B NE2 1 
ATOM   4281 N  N   . THR B 1 117 ? -2.799  47.071 73.563  1.00 66.75  ? 146 THR B N   1 
ATOM   4282 C  CA  . THR B 1 117 ? -2.089  48.278 73.167  1.00 67.59  ? 146 THR B CA  1 
ATOM   4283 C  C   . THR B 1 117 ? -2.459  48.688 71.749  1.00 68.59  ? 146 THR B C   1 
ATOM   4284 O  O   . THR B 1 117 ? -2.448  47.853 70.847  1.00 68.79  ? 146 THR B O   1 
ATOM   4285 C  CB  . THR B 1 117 ? -0.574  48.050 73.280  1.00 68.70  ? 146 THR B CB  1 
ATOM   4286 O  OG1 . THR B 1 117 ? -0.281  47.319 74.467  1.00 69.65  ? 146 THR B OG1 1 
ATOM   4287 C  CG2 . THR B 1 117 ? 0.218   49.350 73.260  1.00 69.05  ? 146 THR B CG2 1 
ATOM   4288 N  N   . HIS B 1 118 ? -2.787  49.973 71.556  1.00 69.01  ? 147 HIS B N   1 
ATOM   4289 C  CA  . HIS B 1 118 ? -3.167  50.526 70.261  1.00 69.85  ? 147 HIS B CA  1 
ATOM   4290 C  C   . HIS B 1 118 ? -2.143  50.235 69.177  1.00 69.50  ? 147 HIS B C   1 
ATOM   4291 O  O   . HIS B 1 118 ? -0.988  50.651 69.293  1.00 69.94  ? 147 HIS B O   1 
ATOM   4292 C  CB  . HIS B 1 118 ? -3.410  52.039 70.360  1.00 71.91  ? 147 HIS B CB  1 
ATOM   4293 C  CG  . HIS B 1 118 ? -3.940  52.609 69.083  1.00 76.45  ? 147 HIS B CG  1 
ATOM   4294 N  ND1 . HIS B 1 118 ? -5.292  52.545 68.771  1.00 78.94  ? 147 HIS B ND1 1 
ATOM   4295 C  CD2 . HIS B 1 118 ? -3.274  53.159 68.038  1.00 78.01  ? 147 HIS B CD2 1 
ATOM   4296 C  CE1 . HIS B 1 118 ? -5.406  53.086 67.567  1.00 79.61  ? 147 HIS B CE1 1 
ATOM   4297 N  NE2 . HIS B 1 118 ? -4.218  53.463 67.082  1.00 79.45  ? 147 HIS B NE2 1 
ATOM   4298 N  N   . GLY B 1 119 ? -2.573  49.501 68.153  1.00 68.66  ? 148 GLY B N   1 
ATOM   4299 C  CA  . GLY B 1 119 ? -1.732  49.117 67.022  1.00 68.17  ? 148 GLY B CA  1 
ATOM   4300 C  C   . GLY B 1 119 ? -0.498  48.309 67.382  1.00 67.25  ? 148 GLY B C   1 
ATOM   4301 O  O   . GLY B 1 119 ? 0.413   48.177 66.564  1.00 67.32  ? 148 GLY B O   1 
ATOM   4302 N  N   . LEU B 1 120 ? -0.443  47.772 68.605  1.00 66.29  ? 149 LEU B N   1 
ATOM   4303 C  CA  . LEU B 1 120 ? 0.711   47.000 69.030  1.00 66.12  ? 149 LEU B CA  1 
ATOM   4304 C  C   . LEU B 1 120 ? 0.380   45.678 69.714  1.00 65.63  ? 149 LEU B C   1 
ATOM   4305 O  O   . LEU B 1 120 ? 1.311   44.950 70.054  1.00 65.67  ? 149 LEU B O   1 
ATOM   4306 C  CB  . LEU B 1 120 ? 1.627   47.856 69.909  1.00 66.38  ? 149 LEU B CB  1 
ATOM   4307 C  CG  . LEU B 1 120 ? 2.465   48.885 69.154  1.00 67.55  ? 149 LEU B CG  1 
ATOM   4308 C  CD1 . LEU B 1 120 ? 3.264   49.722 70.093  1.00 67.82  ? 149 LEU B CD1 1 
ATOM   4309 C  CD2 . LEU B 1 120 ? 3.393   48.214 68.168  1.00 68.53  ? 149 LEU B CD2 1 
ATOM   4310 N  N   . THR B 1 121 ? -0.922  45.355 69.875  1.00 65.07  ? 150 THR B N   1 
ATOM   4311 C  CA  . THR B 1 121 ? -1.442  44.125 70.482  1.00 65.21  ? 150 THR B CA  1 
ATOM   4312 C  C   . THR B 1 121 ? -0.718  42.859 70.022  1.00 65.51  ? 150 THR B C   1 
ATOM   4313 O  O   . THR B 1 121 ? -0.254  42.102 70.866  1.00 65.76  ? 150 THR B O   1 
ATOM   4314 C  CB  . THR B 1 121 ? -2.956  44.000 70.248  1.00 66.13  ? 150 THR B CB  1 
ATOM   4315 O  OG1 . THR B 1 121 ? -3.612  45.182 70.687  1.00 67.24  ? 150 THR B OG1 1 
ATOM   4316 C  CG2 . THR B 1 121 ? -3.553  42.768 70.897  1.00 66.22  ? 150 THR B CG2 1 
ATOM   4317 N  N   . GLY B 1 122 ? -0.612  42.654 68.711  1.00 65.51  ? 151 GLY B N   1 
ATOM   4318 C  CA  . GLY B 1 122 ? 0.047   41.492 68.134  1.00 66.08  ? 151 GLY B CA  1 
ATOM   4319 C  C   . GLY B 1 122 ? 1.495   41.364 68.553  1.00 66.52  ? 151 GLY B C   1 
ATOM   4320 O  O   . GLY B 1 122 ? 1.922   40.295 68.978  1.00 66.61  ? 151 GLY B O   1 
ATOM   4321 N  N   . ARG B 1 123 ? 2.250   42.455 68.475  1.00 66.64  ? 152 ARG B N   1 
ATOM   4322 C  CA  . ARG B 1 123 ? 3.660   42.465 68.852  1.00 67.25  ? 152 ARG B CA  1 
ATOM   4323 C  C   . ARG B 1 123 ? 3.873   42.032 70.310  1.00 66.98  ? 152 ARG B C   1 
ATOM   4324 O  O   . ARG B 1 123 ? 4.670   41.138 70.569  1.00 66.96  ? 152 ARG B O   1 
ATOM   4325 C  CB  . ARG B 1 123 ? 4.236   43.873 68.628  1.00 69.56  ? 152 ARG B CB  1 
ATOM   4326 C  CG  . ARG B 1 123 ? 5.738   43.969 68.775  1.00 73.98  ? 152 ARG B CG  1 
ATOM   4327 C  CD  . ARG B 1 123 ? 6.204   45.406 68.621  1.00 79.38  ? 152 ARG B CD  1 
ATOM   4328 N  NE  . ARG B 1 123 ? 7.528   45.604 69.225  1.00 85.69  ? 152 ARG B NE  1 
ATOM   4329 C  CZ  . ARG B 1 123 ? 7.744   45.840 70.523  1.00 89.55  ? 152 ARG B CZ  1 
ATOM   4330 N  NH1 . ARG B 1 123 ? 6.723   45.940 71.368  1.00 89.17  ? 152 ARG B NH1 1 
ATOM   4331 N  NH2 . ARG B 1 123 ? 8.983   45.981 70.982  1.00 89.81  ? 152 ARG B NH2 1 
ATOM   4332 N  N   . GLN B 1 124 ? 3.136   42.645 71.246  1.00 66.48  ? 153 GLN B N   1 
ATOM   4333 C  CA  . GLN B 1 124 ? 3.229   42.377 72.678  1.00 66.10  ? 153 GLN B CA  1 
ATOM   4334 C  C   . GLN B 1 124 ? 2.748   40.976 73.057  1.00 66.16  ? 153 GLN B C   1 
ATOM   4335 O  O   . GLN B 1 124 ? 3.380   40.337 73.895  1.00 66.42  ? 153 GLN B O   1 
ATOM   4336 C  CB  . GLN B 1 124 ? 2.499   43.464 73.465  1.00 66.71  ? 153 GLN B CB  1 
ATOM   4337 C  CG  . GLN B 1 124 ? 2.904   44.848 72.997  1.00 69.16  ? 153 GLN B CG  1 
ATOM   4338 C  CD  . GLN B 1 124 ? 2.578   45.925 73.980  1.00 72.77  ? 153 GLN B CD  1 
ATOM   4339 O  OE1 . GLN B 1 124 ? 1.629   45.813 74.761  1.00 73.86  ? 153 GLN B OE1 1 
ATOM   4340 N  NE2 . GLN B 1 124 ? 3.355   47.006 73.948  1.00 73.37  ? 153 GLN B NE2 1 
ATOM   4341 N  N   . VAL B 1 125 ? 1.676   40.473 72.413  1.00 65.64  ? 154 VAL B N   1 
ATOM   4342 C  CA  . VAL B 1 125 ? 1.196   39.111 72.661  1.00 65.57  ? 154 VAL B CA  1 
ATOM   4343 C  C   . VAL B 1 125 ? 2.262   38.120 72.157  1.00 65.80  ? 154 VAL B C   1 
ATOM   4344 O  O   . VAL B 1 125 ? 2.591   37.160 72.862  1.00 66.16  ? 154 VAL B O   1 
ATOM   4345 C  CB  . VAL B 1 125 ? -0.204  38.860 72.045  1.00 65.79  ? 154 VAL B CB  1 
ATOM   4346 C  CG1 . VAL B 1 125 ? -0.515  37.374 71.932  1.00 66.31  ? 154 VAL B CG1 1 
ATOM   4347 C  CG2 . VAL B 1 125 ? -1.285  39.564 72.844  1.00 66.09  ? 154 VAL B CG2 1 
ATOM   4348 N  N   . ALA B 1 126 ? 2.841   38.395 70.970  1.00 65.42  ? 155 ALA B N   1 
ATOM   4349 C  CA  . ALA B 1 126 ? 3.921   37.581 70.407  1.00 65.52  ? 155 ALA B CA  1 
ATOM   4350 C  C   . ALA B 1 126 ? 5.162   37.644 71.296  1.00 65.18  ? 155 ALA B C   1 
ATOM   4351 O  O   . ALA B 1 126 ? 5.888   36.656 71.376  1.00 65.87  ? 155 ALA B O   1 
ATOM   4352 C  CB  . ALA B 1 126 ? 4.278   38.053 69.006  1.00 65.65  ? 155 ALA B CB  1 
ATOM   4353 N  N   . MET B 1 127 ? 5.413   38.793 71.958  1.00 63.80  ? 156 MET B N   1 
ATOM   4354 C  CA  . MET B 1 127 ? 6.544   38.937 72.867  1.00 63.10  ? 156 MET B CA  1 
ATOM   4355 C  C   . MET B 1 127 ? 6.481   37.984 74.035  1.00 63.08  ? 156 MET B C   1 
ATOM   4356 O  O   . MET B 1 127 ? 7.520   37.585 74.546  1.00 63.23  ? 156 MET B O   1 
ATOM   4357 C  CB  . MET B 1 127 ? 6.701   40.372 73.376  1.00 63.07  ? 156 MET B CB  1 
ATOM   4358 C  CG  . MET B 1 127 ? 7.388   41.295 72.402  1.00 64.22  ? 156 MET B CG  1 
ATOM   4359 S  SD  . MET B 1 127 ? 8.982   40.691 71.830  1.00 66.29  ? 156 MET B SD  1 
ATOM   4360 C  CE  . MET B 1 127 ? 9.908   40.689 73.383  1.00 64.53  ? 156 MET B CE  1 
ATOM   4361 N  N   . GLY B 1 128 ? 5.281   37.615 74.452  1.00 62.92  ? 157 GLY B N   1 
ATOM   4362 C  CA  . GLY B 1 128 ? 5.110   36.670 75.539  1.00 63.31  ? 157 GLY B CA  1 
ATOM   4363 C  C   . GLY B 1 128 ? 4.020   37.015 76.526  1.00 63.28  ? 157 GLY B C   1 
ATOM   4364 O  O   . GLY B 1 128 ? 3.718   36.203 77.392  1.00 63.37  ? 157 GLY B O   1 
ATOM   4365 N  N   . LEU B 1 129 ? 3.433   38.206 76.427  1.00 63.03  ? 158 LEU B N   1 
ATOM   4366 C  CA  . LEU B 1 129 ? 2.368   38.599 77.334  1.00 63.31  ? 158 LEU B CA  1 
ATOM   4367 C  C   . LEU B 1 129 ? 1.098   37.804 77.082  1.00 63.81  ? 158 LEU B C   1 
ATOM   4368 O  O   . LEU B 1 129 ? 0.680   37.617 75.940  1.00 64.14  ? 158 LEU B O   1 
ATOM   4369 C  CB  . LEU B 1 129 ? 2.115   40.101 77.270  1.00 63.41  ? 158 LEU B CB  1 
ATOM   4370 C  CG  . LEU B 1 129 ? 3.300   40.993 77.591  1.00 64.77  ? 158 LEU B CG  1 
ATOM   4371 C  CD1 . LEU B 1 129 ? 2.901   42.434 77.512  1.00 65.60  ? 158 LEU B CD1 1 
ATOM   4372 C  CD2 . LEU B 1 129 ? 3.849   40.699 78.962  1.00 65.21  ? 158 LEU B CD2 1 
ATOM   4373 N  N   . GLY B 1 130 ? 0.545   37.288 78.164  1.00 63.81  ? 159 GLY B N   1 
ATOM   4374 C  CA  . GLY B 1 130 ? -0.658  36.469 78.178  1.00 64.41  ? 159 GLY B CA  1 
ATOM   4375 C  C   . GLY B 1 130 ? -0.854  35.814 79.534  1.00 64.80  ? 159 GLY B C   1 
ATOM   4376 O  O   . GLY B 1 130 ? 0.100   35.646 80.292  1.00 65.01  ? 159 GLY B O   1 
ATOM   4377 N  N   . GLY B 1 131 ? -2.089  35.467 79.858  1.00 64.41  ? 160 GLY B N   1 
ATOM   4378 C  CA  . GLY B 1 131 ? -2.404  34.831 81.130  1.00 64.31  ? 160 GLY B CA  1 
ATOM   4379 C  C   . GLY B 1 131 ? -3.805  34.265 81.167  1.00 64.00  ? 160 GLY B C   1 
ATOM   4380 O  O   . GLY B 1 131 ? -4.572  34.428 80.216  1.00 63.97  ? 160 GLY B O   1 
ATOM   4381 N  N   . LEU B 1 132 ? -4.158  33.603 82.271  1.00 63.53  ? 161 LEU B N   1 
ATOM   4382 C  CA  . LEU B 1 132 ? -5.479  32.993 82.412  1.00 63.49  ? 161 LEU B CA  1 
ATOM   4383 C  C   . LEU B 1 132 ? -6.324  33.605 83.531  1.00 62.99  ? 161 LEU B C   1 
ATOM   4384 O  O   . LEU B 1 132 ? -5.800  34.253 84.430  1.00 62.98  ? 161 LEU B O   1 
ATOM   4385 C  CB  . LEU B 1 132 ? -5.322  31.495 82.671  1.00 63.51  ? 161 LEU B CB  1 
ATOM   4386 C  CG  . LEU B 1 132 ? -4.782  30.717 81.519  1.00 65.18  ? 161 LEU B CG  1 
ATOM   4387 C  CD1 . LEU B 1 132 ? -3.991  29.543 81.999  1.00 65.60  ? 161 LEU B CD1 1 
ATOM   4388 C  CD2 . LEU B 1 132 ? -5.896  30.296 80.591  1.00 66.16  ? 161 LEU B CD2 1 
ATOM   4389 N  N   . ILE B 1 133 ? -7.639  33.397 83.458  1.00 62.36  ? 162 ILE B N   1 
ATOM   4390 C  CA  . ILE B 1 133 ? -8.602  33.797 84.469  1.00 62.50  ? 162 ILE B CA  1 
ATOM   4391 C  C   . ILE B 1 133 ? -9.529  32.584 84.675  1.00 62.95  ? 162 ILE B C   1 
ATOM   4392 O  O   . ILE B 1 133 ? -10.288 32.229 83.779  1.00 62.85  ? 162 ILE B O   1 
ATOM   4393 C  CB  . ILE B 1 133 ? -9.408  35.080 84.108  1.00 62.60  ? 162 ILE B CB  1 
ATOM   4394 C  CG1 . ILE B 1 133 ? -8.492  36.306 83.892  1.00 63.44  ? 162 ILE B CG1 1 
ATOM   4395 C  CG2 . ILE B 1 133 ? -10.473 35.358 85.172  1.00 62.49  ? 162 ILE B CG2 1 
ATOM   4396 C  CD1 . ILE B 1 133 ? -9.220  37.659 83.541  1.00 64.50  ? 162 ILE B CD1 1 
ATOM   4397 N  N   . ILE B 1 134 ? -9.425  31.913 85.826  1.00 62.97  ? 163 ILE B N   1 
ATOM   4398 C  CA  . ILE B 1 134 ? -10.277 30.779 86.135  1.00 63.12  ? 163 ILE B CA  1 
ATOM   4399 C  C   . ILE B 1 134 ? -11.408 31.274 87.013  1.00 64.21  ? 163 ILE B C   1 
ATOM   4400 O  O   . ILE B 1 134 ? -11.170 31.672 88.147  1.00 63.99  ? 163 ILE B O   1 
ATOM   4401 C  CB  . ILE B 1 134 ? -9.487  29.652 86.824  1.00 62.89  ? 163 ILE B CB  1 
ATOM   4402 C  CG1 . ILE B 1 134 ? -8.293  29.196 85.961  1.00 63.66  ? 163 ILE B CG1 1 
ATOM   4403 C  CG2 . ILE B 1 134 ? -10.402 28.494 87.208  1.00 62.94  ? 163 ILE B CG2 1 
ATOM   4404 C  CD1 . ILE B 1 134 ? -8.618  28.823 84.517  1.00 64.90  ? 163 ILE B CD1 1 
ATOM   4405 N  N   . ILE B 1 135 ? -12.629 31.298 86.481  1.00 65.02  ? 164 ILE B N   1 
ATOM   4406 C  CA  . ILE B 1 135 ? -13.788 31.732 87.250  1.00 66.04  ? 164 ILE B CA  1 
ATOM   4407 C  C   . ILE B 1 135 ? -14.468 30.501 87.863  1.00 67.12  ? 164 ILE B C   1 
ATOM   4408 O  O   . ILE B 1 135 ? -14.571 29.465 87.213  1.00 66.74  ? 164 ILE B O   1 
ATOM   4409 C  CB  . ILE B 1 135 ? -14.739 32.583 86.376  1.00 66.37  ? 164 ILE B CB  1 
ATOM   4410 C  CG1 . ILE B 1 135 ? -14.031 33.852 85.901  1.00 66.69  ? 164 ILE B CG1 1 
ATOM   4411 C  CG2 . ILE B 1 135 ? -16.040 32.922 87.115  1.00 66.96  ? 164 ILE B CG2 1 
ATOM   4412 C  CD1 . ILE B 1 135 ? -14.783 34.591 84.885  1.00 67.52  ? 164 ILE B CD1 1 
ATOM   4413 N  N   . ASP B 1 136 ? -14.874 30.606 89.136  1.00 68.29  ? 165 ASP B N   1 
ATOM   4414 C  CA  . ASP B 1 136 ? -15.526 29.537 89.892  1.00 69.60  ? 165 ASP B CA  1 
ATOM   4415 C  C   . ASP B 1 136 ? -16.905 29.960 90.351  1.00 70.72  ? 165 ASP B C   1 
ATOM   4416 O  O   . ASP B 1 136 ? -17.086 31.101 90.771  1.00 70.77  ? 165 ASP B O   1 
ATOM   4417 C  CB  . ASP B 1 136 ? -14.734 29.264 91.168  1.00 71.34  ? 165 ASP B CB  1 
ATOM   4418 C  CG  . ASP B 1 136 ? -13.540 28.370 91.005  1.00 76.44  ? 165 ASP B CG  1 
ATOM   4419 O  OD1 . ASP B 1 136 ? -13.495 27.614 90.003  1.00 77.22  ? 165 ASP B OD1 1 
ATOM   4420 O  OD2 . ASP B 1 136 ? -12.658 28.402 91.892  1.00 78.87  ? 165 ASP B OD2 1 
ATOM   4421 N  N   . ASP B 1 137 ? -17.854 29.031 90.351  1.00 71.38  ? 166 ASP B N   1 
ATOM   4422 C  CA  . ASP B 1 137 ? -19.177 29.297 90.900  1.00 72.85  ? 166 ASP B CA  1 
ATOM   4423 C  C   . ASP B 1 137 ? -19.707 28.050 91.636  1.00 74.63  ? 166 ASP B C   1 
ATOM   4424 O  O   . ASP B 1 137 ? -19.121 26.974 91.514  1.00 74.92  ? 166 ASP B O   1 
ATOM   4425 C  CB  . ASP B 1 137 ? -20.160 29.891 89.869  1.00 74.01  ? 166 ASP B CB  1 
ATOM   4426 C  CG  . ASP B 1 137 ? -20.549 29.021 88.692  1.00 77.82  ? 166 ASP B CG  1 
ATOM   4427 O  OD1 . ASP B 1 137 ? -20.710 27.805 88.878  1.00 78.34  ? 166 ASP B OD1 1 
ATOM   4428 O  OD2 . ASP B 1 137 ? -20.742 29.569 87.594  1.00 79.59  ? 166 ASP B OD2 1 
ATOM   4429 N  N   . GLU B 1 138 ? -20.763 28.199 92.440  1.00 75.79  ? 167 GLU B N   1 
ATOM   4430 C  CA  . GLU B 1 138 ? -21.310 27.080 93.198  1.00 77.40  ? 167 GLU B CA  1 
ATOM   4431 C  C   . GLU B 1 138 ? -21.839 25.993 92.265  1.00 77.75  ? 167 GLU B C   1 
ATOM   4432 O  O   . GLU B 1 138 ? -21.576 24.814 92.494  1.00 77.75  ? 167 GLU B O   1 
ATOM   4433 C  CB  . GLU B 1 138 ? -22.414 27.566 94.154  1.00 81.69  ? 167 GLU B CB  1 
ATOM   4434 C  CG  . GLU B 1 138 ? -22.985 26.484 95.059  1.00 89.27  ? 167 GLU B CG  1 
ATOM   4435 C  CD  . GLU B 1 138 ? -24.442 26.681 95.440  1.00 98.30  ? 167 GLU B CD  1 
ATOM   4436 O  OE1 . GLU B 1 138 ? -25.304 26.680 94.528  1.00 99.05  ? 167 GLU B OE1 1 
ATOM   4437 O  OE2 . GLU B 1 138 ? -24.724 26.823 96.654  1.00 101.98 ? 167 GLU B OE2 1 
ATOM   4438 N  N   . GLU B 1 139 ? -22.553 26.392 91.198  1.00 77.80  ? 168 GLU B N   1 
ATOM   4439 C  CA  . GLU B 1 139 ? -23.133 25.460 90.231  1.00 78.32  ? 168 GLU B CA  1 
ATOM   4440 C  C   . GLU B 1 139 ? -22.108 24.498 89.616  1.00 78.11  ? 168 GLU B C   1 
ATOM   4441 O  O   . GLU B 1 139 ? -22.332 23.289 89.612  1.00 78.39  ? 168 GLU B O   1 
ATOM   4442 C  CB  . GLU B 1 139 ? -23.900 26.224 89.142  1.00 81.19  ? 168 GLU B CB  1 
ATOM   4443 C  CG  . GLU B 1 139 ? -24.614 25.313 88.161  1.00 87.72  ? 168 GLU B CG  1 
ATOM   4444 C  CD  . GLU B 1 139 ? -25.535 26.021 87.183  1.00 96.38  ? 168 GLU B CD  1 
ATOM   4445 O  OE1 . GLU B 1 139 ? -26.429 25.344 86.621  1.00 98.62  ? 168 GLU B OE1 1 
ATOM   4446 O  OE2 . GLU B 1 139 ? -25.362 27.245 86.971  1.00 98.49  ? 168 GLU B OE2 1 
ATOM   4447 N  N   . SER B 1 140 ? -20.973 25.033 89.143  1.00 77.47  ? 169 SER B N   1 
ATOM   4448 C  CA  . SER B 1 140 ? -19.903 24.264 88.522  1.00 77.48  ? 169 SER B CA  1 
ATOM   4449 C  C   . SER B 1 140 ? -19.172 23.374 89.521  1.00 77.48  ? 169 SER B C   1 
ATOM   4450 O  O   . SER B 1 140 ? -18.745 22.270 89.170  1.00 77.81  ? 169 SER B O   1 
ATOM   4451 C  CB  . SER B 1 140 ? -18.899 25.202 87.857  1.00 78.75  ? 169 SER B CB  1 
ATOM   4452 O  OG  . SER B 1 140 ? -18.059 25.868 88.791  1.00 81.14  ? 169 SER B OG  1 
ATOM   4453 N  N   . THR B 1 141 ? -18.995 23.871 90.751  1.00 76.91  ? 170 THR B N   1 
ATOM   4454 C  CA  . THR B 1 141 ? -18.264 23.176 91.804  1.00 76.97  ? 170 THR B CA  1 
ATOM   4455 C  C   . THR B 1 141 ? -18.950 21.882 92.234  1.00 76.86  ? 170 THR B C   1 
ATOM   4456 O  O   . THR B 1 141 ? -18.265 20.914 92.557  1.00 77.06  ? 170 THR B O   1 
ATOM   4457 C  CB  . THR B 1 141 ? -17.997 24.139 92.952  1.00 78.46  ? 170 THR B CB  1 
ATOM   4458 O  OG1 . THR B 1 141 ? -17.135 25.174 92.469  1.00 79.42  ? 170 THR B OG1 1 
ATOM   4459 C  CG2 . THR B 1 141 ? -17.359 23.467 94.146  1.00 78.98  ? 170 THR B CG2 1 
ATOM   4460 N  N   . LYS B 1 142 ? -20.289 21.834 92.169  1.00 76.46  ? 171 LYS B N   1 
ATOM   4461 C  CA  . LYS B 1 142 ? -21.062 20.639 92.512  1.00 76.45  ? 171 LYS B CA  1 
ATOM   4462 C  C   . LYS B 1 142 ? -20.753 19.476 91.562  1.00 75.77  ? 171 LYS B C   1 
ATOM   4463 O  O   . LYS B 1 142 ? -20.748 18.324 91.987  1.00 75.75  ? 171 LYS B O   1 
ATOM   4464 C  CB  . LYS B 1 142 ? -22.561 20.954 92.464  1.00 79.02  ? 171 LYS B CB  1 
ATOM   4465 C  CG  . LYS B 1 142 ? -23.005 21.944 93.520  1.00 84.68  ? 171 LYS B CG  1 
ATOM   4466 C  CD  . LYS B 1 142 ? -24.463 22.356 93.327  1.00 90.34  ? 171 LYS B CD  1 
ATOM   4467 C  CE  . LYS B 1 142 ? -24.943 23.226 94.470  1.00 94.34  ? 171 LYS B CE  1 
ATOM   4468 N  NZ  . LYS B 1 142 ? -26.301 23.772 94.217  1.00 96.63  ? 171 LYS B NZ  1 
ATOM   4469 N  N   . LEU B 1 143 ? -20.516 19.783 90.275  1.00 75.17  ? 172 LEU B N   1 
ATOM   4470 C  CA  . LEU B 1 143 ? -20.213 18.797 89.237  1.00 74.96  ? 172 LEU B CA  1 
ATOM   4471 C  C   . LEU B 1 143 ? -18.929 18.040 89.560  1.00 74.36  ? 172 LEU B C   1 
ATOM   4472 O  O   . LEU B 1 143 ? -17.982 18.637 90.072  1.00 74.68  ? 172 LEU B O   1 
ATOM   4473 C  CB  . LEU B 1 143 ? -20.073 19.502 87.882  1.00 75.24  ? 172 LEU B CB  1 
ATOM   4474 C  CG  . LEU B 1 143 ? -21.356 20.090 87.325  1.00 76.88  ? 172 LEU B CG  1 
ATOM   4475 C  CD1 . LEU B 1 143 ? -21.080 20.905 86.093  1.00 77.57  ? 172 LEU B CD1 1 
ATOM   4476 C  CD2 . LEU B 1 143 ? -22.362 19.002 87.008  1.00 77.68  ? 172 LEU B CD2 1 
ATOM   4477 N  N   . PRO B 1 144 ? -18.860 16.731 89.255  1.00 73.16  ? 173 PRO B N   1 
ATOM   4478 C  CA  . PRO B 1 144 ? -17.647 15.965 89.590  1.00 72.32  ? 173 PRO B CA  1 
ATOM   4479 C  C   . PRO B 1 144 ? -16.517 16.052 88.566  1.00 71.27  ? 173 PRO B C   1 
ATOM   4480 O  O   . PRO B 1 144 ? -15.843 15.055 88.331  1.00 71.42  ? 173 PRO B O   1 
ATOM   4481 C  CB  . PRO B 1 144 ? -18.166 14.534 89.705  1.00 73.23  ? 173 PRO B CB  1 
ATOM   4482 C  CG  . PRO B 1 144 ? -19.289 14.482 88.709  1.00 74.02  ? 173 PRO B CG  1 
ATOM   4483 C  CD  . PRO B 1 144 ? -19.900 15.873 88.651  1.00 72.59  ? 173 PRO B CD  1 
ATOM   4484 N  N   . LEU B 1 145 ? -16.330 17.226 87.943  1.00 69.93  ? 174 LEU B N   1 
ATOM   4485 C  CA  . LEU B 1 145 ? -15.272 17.444 86.960  1.00 69.04  ? 174 LEU B CA  1 
ATOM   4486 C  C   . LEU B 1 145 ? -13.917 17.475 87.663  1.00 68.53  ? 174 LEU B C   1 
ATOM   4487 O  O   . LEU B 1 145 ? -13.846 17.889 88.820  1.00 68.61  ? 174 LEU B O   1 
ATOM   4488 C  CB  . LEU B 1 145 ? -15.482 18.800 86.275  1.00 68.72  ? 174 LEU B CB  1 
ATOM   4489 C  CG  . LEU B 1 145 ? -16.750 18.985 85.468  1.00 69.75  ? 174 LEU B CG  1 
ATOM   4490 C  CD1 . LEU B 1 145 ? -16.762 20.357 84.820  1.00 70.19  ? 174 LEU B CD1 1 
ATOM   4491 C  CD2 . LEU B 1 145 ? -16.899 17.907 84.402  1.00 70.04  ? 174 LEU B CD2 1 
ATOM   4492 N  N   . PRO B 1 146 ? -12.815 17.096 86.981  1.00 67.69  ? 175 PRO B N   1 
ATOM   4493 C  CA  . PRO B 1 146 ? -11.492 17.176 87.629  1.00 67.12  ? 175 PRO B CA  1 
ATOM   4494 C  C   . PRO B 1 146 ? -11.188 18.599 88.113  1.00 66.69  ? 175 PRO B C   1 
ATOM   4495 O  O   . PRO B 1 146 ? -11.414 19.554 87.378  1.00 66.84  ? 175 PRO B O   1 
ATOM   4496 C  CB  . PRO B 1 146 ? -10.527 16.718 86.527  1.00 67.64  ? 175 PRO B CB  1 
ATOM   4497 C  CG  . PRO B 1 146 ? -11.355 15.942 85.578  1.00 68.11  ? 175 PRO B CG  1 
ATOM   4498 C  CD  . PRO B 1 146 ? -12.713 16.577 85.603  1.00 66.80  ? 175 PRO B CD  1 
ATOM   4499 N  N   . LYS B 1 147 ? -10.776 18.743 89.376  1.00 66.02  ? 176 LYS B N   1 
ATOM   4500 C  CA  . LYS B 1 147 ? -10.528 20.051 89.983  1.00 65.97  ? 176 LYS B CA  1 
ATOM   4501 C  C   . LYS B 1 147 ? -9.101  20.264 90.472  1.00 65.40  ? 176 LYS B C   1 
ATOM   4502 O  O   . LYS B 1 147 ? -8.786  21.375 90.916  1.00 65.81  ? 176 LYS B O   1 
ATOM   4503 C  CB  . LYS B 1 147 ? -11.466 20.259 91.179  1.00 68.51  ? 176 LYS B CB  1 
ATOM   4504 C  CG  . LYS B 1 147 ? -12.930 20.342 90.800  1.00 73.73  ? 176 LYS B CG  1 
ATOM   4505 C  CD  . LYS B 1 147 ? -13.834 19.623 91.793  1.00 77.98  ? 176 LYS B CD  1 
ATOM   4506 C  CE  . LYS B 1 147 ? -15.277 19.829 91.409  1.00 81.94  ? 176 LYS B CE  1 
ATOM   4507 N  NZ  . LYS B 1 147 ? -16.199 19.090 92.308  1.00 84.68  ? 176 LYS B NZ  1 
ATOM   4508 N  N   . GLU B 1 148 ? -8.258  19.217 90.462  1.00 64.17  ? 177 GLU B N   1 
ATOM   4509 C  CA  . GLU B 1 148 ? -6.894  19.357 90.944  1.00 63.87  ? 177 GLU B CA  1 
ATOM   4510 C  C   . GLU B 1 148 ? -6.026  20.090 89.950  1.00 63.20  ? 177 GLU B C   1 
ATOM   4511 O  O   . GLU B 1 148 ? -5.498  19.484 89.015  1.00 63.25  ? 177 GLU B O   1 
ATOM   4512 C  CB  . GLU B 1 148 ? -6.282  18.005 91.294  1.00 66.80  ? 177 GLU B CB  1 
ATOM   4513 C  CG  . GLU B 1 148 ? -4.989  18.139 92.077  1.00 72.34  ? 177 GLU B CG  1 
ATOM   4514 C  CD  . GLU B 1 148 ? -4.505  16.856 92.719  1.00 79.18  ? 177 GLU B CD  1 
ATOM   4515 O  OE1 . GLU B 1 148 ? -3.635  16.941 93.614  1.00 81.73  ? 177 GLU B OE1 1 
ATOM   4516 O  OE2 . GLU B 1 148 ? -4.993  15.768 92.336  1.00 80.74  ? 177 GLU B OE2 1 
ATOM   4517 N  N   . TRP B 1 149 ? -5.872  21.408 90.161  1.00 62.38  ? 178 TRP B N   1 
ATOM   4518 C  CA  . TRP B 1 149 ? -5.074  22.290 89.316  1.00 61.89  ? 178 TRP B CA  1 
ATOM   4519 C  C   . TRP B 1 149 ? -3.675  21.756 89.065  1.00 61.63  ? 178 TRP B C   1 
ATOM   4520 O  O   . TRP B 1 149 ? -3.005  21.313 89.991  1.00 61.95  ? 178 TRP B O   1 
ATOM   4521 C  CB  . TRP B 1 149 ? -4.986  23.685 89.940  1.00 61.40  ? 178 TRP B CB  1 
ATOM   4522 C  CG  . TRP B 1 149 ? -4.272  24.672 89.070  1.00 61.23  ? 178 TRP B CG  1 
ATOM   4523 C  CD1 . TRP B 1 149 ? -3.009  25.151 89.236  1.00 61.93  ? 178 TRP B CD1 1 
ATOM   4524 C  CD2 . TRP B 1 149 ? -4.767  25.255 87.862  1.00 61.08  ? 178 TRP B CD2 1 
ATOM   4525 N  NE1 . TRP B 1 149 ? -2.698  26.022 88.223  1.00 62.17  ? 178 TRP B NE1 1 
ATOM   4526 C  CE2 . TRP B 1 149 ? -3.763  26.109 87.367  1.00 61.81  ? 178 TRP B CE2 1 
ATOM   4527 C  CE3 . TRP B 1 149 ? -5.974  25.159 87.164  1.00 61.44  ? 178 TRP B CE3 1 
ATOM   4528 C  CZ2 . TRP B 1 149 ? -3.926  26.850 86.202  1.00 62.39  ? 178 TRP B CZ2 1 
ATOM   4529 C  CZ3 . TRP B 1 149 ? -6.134  25.899 86.016  1.00 62.33  ? 178 TRP B CZ3 1 
ATOM   4530 C  CH2 . TRP B 1 149 ? -5.125  26.745 85.555  1.00 62.48  ? 178 TRP B CH2 1 
ATOM   4531 N  N   . GLY B 1 150 ? -3.270  21.756 87.813  1.00 61.18  ? 179 GLY B N   1 
ATOM   4532 C  CA  . GLY B 1 150 ? -1.952  21.272 87.437  1.00 61.59  ? 179 GLY B CA  1 
ATOM   4533 C  C   . GLY B 1 150 ? -1.771  19.771 87.490  1.00 61.68  ? 179 GLY B C   1 
ATOM   4534 O  O   . GLY B 1 150 ? -0.706  19.277 87.139  1.00 61.76  ? 179 GLY B O   1 
ATOM   4535 N  N   . VAL B 1 151 ? -2.787  19.032 87.942  1.00 61.68  ? 180 VAL B N   1 
ATOM   4536 C  CA  . VAL B 1 151 ? -2.719  17.579 88.007  1.00 62.04  ? 180 VAL B CA  1 
ATOM   4537 C  C   . VAL B 1 151 ? -3.754  16.981 87.038  1.00 62.65  ? 180 VAL B C   1 
ATOM   4538 O  O   . VAL B 1 151 ? -3.370  16.342 86.055  1.00 62.71  ? 180 VAL B O   1 
ATOM   4539 C  CB  . VAL B 1 151 ? -2.849  17.049 89.460  1.00 62.35  ? 180 VAL B CB  1 
ATOM   4540 C  CG1 . VAL B 1 151 ? -3.079  15.543 89.474  1.00 62.77  ? 180 VAL B CG1 1 
ATOM   4541 C  CG2 . VAL B 1 151 ? -1.627  17.422 90.286  1.00 62.56  ? 180 VAL B CG2 1 
ATOM   4542 N  N   . ASP B 1 152 ? -5.059  17.224 87.288  1.00 62.68  ? 181 ASP B N   1 
ATOM   4543 C  CA  . ASP B 1 152 ? -6.128  16.758 86.408  1.00 63.31  ? 181 ASP B CA  1 
ATOM   4544 C  C   . ASP B 1 152 ? -6.971  17.900 85.827  1.00 62.74  ? 181 ASP B C   1 
ATOM   4545 O  O   . ASP B 1 152 ? -7.839  17.649 85.012  1.00 63.05  ? 181 ASP B O   1 
ATOM   4546 C  CB  . ASP B 1 152 ? -7.009  15.676 87.056  1.00 66.30  ? 181 ASP B CB  1 
ATOM   4547 C  CG  . ASP B 1 152 ? -7.559  15.974 88.439  1.00 73.47  ? 181 ASP B CG  1 
ATOM   4548 O  OD1 . ASP B 1 152 ? -7.923  17.137 88.693  1.00 75.00  ? 181 ASP B OD1 1 
ATOM   4549 O  OD2 . ASP B 1 152 ? -7.677  15.021 89.250  1.00 75.97  ? 181 ASP B OD2 1 
ATOM   4550 N  N   . ASP B 1 153 ? -6.710  19.143 86.226  1.00 62.26  ? 182 ASP B N   1 
ATOM   4551 C  CA  . ASP B 1 153 ? -7.371  20.333 85.704  1.00 62.21  ? 182 ASP B CA  1 
ATOM   4552 C  C   . ASP B 1 153 ? -6.189  21.107 85.152  1.00 61.75  ? 182 ASP B C   1 
ATOM   4553 O  O   . ASP B 1 153 ? -5.449  21.735 85.914  1.00 61.96  ? 182 ASP B O   1 
ATOM   4554 C  CB  . ASP B 1 153 ? -8.047  21.114 86.847  1.00 63.79  ? 182 ASP B CB  1 
ATOM   4555 C  CG  . ASP B 1 153 ? -8.873  22.303 86.404  1.00 68.11  ? 182 ASP B CG  1 
ATOM   4556 O  OD1 . ASP B 1 153 ? -8.942  22.557 85.183  1.00 67.92  ? 182 ASP B OD1 1 
ATOM   4557 O  OD2 . ASP B 1 153 ? -9.457  22.980 87.284  1.00 71.52  ? 182 ASP B OD2 1 
ATOM   4558 N  N   . VAL B 1 154 ? -5.938  20.966 83.849  1.00 60.82  ? 183 VAL B N   1 
ATOM   4559 C  CA  . VAL B 1 154 ? -4.735  21.516 83.250  1.00 60.45  ? 183 VAL B CA  1 
ATOM   4560 C  C   . VAL B 1 154 ? -4.969  22.561 82.168  1.00 60.05  ? 183 VAL B C   1 
ATOM   4561 O  O   . VAL B 1 154 ? -5.601  22.275 81.155  1.00 60.38  ? 183 VAL B O   1 
ATOM   4562 C  CB  . VAL B 1 154 ? -3.856  20.355 82.707  1.00 60.78  ? 183 VAL B CB  1 
ATOM   4563 C  CG1 . VAL B 1 154 ? -2.564  20.876 82.107  1.00 61.21  ? 183 VAL B CG1 1 
ATOM   4564 C  CG2 . VAL B 1 154 ? -3.558  19.330 83.793  1.00 61.00  ? 183 VAL B CG2 1 
ATOM   4565 N  N   . PRO B 1 155 ? -4.335  23.736 82.304  1.00 59.30  ? 184 PRO B N   1 
ATOM   4566 C  CA  . PRO B 1 155 ? -4.424  24.738 81.236  1.00 58.97  ? 184 PRO B CA  1 
ATOM   4567 C  C   . PRO B 1 155 ? -3.487  24.418 80.067  1.00 59.10  ? 184 PRO B C   1 
ATOM   4568 O  O   . PRO B 1 155 ? -2.324  24.070 80.277  1.00 59.64  ? 184 PRO B O   1 
ATOM   4569 C  CB  . PRO B 1 155 ? -3.966  26.014 81.931  1.00 59.58  ? 184 PRO B CB  1 
ATOM   4570 C  CG  . PRO B 1 155 ? -3.007  25.551 82.942  1.00 60.22  ? 184 PRO B CG  1 
ATOM   4571 C  CD  . PRO B 1 155 ? -3.496  24.207 83.428  1.00 58.81  ? 184 PRO B CD  1 
ATOM   4572 N  N   . VAL B 1 156 ? -3.982  24.531 78.835  1.00 58.47  ? 185 VAL B N   1 
ATOM   4573 C  CA  . VAL B 1 156 ? -3.169  24.288 77.650  1.00 58.41  ? 185 VAL B CA  1 
ATOM   4574 C  C   . VAL B 1 156 ? -3.239  25.510 76.718  1.00 58.80  ? 185 VAL B C   1 
ATOM   4575 O  O   . VAL B 1 156 ? -4.197  25.667 75.959  1.00 58.94  ? 185 VAL B O   1 
ATOM   4576 C  CB  . VAL B 1 156 ? -3.567  22.981 76.924  1.00 58.62  ? 185 VAL B CB  1 
ATOM   4577 C  CG1 . VAL B 1 156 ? -2.634  22.698 75.758  1.00 58.80  ? 185 VAL B CG1 1 
ATOM   4578 C  CG2 . VAL B 1 156 ? -3.601  21.799 77.883  1.00 59.01  ? 185 VAL B CG2 1 
ATOM   4579 N  N   . ILE B 1 157 ? -2.237  26.385 76.804  1.00 58.78  ? 186 ILE B N   1 
ATOM   4580 C  CA  . ILE B 1 157 ? -2.122  27.585 75.988  1.00 59.63  ? 186 ILE B CA  1 
ATOM   4581 C  C   . ILE B 1 157 ? -1.272  27.261 74.776  1.00 60.59  ? 186 ILE B C   1 
ATOM   4582 O  O   . ILE B 1 157 ? -0.075  27.016 74.897  1.00 60.77  ? 186 ILE B O   1 
ATOM   4583 C  CB  . ILE B 1 157 ? -1.475  28.719 76.788  1.00 60.34  ? 186 ILE B CB  1 
ATOM   4584 C  CG1 . ILE B 1 157 ? -2.271  29.021 78.063  1.00 61.25  ? 186 ILE B CG1 1 
ATOM   4585 C  CG2 . ILE B 1 157 ? -1.294  29.964 75.918  1.00 60.91  ? 186 ILE B CG2 1 
ATOM   4586 C  CD1 . ILE B 1 157 ? -1.523  29.874 79.018  1.00 62.22  ? 186 ILE B CD1 1 
ATOM   4587 N  N   . LEU B 1 158 ? -1.895  27.271 73.600  1.00 60.69  ? 187 LEU B N   1 
ATOM   4588 C  CA  . LEU B 1 158 ? -1.259  26.935 72.341  1.00 60.39  ? 187 LEU B CA  1 
ATOM   4589 C  C   . LEU B 1 158 ? -0.991  28.170 71.518  1.00 60.35  ? 187 LEU B C   1 
ATOM   4590 O  O   . LEU B 1 158 ? -1.912  28.793 71.017  1.00 59.98  ? 187 LEU B O   1 
ATOM   4591 C  CB  . LEU B 1 158 ? -2.170  25.979 71.575  1.00 60.19  ? 187 LEU B CB  1 
ATOM   4592 C  CG  . LEU B 1 158 ? -2.488  24.683 72.288  1.00 61.54  ? 187 LEU B CG  1 
ATOM   4593 C  CD1 . LEU B 1 158 ? -3.525  23.893 71.538  1.00 62.12  ? 187 LEU B CD1 1 
ATOM   4594 C  CD2 . LEU B 1 158 ? -1.237  23.864 72.500  1.00 62.21  ? 187 LEU B CD2 1 
ATOM   4595 N  N   . GLN B 1 159 ? 0.280   28.528 71.378  1.00 60.72  ? 188 GLN B N   1 
ATOM   4596 C  CA  . GLN B 1 159 ? 0.705   29.681 70.594  1.00 61.08  ? 188 GLN B CA  1 
ATOM   4597 C  C   . GLN B 1 159 ? 1.836   29.258 69.681  1.00 61.62  ? 188 GLN B C   1 
ATOM   4598 O  O   . GLN B 1 159 ? 2.719   28.531 70.111  1.00 61.23  ? 188 GLN B O   1 
ATOM   4599 C  CB  . GLN B 1 159 ? 1.266   30.780 71.507  1.00 62.29  ? 188 GLN B CB  1 
ATOM   4600 C  CG  . GLN B 1 159 ? 0.440   31.121 72.727  1.00 65.56  ? 188 GLN B CG  1 
ATOM   4601 C  CD  . GLN B 1 159 ? 1.167   32.120 73.584  1.00 69.31  ? 188 GLN B CD  1 
ATOM   4602 O  OE1 . GLN B 1 159 ? 2.223   31.819 74.162  1.00 70.44  ? 188 GLN B OE1 1 
ATOM   4603 N  NE2 . GLN B 1 159 ? 0.628   33.338 73.673  1.00 69.30  ? 188 GLN B NE2 1 
ATOM   4604 N  N   . ASP B 1 160 ? 1.860   29.756 68.451  1.00 62.66  ? 189 ASP B N   1 
ATOM   4605 C  CA  . ASP B 1 160 ? 2.990   29.514 67.553  1.00 63.99  ? 189 ASP B CA  1 
ATOM   4606 C  C   . ASP B 1 160 ? 3.881   30.770 67.538  1.00 65.32  ? 189 ASP B C   1 
ATOM   4607 O  O   . ASP B 1 160 ? 3.391   31.885 67.767  1.00 65.70  ? 189 ASP B O   1 
ATOM   4608 C  CB  . ASP B 1 160 ? 2.536   29.126 66.144  1.00 65.73  ? 189 ASP B CB  1 
ATOM   4609 C  CG  . ASP B 1 160 ? 1.896   30.246 65.347  1.00 70.58  ? 189 ASP B CG  1 
ATOM   4610 O  OD1 . ASP B 1 160 ? 1.220   31.109 65.962  1.00 71.89  ? 189 ASP B OD1 1 
ATOM   4611 O  OD2 . ASP B 1 160 ? 2.069   30.262 64.110  1.00 72.02  ? 189 ASP B OD2 1 
ATOM   4612 N  N   . LYS B 1 161 ? 5.184   30.596 67.320  1.00 65.84  ? 190 LYS B N   1 
ATOM   4613 C  CA  . LYS B 1 161 ? 6.106   31.730 67.303  1.00 66.91  ? 190 LYS B CA  1 
ATOM   4614 C  C   . LYS B 1 161 ? 7.134   31.597 66.189  1.00 68.42  ? 190 LYS B C   1 
ATOM   4615 O  O   . LYS B 1 161 ? 7.473   30.487 65.776  1.00 68.37  ? 190 LYS B O   1 
ATOM   4616 C  CB  . LYS B 1 161 ? 6.811   31.912 68.666  1.00 67.99  ? 190 LYS B CB  1 
ATOM   4617 C  CG  . LYS B 1 161 ? 5.917   32.406 69.806  1.00 70.92  ? 190 LYS B CG  1 
ATOM   4618 C  CD  . LYS B 1 161 ? 6.733   33.006 70.949  1.00 73.97  ? 190 LYS B CD  1 
ATOM   4619 C  CE  . LYS B 1 161 ? 5.886   33.391 72.134  1.00 76.69  ? 190 LYS B CE  1 
ATOM   4620 N  NZ  . LYS B 1 161 ? 4.694   34.178 71.727  1.00 78.33  ? 190 LYS B NZ  1 
ATOM   4621 N  N   . ARG B 1 162 ? 7.643   32.731 65.712  1.00 69.61  ? 191 ARG B N   1 
ATOM   4622 C  CA  . ARG B 1 162 ? 8.661   32.741 64.673  1.00 71.52  ? 191 ARG B CA  1 
ATOM   4623 C  C   . ARG B 1 162 ? 9.924   33.367 65.226  1.00 72.74  ? 191 ARG B C   1 
ATOM   4624 O  O   . ARG B 1 162 ? 9.860   34.444 65.817  1.00 72.87  ? 191 ARG B O   1 
ATOM   4625 C  CB  . ARG B 1 162 ? 8.185   33.536 63.449  1.00 73.53  ? 191 ARG B CB  1 
ATOM   4626 C  CG  . ARG B 1 162 ? 9.141   33.437 62.271  1.00 77.42  ? 191 ARG B CG  1 
ATOM   4627 C  CD  . ARG B 1 162 ? 8.413   33.571 60.958  1.00 81.72  ? 191 ARG B CD  1 
ATOM   4628 N  NE  . ARG B 1 162 ? 7.831   34.903 60.793  1.00 86.15  ? 191 ARG B NE  1 
ATOM   4629 C  CZ  . ARG B 1 162 ? 6.763   35.167 60.041  1.00 89.74  ? 191 ARG B CZ  1 
ATOM   4630 N  NH1 . ARG B 1 162 ? 6.131   34.186 59.405  1.00 89.84  ? 191 ARG B NH1 1 
ATOM   4631 N  NH2 . ARG B 1 162 ? 6.298   36.407 59.949  1.00 90.22  ? 191 ARG B NH2 1 
ATOM   4632 N  N   . LEU B 1 163 ? 11.067  32.699 65.052  1.00 73.43  ? 192 LEU B N   1 
ATOM   4633 C  CA  . LEU B 1 163 ? 12.334  33.240 65.526  1.00 74.65  ? 192 LEU B CA  1 
ATOM   4634 C  C   . LEU B 1 163 ? 13.304  33.513 64.374  1.00 75.89  ? 192 LEU B C   1 
ATOM   4635 O  O   . LEU B 1 163 ? 13.353  32.752 63.406  1.00 75.99  ? 192 LEU B O   1 
ATOM   4636 C  CB  . LEU B 1 163 ? 12.993  32.285 66.532  1.00 74.79  ? 192 LEU B CB  1 
ATOM   4637 C  CG  . LEU B 1 163 ? 12.155  31.858 67.729  1.00 76.00  ? 192 LEU B CG  1 
ATOM   4638 C  CD1 . LEU B 1 163 ? 12.938  30.919 68.621  1.00 76.59  ? 192 LEU B CD1 1 
ATOM   4639 C  CD2 . LEU B 1 163 ? 11.676  33.056 68.535  1.00 76.41  ? 192 LEU B CD2 1 
ATOM   4640 N  N   . ASP B 1 164 ? 14.102  34.577 64.492  1.00 76.52  ? 193 ASP B N   1 
ATOM   4641 C  CA  . ASP B 1 164 ? 15.121  34.883 63.492  1.00 77.65  ? 193 ASP B CA  1 
ATOM   4642 C  C   . ASP B 1 164 ? 16.386  33.999 63.729  1.00 78.73  ? 193 ASP B C   1 
ATOM   4643 O  O   . ASP B 1 164 ? 16.464  33.287 64.738  1.00 79.02  ? 193 ASP B O   1 
ATOM   4644 C  CB  . ASP B 1 164 ? 15.441  36.397 63.479  1.00 79.11  ? 193 ASP B CB  1 
ATOM   4645 C  CG  . ASP B 1 164 ? 16.158  36.930 64.705  1.00 84.65  ? 193 ASP B CG  1 
ATOM   4646 O  OD1 . ASP B 1 164 ? 16.577  36.115 65.554  1.00 85.60  ? 193 ASP B OD1 1 
ATOM   4647 O  OD2 . ASP B 1 164 ? 16.309  38.167 64.814  1.00 87.41  ? 193 ASP B OD2 1 
ATOM   4648 N  N   . ALA B 1 165 ? 17.379  34.064 62.826  1.00 79.16  ? 194 ALA B N   1 
ATOM   4649 C  CA  . ALA B 1 165 ? 18.617  33.294 62.949  1.00 79.81  ? 194 ALA B CA  1 
ATOM   4650 C  C   . ALA B 1 165 ? 19.338  33.506 64.289  1.00 79.87  ? 194 ALA B C   1 
ATOM   4651 O  O   . ALA B 1 165 ? 19.914  32.556 64.827  1.00 79.78  ? 194 ALA B O   1 
ATOM   4652 C  CB  . ALA B 1 165 ? 19.549  33.627 61.798  1.00 80.25  ? 194 ALA B CB  1 
ATOM   4653 N  N   . LYS B 1 166 ? 19.283  34.733 64.841  1.00 79.81  ? 195 LYS B N   1 
ATOM   4654 C  CA  . LYS B 1 166 ? 19.924  35.021 66.130  1.00 80.52  ? 195 LYS B CA  1 
ATOM   4655 C  C   . LYS B 1 166 ? 19.106  34.547 67.361  1.00 80.73  ? 195 LYS B C   1 
ATOM   4656 O  O   . LYS B 1 166 ? 19.486  34.857 68.493  1.00 80.80  ? 195 LYS B O   1 
ATOM   4657 C  CB  . LYS B 1 166 ? 20.234  36.522 66.277  1.00 82.69  ? 195 LYS B CB  1 
ATOM   4658 C  CG  . LYS B 1 166 ? 20.854  37.186 65.059  1.00 87.63  ? 195 LYS B CG  1 
ATOM   4659 C  CD  . LYS B 1 166 ? 21.194  38.650 65.376  1.00 92.92  ? 195 LYS B CD  1 
ATOM   4660 C  CE  . LYS B 1 166 ? 21.347  39.532 64.154  1.00 96.44  ? 195 LYS B CE  1 
ATOM   4661 N  NZ  . LYS B 1 166 ? 21.462  40.976 64.524  1.00 97.88  ? 195 LYS B NZ  1 
ATOM   4662 N  N   . GLY B 1 167 ? 17.983  33.861 67.129  1.00 80.37  ? 196 GLY B N   1 
ATOM   4663 C  CA  . GLY B 1 167 ? 17.114  33.362 68.183  1.00 80.46  ? 196 GLY B CA  1 
ATOM   4664 C  C   . GLY B 1 167 ? 16.017  34.314 68.619  1.00 80.51  ? 196 GLY B C   1 
ATOM   4665 O  O   . GLY B 1 167 ? 15.039  33.887 69.232  1.00 80.82  ? 196 GLY B O   1 
ATOM   4666 N  N   . HIS B 1 168 ? 16.163  35.606 68.315  1.00 80.11  ? 197 HIS B N   1 
ATOM   4667 C  CA  . HIS B 1 168 ? 15.192  36.628 68.700  1.00 80.41  ? 197 HIS B CA  1 
ATOM   4668 C  C   . HIS B 1 168 ? 13.810  36.418 68.073  1.00 79.34  ? 197 HIS B C   1 
ATOM   4669 O  O   . HIS B 1 168 ? 13.700  35.752 67.050  1.00 78.96  ? 197 HIS B O   1 
ATOM   4670 C  CB  . HIS B 1 168 ? 15.722  38.023 68.348  1.00 82.52  ? 197 HIS B CB  1 
ATOM   4671 C  CG  . HIS B 1 168 ? 17.105  38.275 68.857  1.00 87.03  ? 197 HIS B CG  1 
ATOM   4672 N  ND1 . HIS B 1 168 ? 18.078  38.845 68.054  1.00 89.72  ? 197 HIS B ND1 1 
ATOM   4673 C  CD2 . HIS B 1 168 ? 17.651  37.972 70.058  1.00 88.64  ? 197 HIS B CD2 1 
ATOM   4674 C  CE1 . HIS B 1 168 ? 19.171  38.902 68.800  1.00 90.36  ? 197 HIS B CE1 1 
ATOM   4675 N  NE2 . HIS B 1 168 ? 18.963  38.385 70.014  1.00 90.13  ? 197 HIS B NE2 1 
ATOM   4676 N  N   . ILE B 1 169 ? 12.757  36.968 68.696  1.00 78.62  ? 198 ILE B N   1 
ATOM   4677 C  CA  . ILE B 1 169 ? 11.409  36.835 68.147  1.00 78.45  ? 198 ILE B CA  1 
ATOM   4678 C  C   . ILE B 1 169 ? 11.305  37.699 66.907  1.00 78.11  ? 198 ILE B C   1 
ATOM   4679 O  O   . ILE B 1 169 ? 11.512  38.913 66.977  1.00 78.26  ? 198 ILE B O   1 
ATOM   4680 C  CB  . ILE B 1 169 ? 10.307  37.159 69.188  1.00 78.83  ? 198 ILE B CB  1 
ATOM   4681 C  CG1 . ILE B 1 169 ? 10.332  36.140 70.354  1.00 79.55  ? 198 ILE B CG1 1 
ATOM   4682 C  CG2 . ILE B 1 169 ? 8.931   37.216 68.520  1.00 79.08  ? 198 ILE B CG2 1 
ATOM   4683 C  CD1 . ILE B 1 169 ? 9.383   36.443 71.493  1.00 80.39  ? 198 ILE B CD1 1 
ATOM   4684 N  N   . ASP B 1 170 ? 11.039  37.065 65.759  1.00 77.36  ? 199 ASP B N   1 
ATOM   4685 C  CA  . ASP B 1 170 ? 10.943  37.751 64.480  1.00 76.96  ? 199 ASP B CA  1 
ATOM   4686 C  C   . ASP B 1 170 ? 9.547   38.281 64.212  1.00 76.65  ? 199 ASP B C   1 
ATOM   4687 O  O   . ASP B 1 170 ? 8.716   37.585 63.633  1.00 77.11  ? 199 ASP B O   1 
ATOM   4688 C  CB  . ASP B 1 170 ? 11.390  36.819 63.355  1.00 78.59  ? 199 ASP B CB  1 
ATOM   4689 C  CG  . ASP B 1 170 ? 11.489  37.472 61.994  1.00 84.19  ? 199 ASP B CG  1 
ATOM   4690 O  OD1 . ASP B 1 170 ? 11.462  38.724 61.928  1.00 85.34  ? 199 ASP B OD1 1 
ATOM   4691 O  OD2 . ASP B 1 170 ? 11.601  36.732 60.990  1.00 86.74  ? 199 ASP B OD2 1 
ATOM   4692 N  N   . TYR B 1 171 ? 9.294   39.522 64.610  1.00 75.95  ? 200 TYR B N   1 
ATOM   4693 C  CA  . TYR B 1 171 ? 8.006   40.155 64.372  1.00 75.85  ? 200 TYR B CA  1 
ATOM   4694 C  C   . TYR B 1 171 ? 8.173   41.504 63.671  1.00 76.49  ? 200 TYR B C   1 
ATOM   4695 O  O   . TYR B 1 171 ? 8.703   42.459 64.250  1.00 76.75  ? 200 TYR B O   1 
ATOM   4696 C  CB  . TYR B 1 171 ? 7.219   40.321 65.668  1.00 75.22  ? 200 TYR B CB  1 
ATOM   4697 C  CG  . TYR B 1 171 ? 5.815   40.854 65.464  1.00 75.45  ? 200 TYR B CG  1 
ATOM   4698 C  CD1 . TYR B 1 171 ? 5.579   42.215 65.316  1.00 76.26  ? 200 TYR B CD1 1 
ATOM   4699 C  CD2 . TYR B 1 171 ? 4.716   40.009 65.516  1.00 76.03  ? 200 TYR B CD2 1 
ATOM   4700 C  CE1 . TYR B 1 171 ? 4.290   42.711 65.153  1.00 77.12  ? 200 TYR B CE1 1 
ATOM   4701 C  CE2 . TYR B 1 171 ? 3.422   40.496 65.373  1.00 76.82  ? 200 TYR B CE2 1 
ATOM   4702 C  CZ  . TYR B 1 171 ? 3.212   41.848 65.184  1.00 77.83  ? 200 TYR B CZ  1 
ATOM   4703 O  OH  . TYR B 1 171 ? 1.934   42.341 65.040  1.00 79.21  ? 200 TYR B OH  1 
ATOM   4704 N  N   . GLN B 1 172 ? 7.705   41.575 62.421  1.00 76.36  ? 201 GLN B N   1 
ATOM   4705 C  CA  . GLN B 1 172 ? 7.697   42.784 61.609  1.00 76.79  ? 201 GLN B CA  1 
ATOM   4706 C  C   . GLN B 1 172 ? 6.264   42.993 61.142  1.00 75.92  ? 201 GLN B C   1 
ATOM   4707 O  O   . GLN B 1 172 ? 5.650   42.042 60.659  1.00 76.37  ? 201 GLN B O   1 
ATOM   4708 C  CB  . GLN B 1 172 ? 8.603   42.621 60.377  1.00 79.96  ? 201 GLN B CB  1 
ATOM   4709 C  CG  . GLN B 1 172 ? 9.997   42.051 60.664  1.00 85.86  ? 201 GLN B CG  1 
ATOM   4710 C  CD  . GLN B 1 172 ? 10.999  43.072 61.168  1.00 91.86  ? 201 GLN B CD  1 
ATOM   4711 O  OE1 . GLN B 1 172 ? 10.646  44.154 61.661  1.00 94.08  ? 201 GLN B OE1 1 
ATOM   4712 N  NE2 . GLN B 1 172 ? 12.283  42.740 61.058  1.00 92.35  ? 201 GLN B NE2 1 
ATOM   4713 N  N   . LEU B 1 173 ? 5.722   44.213 61.274  1.00 74.79  ? 202 LEU B N   1 
ATOM   4714 C  CA  . LEU B 1 173 ? 4.364   44.483 60.809  1.00 74.56  ? 202 LEU B CA  1 
ATOM   4715 C  C   . LEU B 1 173 ? 4.370   44.958 59.344  1.00 75.26  ? 202 LEU B C   1 
ATOM   4716 O  O   . LEU B 1 173 ? 3.854   46.031 59.010  1.00 75.49  ? 202 LEU B O   1 
ATOM   4717 C  CB  . LEU B 1 173 ? 3.613   45.456 61.727  1.00 74.06  ? 202 LEU B CB  1 
ATOM   4718 C  CG  . LEU B 1 173 ? 2.099   45.562 61.503  1.00 74.80  ? 202 LEU B CG  1 
ATOM   4719 C  CD1 . LEU B 1 173 ? 1.412   44.213 61.622  1.00 75.36  ? 202 LEU B CD1 1 
ATOM   4720 C  CD2 . LEU B 1 173 ? 1.478   46.569 62.434  1.00 75.13  ? 202 LEU B CD2 1 
ATOM   4721 N  N   . ASP B 1 174 ? 4.968   44.143 58.461  1.00 75.17  ? 203 ASP B N   1 
ATOM   4722 C  CA  . ASP B 1 174 ? 5.002   44.451 57.038  1.00 75.55  ? 203 ASP B CA  1 
ATOM   4723 C  C   . ASP B 1 174 ? 3.623   44.149 56.372  1.00 75.62  ? 203 ASP B C   1 
ATOM   4724 O  O   . ASP B 1 174 ? 2.708   43.695 57.064  1.00 75.96  ? 203 ASP B O   1 
ATOM   4725 C  CB  . ASP B 1 174 ? 6.178   43.720 56.372  1.00 77.36  ? 203 ASP B CB  1 
ATOM   4726 C  CG  . ASP B 1 174 ? 6.228   42.229 56.603  1.00 81.93  ? 203 ASP B CG  1 
ATOM   4727 O  OD1 . ASP B 1 174 ? 5.238   41.676 57.117  1.00 82.61  ? 203 ASP B OD1 1 
ATOM   4728 O  OD2 . ASP B 1 174 ? 7.258   41.610 56.256  1.00 84.19  ? 203 ASP B OD2 1 
ATOM   4729 N  N   . ILE B 1 175 ? 3.453   44.421 55.058  1.00 75.14  ? 204 ILE B N   1 
ATOM   4730 C  CA  . ILE B 1 175 ? 2.157   44.188 54.405  1.00 75.14  ? 204 ILE B CA  1 
ATOM   4731 C  C   . ILE B 1 175 ? 1.726   42.720 54.422  1.00 75.40  ? 204 ILE B C   1 
ATOM   4732 O  O   . ILE B 1 175 ? 0.523   42.467 54.465  1.00 75.85  ? 204 ILE B O   1 
ATOM   4733 C  CB  . ILE B 1 175 ? 2.054   44.779 52.979  1.00 75.15  ? 204 ILE B CB  1 
ATOM   4734 C  CG1 . ILE B 1 175 ? 3.313   44.505 52.161  1.00 75.75  ? 204 ILE B CG1 1 
ATOM   4735 C  CG2 . ILE B 1 175 ? 1.739   46.261 53.020  1.00 75.63  ? 204 ILE B CG2 1 
ATOM   4736 C  CD1 . ILE B 1 175 ? 3.137   44.685 50.712  1.00 76.54  ? 204 ILE B CD1 1 
ATOM   4737 N  N   . ILE B 1 176 ? 2.681   41.758 54.398  1.00 74.91  ? 205 ILE B N   1 
ATOM   4738 C  CA  . ILE B 1 176 ? 2.323   40.335 54.418  1.00 74.80  ? 205 ILE B CA  1 
ATOM   4739 C  C   . ILE B 1 176 ? 1.753   39.939 55.771  1.00 74.30  ? 205 ILE B C   1 
ATOM   4740 O  O   . ILE B 1 176 ? 0.640   39.412 55.828  1.00 74.26  ? 205 ILE B O   1 
ATOM   4741 C  CB  . ILE B 1 176 ? 3.455   39.368 53.993  1.00 75.43  ? 205 ILE B CB  1 
ATOM   4742 C  CG1 . ILE B 1 176 ? 4.329   39.940 52.875  1.00 77.15  ? 205 ILE B CG1 1 
ATOM   4743 C  CG2 . ILE B 1 176 ? 2.886   38.006 53.621  1.00 75.55  ? 205 ILE B CG2 1 
ATOM   4744 C  CD1 . ILE B 1 176 ? 5.663   40.525 53.371  1.00 78.89  ? 205 ILE B CD1 1 
ATOM   4745 N  N   . THR B 1 177 ? 2.487   40.221 56.862  1.00 73.71  ? 206 THR B N   1 
ATOM   4746 C  CA  . THR B 1 177 ? 1.996   39.882 58.195  1.00 73.71  ? 206 THR B CA  1 
ATOM   4747 C  C   . THR B 1 177 ? 0.750   40.691 58.555  1.00 73.44  ? 206 THR B C   1 
ATOM   4748 O  O   . THR B 1 177 ? -0.067  40.191 59.309  1.00 73.62  ? 206 THR B O   1 
ATOM   4749 C  CB  . THR B 1 177 ? 3.098   39.970 59.254  1.00 74.72  ? 206 THR B CB  1 
ATOM   4750 O  OG1 . THR B 1 177 ? 3.400   41.335 59.502  1.00 75.66  ? 206 THR B OG1 1 
ATOM   4751 C  CG2 . THR B 1 177 ? 4.352   39.210 58.855  1.00 74.86  ? 206 THR B CG2 1 
ATOM   4752 N  N   . ALA B 1 178 ? 0.571   41.901 57.996  1.00 72.86  ? 207 ALA B N   1 
ATOM   4753 C  CA  . ALA B 1 178 ? -0.637  42.678 58.259  1.00 72.95  ? 207 ALA B CA  1 
ATOM   4754 C  C   . ALA B 1 178 ? -1.875  42.092 57.541  1.00 72.96  ? 207 ALA B C   1 
ATOM   4755 O  O   . ALA B 1 178 ? -3.006  42.313 57.979  1.00 73.33  ? 207 ALA B O   1 
ATOM   4756 C  CB  . ALA B 1 178 ? -0.432  44.123 57.849  1.00 73.13  ? 207 ALA B CB  1 
ATOM   4757 N  N   . ALA B 1 179 ? -1.665  41.352 56.449  1.00 72.34  ? 208 ALA B N   1 
ATOM   4758 C  CA  . ALA B 1 179 ? -2.758  40.781 55.681  1.00 72.52  ? 208 ALA B CA  1 
ATOM   4759 C  C   . ALA B 1 179 ? -3.056  39.320 56.017  1.00 72.37  ? 208 ALA B C   1 
ATOM   4760 O  O   . ALA B 1 179 ? -4.222  39.003 56.250  1.00 72.66  ? 208 ALA B O   1 
ATOM   4761 C  CB  . ALA B 1 179 ? -2.499  40.950 54.195  1.00 72.80  ? 208 ALA B CB  1 
ATOM   4762 N  N   . VAL B 1 180 ? -2.043  38.423 56.023  1.00 71.91  ? 209 VAL B N   1 
ATOM   4763 C  CA  . VAL B 1 180 ? -2.305  37.021 56.373  1.00 72.18  ? 209 VAL B CA  1 
ATOM   4764 C  C   . VAL B 1 180 ? -2.225  36.797 57.895  1.00 72.02  ? 209 VAL B C   1 
ATOM   4765 O  O   . VAL B 1 180 ? -2.983  36.001 58.452  1.00 72.22  ? 209 VAL B O   1 
ATOM   4766 C  CB  . VAL B 1 180 ? -1.468  35.983 55.581  1.00 73.01  ? 209 VAL B CB  1 
ATOM   4767 C  CG1 . VAL B 1 180 ? -1.758  36.074 54.090  1.00 73.92  ? 209 VAL B CG1 1 
ATOM   4768 C  CG2 . VAL B 1 180 ? 0.024   36.124 55.856  1.00 73.36  ? 209 VAL B CG2 1 
ATOM   4769 N  N   . GLY B 1 181 ? -1.331  37.521 58.548  1.00 71.41  ? 210 GLY B N   1 
ATOM   4770 C  CA  . GLY B 1 181 ? -1.132  37.415 59.981  1.00 71.12  ? 210 GLY B CA  1 
ATOM   4771 C  C   . GLY B 1 181 ? 0.282   37.021 60.347  1.00 70.37  ? 210 GLY B C   1 
ATOM   4772 O  O   . GLY B 1 181 ? 1.124   36.787 59.471  1.00 70.37  ? 210 GLY B O   1 
ATOM   4773 N  N   . TRP B 1 182 ? 0.553   36.962 61.654  1.00 69.46  ? 211 TRP B N   1 
ATOM   4774 C  CA  . TRP B 1 182 ? 1.851   36.556 62.151  1.00 68.94  ? 211 TRP B CA  1 
ATOM   4775 C  C   . TRP B 1 182 ? 1.747   35.116 62.552  1.00 68.44  ? 211 TRP B C   1 
ATOM   4776 O  O   . TRP B 1 182 ? 0.904   34.741 63.368  1.00 68.30  ? 211 TRP B O   1 
ATOM   4777 C  CB  . TRP B 1 182 ? 2.293   37.393 63.350  1.00 68.87  ? 211 TRP B CB  1 
ATOM   4778 C  CG  . TRP B 1 182 ? 3.723   37.162 63.742  1.00 69.56  ? 211 TRP B CG  1 
ATOM   4779 C  CD1 . TRP B 1 182 ? 4.836   37.595 63.081  1.00 70.62  ? 211 TRP B CD1 1 
ATOM   4780 C  CD2 . TRP B 1 182 ? 4.191   36.468 64.904  1.00 69.71  ? 211 TRP B CD2 1 
ATOM   4781 N  NE1 . TRP B 1 182 ? 5.971   37.225 63.768  1.00 70.90  ? 211 TRP B NE1 1 
ATOM   4782 C  CE2 . TRP B 1 182 ? 5.604   36.526 64.887  1.00 70.61  ? 211 TRP B CE2 1 
ATOM   4783 C  CE3 . TRP B 1 182 ? 3.553   35.798 65.961  1.00 70.00  ? 211 TRP B CE3 1 
ATOM   4784 C  CZ2 . TRP B 1 182 ? 6.385   35.930 65.877  1.00 71.21  ? 211 TRP B CZ2 1 
ATOM   4785 C  CZ3 . TRP B 1 182 ? 4.329   35.191 66.925  1.00 70.83  ? 211 TRP B CZ3 1 
ATOM   4786 C  CH2 . TRP B 1 182 ? 5.725   35.285 66.895  1.00 71.23  ? 211 TRP B CH2 1 
ATOM   4787 N  N   . PHE B 1 183 ? 2.584   34.302 61.948  1.00 68.10  ? 212 PHE B N   1 
ATOM   4788 C  CA  . PHE B 1 183 ? 2.664   32.884 62.242  1.00 68.10  ? 212 PHE B CA  1 
ATOM   4789 C  C   . PHE B 1 183 ? 4.147   32.453 62.320  1.00 67.70  ? 212 PHE B C   1 
ATOM   4790 O  O   . PHE B 1 183 ? 5.042   33.232 61.979  1.00 67.32  ? 212 PHE B O   1 
ATOM   4791 C  CB  . PHE B 1 183 ? 1.858   32.070 61.224  1.00 68.25  ? 212 PHE B CB  1 
ATOM   4792 C  CG  . PHE B 1 183 ? 2.241   32.336 59.794  1.00 69.41  ? 212 PHE B CG  1 
ATOM   4793 C  CD1 . PHE B 1 183 ? 3.281   31.642 59.197  1.00 70.44  ? 212 PHE B CD1 1 
ATOM   4794 C  CD2 . PHE B 1 183 ? 1.547   33.262 59.037  1.00 70.49  ? 212 PHE B CD2 1 
ATOM   4795 C  CE1 . PHE B 1 183 ? 3.634   31.884 57.882  1.00 71.26  ? 212 PHE B CE1 1 
ATOM   4796 C  CE2 . PHE B 1 183 ? 1.899   33.499 57.717  1.00 71.41  ? 212 PHE B CE2 1 
ATOM   4797 C  CZ  . PHE B 1 183 ? 2.940   32.811 57.150  1.00 71.27  ? 212 PHE B CZ  1 
ATOM   4798 N  N   . GLY B 1 184 ? 4.399   31.241 62.796  1.00 67.54  ? 213 GLY B N   1 
ATOM   4799 C  CA  . GLY B 1 184 ? 5.759   30.757 62.943  1.00 67.80  ? 213 GLY B CA  1 
ATOM   4800 C  C   . GLY B 1 184 ? 5.935   29.295 62.648  1.00 68.06  ? 213 GLY B C   1 
ATOM   4801 O  O   . GLY B 1 184 ? 4.964   28.564 62.464  1.00 67.75  ? 213 GLY B O   1 
ATOM   4802 N  N   . ASP B 1 185 ? 7.191   28.877 62.585  1.00 68.66  ? 214 ASP B N   1 
ATOM   4803 C  CA  . ASP B 1 185 ? 7.584   27.491 62.347  1.00 69.75  ? 214 ASP B CA  1 
ATOM   4804 C  C   . ASP B 1 185 ? 7.822   26.724 63.676  1.00 69.77  ? 214 ASP B C   1 
ATOM   4805 O  O   . ASP B 1 185 ? 8.418   25.648 63.656  1.00 70.50  ? 214 ASP B O   1 
ATOM   4806 C  CB  . ASP B 1 185 ? 8.867   27.465 61.496  1.00 72.78  ? 214 ASP B CB  1 
ATOM   4807 C  CG  . ASP B 1 185 ? 10.082  28.075 62.188  1.00 79.86  ? 214 ASP B CG  1 
ATOM   4808 O  OD1 . ASP B 1 185 ? 9.952   29.195 62.756  1.00 80.95  ? 214 ASP B OD1 1 
ATOM   4809 O  OD2 . ASP B 1 185 ? 11.162  27.432 62.168  1.00 82.88  ? 214 ASP B OD2 1 
ATOM   4810 N  N   . MET B 1 186 ? 7.375   27.276 64.820  1.00 68.62  ? 215 MET B N   1 
ATOM   4811 C  CA  . MET B 1 186 ? 7.565   26.679 66.130  1.00 67.88  ? 215 MET B CA  1 
ATOM   4812 C  C   . MET B 1 186 ? 6.263   26.677 66.918  1.00 66.93  ? 215 MET B C   1 
ATOM   4813 O  O   . MET B 1 186 ? 5.688   27.738 67.151  1.00 67.01  ? 215 MET B O   1 
ATOM   4814 C  CB  . MET B 1 186 ? 8.631   27.472 66.899  1.00 68.53  ? 215 MET B CB  1 
ATOM   4815 C  CG  . MET B 1 186 ? 8.784   27.042 68.332  1.00 70.56  ? 215 MET B CG  1 
ATOM   4816 S  SD  . MET B 1 186 ? 9.971   28.061 69.176  1.00 74.43  ? 215 MET B SD  1 
ATOM   4817 C  CE  . MET B 1 186 ? 11.435  27.486 68.416  1.00 74.15  ? 215 MET B CE  1 
ATOM   4818 N  N   . MET B 1 187 ? 5.836   25.499 67.383  1.00 66.07  ? 216 MET B N   1 
ATOM   4819 C  CA  . MET B 1 187 ? 4.622   25.394 68.178  1.00 65.75  ? 216 MET B CA  1 
ATOM   4820 C  C   . MET B 1 187 ? 4.925   25.346 69.671  1.00 65.57  ? 216 MET B C   1 
ATOM   4821 O  O   . MET B 1 187 ? 5.783   24.581 70.121  1.00 65.83  ? 216 MET B O   1 
ATOM   4822 C  CB  . MET B 1 187 ? 3.802   24.171 67.767  1.00 66.12  ? 216 MET B CB  1 
ATOM   4823 C  CG  . MET B 1 187 ? 2.423   24.160 68.367  1.00 67.58  ? 216 MET B CG  1 
ATOM   4824 S  SD  . MET B 1 187 ? 1.425   25.588 67.872  1.00 69.44  ? 216 MET B SD  1 
ATOM   4825 C  CE  . MET B 1 187 ? 0.064   25.361 68.872  1.00 66.72  ? 216 MET B CE  1 
ATOM   4826 N  N   . LEU B 1 188 ? 4.216   26.169 70.445  1.00 64.94  ? 217 LEU B N   1 
ATOM   4827 C  CA  . LEU B 1 188 ? 4.401   26.212 71.885  1.00 64.57  ? 217 LEU B CA  1 
ATOM   4828 C  C   . LEU B 1 188 ? 3.141   25.816 72.623  1.00 63.98  ? 217 LEU B C   1 
ATOM   4829 O  O   . LEU B 1 188 ? 2.030   26.116 72.177  1.00 64.07  ? 217 LEU B O   1 
ATOM   4830 C  CB  . LEU B 1 188 ? 4.850   27.596 72.329  1.00 64.88  ? 217 LEU B CB  1 
ATOM   4831 C  CG  . LEU B 1 188 ? 6.190   28.050 71.791  1.00 66.39  ? 217 LEU B CG  1 
ATOM   4832 C  CD1 . LEU B 1 188 ? 6.440   29.491 72.152  1.00 66.96  ? 217 LEU B CD1 1 
ATOM   4833 C  CD2 . LEU B 1 188 ? 7.310   27.172 72.321  1.00 67.05  ? 217 LEU B CD2 1 
ATOM   4834 N  N   . THR B 1 189 ? 3.328   25.109 73.741  1.00 63.28  ? 218 THR B N   1 
ATOM   4835 C  CA  . THR B 1 189 ? 2.281   24.634 74.645  1.00 63.02  ? 218 THR B CA  1 
ATOM   4836 C  C   . THR B 1 189 ? 2.751   25.106 76.000  1.00 62.85  ? 218 THR B C   1 
ATOM   4837 O  O   . THR B 1 189 ? 3.718   24.562 76.526  1.00 62.83  ? 218 THR B O   1 
ATOM   4838 C  CB  . THR B 1 189 ? 2.204   23.113 74.600  1.00 63.70  ? 218 THR B CB  1 
ATOM   4839 O  OG1 . THR B 1 189 ? 2.081   22.689 73.239  1.00 64.23  ? 218 THR B OG1 1 
ATOM   4840 C  CG2 . THR B 1 189 ? 1.065   22.573 75.432  1.00 63.94  ? 218 THR B CG2 1 
ATOM   4841 N  N   . ASN B 1 190 ? 2.166   26.197 76.498  1.00 62.61  ? 219 ASN B N   1 
ATOM   4842 C  CA  . ASN B 1 190 ? 2.597   26.862 77.722  1.00 62.88  ? 219 ASN B CA  1 
ATOM   4843 C  C   . ASN B 1 190 ? 4.062   27.352 77.609  1.00 63.56  ? 219 ASN B C   1 
ATOM   4844 O  O   . ASN B 1 190 ? 4.789   27.361 78.600  1.00 63.91  ? 219 ASN B O   1 
ATOM   4845 C  CB  . ASN B 1 190 ? 2.326   26.004 78.965  1.00 63.45  ? 219 ASN B CB  1 
ATOM   4846 C  CG  . ASN B 1 190 ? 0.843   25.822 79.250  1.00 65.73  ? 219 ASN B CG  1 
ATOM   4847 O  OD1 . ASN B 1 190 ? -0.015  26.252 78.476  1.00 66.99  ? 219 ASN B OD1 1 
ATOM   4848 N  ND2 . ASN B 1 190 ? 0.491   25.184 80.365  1.00 65.38  ? 219 ASN B ND2 1 
ATOM   4849 N  N   . GLY B 1 191 ? 4.451   27.787 76.401  1.00 63.51  ? 220 GLY B N   1 
ATOM   4850 C  CA  . GLY B 1 191 ? 5.792   28.262 76.079  1.00 63.99  ? 220 GLY B CA  1 
ATOM   4851 C  C   . GLY B 1 191 ? 6.823   27.150 75.988  1.00 64.35  ? 220 GLY B C   1 
ATOM   4852 O  O   . GLY B 1 191 ? 8.011   27.370 76.226  1.00 64.32  ? 220 GLY B O   1 
ATOM   4853 N  N   . THR B 1 192 ? 6.380   25.938 75.650  1.00 64.33  ? 221 THR B N   1 
ATOM   4854 C  CA  . THR B 1 192 ? 7.253   24.777 75.612  1.00 64.73  ? 221 THR B CA  1 
ATOM   4855 C  C   . THR B 1 192 ? 7.035   23.993 74.355  1.00 64.94  ? 221 THR B C   1 
ATOM   4856 O  O   . THR B 1 192 ? 5.888   23.774 73.959  1.00 65.36  ? 221 THR B O   1 
ATOM   4857 C  CB  . THR B 1 192 ? 6.926   23.889 76.802  1.00 66.38  ? 221 THR B CB  1 
ATOM   4858 O  OG1 . THR B 1 192 ? 7.130   24.630 77.995  1.00 67.73  ? 221 THR B OG1 1 
ATOM   4859 C  CG2 . THR B 1 192 ? 7.776   22.681 76.852  1.00 67.05  ? 221 THR B CG2 1 
ATOM   4860 N  N   . VAL B 1 193 ? 8.120   23.537 73.736  1.00 64.66  ? 222 VAL B N   1 
ATOM   4861 C  CA  . VAL B 1 193 ? 7.996   22.757 72.517  1.00 64.85  ? 222 VAL B CA  1 
ATOM   4862 C  C   . VAL B 1 193 ? 7.642   21.312 72.817  1.00 65.01  ? 222 VAL B C   1 
ATOM   4863 O  O   . VAL B 1 193 ? 8.493   20.557 73.296  1.00 64.82  ? 222 VAL B O   1 
ATOM   4864 C  CB  . VAL B 1 193 ? 9.222   22.894 71.600  1.00 64.88  ? 222 VAL B CB  1 
ATOM   4865 C  CG1 . VAL B 1 193 ? 9.057   22.029 70.363  1.00 65.09  ? 222 VAL B CG1 1 
ATOM   4866 C  CG2 . VAL B 1 193 ? 9.430   24.352 71.215  1.00 65.08  ? 222 VAL B CG2 1 
ATOM   4867 N  N   . TYR B 1 194 ? 6.365   20.948 72.556  1.00 65.12  ? 223 TYR B N   1 
ATOM   4868 C  CA  . TYR B 1 194 ? 5.829   19.592 72.735  1.00 65.90  ? 223 TYR B CA  1 
ATOM   4869 C  C   . TYR B 1 194 ? 6.156   19.005 74.116  1.00 65.54  ? 223 TYR B C   1 
ATOM   4870 O  O   . TYR B 1 194 ? 6.956   18.075 74.232  1.00 65.70  ? 223 TYR B O   1 
ATOM   4871 C  CB  . TYR B 1 194 ? 6.328   18.694 71.583  1.00 66.49  ? 223 TYR B CB  1 
ATOM   4872 C  CG  . TYR B 1 194 ? 5.808   17.273 71.517  1.00 68.03  ? 223 TYR B CG  1 
ATOM   4873 C  CD1 . TYR B 1 194 ? 4.624   16.910 72.143  1.00 69.38  ? 223 TYR B CD1 1 
ATOM   4874 C  CD2 . TYR B 1 194 ? 6.461   16.313 70.758  1.00 69.19  ? 223 TYR B CD2 1 
ATOM   4875 C  CE1 . TYR B 1 194 ? 4.149   15.605 72.082  1.00 70.53  ? 223 TYR B CE1 1 
ATOM   4876 C  CE2 . TYR B 1 194 ? 5.983   15.015 70.667  1.00 70.17  ? 223 TYR B CE2 1 
ATOM   4877 C  CZ  . TYR B 1 194 ? 4.827   14.663 71.331  1.00 71.34  ? 223 TYR B CZ  1 
ATOM   4878 O  OH  . TYR B 1 194 ? 4.370   13.374 71.228  1.00 72.86  ? 223 TYR B OH  1 
ATOM   4879 N  N   . PRO B 1 195 ? 5.540   19.545 75.178  1.00 64.79  ? 224 PRO B N   1 
ATOM   4880 C  CA  . PRO B 1 195 ? 5.826   19.025 76.522  1.00 64.27  ? 224 PRO B CA  1 
ATOM   4881 C  C   . PRO B 1 195 ? 5.029   17.760 76.876  1.00 63.92  ? 224 PRO B C   1 
ATOM   4882 O  O   . PRO B 1 195 ? 4.148   17.334 76.127  1.00 63.89  ? 224 PRO B O   1 
ATOM   4883 C  CB  . PRO B 1 195 ? 5.462   20.205 77.426  1.00 64.87  ? 224 PRO B CB  1 
ATOM   4884 C  CG  . PRO B 1 195 ? 4.410   20.947 76.686  1.00 65.29  ? 224 PRO B CG  1 
ATOM   4885 C  CD  . PRO B 1 195 ? 4.577   20.667 75.215  1.00 64.12  ? 224 PRO B CD  1 
ATOM   4886 N  N   . GLN B 1 196 ? 5.343   17.161 78.022  1.00 63.47  ? 225 GLN B N   1 
ATOM   4887 C  CA  . GLN B 1 196 ? 4.630   15.993 78.509  1.00 63.35  ? 225 GLN B CA  1 
ATOM   4888 C  C   . GLN B 1 196 ? 3.925   16.334 79.839  1.00 62.21  ? 225 GLN B C   1 
ATOM   4889 O  O   . GLN B 1 196 ? 4.416   17.169 80.596  1.00 62.38  ? 225 GLN B O   1 
ATOM   4890 C  CB  . GLN B 1 196 ? 5.614   14.844 78.727  1.00 65.75  ? 225 GLN B CB  1 
ATOM   4891 C  CG  . GLN B 1 196 ? 4.950   13.477 78.692  1.00 71.00  ? 225 GLN B CG  1 
ATOM   4892 C  CD  . GLN B 1 196 ? 5.452   12.576 79.793  1.00 76.60  ? 225 GLN B CD  1 
ATOM   4893 O  OE1 . GLN B 1 196 ? 5.625   13.004 80.942  1.00 78.48  ? 225 GLN B OE1 1 
ATOM   4894 N  NE2 . GLN B 1 196 ? 5.686   11.305 79.468  1.00 77.29  ? 225 GLN B NE2 1 
ATOM   4895 N  N   . HIS B 1 197 ? 2.767   15.720 80.107  1.00 60.82  ? 226 HIS B N   1 
ATOM   4896 C  CA  . HIS B 1 197 ? 2.075   15.917 81.369  1.00 60.44  ? 226 HIS B CA  1 
ATOM   4897 C  C   . HIS B 1 197 ? 1.626   14.565 81.912  1.00 60.36  ? 226 HIS B C   1 
ATOM   4898 O  O   . HIS B 1 197 ? 1.104   13.736 81.168  1.00 60.46  ? 226 HIS B O   1 
ATOM   4899 C  CB  . HIS B 1 197 ? 0.893   16.909 81.265  1.00 60.45  ? 226 HIS B CB  1 
ATOM   4900 C  CG  . HIS B 1 197 ? 0.121   17.035 82.550  1.00 60.19  ? 226 HIS B CG  1 
ATOM   4901 N  ND1 . HIS B 1 197 ? 0.682   17.615 83.675  1.00 61.21  ? 226 HIS B ND1 1 
ATOM   4902 C  CD2 . HIS B 1 197 ? -1.117  16.592 82.863  1.00 60.74  ? 226 HIS B CD2 1 
ATOM   4903 C  CE1 . HIS B 1 197 ? -0.232  17.518 84.626  1.00 61.24  ? 226 HIS B CE1 1 
ATOM   4904 N  NE2 . HIS B 1 197 ? -1.329  16.911 84.188  1.00 61.44  ? 226 HIS B NE2 1 
ATOM   4905 N  N   . LEU B 1 198 ? 1.851   14.339 83.205  1.00 60.00  ? 227 LEU B N   1 
ATOM   4906 C  CA  . LEU B 1 198 ? 1.455   13.103 83.861  1.00 60.29  ? 227 LEU B CA  1 
ATOM   4907 C  C   . LEU B 1 198 ? 0.124   13.333 84.553  1.00 60.69  ? 227 LEU B C   1 
ATOM   4908 O  O   . LEU B 1 198 ? 0.014   14.249 85.371  1.00 61.13  ? 227 LEU B O   1 
ATOM   4909 C  CB  . LEU B 1 198 ? 2.497   12.726 84.918  1.00 60.38  ? 227 LEU B CB  1 
ATOM   4910 C  CG  . LEU B 1 198 ? 3.901   12.427 84.427  1.00 61.44  ? 227 LEU B CG  1 
ATOM   4911 C  CD1 . LEU B 1 198 ? 4.813   12.166 85.600  1.00 62.13  ? 227 LEU B CD1 1 
ATOM   4912 C  CD2 . LEU B 1 198 ? 3.910   11.256 83.478  1.00 61.62  ? 227 LEU B CD2 1 
ATOM   4913 N  N   . ALA B 1 199 ? -0.869  12.481 84.290  1.00 60.39  ? 228 ALA B N   1 
ATOM   4914 C  CA  . ALA B 1 199 ? -2.183  12.655 84.905  1.00 60.44  ? 228 ALA B CA  1 
ATOM   4915 C  C   . ALA B 1 199 ? -2.780  11.350 85.461  1.00 59.97  ? 228 ALA B C   1 
ATOM   4916 O  O   . ALA B 1 199 ? -2.495  10.267 84.952  1.00 59.82  ? 228 ALA B O   1 
ATOM   4917 C  CB  . ALA B 1 199 ? -3.125  13.285 83.896  1.00 60.80  ? 228 ALA B CB  1 
ATOM   4918 N  N   . PRO B 1 200 ? -3.621  11.433 86.509  1.00 59.34  ? 229 PRO B N   1 
ATOM   4919 C  CA  . PRO B 1 200 ? -4.233  10.206 87.040  1.00 58.75  ? 229 PRO B CA  1 
ATOM   4920 C  C   . PRO B 1 200 ? -5.239  9.578  86.070  1.00 58.26  ? 229 PRO B C   1 
ATOM   4921 O  O   . PRO B 1 200 ? -5.804  10.257 85.217  1.00 57.86  ? 229 PRO B O   1 
ATOM   4922 C  CB  . PRO B 1 200 ? -4.928  10.681 88.315  1.00 59.38  ? 229 PRO B CB  1 
ATOM   4923 C  CG  . PRO B 1 200 ? -5.217  12.123 88.074  1.00 60.06  ? 229 PRO B CG  1 
ATOM   4924 C  CD  . PRO B 1 200 ? -4.077  12.636 87.241  1.00 58.75  ? 229 PRO B CD  1 
ATOM   4925 N  N   . ARG B 1 201 ? -5.446  8.266  86.205  1.00 57.96  ? 230 ARG B N   1 
ATOM   4926 C  CA  . ARG B 1 201 ? -6.421  7.542  85.413  1.00 58.09  ? 230 ARG B CA  1 
ATOM   4927 C  C   . ARG B 1 201 ? -7.830  7.954  85.871  1.00 57.59  ? 230 ARG B C   1 
ATOM   4928 O  O   . ARG B 1 201 ? -8.071  8.204  87.044  1.00 57.49  ? 230 ARG B O   1 
ATOM   4929 C  CB  . ARG B 1 201 ? -6.218  6.032  85.548  1.00 59.83  ? 230 ARG B CB  1 
ATOM   4930 C  CG  . ARG B 1 201 ? -4.892  5.563  85.023  1.00 64.20  ? 230 ARG B CG  1 
ATOM   4931 C  CD  . ARG B 1 201 ? -4.459  4.290  85.709  1.00 69.87  ? 230 ARG B CD  1 
ATOM   4932 N  NE  . ARG B 1 201 ? -3.175  3.825  85.188  1.00 75.64  ? 230 ARG B NE  1 
ATOM   4933 C  CZ  . ARG B 1 201 ? -3.033  2.808  84.342  1.00 79.74  ? 230 ARG B CZ  1 
ATOM   4934 N  NH1 . ARG B 1 201 ? -4.095  2.113  83.940  1.00 79.55  ? 230 ARG B NH1 1 
ATOM   4935 N  NH2 . ARG B 1 201 ? -1.824  2.461  83.908  1.00 79.96  ? 230 ARG B NH2 1 
ATOM   4936 N  N   . GLY B 1 202 ? -8.737  8.045  84.928  1.00 57.13  ? 231 GLY B N   1 
ATOM   4937 C  CA  . GLY B 1 202 ? -10.088 8.491  85.179  1.00 57.33  ? 231 GLY B CA  1 
ATOM   4938 C  C   . GLY B 1 202 ? -10.389 9.516  84.117  1.00 57.74  ? 231 GLY B C   1 
ATOM   4939 O  O   . GLY B 1 202 ? -10.410 9.187  82.927  1.00 57.80  ? 231 GLY B O   1 
ATOM   4940 N  N   . TRP B 1 203 ? -10.539 10.777 84.527  1.00 57.68  ? 232 TRP B N   1 
ATOM   4941 C  CA  . TRP B 1 203 ? -10.782 11.842 83.567  1.00 58.00  ? 232 TRP B CA  1 
ATOM   4942 C  C   . TRP B 1 203 ? -9.719  12.930 83.659  1.00 58.46  ? 232 TRP B C   1 
ATOM   4943 O  O   . TRP B 1 203 ? -9.071  13.098 84.697  1.00 58.68  ? 232 TRP B O   1 
ATOM   4944 C  CB  . TRP B 1 203 ? -12.205 12.391 83.698  1.00 57.82  ? 232 TRP B CB  1 
ATOM   4945 C  CG  . TRP B 1 203 ? -13.248 11.406 83.262  1.00 58.66  ? 232 TRP B CG  1 
ATOM   4946 C  CD1 . TRP B 1 203 ? -13.887 10.486 84.042  1.00 59.75  ? 232 TRP B CD1 1 
ATOM   4947 C  CD2 . TRP B 1 203 ? -13.721 11.196 81.923  1.00 58.87  ? 232 TRP B CD2 1 
ATOM   4948 N  NE1 . TRP B 1 203 ? -14.750 9.732  83.275  1.00 59.94  ? 232 TRP B NE1 1 
ATOM   4949 C  CE2 . TRP B 1 203 ? -14.675 10.155 81.973  1.00 59.44  ? 232 TRP B CE2 1 
ATOM   4950 C  CE3 . TRP B 1 203 ? -13.444 11.798 80.689  1.00 59.41  ? 232 TRP B CE3 1 
ATOM   4951 C  CZ2 . TRP B 1 203 ? -15.340 9.701  80.839  1.00 59.72  ? 232 TRP B CZ2 1 
ATOM   4952 C  CZ3 . TRP B 1 203 ? -14.101 11.340 79.568  1.00 59.97  ? 232 TRP B CZ3 1 
ATOM   4953 C  CH2 . TRP B 1 203 ? -15.042 10.309 79.651  1.00 59.87  ? 232 TRP B CH2 1 
ATOM   4954 N  N   . LEU B 1 204 ? -9.499  13.634 82.555  1.00 58.32  ? 233 LEU B N   1 
ATOM   4955 C  CA  . LEU B 1 204 ? -8.518  14.717 82.526  1.00 58.36  ? 233 LEU B CA  1 
ATOM   4956 C  C   . LEU B 1 204 ? -9.157  15.918 81.852  1.00 57.69  ? 233 LEU B C   1 
ATOM   4957 O  O   . LEU B 1 204 ? -9.641  15.811 80.738  1.00 57.71  ? 233 LEU B O   1 
ATOM   4958 C  CB  . LEU B 1 204 ? -7.220  14.273 81.816  1.00 58.71  ? 233 LEU B CB  1 
ATOM   4959 C  CG  . LEU B 1 204 ? -6.217  15.371 81.479  1.00 60.13  ? 233 LEU B CG  1 
ATOM   4960 C  CD1 . LEU B 1 204 ? -5.704  16.059 82.728  1.00 60.83  ? 233 LEU B CD1 1 
ATOM   4961 C  CD2 . LEU B 1 204 ? -5.073  14.811 80.689  1.00 60.53  ? 233 LEU B CD2 1 
ATOM   4962 N  N   . ARG B 1 205 ? -9.211  17.039 82.544  1.00 57.26  ? 234 ARG B N   1 
ATOM   4963 C  CA  . ARG B 1 205 ? -9.822  18.255 82.028  1.00 57.59  ? 234 ARG B CA  1 
ATOM   4964 C  C   . ARG B 1 205 ? -8.744  19.196 81.500  1.00 58.17  ? 234 ARG B C   1 
ATOM   4965 O  O   . ARG B 1 205 ? -7.860  19.617 82.253  1.00 58.56  ? 234 ARG B O   1 
ATOM   4966 C  CB  . ARG B 1 205 ? -10.628 18.913 83.149  1.00 58.53  ? 234 ARG B CB  1 
ATOM   4967 C  CG  . ARG B 1 205 ? -11.165 20.304 82.878  1.00 60.66  ? 234 ARG B CG  1 
ATOM   4968 C  CD  . ARG B 1 205 ? -11.618 20.852 84.210  1.00 62.99  ? 234 ARG B CD  1 
ATOM   4969 N  NE  . ARG B 1 205 ? -12.691 21.838 84.117  1.00 64.89  ? 234 ARG B NE  1 
ATOM   4970 C  CZ  . ARG B 1 205 ? -13.345 22.326 85.168  1.00 66.96  ? 234 ARG B CZ  1 
ATOM   4971 N  NH1 . ARG B 1 205 ? -13.051 21.911 86.395  1.00 66.68  ? 234 ARG B NH1 1 
ATOM   4972 N  NH2 . ARG B 1 205 ? -14.303 23.225 85.001  1.00 67.02  ? 234 ARG B NH2 1 
ATOM   4973 N  N   . LEU B 1 206 ? -8.791  19.488 80.192  1.00 57.82  ? 235 LEU B N   1 
ATOM   4974 C  CA  . LEU B 1 206 ? -7.832  20.378 79.543  1.00 57.83  ? 235 LEU B CA  1 
ATOM   4975 C  C   . LEU B 1 206 ? -8.532  21.680 79.180  1.00 57.59  ? 235 LEU B C   1 
ATOM   4976 O  O   . LEU B 1 206 ? -9.537  21.676 78.455  1.00 57.68  ? 235 LEU B O   1 
ATOM   4977 C  CB  . LEU B 1 206 ? -7.273  19.732 78.265  1.00 57.91  ? 235 LEU B CB  1 
ATOM   4978 C  CG  . LEU B 1 206 ? -6.643  18.368 78.430  1.00 59.19  ? 235 LEU B CG  1 
ATOM   4979 C  CD1 . LEU B 1 206 ? -6.498  17.677 77.104  1.00 59.24  ? 235 LEU B CD1 1 
ATOM   4980 C  CD2 . LEU B 1 206 ? -5.319  18.470 79.129  1.00 59.97  ? 235 LEU B CD2 1 
ATOM   4981 N  N   . ARG B 1 207 ? -8.007  22.788 79.677  1.00 57.20  ? 236 ARG B N   1 
ATOM   4982 C  CA  . ARG B 1 207 ? -8.570  24.094 79.375  1.00 57.61  ? 236 ARG B CA  1 
ATOM   4983 C  C   . ARG B 1 207 ? -7.764  24.655 78.202  1.00 57.90  ? 236 ARG B C   1 
ATOM   4984 O  O   . ARG B 1 207 ? -6.708  25.247 78.404  1.00 58.42  ? 236 ARG B O   1 
ATOM   4985 C  CB  . ARG B 1 207 ? -8.498  25.019 80.604  1.00 58.36  ? 236 ARG B CB  1 
ATOM   4986 C  CG  . ARG B 1 207 ? -9.243  24.495 81.827  1.00 60.23  ? 236 ARG B CG  1 
ATOM   4987 C  CD  . ARG B 1 207 ? -8.994  25.442 82.976  1.00 63.35  ? 236 ARG B CD  1 
ATOM   4988 N  NE  . ARG B 1 207 ? -9.633  25.036 84.225  1.00 66.27  ? 236 ARG B NE  1 
ATOM   4989 C  CZ  . ARG B 1 207 ? -10.743 25.581 84.717  1.00 69.00  ? 236 ARG B CZ  1 
ATOM   4990 N  NH1 . ARG B 1 207 ? -11.371 26.543 84.053  1.00 69.54  ? 236 ARG B NH1 1 
ATOM   4991 N  NH2 . ARG B 1 207 ? -11.244 25.155 85.869  1.00 68.76  ? 236 ARG B NH2 1 
ATOM   4992 N  N   . PHE B 1 208 ? -8.235  24.425 76.978  1.00 57.10  ? 237 PHE B N   1 
ATOM   4993 C  CA  . PHE B 1 208 ? -7.528  24.856 75.784  1.00 56.76  ? 237 PHE B CA  1 
ATOM   4994 C  C   . PHE B 1 208 ? -7.721  26.326 75.443  1.00 56.08  ? 237 PHE B C   1 
ATOM   4995 O  O   . PHE B 1 208 ? -8.850  26.789 75.348  1.00 56.22  ? 237 PHE B O   1 
ATOM   4996 C  CB  . PHE B 1 208 ? -7.991  24.017 74.594  1.00 56.87  ? 237 PHE B CB  1 
ATOM   4997 C  CG  . PHE B 1 208 ? -7.471  22.604 74.579  1.00 57.61  ? 237 PHE B CG  1 
ATOM   4998 C  CD1 . PHE B 1 208 ? -6.118  22.351 74.463  1.00 58.46  ? 237 PHE B CD1 1 
ATOM   4999 C  CD2 . PHE B 1 208 ? -8.339  21.530 74.604  1.00 58.46  ? 237 PHE B CD2 1 
ATOM   5000 C  CE1 . PHE B 1 208 ? -5.639  21.050 74.414  1.00 59.11  ? 237 PHE B CE1 1 
ATOM   5001 C  CE2 . PHE B 1 208 ? -7.854  20.228 74.554  1.00 59.33  ? 237 PHE B CE2 1 
ATOM   5002 C  CZ  . PHE B 1 208 ? -6.509  19.998 74.440  1.00 58.96  ? 237 PHE B CZ  1 
ATOM   5003 N  N   . LEU B 1 209 ? -6.619  27.043 75.201  1.00 55.12  ? 238 LEU B N   1 
ATOM   5004 C  CA  . LEU B 1 209 ? -6.658  28.433 74.769  1.00 54.91  ? 238 LEU B CA  1 
ATOM   5005 C  C   . LEU B 1 209 ? -5.783  28.531 73.537  1.00 55.29  ? 238 LEU B C   1 
ATOM   5006 O  O   . LEU B 1 209 ? -4.608  28.197 73.617  1.00 55.81  ? 238 LEU B O   1 
ATOM   5007 C  CB  . LEU B 1 209 ? -6.122  29.384 75.852  1.00 54.70  ? 238 LEU B CB  1 
ATOM   5008 C  CG  . LEU B 1 209 ? -5.667  30.804 75.405  1.00 55.80  ? 238 LEU B CG  1 
ATOM   5009 C  CD1 . LEU B 1 209 ? -6.820  31.639 74.895  1.00 55.82  ? 238 LEU B CD1 1 
ATOM   5010 C  CD2 . LEU B 1 209 ? -4.930  31.529 76.519  1.00 56.63  ? 238 LEU B CD2 1 
ATOM   5011 N  N   . ASN B 1 210 ? -6.330  29.018 72.416  1.00 54.81  ? 239 ASN B N   1 
ATOM   5012 C  CA  . ASN B 1 210 ? -5.530  29.247 71.224  1.00 54.67  ? 239 ASN B CA  1 
ATOM   5013 C  C   . ASN B 1 210 ? -4.994  30.665 71.389  1.00 55.08  ? 239 ASN B C   1 
ATOM   5014 O  O   . ASN B 1 210 ? -5.725  31.627 71.158  1.00 55.35  ? 239 ASN B O   1 
ATOM   5015 C  CB  . ASN B 1 210 ? -6.391  29.134 69.973  1.00 55.07  ? 239 ASN B CB  1 
ATOM   5016 C  CG  . ASN B 1 210 ? -5.706  29.527 68.683  1.00 56.68  ? 239 ASN B CG  1 
ATOM   5017 O  OD1 . ASN B 1 210 ? -4.611  30.097 68.667  1.00 56.98  ? 239 ASN B OD1 1 
ATOM   5018 N  ND2 . ASN B 1 210 ? -6.355  29.246 67.561  1.00 56.50  ? 239 ASN B ND2 1 
ATOM   5019 N  N   . GLY B 1 211 ? -3.744  30.777 71.830  1.00 54.99  ? 240 GLY B N   1 
ATOM   5020 C  CA  . GLY B 1 211 ? -3.090  32.057 72.043  1.00 55.74  ? 240 GLY B CA  1 
ATOM   5021 C  C   . GLY B 1 211 ? -2.283  32.554 70.858  1.00 56.94  ? 240 GLY B C   1 
ATOM   5022 O  O   . GLY B 1 211 ? -1.452  33.455 71.020  1.00 57.40  ? 240 GLY B O   1 
ATOM   5023 N  N   . CYS B 1 212 ? -2.513  31.975 69.648  1.00 56.99  ? 241 CYS B N   1 
ATOM   5024 C  CA  . CYS B 1 212 ? -1.812  32.391 68.433  1.00 57.18  ? 241 CYS B CA  1 
ATOM   5025 C  C   . CYS B 1 212 ? -2.326  33.739 67.986  1.00 58.36  ? 241 CYS B C   1 
ATOM   5026 O  O   . CYS B 1 212 ? -3.518  34.013 68.121  1.00 58.76  ? 241 CYS B O   1 
ATOM   5027 C  CB  . CYS B 1 212 ? -1.976  31.367 67.316  1.00 56.87  ? 241 CYS B CB  1 
ATOM   5028 S  SG  . CYS B 1 212 ? -1.481  29.685 67.752  1.00 57.29  ? 241 CYS B SG  1 
ATOM   5029 N  N   . ASN B 1 213 ? -1.455  34.558 67.390  1.00 58.88  ? 242 ASN B N   1 
ATOM   5030 C  CA  . ASN B 1 213 ? -1.869  35.862 66.882  1.00 59.70  ? 242 ASN B CA  1 
ATOM   5031 C  C   . ASN B 1 213 ? -2.788  35.700 65.676  1.00 60.37  ? 242 ASN B C   1 
ATOM   5032 O  O   . ASN B 1 213 ? -3.779  36.418 65.556  1.00 60.64  ? 242 ASN B O   1 
ATOM   5033 C  CB  . ASN B 1 213 ? -0.660  36.683 66.459  1.00 60.99  ? 242 ASN B CB  1 
ATOM   5034 C  CG  . ASN B 1 213 ? 0.278   36.997 67.566  1.00 64.54  ? 242 ASN B CG  1 
ATOM   5035 O  OD1 . ASN B 1 213 ? 0.361   36.279 68.563  1.00 65.96  ? 242 ASN B OD1 1 
ATOM   5036 N  ND2 . ASN B 1 213 ? 1.014   38.074 67.405  1.00 65.42  ? 242 ASN B ND2 1 
ATOM   5037 N  N   . ALA B 1 214 ? -2.463  34.753 64.787  1.00 60.41  ? 243 ALA B N   1 
ATOM   5038 C  CA  . ALA B 1 214 ? -3.237  34.566 63.579  1.00 61.12  ? 243 ALA B CA  1 
ATOM   5039 C  C   . ALA B 1 214 ? -3.584  33.113 63.280  1.00 61.88  ? 243 ALA B C   1 
ATOM   5040 O  O   . ALA B 1 214 ? -4.508  32.861 62.505  1.00 62.64  ? 243 ALA B O   1 
ATOM   5041 C  CB  . ALA B 1 214 ? -2.469  35.148 62.406  1.00 61.22  ? 243 ALA B CB  1 
ATOM   5042 N  N   . ARG B 1 215 ? -2.820  32.159 63.818  1.00 61.30  ? 244 ARG B N   1 
ATOM   5043 C  CA  . ARG B 1 215 ? -3.028  30.749 63.500  1.00 60.91  ? 244 ARG B CA  1 
ATOM   5044 C  C   . ARG B 1 215 ? -4.255  30.108 64.128  1.00 61.04  ? 244 ARG B C   1 
ATOM   5045 O  O   . ARG B 1 215 ? -4.369  30.076 65.345  1.00 61.56  ? 244 ARG B O   1 
ATOM   5046 C  CB  . ARG B 1 215 ? -1.773  29.945 63.865  1.00 61.22  ? 244 ARG B CB  1 
ATOM   5047 C  CG  . ARG B 1 215 ? -1.892  28.444 63.641  1.00 62.77  ? 244 ARG B CG  1 
ATOM   5048 C  CD  . ARG B 1 215 ? -0.564  27.756 63.850  1.00 64.80  ? 244 ARG B CD  1 
ATOM   5049 N  NE  . ARG B 1 215 ? 0.479   28.318 62.997  1.00 66.71  ? 244 ARG B NE  1 
ATOM   5050 C  CZ  . ARG B 1 215 ? 0.716   27.937 61.746  1.00 69.13  ? 244 ARG B CZ  1 
ATOM   5051 N  NH1 . ARG B 1 215 ? 0.007   26.956 61.198  1.00 68.73  ? 244 ARG B NH1 1 
ATOM   5052 N  NH2 . ARG B 1 215 ? 1.686   28.509 61.045  1.00 69.10  ? 244 ARG B NH2 1 
ATOM   5053 N  N   . SER B 1 216 ? -5.127  29.522 63.308  1.00 60.86  ? 245 SER B N   1 
ATOM   5054 C  CA  . SER B 1 216 ? -6.255  28.748 63.828  1.00 61.58  ? 245 SER B CA  1 
ATOM   5055 C  C   . SER B 1 216 ? -5.781  27.289 63.989  1.00 61.97  ? 245 SER B C   1 
ATOM   5056 O  O   . SER B 1 216 ? -4.856  26.857 63.292  1.00 62.33  ? 245 SER B O   1 
ATOM   5057 C  CB  . SER B 1 216 ? -7.469  28.831 62.910  1.00 63.12  ? 245 SER B CB  1 
ATOM   5058 O  OG  . SER B 1 216 ? -7.238  28.166 61.680  1.00 65.90  ? 245 SER B OG  1 
ATOM   5059 N  N   . LEU B 1 217 ? -6.364  26.546 64.939  1.00 61.77  ? 246 LEU B N   1 
ATOM   5060 C  CA  . LEU B 1 217 ? -5.927  25.176 65.204  1.00 62.39  ? 246 LEU B CA  1 
ATOM   5061 C  C   . LEU B 1 217 ? -7.064  24.162 65.123  1.00 63.25  ? 246 LEU B C   1 
ATOM   5062 O  O   . LEU B 1 217 ? -8.227  24.552 65.195  1.00 63.83  ? 246 LEU B O   1 
ATOM   5063 C  CB  . LEU B 1 217 ? -5.249  25.125 66.583  1.00 62.58  ? 246 LEU B CB  1 
ATOM   5064 C  CG  . LEU B 1 217 ? -4.051  26.074 66.759  1.00 63.54  ? 246 LEU B CG  1 
ATOM   5065 C  CD1 . LEU B 1 217 ? -3.735  26.324 68.223  1.00 63.31  ? 246 LEU B CD1 1 
ATOM   5066 C  CD2 . LEU B 1 217 ? -2.853  25.580 65.989  1.00 64.25  ? 246 LEU B CD2 1 
ATOM   5067 N  N   . ASN B 1 218 ? -6.748  22.864 64.955  1.00 63.11  ? 247 ASN B N   1 
ATOM   5068 C  CA  . ASN B 1 218 ? -7.791  21.830 64.908  1.00 63.35  ? 247 ASN B CA  1 
ATOM   5069 C  C   . ASN B 1 218 ? -7.371  20.669 65.773  1.00 62.65  ? 247 ASN B C   1 
ATOM   5070 O  O   . ASN B 1 218 ? -6.688  19.766 65.310  1.00 63.14  ? 247 ASN B O   1 
ATOM   5071 C  CB  . ASN B 1 218 ? -8.078  21.354 63.485  1.00 65.22  ? 247 ASN B CB  1 
ATOM   5072 C  CG  . ASN B 1 218 ? -9.385  20.592 63.377  1.00 69.32  ? 247 ASN B CG  1 
ATOM   5073 O  OD1 . ASN B 1 218 ? -10.242 20.634 64.270  1.00 70.46  ? 247 ASN B OD1 1 
ATOM   5074 N  ND2 . ASN B 1 218 ? -9.577  19.886 62.276  1.00 70.24  ? 247 ASN B ND2 1 
ATOM   5075 N  N   . LEU B 1 219 ? -7.778  20.688 67.024  1.00 61.66  ? 248 LEU B N   1 
ATOM   5076 C  CA  . LEU B 1 219 ? -7.349  19.694 68.000  1.00 61.36  ? 248 LEU B CA  1 
ATOM   5077 C  C   . LEU B 1 219 ? -8.017  18.344 67.859  1.00 60.77  ? 248 LEU B C   1 
ATOM   5078 O  O   . LEU B 1 219 ? -9.174  18.248 67.507  1.00 60.55  ? 248 LEU B O   1 
ATOM   5079 C  CB  . LEU B 1 219 ? -7.502  20.227 69.425  1.00 61.54  ? 248 LEU B CB  1 
ATOM   5080 C  CG  . LEU B 1 219 ? -7.024  21.660 69.630  1.00 63.44  ? 248 LEU B CG  1 
ATOM   5081 C  CD1 . LEU B 1 219 ? -7.343  22.137 71.008  1.00 64.71  ? 248 LEU B CD1 1 
ATOM   5082 C  CD2 . LEU B 1 219 ? -5.543  21.812 69.317  1.00 63.85  ? 248 LEU B CD2 1 
ATOM   5083 N  N   . ALA B 1 220 ? -7.261  17.299 68.116  1.00 60.51  ? 249 ALA B N   1 
ATOM   5084 C  CA  . ALA B 1 220 ? -7.709  15.918 68.031  1.00 61.21  ? 249 ALA B CA  1 
ATOM   5085 C  C   . ALA B 1 220 ? -6.738  15.047 68.865  1.00 61.75  ? 249 ALA B C   1 
ATOM   5086 O  O   . ALA B 1 220 ? -5.736  15.557 69.357  1.00 61.79  ? 249 ALA B O   1 
ATOM   5087 C  CB  . ALA B 1 220 ? -7.714  15.468 66.559  1.00 61.48  ? 249 ALA B CB  1 
ATOM   5088 N  N   . THR B 1 221 ? -7.051  13.764 69.079  1.00 62.04  ? 250 THR B N   1 
ATOM   5089 C  CA  . THR B 1 221 ? -6.139  12.858 69.767  1.00 62.59  ? 250 THR B CA  1 
ATOM   5090 C  C   . THR B 1 221 ? -5.387  12.016 68.709  1.00 62.58  ? 250 THR B C   1 
ATOM   5091 O  O   . THR B 1 221 ? -5.885  11.784 67.606  1.00 62.26  ? 250 THR B O   1 
ATOM   5092 C  CB  . THR B 1 221 ? -6.892  12.007 70.780  1.00 64.08  ? 250 THR B CB  1 
ATOM   5093 O  OG1 . THR B 1 221 ? -7.955  11.361 70.092  1.00 65.48  ? 250 THR B OG1 1 
ATOM   5094 C  CG2 . THR B 1 221 ? -7.456  12.835 71.917  1.00 64.29  ? 250 THR B CG2 1 
ATOM   5095 N  N   . SER B 1 222 ? -4.180  11.584 69.048  1.00 62.62  ? 251 SER B N   1 
ATOM   5096 C  CA  . SER B 1 222 ? -3.357  10.786 68.153  1.00 63.05  ? 251 SER B CA  1 
ATOM   5097 C  C   . SER B 1 222 ? -3.958  9.408  67.908  1.00 63.50  ? 251 SER B C   1 
ATOM   5098 O  O   . SER B 1 222 ? -3.865  8.896  66.797  1.00 63.81  ? 251 SER B O   1 
ATOM   5099 C  CB  . SER B 1 222 ? -1.953  10.647 68.723  1.00 64.38  ? 251 SER B CB  1 
ATOM   5100 O  OG  . SER B 1 222 ? -2.015  10.158 70.051  1.00 66.70  ? 251 SER B OG  1 
ATOM   5101 N  N   . ASP B 1 223 ? -4.585  8.807  68.931  1.00 63.48  ? 252 ASP B N   1 
ATOM   5102 C  CA  . ASP B 1 223 ? -5.180  7.476  68.783  1.00 63.64  ? 252 ASP B CA  1 
ATOM   5103 C  C   . ASP B 1 223 ? -6.688  7.482  68.584  1.00 63.47  ? 252 ASP B C   1 
ATOM   5104 O  O   . ASP B 1 223 ? -7.357  6.516  68.956  1.00 63.52  ? 252 ASP B O   1 
ATOM   5105 C  CB  . ASP B 1 223 ? -4.793  6.546  69.943  1.00 65.69  ? 252 ASP B CB  1 
ATOM   5106 C  CG  . ASP B 1 223 ? -5.253  6.972  71.320  1.00 71.13  ? 252 ASP B CG  1 
ATOM   5107 O  OD1 . ASP B 1 223 ? -6.271  7.689  71.411  1.00 72.04  ? 252 ASP B OD1 1 
ATOM   5108 O  OD2 . ASP B 1 223 ? -4.597  6.577  72.310  1.00 74.02  ? 252 ASP B OD2 1 
ATOM   5109 N  N   . GLY B 1 224 ? -7.210  8.574  68.034  1.00 63.23  ? 253 GLY B N   1 
ATOM   5110 C  CA  . GLY B 1 224 ? -8.627  8.722  67.721  1.00 63.37  ? 253 GLY B CA  1 
ATOM   5111 C  C   . GLY B 1 224 ? -9.623  8.793  68.867  1.00 63.01  ? 253 GLY B C   1 
ATOM   5112 O  O   . GLY B 1 224 ? -10.822 8.960  68.620  1.00 63.29  ? 253 GLY B O   1 
ATOM   5113 N  N   . ARG B 1 225 ? -9.159  8.705  70.127  1.00 62.19  ? 254 ARG B N   1 
ATOM   5114 C  CA  . ARG B 1 225 ? -10.064 8.785  71.272  1.00 62.14  ? 254 ARG B CA  1 
ATOM   5115 C  C   . ARG B 1 225 ? -10.842 10.102 71.301  1.00 62.96  ? 254 ARG B C   1 
ATOM   5116 O  O   . ARG B 1 225 ? -10.396 11.110 70.738  1.00 63.55  ? 254 ARG B O   1 
ATOM   5117 C  CB  . ARG B 1 225 ? -9.338  8.504  72.592  1.00 62.44  ? 254 ARG B CB  1 
ATOM   5118 C  CG  . ARG B 1 225 ? -8.580  9.669  73.195  1.00 63.58  ? 254 ARG B CG  1 
ATOM   5119 C  CD  . ARG B 1 225 ? -7.970  9.248  74.511  1.00 64.73  ? 254 ARG B CD  1 
ATOM   5120 N  NE  . ARG B 1 225 ? -6.933  8.237  74.321  1.00 66.53  ? 254 ARG B NE  1 
ATOM   5121 C  CZ  . ARG B 1 225 ? -6.586  7.336  75.234  1.00 68.92  ? 254 ARG B CZ  1 
ATOM   5122 N  NH1 . ARG B 1 225 ? -7.195  7.306  76.414  1.00 69.14  ? 254 ARG B NH1 1 
ATOM   5123 N  NH2 . ARG B 1 225 ? -5.619  6.468  74.980  1.00 68.42  ? 254 ARG B NH2 1 
ATOM   5124 N  N   . PRO B 1 226 ? -12.055 10.089 71.866  1.00 62.67  ? 255 PRO B N   1 
ATOM   5125 C  CA  . PRO B 1 226 ? -12.880 11.307 71.829  1.00 62.18  ? 255 PRO B CA  1 
ATOM   5126 C  C   . PRO B 1 226 ? -12.412 12.428 72.733  1.00 61.50  ? 255 PRO B C   1 
ATOM   5127 O  O   . PRO B 1 226 ? -11.763 12.204 73.745  1.00 61.97  ? 255 PRO B O   1 
ATOM   5128 C  CB  . PRO B 1 226 ? -14.279 10.815 72.239  1.00 63.06  ? 255 PRO B CB  1 
ATOM   5129 C  CG  . PRO B 1 226 ? -14.194 9.312  72.275  1.00 63.86  ? 255 PRO B CG  1 
ATOM   5130 C  CD  . PRO B 1 226 ? -12.764 8.969  72.510  1.00 62.24  ? 255 PRO B CD  1 
ATOM   5131 N  N   . LEU B 1 227 ? -12.755 13.641 72.351  1.00 60.66  ? 256 LEU B N   1 
ATOM   5132 C  CA  . LEU B 1 227 ? -12.547 14.851 73.130  1.00 60.60  ? 256 LEU B CA  1 
ATOM   5133 C  C   . LEU B 1 227 ? -13.977 15.264 73.488  1.00 60.80  ? 256 LEU B C   1 
ATOM   5134 O  O   . LEU B 1 227 ? -14.788 15.484 72.583  1.00 61.07  ? 256 LEU B O   1 
ATOM   5135 C  CB  . LEU B 1 227 ? -11.874 15.956 72.293  1.00 60.33  ? 256 LEU B CB  1 
ATOM   5136 C  CG  . LEU B 1 227 ? -10.385 15.799 72.001  1.00 61.55  ? 256 LEU B CG  1 
ATOM   5137 C  CD1 . LEU B 1 227 ? -9.861  17.009 71.295  1.00 62.27  ? 256 LEU B CD1 1 
ATOM   5138 C  CD2 . LEU B 1 227 ? -9.581  15.611 73.265  1.00 61.99  ? 256 LEU B CD2 1 
ATOM   5139 N  N   . TYR B 1 228 ? -14.325 15.263 74.777  1.00 60.30  ? 257 TYR B N   1 
ATOM   5140 C  CA  . TYR B 1 228 ? -15.685 15.598 75.184  1.00 60.30  ? 257 TYR B CA  1 
ATOM   5141 C  C   . TYR B 1 228 ? -15.723 17.042 75.607  1.00 60.01  ? 257 TYR B C   1 
ATOM   5142 O  O   . TYR B 1 228 ? -15.314 17.358 76.731  1.00 60.07  ? 257 TYR B O   1 
ATOM   5143 C  CB  . TYR B 1 228 ? -16.175 14.695 76.329  1.00 60.36  ? 257 TYR B CB  1 
ATOM   5144 C  CG  . TYR B 1 228 ? -16.174 13.215 76.009  1.00 61.37  ? 257 TYR B CG  1 
ATOM   5145 C  CD1 . TYR B 1 228 ? -15.009 12.467 76.094  1.00 62.38  ? 257 TYR B CD1 1 
ATOM   5146 C  CD2 . TYR B 1 228 ? -17.348 12.552 75.691  1.00 62.52  ? 257 TYR B CD2 1 
ATOM   5147 C  CE1 . TYR B 1 228 ? -15.001 11.105 75.825  1.00 63.31  ? 257 TYR B CE1 1 
ATOM   5148 C  CE2 . TYR B 1 228 ? -17.357 11.186 75.430  1.00 63.60  ? 257 TYR B CE2 1 
ATOM   5149 C  CZ  . TYR B 1 228 ? -16.180 10.464 75.509  1.00 64.55  ? 257 TYR B CZ  1 
ATOM   5150 O  OH  . TYR B 1 228 ? -16.164 9.111  75.264  1.00 66.30  ? 257 TYR B OH  1 
ATOM   5151 N  N   . VAL B 1 229 ? -16.192 17.927 74.716  1.00 59.35  ? 258 VAL B N   1 
ATOM   5152 C  CA  . VAL B 1 229 ? -16.263 19.345 75.053  1.00 59.35  ? 258 VAL B CA  1 
ATOM   5153 C  C   . VAL B 1 229 ? -17.268 19.588 76.176  1.00 59.39  ? 258 VAL B C   1 
ATOM   5154 O  O   . VAL B 1 229 ? -18.413 19.152 76.079  1.00 59.38  ? 258 VAL B O   1 
ATOM   5155 C  CB  . VAL B 1 229 ? -16.535 20.241 73.827  1.00 59.56  ? 258 VAL B CB  1 
ATOM   5156 C  CG1 . VAL B 1 229 ? -16.543 21.707 74.228  1.00 59.91  ? 258 VAL B CG1 1 
ATOM   5157 C  CG2 . VAL B 1 229 ? -15.503 19.992 72.739  1.00 59.80  ? 258 VAL B CG2 1 
ATOM   5158 N  N   . VAL B 1 230 ? -16.818 20.219 77.266  1.00 59.34  ? 259 VAL B N   1 
ATOM   5159 C  CA  . VAL B 1 230 ? -17.687 20.538 78.403  1.00 60.05  ? 259 VAL B CA  1 
ATOM   5160 C  C   . VAL B 1 230 ? -17.878 22.039 78.620  1.00 60.86  ? 259 VAL B C   1 
ATOM   5161 O  O   . VAL B 1 230 ? -18.761 22.425 79.377  1.00 60.89  ? 259 VAL B O   1 
ATOM   5162 C  CB  . VAL B 1 230 ? -17.263 19.868 79.730  1.00 60.39  ? 259 VAL B CB  1 
ATOM   5163 C  CG1 . VAL B 1 230 ? -17.400 18.351 79.660  1.00 60.79  ? 259 VAL B CG1 1 
ATOM   5164 C  CG2 . VAL B 1 230 ? -15.858 20.293 80.136  1.00 60.64  ? 259 VAL B CG2 1 
ATOM   5165 N  N   . GLY B 1 231 ? -17.036 22.869 78.010  1.00 61.10  ? 260 GLY B N   1 
ATOM   5166 C  CA  . GLY B 1 231 ? -17.132 24.310 78.180  1.00 61.37  ? 260 GLY B CA  1 
ATOM   5167 C  C   . GLY B 1 231 ? -16.619 25.072 76.987  1.00 61.54  ? 260 GLY B C   1 
ATOM   5168 O  O   . GLY B 1 231 ? -15.847 24.545 76.189  1.00 61.84  ? 260 GLY B O   1 
ATOM   5169 N  N   . SER B 1 232 ? -17.058 26.310 76.851  1.00 61.36  ? 261 SER B N   1 
ATOM   5170 C  CA  . SER B 1 232 ? -16.625 27.199 75.785  1.00 61.52  ? 261 SER B CA  1 
ATOM   5171 C  C   . SER B 1 232 ? -16.141 28.531 76.398  1.00 61.53  ? 261 SER B C   1 
ATOM   5172 O  O   . SER B 1 232 ? -16.006 28.622 77.619  1.00 61.73  ? 261 SER B O   1 
ATOM   5173 C  CB  . SER B 1 232 ? -17.753 27.403 74.776  1.00 62.86  ? 261 SER B CB  1 
ATOM   5174 O  OG  . SER B 1 232 ? -18.968 27.783 75.397  1.00 65.35  ? 261 SER B OG  1 
ATOM   5175 N  N   . ASP B 1 233 ? -15.847 29.554 75.559  1.00 61.25  ? 262 ASP B N   1 
ATOM   5176 C  CA  . ASP B 1 233 ? -15.354 30.874 75.962  1.00 61.03  ? 262 ASP B CA  1 
ATOM   5177 C  C   . ASP B 1 233 ? -15.934 31.423 77.230  1.00 61.65  ? 262 ASP B C   1 
ATOM   5178 O  O   . ASP B 1 233 ? -15.218 32.105 77.950  1.00 61.92  ? 262 ASP B O   1 
ATOM   5179 C  CB  . ASP B 1 233 ? -15.620 31.915 74.882  1.00 61.45  ? 262 ASP B CB  1 
ATOM   5180 C  CG  . ASP B 1 233 ? -15.050 31.615 73.535  1.00 65.68  ? 262 ASP B CG  1 
ATOM   5181 O  OD1 . ASP B 1 233 ? -14.207 30.701 73.436  1.00 67.71  ? 262 ASP B OD1 1 
ATOM   5182 O  OD2 . ASP B 1 233 ? -15.436 32.294 72.578  1.00 66.89  ? 262 ASP B OD2 1 
ATOM   5183 N  N   . GLY B 1 234 ? -17.227 31.202 77.469  1.00 61.80  ? 263 GLY B N   1 
ATOM   5184 C  CA  . GLY B 1 234 ? -17.885 31.784 78.628  1.00 62.44  ? 263 GLY B CA  1 
ATOM   5185 C  C   . GLY B 1 234 ? -18.764 30.923 79.506  1.00 62.69  ? 263 GLY B C   1 
ATOM   5186 O  O   . GLY B 1 234 ? -19.712 31.431 80.112  1.00 62.73  ? 263 GLY B O   1 
ATOM   5187 N  N   . GLY B 1 235 ? -18.395 29.661 79.668  1.00 62.56  ? 264 GLY B N   1 
ATOM   5188 C  CA  . GLY B 1 235 ? -19.123 28.776 80.557  1.00 62.95  ? 264 GLY B CA  1 
ATOM   5189 C  C   . GLY B 1 235 ? -19.269 27.375 80.041  1.00 63.43  ? 264 GLY B C   1 
ATOM   5190 O  O   . GLY B 1 235 ? -18.991 27.099 78.876  1.00 63.00  ? 264 GLY B O   1 
ATOM   5191 N  N   . LEU B 1 236 ? -19.725 26.493 80.913  1.00 64.44  ? 265 LEU B N   1 
ATOM   5192 C  CA  . LEU B 1 236 ? -19.947 25.108 80.546  1.00 66.00  ? 265 LEU B CA  1 
ATOM   5193 C  C   . LEU B 1 236 ? -21.176 24.994 79.650  1.00 67.41  ? 265 LEU B C   1 
ATOM   5194 O  O   . LEU B 1 236 ? -22.099 25.811 79.735  1.00 67.90  ? 265 LEU B O   1 
ATOM   5195 C  CB  . LEU B 1 236 ? -20.139 24.243 81.800  1.00 66.38  ? 265 LEU B CB  1 
ATOM   5196 C  CG  . LEU B 1 236 ? -19.073 24.374 82.885  1.00 68.29  ? 265 LEU B CG  1 
ATOM   5197 C  CD1 . LEU B 1 236 ? -19.431 23.531 84.093  1.00 69.05  ? 265 LEU B CD1 1 
ATOM   5198 C  CD2 . LEU B 1 236 ? -17.693 23.989 82.359  1.00 68.94  ? 265 LEU B CD2 1 
ATOM   5199 N  N   . LEU B 1 237 ? -21.188 23.984 78.782  1.00 67.77  ? 266 LEU B N   1 
ATOM   5200 C  CA  . LEU B 1 237 ? -22.340 23.736 77.916  1.00 68.67  ? 266 LEU B CA  1 
ATOM   5201 C  C   . LEU B 1 237 ? -23.458 23.089 78.772  1.00 69.61  ? 266 LEU B C   1 
ATOM   5202 O  O   . LEU B 1 237 ? -23.245 22.800 79.956  1.00 70.13  ? 266 LEU B O   1 
ATOM   5203 C  CB  . LEU B 1 237 ? -21.937 22.793 76.760  1.00 68.89  ? 266 LEU B CB  1 
ATOM   5204 C  CG  . LEU B 1 237 ? -20.663 23.147 75.999  1.00 70.18  ? 266 LEU B CG  1 
ATOM   5205 C  CD1 . LEU B 1 237 ? -20.281 22.040 75.055  1.00 70.54  ? 266 LEU B CD1 1 
ATOM   5206 C  CD2 . LEU B 1 237 ? -20.819 24.447 75.258  1.00 70.94  ? 266 LEU B CD2 1 
ATOM   5207 N  N   . GLY B 1 238 ? -24.637 22.878 78.190  1.00 69.60  ? 267 GLY B N   1 
ATOM   5208 C  CA  . GLY B 1 238 ? -25.734 22.236 78.904  1.00 70.24  ? 267 GLY B CA  1 
ATOM   5209 C  C   . GLY B 1 238 ? -25.433 20.788 79.243  1.00 70.81  ? 267 GLY B C   1 
ATOM   5210 O  O   . GLY B 1 238 ? -25.845 20.279 80.286  1.00 70.95  ? 267 GLY B O   1 
ATOM   5211 N  N   . GLU B 1 239 ? -24.683 20.128 78.360  1.00 70.95  ? 268 GLU B N   1 
ATOM   5212 C  CA  . GLU B 1 239 ? -24.258 18.737 78.449  1.00 71.40  ? 268 GLU B CA  1 
ATOM   5213 C  C   . GLU B 1 239 ? -23.042 18.536 77.524  1.00 71.43  ? 268 GLU B C   1 
ATOM   5214 O  O   . GLU B 1 239 ? -22.892 19.248 76.516  1.00 71.93  ? 268 GLU B O   1 
ATOM   5215 C  CB  . GLU B 1 239 ? -25.410 17.806 78.036  1.00 74.45  ? 268 GLU B CB  1 
ATOM   5216 C  CG  . GLU B 1 239 ? -26.055 18.184 76.715  1.00 81.20  ? 268 GLU B CG  1 
ATOM   5217 C  CD  . GLU B 1 239 ? -26.860 17.075 76.069  1.00 90.02  ? 268 GLU B CD  1 
ATOM   5218 O  OE1 . GLU B 1 239 ? -26.937 17.055 74.819  1.00 91.58  ? 268 GLU B OE1 1 
ATOM   5219 O  OE2 . GLU B 1 239 ? -27.405 16.223 76.809  1.00 92.98  ? 268 GLU B OE2 1 
ATOM   5220 N  N   . PRO B 1 240 ? -22.141 17.590 77.852  1.00 70.75  ? 269 PRO B N   1 
ATOM   5221 C  CA  . PRO B 1 240 ? -20.948 17.396 77.012  1.00 70.64  ? 269 PRO B CA  1 
ATOM   5222 C  C   . PRO B 1 240 ? -21.229 17.021 75.558  1.00 70.93  ? 269 PRO B C   1 
ATOM   5223 O  O   . PRO B 1 240 ? -22.217 16.341 75.250  1.00 70.81  ? 269 PRO B O   1 
ATOM   5224 C  CB  . PRO B 1 240 ? -20.183 16.292 77.736  1.00 71.09  ? 269 PRO B CB  1 
ATOM   5225 C  CG  . PRO B 1 240 ? -20.686 16.334 79.134  1.00 71.43  ? 269 PRO B CG  1 
ATOM   5226 C  CD  . PRO B 1 240 ? -22.125 16.688 79.014  1.00 69.95  ? 269 PRO B CD  1 
ATOM   5227 N  N   . VAL B 1 241 ? -20.370 17.514 74.658  1.00 70.98  ? 270 VAL B N   1 
ATOM   5228 C  CA  . VAL B 1 241 ? -20.459 17.263 73.222  1.00 71.23  ? 270 VAL B CA  1 
ATOM   5229 C  C   . VAL B 1 241 ? -19.252 16.426 72.788  1.00 71.13  ? 270 VAL B C   1 
ATOM   5230 O  O   . VAL B 1 241 ? -18.123 16.916 72.817  1.00 71.28  ? 270 VAL B O   1 
ATOM   5231 C  CB  . VAL B 1 241 ? -20.539 18.593 72.442  1.00 72.12  ? 270 VAL B CB  1 
ATOM   5232 C  CG1 . VAL B 1 241 ? -20.539 18.356 70.933  1.00 72.69  ? 270 VAL B CG1 1 
ATOM   5233 C  CG2 . VAL B 1 241 ? -21.762 19.392 72.866  1.00 72.79  ? 270 VAL B CG2 1 
ATOM   5234 N  N   . LYS B 1 242 ? -19.485 15.154 72.430  1.00 70.68  ? 271 LYS B N   1 
ATOM   5235 C  CA  . LYS B 1 242 ? -18.426 14.234 72.014  1.00 70.60  ? 271 LYS B CA  1 
ATOM   5236 C  C   . LYS B 1 242 ? -17.935 14.608 70.611  1.00 70.23  ? 271 LYS B C   1 
ATOM   5237 O  O   . LYS B 1 242 ? -18.723 14.590 69.667  1.00 70.39  ? 271 LYS B O   1 
ATOM   5238 C  CB  . LYS B 1 242 ? -18.952 12.789 72.040  1.00 72.28  ? 271 LYS B CB  1 
ATOM   5239 C  CG  . LYS B 1 242 ? -17.894 11.721 71.807  1.00 76.31  ? 271 LYS B CG  1 
ATOM   5240 C  CD  . LYS B 1 242 ? -18.468 10.534 71.037  1.00 80.91  ? 271 LYS B CD  1 
ATOM   5241 C  CE  . LYS B 1 242 ? -17.583 9.316  71.133  1.00 85.44  ? 271 LYS B CE  1 
ATOM   5242 N  NZ  . LYS B 1 242 ? -16.940 8.938  69.842  1.00 88.21  ? 271 LYS B NZ  1 
ATOM   5243 N  N   . LEU B 1 243 ? -16.646 14.977 70.486  1.00 69.51  ? 272 LEU B N   1 
ATOM   5244 C  CA  . LEU B 1 243 ? -16.027 15.387 69.216  1.00 69.47  ? 272 LEU B CA  1 
ATOM   5245 C  C   . LEU B 1 243 ? -14.727 14.632 68.965  1.00 69.67  ? 272 LEU B C   1 
ATOM   5246 O  O   . LEU B 1 243 ? -14.062 14.245 69.925  1.00 70.35  ? 272 LEU B O   1 
ATOM   5247 C  CB  . LEU B 1 243 ? -15.655 16.888 69.260  1.00 69.28  ? 272 LEU B CB  1 
ATOM   5248 C  CG  . LEU B 1 243 ? -16.764 17.929 69.273  1.00 70.38  ? 272 LEU B CG  1 
ATOM   5249 C  CD1 . LEU B 1 243 ? -16.184 19.308 69.149  1.00 70.63  ? 272 LEU B CD1 1 
ATOM   5250 C  CD2 . LEU B 1 243 ? -17.720 17.725 68.132  1.00 71.22  ? 272 LEU B CD2 1 
ATOM   5251 N  N   . THR B 1 244 ? -14.318 14.477 67.691  1.00 68.72  ? 273 THR B N   1 
ATOM   5252 C  CA  . THR B 1 244 ? -12.993 13.918 67.400  1.00 68.36  ? 273 THR B CA  1 
ATOM   5253 C  C   . THR B 1 244 ? -12.076 15.091 67.048  1.00 67.33  ? 273 THR B C   1 
ATOM   5254 O  O   . THR B 1 244 ? -10.969 15.174 67.574  1.00 67.72  ? 273 THR B O   1 
ATOM   5255 C  CB  . THR B 1 244 ? -12.990 12.763 66.386  1.00 70.23  ? 273 THR B CB  1 
ATOM   5256 O  OG1 . THR B 1 244 ? -13.703 13.143 65.215  1.00 72.02  ? 273 THR B OG1 1 
ATOM   5257 C  CG2 . THR B 1 244 ? -13.561 11.480 66.958  1.00 70.58  ? 273 THR B CG2 1 
ATOM   5258 N  N   . GLU B 1 245 ? -12.564 16.040 66.229  1.00 65.80  ? 274 GLU B N   1 
ATOM   5259 C  CA  . GLU B 1 245 ? -11.822 17.242 65.892  1.00 65.09  ? 274 GLU B CA  1 
ATOM   5260 C  C   . GLU B 1 245 ? -12.483 18.471 66.531  1.00 64.08  ? 274 GLU B C   1 
ATOM   5261 O  O   . GLU B 1 245 ? -13.699 18.640 66.458  1.00 64.03  ? 274 GLU B O   1 
ATOM   5262 C  CB  . GLU B 1 245 ? -11.763 17.437 64.383  1.00 68.22  ? 274 GLU B CB  1 
ATOM   5263 C  CG  . GLU B 1 245 ? -11.339 16.206 63.608  1.00 74.46  ? 274 GLU B CG  1 
ATOM   5264 C  CD  . GLU B 1 245 ? -11.059 16.441 62.137  1.00 81.55  ? 274 GLU B CD  1 
ATOM   5265 O  OE1 . GLU B 1 245 ? -10.595 15.489 61.468  1.00 83.45  ? 274 GLU B OE1 1 
ATOM   5266 O  OE2 . GLU B 1 245 ? -11.278 17.578 61.658  1.00 83.45  ? 274 GLU B OE2 1 
ATOM   5267 N  N   . LEU B 1 246 ? -11.674 19.335 67.147  1.00 63.26  ? 275 LEU B N   1 
ATOM   5268 C  CA  . LEU B 1 246 ? -12.131 20.558 67.796  1.00 62.75  ? 275 LEU B CA  1 
ATOM   5269 C  C   . LEU B 1 246 ? -11.391 21.760 67.240  1.00 62.49  ? 275 LEU B C   1 
ATOM   5270 O  O   . LEU B 1 246 ? -10.279 22.081 67.676  1.00 62.31  ? 275 LEU B O   1 
ATOM   5271 C  CB  . LEU B 1 246 ? -11.945 20.496 69.320  1.00 62.34  ? 275 LEU B CB  1 
ATOM   5272 C  CG  . LEU B 1 246 ? -12.371 21.746 70.102  1.00 62.81  ? 275 LEU B CG  1 
ATOM   5273 C  CD1 . LEU B 1 246 ? -13.828 22.080 69.888  1.00 63.04  ? 275 LEU B CD1 1 
ATOM   5274 C  CD2 . LEU B 1 246 ? -12.113 21.572 71.545  1.00 63.19  ? 275 LEU B CD2 1 
ATOM   5275 N  N   . PRO B 1 247 ? -11.977 22.410 66.230  1.00 62.05  ? 276 PRO B N   1 
ATOM   5276 C  CA  . PRO B 1 247 ? -11.336 23.609 65.685  1.00 61.57  ? 276 PRO B CA  1 
ATOM   5277 C  C   . PRO B 1 247 ? -11.431 24.745 66.709  1.00 60.57  ? 276 PRO B C   1 
ATOM   5278 O  O   . PRO B 1 247 ? -12.509 25.019 67.242  1.00 60.12  ? 276 PRO B O   1 
ATOM   5279 C  CB  . PRO B 1 247 ? -12.136 23.904 64.405  1.00 62.36  ? 276 PRO B CB  1 
ATOM   5280 C  CG  . PRO B 1 247 ? -13.082 22.742 64.232  1.00 62.99  ? 276 PRO B CG  1 
ATOM   5281 C  CD  . PRO B 1 247 ? -13.271 22.138 65.581  1.00 61.54  ? 276 PRO B CD  1 
ATOM   5282 N  N   . ILE B 1 248 ? -10.289 25.350 67.028  1.00 59.92  ? 277 ILE B N   1 
ATOM   5283 C  CA  . ILE B 1 248 ? -10.250 26.429 67.988  1.00 60.03  ? 277 ILE B CA  1 
ATOM   5284 C  C   . ILE B 1 248 ? -9.651  27.663 67.341  1.00 59.57  ? 277 ILE B C   1 
ATOM   5285 O  O   . ILE B 1 248 ? -8.578  27.590 66.755  1.00 59.68  ? 277 ILE B O   1 
ATOM   5286 C  CB  . ILE B 1 248 ? -9.556  25.981 69.297  1.00 61.13  ? 277 ILE B CB  1 
ATOM   5287 C  CG1 . ILE B 1 248 ? -9.585  27.084 70.357  1.00 62.28  ? 277 ILE B CG1 1 
ATOM   5288 C  CG2 . ILE B 1 248 ? -8.143  25.457 69.043  1.00 61.96  ? 277 ILE B CG2 1 
ATOM   5289 C  CD1 . ILE B 1 248 ? -9.204  26.620 71.710  1.00 63.65  ? 277 ILE B CD1 1 
ATOM   5290 N  N   . LEU B 1 249 ? -10.389 28.781 67.371  1.00 59.03  ? 278 LEU B N   1 
ATOM   5291 C  CA  . LEU B 1 249 ? -9.945  30.029 66.754  1.00 58.92  ? 278 LEU B CA  1 
ATOM   5292 C  C   . LEU B 1 249 ? -9.117  30.881 67.703  1.00 58.73  ? 278 LEU B C   1 
ATOM   5293 O  O   . LEU B 1 249 ? -9.205  30.716 68.914  1.00 58.76  ? 278 LEU B O   1 
ATOM   5294 C  CB  . LEU B 1 249 ? -11.158 30.842 66.275  1.00 59.18  ? 278 LEU B CB  1 
ATOM   5295 C  CG  . LEU B 1 249 ? -12.059 30.198 65.222  1.00 60.44  ? 278 LEU B CG  1 
ATOM   5296 C  CD1 . LEU B 1 249 ? -13.216 31.127 64.862  1.00 60.95  ? 278 LEU B CD1 1 
ATOM   5297 C  CD2 . LEU B 1 249 ? -11.271 29.781 63.989  1.00 60.54  ? 278 LEU B CD2 1 
ATOM   5298 N  N   . MET B 1 250 ? -8.324  31.816 67.155  1.00 58.54  ? 279 MET B N   1 
ATOM   5299 C  CA  . MET B 1 250 ? -7.483  32.720 67.942  1.00 58.92  ? 279 MET B CA  1 
ATOM   5300 C  C   . MET B 1 250 ? -8.304  33.481 68.987  1.00 59.42  ? 279 MET B C   1 
ATOM   5301 O  O   . MET B 1 250 ? -9.258  34.191 68.641  1.00 59.07  ? 279 MET B O   1 
ATOM   5302 C  CB  . MET B 1 250 ? -6.727  33.714 67.040  1.00 59.26  ? 279 MET B CB  1 
ATOM   5303 C  CG  . MET B 1 250 ? -5.915  33.058 65.947  1.00 61.26  ? 279 MET B CG  1 
ATOM   5304 S  SD  . MET B 1 250 ? -6.919  32.659 64.482  1.00 64.77  ? 279 MET B SD  1 
ATOM   5305 C  CE  . MET B 1 250 ? -7.167  34.264 63.837  1.00 64.73  ? 279 MET B CE  1 
ATOM   5306 N  N   . GLY B 1 251 ? -7.939  33.287 70.256  1.00 59.59  ? 280 GLY B N   1 
ATOM   5307 C  CA  . GLY B 1 251 ? -8.608  33.927 71.381  1.00 59.80  ? 280 GLY B CA  1 
ATOM   5308 C  C   . GLY B 1 251 ? -9.652  33.059 72.053  1.00 59.87  ? 280 GLY B C   1 
ATOM   5309 O  O   . GLY B 1 251 ? -10.062 33.361 73.169  1.00 60.30  ? 280 GLY B O   1 
ATOM   5310 N  N   . GLU B 1 252 ? -10.108 31.983 71.394  1.00 59.45  ? 281 GLU B N   1 
ATOM   5311 C  CA  . GLU B 1 252 ? -11.142 31.112 71.964  1.00 59.44  ? 281 GLU B CA  1 
ATOM   5312 C  C   . GLU B 1 252 ? -10.616 30.179 73.038  1.00 59.29  ? 281 GLU B C   1 
ATOM   5313 O  O   . GLU B 1 252 ? -9.430  29.842 73.058  1.00 59.37  ? 281 GLU B O   1 
ATOM   5314 C  CB  . GLU B 1 252 ? -11.825 30.270 70.870  1.00 61.50  ? 281 GLU B CB  1 
ATOM   5315 C  CG  . GLU B 1 252 ? -12.557 31.085 69.828  1.00 65.77  ? 281 GLU B CG  1 
ATOM   5316 C  CD  . GLU B 1 252 ? -13.485 30.272 68.950  1.00 69.45  ? 281 GLU B CD  1 
ATOM   5317 O  OE1 . GLU B 1 252 ? -14.577 30.785 68.616  1.00 68.92  ? 281 GLU B OE1 1 
ATOM   5318 O  OE2 . GLU B 1 252 ? -13.120 29.127 68.594  1.00 70.34  ? 281 GLU B OE2 1 
ATOM   5319 N  N   . ARG B 1 253 ? -11.520 29.727 73.920  1.00 58.98  ? 282 ARG B N   1 
ATOM   5320 C  CA  . ARG B 1 253 ? -11.205 28.773 74.979  1.00 58.88  ? 282 ARG B CA  1 
ATOM   5321 C  C   . ARG B 1 253 ? -12.217 27.652 74.967  1.00 59.68  ? 282 ARG B C   1 
ATOM   5322 O  O   . ARG B 1 253 ? -13.415 27.901 74.848  1.00 59.68  ? 282 ARG B O   1 
ATOM   5323 C  CB  . ARG B 1 253 ? -11.183 29.423 76.366  1.00 58.63  ? 282 ARG B CB  1 
ATOM   5324 C  CG  . ARG B 1 253 ? -9.949  30.256 76.626  1.00 59.19  ? 282 ARG B CG  1 
ATOM   5325 C  CD  . ARG B 1 253 ? -10.155 31.677 76.169  1.00 60.23  ? 282 ARG B CD  1 
ATOM   5326 N  NE  . ARG B 1 253 ? -11.209 32.349 76.919  1.00 61.85  ? 282 ARG B NE  1 
ATOM   5327 C  CZ  . ARG B 1 253 ? -12.174 33.082 76.376  1.00 63.07  ? 282 ARG B CZ  1 
ATOM   5328 N  NH1 . ARG B 1 253 ? -12.253 33.220 75.060  1.00 62.71  ? 282 ARG B NH1 1 
ATOM   5329 N  NH2 . ARG B 1 253 ? -13.078 33.668 77.143  1.00 62.47  ? 282 ARG B NH2 1 
ATOM   5330 N  N   . PHE B 1 254 ? -11.740 26.416 75.080  1.00 60.20  ? 283 PHE B N   1 
ATOM   5331 C  CA  . PHE B 1 254 ? -12.610 25.254 75.110  1.00 61.20  ? 283 PHE B CA  1 
ATOM   5332 C  C   . PHE B 1 254 ? -12.159 24.331 76.205  1.00 61.91  ? 283 PHE B C   1 
ATOM   5333 O  O   . PHE B 1 254 ? -11.003 23.928 76.198  1.00 62.38  ? 283 PHE B O   1 
ATOM   5334 C  CB  . PHE B 1 254 ? -12.535 24.502 73.780  1.00 61.54  ? 283 PHE B CB  1 
ATOM   5335 C  CG  . PHE B 1 254 ? -13.524 24.959 72.735  1.00 62.65  ? 283 PHE B CG  1 
ATOM   5336 C  CD1 . PHE B 1 254 ? -14.880 24.724 72.891  1.00 63.20  ? 283 PHE B CD1 1 
ATOM   5337 C  CD2 . PHE B 1 254 ? -13.093 25.604 71.584  1.00 63.79  ? 283 PHE B CD2 1 
ATOM   5338 C  CE1 . PHE B 1 254 ? -15.790 25.156 71.935  1.00 64.13  ? 283 PHE B CE1 1 
ATOM   5339 C  CE2 . PHE B 1 254 ? -14.007 26.030 70.623  1.00 64.55  ? 283 PHE B CE2 1 
ATOM   5340 C  CZ  . PHE B 1 254 ? -15.350 25.803 70.805  1.00 64.19  ? 283 PHE B CZ  1 
ATOM   5341 N  N   . GLU B 1 255 ? -13.041 23.991 77.150  1.00 62.16  ? 284 GLU B N   1 
ATOM   5342 C  CA  . GLU B 1 255 ? -12.691 23.044 78.209  1.00 62.77  ? 284 GLU B CA  1 
ATOM   5343 C  C   . GLU B 1 255 ? -13.099 21.666 77.716  1.00 63.25  ? 284 GLU B C   1 
ATOM   5344 O  O   . GLU B 1 255 ? -14.245 21.487 77.308  1.00 63.08  ? 284 GLU B O   1 
ATOM   5345 C  CB  . GLU B 1 255 ? -13.401 23.384 79.527  1.00 64.20  ? 284 GLU B CB  1 
ATOM   5346 C  CG  . GLU B 1 255 ? -13.024 24.747 80.075  1.00 68.28  ? 284 GLU B CG  1 
ATOM   5347 C  CD  . GLU B 1 255 ? -13.560 25.031 81.466  1.00 75.76  ? 284 GLU B CD  1 
ATOM   5348 O  OE1 . GLU B 1 255 ? -14.009 26.173 81.717  1.00 77.41  ? 284 GLU B OE1 1 
ATOM   5349 O  OE2 . GLU B 1 255 ? -13.527 24.108 82.309  1.00 78.29  ? 284 GLU B OE2 1 
ATOM   5350 N  N   . VAL B 1 256 ? -12.147 20.717 77.655  1.00 63.73  ? 285 VAL B N   1 
ATOM   5351 C  CA  . VAL B 1 256 ? -12.469 19.371 77.168  1.00 64.78  ? 285 VAL B CA  1 
ATOM   5352 C  C   . VAL B 1 256 ? -12.080 18.311 78.184  1.00 65.90  ? 285 VAL B C   1 
ATOM   5353 O  O   . VAL B 1 256 ? -11.082 18.458 78.895  1.00 66.16  ? 285 VAL B O   1 
ATOM   5354 C  CB  . VAL B 1 256 ? -11.954 19.017 75.734  1.00 65.23  ? 285 VAL B CB  1 
ATOM   5355 C  CG1 . VAL B 1 256 ? -11.867 20.250 74.843  1.00 65.90  ? 285 VAL B CG1 1 
ATOM   5356 C  CG2 . VAL B 1 256 ? -10.626 18.260 75.753  1.00 65.36  ? 285 VAL B CG2 1 
ATOM   5357 N  N   . LEU B 1 257 ? -12.860 17.227 78.226  1.00 65.73  ? 286 LEU B N   1 
ATOM   5358 C  CA  . LEU B 1 257 ? -12.577 16.113 79.108  1.00 65.82  ? 286 LEU B CA  1 
ATOM   5359 C  C   . LEU B 1 257 ? -12.075 14.930 78.296  1.00 65.24  ? 286 LEU B C   1 
ATOM   5360 O  O   . LEU B 1 257 ? -12.648 14.596 77.266  1.00 65.02  ? 286 LEU B O   1 
ATOM   5361 C  CB  . LEU B 1 257 ? -13.828 15.726 79.891  1.00 66.32  ? 286 LEU B CB  1 
ATOM   5362 C  CG  . LEU B 1 257 ? -13.923 16.269 81.294  1.00 68.18  ? 286 LEU B CG  1 
ATOM   5363 C  CD1 . LEU B 1 257 ? -15.183 15.783 81.954  1.00 68.67  ? 286 LEU B CD1 1 
ATOM   5364 C  CD2 . LEU B 1 257 ? -12.782 15.780 82.126  1.00 69.50  ? 286 LEU B CD2 1 
ATOM   5365 N  N   . VAL B 1 258 ? -10.983 14.315 78.742  1.00 64.89  ? 287 VAL B N   1 
ATOM   5366 C  CA  . VAL B 1 258 ? -10.404 13.169 78.049  1.00 64.80  ? 287 VAL B CA  1 
ATOM   5367 C  C   . VAL B 1 258 ? -10.377 11.960 78.974  1.00 64.30  ? 287 VAL B C   1 
ATOM   5368 O  O   . VAL B 1 258 ? -10.042 12.086 80.153  1.00 64.04  ? 287 VAL B O   1 
ATOM   5369 C  CB  . VAL B 1 258 ? -9.006  13.425 77.444  1.00 65.51  ? 287 VAL B CB  1 
ATOM   5370 C  CG1 . VAL B 1 258 ? -8.710  12.394 76.371  1.00 66.18  ? 287 VAL B CG1 1 
ATOM   5371 C  CG2 . VAL B 1 258 ? -8.891  14.825 76.859  1.00 66.24  ? 287 VAL B CG2 1 
ATOM   5372 N  N   . ASP B 1 259 ? -10.743 10.788 78.437  1.00 63.64  ? 288 ASP B N   1 
ATOM   5373 C  CA  . ASP B 1 259 ? -10.760 9.549  79.196  1.00 63.29  ? 288 ASP B CA  1 
ATOM   5374 C  C   . ASP B 1 259 ? -9.352  8.937  79.317  1.00 62.97  ? 288 ASP B C   1 
ATOM   5375 O  O   . ASP B 1 259 ? -8.741  8.545  78.326  1.00 63.03  ? 288 ASP B O   1 
ATOM   5376 C  CB  . ASP B 1 259 ? -11.729 8.565  78.538  1.00 64.50  ? 288 ASP B CB  1 
ATOM   5377 C  CG  . ASP B 1 259 ? -12.322 7.541  79.478  1.00 67.54  ? 288 ASP B CG  1 
ATOM   5378 O  OD1 . ASP B 1 259 ? -11.723 7.299  80.542  1.00 67.73  ? 288 ASP B OD1 1 
ATOM   5379 O  OD2 . ASP B 1 259 ? -13.376 6.965  79.135  1.00 69.15  ? 288 ASP B OD2 1 
ATOM   5380 N  N   . THR B 1 260 ? -8.842  8.861  80.536  1.00 62.48  ? 289 THR B N   1 
ATOM   5381 C  CA  . THR B 1 260 ? -7.529  8.279  80.793  1.00 62.42  ? 289 THR B CA  1 
ATOM   5382 C  C   . THR B 1 260 ? -7.621  6.956  81.576  1.00 62.90  ? 289 THR B C   1 
ATOM   5383 O  O   . THR B 1 260 ? -6.599  6.471  82.048  1.00 63.17  ? 289 THR B O   1 
ATOM   5384 C  CB  . THR B 1 260 ? -6.654  9.290  81.525  1.00 62.66  ? 289 THR B CB  1 
ATOM   5385 O  OG1 . THR B 1 260 ? -7.269  9.588  82.769  1.00 63.04  ? 289 THR B OG1 1 
ATOM   5386 C  CG2 . THR B 1 260 ? -6.476  10.573 80.742  1.00 62.97  ? 289 THR B CG2 1 
ATOM   5387 N  N   . ARG B 1 261 ? -8.831  6.378  81.720  1.00 62.76  ? 290 ARG B N   1 
ATOM   5388 C  CA  . ARG B 1 261 ? -9.063  5.137  82.447  1.00 63.09  ? 290 ARG B CA  1 
ATOM   5389 C  C   . ARG B 1 261 ? -8.317  3.955  81.854  1.00 64.46  ? 290 ARG B C   1 
ATOM   5390 O  O   . ARG B 1 261 ? -7.905  3.068  82.598  1.00 64.78  ? 290 ARG B O   1 
ATOM   5391 C  CB  . ARG B 1 261 ? -10.565 4.851  82.573  1.00 63.23  ? 290 ARG B CB  1 
ATOM   5392 C  CG  . ARG B 1 261 ? -11.230 5.787  83.568  1.00 64.88  ? 290 ARG B CG  1 
ATOM   5393 C  CD  . ARG B 1 261 ? -12.724 5.639  83.664  1.00 67.85  ? 290 ARG B CD  1 
ATOM   5394 N  NE  . ARG B 1 261 ? -13.404 5.848  82.382  1.00 70.75  ? 290 ARG B NE  1 
ATOM   5395 C  CZ  . ARG B 1 261 ? -14.726 5.904  82.238  1.00 73.21  ? 290 ARG B CZ  1 
ATOM   5396 N  NH1 . ARG B 1 261 ? -15.523 5.793  83.295  1.00 73.16  ? 290 ARG B NH1 1 
ATOM   5397 N  NH2 . ARG B 1 261 ? -15.261 6.090  81.041  1.00 73.43  ? 290 ARG B NH2 1 
ATOM   5398 N  N   . ASP B 1 262 ? -8.092  3.957  80.534  1.00 65.24  ? 291 ASP B N   1 
ATOM   5399 C  CA  . ASP B 1 262 ? -7.347  2.877  79.890  1.00 66.88  ? 291 ASP B CA  1 
ATOM   5400 C  C   . ASP B 1 262 ? -5.833  2.874  80.207  1.00 67.19  ? 291 ASP B C   1 
ATOM   5401 O  O   . ASP B 1 262 ? -5.146  1.894  79.895  1.00 67.57  ? 291 ASP B O   1 
ATOM   5402 C  CB  . ASP B 1 262 ? -7.584  2.861  78.370  1.00 70.24  ? 291 ASP B CB  1 
ATOM   5403 C  CG  . ASP B 1 262 ? -6.962  4.031  77.636  1.00 77.79  ? 291 ASP B CG  1 
ATOM   5404 O  OD1 . ASP B 1 262 ? -6.852  5.129  78.245  1.00 79.66  ? 291 ASP B OD1 1 
ATOM   5405 O  OD2 . ASP B 1 262 ? -6.590  3.858  76.453  1.00 80.36  ? 291 ASP B OD2 1 
ATOM   5406 N  N   . GLY B 1 263 ? -5.329  3.984  80.748  1.00 66.69  ? 292 GLY B N   1 
ATOM   5407 C  CA  . GLY B 1 263 ? -3.935  4.138  81.143  1.00 66.84  ? 292 GLY B CA  1 
ATOM   5408 C  C   . GLY B 1 263 ? -2.936  4.331  80.027  1.00 66.75  ? 292 GLY B C   1 
ATOM   5409 O  O   . GLY B 1 263 ? -1.760  4.597  80.286  1.00 66.45  ? 292 GLY B O   1 
ATOM   5410 N  N   . LYS B 1 264 ? -3.387  4.198  78.779  1.00 67.09  ? 293 LYS B N   1 
ATOM   5411 C  CA  . LYS B 1 264 ? -2.500  4.342  77.628  1.00 67.78  ? 293 LYS B CA  1 
ATOM   5412 C  C   . LYS B 1 264 ? -2.136  5.797  77.349  1.00 67.58  ? 293 LYS B C   1 
ATOM   5413 O  O   . LYS B 1 264 ? -2.981  6.693  77.441  1.00 67.60  ? 293 LYS B O   1 
ATOM   5414 C  CB  . LYS B 1 264 ? -3.082  3.664  76.368  1.00 70.33  ? 293 LYS B CB  1 
ATOM   5415 C  CG  . LYS B 1 264 ? -2.841  2.156  76.315  1.00 75.95  ? 293 LYS B CG  1 
ATOM   5416 C  CD  . LYS B 1 264 ? -4.161  1.359  76.171  1.00 81.23  ? 293 LYS B CD  1 
ATOM   5417 C  CE  . LYS B 1 264 ? -4.182  0.034  76.924  1.00 84.41  ? 293 LYS B CE  1 
ATOM   5418 N  NZ  . LYS B 1 264 ? -3.331  -1.002 76.272  1.00 85.97  ? 293 LYS B NZ  1 
ATOM   5419 N  N   . ALA B 1 265 ? -0.868  6.029  77.027  1.00 67.07  ? 294 ALA B N   1 
ATOM   5420 C  CA  . ALA B 1 265 ? -0.398  7.363  76.690  1.00 66.90  ? 294 ALA B CA  1 
ATOM   5421 C  C   . ALA B 1 265 ? -0.878  7.731  75.293  1.00 66.24  ? 294 ALA B C   1 
ATOM   5422 O  O   . ALA B 1 265 ? -1.132  6.860  74.454  1.00 66.11  ? 294 ALA B O   1 
ATOM   5423 C  CB  . ALA B 1 265 ? 1.122   7.417  76.754  1.00 67.23  ? 294 ALA B CB  1 
ATOM   5424 N  N   . PHE B 1 266 ? -1.008  9.026  75.049  1.00 65.82  ? 295 PHE B N   1 
ATOM   5425 C  CA  . PHE B 1 266 ? -1.485  9.545  73.769  1.00 66.03  ? 295 PHE B CA  1 
ATOM   5426 C  C   . PHE B 1 266 ? -1.115  11.031 73.621  1.00 66.27  ? 295 PHE B C   1 
ATOM   5427 O  O   . PHE B 1 266 ? -0.744  11.682 74.601  1.00 66.51  ? 295 PHE B O   1 
ATOM   5428 C  CB  . PHE B 1 266 ? -3.017  9.349  73.644  1.00 65.74  ? 295 PHE B CB  1 
ATOM   5429 C  CG  . PHE B 1 266 ? -3.832  10.063 74.695  1.00 66.23  ? 295 PHE B CG  1 
ATOM   5430 C  CD1 . PHE B 1 266 ? -3.995  9.520  75.955  1.00 67.20  ? 295 PHE B CD1 1 
ATOM   5431 C  CD2 . PHE B 1 266 ? -4.447  11.270 74.418  1.00 67.06  ? 295 PHE B CD2 1 
ATOM   5432 C  CE1 . PHE B 1 266 ? -4.743  10.176 76.924  1.00 68.00  ? 295 PHE B CE1 1 
ATOM   5433 C  CE2 . PHE B 1 266 ? -5.188  11.929 75.390  1.00 67.91  ? 295 PHE B CE2 1 
ATOM   5434 C  CZ  . PHE B 1 266 ? -5.328  11.379 76.638  1.00 67.75  ? 295 PHE B CZ  1 
ATOM   5435 N  N   . ASP B 1 267 ? -1.258  11.576 72.412  1.00 65.80  ? 296 ASP B N   1 
ATOM   5436 C  CA  . ASP B 1 267 ? -0.972  12.977 72.163  1.00 65.93  ? 296 ASP B CA  1 
ATOM   5437 C  C   . ASP B 1 267 ? -2.217  13.784 71.851  1.00 65.32  ? 296 ASP B C   1 
ATOM   5438 O  O   . ASP B 1 267 ? -3.196  13.273 71.308  1.00 65.53  ? 296 ASP B O   1 
ATOM   5439 C  CB  . ASP B 1 267 ? -0.035  13.105 70.959  1.00 68.20  ? 296 ASP B CB  1 
ATOM   5440 C  CG  . ASP B 1 267 ? 1.350   12.602 71.238  1.00 74.43  ? 296 ASP B CG  1 
ATOM   5441 O  OD1 . ASP B 1 267 ? 1.846   12.829 72.360  1.00 75.04  ? 296 ASP B OD1 1 
ATOM   5442 O  OD2 . ASP B 1 267 ? 1.951   11.985 70.331  1.00 77.87  ? 296 ASP B OD2 1 
ATOM   5443 N  N   . ILE B 1 268 ? -2.150  15.070 72.157  1.00 64.28  ? 297 ILE B N   1 
ATOM   5444 C  CA  . ILE B 1 268 ? -3.137  16.046 71.744  1.00 63.68  ? 297 ILE B CA  1 
ATOM   5445 C  C   . ILE B 1 268 ? -2.457  16.590 70.505  1.00 63.27  ? 297 ILE B C   1 
ATOM   5446 O  O   . ILE B 1 268 ? -1.316  17.035 70.591  1.00 63.25  ? 297 ILE B O   1 
ATOM   5447 C  CB  . ILE B 1 268 ? -3.351  17.162 72.792  1.00 63.73  ? 297 ILE B CB  1 
ATOM   5448 C  CG1 . ILE B 1 268 ? -4.085  16.627 74.031  1.00 64.03  ? 297 ILE B CG1 1 
ATOM   5449 C  CG2 . ILE B 1 268 ? -4.094  18.343 72.172  1.00 63.96  ? 297 ILE B CG2 1 
ATOM   5450 C  CD1 . ILE B 1 268 ? -5.456  16.071 73.761  1.00 64.86  ? 297 ILE B CD1 1 
ATOM   5451 N  N   . ILE B 1 269 ? -3.081  16.442 69.343  1.00 63.03  ? 298 ILE B N   1 
ATOM   5452 C  CA  . ILE B 1 269 ? -2.488  16.883 68.083  1.00 63.23  ? 298 ILE B CA  1 
ATOM   5453 C  C   . ILE B 1 269 ? -3.322  17.960 67.413  1.00 63.66  ? 298 ILE B C   1 
ATOM   5454 O  O   . ILE B 1 269 ? -4.526  18.041 67.635  1.00 63.66  ? 298 ILE B O   1 
ATOM   5455 C  CB  . ILE B 1 269 ? -2.273  15.685 67.127  1.00 63.34  ? 298 ILE B CB  1 
ATOM   5456 C  CG1 . ILE B 1 269 ? -3.599  14.963 66.858  1.00 64.37  ? 298 ILE B CG1 1 
ATOM   5457 C  CG2 . ILE B 1 269 ? -1.232  14.721 67.673  1.00 63.62  ? 298 ILE B CG2 1 
ATOM   5458 C  CD1 . ILE B 1 269 ? -3.541  13.864 65.849  1.00 65.70  ? 298 ILE B CD1 1 
ATOM   5459 N  N   . THR B 1 270 ? -2.681  18.792 66.590  1.00 63.97  ? 299 THR B N   1 
ATOM   5460 C  CA  . THR B 1 270 ? -3.396  19.797 65.815  1.00 64.58  ? 299 THR B CA  1 
ATOM   5461 C  C   . THR B 1 270 ? -3.260  19.431 64.338  1.00 64.98  ? 299 THR B C   1 
ATOM   5462 O  O   . THR B 1 270 ? -2.195  19.024 63.872  1.00 64.62  ? 299 THR B O   1 
ATOM   5463 C  CB  . THR B 1 270 ? -3.040  21.243 66.193  1.00 65.78  ? 299 THR B CB  1 
ATOM   5464 O  OG1 . THR B 1 270 ? -3.915  22.127 65.486  1.00 66.88  ? 299 THR B OG1 1 
ATOM   5465 C  CG2 . THR B 1 270 ? -1.581  21.593 65.913  1.00 65.99  ? 299 THR B CG2 1 
ATOM   5466 N  N   . LEU B 1 271 ? -4.384  19.479 63.636  1.00 65.51  ? 300 LEU B N   1 
ATOM   5467 C  CA  . LEU B 1 271 ? -4.495  19.089 62.237  1.00 66.17  ? 300 LEU B CA  1 
ATOM   5468 C  C   . LEU B 1 271 ? -4.264  20.264 61.299  1.00 67.43  ? 300 LEU B C   1 
ATOM   5469 O  O   . LEU B 1 271 ? -4.498  21.413 61.680  1.00 67.85  ? 300 LEU B O   1 
ATOM   5470 C  CB  . LEU B 1 271 ? -5.884  18.478 62.011  1.00 65.60  ? 300 LEU B CB  1 
ATOM   5471 C  CG  . LEU B 1 271 ? -6.164  17.250 62.849  1.00 66.13  ? 300 LEU B CG  1 
ATOM   5472 C  CD1 . LEU B 1 271 ? -7.602  16.858 62.764  1.00 66.53  ? 300 LEU B CD1 1 
ATOM   5473 C  CD2 . LEU B 1 271 ? -5.271  16.112 62.453  1.00 66.34  ? 300 LEU B CD2 1 
ATOM   5474 N  N   . PRO B 1 272 ? -3.777  20.009 60.070  1.00 67.76  ? 301 PRO B N   1 
ATOM   5475 C  CA  . PRO B 1 272 ? -3.542  21.114 59.139  1.00 68.36  ? 301 PRO B CA  1 
ATOM   5476 C  C   . PRO B 1 272 ? -4.836  21.855 58.811  1.00 69.35  ? 301 PRO B C   1 
ATOM   5477 O  O   . PRO B 1 272 ? -5.878  21.222 58.636  1.00 69.35  ? 301 PRO B O   1 
ATOM   5478 C  CB  . PRO B 1 272 ? -2.956  20.406 57.909  1.00 68.73  ? 301 PRO B CB  1 
ATOM   5479 C  CG  . PRO B 1 272 ? -2.425  19.124 58.422  1.00 68.85  ? 301 PRO B CG  1 
ATOM   5480 C  CD  . PRO B 1 272 ? -3.407  18.720 59.464  1.00 67.23  ? 301 PRO B CD  1 
ATOM   5481 N  N   . VAL B 1 273 ? -4.785  23.193 58.785  1.00 70.14  ? 302 VAL B N   1 
ATOM   5482 C  CA  . VAL B 1 273 ? -5.975  23.978 58.478  1.00 71.77  ? 302 VAL B CA  1 
ATOM   5483 C  C   . VAL B 1 273 ? -5.920  24.578 57.068  1.00 74.12  ? 302 VAL B C   1 
ATOM   5484 O  O   . VAL B 1 273 ? -4.838  24.795 56.525  1.00 74.41  ? 302 VAL B O   1 
ATOM   5485 C  CB  . VAL B 1 273 ? -6.286  25.041 59.551  1.00 71.77  ? 302 VAL B CB  1 
ATOM   5486 C  CG1 . VAL B 1 273 ? -6.459  24.397 60.919  1.00 72.09  ? 302 VAL B CG1 1 
ATOM   5487 C  CG2 . VAL B 1 273 ? -5.206  26.108 59.589  1.00 72.23  ? 302 VAL B CG2 1 
ATOM   5488 N  N   . LYS B 1 274 ? -7.088  24.858 56.479  1.00 75.44  ? 303 LYS B N   1 
ATOM   5489 C  CA  . LYS B 1 274 ? -7.158  25.445 55.141  1.00 77.06  ? 303 LYS B CA  1 
ATOM   5490 C  C   . LYS B 1 274 ? -7.057  26.980 55.193  1.00 77.69  ? 303 LYS B C   1 
ATOM   5491 O  O   . LYS B 1 274 ? -7.606  27.659 54.330  1.00 78.08  ? 303 LYS B O   1 
ATOM   5492 C  CB  . LYS B 1 274 ? -8.442  25.004 54.418  1.00 79.94  ? 303 LYS B CB  1 
ATOM   5493 C  CG  . LYS B 1 274 ? -8.607  23.488 54.389  1.00 86.10  ? 303 LYS B CG  1 
ATOM   5494 C  CD  . LYS B 1 274 ? -10.063 23.066 54.234  1.00 91.83  ? 303 LYS B CD  1 
ATOM   5495 C  CE  . LYS B 1 274 ? -10.261 21.590 54.534  1.00 96.03  ? 303 LYS B CE  1 
ATOM   5496 N  NZ  . LYS B 1 274 ? -11.669 21.146 54.317  1.00 98.56  ? 303 LYS B NZ  1 
ATOM   5497 N  N   . GLN B 1 275 ? -6.360  27.522 56.192  1.00 77.68  ? 304 GLN B N   1 
ATOM   5498 C  CA  . GLN B 1 275 ? -6.187  28.959 56.352  1.00 78.31  ? 304 GLN B CA  1 
ATOM   5499 C  C   . GLN B 1 275 ? -4.909  29.379 55.642  1.00 79.15  ? 304 GLN B C   1 
ATOM   5500 O  O   . GLN B 1 275 ? -3.958  28.598 55.581  1.00 79.72  ? 304 GLN B O   1 
ATOM   5501 C  CB  . GLN B 1 275 ? -6.109  29.301 57.841  1.00 79.53  ? 304 GLN B CB  1 
ATOM   5502 C  CG  . GLN B 1 275 ? -6.471  30.735 58.188  1.00 81.71  ? 304 GLN B CG  1 
ATOM   5503 C  CD  . GLN B 1 275 ? -5.984  31.105 59.564  1.00 84.40  ? 304 GLN B CD  1 
ATOM   5504 O  OE1 . GLN B 1 275 ? -5.857  30.265 60.452  1.00 85.68  ? 304 GLN B OE1 1 
ATOM   5505 N  NE2 . GLN B 1 275 ? -5.677  32.373 59.767  1.00 84.60  ? 304 GLN B NE2 1 
ATOM   5506 N  N   . MET B 1 276 ? -4.882  30.598 55.099  1.00 79.30  ? 305 MET B N   1 
ATOM   5507 C  CA  . MET B 1 276 ? -3.723  31.061 54.356  1.00 80.32  ? 305 MET B CA  1 
ATOM   5508 C  C   . MET B 1 276 ? -2.477  31.237 55.188  1.00 80.83  ? 305 MET B C   1 
ATOM   5509 O  O   . MET B 1 276 ? -2.519  31.896 56.217  1.00 81.29  ? 305 MET B O   1 
ATOM   5510 C  CB  . MET B 1 276 ? -4.021  32.345 53.591  1.00 81.57  ? 305 MET B CB  1 
ATOM   5511 C  CG  . MET B 1 276 ? -3.021  32.589 52.480  1.00 84.74  ? 305 MET B CG  1 
ATOM   5512 S  SD  . MET B 1 276 ? -3.441  33.983 51.443  1.00 92.77  ? 305 MET B SD  1 
ATOM   5513 C  CE  . MET B 1 276 ? -5.064  33.517 50.885  1.00 90.84  ? 305 MET B CE  1 
ATOM   5514 N  N   . GLY B 1 277 ? -1.375  30.658 54.729  1.00 80.73  ? 306 GLY B N   1 
ATOM   5515 C  CA  . GLY B 1 277 ? -0.092  30.756 55.408  1.00 81.34  ? 306 GLY B CA  1 
ATOM   5516 C  C   . GLY B 1 277 ? 0.090   29.766 56.539  1.00 81.95  ? 306 GLY B C   1 
ATOM   5517 O  O   . GLY B 1 277 ? 1.219   29.485 56.944  1.00 82.13  ? 306 GLY B O   1 
ATOM   5518 N  N   . MET B 1 278 ? -1.017  29.215 57.050  1.00 82.04  ? 307 MET B N   1 
ATOM   5519 C  CA  . MET B 1 278 ? -1.005  28.265 58.160  1.00 82.49  ? 307 MET B CA  1 
ATOM   5520 C  C   . MET B 1 278 ? -0.836  26.799 57.727  1.00 83.84  ? 307 MET B C   1 
ATOM   5521 O  O   . MET B 1 278 ? -1.032  25.892 58.537  1.00 84.36  ? 307 MET B O   1 
ATOM   5522 C  CB  . MET B 1 278 ? -2.287  28.422 59.001  1.00 82.12  ? 307 MET B CB  1 
ATOM   5523 C  CG  . MET B 1 278 ? -2.686  29.864 59.270  1.00 82.36  ? 307 MET B CG  1 
ATOM   5524 S  SD  . MET B 1 278 ? -1.403  30.878 60.047  1.00 80.95  ? 307 MET B SD  1 
ATOM   5525 C  CE  . MET B 1 278 ? -2.101  32.466 59.843  1.00 78.35  ? 307 MET B CE  1 
ATOM   5526 N  N   . THR B 1 279 ? -0.459  26.570 56.464  1.00 84.25  ? 308 THR B N   1 
ATOM   5527 C  CA  . THR B 1 279 ? -0.303  25.251 55.854  1.00 84.78  ? 308 THR B CA  1 
ATOM   5528 C  C   . THR B 1 279 ? 1.159   24.773 55.798  1.00 84.59  ? 308 THR B C   1 
ATOM   5529 O  O   . THR B 1 279 ? 1.410   23.573 55.731  1.00 84.35  ? 308 THR B O   1 
ATOM   5530 C  CB  . THR B 1 279 ? -0.884  25.328 54.429  1.00 86.44  ? 308 THR B CB  1 
ATOM   5531 O  OG1 . THR B 1 279 ? -0.144  26.303 53.689  1.00 87.92  ? 308 THR B OG1 1 
ATOM   5532 C  CG2 . THR B 1 279 ? -2.348  25.739 54.416  1.00 86.69  ? 308 THR B CG2 1 
ATOM   5533 N  N   . LEU B 1 280 ? 2.111   25.712 55.796  1.00 84.71  ? 309 LEU B N   1 
ATOM   5534 C  CA  . LEU B 1 280 ? 3.544   25.433 55.673  1.00 85.35  ? 309 LEU B CA  1 
ATOM   5535 C  C   . LEU B 1 280 ? 4.100   24.654 56.866  1.00 85.75  ? 309 LEU B C   1 
ATOM   5536 O  O   . LEU B 1 280 ? 3.597   24.784 57.980  1.00 85.98  ? 309 LEU B O   1 
ATOM   5537 C  CB  . LEU B 1 280 ? 4.343   26.748 55.486  1.00 85.79  ? 309 LEU B CB  1 
ATOM   5538 C  CG  . LEU B 1 280 ? 3.730   27.828 54.582  1.00 87.32  ? 309 LEU B CG  1 
ATOM   5539 C  CD1 . LEU B 1 280 ? 4.521   29.128 54.665  1.00 87.69  ? 309 LEU B CD1 1 
ATOM   5540 C  CD2 . LEU B 1 280 ? 3.584   27.336 53.148  1.00 87.98  ? 309 LEU B CD2 1 
ATOM   5541 N  N   . PRO B 1 281 ? 5.163   23.861 56.651  1.00 85.59  ? 310 PRO B N   1 
ATOM   5542 C  CA  . PRO B 1 281 ? 5.762   23.099 57.763  1.00 85.44  ? 310 PRO B CA  1 
ATOM   5543 C  C   . PRO B 1 281 ? 6.113   23.904 59.021  1.00 84.90  ? 310 PRO B C   1 
ATOM   5544 O  O   . PRO B 1 281 ? 6.420   25.098 58.940  1.00 84.88  ? 310 PRO B O   1 
ATOM   5545 C  CB  . PRO B 1 281 ? 7.011   22.481 57.124  1.00 86.29  ? 310 PRO B CB  1 
ATOM   5546 C  CG  . PRO B 1 281 ? 6.673   22.371 55.689  1.00 86.89  ? 310 PRO B CG  1 
ATOM   5547 C  CD  . PRO B 1 281 ? 5.859   23.592 55.380  1.00 85.29  ? 310 PRO B CD  1 
ATOM   5548 N  N   . PRO B 1 282 ? 6.039   23.273 60.210  1.00 84.36  ? 311 PRO B N   1 
ATOM   5549 C  CA  . PRO B 1 282 ? 5.711   21.854 60.473  1.00 84.08  ? 311 PRO B CA  1 
ATOM   5550 C  C   . PRO B 1 282 ? 4.223   21.490 60.497  1.00 83.71  ? 311 PRO B C   1 
ATOM   5551 O  O   . PRO B 1 282 ? 3.873   20.350 60.791  1.00 83.78  ? 311 PRO B O   1 
ATOM   5552 C  CB  . PRO B 1 282 ? 6.333   21.625 61.852  1.00 84.85  ? 311 PRO B CB  1 
ATOM   5553 C  CG  . PRO B 1 282 ? 6.163   22.952 62.539  1.00 85.37  ? 311 PRO B CG  1 
ATOM   5554 C  CD  . PRO B 1 282 ? 6.373   23.990 61.458  1.00 83.84  ? 311 PRO B CD  1 
ATOM   5555 N  N   . PHE B 1 283 ? 3.363   22.436 60.146  1.00 83.22  ? 312 PHE B N   1 
ATOM   5556 C  CA  . PHE B 1 283 ? 1.915   22.291 60.213  1.00 83.44  ? 312 PHE B CA  1 
ATOM   5557 C  C   . PHE B 1 283 ? 1.264   21.554 59.044  1.00 83.76  ? 312 PHE B C   1 
ATOM   5558 O  O   . PHE B 1 283 ? 0.049   21.342 59.064  1.00 83.51  ? 312 PHE B O   1 
ATOM   5559 C  CB  . PHE B 1 283 ? 1.278   23.674 60.393  1.00 83.30  ? 312 PHE B CB  1 
ATOM   5560 C  CG  . PHE B 1 283 ? 1.807   24.398 61.610  1.00 83.74  ? 312 PHE B CG  1 
ATOM   5561 C  CD1 . PHE B 1 283 ? 1.231   24.210 62.852  1.00 84.47  ? 312 PHE B CD1 1 
ATOM   5562 C  CD2 . PHE B 1 283 ? 2.913   25.220 61.521  1.00 84.41  ? 312 PHE B CD2 1 
ATOM   5563 C  CE1 . PHE B 1 283 ? 1.733   24.854 63.971  1.00 85.07  ? 312 PHE B CE1 1 
ATOM   5564 C  CE2 . PHE B 1 283 ? 3.424   25.844 62.645  1.00 85.03  ? 312 PHE B CE2 1 
ATOM   5565 C  CZ  . PHE B 1 283 ? 2.826   25.668 63.860  1.00 84.83  ? 312 PHE B CZ  1 
ATOM   5566 N  N   . ASP B 1 284 ? 2.061   21.166 58.035  1.00 84.08  ? 313 ASP B N   1 
ATOM   5567 C  CA  . ASP B 1 284 ? 1.600   20.445 56.840  1.00 84.62  ? 313 ASP B CA  1 
ATOM   5568 C  C   . ASP B 1 284 ? 1.014   19.055 57.188  1.00 84.36  ? 313 ASP B C   1 
ATOM   5569 O  O   . ASP B 1 284 ? 0.158   18.543 56.468  1.00 84.60  ? 313 ASP B O   1 
ATOM   5570 C  CB  . ASP B 1 284 ? 2.758   20.305 55.844  1.00 86.75  ? 313 ASP B CB  1 
ATOM   5571 C  CG  . ASP B 1 284 ? 3.914   19.488 56.397  1.00 92.34  ? 313 ASP B CG  1 
ATOM   5572 O  OD1 . ASP B 1 284 ? 4.640   20.003 57.274  1.00 92.80  ? 313 ASP B OD1 1 
ATOM   5573 O  OD2 . ASP B 1 284 ? 4.083   18.329 55.963  1.00 95.21  ? 313 ASP B OD2 1 
ATOM   5574 N  N   . ARG B 1 285 ? 1.501   18.450 58.281  1.00 83.55  ? 314 ARG B N   1 
ATOM   5575 C  CA  . ARG B 1 285 ? 1.042   17.168 58.805  1.00 83.10  ? 314 ARG B CA  1 
ATOM   5576 C  C   . ARG B 1 285 ? 0.453   17.373 60.226  1.00 81.49  ? 314 ARG B C   1 
ATOM   5577 O  O   . ARG B 1 285 ? 0.523   18.476 60.778  1.00 81.60  ? 314 ARG B O   1 
ATOM   5578 C  CB  . ARG B 1 285 ? 2.225   16.196 58.878  1.00 85.44  ? 314 ARG B CB  1 
ATOM   5579 C  CG  . ARG B 1 285 ? 2.643   15.649 57.530  1.00 90.54  ? 314 ARG B CG  1 
ATOM   5580 C  CD  . ARG B 1 285 ? 4.031   15.086 57.612  1.00 95.78  ? 314 ARG B CD  1 
ATOM   5581 N  NE  . ARG B 1 285 ? 4.489   14.625 56.295  1.00 100.66 ? 314 ARG B NE  1 
ATOM   5582 C  CZ  . ARG B 1 285 ? 4.705   13.350 55.979  1.00 104.05 ? 314 ARG B CZ  1 
ATOM   5583 N  NH1 . ARG B 1 285 ? 4.540   12.395 56.888  1.00 104.27 ? 314 ARG B NH1 1 
ATOM   5584 N  NH2 . ARG B 1 285 ? 5.109   13.023 54.756  1.00 103.95 ? 314 ARG B NH2 1 
ATOM   5585 N  N   . ALA B 1 286 ? -0.113  16.310 60.824  1.00 79.81  ? 315 ALA B N   1 
ATOM   5586 C  CA  . ALA B 1 286 ? -0.636  16.374 62.182  1.00 78.89  ? 315 ALA B CA  1 
ATOM   5587 C  C   . ALA B 1 286 ? 0.538   16.616 63.148  1.00 77.57  ? 315 ALA B C   1 
ATOM   5588 O  O   . ALA B 1 286 ? 1.571   15.952 63.056  1.00 77.87  ? 315 ALA B O   1 
ATOM   5589 C  CB  . ALA B 1 286 ? -1.352  15.082 62.530  1.00 79.05  ? 315 ALA B CB  1 
ATOM   5590 N  N   . LEU B 1 287 ? 0.398   17.611 64.020  1.00 75.82  ? 316 LEU B N   1 
ATOM   5591 C  CA  . LEU B 1 287 ? 1.463   18.005 64.916  1.00 74.50  ? 316 LEU B CA  1 
ATOM   5592 C  C   . LEU B 1 287 ? 1.109   17.807 66.392  1.00 73.59  ? 316 LEU B C   1 
ATOM   5593 O  O   . LEU B 1 287 ? 0.194   18.451 66.915  1.00 73.67  ? 316 LEU B O   1 
ATOM   5594 C  CB  . LEU B 1 287 ? 1.795   19.473 64.627  1.00 74.38  ? 316 LEU B CB  1 
ATOM   5595 C  CG  . LEU B 1 287 ? 2.837   20.139 65.503  1.00 75.62  ? 316 LEU B CG  1 
ATOM   5596 C  CD1 . LEU B 1 287 ? 4.167   19.418 65.417  1.00 76.27  ? 316 LEU B CD1 1 
ATOM   5597 C  CD2 . LEU B 1 287 ? 2.997   21.603 65.129  1.00 75.81  ? 316 LEU B CD2 1 
ATOM   5598 N  N   . PRO B 1 288 ? 1.861   16.942 67.094  1.00 72.30  ? 317 PRO B N   1 
ATOM   5599 C  CA  . PRO B 1 288 ? 1.595   16.747 68.524  1.00 71.42  ? 317 PRO B CA  1 
ATOM   5600 C  C   . PRO B 1 288 ? 1.985   17.982 69.336  1.00 70.59  ? 317 PRO B C   1 
ATOM   5601 O  O   . PRO B 1 288 ? 3.119   18.460 69.240  1.00 70.85  ? 317 PRO B O   1 
ATOM   5602 C  CB  . PRO B 1 288 ? 2.433   15.512 68.884  1.00 72.00  ? 317 PRO B CB  1 
ATOM   5603 C  CG  . PRO B 1 288 ? 2.927   14.955 67.567  1.00 72.51  ? 317 PRO B CG  1 
ATOM   5604 C  CD  . PRO B 1 288 ? 2.985   16.105 66.634  1.00 71.35  ? 317 PRO B CD  1 
ATOM   5605 N  N   . VAL B 1 289 ? 1.029   18.533 70.084  1.00 69.27  ? 318 VAL B N   1 
ATOM   5606 C  CA  . VAL B 1 289 ? 1.281   19.714 70.891  1.00 68.61  ? 318 VAL B CA  1 
ATOM   5607 C  C   . VAL B 1 289 ? 1.473   19.372 72.377  1.00 68.11  ? 318 VAL B C   1 
ATOM   5608 O  O   . VAL B 1 289 ? 2.187   20.090 73.078  1.00 68.39  ? 318 VAL B O   1 
ATOM   5609 C  CB  . VAL B 1 289 ? 0.214   20.815 70.669  1.00 68.97  ? 318 VAL B CB  1 
ATOM   5610 C  CG1 . VAL B 1 289 ? 0.257   21.334 69.243  1.00 69.32  ? 318 VAL B CG1 1 
ATOM   5611 C  CG2 . VAL B 1 289 ? -1.185  20.321 71.016  1.00 69.43  ? 318 VAL B CG2 1 
ATOM   5612 N  N   . LEU B 1 290 ? 0.854   18.284 72.858  1.00 67.15  ? 319 LEU B N   1 
ATOM   5613 C  CA  . LEU B 1 290 ? 0.961   17.914 74.266  1.00 66.80  ? 319 LEU B CA  1 
ATOM   5614 C  C   . LEU B 1 290 ? 0.880   16.405 74.415  1.00 66.34  ? 319 LEU B C   1 
ATOM   5615 O  O   . LEU B 1 290 ? 0.042   15.775 73.780  1.00 66.23  ? 319 LEU B O   1 
ATOM   5616 C  CB  . LEU B 1 290 ? -0.160  18.605 75.070  1.00 66.87  ? 319 LEU B CB  1 
ATOM   5617 C  CG  . LEU B 1 290 ? -0.359  18.169 76.530  1.00 67.92  ? 319 LEU B CG  1 
ATOM   5618 C  CD1 . LEU B 1 290 ? 0.836   18.530 77.392  1.00 68.25  ? 319 LEU B CD1 1 
ATOM   5619 C  CD2 . LEU B 1 290 ? -1.605  18.783 77.108  1.00 68.24  ? 319 LEU B CD2 1 
ATOM   5620 N  N   . HIS B 1 291 ? 1.760   15.819 75.234  1.00 65.88  ? 320 HIS B N   1 
ATOM   5621 C  CA  . HIS B 1 291 ? 1.758   14.378 75.438  1.00 65.98  ? 320 HIS B CA  1 
ATOM   5622 C  C   . HIS B 1 291 ? 1.166   14.028 76.780  1.00 65.70  ? 320 HIS B C   1 
ATOM   5623 O  O   . HIS B 1 291 ? 1.708   14.404 77.811  1.00 66.05  ? 320 HIS B O   1 
ATOM   5624 C  CB  . HIS B 1 291 ? 3.171   13.787 75.311  1.00 66.76  ? 320 HIS B CB  1 
ATOM   5625 C  CG  . HIS B 1 291 ? 3.188   12.291 75.275  1.00 68.82  ? 320 HIS B CG  1 
ATOM   5626 N  ND1 . HIS B 1 291 ? 3.015   11.598 74.092  1.00 70.81  ? 320 HIS B ND1 1 
ATOM   5627 C  CD2 . HIS B 1 291 ? 3.360   11.401 76.280  1.00 69.93  ? 320 HIS B CD2 1 
ATOM   5628 C  CE1 . HIS B 1 291 ? 3.094   10.314 74.411  1.00 71.24  ? 320 HIS B CE1 1 
ATOM   5629 N  NE2 . HIS B 1 291 ? 3.303   10.147 75.714  1.00 71.09  ? 320 HIS B NE2 1 
ATOM   5630 N  N   . ILE B 1 292 ? 0.061   13.296 76.772  1.00 64.91  ? 321 ILE B N   1 
ATOM   5631 C  CA  . ILE B 1 292 ? -0.579  12.857 77.999  1.00 64.71  ? 321 ILE B CA  1 
ATOM   5632 C  C   . ILE B 1 292 ? -0.081  11.454 78.350  1.00 64.22  ? 321 ILE B C   1 
ATOM   5633 O  O   . ILE B 1 292 ? -0.110  10.562 77.500  1.00 64.56  ? 321 ILE B O   1 
ATOM   5634 C  CB  . ILE B 1 292 ? -2.109  12.879 77.829  1.00 65.15  ? 321 ILE B CB  1 
ATOM   5635 C  CG1 . ILE B 1 292 ? -2.604  14.266 77.387  1.00 65.89  ? 321 ILE B CG1 1 
ATOM   5636 C  CG2 . ILE B 1 292 ? -2.800  12.391 79.092  1.00 65.55  ? 321 ILE B CG2 1 
ATOM   5637 C  CD1 . ILE B 1 292 ? -2.285  15.348 78.339  1.00 67.19  ? 321 ILE B CD1 1 
ATOM   5638 N  N   . GLN B 1 293 ? 0.377   11.261 79.596  1.00 63.07  ? 322 GLN B N   1 
ATOM   5639 C  CA  . GLN B 1 293 ? 0.869   9.979  80.074  1.00 62.48  ? 322 GLN B CA  1 
ATOM   5640 C  C   . GLN B 1 293 ? 0.218   9.658  81.405  1.00 61.75  ? 322 GLN B C   1 
ATOM   5641 O  O   . GLN B 1 293 ? 0.606   10.214 82.435  1.00 61.74  ? 322 GLN B O   1 
ATOM   5642 C  CB  . GLN B 1 293 ? 2.408   9.992  80.216  1.00 64.00  ? 322 GLN B CB  1 
ATOM   5643 C  CG  . GLN B 1 293 ? 3.019   8.729  80.871  1.00 66.59  ? 322 GLN B CG  1 
ATOM   5644 C  CD  . GLN B 1 293 ? 2.826   7.458  80.077  1.00 69.54  ? 322 GLN B CD  1 
ATOM   5645 O  OE1 . GLN B 1 293 ? 3.520   7.203  79.094  1.00 71.09  ? 322 GLN B OE1 1 
ATOM   5646 N  NE2 . GLN B 1 293 ? 1.890   6.623  80.494  1.00 69.62  ? 322 GLN B NE2 1 
ATOM   5647 N  N   . PRO B 1 294 ? -0.767  8.742  81.401  1.00 61.08  ? 323 PRO B N   1 
ATOM   5648 C  CA  . PRO B 1 294 ? -1.436  8.375  82.654  1.00 60.96  ? 323 PRO B CA  1 
ATOM   5649 C  C   . PRO B 1 294 ? -0.540  7.651  83.659  1.00 61.55  ? 323 PRO B C   1 
ATOM   5650 O  O   . PRO B 1 294 ? 0.217   6.740  83.319  1.00 61.53  ? 323 PRO B O   1 
ATOM   5651 C  CB  . PRO B 1 294 ? -2.610  7.505  82.192  1.00 61.32  ? 323 PRO B CB  1 
ATOM   5652 C  CG  . PRO B 1 294 ? -2.760  7.785  80.733  1.00 61.73  ? 323 PRO B CG  1 
ATOM   5653 C  CD  . PRO B 1 294 ? -1.360  8.029  80.260  1.00 60.41  ? 323 PRO B CD  1 
ATOM   5654 N  N   . THR B 1 295 ? -0.615  8.084  84.908  1.00 62.03  ? 324 THR B N   1 
ATOM   5655 C  CA  . THR B 1 295 ? 0.184   7.497  85.986  1.00 62.96  ? 324 THR B CA  1 
ATOM   5656 C  C   . THR B 1 295 ? -0.564  6.295  86.604  1.00 63.70  ? 324 THR B C   1 
ATOM   5657 O  O   . THR B 1 295 ? -1.676  5.991  86.168  1.00 64.10  ? 324 THR B O   1 
ATOM   5658 C  CB  . THR B 1 295 ? 0.555   8.588  87.009  1.00 64.25  ? 324 THR B CB  1 
ATOM   5659 O  OG1 . THR B 1 295 ? -0.593  8.913  87.793  1.00 65.29  ? 324 THR B OG1 1 
ATOM   5660 C  CG2 . THR B 1 295 ? 1.127   9.839  86.353  1.00 64.76  ? 324 THR B CG2 1 
ATOM   5661 N  N   . LEU B 1 296 ? 0.036   5.594  87.593  1.00 63.68  ? 325 LEU B N   1 
ATOM   5662 C  CA  . LEU B 1 296 ? -0.663  4.481  88.233  1.00 64.06  ? 325 LEU B CA  1 
ATOM   5663 C  C   . LEU B 1 296 ? -1.822  4.962  89.124  1.00 64.12  ? 325 LEU B C   1 
ATOM   5664 O  O   . LEU B 1 296 ? -2.816  4.251  89.270  1.00 63.78  ? 325 LEU B O   1 
ATOM   5665 C  CB  . LEU B 1 296 ? 0.310   3.567  88.968  1.00 64.30  ? 325 LEU B CB  1 
ATOM   5666 C  CG  . LEU B 1 296 ? 1.320   2.858  88.066  1.00 66.12  ? 325 LEU B CG  1 
ATOM   5667 C  CD1 . LEU B 1 296 ? 2.177   1.948  88.854  1.00 67.13  ? 325 LEU B CD1 1 
ATOM   5668 C  CD2 . LEU B 1 296 ? 0.641   2.013  87.011  1.00 66.74  ? 325 LEU B CD2 1 
ATOM   5669 N  N   . LYS B 1 297 ? -1.718  6.215  89.642  1.00 64.28  ? 326 LYS B N   1 
ATOM   5670 C  CA  . LYS B 1 297 ? -2.736  6.885  90.451  1.00 64.76  ? 326 LYS B CA  1 
ATOM   5671 C  C   . LYS B 1 297 ? -4.024  7.164  89.652  1.00 64.92  ? 326 LYS B C   1 
ATOM   5672 O  O   . LYS B 1 297 ? -4.022  7.064  88.423  1.00 65.02  ? 326 LYS B O   1 
ATOM   5673 C  CB  . LYS B 1 297 ? -2.169  8.180  91.047  1.00 66.67  ? 326 LYS B CB  1 
ATOM   5674 C  CG  . LYS B 1 297 ? -1.560  7.987  92.423  1.00 72.03  ? 326 LYS B CG  1 
ATOM   5675 C  CD  . LYS B 1 297 ? -1.327  9.341  93.135  1.00 78.04  ? 326 LYS B CD  1 
ATOM   5676 C  CE  . LYS B 1 297 ? -1.743  9.366  94.602  1.00 81.95  ? 326 LYS B CE  1 
ATOM   5677 N  NZ  . LYS B 1 297 ? -1.444  10.676 95.243  1.00 83.96  ? 326 LYS B NZ  1 
ATOM   5678 N  N   . SER B 1 298 ? -5.117  7.512  90.357  1.00 64.76  ? 327 SER B N   1 
ATOM   5679 C  CA  . SER B 1 298 ? -6.423  7.750  89.739  1.00 65.13  ? 327 SER B CA  1 
ATOM   5680 C  C   . SER B 1 298 ? -7.273  8.813  90.466  1.00 65.39  ? 327 SER B C   1 
ATOM   5681 O  O   . SER B 1 298 ? -6.851  9.319  91.506  1.00 65.40  ? 327 SER B O   1 
ATOM   5682 C  CB  . SER B 1 298 ? -7.178  6.430  89.598  1.00 66.40  ? 327 SER B CB  1 
ATOM   5683 O  OG  . SER B 1 298 ? -7.041  5.633  90.762  1.00 69.17  ? 327 SER B OG  1 
ATOM   5684 N  N   . ASN B 1 299 ? -8.447  9.182  89.913  1.00 65.73  ? 328 ASN B N   1 
ATOM   5685 C  CA  . ASN B 1 299 ? -9.296  10.190 90.551  1.00 66.91  ? 328 ASN B CA  1 
ATOM   5686 C  C   . ASN B 1 299 ? -10.785 9.851  90.534  1.00 68.29  ? 328 ASN B C   1 
ATOM   5687 O  O   . ASN B 1 299 ? -11.251 9.152  89.633  1.00 68.10  ? 328 ASN B O   1 
ATOM   5688 C  CB  . ASN B 1 299 ? -9.048  11.597 89.982  1.00 67.75  ? 328 ASN B CB  1 
ATOM   5689 C  CG  . ASN B 1 299 ? -9.238  11.783 88.489  1.00 69.76  ? 328 ASN B CG  1 
ATOM   5690 O  OD1 . ASN B 1 299 ? -9.915  11.019 87.788  1.00 70.50  ? 328 ASN B OD1 1 
ATOM   5691 N  ND2 . ASN B 1 299 ? -8.646  12.835 87.974  1.00 69.91  ? 328 ASN B ND2 1 
ATOM   5692 N  N   . GLU B 1 300 ? -11.538 10.384 91.523  1.00 69.72  ? 329 GLU B N   1 
ATOM   5693 C  CA  . GLU B 1 300 ? -12.991 10.178 91.649  1.00 71.54  ? 329 GLU B CA  1 
ATOM   5694 C  C   . GLU B 1 300 ? -13.794 10.885 90.526  1.00 71.92  ? 329 GLU B C   1 
ATOM   5695 O  O   . GLU B 1 300 ? -15.002 10.669 90.441  1.00 72.27  ? 329 GLU B O   1 
ATOM   5696 C  CB  . GLU B 1 300 ? -13.530 10.695 93.014  1.00 75.77  ? 329 GLU B CB  1 
ATOM   5697 C  CG  . GLU B 1 300 ? -12.799 10.273 94.288  1.00 83.27  ? 329 GLU B CG  1 
ATOM   5698 C  CD  . GLU B 1 300 ? -13.503 10.654 95.591  1.00 92.23  ? 329 GLU B CD  1 
ATOM   5699 O  OE1 . GLU B 1 300 ? -12.974 10.309 96.675  1.00 94.45  ? 329 GLU B OE1 1 
ATOM   5700 O  OE2 . GLU B 1 300 ? -14.588 11.281 95.532  1.00 94.22  ? 329 GLU B OE2 1 
ATOM   5701 N  N   . ALA B 1 301 ? -13.142 11.767 89.725  1.00 71.65  ? 330 ALA B N   1 
ATOM   5702 C  CA  . ALA B 1 301 ? -13.733 12.543 88.632  1.00 71.80  ? 330 ALA B CA  1 
ATOM   5703 C  C   . ALA B 1 301 ? -14.570 11.730 87.650  1.00 72.22  ? 330 ALA B C   1 
ATOM   5704 O  O   . ALA B 1 301 ? -14.212 10.604 87.294  1.00 72.16  ? 330 ALA B O   1 
ATOM   5705 C  CB  . ALA B 1 301 ? -12.657 13.319 87.892  1.00 71.68  ? 330 ALA B CB  1 
ATOM   5706 N  N   . LYS B 1 302 ? -15.719 12.303 87.246  1.00 72.48  ? 331 LYS B N   1 
ATOM   5707 C  CA  . LYS B 1 302 ? -16.671 11.670 86.330  1.00 73.07  ? 331 LYS B CA  1 
ATOM   5708 C  C   . LYS B 1 302 ? -17.159 12.656 85.245  1.00 73.14  ? 331 LYS B C   1 
ATOM   5709 O  O   . LYS B 1 302 ? -17.224 13.859 85.484  1.00 73.54  ? 331 LYS B O   1 
ATOM   5710 C  CB  . LYS B 1 302 ? -17.876 11.104 87.118  1.00 74.81  ? 331 LYS B CB  1 
ATOM   5711 C  CG  . LYS B 1 302 ? -17.510 9.981  88.095  1.00 78.79  ? 331 LYS B CG  1 
ATOM   5712 C  CD  . LYS B 1 302 ? -18.733 9.358  88.774  1.00 83.37  ? 331 LYS B CD  1 
ATOM   5713 C  CE  . LYS B 1 302 ? -19.084 9.997  90.100  1.00 87.11  ? 331 LYS B CE  1 
ATOM   5714 N  NZ  . LYS B 1 302 ? -20.428 9.568  90.590  1.00 89.11  ? 331 LYS B NZ  1 
ATOM   5715 N  N   . LEU B 1 303 ? -17.486 12.147 84.062  1.00 72.56  ? 332 LEU B N   1 
ATOM   5716 C  CA  . LEU B 1 303 ? -18.020 12.954 82.980  1.00 73.08  ? 332 LEU B CA  1 
ATOM   5717 C  C   . LEU B 1 303 ? -19.543 12.992 83.194  1.00 74.48  ? 332 LEU B C   1 
ATOM   5718 O  O   . LEU B 1 303 ? -20.199 11.956 83.065  1.00 75.26  ? 332 LEU B O   1 
ATOM   5719 C  CB  . LEU B 1 303 ? -17.688 12.251 81.665  1.00 72.74  ? 332 LEU B CB  1 
ATOM   5720 C  CG  . LEU B 1 303 ? -18.304 12.826 80.417  1.00 73.33  ? 332 LEU B CG  1 
ATOM   5721 C  CD1 . LEU B 1 303 ? -17.479 13.963 79.880  1.00 73.42  ? 332 LEU B CD1 1 
ATOM   5722 C  CD2 . LEU B 1 303 ? -18.429 11.771 79.378  1.00 73.95  ? 332 LEU B CD2 1 
ATOM   5723 N  N   . PRO B 1 304 ? -20.130 14.136 83.588  1.00 74.73  ? 333 PRO B N   1 
ATOM   5724 C  CA  . PRO B 1 304 ? -21.571 14.150 83.907  1.00 75.14  ? 333 PRO B CA  1 
ATOM   5725 C  C   . PRO B 1 304 ? -22.498 14.159 82.710  1.00 76.18  ? 333 PRO B C   1 
ATOM   5726 O  O   . PRO B 1 304 ? -22.195 14.822 81.725  1.00 76.65  ? 333 PRO B O   1 
ATOM   5727 C  CB  . PRO B 1 304 ? -21.750 15.420 84.751  1.00 75.72  ? 333 PRO B CB  1 
ATOM   5728 C  CG  . PRO B 1 304 ? -20.383 16.045 84.884  1.00 76.15  ? 333 PRO B CG  1 
ATOM   5729 C  CD  . PRO B 1 304 ? -19.506 15.447 83.831  1.00 74.45  ? 333 PRO B CD  1 
ATOM   5730 N  N   . ASP B 1 305 ? -23.648 13.463 82.802  1.00 76.35  ? 334 ASP B N   1 
ATOM   5731 C  CA  . ASP B 1 305 ? -24.621 13.434 81.706  1.00 76.97  ? 334 ASP B CA  1 
ATOM   5732 C  C   . ASP B 1 305 ? -25.122 14.849 81.378  1.00 76.61  ? 334 ASP B C   1 
ATOM   5733 O  O   . ASP B 1 305 ? -25.282 15.203 80.207  1.00 76.50  ? 334 ASP B O   1 
ATOM   5734 C  CB  . ASP B 1 305 ? -25.794 12.517 82.059  1.00 79.54  ? 334 ASP B CB  1 
ATOM   5735 C  CG  . ASP B 1 305 ? -25.398 11.066 82.179  1.00 86.12  ? 334 ASP B CG  1 
ATOM   5736 O  OD1 . ASP B 1 305 ? -24.574 10.606 81.358  1.00 87.16  ? 334 ASP B OD1 1 
ATOM   5737 O  OD2 . ASP B 1 305 ? -25.914 10.385 83.094  1.00 89.31  ? 334 ASP B OD2 1 
ATOM   5738 N  N   . ALA B 1 306 ? -25.334 15.656 82.421  1.00 76.16  ? 335 ALA B N   1 
ATOM   5739 C  CA  . ALA B 1 306 ? -25.757 17.043 82.289  1.00 76.29  ? 335 ALA B CA  1 
ATOM   5740 C  C   . ALA B 1 306 ? -24.792 17.930 83.077  1.00 76.43  ? 335 ALA B C   1 
ATOM   5741 O  O   . ALA B 1 306 ? -24.340 17.547 84.157  1.00 76.68  ? 335 ALA B O   1 
ATOM   5742 C  CB  . ALA B 1 306 ? -27.169 17.212 82.819  1.00 76.30  ? 335 ALA B CB  1 
ATOM   5743 N  N   . LEU B 1 307 ? -24.461 19.108 82.535  1.00 76.13  ? 336 LEU B N   1 
ATOM   5744 C  CA  . LEU B 1 307 ? -23.535 20.017 83.200  1.00 76.40  ? 336 LEU B CA  1 
ATOM   5745 C  C   . LEU B 1 307 ? -24.287 21.132 83.968  1.00 77.02  ? 336 LEU B C   1 
ATOM   5746 O  O   . LEU B 1 307 ? -24.736 20.885 85.084  1.00 77.14  ? 336 LEU B O   1 
ATOM   5747 C  CB  . LEU B 1 307 ? -22.476 20.549 82.211  1.00 76.22  ? 336 LEU B CB  1 
ATOM   5748 C  CG  . LEU B 1 307 ? -21.696 19.481 81.473  1.00 77.17  ? 336 LEU B CG  1 
ATOM   5749 C  CD1 . LEU B 1 307 ? -21.077 20.031 80.213  1.00 77.65  ? 336 LEU B CD1 1 
ATOM   5750 C  CD2 . LEU B 1 307 ? -20.672 18.847 82.368  1.00 77.58  ? 336 LEU B CD2 1 
ATOM   5751 N  N   . VAL B 1 308 ? -24.465 22.320 83.383  1.00 77.29  ? 337 VAL B N   1 
ATOM   5752 C  CA  . VAL B 1 308 ? -25.175 23.427 84.028  1.00 77.95  ? 337 VAL B CA  1 
ATOM   5753 C  C   . VAL B 1 308 ? -26.530 23.661 83.336  1.00 78.64  ? 337 VAL B C   1 
ATOM   5754 O  O   . VAL B 1 308 ? -26.820 22.987 82.338  1.00 78.84  ? 337 VAL B O   1 
ATOM   5755 C  CB  . VAL B 1 308 ? -24.284 24.698 83.979  1.00 78.46  ? 337 VAL B CB  1 
ATOM   5756 C  CG1 . VAL B 1 308 ? -22.973 24.474 84.726  1.00 79.07  ? 337 VAL B CG1 1 
ATOM   5757 C  CG2 . VAL B 1 308 ? -24.030 25.132 82.537  1.00 78.61  ? 337 VAL B CG2 1 
ATOM   5758 N  N   . ASN B 1 309 ? -27.374 24.587 83.853  1.00 78.86  ? 338 ASN B N   1 
ATOM   5759 C  CA  . ASN B 1 309 ? -28.624 24.890 83.161  1.00 79.64  ? 338 ASN B CA  1 
ATOM   5760 C  C   . ASN B 1 309 ? -28.292 25.884 82.070  1.00 79.23  ? 338 ASN B C   1 
ATOM   5761 O  O   . ASN B 1 309 ? -27.984 27.037 82.367  1.00 78.98  ? 338 ASN B O   1 
ATOM   5762 C  CB  . ASN B 1 309 ? -29.700 25.472 84.079  1.00 81.78  ? 338 ASN B CB  1 
ATOM   5763 C  CG  . ASN B 1 309 ? -30.948 25.878 83.312  1.00 85.95  ? 338 ASN B CG  1 
ATOM   5764 O  OD1 . ASN B 1 309 ? -31.636 25.035 82.712  1.00 87.74  ? 338 ASN B OD1 1 
ATOM   5765 N  ND2 . ASN B 1 309 ? -31.234 27.182 83.271  1.00 86.26  ? 338 ASN B ND2 1 
ATOM   5766 N  N   . MET B 1 310 ? -28.353 25.440 80.816  1.00 79.01  ? 339 MET B N   1 
ATOM   5767 C  CA  . MET B 1 310 ? -28.092 26.324 79.690  1.00 79.29  ? 339 MET B CA  1 
ATOM   5768 C  C   . MET B 1 310 ? -29.428 26.928 79.249  1.00 79.78  ? 339 MET B C   1 
ATOM   5769 O  O   . MET B 1 310 ? -30.328 26.194 78.831  1.00 80.07  ? 339 MET B O   1 
ATOM   5770 C  CB  . MET B 1 310 ? -27.407 25.555 78.542  1.00 79.26  ? 339 MET B CB  1 
ATOM   5771 C  CG  . MET B 1 310 ? -27.201 26.375 77.280  1.00 79.86  ? 339 MET B CG  1 
ATOM   5772 S  SD  . MET B 1 310 ? -26.297 27.914 77.544  1.00 79.38  ? 339 MET B SD  1 
ATOM   5773 C  CE  . MET B 1 310 ? -24.754 27.291 78.149  1.00 76.65  ? 339 MET B CE  1 
ATOM   5774 N  N   . PRO B 1 311 ? -29.602 28.256 79.390  1.00 79.51  ? 340 PRO B N   1 
ATOM   5775 C  CA  . PRO B 1 311 ? -30.886 28.861 79.012  1.00 79.58  ? 340 PRO B CA  1 
ATOM   5776 C  C   . PRO B 1 311 ? -31.181 28.753 77.526  1.00 79.84  ? 340 PRO B C   1 
ATOM   5777 O  O   . PRO B 1 311 ? -30.264 28.609 76.707  1.00 80.06  ? 340 PRO B O   1 
ATOM   5778 C  CB  . PRO B 1 311 ? -30.733 30.329 79.430  1.00 80.31  ? 340 PRO B CB  1 
ATOM   5779 C  CG  . PRO B 1 311 ? -29.526 30.377 80.317  1.00 80.62  ? 340 PRO B CG  1 
ATOM   5780 C  CD  . PRO B 1 311 ? -28.644 29.267 79.869  1.00 78.98  ? 340 PRO B CD  1 
ATOM   5781 N  N   . ALA B 1 312 ? -32.465 28.815 77.179  1.00 79.63  ? 341 ALA B N   1 
ATOM   5782 C  CA  . ALA B 1 312 ? -32.857 28.765 75.779  1.00 80.04  ? 341 ALA B CA  1 
ATOM   5783 C  C   . ALA B 1 312 ? -32.490 30.088 75.107  1.00 80.41  ? 341 ALA B C   1 
ATOM   5784 O  O   . ALA B 1 312 ? -32.380 31.119 75.780  1.00 80.68  ? 341 ALA B O   1 
ATOM   5785 C  CB  . ALA B 1 312 ? -34.345 28.513 75.665  1.00 80.20  ? 341 ALA B CB  1 
ATOM   5786 N  N   . VAL B 1 313 ? -32.267 30.058 73.790  1.00 80.29  ? 342 VAL B N   1 
ATOM   5787 C  CA  . VAL B 1 313 ? -31.944 31.283 73.066  1.00 80.82  ? 342 VAL B CA  1 
ATOM   5788 C  C   . VAL B 1 313 ? -33.249 32.031 72.790  1.00 81.35  ? 342 VAL B C   1 
ATOM   5789 O  O   . VAL B 1 313 ? -34.156 31.498 72.140  1.00 81.24  ? 342 VAL B O   1 
ATOM   5790 C  CB  . VAL B 1 313 ? -31.159 31.040 71.762  1.00 81.52  ? 342 VAL B CB  1 
ATOM   5791 C  CG1 . VAL B 1 313 ? -30.579 32.347 71.239  1.00 81.84  ? 342 VAL B CG1 1 
ATOM   5792 C  CG2 . VAL B 1 313 ? -30.065 30.005 71.960  1.00 82.12  ? 342 VAL B CG2 1 
ATOM   5793 N  N   . PRO B 1 314 ? -33.382 33.257 73.313  1.00 81.61  ? 343 PRO B N   1 
ATOM   5794 C  CA  . PRO B 1 314 ? -34.615 34.016 73.065  1.00 81.94  ? 343 PRO B CA  1 
ATOM   5795 C  C   . PRO B 1 314 ? -34.740 34.393 71.588  1.00 82.91  ? 343 PRO B C   1 
ATOM   5796 O  O   . PRO B 1 314 ? -33.754 34.842 70.990  1.00 83.16  ? 343 PRO B O   1 
ATOM   5797 C  CB  . PRO B 1 314 ? -34.445 35.280 73.919  1.00 82.24  ? 343 PRO B CB  1 
ATOM   5798 C  CG  . PRO B 1 314 ? -33.247 35.057 74.769  1.00 82.70  ? 343 PRO B CG  1 
ATOM   5799 C  CD  . PRO B 1 314 ? -32.406 34.025 74.107  1.00 81.16  ? 343 PRO B CD  1 
ATOM   5800 N  N   . ALA B 1 315 ? -35.936 34.203 70.988  1.00 82.79  ? 344 ALA B N   1 
ATOM   5801 C  CA  . ALA B 1 315 ? -36.143 34.634 69.609  1.00 82.93  ? 344 ALA B CA  1 
ATOM   5802 C  C   . ALA B 1 315 ? -36.386 36.125 69.743  1.00 83.23  ? 344 ALA B C   1 
ATOM   5803 O  O   . ALA B 1 315 ? -37.490 36.541 70.091  1.00 83.47  ? 344 ALA B O   1 
ATOM   5804 C  CB  . ALA B 1 315 ? -37.363 33.959 69.005  1.00 82.93  ? 344 ALA B CB  1 
ATOM   5805 N  N   . ALA B 1 316 ? -35.309 36.909 69.646  1.00 83.20  ? 345 ALA B N   1 
ATOM   5806 C  CA  . ALA B 1 316 ? -35.369 38.353 69.811  1.00 83.71  ? 345 ALA B CA  1 
ATOM   5807 C  C   . ALA B 1 316 ? -35.840 38.980 68.502  1.00 84.17  ? 345 ALA B C   1 
ATOM   5808 O  O   . ALA B 1 316 ? -35.049 39.490 67.707  1.00 84.14  ? 345 ALA B O   1 
ATOM   5809 C  CB  . ALA B 1 316 ? -34.007 38.884 70.213  1.00 83.80  ? 345 ALA B CB  1 
ATOM   5810 N  N   . ASP B 1 317 ? -37.150 38.862 68.273  1.00 84.25  ? 346 ASP B N   1 
ATOM   5811 C  CA  . ASP B 1 317 ? -37.911 39.308 67.115  1.00 84.50  ? 346 ASP B CA  1 
ATOM   5812 C  C   . ASP B 1 317 ? -37.866 40.815 66.855  1.00 84.60  ? 346 ASP B C   1 
ATOM   5813 O  O   . ASP B 1 317 ? -37.547 41.216 65.726  1.00 84.84  ? 346 ASP B O   1 
ATOM   5814 C  CB  . ASP B 1 317 ? -39.354 38.813 67.251  1.00 86.04  ? 346 ASP B CB  1 
ATOM   5815 C  CG  . ASP B 1 317 ? -39.613 37.434 66.672  1.00 91.20  ? 346 ASP B CG  1 
ATOM   5816 O  OD1 . ASP B 1 317 ? -38.648 36.807 66.160  1.00 91.81  ? 346 ASP B OD1 1 
ATOM   5817 O  OD2 . ASP B 1 317 ? -40.783 36.985 66.711  1.00 93.71  ? 346 ASP B OD2 1 
ATOM   5818 N  N   . ASN B 1 318 ? -38.172 41.653 67.871  1.00 84.06  ? 347 ASN B N   1 
ATOM   5819 C  CA  . ASN B 1 318 ? -38.154 43.105 67.648  1.00 84.04  ? 347 ASN B CA  1 
ATOM   5820 C  C   . ASN B 1 318 ? -37.098 43.817 68.483  1.00 83.19  ? 347 ASN B C   1 
ATOM   5821 O  O   . ASN B 1 318 ? -37.429 44.599 69.373  1.00 83.49  ? 347 ASN B O   1 
ATOM   5822 C  CB  . ASN B 1 318 ? -39.543 43.728 67.844  1.00 85.66  ? 347 ASN B CB  1 
ATOM   5823 C  CG  . ASN B 1 318 ? -40.657 42.971 67.163  1.00 89.50  ? 347 ASN B CG  1 
ATOM   5824 O  OD1 . ASN B 1 318 ? -40.886 43.105 65.950  1.00 90.75  ? 347 ASN B OD1 1 
ATOM   5825 N  ND2 . ASN B 1 318 ? -41.379 42.154 67.936  1.00 90.24  ? 347 ASN B ND2 1 
ATOM   5826 N  N   . VAL B 1 319 ? -35.826 43.527 68.208  1.00 81.98  ? 348 VAL B N   1 
ATOM   5827 C  CA  . VAL B 1 319 ? -34.721 44.151 68.933  1.00 81.42  ? 348 VAL B CA  1 
ATOM   5828 C  C   . VAL B 1 319 ? -33.875 45.013 67.999  1.00 81.07  ? 348 VAL B C   1 
ATOM   5829 O  O   . VAL B 1 319 ? -33.957 44.867 66.778  1.00 81.29  ? 348 VAL B O   1 
ATOM   5830 C  CB  . VAL B 1 319 ? -33.845 43.101 69.653  1.00 81.62  ? 348 VAL B CB  1 
ATOM   5831 C  CG1 . VAL B 1 319 ? -34.656 42.322 70.678  1.00 81.94  ? 348 VAL B CG1 1 
ATOM   5832 C  CG2 . VAL B 1 319 ? -33.170 42.176 68.644  1.00 81.93  ? 348 VAL B CG2 1 
ATOM   5833 N  N   . LYS B 1 320 ? -33.048 45.907 68.565  1.00 80.37  ? 349 LYS B N   1 
ATOM   5834 C  CA  . LYS B 1 320 ? -32.164 46.739 67.762  1.00 80.54  ? 349 LYS B CA  1 
ATOM   5835 C  C   . LYS B 1 320 ? -31.122 45.838 67.093  1.00 81.36  ? 349 LYS B C   1 
ATOM   5836 O  O   . LYS B 1 320 ? -30.727 44.822 67.664  1.00 81.38  ? 349 LYS B O   1 
ATOM   5837 C  CB  . LYS B 1 320 ? -31.502 47.825 68.636  1.00 81.47  ? 349 LYS B CB  1 
ATOM   5838 C  CG  . LYS B 1 320 ? -30.605 48.817 67.891  1.00 84.36  ? 349 LYS B CG  1 
ATOM   5839 C  CD  . LYS B 1 320 ? -31.346 49.608 66.822  1.00 87.98  ? 349 LYS B CD  1 
ATOM   5840 C  CE  . LYS B 1 320 ? -30.455 50.601 66.117  1.00 91.09  ? 349 LYS B CE  1 
ATOM   5841 N  NZ  . LYS B 1 320 ? -30.138 51.767 66.984  1.00 93.04  ? 349 LYS B NZ  1 
ATOM   5842 N  N   . THR B 1 321 ? -30.773 46.136 65.840  1.00 81.88  ? 350 THR B N   1 
ATOM   5843 C  CA  . THR B 1 321 ? -29.797 45.341 65.105  1.00 82.82  ? 350 THR B CA  1 
ATOM   5844 C  C   . THR B 1 321 ? -28.596 46.184 64.667  1.00 84.17  ? 350 THR B C   1 
ATOM   5845 O  O   . THR B 1 321 ? -28.687 47.410 64.620  1.00 84.56  ? 350 THR B O   1 
ATOM   5846 C  CB  . THR B 1 321 ? -30.455 44.630 63.905  1.00 83.46  ? 350 THR B CB  1 
ATOM   5847 O  OG1 . THR B 1 321 ? -30.723 45.569 62.859  1.00 84.12  ? 350 THR B OG1 1 
ATOM   5848 C  CG2 . THR B 1 321 ? -31.714 43.860 64.288  1.00 83.56  ? 350 THR B CG2 1 
ATOM   5849 N  N   . ARG B 1 322 ? -27.464 45.534 64.359  1.00 84.81  ? 351 ARG B N   1 
ATOM   5850 C  CA  . ARG B 1 322 ? -26.282 46.243 63.867  1.00 85.88  ? 351 ARG B CA  1 
ATOM   5851 C  C   . ARG B 1 322 ? -25.623 45.459 62.727  1.00 86.88  ? 351 ARG B C   1 
ATOM   5852 O  O   . ARG B 1 322 ? -25.675 44.226 62.703  1.00 86.84  ? 351 ARG B O   1 
ATOM   5853 C  CB  . ARG B 1 322 ? -25.237 46.476 64.972  1.00 87.03  ? 351 ARG B CB  1 
ATOM   5854 C  CG  . ARG B 1 322 ? -25.775 46.954 66.304  1.00 89.25  ? 351 ARG B CG  1 
ATOM   5855 C  CD  . ARG B 1 322 ? -25.954 48.447 66.363  1.00 91.59  ? 351 ARG B CD  1 
ATOM   5856 N  NE  . ARG B 1 322 ? -26.465 48.843 67.672  1.00 93.97  ? 351 ARG B NE  1 
ATOM   5857 C  CZ  . ARG B 1 322 ? -26.759 50.089 68.023  1.00 96.01  ? 351 ARG B CZ  1 
ATOM   5858 N  NH1 . ARG B 1 322 ? -26.568 51.090 67.173  1.00 95.74  ? 351 ARG B NH1 1 
ATOM   5859 N  NH2 . ARG B 1 322 ? -27.218 50.349 69.240  1.00 95.87  ? 351 ARG B NH2 1 
ATOM   5860 N  N   . TRP B 1 323 ? -24.985 46.175 61.795  1.00 87.53  ? 352 TRP B N   1 
ATOM   5861 C  CA  . TRP B 1 323 ? -24.259 45.540 60.701  1.00 88.63  ? 352 TRP B CA  1 
ATOM   5862 C  C   . TRP B 1 323 ? -22.788 45.956 60.773  1.00 89.44  ? 352 TRP B C   1 
ATOM   5863 O  O   . TRP B 1 323 ? -22.472 47.149 60.801  1.00 89.52  ? 352 TRP B O   1 
ATOM   5864 C  CB  . TRP B 1 323 ? -24.847 45.906 59.328  1.00 88.71  ? 352 TRP B CB  1 
ATOM   5865 C  CG  . TRP B 1 323 ? -24.148 45.236 58.175  1.00 89.41  ? 352 TRP B CG  1 
ATOM   5866 C  CD1 . TRP B 1 323 ? -23.034 45.675 57.519  1.00 90.36  ? 352 TRP B CD1 1 
ATOM   5867 C  CD2 . TRP B 1 323 ? -24.532 44.010 57.540  1.00 89.63  ? 352 TRP B CD2 1 
ATOM   5868 N  NE1 . TRP B 1 323 ? -22.679 44.777 56.538  1.00 90.67  ? 352 TRP B NE1 1 
ATOM   5869 C  CE2 . TRP B 1 323 ? -23.593 43.754 56.518  1.00 90.39  ? 352 TRP B CE2 1 
ATOM   5870 C  CE3 . TRP B 1 323 ? -25.586 43.106 57.729  1.00 90.19  ? 352 TRP B CE3 1 
ATOM   5871 C  CZ2 . TRP B 1 323 ? -23.678 42.636 55.692  1.00 91.00  ? 352 TRP B CZ2 1 
ATOM   5872 C  CZ3 . TRP B 1 323 ? -25.672 42.005 56.901  1.00 91.05  ? 352 TRP B CZ3 1 
ATOM   5873 C  CH2 . TRP B 1 323 ? -24.714 41.766 55.912  1.00 91.13  ? 352 TRP B CH2 1 
ATOM   5874 N  N   . LEU B 1 324 ? -21.890 44.971 60.796  1.00 89.61  ? 353 LEU B N   1 
ATOM   5875 C  CA  . LEU B 1 324 ? -20.471 45.237 60.850  1.00 90.41  ? 353 LEU B CA  1 
ATOM   5876 C  C   . LEU B 1 324 ? -19.784 44.604 59.657  1.00 91.23  ? 353 LEU B C   1 
ATOM   5877 O  O   . LEU B 1 324 ? -19.519 43.410 59.659  1.00 91.53  ? 353 LEU B O   1 
ATOM   5878 C  CB  . LEU B 1 324 ? -19.885 44.716 62.167  1.00 90.69  ? 353 LEU B CB  1 
ATOM   5879 C  CG  . LEU B 1 324 ? -20.495 45.299 63.448  1.00 92.18  ? 353 LEU B CG  1 
ATOM   5880 C  CD1 . LEU B 1 324 ? -19.857 44.702 64.686  1.00 92.88  ? 353 LEU B CD1 1 
ATOM   5881 C  CD2 . LEU B 1 324 ? -20.350 46.791 63.495  1.00 92.66  ? 353 LEU B CD2 1 
ATOM   5882 N  N   . GLN B 1 325 ? -19.508 45.397 58.631  1.00 91.48  ? 354 GLN B N   1 
ATOM   5883 C  CA  . GLN B 1 325 ? -18.851 44.913 57.433  1.00 92.43  ? 354 GLN B CA  1 
ATOM   5884 C  C   . GLN B 1 325 ? -17.333 44.966 57.579  1.00 92.57  ? 354 GLN B C   1 
ATOM   5885 O  O   . GLN B 1 325 ? -16.745 46.047 57.614  1.00 92.62  ? 354 GLN B O   1 
ATOM   5886 C  CB  . GLN B 1 325 ? -19.308 45.720 56.207  1.00 94.80  ? 354 GLN B CB  1 
ATOM   5887 C  CG  . GLN B 1 325 ? -18.617 45.317 54.901  1.00 99.33  ? 354 GLN B CG  1 
ATOM   5888 C  CD  . GLN B 1 325 ? -18.866 43.875 54.523  1.00 104.70 ? 354 GLN B CD  1 
ATOM   5889 O  OE1 . GLN B 1 325 ? -20.008 43.403 54.480  1.00 106.39 ? 354 GLN B OE1 1 
ATOM   5890 N  NE2 . GLN B 1 325 ? -17.797 43.146 54.226  1.00 105.40 ? 354 GLN B NE2 1 
ATOM   5891 N  N   . LEU B 1 326 ? -16.700 43.797 57.665  1.00 92.44  ? 355 LEU B N   1 
ATOM   5892 C  CA  . LEU B 1 326 ? -15.249 43.711 57.749  1.00 92.71  ? 355 LEU B CA  1 
ATOM   5893 C  C   . LEU B 1 326 ? -14.703 43.886 56.340  1.00 93.09  ? 355 LEU B C   1 
ATOM   5894 O  O   . LEU B 1 326 ? -15.183 43.247 55.403  1.00 92.96  ? 355 LEU B O   1 
ATOM   5895 C  CB  . LEU B 1 326 ? -14.804 42.360 58.329  1.00 92.68  ? 355 LEU B CB  1 
ATOM   5896 C  CG  . LEU B 1 326 ? -15.339 42.026 59.710  1.00 93.79  ? 355 LEU B CG  1 
ATOM   5897 C  CD1 . LEU B 1 326 ? -15.018 40.605 60.082  1.00 94.21  ? 355 LEU B CD1 1 
ATOM   5898 C  CD2 . LEU B 1 326 ? -14.794 42.979 60.748  1.00 94.32  ? 355 LEU B CD2 1 
ATOM   5899 N  N   . MET B 1 327 ? -13.719 44.770 56.185  1.00 93.38  ? 356 MET B N   1 
ATOM   5900 C  CA  . MET B 1 327 ? -13.150 45.056 54.879  1.00 94.05  ? 356 MET B CA  1 
ATOM   5901 C  C   . MET B 1 327 ? -11.659 44.869 54.829  1.00 94.04  ? 356 MET B C   1 
ATOM   5902 O  O   . MET B 1 327 ? -10.935 45.392 55.670  1.00 93.87  ? 356 MET B O   1 
ATOM   5903 C  CB  . MET B 1 327 ? -13.479 46.494 54.444  1.00 95.17  ? 356 MET B CB  1 
ATOM   5904 C  CG  . MET B 1 327 ? -14.906 46.690 54.003  1.00 98.14  ? 356 MET B CG  1 
ATOM   5905 S  SD  . MET B 1 327 ? -15.673 48.078 54.870  1.00 104.46 ? 356 MET B SD  1 
ATOM   5906 C  CE  . MET B 1 327 ? -17.050 48.427 53.760  1.00 103.75 ? 356 MET B CE  1 
ATOM   5907 N  N   . MET B 1 328 ? -11.202 44.169 53.794  1.00 94.16  ? 357 MET B N   1 
ATOM   5908 C  CA  . MET B 1 328 ? -9.792  43.961 53.484  1.00 94.81  ? 357 MET B CA  1 
ATOM   5909 C  C   . MET B 1 328 ? -9.573  44.335 52.004  1.00 95.65  ? 357 MET B C   1 
ATOM   5910 O  O   . MET B 1 328 ? -8.922  43.604 51.260  1.00 95.72  ? 357 MET B O   1 
ATOM   5911 C  CB  . MET B 1 328 ? -9.403  42.498 53.717  1.00 94.98  ? 357 MET B CB  1 
ATOM   5912 C  CG  . MET B 1 328 ? -9.358  42.115 55.150  1.00 95.57  ? 357 MET B CG  1 
ATOM   5913 S  SD  . MET B 1 328 ? -8.502  40.555 55.312  1.00 94.22  ? 357 MET B SD  1 
ATOM   5914 C  CE  . MET B 1 328 ? -6.847  41.062 55.008  1.00 92.62  ? 357 MET B CE  1 
ATOM   5915 N  N   . ASP B 1 329 ? -10.137 45.468 51.576  1.00 96.12  ? 358 ASP B N   1 
ATOM   5916 C  CA  . ASP B 1 329 ? -10.047 45.889 50.187  1.00 97.00  ? 358 ASP B CA  1 
ATOM   5917 C  C   . ASP B 1 329 ? -9.412  47.258 50.014  1.00 97.21  ? 358 ASP B C   1 
ATOM   5918 O  O   . ASP B 1 329 ? -9.661  48.181 50.797  1.00 97.44  ? 358 ASP B O   1 
ATOM   5919 C  CB  . ASP B 1 329 ? -11.419 45.807 49.461  1.00 99.27  ? 358 ASP B CB  1 
ATOM   5920 C  CG  . ASP B 1 329 ? -12.676 45.981 50.313  1.00 103.90 ? 358 ASP B CG  1 
ATOM   5921 O  OD1 . ASP B 1 329 ? -12.907 47.110 50.810  1.00 104.61 ? 358 ASP B OD1 1 
ATOM   5922 O  OD2 . ASP B 1 329 ? -13.442 44.994 50.454  1.00 105.96 ? 358 ASP B OD2 1 
ATOM   5923 N  N   . GLY B 1 330 A -8.585  47.362 48.982  1.00 96.91  ? 358 GLY B N   1 
ATOM   5924 C  CA  . GLY B 1 330 A -7.901  48.596 48.622  1.00 97.01  ? 358 GLY B CA  1 
ATOM   5925 C  C   . GLY B 1 330 A -6.768  48.991 49.547  1.00 96.64  ? 358 GLY B C   1 
ATOM   5926 O  O   . GLY B 1 330 A -5.662  48.450 49.456  1.00 96.71  ? 358 GLY B O   1 
ATOM   5927 N  N   . GLY B 1 331 B -7.043  49.964 50.412  1.00 95.92  ? 358 GLY B N   1 
ATOM   5928 C  CA  . GLY B 1 331 B -6.065  50.489 51.360  1.00 95.42  ? 358 GLY B CA  1 
ATOM   5929 C  C   . GLY B 1 331 B -5.649  49.503 52.428  1.00 94.30  ? 358 GLY B C   1 
ATOM   5930 O  O   . GLY B 1 331 B -4.454  49.350 52.698  1.00 94.40  ? 358 GLY B O   1 
ATOM   5931 N  N   . GLY B 1 332 ? -6.629  48.826 53.020  1.00 93.00  ? 431 GLY B N   1 
ATOM   5932 C  CA  . GLY B 1 332 ? -6.337  47.846 54.051  1.00 92.48  ? 431 GLY B CA  1 
ATOM   5933 C  C   . GLY B 1 332 ? -7.524  47.287 54.804  1.00 91.70  ? 431 GLY B C   1 
ATOM   5934 O  O   . GLY B 1 332 ? -8.553  46.954 54.208  1.00 91.67  ? 431 GLY B O   1 
ATOM   5935 N  N   . ASN B 1 333 ? -7.350  47.153 56.132  1.00 90.70  ? 432 ASN B N   1 
ATOM   5936 C  CA  . ASN B 1 333 ? -8.325  46.617 57.072  1.00 90.02  ? 432 ASN B CA  1 
ATOM   5937 C  C   . ASN B 1 333 ? -9.120  47.736 57.704  1.00 89.63  ? 432 ASN B C   1 
ATOM   5938 O  O   . ASN B 1 333 ? -8.540  48.715 58.163  1.00 89.36  ? 432 ASN B O   1 
ATOM   5939 C  CB  . ASN B 1 333 ? -7.615  45.821 58.158  1.00 90.46  ? 432 ASN B CB  1 
ATOM   5940 C  CG  . ASN B 1 333 ? -6.780  44.704 57.606  1.00 92.59  ? 432 ASN B CG  1 
ATOM   5941 O  OD1 . ASN B 1 333 ? -7.147  44.069 56.624  1.00 93.46  ? 432 ASN B OD1 1 
ATOM   5942 N  ND2 . ASN B 1 333 ? -5.635  44.445 58.214  1.00 92.88  ? 432 ASN B ND2 1 
ATOM   5943 N  N   . LYS B 1 334 ? -10.446 47.591 57.732  1.00 89.61  ? 433 LYS B N   1 
ATOM   5944 C  CA  . LYS B 1 334 ? -11.353 48.592 58.300  1.00 90.14  ? 433 LYS B CA  1 
ATOM   5945 C  C   . LYS B 1 334 ? -12.759 48.012 58.480  1.00 90.47  ? 433 LYS B C   1 
ATOM   5946 O  O   . LYS B 1 334 ? -13.137 47.091 57.760  1.00 90.73  ? 433 LYS B O   1 
ATOM   5947 C  CB  . LYS B 1 334 ? -11.411 49.840 57.394  1.00 91.86  ? 433 LYS B CB  1 
ATOM   5948 C  CG  . LYS B 1 334 ? -11.650 49.537 55.912  1.00 95.54  ? 433 LYS B CG  1 
ATOM   5949 C  CD  . LYS B 1 334 ? -10.757 50.382 54.994  1.00 99.10  ? 433 LYS B CD  1 
ATOM   5950 C  CE  . LYS B 1 334 ? -10.904 49.995 53.538  1.00 102.26 ? 433 LYS B CE  1 
ATOM   5951 N  NZ  . LYS B 1 334 ? -9.982  50.764 52.662  1.00 104.24 ? 433 LYS B NZ  1 
ATOM   5952 N  N   . ILE B 1 335 ? -13.536 48.540 59.429  1.00 90.34  ? 434 ILE B N   1 
ATOM   5953 C  CA  . ILE B 1 335 ? -14.908 48.073 59.637  1.00 90.92  ? 434 ILE B CA  1 
ATOM   5954 C  C   . ILE B 1 335 ? -15.856 49.190 59.220  1.00 91.37  ? 434 ILE B C   1 
ATOM   5955 O  O   . ILE B 1 335 ? -15.637 50.337 59.609  1.00 91.33  ? 434 ILE B O   1 
ATOM   5956 C  CB  . ILE B 1 335 ? -15.171 47.594 61.093  1.00 91.48  ? 434 ILE B CB  1 
ATOM   5957 C  CG1 . ILE B 1 335 ? -14.108 46.576 61.555  1.00 92.31  ? 434 ILE B CG1 1 
ATOM   5958 C  CG2 . ILE B 1 335 ? -16.595 47.030 61.241  1.00 91.90  ? 434 ILE B CG2 1 
ATOM   5959 C  CD1 . ILE B 1 335 ? -14.260 46.105 62.980  1.00 93.40  ? 434 ILE B CD1 1 
ATOM   5960 N  N   . ASN B 1 336 ? -16.883 48.866 58.405  1.00 91.58  ? 435 ASN B N   1 
ATOM   5961 C  CA  . ASN B 1 336 ? -17.870 49.824 57.896  1.00 92.23  ? 435 ASN B CA  1 
ATOM   5962 C  C   . ASN B 1 336 ? -17.198 50.991 57.184  1.00 93.10  ? 435 ASN B C   1 
ATOM   5963 O  O   . ASN B 1 336 ? -17.566 52.145 57.390  1.00 93.23  ? 435 ASN B O   1 
ATOM   5964 C  CB  . ASN B 1 336 ? -18.812 50.311 59.007  1.00 92.74  ? 435 ASN B CB  1 
ATOM   5965 C  CG  . ASN B 1 336 ? -19.822 49.282 59.441  1.00 94.71  ? 435 ASN B CG  1 
ATOM   5966 O  OD1 . ASN B 1 336 ? -19.796 48.130 59.013  1.00 95.10  ? 435 ASN B OD1 1 
ATOM   5967 N  ND2 . ASN B 1 336 ? -20.744 49.682 60.298  1.00 95.30  ? 435 ASN B ND2 1 
ATOM   5968 N  N   . GLY B 1 337 ? -16.179 50.678 56.396  1.00 93.66  ? 436 GLY B N   1 
ATOM   5969 C  CA  . GLY B 1 337 ? -15.406 51.670 55.662  1.00 94.90  ? 436 GLY B CA  1 
ATOM   5970 C  C   . GLY B 1 337 ? -14.404 52.413 56.523  1.00 96.20  ? 436 GLY B C   1 
ATOM   5971 O  O   . GLY B 1 337 ? -13.349 52.836 56.044  1.00 96.44  ? 436 GLY B O   1 
ATOM   5972 N  N   . ILE B 1 338 ? -14.721 52.574 57.805  1.00 96.89  ? 437 ILE B N   1 
ATOM   5973 C  CA  . ILE B 1 338 ? -13.877 53.306 58.740  1.00 98.06  ? 437 ILE B CA  1 
ATOM   5974 C  C   . ILE B 1 338 ? -12.817 52.405 59.362  1.00 99.40  ? 437 ILE B C   1 
ATOM   5975 O  O   . ILE B 1 338 ? -13.158 51.373 59.936  1.00 99.58  ? 437 ILE B O   1 
ATOM   5976 C  CB  . ILE B 1 338 ? -14.726 53.969 59.866  1.00 98.35  ? 437 ILE B CB  1 
ATOM   5977 C  CG1 . ILE B 1 338 ? -16.063 54.555 59.361  1.00 99.18  ? 437 ILE B CG1 1 
ATOM   5978 C  CG2 . ILE B 1 338 ? -13.912 55.015 60.612  1.00 98.80  ? 437 ILE B CG2 1 
ATOM   5979 C  CD1 . ILE B 1 338 ? -17.053 54.777 60.435  1.00 100.51 ? 437 ILE B CD1 1 
ATOM   5980 N  N   . ALA B 1 339 ? -11.535 52.805 59.298  1.00 100.12 ? 438 ALA B N   1 
ATOM   5981 C  CA  . ALA B 1 339 ? -10.474 52.061 59.993  1.00 100.96 ? 438 ALA B CA  1 
ATOM   5982 C  C   . ALA B 1 339 ? -10.529 52.474 61.494  1.00 101.84 ? 438 ALA B C   1 
ATOM   5983 O  O   . ALA B 1 339 ? -11.174 53.476 61.834  1.00 102.39 ? 438 ALA B O   1 
ATOM   5984 C  CB  . ALA B 1 339 ? -9.113  52.383 59.394  1.00 100.92 ? 438 ALA B CB  1 
ATOM   5985 N  N   . PHE B 1 340 ? -9.886  51.712 62.392  1.00 101.76 ? 439 PHE B N   1 
ATOM   5986 C  CA  . PHE B 1 340 ? -9.977  51.990 63.827  1.00 102.11 ? 439 PHE B CA  1 
ATOM   5987 C  C   . PHE B 1 340 ? -9.566  53.415 64.259  1.00 102.27 ? 439 PHE B C   1 
ATOM   5988 O  O   . PHE B 1 340 ? -8.389  53.788 64.224  1.00 102.12 ? 439 PHE B O   1 
ATOM   5989 C  CB  . PHE B 1 340 ? -9.234  50.950 64.676  1.00 101.95 ? 439 PHE B CB  1 
ATOM   5990 C  CG  . PHE B 1 340 ? -9.439  51.173 66.157  1.00 102.48 ? 439 PHE B CG  1 
ATOM   5991 C  CD1 . PHE B 1 340 ? -10.712 51.228 66.696  1.00 103.19 ? 439 PHE B CD1 1 
ATOM   5992 C  CD2 . PHE B 1 340 ? -8.363  51.401 66.994  1.00 103.21 ? 439 PHE B CD2 1 
ATOM   5993 C  CE1 . PHE B 1 340 ? -10.901 51.462 68.049  1.00 103.89 ? 439 PHE B CE1 1 
ATOM   5994 C  CE2 . PHE B 1 340 ? -8.556  51.638 68.346  1.00 103.88 ? 439 PHE B CE2 1 
ATOM   5995 C  CZ  . PHE B 1 340 ? -9.822  51.654 68.866  1.00 103.69 ? 439 PHE B CZ  1 
ATOM   5996 N  N   . ASP B 1 341 ? -10.575 54.178 64.718  1.00 102.27 ? 440 ASP B N   1 
ATOM   5997 C  CA  . ASP B 1 341 ? -10.410 55.504 65.295  1.00 102.80 ? 440 ASP B CA  1 
ATOM   5998 C  C   . ASP B 1 341 ? -10.900 55.431 66.751  1.00 102.61 ? 440 ASP B C   1 
ATOM   5999 O  O   . ASP B 1 341 ? -12.087 55.198 67.010  1.00 102.61 ? 440 ASP B O   1 
ATOM   6000 C  CB  . ASP B 1 341 ? -11.181 56.575 64.512  1.00 104.88 ? 440 ASP B CB  1 
ATOM   6001 C  CG  . ASP B 1 341 ? -10.986 57.972 65.083  1.00 109.60 ? 440 ASP B CG  1 
ATOM   6002 O  OD1 . ASP B 1 341 ? -9.914  58.225 65.688  1.00 110.34 ? 440 ASP B OD1 1 
ATOM   6003 O  OD2 . ASP B 1 341 ? -11.900 58.810 64.927  1.00 111.56 ? 440 ASP B OD2 1 
ATOM   6004 N  N   . MET B 1 342 ? -9.963  55.601 67.691  1.00 102.10 ? 441 MET B N   1 
ATOM   6005 C  CA  . MET B 1 342 ? -10.201 55.519 69.129  1.00 102.14 ? 441 MET B CA  1 
ATOM   6006 C  C   . MET B 1 342 ? -11.061 56.664 69.660  1.00 101.41 ? 441 MET B C   1 
ATOM   6007 O  O   . MET B 1 342 ? -11.813 56.478 70.619  1.00 101.35 ? 441 MET B O   1 
ATOM   6008 C  CB  . MET B 1 342 ? -8.850  55.518 69.857  1.00 103.23 ? 441 MET B CB  1 
ATOM   6009 C  CG  . MET B 1 342 ? -8.711  54.419 70.874  1.00 106.29 ? 441 MET B CG  1 
ATOM   6010 S  SD  . MET B 1 342 ? -7.077  54.416 71.650  1.00 112.99 ? 441 MET B SD  1 
ATOM   6011 C  CE  . MET B 1 342 ? -7.172  55.932 72.589  1.00 112.02 ? 441 MET B CE  1 
ATOM   6012 N  N   . ALA B 1 343 ? -10.934 57.853 69.045  1.00 100.62 ? 442 ALA B N   1 
ATOM   6013 C  CA  . ALA B 1 343 ? -11.633 59.075 69.452  1.00 100.09 ? 442 ALA B CA  1 
ATOM   6014 C  C   . ALA B 1 343 ? -13.134 59.085 69.191  1.00 99.02  ? 442 ALA B C   1 
ATOM   6015 O  O   . ALA B 1 343 ? -13.828 59.952 69.723  1.00 99.26  ? 442 ALA B O   1 
ATOM   6016 C  CB  . ALA B 1 343 ? -10.990 60.285 68.793  1.00 100.24 ? 442 ALA B CB  1 
ATOM   6017 N  N   . LYS B 1 344 ? -13.639 58.153 68.371  1.00 97.78  ? 443 LYS B N   1 
ATOM   6018 C  CA  . LYS B 1 344 ? -15.064 58.120 68.054  1.00 96.89  ? 443 LYS B CA  1 
ATOM   6019 C  C   . LYS B 1 344 ? -15.714 56.744 68.175  1.00 95.30  ? 443 LYS B C   1 
ATOM   6020 O  O   . LYS B 1 344 ? -15.638 55.927 67.251  1.00 95.29  ? 443 LYS B O   1 
ATOM   6021 C  CB  . LYS B 1 344 ? -15.323 58.691 66.649  1.00 99.10  ? 443 LYS B CB  1 
ATOM   6022 C  CG  . LYS B 1 344 ? -15.631 60.185 66.610  1.00 103.16 ? 443 LYS B CG  1 
ATOM   6023 C  CD  . LYS B 1 344 ? -15.600 60.722 65.178  1.00 107.91 ? 443 LYS B CD  1 
ATOM   6024 C  CE  . LYS B 1 344 ? -14.199 61.061 64.711  1.00 112.04 ? 443 LYS B CE  1 
ATOM   6025 N  NZ  . LYS B 1 344 ? -14.088 61.099 63.220  1.00 114.26 ? 443 LYS B NZ  1 
ATOM   6026 N  N   . PRO B 1 345 ? -16.440 56.500 69.275  1.00 93.89  ? 444 PRO B N   1 
ATOM   6027 C  CA  . PRO B 1 345 ? -17.173 55.232 69.397  1.00 92.87  ? 444 PRO B CA  1 
ATOM   6028 C  C   . PRO B 1 345 ? -18.284 55.186 68.352  1.00 91.56  ? 444 PRO B C   1 
ATOM   6029 O  O   . PRO B 1 345 ? -19.004 56.167 68.193  1.00 91.78  ? 444 PRO B O   1 
ATOM   6030 C  CB  . PRO B 1 345 ? -17.764 55.287 70.812  1.00 93.76  ? 444 PRO B CB  1 
ATOM   6031 C  CG  . PRO B 1 345 ? -17.052 56.407 71.508  1.00 94.43  ? 444 PRO B CG  1 
ATOM   6032 C  CD  . PRO B 1 345 ? -16.663 57.374 70.441  1.00 93.22  ? 444 PRO B CD  1 
ATOM   6033 N  N   . MET B 1 346 ? -18.382 54.074 67.619  1.00 90.03  ? 445 MET B N   1 
ATOM   6034 C  CA  . MET B 1 346 ? -19.354 53.860 66.552  1.00 88.80  ? 445 MET B CA  1 
ATOM   6035 C  C   . MET B 1 346 ? -20.799 54.112 66.952  1.00 87.92  ? 445 MET B C   1 
ATOM   6036 O  O   . MET B 1 346 ? -21.503 54.790 66.218  1.00 87.92  ? 445 MET B O   1 
ATOM   6037 C  CB  . MET B 1 346 ? -19.202 52.456 65.953  1.00 88.66  ? 445 MET B CB  1 
ATOM   6038 C  CG  . MET B 1 346 ? -19.821 52.336 64.589  1.00 89.28  ? 445 MET B CG  1 
ATOM   6039 S  SD  . MET B 1 346 ? -18.707 51.612 63.374  1.00 87.87  ? 445 MET B SD  1 
ATOM   6040 C  CE  . MET B 1 346 ? -18.948 49.968 63.698  1.00 85.40  ? 445 MET B CE  1 
ATOM   6041 N  N   . PHE B 1 347 ? -21.243 53.592 68.100  1.00 87.24  ? 446 PHE B N   1 
ATOM   6042 C  CA  . PHE B 1 347 ? -22.627 53.774 68.541  1.00 87.20  ? 446 PHE B CA  1 
ATOM   6043 C  C   . PHE B 1 347 ? -22.813 53.527 70.047  1.00 87.21  ? 446 PHE B C   1 
ATOM   6044 O  O   . PHE B 1 347 ? -21.869 53.135 70.726  1.00 87.29  ? 446 PHE B O   1 
ATOM   6045 C  CB  . PHE B 1 347 ? -23.584 52.888 67.709  1.00 87.06  ? 446 PHE B CB  1 
ATOM   6046 C  CG  . PHE B 1 347 ? -23.181 51.439 67.623  1.00 87.62  ? 446 PHE B CG  1 
ATOM   6047 C  CD1 . PHE B 1 347 ? -23.459 50.563 68.656  1.00 88.42  ? 446 PHE B CD1 1 
ATOM   6048 C  CD2 . PHE B 1 347 ? -22.523 50.952 66.509  1.00 88.32  ? 446 PHE B CD2 1 
ATOM   6049 C  CE1 . PHE B 1 347 ? -23.084 49.232 68.577  1.00 89.05  ? 446 PHE B CE1 1 
ATOM   6050 C  CE2 . PHE B 1 347 ? -22.128 49.625 66.443  1.00 89.03  ? 446 PHE B CE2 1 
ATOM   6051 C  CZ  . PHE B 1 347 ? -22.421 48.771 67.471  1.00 88.82  ? 446 PHE B CZ  1 
ATOM   6052 N  N   . ASP B 1 348 ? -24.028 53.762 70.570  1.00 87.08  ? 447 ASP B N   1 
ATOM   6053 C  CA  . ASP B 1 348 ? -24.333 53.534 71.977  1.00 87.43  ? 447 ASP B CA  1 
ATOM   6054 C  C   . ASP B 1 348 ? -25.378 52.442 72.108  1.00 87.57  ? 447 ASP B C   1 
ATOM   6055 O  O   . ASP B 1 348 ? -26.339 52.412 71.345  1.00 87.77  ? 447 ASP B O   1 
ATOM   6056 C  CB  . ASP B 1 348 ? -24.827 54.812 72.663  1.00 89.07  ? 447 ASP B CB  1 
ATOM   6057 C  CG  . ASP B 1 348 ? -25.028 54.640 74.156  1.00 93.98  ? 447 ASP B CG  1 
ATOM   6058 O  OD1 . ASP B 1 348 ? -24.016 54.677 74.902  1.00 95.01  ? 447 ASP B OD1 1 
ATOM   6059 O  OD2 . ASP B 1 348 ? -26.193 54.458 74.584  1.00 95.74  ? 447 ASP B OD2 1 
ATOM   6060 N  N   . VAL B 1 349 ? -25.187 51.546 73.079  1.00 87.34  ? 448 VAL B N   1 
ATOM   6061 C  CA  . VAL B 1 349 ? -26.081 50.435 73.348  1.00 87.65  ? 448 VAL B CA  1 
ATOM   6062 C  C   . VAL B 1 349 ? -26.739 50.623 74.709  1.00 88.32  ? 448 VAL B C   1 
ATOM   6063 O  O   . VAL B 1 349 ? -26.054 50.864 75.696  1.00 88.60  ? 448 VAL B O   1 
ATOM   6064 C  CB  . VAL B 1 349 ? -25.305 49.110 73.281  1.00 88.16  ? 448 VAL B CB  1 
ATOM   6065 C  CG1 . VAL B 1 349 ? -26.170 47.939 73.740  1.00 88.74  ? 448 VAL B CG1 1 
ATOM   6066 C  CG2 . VAL B 1 349 ? -24.755 48.874 71.877  1.00 88.53  ? 448 VAL B CG2 1 
ATOM   6067 N  N   . LYS B 1 350 ? -28.067 50.545 74.761  1.00 88.45  ? 449 LYS B N   1 
ATOM   6068 C  CA  . LYS B 1 350 ? -28.796 50.694 76.011  1.00 88.97  ? 449 LYS B CA  1 
ATOM   6069 C  C   . LYS B 1 350 ? -28.506 49.475 76.887  1.00 89.21  ? 449 LYS B C   1 
ATOM   6070 O  O   . LYS B 1 350 ? -28.804 48.349 76.482  1.00 89.40  ? 449 LYS B O   1 
ATOM   6071 C  CB  . LYS B 1 350 ? -30.301 50.841 75.717  1.00 90.83  ? 449 LYS B CB  1 
ATOM   6072 C  CG  . LYS B 1 350 ? -31.199 50.885 76.956  1.00 95.08  ? 449 LYS B CG  1 
ATOM   6073 C  CD  . LYS B 1 350 ? -32.467 51.725 76.753  1.00 99.86  ? 449 LYS B CD  1 
ATOM   6074 C  CE  . LYS B 1 350 ? -33.539 51.121 75.856  1.00 103.85 ? 449 LYS B CE  1 
ATOM   6075 N  NZ  . LYS B 1 350 ? -34.335 50.068 76.546  1.00 106.25 ? 449 LYS B NZ  1 
ATOM   6076 N  N   . ARG B 1 351 ? -27.844 49.696 78.039  1.00 88.97  ? 450 ARG B N   1 
ATOM   6077 C  CA  . ARG B 1 351 ? -27.457 48.642 78.982  1.00 89.35  ? 450 ARG B CA  1 
ATOM   6078 C  C   . ARG B 1 351 ? -28.606 47.694 79.369  1.00 89.16  ? 450 ARG B C   1 
ATOM   6079 O  O   . ARG B 1 351 ? -29.757 48.122 79.492  1.00 89.36  ? 450 ARG B O   1 
ATOM   6080 C  CB  . ARG B 1 351 ? -26.817 49.259 80.237  1.00 91.25  ? 450 ARG B CB  1 
ATOM   6081 C  CG  . ARG B 1 351 ? -26.058 48.253 81.098  1.00 95.29  ? 450 ARG B CG  1 
ATOM   6082 C  CD  . ARG B 1 351 ? -25.661 48.794 82.460  1.00 99.27  ? 450 ARG B CD  1 
ATOM   6083 N  NE  . ARG B 1 351 ? -26.820 49.262 83.218  1.00 102.94 ? 450 ARG B NE  1 
ATOM   6084 C  CZ  . ARG B 1 351 ? -26.791 49.610 84.500  1.00 105.66 ? 450 ARG B CZ  1 
ATOM   6085 N  NH1 . ARG B 1 351 ? -25.661 49.526 85.194  1.00 105.52 ? 450 ARG B NH1 1 
ATOM   6086 N  NH2 . ARG B 1 351 ? -27.893 50.040 85.102  1.00 105.66 ? 450 ARG B NH2 1 
ATOM   6087 N  N   . GLY B 1 352 ? -28.282 46.409 79.513  1.00 88.45  ? 451 GLY B N   1 
ATOM   6088 C  CA  . GLY B 1 352 ? -29.232 45.371 79.891  1.00 88.24  ? 451 GLY B CA  1 
ATOM   6089 C  C   . GLY B 1 352 ? -30.212 44.951 78.814  1.00 87.80  ? 451 GLY B C   1 
ATOM   6090 O  O   . GLY B 1 352 ? -31.009 44.034 79.034  1.00 87.99  ? 451 GLY B O   1 
ATOM   6091 N  N   . THR B 1 353 ? -30.181 45.612 77.647  1.00 87.18  ? 452 THR B N   1 
ATOM   6092 C  CA  . THR B 1 353 ? -31.108 45.276 76.569  1.00 87.08  ? 452 THR B CA  1 
ATOM   6093 C  C   . THR B 1 353 ? -30.462 44.410 75.501  1.00 86.40  ? 452 THR B C   1 
ATOM   6094 O  O   . THR B 1 353 ? -29.243 44.434 75.322  1.00 86.33  ? 452 THR B O   1 
ATOM   6095 C  CB  . THR B 1 353 ? -31.785 46.526 75.988  1.00 88.46  ? 452 THR B CB  1 
ATOM   6096 O  OG1 . THR B 1 353 ? -30.845 47.282 75.218  1.00 89.12  ? 452 THR B OG1 1 
ATOM   6097 C  CG2 . THR B 1 353 ? -32.438 47.387 77.073  1.00 88.98  ? 452 THR B CG2 1 
ATOM   6098 N  N   . TYR B 1 354 ? -31.291 43.634 74.797  1.00 85.66  ? 453 TYR B N   1 
ATOM   6099 C  CA  . TYR B 1 354 ? -30.837 42.722 73.755  1.00 85.17  ? 453 TYR B CA  1 
ATOM   6100 C  C   . TYR B 1 354 ? -30.607 43.403 72.403  1.00 84.02  ? 453 TYR B C   1 
ATOM   6101 O  O   . TYR B 1 354 ? -31.250 44.395 72.061  1.00 84.06  ? 453 TYR B O   1 
ATOM   6102 C  CB  . TYR B 1 354 ? -31.831 41.564 73.593  1.00 85.49  ? 453 TYR B CB  1 
ATOM   6103 C  CG  . TYR B 1 354 ? -31.523 40.342 74.431  1.00 86.71  ? 453 TYR B CG  1 
ATOM   6104 C  CD1 . TYR B 1 354 ? -30.327 39.655 74.281  1.00 87.80  ? 453 TYR B CD1 1 
ATOM   6105 C  CD2 . TYR B 1 354 ? -32.463 39.826 75.312  1.00 87.88  ? 453 TYR B CD2 1 
ATOM   6106 C  CE1 . TYR B 1 354 ? -30.057 38.506 75.011  1.00 88.94  ? 453 TYR B CE1 1 
ATOM   6107 C  CE2 . TYR B 1 354 ? -32.205 38.677 76.049  1.00 89.11  ? 453 TYR B CE2 1 
ATOM   6108 C  CZ  . TYR B 1 354 ? -30.998 38.019 75.897  1.00 90.21  ? 453 TYR B CZ  1 
ATOM   6109 O  OH  . TYR B 1 354 ? -30.730 36.885 76.626  1.00 92.05  ? 453 TYR B OH  1 
ATOM   6110 N  N   . GLU B 1 355 ? -29.686 42.847 71.634  1.00 82.91  ? 454 GLU B N   1 
ATOM   6111 C  CA  . GLU B 1 355 ? -29.335 43.321 70.303  1.00 82.36  ? 454 GLU B CA  1 
ATOM   6112 C  C   . GLU B 1 355 ? -28.998 42.133 69.402  1.00 81.81  ? 454 GLU B C   1 
ATOM   6113 O  O   . GLU B 1 355 ? -28.652 41.057 69.888  1.00 81.82  ? 454 GLU B O   1 
ATOM   6114 C  CB  . GLU B 1 355 ? -28.149 44.294 70.360  1.00 83.98  ? 454 GLU B CB  1 
ATOM   6115 C  CG  . GLU B 1 355 ? -28.503 45.668 70.903  1.00 87.16  ? 454 GLU B CG  1 
ATOM   6116 C  CD  . GLU B 1 355 ? -27.838 46.828 70.195  1.00 91.52  ? 454 GLU B CD  1 
ATOM   6117 O  OE1 . GLU B 1 355 ? -28.006 47.979 70.658  1.00 92.05  ? 454 GLU B OE1 1 
ATOM   6118 O  OE2 . GLU B 1 355 ? -27.150 46.589 69.177  1.00 93.16  ? 454 GLU B OE2 1 
ATOM   6119 N  N   . LYS B 1 356 ? -29.116 42.320 68.089  1.00 81.23  ? 455 LYS B N   1 
ATOM   6120 C  CA  . LYS B 1 356 ? -28.821 41.265 67.133  1.00 81.10  ? 455 LYS B CA  1 
ATOM   6121 C  C   . LYS B 1 356 ? -27.726 41.798 66.226  1.00 80.03  ? 455 LYS B C   1 
ATOM   6122 O  O   . LYS B 1 356 ? -27.992 42.640 65.373  1.00 80.30  ? 455 LYS B O   1 
ATOM   6123 C  CB  . LYS B 1 356 ? -30.084 40.897 66.337  1.00 84.12  ? 455 LYS B CB  1 
ATOM   6124 C  CG  . LYS B 1 356 ? -30.004 39.535 65.668  1.00 90.41  ? 455 LYS B CG  1 
ATOM   6125 C  CD  . LYS B 1 356 ? -31.120 39.323 64.620  1.00 96.61  ? 455 LYS B CD  1 
ATOM   6126 C  CE  . LYS B 1 356 ? -31.026 40.219 63.399  1.00 100.51 ? 455 LYS B CE  1 
ATOM   6127 N  NZ  . LYS B 1 356 ? -32.024 39.837 62.363  1.00 102.46 ? 455 LYS B NZ  1 
ATOM   6128 N  N   . TRP B 1 357 ? -26.489 41.345 66.430  1.00 78.77  ? 456 TRP B N   1 
ATOM   6129 C  CA  . TRP B 1 357 ? -25.362 41.857 65.659  1.00 78.03  ? 456 TRP B CA  1 
ATOM   6130 C  C   . TRP B 1 357 ? -24.990 40.966 64.515  1.00 77.88  ? 456 TRP B C   1 
ATOM   6131 O  O   . TRP B 1 357 ? -24.765 39.786 64.726  1.00 78.03  ? 456 TRP B O   1 
ATOM   6132 C  CB  . TRP B 1 357 ? -24.141 42.046 66.562  1.00 77.37  ? 456 TRP B CB  1 
ATOM   6133 C  CG  . TRP B 1 357 ? -24.235 43.205 67.501  1.00 76.99  ? 456 TRP B CG  1 
ATOM   6134 C  CD1 . TRP B 1 357 ? -25.360 43.700 68.094  1.00 77.67  ? 456 TRP B CD1 1 
ATOM   6135 C  CD2 . TRP B 1 357 ? -23.141 43.974 68.006  1.00 76.84  ? 456 TRP B CD2 1 
ATOM   6136 N  NE1 . TRP B 1 357 ? -25.036 44.755 68.912  1.00 77.94  ? 456 TRP B NE1 1 
ATOM   6137 C  CE2 . TRP B 1 357 ? -23.676 44.938 68.884  1.00 77.66  ? 456 TRP B CE2 1 
ATOM   6138 C  CE3 . TRP B 1 357 ? -21.756 43.942 67.801  1.00 77.07  ? 456 TRP B CE3 1 
ATOM   6139 C  CZ2 . TRP B 1 357 ? -22.870 45.848 69.566  1.00 78.07  ? 456 TRP B CZ2 1 
ATOM   6140 C  CZ3 . TRP B 1 357 ? -20.964 44.856 68.462  1.00 77.68  ? 456 TRP B CZ3 1 
ATOM   6141 C  CH2 . TRP B 1 357 ? -21.519 45.795 69.331  1.00 77.92  ? 456 TRP B CH2 1 
ATOM   6142 N  N   . THR B 1 358 ? -24.870 41.524 63.316  1.00 77.57  ? 457 THR B N   1 
ATOM   6143 C  CA  . THR B 1 358 ? -24.437 40.751 62.161  1.00 77.91  ? 457 THR B CA  1 
ATOM   6144 C  C   . THR B 1 358 ? -23.068 41.269 61.720  1.00 78.10  ? 457 THR B C   1 
ATOM   6145 O  O   . THR B 1 358 ? -22.871 42.474 61.593  1.00 78.36  ? 457 THR B O   1 
ATOM   6146 C  CB  . THR B 1 358 ? -25.498 40.769 61.058  1.00 79.22  ? 457 THR B CB  1 
ATOM   6147 O  OG1 . THR B 1 358 ? -26.707 40.210 61.569  1.00 80.24  ? 457 THR B OG1 1 
ATOM   6148 C  CG2 . THR B 1 358 ? -25.072 39.991 59.838  1.00 79.55  ? 457 THR B CG2 1 
ATOM   6149 N  N   . ILE B 1 359 ? -22.103 40.370 61.562  1.00 77.72  ? 458 ILE B N   1 
ATOM   6150 C  CA  . ILE B 1 359 ? -20.757 40.736 61.151  1.00 78.00  ? 458 ILE B CA  1 
ATOM   6151 C  C   . ILE B 1 359 ? -20.472 40.023 59.854  1.00 78.61  ? 458 ILE B C   1 
ATOM   6152 O  O   . ILE B 1 359 ? -20.670 38.817 59.779  1.00 78.84  ? 458 ILE B O   1 
ATOM   6153 C  CB  . ILE B 1 359 ? -19.724 40.366 62.235  1.00 78.23  ? 458 ILE B CB  1 
ATOM   6154 C  CG1 . ILE B 1 359 ? -20.005 41.112 63.556  1.00 78.90  ? 458 ILE B CG1 1 
ATOM   6155 C  CG2 . ILE B 1 359 ? -18.316 40.649 61.741  1.00 78.53  ? 458 ILE B CG2 1 
ATOM   6156 C  CD1 . ILE B 1 359 ? -20.738 40.312 64.618  1.00 79.81  ? 458 ILE B CD1 1 
ATOM   6157 N  N   . SER B 1 360 ? -20.030 40.757 58.825  1.00 78.91  ? 459 SER B N   1 
ATOM   6158 C  CA  . SER B 1 360 ? -19.785 40.201 57.496  1.00 79.68  ? 459 SER B CA  1 
ATOM   6159 C  C   . SER B 1 360 ? -18.333 40.210 57.044  1.00 80.65  ? 459 SER B C   1 
ATOM   6160 O  O   . SER B 1 360 ? -17.602 41.166 57.256  1.00 80.31  ? 459 SER B O   1 
ATOM   6161 C  CB  . SER B 1 360 ? -20.656 40.911 56.464  1.00 80.49  ? 459 SER B CB  1 
ATOM   6162 O  OG  . SER B 1 360 ? -20.249 40.723 55.118  1.00 81.89  ? 459 SER B OG  1 
ATOM   6163 N  N   . GLY B 1 361 ? -17.978 39.152 56.341  1.00 81.75  ? 460 GLY B N   1 
ATOM   6164 C  CA  . GLY B 1 361 ? -16.663 38.957 55.749  1.00 83.31  ? 460 GLY B CA  1 
ATOM   6165 C  C   . GLY B 1 361 ? -16.736 38.632 54.268  1.00 84.88  ? 460 GLY B C   1 
ATOM   6166 O  O   . GLY B 1 361 ? -15.793 38.063 53.713  1.00 85.20  ? 460 GLY B O   1 
ATOM   6167 N  N   . GLU B 1 362 ? -17.867 38.979 53.615  1.00 85.74  ? 461 GLU B N   1 
ATOM   6168 C  CA  . GLU B 1 362 ? -18.071 38.779 52.183  1.00 87.03  ? 461 GLU B CA  1 
ATOM   6169 C  C   . GLU B 1 362 ? -17.121 39.705 51.434  1.00 88.20  ? 461 GLU B C   1 
ATOM   6170 O  O   . GLU B 1 362 ? -16.852 40.825 51.883  1.00 88.37  ? 461 GLU B O   1 
ATOM   6171 C  CB  . GLU B 1 362 ? -19.515 39.104 51.794  1.00 89.28  ? 461 GLU B CB  1 
ATOM   6172 C  CG  . GLU B 1 362 ? -20.554 38.446 52.673  1.00 94.02  ? 461 GLU B CG  1 
ATOM   6173 C  CD  . GLU B 1 362 ? -21.873 39.189 52.670  1.00 101.13 ? 461 GLU B CD  1 
ATOM   6174 O  OE1 . GLU B 1 362 ? -22.517 39.263 51.600  1.00 102.84 ? 461 GLU B OE1 1 
ATOM   6175 O  OE2 . GLU B 1 362 ? -22.256 39.719 53.738  1.00 103.34 ? 461 GLU B OE2 1 
ATOM   6176 N  N   . GLY B 1 363 ? -16.611 39.236 50.305  1.00 88.81  ? 462 GLY B N   1 
ATOM   6177 C  CA  . GLY B 1 363 ? -15.646 40.014 49.533  1.00 89.81  ? 462 GLY B CA  1 
ATOM   6178 C  C   . GLY B 1 363 ? -14.336 40.085 50.290  1.00 90.28  ? 462 GLY B C   1 
ATOM   6179 O  O   . GLY B 1 363 ? -13.757 41.165 50.486  1.00 90.31  ? 462 GLY B O   1 
ATOM   6180 N  N   . ASP B 1 364 ? -13.908 38.904 50.756  1.00 90.32  ? 463 ASP B N   1 
ATOM   6181 C  CA  . ASP B 1 364 ? -12.732 38.685 51.567  1.00 90.88  ? 463 ASP B CA  1 
ATOM   6182 C  C   . ASP B 1 364 ? -12.789 37.218 51.967  1.00 90.65  ? 463 ASP B C   1 
ATOM   6183 O  O   . ASP B 1 364 ? -13.767 36.810 52.606  1.00 90.84  ? 463 ASP B O   1 
ATOM   6184 C  CB  . ASP B 1 364 ? -12.847 39.550 52.831  1.00 93.18  ? 463 ASP B CB  1 
ATOM   6185 C  CG  . ASP B 1 364 ? -11.672 39.453 53.763  1.00 98.92  ? 463 ASP B CG  1 
ATOM   6186 O  OD1 . ASP B 1 364 ? -10.580 39.063 53.302  1.00 100.28 ? 463 ASP B OD1 1 
ATOM   6187 O  OD2 . ASP B 1 364 ? -11.837 39.779 54.948  1.00 101.37 ? 463 ASP B OD2 1 
ATOM   6188 N  N   . MET B 1 365 ? -11.777 36.417 51.583  1.00 89.97  ? 464 MET B N   1 
ATOM   6189 C  CA  . MET B 1 365 ? -11.781 35.006 51.979  1.00 89.80  ? 464 MET B CA  1 
ATOM   6190 C  C   . MET B 1 365 ? -10.914 34.702 53.209  1.00 88.30  ? 464 MET B C   1 
ATOM   6191 O  O   . MET B 1 365 ? -10.610 33.541 53.477  1.00 88.32  ? 464 MET B O   1 
ATOM   6192 C  CB  . MET B 1 365 ? -11.441 34.064 50.821  1.00 91.33  ? 464 MET B CB  1 
ATOM   6193 C  CG  . MET B 1 365 ? -12.681 33.441 50.167  1.00 95.01  ? 464 MET B CG  1 
ATOM   6194 S  SD  . MET B 1 365 ? -13.956 32.775 51.302  1.00 102.51 ? 464 MET B SD  1 
ATOM   6195 C  CE  . MET B 1 365 ? -13.045 31.412 52.082  1.00 101.37 ? 464 MET B CE  1 
ATOM   6196 N  N   . MET B 1 366 ? -10.576 35.731 53.985  1.00 86.68  ? 465 MET B N   1 
ATOM   6197 C  CA  . MET B 1 366 ? -9.772  35.563 55.178  1.00 85.53  ? 465 MET B CA  1 
ATOM   6198 C  C   . MET B 1 366 ? -10.617 35.138 56.388  1.00 84.31  ? 465 MET B C   1 
ATOM   6199 O  O   . MET B 1 366 ? -11.851 35.246 56.364  1.00 84.64  ? 465 MET B O   1 
ATOM   6200 C  CB  . MET B 1 366 ? -8.984  36.849 55.455  1.00 85.77  ? 465 MET B CB  1 
ATOM   6201 C  CG  . MET B 1 366 ? -8.079  37.237 54.308  1.00 87.18  ? 465 MET B CG  1 
ATOM   6202 S  SD  . MET B 1 366 ? -6.802  36.025 53.945  1.00 90.01  ? 465 MET B SD  1 
ATOM   6203 C  CE  . MET B 1 366 ? -5.921  36.046 55.461  1.00 90.56  ? 465 MET B CE  1 
ATOM   6204 N  N   . LEU B 1 367 ? -9.949  34.626 57.440  1.00 82.51  ? 466 LEU B N   1 
ATOM   6205 C  CA  . LEU B 1 367 ? -10.619 34.175 58.658  1.00 80.88  ? 466 LEU B CA  1 
ATOM   6206 C  C   . LEU B 1 367 ? -10.692 35.304 59.680  1.00 78.70  ? 466 LEU B C   1 
ATOM   6207 O  O   . LEU B 1 367 ? -9.671  35.916 60.000  1.00 78.95  ? 466 LEU B O   1 
ATOM   6208 C  CB  . LEU B 1 367 ? -9.877  32.966 59.251  1.00 81.03  ? 466 LEU B CB  1 
ATOM   6209 C  CG  . LEU B 1 367 ? -10.396 32.448 60.589  1.00 82.15  ? 466 LEU B CG  1 
ATOM   6210 C  CD1 . LEU B 1 367 ? -11.794 31.901 60.456  1.00 82.44  ? 466 LEU B CD1 1 
ATOM   6211 C  CD2 . LEU B 1 367 ? -9.474  31.404 61.150  1.00 82.76  ? 466 LEU B CD2 1 
ATOM   6212 N  N   . HIS B 1 368 ? -11.892 35.573 60.198  1.00 76.52  ? 467 HIS B N   1 
ATOM   6213 C  CA  . HIS B 1 368 ? -12.064 36.625 61.182  1.00 75.32  ? 467 HIS B CA  1 
ATOM   6214 C  C   . HIS B 1 368 ? -12.800 36.165 62.411  1.00 73.80  ? 467 HIS B C   1 
ATOM   6215 O  O   . HIS B 1 368 ? -14.031 36.179 62.424  1.00 73.92  ? 467 HIS B O   1 
ATOM   6216 C  CB  . HIS B 1 368 ? -12.798 37.821 60.588  1.00 76.47  ? 467 HIS B CB  1 
ATOM   6217 C  CG  . HIS B 1 368 ? -12.172 38.342 59.344  1.00 79.13  ? 467 HIS B CG  1 
ATOM   6218 N  ND1 . HIS B 1 368 ? -11.073 39.176 59.390  1.00 80.94  ? 467 HIS B ND1 1 
ATOM   6219 C  CD2 . HIS B 1 368 ? -12.501 38.112 58.053  1.00 80.26  ? 467 HIS B CD2 1 
ATOM   6220 C  CE1 . HIS B 1 368 ? -10.764 39.423 58.132  1.00 81.55  ? 467 HIS B CE1 1 
ATOM   6221 N  NE2 . HIS B 1 368 ? -11.596 38.803 57.292  1.00 81.48  ? 467 HIS B NE2 1 
ATOM   6222 N  N   . PRO B 1 369 ? -12.076 35.816 63.489  1.00 72.09  ? 468 PRO B N   1 
ATOM   6223 C  CA  . PRO B 1 369 ? -12.767 35.438 64.724  1.00 70.88  ? 468 PRO B CA  1 
ATOM   6224 C  C   . PRO B 1 369 ? -13.264 36.724 65.390  1.00 69.68  ? 468 PRO B C   1 
ATOM   6225 O  O   . PRO B 1 369 ? -12.491 37.414 66.051  1.00 69.70  ? 468 PRO B O   1 
ATOM   6226 C  CB  . PRO B 1 369 ? -11.677 34.725 65.533  1.00 71.47  ? 468 PRO B CB  1 
ATOM   6227 C  CG  . PRO B 1 369 ? -10.475 34.650 64.642  1.00 72.06  ? 468 PRO B CG  1 
ATOM   6228 C  CD  . PRO B 1 369 ? -10.613 35.743 63.650  1.00 71.03  ? 468 PRO B CD  1 
ATOM   6229 N  N   . PHE B 1 370 ? -14.521 37.101 65.121  1.00 68.45  ? 469 PHE B N   1 
ATOM   6230 C  CA  . PHE B 1 370 ? -15.065 38.333 65.666  1.00 67.72  ? 469 PHE B CA  1 
ATOM   6231 C  C   . PHE B 1 370 ? -15.261 38.287 67.174  1.00 67.61  ? 469 PHE B C   1 
ATOM   6232 O  O   . PHE B 1 370 ? -16.117 37.557 67.673  1.00 67.79  ? 469 PHE B O   1 
ATOM   6233 C  CB  . PHE B 1 370 ? -16.344 38.768 64.955  1.00 66.73  ? 469 PHE B CB  1 
ATOM   6234 C  CG  . PHE B 1 370 ? -16.486 40.261 65.095  1.00 66.17  ? 469 PHE B CG  1 
ATOM   6235 C  CD1 . PHE B 1 370 ? -15.626 41.115 64.433  1.00 66.39  ? 469 PHE B CD1 1 
ATOM   6236 C  CD2 . PHE B 1 370 ? -17.394 40.804 65.981  1.00 66.58  ? 469 PHE B CD2 1 
ATOM   6237 C  CE1 . PHE B 1 370 ? -15.728 42.486 64.595  1.00 66.97  ? 469 PHE B CE1 1 
ATOM   6238 C  CE2 . PHE B 1 370 ? -17.497 42.178 66.139  1.00 67.10  ? 469 PHE B CE2 1 
ATOM   6239 C  CZ  . PHE B 1 370 ? -16.661 43.009 65.449  1.00 66.81  ? 469 PHE B CZ  1 
ATOM   6240 N  N   . HIS B 1 371 ? -14.471 39.088 67.892  1.00 66.98  ? 470 HIS B N   1 
ATOM   6241 C  CA  . HIS B 1 371 ? -14.507 39.178 69.344  1.00 67.01  ? 470 HIS B CA  1 
ATOM   6242 C  C   . HIS B 1 371 ? -15.193 40.466 69.812  1.00 66.71  ? 470 HIS B C   1 
ATOM   6243 O  O   . HIS B 1 371 ? -14.895 41.539 69.297  1.00 66.74  ? 470 HIS B O   1 
ATOM   6244 C  CB  . HIS B 1 371 ? -13.078 39.071 69.912  1.00 67.51  ? 470 HIS B CB  1 
ATOM   6245 C  CG  . HIS B 1 371 ? -12.990 39.265 71.391  1.00 69.27  ? 470 HIS B CG  1 
ATOM   6246 N  ND1 . HIS B 1 371 ? -13.763 38.517 72.268  1.00 70.95  ? 470 HIS B ND1 1 
ATOM   6247 C  CD2 . HIS B 1 371 ? -12.203 40.104 72.103  1.00 70.14  ? 470 HIS B CD2 1 
ATOM   6248 C  CE1 . HIS B 1 371 ? -13.431 38.936 73.476  1.00 71.48  ? 470 HIS B CE1 1 
ATOM   6249 N  NE2 . HIS B 1 371 ? -12.488 39.883 73.425  1.00 71.25  ? 470 HIS B NE2 1 
ATOM   6250 N  N   . ILE B 1 372 ? -16.118 40.354 70.782  1.00 66.25  ? 471 ILE B N   1 
ATOM   6251 C  CA  . ILE B 1 372 ? -16.830 41.503 71.338  1.00 66.11  ? 471 ILE B CA  1 
ATOM   6252 C  C   . ILE B 1 372 ? -16.497 41.667 72.827  1.00 66.27  ? 471 ILE B C   1 
ATOM   6253 O  O   . ILE B 1 372 ? -16.631 40.717 73.603  1.00 67.28  ? 471 ILE B O   1 
ATOM   6254 C  CB  . ILE B 1 372 ? -18.354 41.381 71.096  1.00 66.30  ? 471 ILE B CB  1 
ATOM   6255 C  CG1 . ILE B 1 372 ? -18.668 41.260 69.589  1.00 66.86  ? 471 ILE B CG1 1 
ATOM   6256 C  CG2 . ILE B 1 372 ? -19.094 42.560 71.727  1.00 66.56  ? 471 ILE B CG2 1 
ATOM   6257 C  CD1 . ILE B 1 372 ? -20.045 40.870 69.295  1.00 67.57  ? 471 ILE B CD1 1 
ATOM   6258 N  N   . HIS B 1 373 ? -16.056 42.860 73.230  1.00 65.11  ? 472 HIS B N   1 
ATOM   6259 C  CA  . HIS B 1 373 ? -15.685 43.117 74.619  1.00 64.45  ? 472 HIS B CA  1 
ATOM   6260 C  C   . HIS B 1 373 ? -16.884 43.237 75.567  1.00 65.11  ? 472 HIS B C   1 
ATOM   6261 O  O   . HIS B 1 373 ? -17.996 43.506 75.136  1.00 65.22  ? 472 HIS B O   1 
ATOM   6262 C  CB  . HIS B 1 373 ? -14.823 44.381 74.708  1.00 63.48  ? 472 HIS B CB  1 
ATOM   6263 C  CG  . HIS B 1 373 ? -13.449 44.245 74.135  1.00 62.97  ? 472 HIS B CG  1 
ATOM   6264 N  ND1 . HIS B 1 373 ? -12.379 44.905 74.691  1.00 64.16  ? 472 HIS B ND1 1 
ATOM   6265 C  CD2 . HIS B 1 373 ? -13.017 43.545 73.062  1.00 63.72  ? 472 HIS B CD2 1 
ATOM   6266 C  CE1 . HIS B 1 373 ? -11.331 44.587 73.949  1.00 64.52  ? 472 HIS B CE1 1 
ATOM   6267 N  NE2 . HIS B 1 373 ? -11.668 43.781 72.949  1.00 64.48  ? 472 HIS B NE2 1 
ATOM   6268 N  N   . GLY B 1 374 ? -16.634 43.025 76.852  1.00 65.59  ? 473 GLY B N   1 
ATOM   6269 C  CA  . GLY B 1 374 ? -17.624 43.158 77.913  1.00 66.31  ? 473 GLY B CA  1 
ATOM   6270 C  C   . GLY B 1 374 ? -18.854 42.276 77.851  1.00 66.75  ? 473 GLY B C   1 
ATOM   6271 O  O   . GLY B 1 374 ? -19.848 42.573 78.522  1.00 67.20  ? 473 GLY B O   1 
ATOM   6272 N  N   . THR B 1 375 ? -18.816 41.188 77.062  1.00 66.50  ? 474 THR B N   1 
ATOM   6273 C  CA  . THR B 1 375 ? -19.976 40.312 76.964  1.00 66.95  ? 474 THR B CA  1 
ATOM   6274 C  C   . THR B 1 375 ? -19.610 38.837 76.691  1.00 67.31  ? 474 THR B C   1 
ATOM   6275 O  O   . THR B 1 375 ? -18.465 38.495 76.379  1.00 67.29  ? 474 THR B O   1 
ATOM   6276 C  CB  . THR B 1 375 ? -20.974 40.879 75.919  1.00 68.32  ? 474 THR B CB  1 
ATOM   6277 O  OG1 . THR B 1 375 ? -22.264 40.312 76.164  1.00 69.57  ? 474 THR B OG1 1 
ATOM   6278 C  CG2 . THR B 1 375 ? -20.542 40.595 74.497  1.00 68.49  ? 474 THR B CG2 1 
ATOM   6279 N  N   . GLN B 1 376 ? -20.617 37.974 76.862  1.00 67.28  ? 475 GLN B N   1 
ATOM   6280 C  CA  . GLN B 1 376 ? -20.652 36.558 76.575  1.00 67.47  ? 475 GLN B CA  1 
ATOM   6281 C  C   . GLN B 1 376 ? -22.010 36.409 75.906  1.00 67.92  ? 475 GLN B C   1 
ATOM   6282 O  O   . GLN B 1 376 ? -23.033 36.680 76.535  1.00 68.33  ? 475 GLN B O   1 
ATOM   6283 C  CB  . GLN B 1 376 ? -20.592 35.758 77.873  1.00 68.68  ? 475 GLN B CB  1 
ATOM   6284 C  CG  . GLN B 1 376 ? -19.702 34.539 77.777  1.00 71.40  ? 475 GLN B CG  1 
ATOM   6285 C  CD  . GLN B 1 376 ? -18.286 34.856 77.367  1.00 74.32  ? 475 GLN B CD  1 
ATOM   6286 O  OE1 . GLN B 1 376 ? -17.588 35.642 77.994  1.00 75.65  ? 475 GLN B OE1 1 
ATOM   6287 N  NE2 . GLN B 1 376 ? -17.829 34.235 76.312  1.00 74.45  ? 475 GLN B NE2 1 
ATOM   6288 N  N   . PHE B 1 377 ? -22.021 36.106 74.605  1.00 67.50  ? 476 PHE B N   1 
ATOM   6289 C  CA  . PHE B 1 377 ? -23.250 36.035 73.822  1.00 67.27  ? 476 PHE B CA  1 
ATOM   6290 C  C   . PHE B 1 377 ? -23.640 34.606 73.358  1.00 67.35  ? 476 PHE B C   1 
ATOM   6291 O  O   . PHE B 1 377 ? -23.026 33.634 73.779  1.00 67.50  ? 476 PHE B O   1 
ATOM   6292 C  CB  . PHE B 1 377 ? -23.122 37.006 72.629  1.00 66.87  ? 476 PHE B CB  1 
ATOM   6293 C  CG  . PHE B 1 377 ? -21.902 36.815 71.762  1.00 66.93  ? 476 PHE B CG  1 
ATOM   6294 C  CD1 . PHE B 1 377 ? -21.778 35.705 70.944  1.00 67.46  ? 476 PHE B CD1 1 
ATOM   6295 C  CD2 . PHE B 1 377 ? -20.885 37.748 71.756  1.00 67.50  ? 476 PHE B CD2 1 
ATOM   6296 C  CE1 . PHE B 1 377 ? -20.643 35.517 70.164  1.00 67.85  ? 476 PHE B CE1 1 
ATOM   6297 C  CE2 . PHE B 1 377 ? -19.763 37.569 70.952  1.00 68.00  ? 476 PHE B CE2 1 
ATOM   6298 C  CZ  . PHE B 1 377 ? -19.655 36.459 70.157  1.00 67.53  ? 476 PHE B CZ  1 
ATOM   6299 N  N   . ARG B 1 378 ? -24.684 34.485 72.521  1.00 67.31  ? 477 ARG B N   1 
ATOM   6300 C  CA  . ARG B 1 378 ? -25.095 33.216 71.944  1.00 67.93  ? 477 ARG B CA  1 
ATOM   6301 C  C   . ARG B 1 378 ? -25.064 33.393 70.425  1.00 68.89  ? 477 ARG B C   1 
ATOM   6302 O  O   . ARG B 1 378 ? -25.656 34.344 69.914  1.00 69.01  ? 477 ARG B O   1 
ATOM   6303 C  CB  . ARG B 1 378 ? -26.508 32.842 72.389  1.00 68.75  ? 477 ARG B CB  1 
ATOM   6304 C  CG  . ARG B 1 378 ? -26.701 32.858 73.889  1.00 70.85  ? 477 ARG B CG  1 
ATOM   6305 C  CD  . ARG B 1 378 ? -25.951 31.738 74.562  1.00 73.08  ? 477 ARG B CD  1 
ATOM   6306 N  NE  . ARG B 1 378 ? -26.420 30.420 74.135  1.00 75.54  ? 477 ARG B NE  1 
ATOM   6307 C  CZ  . ARG B 1 378 ? -27.472 29.796 74.652  1.00 78.37  ? 477 ARG B CZ  1 
ATOM   6308 N  NH1 . ARG B 1 378 ? -28.193 30.373 75.606  1.00 78.85  ? 477 ARG B NH1 1 
ATOM   6309 N  NH2 . ARG B 1 378 ? -27.814 28.591 74.219  1.00 78.46  ? 477 ARG B NH2 1 
ATOM   6310 N  N   . ILE B 1 379 ? -24.335 32.526 69.706  1.00 69.28  ? 478 ILE B N   1 
ATOM   6311 C  CA  . ILE B 1 379 ? -24.263 32.626 68.248  1.00 69.98  ? 478 ILE B CA  1 
ATOM   6312 C  C   . ILE B 1 379 ? -25.587 32.150 67.637  1.00 70.53  ? 478 ILE B C   1 
ATOM   6313 O  O   . ILE B 1 379 ? -26.051 31.054 67.956  1.00 70.71  ? 478 ILE B O   1 
ATOM   6314 C  CB  . ILE B 1 379 ? -23.063 31.822 67.686  1.00 70.40  ? 478 ILE B CB  1 
ATOM   6315 C  CG1 . ILE B 1 379 ? -21.726 32.315 68.274  1.00 71.22  ? 478 ILE B CG1 1 
ATOM   6316 C  CG2 . ILE B 1 379 ? -23.055 31.837 66.160  1.00 70.67  ? 478 ILE B CG2 1 
ATOM   6317 C  CD1 . ILE B 1 379 ? -20.508 31.464 67.875  1.00 72.13  ? 478 ILE B CD1 1 
ATOM   6318 N  N   . LEU B 1 380 ? -26.226 32.993 66.812  1.00 70.54  ? 479 LEU B N   1 
ATOM   6319 C  CA  . LEU B 1 380 ? -27.480 32.625 66.152  1.00 70.73  ? 479 LEU B CA  1 
ATOM   6320 C  C   . LEU B 1 380 ? -27.137 31.926 64.848  1.00 71.60  ? 479 LEU B C   1 
ATOM   6321 O  O   . LEU B 1 380 ? -27.651 30.844 64.571  1.00 71.99  ? 479 LEU B O   1 
ATOM   6322 C  CB  . LEU B 1 380 ? -28.375 33.857 65.904  1.00 70.30  ? 479 LEU B CB  1 
ATOM   6323 C  CG  . LEU B 1 380 ? -28.716 34.697 67.134  1.00 70.92  ? 479 LEU B CG  1 
ATOM   6324 C  CD1 . LEU B 1 380 ? -29.535 35.915 66.754  1.00 71.24  ? 479 LEU B CD1 1 
ATOM   6325 C  CD2 . LEU B 1 380 ? -29.449 33.880 68.162  1.00 71.27  ? 479 LEU B CD2 1 
ATOM   6326 N  N   . SER B 1 381 ? -26.225 32.515 64.069  1.00 71.78  ? 480 SER B N   1 
ATOM   6327 C  CA  . SER B 1 381 ? -25.775 31.939 62.817  1.00 72.33  ? 480 SER B CA  1 
ATOM   6328 C  C   . SER B 1 381 ? -24.264 32.130 62.710  1.00 72.81  ? 480 SER B C   1 
ATOM   6329 O  O   . SER B 1 381 ? -23.763 33.236 62.896  1.00 72.67  ? 480 SER B O   1 
ATOM   6330 C  CB  . SER B 1 381 ? -26.482 32.613 61.645  1.00 73.59  ? 480 SER B CB  1 
ATOM   6331 O  OG  . SER B 1 381 ? -25.909 32.245 60.401  1.00 75.85  ? 480 SER B OG  1 
ATOM   6332 N  N   . GLU B 1 382 ? -23.538 31.050 62.446  1.00 73.21  ? 481 GLU B N   1 
ATOM   6333 C  CA  . GLU B 1 382 ? -22.099 31.122 62.279  1.00 74.18  ? 481 GLU B CA  1 
ATOM   6334 C  C   . GLU B 1 382 ? -21.758 30.846 60.819  1.00 75.04  ? 481 GLU B C   1 
ATOM   6335 O  O   . GLU B 1 382 ? -21.868 29.695 60.382  1.00 75.25  ? 481 GLU B O   1 
ATOM   6336 C  CB  . GLU B 1 382 ? -21.392 30.125 63.197  1.00 76.07  ? 481 GLU B CB  1 
ATOM   6337 C  CG  . GLU B 1 382 ? -19.889 30.319 63.238  1.00 80.61  ? 481 GLU B CG  1 
ATOM   6338 C  CD  . GLU B 1 382 ? -19.270 29.781 64.509  1.00 87.78  ? 481 GLU B CD  1 
ATOM   6339 O  OE1 . GLU B 1 382 ? -19.731 28.721 64.994  1.00 90.01  ? 481 GLU B OE1 1 
ATOM   6340 O  OE2 . GLU B 1 382 ? -18.337 30.430 65.032  1.00 89.74  ? 481 GLU B OE2 1 
ATOM   6341 N  N   . ASN B 1 383 ? -21.384 31.906 60.062  1.00 75.09  ? 482 ASN B N   1 
ATOM   6342 C  CA  . ASN B 1 383 ? -21.010 31.827 58.650  1.00 75.70  ? 482 ASN B CA  1 
ATOM   6343 C  C   . ASN B 1 383 ? -22.126 31.208 57.797  1.00 76.14  ? 482 ASN B C   1 
ATOM   6344 O  O   . ASN B 1 383 ? -21.859 30.414 56.900  1.00 76.30  ? 482 ASN B O   1 
ATOM   6345 C  CB  . ASN B 1 383 ? -19.706 31.052 58.487  1.00 76.84  ? 482 ASN B CB  1 
ATOM   6346 C  CG  . ASN B 1 383 ? -18.683 31.743 57.635  1.00 80.15  ? 482 ASN B CG  1 
ATOM   6347 O  OD1 . ASN B 1 383 ? -18.803 32.922 57.300  1.00 80.83  ? 482 ASN B OD1 1 
ATOM   6348 N  ND2 . ASN B 1 383 ? -17.638 31.014 57.274  1.00 81.53  ? 482 ASN B ND2 1 
ATOM   6349 N  N   . GLY B 1 384 ? -23.366 31.569 58.096  1.00 76.06  ? 483 GLY B N   1 
ATOM   6350 C  CA  . GLY B 1 384 ? -24.513 31.041 57.373  1.00 76.37  ? 483 GLY B CA  1 
ATOM   6351 C  C   . GLY B 1 384 ? -25.169 29.876 58.082  1.00 76.46  ? 483 GLY B C   1 
ATOM   6352 O  O   . GLY B 1 384 ? -26.347 29.958 58.442  1.00 76.65  ? 483 GLY B O   1 
ATOM   6353 N  N   . LYS B 1 385 ? -24.413 28.788 58.306  1.00 75.99  ? 484 LYS B N   1 
ATOM   6354 C  CA  . LYS B 1 385 ? -24.941 27.607 58.993  1.00 75.99  ? 484 LYS B CA  1 
ATOM   6355 C  C   . LYS B 1 385 ? -25.189 27.892 60.498  1.00 75.78  ? 484 LYS B C   1 
ATOM   6356 O  O   . LYS B 1 385 ? -24.501 28.734 61.079  1.00 76.12  ? 484 LYS B O   1 
ATOM   6357 C  CB  . LYS B 1 385 ? -23.960 26.425 58.861  1.00 77.79  ? 484 LYS B CB  1 
ATOM   6358 C  CG  . LYS B 1 385 ? -23.345 26.185 57.485  1.00 81.87  ? 484 LYS B CG  1 
ATOM   6359 C  CD  . LYS B 1 385 ? -22.348 24.991 57.569  1.00 86.29  ? 484 LYS B CD  1 
ATOM   6360 C  CE  . LYS B 1 385 ? -21.240 25.043 56.531  1.00 90.04  ? 484 LYS B CE  1 
ATOM   6361 N  NZ  . LYS B 1 385 ? -19.989 24.349 56.968  1.00 91.45  ? 484 LYS B NZ  1 
ATOM   6362 N  N   . PRO B 1 386 ? -26.124 27.180 61.168  1.00 74.97  ? 485 PRO B N   1 
ATOM   6363 C  CA  . PRO B 1 386 ? -26.286 27.370 62.625  1.00 74.46  ? 485 PRO B CA  1 
ATOM   6364 C  C   . PRO B 1 386 ? -25.016 26.928 63.389  1.00 74.02  ? 485 PRO B C   1 
ATOM   6365 O  O   . PRO B 1 386 ? -24.200 26.171 62.841  1.00 74.38  ? 485 PRO B O   1 
ATOM   6366 C  CB  . PRO B 1 386 ? -27.488 26.473 62.964  1.00 74.91  ? 485 PRO B CB  1 
ATOM   6367 C  CG  . PRO B 1 386 ? -28.124 26.151 61.670  1.00 75.43  ? 485 PRO B CG  1 
ATOM   6368 C  CD  . PRO B 1 386 ? -27.016 26.119 60.675  1.00 74.15  ? 485 PRO B CD  1 
ATOM   6369 N  N   . PRO B 1 387 ? -24.791 27.395 64.632  1.00 73.10  ? 486 PRO B N   1 
ATOM   6370 C  CA  . PRO B 1 387 ? -23.561 27.008 65.343  1.00 72.69  ? 486 PRO B CA  1 
ATOM   6371 C  C   . PRO B 1 387 ? -23.557 25.540 65.755  1.00 72.16  ? 486 PRO B C   1 
ATOM   6372 O  O   . PRO B 1 387 ? -24.615 24.980 66.054  1.00 72.07  ? 486 PRO B O   1 
ATOM   6373 C  CB  . PRO B 1 387 ? -23.559 27.924 66.565  1.00 73.45  ? 486 PRO B CB  1 
ATOM   6374 C  CG  . PRO B 1 387 ? -24.993 28.179 66.818  1.00 74.02  ? 486 PRO B CG  1 
ATOM   6375 C  CD  . PRO B 1 387 ? -25.622 28.293 65.453  1.00 72.52  ? 486 PRO B CD  1 
ATOM   6376 N  N   . ALA B 1 388 ? -22.362 24.918 65.775  1.00 71.29  ? 487 ALA B N   1 
ATOM   6377 C  CA  . ALA B 1 388 ? -22.205 23.526 66.193  1.00 70.71  ? 487 ALA B CA  1 
ATOM   6378 C  C   . ALA B 1 388 ? -22.698 23.329 67.647  1.00 70.22  ? 487 ALA B C   1 
ATOM   6379 O  O   . ALA B 1 388 ? -22.900 24.318 68.365  1.00 70.52  ? 487 ALA B O   1 
ATOM   6380 C  CB  . ALA B 1 388 ? -20.743 23.120 66.067  1.00 70.72  ? 487 ALA B CB  1 
ATOM   6381 N  N   . ALA B 1 389 ? -22.896 22.071 68.098  1.00 69.24  ? 488 ALA B N   1 
ATOM   6382 C  CA  . ALA B 1 389 ? -23.356 21.819 69.462  1.00 68.87  ? 488 ALA B CA  1 
ATOM   6383 C  C   . ALA B 1 389 ? -22.439 22.457 70.516  1.00 68.43  ? 488 ALA B C   1 
ATOM   6384 O  O   . ALA B 1 389 ? -22.926 23.152 71.404  1.00 68.67  ? 488 ALA B O   1 
ATOM   6385 C  CB  . ALA B 1 389 ? -23.498 20.328 69.707  1.00 69.07  ? 488 ALA B CB  1 
ATOM   6386 N  N   . HIS B 1 390 ? -21.119 22.304 70.365  1.00 67.63  ? 489 HIS B N   1 
ATOM   6387 C  CA  . HIS B 1 390 ? -20.170 22.892 71.304  1.00 67.45  ? 489 HIS B CA  1 
ATOM   6388 C  C   . HIS B 1 390 ? -19.998 24.416 71.124  1.00 67.32  ? 489 HIS B C   1 
ATOM   6389 O  O   . HIS B 1 390 ? -19.534 25.091 72.045  1.00 67.67  ? 489 HIS B O   1 
ATOM   6390 C  CB  . HIS B 1 390 ? -18.820 22.168 71.227  1.00 67.81  ? 489 HIS B CB  1 
ATOM   6391 C  CG  . HIS B 1 390 ? -18.177 22.280 69.884  1.00 69.26  ? 489 HIS B CG  1 
ATOM   6392 N  ND1 . HIS B 1 390 ? -18.782 21.769 68.752  1.00 70.93  ? 489 HIS B ND1 1 
ATOM   6393 C  CD2 . HIS B 1 390 ? -17.004 22.854 69.533  1.00 70.09  ? 489 HIS B CD2 1 
ATOM   6394 C  CE1 . HIS B 1 390 ? -17.964 22.053 67.751  1.00 71.23  ? 489 HIS B CE1 1 
ATOM   6395 N  NE2 . HIS B 1 390 ? -16.879 22.703 68.174  1.00 71.05  ? 489 HIS B NE2 1 
ATOM   6396 N  N   . ARG B 1 391 ? -20.392 24.964 69.970  1.00 66.65  ? 490 ARG B N   1 
ATOM   6397 C  CA  . ARG B 1 391 ? -20.285 26.405 69.725  1.00 66.99  ? 490 ARG B CA  1 
ATOM   6398 C  C   . ARG B 1 391 ? -21.604 27.181 69.943  1.00 67.89  ? 490 ARG B C   1 
ATOM   6399 O  O   . ARG B 1 391 ? -21.688 28.363 69.603  1.00 68.01  ? 490 ARG B O   1 
ATOM   6400 C  CB  . ARG B 1 391 ? -19.750 26.651 68.316  1.00 67.28  ? 490 ARG B CB  1 
ATOM   6401 C  CG  . ARG B 1 391 ? -18.417 25.969 68.096  1.00 68.05  ? 490 ARG B CG  1 
ATOM   6402 C  CD  . ARG B 1 391 ? -17.830 26.288 66.746  1.00 68.49  ? 490 ARG B CD  1 
ATOM   6403 N  NE  . ARG B 1 391 ? -17.523 27.710 66.584  1.00 68.92  ? 490 ARG B NE  1 
ATOM   6404 C  CZ  . ARG B 1 391 ? -16.413 28.296 67.018  1.00 69.63  ? 490 ARG B CZ  1 
ATOM   6405 N  NH1 . ARG B 1 391 ? -15.507 27.602 67.694  1.00 69.81  ? 490 ARG B NH1 1 
ATOM   6406 N  NH2 . ARG B 1 391 ? -16.216 29.589 66.809  1.00 68.55  ? 490 ARG B NH2 1 
ATOM   6407 N  N   . SER B 1 392 ? -22.624 26.527 70.527  1.00 68.02  ? 491 SER B N   1 
ATOM   6408 C  CA  . SER B 1 392 ? -23.932 27.137 70.742  1.00 68.25  ? 491 SER B CA  1 
ATOM   6409 C  C   . SER B 1 392 ? -24.190 27.661 72.167  1.00 68.17  ? 491 SER B C   1 
ATOM   6410 O  O   . SER B 1 392 ? -25.297 28.105 72.467  1.00 68.12  ? 491 SER B O   1 
ATOM   6411 C  CB  . SER B 1 392 ? -25.016 26.142 70.369  1.00 69.73  ? 491 SER B CB  1 
ATOM   6412 O  OG  . SER B 1 392 ? -24.902 25.013 71.220  1.00 72.20  ? 491 SER B OG  1 
ATOM   6413 N  N   . GLY B 1 393 ? -23.189 27.600 73.034  1.00 67.82  ? 492 GLY B N   1 
ATOM   6414 C  CA  . GLY B 1 393 ? -23.324 28.069 74.406  1.00 67.52  ? 492 GLY B CA  1 
ATOM   6415 C  C   . GLY B 1 393 ? -22.841 29.490 74.542  1.00 66.91  ? 492 GLY B C   1 
ATOM   6416 O  O   . GLY B 1 393 ? -23.112 30.316 73.675  1.00 66.70  ? 492 GLY B O   1 
ATOM   6417 N  N   . TRP B 1 394 ? -22.098 29.777 75.612  1.00 66.87  ? 493 TRP B N   1 
ATOM   6418 C  CA  . TRP B 1 394 ? -21.565 31.116 75.825  1.00 67.36  ? 493 TRP B CA  1 
ATOM   6419 C  C   . TRP B 1 394 ? -20.249 31.346 75.097  1.00 67.37  ? 493 TRP B C   1 
ATOM   6420 O  O   . TRP B 1 394 ? -19.230 30.732 75.415  1.00 67.74  ? 493 TRP B O   1 
ATOM   6421 C  CB  . TRP B 1 394 ? -21.457 31.438 77.310  1.00 67.52  ? 493 TRP B CB  1 
ATOM   6422 C  CG  . TRP B 1 394 ? -22.783 31.417 77.998  1.00 68.53  ? 493 TRP B CG  1 
ATOM   6423 C  CD1 . TRP B 1 394 ? -23.249 30.460 78.848  1.00 69.71  ? 493 TRP B CD1 1 
ATOM   6424 C  CD2 . TRP B 1 394 ? -23.852 32.353 77.820  1.00 68.80  ? 493 TRP B CD2 1 
ATOM   6425 N  NE1 . TRP B 1 394 ? -24.542 30.746 79.219  1.00 70.09  ? 493 TRP B NE1 1 
ATOM   6426 C  CE2 . TRP B 1 394 ? -24.938 31.902 78.598  1.00 69.66  ? 493 TRP B CE2 1 
ATOM   6427 C  CE3 . TRP B 1 394 ? -24.005 33.518 77.060  1.00 69.23  ? 493 TRP B CE3 1 
ATOM   6428 C  CZ2 . TRP B 1 394 ? -26.144 32.591 78.660  1.00 70.08  ? 493 TRP B CZ2 1 
ATOM   6429 C  CZ3 . TRP B 1 394 ? -25.201 34.198 77.124  1.00 69.88  ? 493 TRP B CZ3 1 
ATOM   6430 C  CH2 . TRP B 1 394 ? -26.249 33.741 77.923  1.00 70.06  ? 493 TRP B CH2 1 
ATOM   6431 N  N   . LYS B 1 395 ? -20.283 32.228 74.102  1.00 66.65  ? 494 LYS B N   1 
ATOM   6432 C  CA  . LYS B 1 395 ? -19.119 32.541 73.293  1.00 66.71  ? 494 LYS B CA  1 
ATOM   6433 C  C   . LYS B 1 395 ? -18.840 34.038 73.263  1.00 66.56  ? 494 LYS B C   1 
ATOM   6434 O  O   . LYS B 1 395 ? -19.762 34.821 73.333  1.00 66.74  ? 494 LYS B O   1 
ATOM   6435 C  CB  . LYS B 1 395 ? -19.362 32.064 71.847  1.00 68.16  ? 494 LYS B CB  1 
ATOM   6436 C  CG  . LYS B 1 395 ? -19.568 30.561 71.700  1.00 70.54  ? 494 LYS B CG  1 
ATOM   6437 C  CD  . LYS B 1 395 ? -18.269 29.791 71.785  1.00 72.76  ? 494 LYS B CD  1 
ATOM   6438 C  CE  . LYS B 1 395 ? -17.553 29.741 70.470  1.00 75.14  ? 494 LYS B CE  1 
ATOM   6439 N  NZ  . LYS B 1 395 ? -16.721 30.944 70.247  1.00 76.97  ? 494 LYS B NZ  1 
ATOM   6440 N  N   . ASP B 1 396 ? -17.577 34.438 73.208  1.00 66.32  ? 495 ASP B N   1 
ATOM   6441 C  CA  . ASP B 1 396 ? -17.204 35.845 73.022  1.00 66.95  ? 495 ASP B CA  1 
ATOM   6442 C  C   . ASP B 1 396 ? -16.524 36.089 71.667  1.00 67.04  ? 495 ASP B C   1 
ATOM   6443 O  O   . ASP B 1 396 ? -16.087 37.200 71.382  1.00 66.77  ? 495 ASP B O   1 
ATOM   6444 C  CB  . ASP B 1 396 ? -16.350 36.414 74.172  1.00 69.68  ? 495 ASP B CB  1 
ATOM   6445 C  CG  . ASP B 1 396 ? -15.073 35.667 74.509  1.00 75.51  ? 495 ASP B CG  1 
ATOM   6446 O  OD1 . ASP B 1 396 ? -14.159 35.618 73.645  1.00 76.63  ? 495 ASP B OD1 1 
ATOM   6447 O  OD2 . ASP B 1 396 ? -14.967 35.169 75.648  1.00 77.64  ? 495 ASP B OD2 1 
ATOM   6448 N  N   . THR B 1 397 ? -16.441 35.037 70.843  1.00 67.40  ? 496 THR B N   1 
ATOM   6449 C  CA  . THR B 1 397 ? -15.842 34.974 69.532  1.00 68.00  ? 496 THR B CA  1 
ATOM   6450 C  C   . THR B 1 397 ? -16.830 34.229 68.615  1.00 68.72  ? 496 THR B C   1 
ATOM   6451 O  O   . THR B 1 397 ? -17.539 33.318 69.056  1.00 68.59  ? 496 THR B O   1 
ATOM   6452 C  CB  . THR B 1 397 ? -14.494 34.241 69.646  1.00 69.05  ? 496 THR B CB  1 
ATOM   6453 O  OG1 . THR B 1 397 ? -13.704 34.838 70.677  1.00 69.75  ? 496 THR B OG1 1 
ATOM   6454 C  CG2 . THR B 1 397 ? -13.719 34.233 68.350  1.00 69.61  ? 496 THR B CG2 1 
ATOM   6455 N  N   . VAL B 1 398 ? -16.911 34.650 67.354  1.00 69.30  ? 497 VAL B N   1 
ATOM   6456 C  CA  . VAL B 1 398 ? -17.769 34.017 66.358  1.00 70.27  ? 497 VAL B CA  1 
ATOM   6457 C  C   . VAL B 1 398 ? -16.998 33.989 65.040  1.00 71.56  ? 497 VAL B C   1 
ATOM   6458 O  O   . VAL B 1 398 ? -16.339 34.972 64.703  1.00 71.98  ? 497 VAL B O   1 
ATOM   6459 C  CB  . VAL B 1 398 ? -19.157 34.712 66.248  1.00 70.87  ? 497 VAL B CB  1 
ATOM   6460 C  CG1 . VAL B 1 398 ? -19.029 36.203 65.954  1.00 71.27  ? 497 VAL B CG1 1 
ATOM   6461 C  CG2 . VAL B 1 398 ? -20.043 34.028 65.218  1.00 71.38  ? 497 VAL B CG2 1 
ATOM   6462 N  N   . ARG B 1 399 ? -17.013 32.860 64.322  1.00 72.20  ? 498 ARG B N   1 
ATOM   6463 C  CA  . ARG B 1 399 ? -16.276 32.752 63.059  1.00 73.24  ? 498 ARG B CA  1 
ATOM   6464 C  C   . ARG B 1 399 ? -16.877 33.601 61.930  1.00 73.82  ? 498 ARG B C   1 
ATOM   6465 O  O   . ARG B 1 399 ? -18.066 33.488 61.638  1.00 74.15  ? 498 ARG B O   1 
ATOM   6466 C  CB  . ARG B 1 399 ? -16.178 31.289 62.609  1.00 74.75  ? 498 ARG B CB  1 
ATOM   6467 C  CG  . ARG B 1 399 ? -15.246 31.107 61.436  1.00 78.13  ? 498 ARG B CG  1 
ATOM   6468 C  CD  . ARG B 1 399 ? -15.493 29.816 60.708  1.00 82.97  ? 498 ARG B CD  1 
ATOM   6469 N  NE  . ARG B 1 399 ? -14.240 29.301 60.165  1.00 88.98  ? 498 ARG B NE  1 
ATOM   6470 C  CZ  . ARG B 1 399 ? -13.484 28.381 60.765  1.00 93.57  ? 498 ARG B CZ  1 
ATOM   6471 N  NH1 . ARG B 1 399 ? -13.870 27.840 61.918  1.00 93.14  ? 498 ARG B NH1 1 
ATOM   6472 N  NH2 . ARG B 1 399 ? -12.348 27.979 60.204  1.00 94.69  ? 498 ARG B NH2 1 
ATOM   6473 N  N   . VAL B 1 400 ? -16.067 34.453 61.302  1.00 74.02  ? 499 VAL B N   1 
ATOM   6474 C  CA  . VAL B 1 400 ? -16.524 35.262 60.169  1.00 75.11  ? 499 VAL B CA  1 
ATOM   6475 C  C   . VAL B 1 400 ? -15.517 35.046 59.033  1.00 76.00  ? 499 VAL B C   1 
ATOM   6476 O  O   . VAL B 1 400 ? -14.511 35.746 58.963  1.00 76.47  ? 499 VAL B O   1 
ATOM   6477 C  CB  . VAL B 1 400 ? -16.690 36.766 60.514  1.00 75.82  ? 499 VAL B CB  1 
ATOM   6478 C  CG1 . VAL B 1 400 ? -17.292 37.523 59.344  1.00 76.06  ? 499 VAL B CG1 1 
ATOM   6479 C  CG2 . VAL B 1 400 ? -17.546 36.958 61.760  1.00 76.44  ? 499 VAL B CG2 1 
ATOM   6480 N  N   . GLU B 1 401 ? -15.759 34.056 58.171  1.00 76.12  ? 500 GLU B N   1 
ATOM   6481 C  CA  . GLU B 1 401 ? -14.820 33.718 57.107  1.00 76.96  ? 500 GLU B CA  1 
ATOM   6482 C  C   . GLU B 1 401 ? -15.522 33.570 55.758  1.00 78.06  ? 500 GLU B C   1 
ATOM   6483 O  O   . GLU B 1 401 ? -16.016 32.494 55.434  1.00 77.90  ? 500 GLU B O   1 
ATOM   6484 C  CB  . GLU B 1 401 ? -14.108 32.413 57.489  1.00 78.54  ? 500 GLU B CB  1 
ATOM   6485 C  CG  . GLU B 1 401 ? -12.972 31.972 56.585  1.00 82.51  ? 500 GLU B CG  1 
ATOM   6486 C  CD  . GLU B 1 401 ? -12.496 30.563 56.887  1.00 87.11  ? 500 GLU B CD  1 
ATOM   6487 O  OE1 . GLU B 1 401 ? -11.299 30.273 56.657  1.00 87.60  ? 500 GLU B OE1 1 
ATOM   6488 O  OE2 . GLU B 1 401 ? -13.321 29.748 57.362  1.00 88.63  ? 500 GLU B OE2 1 
ATOM   6489 N  N   . GLY B 1 402 ? -15.567 34.649 54.985  1.00 79.00  ? 501 GLY B N   1 
ATOM   6490 C  CA  . GLY B 1 402 ? -16.173 34.623 53.658  1.00 80.23  ? 501 GLY B CA  1 
ATOM   6491 C  C   . GLY B 1 402 ? -17.641 34.985 53.568  1.00 81.13  ? 501 GLY B C   1 
ATOM   6492 O  O   . GLY B 1 402 ? -18.068 35.558 52.564  1.00 81.38  ? 501 GLY B O   1 
ATOM   6493 N  N   . TRP B 1 403 ? -18.438 34.618 54.576  1.00 81.47  ? 502 TRP B N   1 
ATOM   6494 C  CA  . TRP B 1 403 ? -19.864 34.948 54.577  1.00 82.26  ? 502 TRP B CA  1 
ATOM   6495 C  C   . TRP B 1 403 ? -20.204 35.825 55.832  1.00 82.17  ? 502 TRP B C   1 
ATOM   6496 O  O   . TRP B 1 403 ? -19.315 36.498 56.351  1.00 81.99  ? 502 TRP B O   1 
ATOM   6497 C  CB  . TRP B 1 403 ? -20.736 33.663 54.386  1.00 82.68  ? 502 TRP B CB  1 
ATOM   6498 C  CG  . TRP B 1 403 ? -22.216 33.896 54.183  1.00 83.66  ? 502 TRP B CG  1 
ATOM   6499 C  CD1 . TRP B 1 403 ? -23.231 33.426 54.964  1.00 84.61  ? 502 TRP B CD1 1 
ATOM   6500 C  CD2 . TRP B 1 403 ? -22.836 34.691 53.157  1.00 83.95  ? 502 TRP B CD2 1 
ATOM   6501 N  NE1 . TRP B 1 403 ? -24.441 33.869 54.485  1.00 84.94  ? 502 TRP B NE1 1 
ATOM   6502 C  CE2 . TRP B 1 403 ? -24.228 34.646 53.376  1.00 84.81  ? 502 TRP B CE2 1 
ATOM   6503 C  CE3 . TRP B 1 403 ? -22.353 35.417 52.061  1.00 84.51  ? 502 TRP B CE3 1 
ATOM   6504 C  CZ2 . TRP B 1 403 ? -25.136 35.314 52.550  1.00 85.51  ? 502 TRP B CZ2 1 
ATOM   6505 C  CZ3 . TRP B 1 403 ? -23.254 36.078 51.248  1.00 85.31  ? 502 TRP B CZ3 1 
ATOM   6506 C  CH2 . TRP B 1 403 ? -24.625 36.030 51.499  1.00 85.46  ? 502 TRP B CH2 1 
ATOM   6507 N  N   . ARG B 1 404 ? -21.461 35.869 56.279  1.00 82.20  ? 503 ARG B N   1 
ATOM   6508 C  CA  . ARG B 1 404 ? -21.862 36.680 57.418  1.00 82.67  ? 503 ARG B CA  1 
ATOM   6509 C  C   . ARG B 1 404 ? -22.330 35.825 58.607  1.00 82.03  ? 503 ARG B C   1 
ATOM   6510 O  O   . ARG B 1 404 ? -22.933 34.765 58.425  1.00 82.01  ? 503 ARG B O   1 
ATOM   6511 C  CB  . ARG B 1 404 ? -22.932 37.718 57.003  1.00 84.85  ? 503 ARG B CB  1 
ATOM   6512 C  CG  . ARG B 1 404 ? -24.040 37.153 56.107  1.00 89.07  ? 503 ARG B CG  1 
ATOM   6513 C  CD  . ARG B 1 404 ? -25.145 38.153 55.814  1.00 93.27  ? 503 ARG B CD  1 
ATOM   6514 N  NE  . ARG B 1 404 ? -25.759 37.889 54.510  1.00 97.08  ? 503 ARG B NE  1 
ATOM   6515 C  CZ  . ARG B 1 404 ? -25.698 38.717 53.469  1.00 99.89  ? 503 ARG B CZ  1 
ATOM   6516 N  NH1 . ARG B 1 404 ? -25.094 39.894 53.581  1.00 99.99  ? 503 ARG B NH1 1 
ATOM   6517 N  NH2 . ARG B 1 404 ? -26.263 38.384 52.315  1.00 99.66  ? 503 ARG B NH2 1 
ATOM   6518 N  N   . SER B 1 405 ? -22.010 36.279 59.826  1.00 81.28  ? 504 SER B N   1 
ATOM   6519 C  CA  . SER B 1 405 ? -22.380 35.627 61.080  1.00 80.85  ? 504 SER B CA  1 
ATOM   6520 C  C   . SER B 1 405 ? -23.259 36.580 61.891  1.00 80.40  ? 504 SER B C   1 
ATOM   6521 O  O   . SER B 1 405 ? -23.109 37.790 61.792  1.00 80.60  ? 504 SER B O   1 
ATOM   6522 C  CB  . SER B 1 405 ? -21.134 35.262 61.880  1.00 81.81  ? 504 SER B CB  1 
ATOM   6523 O  OG  . SER B 1 405 ? -20.246 34.445 61.135  1.00 83.60  ? 504 SER B OG  1 
ATOM   6524 N  N   . GLU B 1 406 ? -24.159 36.044 62.700  1.00 79.70  ? 505 GLU B N   1 
ATOM   6525 C  CA  . GLU B 1 406 ? -25.080 36.853 63.482  1.00 79.71  ? 505 GLU B CA  1 
ATOM   6526 C  C   . GLU B 1 406 ? -25.189 36.302 64.899  1.00 79.17  ? 505 GLU B C   1 
ATOM   6527 O  O   . GLU B 1 406 ? -25.353 35.101 65.072  1.00 79.26  ? 505 GLU B O   1 
ATOM   6528 C  CB  . GLU B 1 406 ? -26.440 36.870 62.775  1.00 82.54  ? 505 GLU B CB  1 
ATOM   6529 C  CG  . GLU B 1 406 ? -27.585 37.482 63.554  1.00 88.69  ? 505 GLU B CG  1 
ATOM   6530 C  CD  . GLU B 1 406 ? -28.905 37.267 62.842  1.00 98.09  ? 505 GLU B CD  1 
ATOM   6531 O  OE1 . GLU B 1 406 ? -29.157 37.968 61.834  1.00 100.88 ? 505 GLU B OE1 1 
ATOM   6532 O  OE2 . GLU B 1 406 ? -29.678 36.381 63.273  1.00 100.67 ? 505 GLU B OE2 1 
ATOM   6533 N  N   . VAL B 1 407 ? -25.057 37.174 65.914  1.00 78.42  ? 506 VAL B N   1 
ATOM   6534 C  CA  . VAL B 1 407 ? -25.101 36.794 67.329  1.00 77.99  ? 506 VAL B CA  1 
ATOM   6535 C  C   . VAL B 1 407 ? -26.124 37.621 68.134  1.00 77.40  ? 506 VAL B C   1 
ATOM   6536 O  O   . VAL B 1 407 ? -26.498 38.718 67.732  1.00 77.15  ? 506 VAL B O   1 
ATOM   6537 C  CB  . VAL B 1 407 ? -23.686 36.877 67.969  1.00 78.53  ? 506 VAL B CB  1 
ATOM   6538 C  CG1 . VAL B 1 407 ? -22.706 35.935 67.270  1.00 79.30  ? 506 VAL B CG1 1 
ATOM   6539 C  CG2 . VAL B 1 407 ? -23.155 38.308 67.953  1.00 78.55  ? 506 VAL B CG2 1 
ATOM   6540 N  N   . LEU B 1 408 ? -26.564 37.092 69.278  1.00 77.21  ? 507 LEU B N   1 
ATOM   6541 C  CA  . LEU B 1 408 ? -27.518 37.747 70.181  1.00 77.26  ? 507 LEU B CA  1 
ATOM   6542 C  C   . LEU B 1 408 ? -26.785 38.254 71.435  1.00 77.62  ? 507 LEU B C   1 
ATOM   6543 O  O   . LEU B 1 408 ? -26.472 37.469 72.338  1.00 77.49  ? 507 LEU B O   1 
ATOM   6544 C  CB  . LEU B 1 408 ? -28.627 36.754 70.572  1.00 77.03  ? 507 LEU B CB  1 
ATOM   6545 C  CG  . LEU B 1 408 ? -29.693 37.260 71.527  1.00 77.95  ? 507 LEU B CG  1 
ATOM   6546 C  CD1 . LEU B 1 408 ? -30.424 38.440 70.955  1.00 78.59  ? 507 LEU B CD1 1 
ATOM   6547 C  CD2 . LEU B 1 408 ? -30.675 36.175 71.837  1.00 78.37  ? 507 LEU B CD2 1 
ATOM   6548 N  N   . VAL B 1 409 ? -26.493 39.562 71.472  1.00 77.72  ? 508 VAL B N   1 
ATOM   6549 C  CA  . VAL B 1 409 ? -25.744 40.177 72.558  1.00 78.48  ? 508 VAL B CA  1 
ATOM   6550 C  C   . VAL B 1 409 ? -26.585 41.024 73.532  1.00 79.77  ? 508 VAL B C   1 
ATOM   6551 O  O   . VAL B 1 409 ? -27.652 41.532 73.197  1.00 80.06  ? 508 VAL B O   1 
ATOM   6552 C  CB  . VAL B 1 409 ? -24.577 41.007 71.993  1.00 78.83  ? 508 VAL B CB  1 
ATOM   6553 C  CG1 . VAL B 1 409 ? -23.661 40.139 71.155  1.00 79.38  ? 508 VAL B CG1 1 
ATOM   6554 C  CG2 . VAL B 1 409 ? -25.100 42.176 71.175  1.00 79.19  ? 508 VAL B CG2 1 
ATOM   6555 N  N   . LYS B 1 410 ? -26.064 41.186 74.748  1.00 80.07  ? 509 LYS B N   1 
ATOM   6556 C  CA  . LYS B 1 410 ? -26.664 41.987 75.797  1.00 80.57  ? 509 LYS B CA  1 
ATOM   6557 C  C   . LYS B 1 410 ? -25.505 42.472 76.665  1.00 81.29  ? 509 LYS B C   1 
ATOM   6558 O  O   . LYS B 1 410 ? -24.670 41.673 77.090  1.00 81.15  ? 509 LYS B O   1 
ATOM   6559 C  CB  . LYS B 1 410 ? -27.670 41.156 76.600  1.00 81.87  ? 509 LYS B CB  1 
ATOM   6560 C  CG  . LYS B 1 410 ? -28.372 41.929 77.698  1.00 85.05  ? 509 LYS B CG  1 
ATOM   6561 C  CD  . LYS B 1 410 ? -29.501 41.105 78.266  1.00 89.13  ? 509 LYS B CD  1 
ATOM   6562 C  CE  . LYS B 1 410 ? -29.376 40.956 79.757  1.00 93.12  ? 509 LYS B CE  1 
ATOM   6563 N  NZ  . LYS B 1 410 ? -28.129 40.241 80.138  1.00 95.10  ? 509 LYS B NZ  1 
ATOM   6564 N  N   . PHE B 1 411 ? -25.407 43.784 76.859  1.00 81.96  ? 510 PHE B N   1 
ATOM   6565 C  CA  . PHE B 1 411 ? -24.319 44.365 77.634  1.00 82.92  ? 510 PHE B CA  1 
ATOM   6566 C  C   . PHE B 1 411 ? -24.817 44.760 78.985  1.00 83.55  ? 510 PHE B C   1 
ATOM   6567 O  O   . PHE B 1 411 ? -25.537 45.743 79.106  1.00 83.87  ? 510 PHE B O   1 
ATOM   6568 C  CB  . PHE B 1 411 ? -23.709 45.556 76.897  1.00 82.91  ? 510 PHE B CB  1 
ATOM   6569 C  CG  . PHE B 1 411 ? -23.074 45.094 75.616  1.00 83.63  ? 510 PHE B CG  1 
ATOM   6570 C  CD1 . PHE B 1 411 ? -23.833 44.918 74.473  1.00 84.53  ? 510 PHE B CD1 1 
ATOM   6571 C  CD2 . PHE B 1 411 ? -21.734 44.761 75.572  1.00 84.45  ? 510 PHE B CD2 1 
ATOM   6572 C  CE1 . PHE B 1 411 ? -23.261 44.437 73.308  1.00 85.34  ? 510 PHE B CE1 1 
ATOM   6573 C  CE2 . PHE B 1 411 ? -21.167 44.276 74.407  1.00 85.33  ? 510 PHE B CE2 1 
ATOM   6574 C  CZ  . PHE B 1 411 ? -21.933 44.120 73.282  1.00 85.23  ? 510 PHE B CZ  1 
ATOM   6575 N  N   . ASP B 1 412 ? -24.461 43.981 80.003  1.00 83.58  ? 511 ASP B N   1 
ATOM   6576 C  CA  . ASP B 1 412 ? -24.924 44.252 81.354  1.00 84.24  ? 511 ASP B CA  1 
ATOM   6577 C  C   . ASP B 1 412 ? -24.116 45.310 82.100  1.00 84.25  ? 511 ASP B C   1 
ATOM   6578 O  O   . ASP B 1 412 ? -24.448 45.613 83.241  1.00 84.24  ? 511 ASP B O   1 
ATOM   6579 C  CB  . ASP B 1 412 ? -24.994 42.948 82.161  1.00 86.33  ? 511 ASP B CB  1 
ATOM   6580 C  CG  . ASP B 1 412 ? -26.279 42.175 81.932  1.00 91.48  ? 511 ASP B CG  1 
ATOM   6581 O  OD1 . ASP B 1 412 ? -27.330 42.818 81.736  1.00 92.50  ? 511 ASP B OD1 1 
ATOM   6582 O  OD2 . ASP B 1 412 ? -26.235 40.926 81.965  1.00 93.70  ? 511 ASP B OD2 1 
ATOM   6583 N  N   . HIS B 1 413 ? -23.060 45.863 81.485  1.00 84.17  ? 512 HIS B N   1 
ATOM   6584 C  CA  . HIS B 1 413 ? -22.219 46.849 82.156  1.00 84.76  ? 512 HIS B CA  1 
ATOM   6585 C  C   . HIS B 1 413 ? -21.980 48.078 81.296  1.00 85.71  ? 512 HIS B C   1 
ATOM   6586 O  O   . HIS B 1 413 ? -21.936 47.973 80.076  1.00 86.04  ? 512 HIS B O   1 
ATOM   6587 C  CB  . HIS B 1 413 ? -20.892 46.212 82.602  1.00 85.17  ? 512 HIS B CB  1 
ATOM   6588 C  CG  . HIS B 1 413 ? -21.091 45.004 83.455  1.00 86.75  ? 512 HIS B CG  1 
ATOM   6589 N  ND1 . HIS B 1 413 ? -21.196 45.105 84.826  1.00 88.38  ? 512 HIS B ND1 1 
ATOM   6590 C  CD2 . HIS B 1 413 ? -21.277 43.713 83.095  1.00 87.71  ? 512 HIS B CD2 1 
ATOM   6591 C  CE1 . HIS B 1 413 ? -21.407 43.874 85.259  1.00 88.85  ? 512 HIS B CE1 1 
ATOM   6592 N  NE2 . HIS B 1 413 ? -21.476 43.005 84.250  1.00 88.72  ? 512 HIS B NE2 1 
ATOM   6593 N  N   . GLU B 1 414 ? -21.827 49.244 81.923  1.00 85.97  ? 513 GLU B N   1 
ATOM   6594 C  CA  . GLU B 1 414 ? -21.618 50.489 81.190  1.00 86.92  ? 513 GLU B CA  1 
ATOM   6595 C  C   . GLU B 1 414 ? -20.193 50.647 80.644  1.00 87.56  ? 513 GLU B C   1 
ATOM   6596 O  O   . GLU B 1 414 ? -19.252 50.059 81.170  1.00 87.68  ? 513 GLU B O   1 
ATOM   6597 C  CB  . GLU B 1 414 ? -21.998 51.699 82.063  1.00 89.43  ? 513 GLU B CB  1 
ATOM   6598 C  CG  . GLU B 1 414 ? -23.482 51.794 82.379  1.00 94.40  ? 513 GLU B CG  1 
ATOM   6599 C  CD  . GLU B 1 414 ? -23.878 52.948 83.280  1.00 100.12 ? 513 GLU B CD  1 
ATOM   6600 O  OE1 . GLU B 1 414 ? -23.430 54.089 83.023  1.00 101.20 ? 513 GLU B OE1 1 
ATOM   6601 O  OE2 . GLU B 1 414 ? -24.645 52.711 84.241  1.00 101.98 ? 513 GLU B OE2 1 
ATOM   6602 N  N   . ALA B 1 415 ? -20.046 51.446 79.583  1.00 87.88  ? 514 ALA B N   1 
ATOM   6603 C  CA  . ALA B 1 415 ? -18.761 51.758 78.974  1.00 88.78  ? 514 ALA B CA  1 
ATOM   6604 C  C   . ALA B 1 415 ? -18.854 53.174 78.446  1.00 90.03  ? 514 ALA B C   1 
ATOM   6605 O  O   . ALA B 1 415 ? -19.528 53.420 77.456  1.00 90.35  ? 514 ALA B O   1 
ATOM   6606 C  CB  . ALA B 1 415 ? -18.458 50.806 77.835  1.00 88.74  ? 514 ALA B CB  1 
ATOM   6607 N  N   . PRO B 1 416 ? -18.221 54.137 79.117  1.00 90.54  ? 515 PRO B N   1 
ATOM   6608 C  CA  . PRO B 1 416 ? -18.286 55.533 78.645  1.00 90.81  ? 515 PRO B CA  1 
ATOM   6609 C  C   . PRO B 1 416 ? -17.477 55.794 77.364  1.00 90.83  ? 515 PRO B C   1 
ATOM   6610 O  O   . PRO B 1 416 ? -16.812 54.892 76.873  1.00 91.12  ? 515 PRO B O   1 
ATOM   6611 C  CB  . PRO B 1 416 ? -17.724 56.313 79.836  1.00 91.74  ? 515 PRO B CB  1 
ATOM   6612 C  CG  . PRO B 1 416 ? -16.761 55.361 80.469  1.00 92.20  ? 515 PRO B CG  1 
ATOM   6613 C  CD  . PRO B 1 416 ? -17.391 54.003 80.329  1.00 90.39  ? 515 PRO B CD  1 
ATOM   6614 N  N   . LYS B 1 417 ? -17.526 57.022 76.815  1.00 90.45  ? 516 LYS B N   1 
ATOM   6615 C  CA  . LYS B 1 417 ? -16.770 57.352 75.604  1.00 90.64  ? 516 LYS B CA  1 
ATOM   6616 C  C   . LYS B 1 417 ? -15.270 57.192 75.843  1.00 90.33  ? 516 LYS B C   1 
ATOM   6617 O  O   . LYS B 1 417 ? -14.557 56.649 75.005  1.00 90.08  ? 516 LYS B O   1 
ATOM   6618 C  CB  . LYS B 1 417 ? -17.093 58.789 75.143  1.00 92.95  ? 516 LYS B CB  1 
ATOM   6619 C  CG  . LYS B 1 417 ? -16.363 59.217 73.873  1.00 97.39  ? 516 LYS B CG  1 
ATOM   6620 C  CD  . LYS B 1 417 ? -16.333 60.740 73.680  1.00 102.12 ? 516 LYS B CD  1 
ATOM   6621 C  CE  . LYS B 1 417 ? -15.486 61.158 72.490  1.00 106.30 ? 516 LYS B CE  1 
ATOM   6622 N  NZ  . LYS B 1 417 ? -14.778 62.452 72.724  1.00 108.68 ? 516 LYS B NZ  1 
ATOM   6623 N  N   . GLU B 1 418 ? -14.811 57.640 77.012  1.00 90.41  ? 517 GLU B N   1 
ATOM   6624 C  CA  . GLU B 1 418 ? -13.409 57.621 77.425  1.00 90.80  ? 517 GLU B CA  1 
ATOM   6625 C  C   . GLU B 1 418 ? -12.873 56.197 77.547  1.00 90.88  ? 517 GLU B C   1 
ATOM   6626 O  O   . GLU B 1 418 ? -11.718 55.936 77.207  1.00 90.94  ? 517 GLU B O   1 
ATOM   6627 C  CB  . GLU B 1 418 ? -13.225 58.384 78.754  1.00 92.51  ? 517 GLU B CB  1 
ATOM   6628 C  CG  . GLU B 1 418 ? -14.121 59.604 78.920  1.00 96.00  ? 517 GLU B CG  1 
ATOM   6629 C  CD  . GLU B 1 418 ? -15.392 59.329 79.701  1.00 100.83 ? 517 GLU B CD  1 
ATOM   6630 O  OE1 . GLU B 1 418 ? -16.461 59.853 79.315  1.00 100.63 ? 517 GLU B OE1 1 
ATOM   6631 O  OE2 . GLU B 1 418 ? -15.317 58.578 80.700  1.00 103.44 ? 517 GLU B OE2 1 
ATOM   6632 N  N   . ARG B 1 419 ? -13.715 55.281 78.043  1.00 90.56  ? 518 ARG B N   1 
ATOM   6633 C  CA  . ARG B 1 419 ? -13.370 53.875 78.225  1.00 90.46  ? 518 ARG B CA  1 
ATOM   6634 C  C   . ARG B 1 419 ? -14.440 53.012 77.569  1.00 89.38  ? 518 ARG B C   1 
ATOM   6635 O  O   . ARG B 1 419 ? -15.252 52.381 78.243  1.00 89.53  ? 518 ARG B O   1 
ATOM   6636 C  CB  . ARG B 1 419 ? -13.245 53.561 79.716  1.00 92.59  ? 518 ARG B CB  1 
ATOM   6637 C  CG  . ARG B 1 419 ? -12.105 54.327 80.375  1.00 97.37  ? 518 ARG B CG  1 
ATOM   6638 C  CD  . ARG B 1 419 ? -10.770 53.677 80.091  1.00 102.45 ? 518 ARG B CD  1 
ATOM   6639 N  NE  . ARG B 1 419 ? -10.421 52.732 81.150  1.00 107.75 ? 518 ARG B NE  1 
ATOM   6640 C  CZ  . ARG B 1 419 ? -9.430  52.915 82.017  1.00 112.13 ? 518 ARG B CZ  1 
ATOM   6641 N  NH1 . ARG B 1 419 ? -8.641  53.982 81.923  1.00 112.49 ? 518 ARG B NH1 1 
ATOM   6642 N  NH2 . ARG B 1 419 ? -9.190  52.011 82.959  1.00 112.84 ? 518 ARG B NH2 1 
ATOM   6643 N  N   . ALA B 1 420 ? -14.452 53.007 76.243  1.00 88.17  ? 519 ALA B N   1 
ATOM   6644 C  CA  . ALA B 1 420 ? -15.440 52.270 75.468  1.00 87.63  ? 519 ALA B CA  1 
ATOM   6645 C  C   . ALA B 1 420 ? -15.038 50.823 75.194  1.00 86.57  ? 519 ALA B C   1 
ATOM   6646 O  O   . ALA B 1 420 ? -13.848 50.500 75.166  1.00 86.94  ? 519 ALA B O   1 
ATOM   6647 C  CB  . ALA B 1 420 ? -15.687 52.991 74.149  1.00 87.90  ? 519 ALA B CB  1 
ATOM   6648 N  N   . TYR B 1 421 ? -16.034 49.957 74.960  1.00 84.93  ? 520 TYR B N   1 
ATOM   6649 C  CA  . TYR B 1 421 ? -15.775 48.568 74.615  1.00 83.61  ? 520 TYR B CA  1 
ATOM   6650 C  C   . TYR B 1 421 ? -15.239 48.482 73.193  1.00 82.25  ? 520 TYR B C   1 
ATOM   6651 O  O   . TYR B 1 421 ? -15.558 49.318 72.359  1.00 82.17  ? 520 TYR B O   1 
ATOM   6652 C  CB  . TYR B 1 421 ? -17.074 47.759 74.666  1.00 83.46  ? 520 TYR B CB  1 
ATOM   6653 C  CG  . TYR B 1 421 ? -17.596 47.495 76.055  1.00 84.11  ? 520 TYR B CG  1 
ATOM   6654 C  CD1 . TYR B 1 421 ? -16.750 47.066 77.066  1.00 85.01  ? 520 TYR B CD1 1 
ATOM   6655 C  CD2 . TYR B 1 421 ? -18.949 47.595 76.338  1.00 84.86  ? 520 TYR B CD2 1 
ATOM   6656 C  CE1 . TYR B 1 421 ? -17.231 46.788 78.337  1.00 85.81  ? 520 TYR B CE1 1 
ATOM   6657 C  CE2 . TYR B 1 421 ? -19.442 47.318 77.605  1.00 85.76  ? 520 TYR B CE2 1 
ATOM   6658 C  CZ  . TYR B 1 421 ? -18.578 46.915 78.603  1.00 86.76  ? 520 TYR B CZ  1 
ATOM   6659 O  OH  . TYR B 1 421 ? -19.067 46.636 79.852  1.00 88.54  ? 520 TYR B OH  1 
ATOM   6660 N  N   . MET B 1 422 ? -14.462 47.451 72.907  1.00 81.05  ? 521 MET B N   1 
ATOM   6661 C  CA  . MET B 1 422 ? -13.960 47.197 71.563  1.00 80.21  ? 521 MET B CA  1 
ATOM   6662 C  C   . MET B 1 422 ? -14.707 45.991 70.961  1.00 79.25  ? 521 MET B C   1 
ATOM   6663 O  O   . MET B 1 422 ? -15.342 45.218 71.668  1.00 79.28  ? 521 MET B O   1 
ATOM   6664 C  CB  . MET B 1 422 ? -12.454 46.892 71.596  1.00 80.73  ? 521 MET B CB  1 
ATOM   6665 C  CG  . MET B 1 422 ? -11.635 47.902 72.330  1.00 82.45  ? 521 MET B CG  1 
ATOM   6666 S  SD  . MET B 1 422 ? -11.094 49.207 71.226  1.00 84.91  ? 521 MET B SD  1 
ATOM   6667 C  CE  . MET B 1 422 ? -11.462 50.610 72.242  1.00 83.82  ? 521 MET B CE  1 
ATOM   6668 N  N   . ALA B 1 423 ? -14.634 45.838 69.655  1.00 78.55  ? 522 ALA B N   1 
ATOM   6669 C  CA  . ALA B 1 423 ? -15.222 44.715 68.936  1.00 78.48  ? 522 ALA B CA  1 
ATOM   6670 C  C   . ALA B 1 423 ? -14.354 44.607 67.709  1.00 78.14  ? 522 ALA B C   1 
ATOM   6671 O  O   . ALA B 1 423 ? -14.231 45.579 66.962  1.00 78.44  ? 522 ALA B O   1 
ATOM   6672 C  CB  . ALA B 1 423 ? -16.667 45.003 68.563  1.00 78.63  ? 522 ALA B CB  1 
ATOM   6673 N  N   . HIS B 1 424 ? -13.682 43.471 67.536  1.00 77.40  ? 523 HIS B N   1 
ATOM   6674 C  CA  . HIS B 1 424 ? -12.692 43.357 66.473  1.00 77.32  ? 523 HIS B CA  1 
ATOM   6675 C  C   . HIS B 1 424 ? -12.411 41.938 66.019  1.00 76.50  ? 523 HIS B C   1 
ATOM   6676 O  O   . HIS B 1 424 ? -12.881 40.977 66.608  1.00 76.52  ? 523 HIS B O   1 
ATOM   6677 C  CB  . HIS B 1 424 ? -11.381 44.011 66.972  1.00 78.52  ? 523 HIS B CB  1 
ATOM   6678 C  CG  . HIS B 1 424 ? -10.907 43.473 68.285  1.00 80.64  ? 523 HIS B CG  1 
ATOM   6679 N  ND1 . HIS B 1 424 ? -10.035 42.397 68.354  1.00 82.44  ? 523 HIS B ND1 1 
ATOM   6680 C  CD2 . HIS B 1 424 ? -11.243 43.849 69.541  1.00 81.81  ? 523 HIS B CD2 1 
ATOM   6681 C  CE1 . HIS B 1 424 ? -9.855  42.168 69.645  1.00 83.13  ? 523 HIS B CE1 1 
ATOM   6682 N  NE2 . HIS B 1 424 ? -10.565 43.013 70.398  1.00 83.04  ? 523 HIS B NE2 1 
ATOM   6683 N  N   . CYS B 1 425 ? -11.630 41.819 64.958  1.00 75.75  ? 524 CYS B N   1 
ATOM   6684 C  CA  . CYS B 1 425 ? -11.159 40.558 64.436  1.00 75.63  ? 524 CYS B CA  1 
ATOM   6685 C  C   . CYS B 1 425 ? -10.040 40.143 65.382  1.00 75.08  ? 524 CYS B C   1 
ATOM   6686 O  O   . CYS B 1 425 ? -9.110  40.930 65.600  1.00 75.14  ? 524 CYS B O   1 
ATOM   6687 C  CB  . CYS B 1 425 ? -10.631 40.775 63.024  1.00 76.55  ? 524 CYS B CB  1 
ATOM   6688 S  SG  . CYS B 1 425 ? -9.818  39.336 62.298  1.00 80.20  ? 524 CYS B SG  1 
ATOM   6689 N  N   . HIS B 1 426 ? -10.125 38.934 65.967  1.00 74.31  ? 525 HIS B N   1 
ATOM   6690 C  CA  . HIS B 1 426 ? -9.078  38.499 66.882  1.00 74.23  ? 525 HIS B CA  1 
ATOM   6691 C  C   . HIS B 1 426 ? -7.816  37.986 66.175  1.00 74.14  ? 525 HIS B C   1 
ATOM   6692 O  O   . HIS B 1 426 ? -6.904  37.491 66.841  1.00 74.60  ? 525 HIS B O   1 
ATOM   6693 C  CB  . HIS B 1 426 ? -9.553  37.519 67.945  1.00 74.90  ? 525 HIS B CB  1 
ATOM   6694 C  CG  . HIS B 1 426 ? -8.845  37.725 69.251  1.00 76.83  ? 525 HIS B CG  1 
ATOM   6695 N  ND1 . HIS B 1 426 ? -7.636  37.104 69.528  1.00 78.38  ? 525 HIS B ND1 1 
ATOM   6696 C  CD2 . HIS B 1 426 ? -9.176  38.521 70.294  1.00 77.89  ? 525 HIS B CD2 1 
ATOM   6697 C  CE1 . HIS B 1 426 ? -7.292  37.515 70.735  1.00 78.89  ? 525 HIS B CE1 1 
ATOM   6698 N  NE2 . HIS B 1 426 ? -8.186  38.373 71.235  1.00 78.83  ? 525 HIS B NE2 1 
ATOM   6699 N  N   . LEU B 1 427 ? -7.691  38.203 64.850  1.00 73.28  ? 526 LEU B N   1 
ATOM   6700 C  CA  . LEU B 1 427 ? -6.442  37.946 64.150  1.00 73.01  ? 526 LEU B CA  1 
ATOM   6701 C  C   . LEU B 1 427 ? -5.741  39.264 64.455  1.00 73.21  ? 526 LEU B C   1 
ATOM   6702 O  O   . LEU B 1 427 ? -6.104  40.295 63.893  1.00 73.57  ? 526 LEU B O   1 
ATOM   6703 C  CB  . LEU B 1 427 ? -6.676  37.792 62.649  1.00 72.74  ? 526 LEU B CB  1 
ATOM   6704 C  CG  . LEU B 1 427 ? -5.562  37.141 61.867  1.00 73.43  ? 526 LEU B CG  1 
ATOM   6705 C  CD1 . LEU B 1 427 ? -6.103  36.458 60.652  1.00 73.64  ? 526 LEU B CD1 1 
ATOM   6706 C  CD2 . LEU B 1 427 ? -4.493  38.144 61.495  1.00 73.94  ? 526 LEU B CD2 1 
ATOM   6707 N  N   . LEU B 1 428 ? -4.907  39.251 65.496  1.00 72.65  ? 527 LEU B N   1 
ATOM   6708 C  CA  . LEU B 1 428 ? -4.275  40.429 66.063  1.00 72.66  ? 527 LEU B CA  1 
ATOM   6709 C  C   . LEU B 1 428 ? -3.734  41.445 65.061  1.00 72.40  ? 527 LEU B C   1 
ATOM   6710 O  O   . LEU B 1 428 ? -3.952  42.636 65.265  1.00 72.83  ? 527 LEU B O   1 
ATOM   6711 C  CB  . LEU B 1 428 ? -3.186  40.027 67.054  1.00 72.98  ? 527 LEU B CB  1 
ATOM   6712 C  CG  . LEU B 1 428 ? -3.635  39.138 68.221  1.00 73.96  ? 527 LEU B CG  1 
ATOM   6713 C  CD1 . LEU B 1 428 ? -2.496  38.901 69.161  1.00 74.17  ? 527 LEU B CD1 1 
ATOM   6714 C  CD2 . LEU B 1 428 ? -4.823  39.735 68.975  1.00 74.36  ? 527 LEU B CD2 1 
ATOM   6715 N  N   . GLU B 1 429 ? -3.084  41.003 63.979  1.00 71.53  ? 528 GLU B N   1 
ATOM   6716 C  CA  . GLU B 1 429 ? -2.558  41.943 62.989  1.00 71.17  ? 528 GLU B CA  1 
ATOM   6717 C  C   . GLU B 1 429 ? -3.678  42.682 62.244  1.00 70.56  ? 528 GLU B C   1 
ATOM   6718 O  O   . GLU B 1 429 ? -3.524  43.864 61.970  1.00 70.53  ? 528 GLU B O   1 
ATOM   6719 C  CB  . GLU B 1 429 ? -1.557  41.277 62.045  1.00 73.04  ? 528 GLU B CB  1 
ATOM   6720 C  CG  . GLU B 1 429 ? -0.247  40.919 62.735  1.00 77.22  ? 528 GLU B CG  1 
ATOM   6721 C  CD  . GLU B 1 429 ? -0.325  39.746 63.694  1.00 81.91  ? 528 GLU B CD  1 
ATOM   6722 O  OE1 . GLU B 1 429 ? 0.293   39.808 64.781  1.00 82.38  ? 528 GLU B OE1 1 
ATOM   6723 O  OE2 . GLU B 1 429 ? -1.006  38.754 63.350  1.00 83.79  ? 528 GLU B OE2 1 
ATOM   6724 N  N   . HIS B 1 430 ? -4.833  42.030 61.995  1.00 69.85  ? 529 HIS B N   1 
ATOM   6725 C  CA  . HIS B 1 430 ? -5.970  42.706 61.362  1.00 69.57  ? 529 HIS B CA  1 
ATOM   6726 C  C   . HIS B 1 430 ? -6.477  43.801 62.286  1.00 70.22  ? 529 HIS B C   1 
ATOM   6727 O  O   . HIS B 1 430 ? -6.677  44.931 61.849  1.00 70.34  ? 529 HIS B O   1 
ATOM   6728 C  CB  . HIS B 1 430 ? -7.123  41.731 61.054  1.00 68.90  ? 529 HIS B CB  1 
ATOM   6729 C  CG  . HIS B 1 430 ? -6.880  40.814 59.902  1.00 69.21  ? 529 HIS B CG  1 
ATOM   6730 N  ND1 . HIS B 1 430 ? -7.773  39.803 59.597  1.00 70.67  ? 529 HIS B ND1 1 
ATOM   6731 C  CD2 . HIS B 1 430 ? -5.860  40.780 59.012  1.00 69.77  ? 529 HIS B CD2 1 
ATOM   6732 C  CE1 . HIS B 1 430 ? -7.268  39.183 58.545  1.00 70.86  ? 529 HIS B CE1 1 
ATOM   6733 N  NE2 . HIS B 1 430 ? -6.125  39.745 58.149  1.00 70.67  ? 529 HIS B NE2 1 
ATOM   6734 N  N   . GLU B 1 431 ? -6.639  43.465 63.575  1.00 70.33  ? 530 GLU B N   1 
ATOM   6735 C  CA  . GLU B 1 431 ? -7.099  44.374 64.613  1.00 70.60  ? 530 GLU B CA  1 
ATOM   6736 C  C   . GLU B 1 431 ? -6.149  45.584 64.716  1.00 70.68  ? 530 GLU B C   1 
ATOM   6737 O  O   . GLU B 1 431 ? -6.611  46.726 64.755  1.00 70.83  ? 530 GLU B O   1 
ATOM   6738 C  CB  . GLU B 1 431 ? -7.175  43.606 65.942  1.00 72.34  ? 530 GLU B CB  1 
ATOM   6739 C  CG  . GLU B 1 431 ? -7.376  44.471 67.167  1.00 76.11  ? 530 GLU B CG  1 
ATOM   6740 C  CD  . GLU B 1 431 ? -6.788  43.880 68.430  1.00 81.27  ? 530 GLU B CD  1 
ATOM   6741 O  OE1 . GLU B 1 431 ? -6.315  44.665 69.283  1.00 82.18  ? 530 GLU B OE1 1 
ATOM   6742 O  OE2 . GLU B 1 431 ? -6.797  42.635 68.569  1.00 83.21  ? 530 GLU B OE2 1 
ATOM   6743 N  N   . ASP B 1 432 ? -4.829  45.331 64.725  1.00 70.38  ? 531 ASP B N   1 
ATOM   6744 C  CA  . ASP B 1 432 ? -3.818  46.379 64.834  1.00 70.84  ? 531 ASP B CA  1 
ATOM   6745 C  C   . ASP B 1 432 ? -3.785  47.307 63.633  1.00 71.57  ? 531 ASP B C   1 
ATOM   6746 O  O   . ASP B 1 432 ? -3.485  48.492 63.773  1.00 71.80  ? 531 ASP B O   1 
ATOM   6747 C  CB  . ASP B 1 432 ? -2.424  45.764 65.043  1.00 71.48  ? 531 ASP B CB  1 
ATOM   6748 C  CG  . ASP B 1 432 ? -2.155  45.302 66.454  1.00 73.65  ? 531 ASP B CG  1 
ATOM   6749 O  OD1 . ASP B 1 432 ? -2.905  45.720 67.372  1.00 73.69  ? 531 ASP B OD1 1 
ATOM   6750 O  OD2 . ASP B 1 432 ? -1.178  44.544 66.654  1.00 75.12  ? 531 ASP B OD2 1 
ATOM   6751 N  N   . THR B 1 433 ? -4.073  46.766 62.455  1.00 71.60  ? 532 THR B N   1 
ATOM   6752 C  CA  . THR B 1 433 ? -4.040  47.538 61.232  1.00 71.82  ? 532 THR B CA  1 
ATOM   6753 C  C   . THR B 1 433 ? -5.407  48.088 60.838  1.00 72.35  ? 532 THR B C   1 
ATOM   6754 O  O   . THR B 1 433 ? -5.662  48.274 59.650  1.00 72.96  ? 532 THR B O   1 
ATOM   6755 C  CB  . THR B 1 433 ? -3.392  46.722 60.126  1.00 72.68  ? 532 THR B CB  1 
ATOM   6756 O  OG1 . THR B 1 433 ? -4.103  45.489 59.987  1.00 73.93  ? 532 THR B OG1 1 
ATOM   6757 C  CG2 . THR B 1 433 ? -1.920  46.458 60.400  1.00 72.53  ? 532 THR B CG2 1 
ATOM   6758 N  N   . GLY B 1 434 ? -6.263  48.368 61.817  1.00 72.12  ? 533 GLY B N   1 
ATOM   6759 C  CA  . GLY B 1 434 ? -7.550  48.988 61.538  1.00 72.46  ? 533 GLY B CA  1 
ATOM   6760 C  C   . GLY B 1 434 ? -8.827  48.218 61.776  1.00 72.88  ? 533 GLY B C   1 
ATOM   6761 O  O   . GLY B 1 434 ? -9.855  48.853 62.003  1.00 73.17  ? 533 GLY B O   1 
ATOM   6762 N  N   . MET B 1 435 ? -8.817  46.880 61.688  1.00 73.01  ? 534 MET B N   1 
ATOM   6763 C  CA  . MET B 1 435 ? -10.042 46.100 61.871  1.00 73.92  ? 534 MET B CA  1 
ATOM   6764 C  C   . MET B 1 435 ? -10.481 45.971 63.331  1.00 75.49  ? 534 MET B C   1 
ATOM   6765 O  O   . MET B 1 435 ? -10.404 44.894 63.923  1.00 76.00  ? 534 MET B O   1 
ATOM   6766 C  CB  . MET B 1 435 ? -9.923  44.725 61.219  1.00 74.21  ? 534 MET B CB  1 
ATOM   6767 C  CG  . MET B 1 435 ? -11.263 44.118 60.875  1.00 75.61  ? 534 MET B CG  1 
ATOM   6768 S  SD  . MET B 1 435 ? -11.119 42.569 59.968  1.00 77.20  ? 534 MET B SD  1 
ATOM   6769 C  CE  . MET B 1 435 ? -10.160 43.095 58.571  1.00 72.92  ? 534 MET B CE  1 
ATOM   6770 N  N   . MET B 1 436 ? -10.954 47.073 63.903  1.00 76.00  ? 535 MET B N   1 
ATOM   6771 C  CA  . MET B 1 436 ? -11.435 47.166 65.278  1.00 76.85  ? 535 MET B CA  1 
ATOM   6772 C  C   . MET B 1 436 ? -12.405 48.337 65.359  1.00 77.95  ? 535 MET B C   1 
ATOM   6773 O  O   . MET B 1 436 ? -12.258 49.316 64.624  1.00 78.42  ? 535 MET B O   1 
ATOM   6774 C  CB  . MET B 1 436 ? -10.262 47.386 66.238  1.00 77.19  ? 535 MET B CB  1 
ATOM   6775 C  CG  . MET B 1 436 ? -10.687 47.564 67.671  1.00 79.08  ? 535 MET B CG  1 
ATOM   6776 S  SD  . MET B 1 436 ? -9.438  47.036 68.852  1.00 83.30  ? 535 MET B SD  1 
ATOM   6777 C  CE  . MET B 1 436 ? -8.048  48.043 68.346  1.00 80.72  ? 535 MET B CE  1 
ATOM   6778 N  N   . MET B 1 437 ? -13.408 48.234 66.221  1.00 78.24  ? 536 MET B N   1 
ATOM   6779 C  CA  . MET B 1 437 ? -14.383 49.302 66.395  1.00 79.26  ? 536 MET B CA  1 
ATOM   6780 C  C   . MET B 1 437 ? -14.696 49.484 67.865  1.00 80.32  ? 536 MET B C   1 
ATOM   6781 O  O   . MET B 1 437 ? -14.685 48.521 68.628  1.00 80.37  ? 536 MET B O   1 
ATOM   6782 C  CB  . MET B 1 437 ? -15.671 49.017 65.606  1.00 79.83  ? 536 MET B CB  1 
ATOM   6783 C  CG  . MET B 1 437 ? -16.237 47.642 65.881  1.00 81.85  ? 536 MET B CG  1 
ATOM   6784 S  SD  . MET B 1 437 ? -18.001 47.506 66.252  1.00 85.75  ? 536 MET B SD  1 
ATOM   6785 C  CE  . MET B 1 437 ? -18.271 48.931 67.248  1.00 84.55  ? 536 MET B CE  1 
ATOM   6786 N  N   . SER B 1 438 ? -14.959 50.720 68.270  1.00 81.01  ? 537 SER B N   1 
ATOM   6787 C  CA  . SER B 1 438 ? -15.318 51.005 69.656  1.00 82.01  ? 537 SER B CA  1 
ATOM   6788 C  C   . SER B 1 438 ? -16.806 51.300 69.772  1.00 82.79  ? 537 SER B C   1 
ATOM   6789 O  O   . SER B 1 438 ? -17.441 51.660 68.787  1.00 83.22  ? 537 SER B O   1 
ATOM   6790 C  CB  . SER B 1 438 ? -14.471 52.136 70.241  1.00 83.39  ? 537 SER B CB  1 
ATOM   6791 O  OG  . SER B 1 438 ? -14.225 53.184 69.317  1.00 85.87  ? 537 SER B OG  1 
ATOM   6792 N  N   . PHE B 1 439 ? -17.373 51.118 70.960  1.00 82.92  ? 538 PHE B N   1 
ATOM   6793 C  CA  . PHE B 1 439 ? -18.788 51.389 71.189  1.00 83.46  ? 538 PHE B CA  1 
ATOM   6794 C  C   . PHE B 1 439 ? -19.079 51.582 72.674  1.00 83.96  ? 538 PHE B C   1 
ATOM   6795 O  O   . PHE B 1 439 ? -18.396 51.016 73.529  1.00 83.88  ? 538 PHE B O   1 
ATOM   6796 C  CB  . PHE B 1 439 ? -19.691 50.310 70.568  1.00 83.33  ? 538 PHE B CB  1 
ATOM   6797 C  CG  . PHE B 1 439 ? -19.546 48.928 71.157  1.00 84.03  ? 538 PHE B CG  1 
ATOM   6798 C  CD1 . PHE B 1 439 ? -18.585 48.053 70.685  1.00 84.77  ? 538 PHE B CD1 1 
ATOM   6799 C  CD2 . PHE B 1 439 ? -20.405 48.485 72.146  1.00 84.75  ? 538 PHE B CD2 1 
ATOM   6800 C  CE1 . PHE B 1 439 ? -18.472 46.773 71.206  1.00 85.30  ? 538 PHE B CE1 1 
ATOM   6801 C  CE2 . PHE B 1 439 ? -20.285 47.208 72.665  1.00 85.29  ? 538 PHE B CE2 1 
ATOM   6802 C  CZ  . PHE B 1 439 ? -19.324 46.358 72.187  1.00 85.06  ? 538 PHE B CZ  1 
ATOM   6803 N  N   . THR B 1 440 ? -20.098 52.382 72.977  1.00 84.16  ? 539 THR B N   1 
ATOM   6804 C  CA  . THR B 1 440 ? -20.461 52.680 74.353  1.00 84.67  ? 539 THR B CA  1 
ATOM   6805 C  C   . THR B 1 440 ? -21.729 51.958 74.808  1.00 85.10  ? 539 THR B C   1 
ATOM   6806 O  O   . THR B 1 440 ? -22.503 51.481 73.988  1.00 84.80  ? 539 THR B O   1 
ATOM   6807 C  CB  . THR B 1 440 ? -20.548 54.198 74.542  1.00 85.80  ? 539 THR B CB  1 
ATOM   6808 O  OG1 . THR B 1 440 ? -21.572 54.729 73.701  1.00 86.87  ? 539 THR B OG1 1 
ATOM   6809 C  CG2 . THR B 1 440 ? -19.236 54.883 74.249  1.00 86.00  ? 539 THR B CG2 1 
ATOM   6810 N  N   . VAL B 1 441 ? -21.901 51.838 76.131  1.00 85.72  ? 540 VAL B N   1 
ATOM   6811 C  CA  . VAL B 1 441 ? -23.059 51.225 76.780  1.00 86.82  ? 540 VAL B CA  1 
ATOM   6812 C  C   . VAL B 1 441 ? -23.485 52.146 77.937  1.00 87.65  ? 540 VAL B C   1 
ATOM   6813 O  O   . VAL B 1 441 ? -22.629 52.584 78.707  1.00 87.57  ? 540 VAL B O   1 
ATOM   6814 C  CB  . VAL B 1 441 ? -22.787 49.775 77.269  1.00 87.48  ? 540 VAL B CB  1 
ATOM   6815 C  CG1 . VAL B 1 441 ? -24.024 49.184 77.925  1.00 87.93  ? 540 VAL B CG1 1 
ATOM   6816 C  CG2 . VAL B 1 441 ? -22.326 48.879 76.128  1.00 87.92  ? 540 VAL B CG2 1 
ATOM   6817 N  N   . SER B 1 442 ? -24.785 52.479 78.036  1.00 88.53  ? 541 SER B N   1 
ATOM   6818 C  CA  . SER B 1 442 ? -25.249 53.382 79.095  1.00 89.69  ? 541 SER B CA  1 
ATOM   6819 C  C   . SER B 1 442 ? -26.647 53.056 79.606  1.00 90.69  ? 541 SER B C   1 
ATOM   6820 O  O   . SER B 1 442 ? -27.484 52.600 78.800  1.00 91.03  ? 541 SER B O   1 
ATOM   6821 C  CB  . SER B 1 442 ? -25.199 54.831 78.624  1.00 91.05  ? 541 SER B CB  1 
ATOM   6822 O  OG  . SER B 1 442 ? -25.834 54.966 77.364  1.00 93.24  ? 541 SER B OG  1 
HETATM 6823 CU CU  . CU  C 2 .   ? 6.352   39.178 31.135  1.00 75.50  ? 601 CU  A CU  1 
HETATM 6824 CU CU  . CU  D 2 .   ? 7.680   42.837 32.304  1.00 101.14 ? 602 CU  A CU  1 
HETATM 6825 CU CU  . CU  E 2 .   ? 10.084  41.376 29.853  0.50 101.50 ? 603 CU  A CU  1 
HETATM 6826 CU CU  . CU  F 2 .   ? 7.229   39.671 44.321  1.00 75.69  ? 604 CU  A CU  1 
HETATM 6827 C  C1  . EDO G 3 .   ? -7.572  5.823  33.900  1.00 61.84  ? 605 EDO A C1  1 
HETATM 6828 O  O1  . EDO G 3 .   ? -8.099  4.735  33.141  1.00 61.40  ? 605 EDO A O1  1 
HETATM 6829 C  C2  . EDO G 3 .   ? -8.100  7.194  33.427  1.00 62.06  ? 605 EDO A C2  1 
HETATM 6830 O  O2  . EDO G 3 .   ? -7.346  7.770  32.350  1.00 61.81  ? 605 EDO A O2  1 
HETATM 6831 C  C1  . EDO H 3 .   ? 30.978  55.579 22.014  1.00 78.12  ? 606 EDO A C1  1 
HETATM 6832 O  O1  . EDO H 3 .   ? 29.784  55.461 22.788  1.00 78.01  ? 606 EDO A O1  1 
HETATM 6833 C  C2  . EDO H 3 .   ? 32.118  56.189 22.817  1.00 78.13  ? 606 EDO A C2  1 
HETATM 6834 O  O2  . EDO H 3 .   ? 33.148  55.230 23.040  1.00 78.03  ? 606 EDO A O2  1 
HETATM 6835 C  C1  . EDO I 3 .   ? 18.800  49.495 17.831  1.00 80.39  ? 607 EDO A C1  1 
HETATM 6836 O  O1  . EDO I 3 .   ? 18.716  48.080 17.766  1.00 80.56  ? 607 EDO A O1  1 
HETATM 6837 C  C2  . EDO I 3 .   ? 19.237  49.899 19.212  1.00 80.10  ? 607 EDO A C2  1 
HETATM 6838 O  O2  . EDO I 3 .   ? 20.614  49.610 19.368  1.00 79.91  ? 607 EDO A O2  1 
HETATM 6839 C  C1  . EDO J 3 .   ? -7.381  11.978 30.289  1.00 69.76  ? 608 EDO A C1  1 
HETATM 6840 O  O1  . EDO J 3 .   ? -7.796  12.992 29.388  1.00 69.53  ? 608 EDO A O1  1 
HETATM 6841 C  C2  . EDO J 3 .   ? -7.273  10.646 29.567  1.00 70.04  ? 608 EDO A C2  1 
HETATM 6842 O  O2  . EDO J 3 .   ? -7.266  9.574  30.510  1.00 70.27  ? 608 EDO A O2  1 
HETATM 6843 C  C1  . EDO K 3 .   ? -5.980  31.137 18.901  1.00 66.72  ? 609 EDO A C1  1 
HETATM 6844 O  O1  . EDO K 3 .   ? -5.707  30.422 20.109  1.00 66.66  ? 609 EDO A O1  1 
HETATM 6845 C  C2  . EDO K 3 .   ? -4.704  31.468 18.127  1.00 66.53  ? 609 EDO A C2  1 
HETATM 6846 O  O2  . EDO K 3 .   ? -4.960  31.547 16.731  1.00 66.20  ? 609 EDO A O2  1 
HETATM 6847 CU CU  . CU  L 2 .   ? -8.470  39.035 73.503  1.00 87.70  ? 601 CU  B CU  1 
HETATM 6848 CU CU  . CU  M 2 .   ? -9.913  42.556 72.265  1.00 105.38 ? 602 CU  B CU  1 
HETATM 6849 CU CU  . CU  N 2 .   ? -12.096 41.169 74.622  0.50 82.61  ? 603 CU  B CU  1 
HETATM 6850 CU CU  . CU  O 2 .   ? -9.502  39.478 60.265  1.00 83.61  ? 604 CU  B CU  1 
HETATM 6851 C  C1  . EDO P 3 .   ? 7.125   12.587 75.661  1.00 65.36  ? 605 EDO B C1  1 
HETATM 6852 O  O1  . EDO P 3 .   ? 6.722   13.878 75.232  1.00 65.66  ? 605 EDO B O1  1 
HETATM 6853 C  C2  . EDO P 3 .   ? 6.610   11.501 74.735  1.00 65.22  ? 605 EDO B C2  1 
HETATM 6854 O  O2  . EDO P 3 .   ? 6.789   11.823 73.360  1.00 64.84  ? 605 EDO B O2  1 
HETATM 6855 C  C1  . EDO Q 3 .   ? 4.503   32.861 86.355  1.00 58.51  ? 606 EDO B C1  1 
HETATM 6856 O  O1  . EDO Q 3 .   ? 4.780   31.911 85.323  1.00 58.38  ? 606 EDO B O1  1 
HETATM 6857 C  C2  . EDO Q 3 .   ? 3.937   32.212 87.601  1.00 58.37  ? 606 EDO B C2  1 
HETATM 6858 O  O2  . EDO Q 3 .   ? 2.866   31.375 87.208  1.00 58.45  ? 606 EDO B O2  1 
HETATM 6859 C  C1  . EDO R 3 .   ? -38.140 35.410 73.702  1.00 55.55  ? 607 EDO B C1  1 
HETATM 6860 O  O1  . EDO R 3 .   ? -37.832 36.533 72.887  1.00 55.95  ? 607 EDO B O1  1 
HETATM 6861 C  C2  . EDO R 3 .   ? -39.401 34.770 73.241  1.00 54.94  ? 607 EDO B C2  1 
HETATM 6862 O  O2  . EDO R 3 .   ? -39.254 34.346 71.901  1.00 54.55  ? 607 EDO B O2  1 
HETATM 6863 C  C1  . EDO S 3 .   ? -9.552  3.481  70.573  1.00 68.13  ? 608 EDO B C1  1 
HETATM 6864 O  O1  . EDO S 3 .   ? -8.351  4.103  71.027  1.00 68.02  ? 608 EDO B O1  1 
HETATM 6865 C  C2  . EDO S 3 .   ? -9.478  3.160  69.082  1.00 68.15  ? 608 EDO B C2  1 
HETATM 6866 O  O2  . EDO S 3 .   ? -9.591  4.328  68.270  1.00 68.06  ? 608 EDO B O2  1 
HETATM 6867 C  C1  . EDO T 3 .   ? 10.571  11.728 76.034  1.00 61.46  ? 609 EDO B C1  1 
HETATM 6868 O  O1  . EDO T 3 .   ? 10.826  11.892 77.430  1.00 61.64  ? 609 EDO B O1  1 
HETATM 6869 C  C2  . EDO T 3 .   ? 11.225  10.491 75.450  1.00 61.06  ? 609 EDO B C2  1 
HETATM 6870 O  O2  . EDO T 3 .   ? 10.775  10.239 74.123  1.00 60.71  ? 609 EDO B O2  1 
HETATM 6871 C  C1  . EDO U 3 .   ? -29.465 52.061 82.590  1.00 90.48  ? 610 EDO B C1  1 
HETATM 6872 O  O1  . EDO U 3 .   ? -29.338 53.206 81.759  1.00 90.34  ? 610 EDO B O1  1 
HETATM 6873 C  C2  . EDO U 3 .   ? -30.657 51.232 82.160  1.00 90.59  ? 610 EDO B C2  1 
HETATM 6874 O  O2  . EDO U 3 .   ? -30.440 50.703 80.858  1.00 90.63  ? 610 EDO B O2  1 
HETATM 6875 C  C1  . EDO V 3 .   ? -22.153 49.952 85.564  1.00 72.11  ? 611 EDO B C1  1 
HETATM 6876 O  O1  . EDO V 3 .   ? -22.454 48.661 85.072  1.00 71.80  ? 611 EDO B O1  1 
HETATM 6877 C  C2  . EDO V 3 .   ? -20.882 49.899 86.375  1.00 72.39  ? 611 EDO B C2  1 
HETATM 6878 O  O2  . EDO V 3 .   ? -19.917 50.798 85.844  1.00 72.47  ? 611 EDO B O2  1 
HETATM 6879 O  O   . HOH W 4 .   ? 12.187  42.189 50.852  1.00 74.34  ? 701 HOH A O   1 
HETATM 6880 O  O   . HOH W 4 .   ? -3.112  33.070 37.351  1.00 42.60  ? 702 HOH A O   1 
HETATM 6881 O  O   . HOH W 4 .   ? 13.469  25.068 37.075  1.00 51.99  ? 703 HOH A O   1 
HETATM 6882 O  O   . HOH W 4 .   ? -13.319 43.500 20.988  1.00 48.89  ? 704 HOH A O   1 
HETATM 6883 O  O   . HOH W 4 .   ? -0.340  43.393 6.112   1.00 50.43  ? 705 HOH A O   1 
HETATM 6884 O  O   . HOH W 4 .   ? 19.151  45.144 25.160  1.00 80.21  ? 706 HOH A O   1 
HETATM 6885 O  O   . HOH W 4 .   ? -1.631  32.796 39.604  1.00 61.92  ? 707 HOH A O   1 
HETATM 6886 O  O   . HOH W 4 .   ? 2.958   36.186 35.968  1.00 85.03  ? 708 HOH A O   1 
HETATM 6887 O  O   . HOH W 4 .   ? 22.803  24.759 43.052  1.00 62.94  ? 709 HOH A O   1 
HETATM 6888 O  O   . HOH W 4 .   ? 20.931  28.860 18.418  1.00 50.72  ? 710 HOH A O   1 
HETATM 6889 O  O   . HOH W 4 .   ? 22.628  39.606 29.167  1.00 52.18  ? 711 HOH A O   1 
HETATM 6890 O  O   . HOH W 4 .   ? 30.652  37.706 25.556  1.00 64.84  ? 712 HOH A O   1 
HETATM 6891 O  O   . HOH W 4 .   ? 23.303  35.853 45.277  1.00 66.90  ? 713 HOH A O   1 
HETATM 6892 O  O   . HOH W 4 .   ? 17.657  8.984  21.223  1.00 54.38  ? 714 HOH A O   1 
HETATM 6893 O  O   . HOH W 4 .   ? 19.750  28.718 27.166  1.00 34.36  ? 715 HOH A O   1 
HETATM 6894 O  O   . HOH W 4 .   ? -6.707  33.933 20.577  1.00 51.17  ? 716 HOH A O   1 
HETATM 6895 O  O   . HOH W 4 .   ? -0.190  48.232 7.246   1.00 59.67  ? 717 HOH A O   1 
HETATM 6896 O  O   . HOH W 4 .   ? -4.366  33.252 34.348  1.00 46.81  ? 718 HOH A O   1 
HETATM 6897 O  O   . HOH W 4 .   ? -4.004  44.613 38.123  1.00 66.00  ? 719 HOH A O   1 
HETATM 6898 O  O   . HOH W 4 .   ? 3.891   -1.041 30.610  1.00 53.72  ? 720 HOH A O   1 
HETATM 6899 O  O   . HOH W 4 .   ? 12.685  27.342 17.950  1.00 51.67  ? 721 HOH A O   1 
HETATM 6900 O  O   . HOH W 4 .   ? 14.864  8.121  12.906  1.00 65.63  ? 722 HOH A O   1 
HETATM 6901 O  O   . HOH W 4 .   ? -5.848  35.628 45.652  1.00 46.95  ? 723 HOH A O   1 
HETATM 6902 O  O   . HOH W 4 .   ? 2.158   30.950 7.901   1.00 75.82  ? 724 HOH A O   1 
HETATM 6903 O  O   . HOH W 4 .   ? -4.077  28.598 29.769  1.00 57.49  ? 725 HOH A O   1 
HETATM 6904 O  O   . HOH W 4 .   ? 30.765  38.351 42.365  1.00 64.28  ? 726 HOH A O   1 
HETATM 6905 O  O   . HOH W 4 .   ? -0.511  20.698 42.812  1.00 45.17  ? 727 HOH A O   1 
HETATM 6906 O  O   . HOH W 4 .   ? -6.119  23.290 17.922  1.00 53.84  ? 728 HOH A O   1 
HETATM 6907 O  O   . HOH W 4 .   ? -9.582  38.371 43.584  1.00 60.89  ? 729 HOH A O   1 
HETATM 6908 O  O   . HOH W 4 .   ? 5.741   55.939 24.971  1.00 66.27  ? 730 HOH A O   1 
HETATM 6909 O  O   . HOH W 4 .   ? 0.446   36.054 8.369   1.00 62.56  ? 731 HOH A O   1 
HETATM 6910 O  O   . HOH W 4 .   ? 11.910  53.577 38.139  1.00 61.68  ? 732 HOH A O   1 
HETATM 6911 O  O   . HOH W 4 .   ? 9.373   16.841 13.538  1.00 43.59  ? 733 HOH A O   1 
HETATM 6912 O  O   . HOH W 4 .   ? 24.258  24.163 29.319  1.00 59.01  ? 734 HOH A O   1 
HETATM 6913 O  O   . HOH W 4 .   ? 18.961  28.597 21.065  1.00 57.52  ? 735 HOH A O   1 
HETATM 6914 O  O   . HOH W 4 .   ? -6.077  29.600 22.874  1.00 50.89  ? 736 HOH A O   1 
HETATM 6915 O  O   . HOH W 4 .   ? 9.605   5.563  25.725  1.00 48.57  ? 737 HOH A O   1 
HETATM 6916 O  O   . HOH W 4 .   ? -2.992  37.942 11.661  1.00 42.36  ? 738 HOH A O   1 
HETATM 6917 O  O   . HOH W 4 .   ? -15.227 12.690 26.546  1.00 40.49  ? 739 HOH A O   1 
HETATM 6918 O  O   . HOH W 4 .   ? 8.305   12.619 36.858  1.00 51.47  ? 740 HOH A O   1 
HETATM 6919 O  O   . HOH W 4 .   ? 26.738  54.198 36.458  1.00 68.19  ? 741 HOH A O   1 
HETATM 6920 O  O   . HOH W 4 .   ? 14.197  26.685 20.299  1.00 44.28  ? 742 HOH A O   1 
HETATM 6921 O  O   . HOH W 4 .   ? 0.993   33.218 8.651   1.00 40.83  ? 743 HOH A O   1 
HETATM 6922 O  O   . HOH W 4 .   ? -8.550  30.500 21.148  1.00 53.62  ? 744 HOH A O   1 
HETATM 6923 O  O   . HOH W 4 .   ? 21.888  36.411 24.505  1.00 54.76  ? 745 HOH A O   1 
HETATM 6924 O  O   . HOH W 4 .   ? 8.816   45.146 7.996   1.00 59.70  ? 746 HOH A O   1 
HETATM 6925 O  O   . HOH W 4 .   ? -19.735 24.397 36.810  1.00 61.91  ? 747 HOH A O   1 
HETATM 6926 O  O   . HOH W 4 .   ? -11.759 18.050 32.827  1.00 49.22  ? 748 HOH A O   1 
HETATM 6927 O  O   . HOH W 4 .   ? 7.213   47.840 58.842  1.00 52.62  ? 749 HOH A O   1 
HETATM 6928 O  O   . HOH W 4 .   ? 26.846  55.363 23.769  1.00 69.59  ? 750 HOH A O   1 
HETATM 6929 O  O   . HOH W 4 .   ? 8.376   50.442 17.247  1.00 55.98  ? 751 HOH A O   1 
HETATM 6930 O  O   . HOH W 4 .   ? 1.180   53.044 14.611  1.00 67.66  ? 752 HOH A O   1 
HETATM 6931 O  O   . HOH W 4 .   ? -4.349  33.960 14.857  1.00 54.83  ? 753 HOH A O   1 
HETATM 6932 O  O   . HOH W 4 .   ? 15.754  13.341 11.755  1.00 45.99  ? 754 HOH A O   1 
HETATM 6933 O  O   . HOH W 4 .   ? 9.375   5.949  28.479  1.00 59.07  ? 755 HOH A O   1 
HETATM 6934 O  O   . HOH W 4 .   ? -4.458  54.072 14.877  1.00 56.69  ? 756 HOH A O   1 
HETATM 6935 O  O   . HOH W 4 .   ? 24.384  54.974 38.107  1.00 55.30  ? 757 HOH A O   1 
HETATM 6936 O  O   . HOH W 4 .   ? 14.536  22.790 15.830  1.00 56.17  ? 758 HOH A O   1 
HETATM 6937 O  O   . HOH W 4 .   ? 32.127  47.435 41.120  1.00 49.67  ? 759 HOH A O   1 
HETATM 6938 O  O   . HOH W 4 .   ? 19.793  20.348 37.259  1.00 59.36  ? 760 HOH A O   1 
HETATM 6939 O  O   . HOH W 4 .   ? 15.033  15.954 39.404  1.00 41.37  ? 761 HOH A O   1 
HETATM 6940 O  O   . HOH W 4 .   ? 24.327  34.130 19.731  1.00 56.93  ? 762 HOH A O   1 
HETATM 6941 O  O   . HOH W 4 .   ? -0.039  39.108 9.405   1.00 56.82  ? 763 HOH A O   1 
HETATM 6942 O  O   . HOH W 4 .   ? -3.438  6.092  15.945  1.00 53.19  ? 764 HOH A O   1 
HETATM 6943 O  O   . HOH W 4 .   ? 8.346   56.248 46.284  1.00 57.37  ? 765 HOH A O   1 
HETATM 6944 O  O   . HOH W 4 .   ? 1.954   34.770 6.029   1.00 64.29  ? 766 HOH A O   1 
HETATM 6945 O  O   . HOH W 4 .   ? 12.566  32.921 7.167   1.00 53.49  ? 767 HOH A O   1 
HETATM 6946 O  O   . HOH W 4 .   ? -18.493 23.075 30.855  1.00 55.55  ? 768 HOH A O   1 
HETATM 6947 O  O   . HOH W 4 .   ? 3.545   53.238 16.286  1.00 44.08  ? 769 HOH A O   1 
HETATM 6948 O  O   . HOH W 4 .   ? 4.466   7.354  10.476  1.00 53.27  ? 770 HOH A O   1 
HETATM 6949 O  O   . HOH W 4 .   ? -12.738 50.189 20.493  1.00 58.12  ? 771 HOH A O   1 
HETATM 6950 O  O   . HOH W 4 .   ? -12.547 19.357 22.011  1.00 45.57  ? 772 HOH A O   1 
HETATM 6951 O  O   . HOH W 4 .   ? 20.812  32.338 12.096  1.00 37.31  ? 773 HOH A O   1 
HETATM 6952 O  O   . HOH W 4 .   ? 24.234  31.379 7.969   1.00 67.61  ? 774 HOH A O   1 
HETATM 6953 O  O   . HOH W 4 .   ? -2.376  8.203  7.482   1.00 57.67  ? 775 HOH A O   1 
HETATM 6954 O  O   . HOH X 4 .   ? 0.769   34.479 69.994  1.00 50.79  ? 701 HOH B O   1 
HETATM 6955 O  O   . HOH X 4 .   ? 15.881  30.518 72.235  1.00 59.45  ? 702 HOH B O   1 
HETATM 6956 O  O   . HOH X 4 .   ? -20.408 27.041 73.155  1.00 73.19  ? 703 HOH B O   1 
HETATM 6957 O  O   . HOH X 4 .   ? -23.577 23.904 62.312  1.00 61.31  ? 704 HOH B O   1 
HETATM 6958 O  O   . HOH X 4 .   ? 1.368   33.163 67.311  1.00 55.66  ? 705 HOH B O   1 
HETATM 6959 O  O   . HOH X 4 .   ? 4.151   20.664 68.843  1.00 48.81  ? 706 HOH B O   1 
HETATM 6960 O  O   . HOH X 4 .   ? -27.462 45.781 76.459  1.00 88.86  ? 707 HOH B O   1 
HETATM 6961 O  O   . HOH X 4 .   ? -11.519 36.073 70.352  1.00 55.73  ? 708 HOH B O   1 
HETATM 6962 O  O   . HOH X 4 .   ? -32.965 38.325 66.849  1.00 46.24  ? 709 HOH B O   1 
HETATM 6963 O  O   . HOH X 4 .   ? -15.034 24.773 67.484  1.00 43.70  ? 710 HOH B O   1 
HETATM 6964 O  O   . HOH X 4 .   ? 2.572   27.726 58.270  1.00 67.85  ? 711 HOH B O   1 
HETATM 6965 O  O   . HOH X 4 .   ? -2.726  22.952 62.801  1.00 44.12  ? 712 HOH B O   1 
HETATM 6966 O  O   . HOH X 4 .   ? 4.851   34.518 83.530  1.00 53.31  ? 713 HOH B O   1 
HETATM 6967 O  O   . HOH X 4 .   ? -21.627 11.351 80.936  1.00 71.65  ? 714 HOH B O   1 
HETATM 6968 O  O   . HOH X 4 .   ? -28.690 21.086 82.311  1.00 68.77  ? 715 HOH B O   1 
HETATM 6969 O  O   . HOH X 4 .   ? -1.661  43.506 98.857  1.00 44.30  ? 716 HOH B O   1 
HETATM 6970 O  O   . HOH X 4 .   ? 6.445   30.928 83.449  1.00 49.44  ? 717 HOH B O   1 
HETATM 6971 O  O   . HOH X 4 .   ? -6.668  50.040 56.741  1.00 65.30  ? 718 HOH B O   1 
HETATM 6972 O  O   . HOH X 4 .   ? -13.628 27.483 85.592  1.00 53.76  ? 719 HOH B O   1 
HETATM 6973 O  O   . HOH X 4 .   ? -15.670 63.215 62.407  1.00 39.12  ? 720 HOH B O   1 
HETATM 6974 O  O   . HOH X 4 .   ? -0.803  29.217 52.373  1.00 56.10  ? 721 HOH B O   1 
HETATM 6975 O  O   . HOH X 4 .   ? 6.864   39.281 61.004  1.00 52.35  ? 722 HOH B O   1 
HETATM 6976 O  O   . HOH X 4 .   ? -3.947  -1.613 73.580  1.00 52.90  ? 723 HOH B O   1 
HETATM 6977 O  O   . HOH X 4 .   ? -6.393  0.462  84.092  1.00 44.83  ? 724 HOH B O   1 
HETATM 6978 O  O   . HOH X 4 .   ? 13.461  29.663 63.988  1.00 89.94  ? 725 HOH B O   1 
HETATM 6979 O  O   . HOH X 4 .   ? 2.423   28.668 74.602  1.00 44.58  ? 726 HOH B O   1 
HETATM 6980 O  O   . HOH X 4 .   ? -0.399  27.528 92.133  1.00 51.54  ? 727 HOH B O   1 
HETATM 6981 O  O   . HOH X 4 .   ? -25.734 23.170 75.562  1.00 51.93  ? 728 HOH B O   1 
HETATM 6982 O  O   . HOH X 4 .   ? -27.229 34.147 55.075  1.00 54.60  ? 729 HOH B O   1 
HETATM 6983 O  O   . HOH X 4 .   ? 10.589  18.655 71.994  1.00 49.58  ? 730 HOH B O   1 
HETATM 6984 O  O   . HOH X 4 .   ? -4.871  52.845 88.530  1.00 63.23  ? 731 HOH B O   1 
HETATM 6985 O  O   . HOH X 4 .   ? 11.712  26.356 64.793  1.00 65.86  ? 732 HOH B O   1 
HETATM 6986 O  O   . HOH X 4 .   ? -32.860 37.158 61.605  1.00 50.59  ? 733 HOH B O   1 
HETATM 6987 O  O   . HOH X 4 .   ? -0.945  21.084 61.808  1.00 47.70  ? 734 HOH B O   1 
HETATM 6988 O  O   . HOH X 4 .   ? 10.830  24.048 74.755  1.00 55.00  ? 735 HOH B O   1 
HETATM 6989 O  O   . HOH X 4 .   ? -9.360  12.543 67.626  1.00 52.04  ? 736 HOH B O   1 
HETATM 6990 O  O   . HOH X 4 .   ? -24.599 49.068 62.442  1.00 50.48  ? 737 HOH B O   1 
HETATM 6991 O  O   . HOH X 4 .   ? -27.355 53.596 85.161  1.00 76.55  ? 738 HOH B O   1 
HETATM 6992 O  O   . HOH X 4 .   ? 2.578   6.414  89.022  1.00 48.26  ? 739 HOH B O   1 
HETATM 6993 O  O   . HOH X 4 .   ? -11.221 44.990 96.473  1.00 54.38  ? 740 HOH B O   1 
HETATM 6994 O  O   . HOH X 4 .   ? -7.149  52.699 48.996  1.00 48.75  ? 741 HOH B O   1 
HETATM 6995 O  O   . HOH X 4 .   ? -3.775  46.875 47.581  1.00 56.34  ? 742 HOH B O   1 
HETATM 6996 O  O   . HOH X 4 .   ? -5.539  2.875  88.638  1.00 51.96  ? 743 HOH B O   1 
HETATM 6997 O  O   . HOH X 4 .   ? 1.993   9.213  71.758  1.00 43.02  ? 744 HOH B O   1 
HETATM 6998 O  O   . HOH X 4 .   ? -3.869  29.942 95.855  1.00 57.27  ? 745 HOH B O   1 
HETATM 6999 O  O   . HOH X 4 .   ? 8.112   8.997  73.062  1.00 59.30  ? 746 HOH B O   1 
HETATM 7000 O  O   . HOH X 4 .   ? -2.398  32.485 95.607  1.00 55.56  ? 747 HOH B O   1 
HETATM 7001 O  O   . HOH X 4 .   ? -20.849 19.734 67.567  1.00 40.57  ? 748 HOH B O   1 
HETATM 7002 O  O   . HOH X 4 .   ? 13.926  26.135 62.964  1.00 65.99  ? 749 HOH B O   1 
HETATM 7003 O  O   . HOH X 4 .   ? 6.270   53.657 75.085  1.00 63.40  ? 750 HOH B O   1 
HETATM 7004 O  O   . HOH X 4 .   ? -7.961  11.307 65.240  1.00 49.11  ? 751 HOH B O   1 
HETATM 7005 O  O   . HOH X 4 .   ? -15.797 26.015 84.404  1.00 50.06  ? 752 HOH B O   1 
HETATM 7006 O  O   . HOH X 4 .   ? -4.741  6.525  93.471  1.00 58.70  ? 753 HOH B O   1 
HETATM 7007 O  O   . HOH X 4 .   ? -27.704 41.364 52.160  1.00 78.16  ? 754 HOH B O   1 
HETATM 7008 O  O   . HOH X 4 .   ? -23.725 11.669 85.593  1.00 66.95  ? 755 HOH B O   1 
HETATM 7009 O  O   . HOH X 4 .   ? 15.994  36.978 81.715  1.00 58.52  ? 756 HOH B O   1 
HETATM 7010 O  O   . HOH X 4 .   ? -16.087 15.443 64.839  1.00 34.94  ? 757 HOH B O   1 
HETATM 7011 O  O   . HOH X 4 .   ? 8.993   38.533 59.654  1.00 52.97  ? 758 HOH B O   1 
HETATM 7012 O  O   . HOH X 4 .   ? -10.214 5.353  78.126  1.00 49.06  ? 759 HOH B O   1 
HETATM 7013 O  O   . HOH X 4 .   ? -27.941 39.958 49.819  1.00 52.47  ? 760 HOH B O   1 
HETATM 7014 O  O   . HOH X 4 .   ? -17.901 26.872 56.073  1.00 60.47  ? 761 HOH B O   1 
HETATM 7015 O  O   . HOH X 4 .   ? 11.724  19.469 82.070  1.00 59.93  ? 762 HOH B O   1 
HETATM 7016 O  O   . HOH X 4 .   ? -13.880 14.722 91.331  1.00 53.01  ? 763 HOH B O   1 
HETATM 7017 O  O   . HOH X 4 .   ? -28.834 19.405 78.632  1.00 64.58  ? 764 HOH B O   1 
HETATM 7018 O  O   . HOH X 4 .   ? 17.889  24.806 73.711  1.00 49.87  ? 765 HOH B O   1 
HETATM 7019 O  O   . HOH X 4 .   ? -14.554 52.771 65.388  1.00 68.23  ? 766 HOH B O   1 
HETATM 7020 O  O   . HOH X 4 .   ? 5.061   29.764 81.451  1.00 50.87  ? 767 HOH B O   1 
HETATM 7021 O  O   . HOH X 4 .   ? -18.248 8.609  82.793  1.00 53.38  ? 768 HOH B O   1 
# 
